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Conserved domains on  [gi|530407637|ref|XP_005255181|]
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CREB-binding protein isoform X2 [Homo sapiens]

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 ...
1327-1634 6.61e-95

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


:

Pssm-ID: 400497  Cd Length: 348  Bit Score: 311.64  E-value: 6.61e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1327 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1407 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1482 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1537 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1591
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 530407637  1592 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1634
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.72e-77

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: 251.59  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1072 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1151
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 530407637 1152 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1179
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 ...
587-667 1.11e-47

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: 165.36  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   587 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 666
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 530407637   667 E 667
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 2.52e-33

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: 123.94  E-value: 2.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637 1191 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1263
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-430 2.02e-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: 109.78  E-value: 2.02e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 430
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 7.61e-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: 107.26  E-value: 7.61e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530407637 1690 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1730
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 ...
1757-1825 4.49e-24

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.46  E-value: 4.49e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530407637  1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1998-2099 8.63e-20

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: 86.81  E-value: 8.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1998 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2066
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 530407637  2067 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2099
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1265-1296 9.38e-19

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: 81.16  E-value: 9.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530407637 1265 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1296
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHA03247 super family cl33720
large tegument protein UL36; Provisional
683-1010 8.70e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.96  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  683 PALPAPGAQPPVIPQAQPVRPPRMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPnmmg 762
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP---- 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  763 ahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQLPCPPVTQSPlHPTP 842
Cdd:PHA03247 2840 ----------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRRLARPAVSRST-ESFA 2899
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  843 PPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPP 922
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  923 SVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQAEDTEPDPGESKGEP 1002
Cdd:PHA03247 2971 RVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWPPDDTEDSDADSLFDS 3045

                  ....*...
gi 530407637 1003 RSEMMEED 1010
Cdd:PHA03247 3046 DSERSDLE 3053
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2095-2408 1.03e-05

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.16  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2095 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2157
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2158 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2237
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2238 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2314
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2315 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2394
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 530407637  2395 PQLNtPSRSALSSE 2408
Cdd:pfam09606  462 SPLN-PQEEQLYRE 474
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1327-1634 6.61e-95

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


Pssm-ID: 400497  Cd Length: 348  Bit Score: 311.64  E-value: 6.61e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1327 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1407 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1482 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1537 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1591
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 530407637  1592 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1634
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.72e-77

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: 251.59  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1072 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1151
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 530407637 1152 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1179
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 ...
587-667 1.11e-47

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: 165.36  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   587 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 666
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 530407637   667 E 667
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1069-1177 7.76e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.76e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   1069 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1148
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 530407637   1149 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1177
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 2.52e-33

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: 123.94  E-value: 2.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637 1191 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1263
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-430 2.02e-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: 109.78  E-value: 2.02e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 430
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 7.61e-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: 107.26  E-value: 7.61e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530407637 1690 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1730
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1177-1216 3.75e-24

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: 96.62  E-value: 3.75e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530407637  1177 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1216
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1757-1825 4.49e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.46  E-value: 4.49e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530407637  1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1751-1829 1.22e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 96.67  E-value: 1.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   1751 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1826
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 530407637   1827 FCL 1829
Cdd:smart00551   77 KCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
363-433 4.56e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 4.56e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530407637    363 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGKaCQVAHCASSRQIISHWKNCTRHDCPVCLPL 433
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1998-2099 8.63e-20

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: 86.81  E-value: 8.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1998 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2066
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 530407637  2067 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2099
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1089-1161 5.06e-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: 5.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530407637  1089 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1161
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1265-1296 9.38e-19

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: 81.16  E-value: 9.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530407637 1265 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1296
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1686-1728 4.32e-17

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: 76.71  E-value: 4.32e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530407637   1686 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHKMV 1728
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1686-1727 2.76e-15

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.75  E-value: 2.76e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530407637  1686 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHAHKM 1727
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1060-1178 7.77e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 78.69  E-value: 7.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1060 TSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYV 1139
Cdd:COG5076   134 KTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFV 210
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530407637 1140 DDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 1178
Cdd:COG5076   211 SDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
PHA03247 PHA03247
large tegument protein UL36; Provisional
683-1010 8.70e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.96  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  683 PALPAPGAQPPVIPQAQPVRPPRMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPnmmg 762
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP---- 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  763 ahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQLPCPPVTQSPlHPTP 842
Cdd:PHA03247 2840 ----------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRRLARPAVSRST-ESFA 2899
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  843 PPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPP 922
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  923 SVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQAEDTEPDPGESKGEP 1002
Cdd:PHA03247 2971 RVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWPPDDTEDSDADSLFDS 3045

                  ....*...
gi 530407637 1003 RSEMMEED 1010
Cdd:PHA03247 3046 DSERSDLE 3053
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2051-2093 1.59e-09

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: 55.35  E-value: 1.59e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530407637 2051 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2093
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
467-932 2.69e-09

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: 62.86  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   467 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTdQQPPNLI 546
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-SQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   547 SESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 626
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   627 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPAPGAQ----PPVIPQAQPVR 702
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQrihtPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   703 PPRMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMM---GAHTNNMMAQAPAQSQFL 779
Cdd:pfam03154  339 PPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKplsSLSTHHPPSAHPPPLQLM 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   780 PQNQFPSSSGAmsvgmgQPPAQTGVSQGQVPGAALPNPlNMLGPQASQLPCPPVTQSPLHPTP------PPASTAAGMPS 853
Cdd:pfam03154  419 PQSQQLPPPPA------QPPVLTQSQSLPPPAASHPPT-SGLHQVPSQSPFPQHPFVPGGPPPitppsgPPTSTSSAMPG 491
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   854 LQhttPPgmtppqpaaptqPSTPVSSSGQTPTPTPGSVPsATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVA-TPQSSQQ 932
Cdd:pfam03154  492 IQ---PP------------SSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEEPESPPPPPRSPSPEPTVVnTPSHASQ 555
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2095-2408 1.03e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.16  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2095 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2157
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2158 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2237
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2238 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2314
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2315 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2394
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 530407637  2395 PQLNtPSRSALSSE 2408
Cdd:pfam09606  462 SPLN-PQEEQLYRE 474
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
711-1030 1.95e-05

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 50.05  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  711 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPG-MAISPSRMPQPPNMMGAHT-NNMMAQAPAQSQFLPQNQFPSSS 788
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNAVDYSVlVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  789 GAMSVGMGQPPAQTGVSQGQVPGAALPNPLnmlGPQASQLPCppvTQSPLHPTPPPASTAagmPSLQHttpPGMTPPQPA 868
Cdd:COG5665   219 SGRSQHIVQAAKRVGVEWWGDPSLLATPPA---TPATEEKSS---QQPKSQPTSPSGGTT---PPSTN---QLTTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  869 APTQPSTPVSSSGQTPTPTP-------GSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQ 940
Cdd:COG5665   287 STAKAQPQPPTKKQPAKEPPsdtasgnPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTPAtDLA 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  941 PPGTPLSQAAASIDNRVP--------------TPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEM 1006
Cdd:COG5665   367 TPVSPTPPETSVDKKVSPdsatsstksekeggTASSPMPPNIAIGAKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSV 446
                         330       340
                  ....*....|....*....|....
gi 530407637 1007 MEEDLQGASQVKEETDIAEQKSEP 1030
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAP 470
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1327-1634 6.61e-95

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


Pssm-ID: 400497  Cd Length: 348  Bit Score: 311.64  E-value: 6.61e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1327 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1407 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1482 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1537 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1591
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 530407637  1592 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1634
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.72e-77

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: 251.59  E-value: 1.72e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1072 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1151
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 530407637 1152 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1179
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 ...
587-667 1.11e-47

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: 165.36  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   587 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 666
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 530407637   667 E 667
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1069-1177 7.76e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.76e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   1069 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1148
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 530407637   1149 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1177
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 2.52e-33

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: 123.94  E-value: 2.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637 1191 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1263
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1075-1174 2.86e-31

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


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 119.01  E-value: 2.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1075 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1153
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 530407637 1154 RKTSRVYKFCSKLAEVFEQEI 1174
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 ...
1095-1172 8.33e-31

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: 117.76  E-value: 8.33e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637 1095 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1172
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-430 2.02e-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: 109.78  E-value: 2.02e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407637   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 430
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 7.61e-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: 107.26  E-value: 7.61e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530407637 1690 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1730
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1074-1174 1.28e-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: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1074 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1153
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|.
gi 530407637 1154 RKTSRVYKFCSKLAEVFEQEI 1174
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1088-1171 1.66e-26

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


Pssm-ID: 99938  Cd Length: 99  Bit Score: 105.49  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1088 RQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1167
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                  ....
gi 530407637 1168 EVFE 1171
Cdd:cd05506    93 KIFE 96
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1177-1216 3.75e-24

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: 96.62  E-value: 3.75e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530407637  1177 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1216
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1757-1825 4.49e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.46  E-value: 4.49e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530407637  1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1082-1174 5.19e-24

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


Pssm-ID: 99932  Cd Length: 103  Bit Score: 98.54  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1082 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1161
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                          90
                  ....*....|...
gi 530407637 1162 FCSKLAEVFEQEI 1174
Cdd:cd05500    91 MGKRLQAAFEKHL 103
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1751-1829 1.22e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 96.67  E-value: 1.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   1751 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1826
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 530407637   1827 FCL 1829
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 ...
1077-1176 1.65e-22

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 94.41  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1077 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1155
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                          90       100
                  ....*....|....*....|.
gi 530407637 1156 TSRVYKFCSKLAEVFEQEIDP 1176
Cdd:cd05497    86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1070-1172 3.59e-22

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: 93.51  E-value: 3.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1070 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKNPMDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 1146
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                          90       100
                  ....*....|....*....|....*.
gi 530407637 1147 NNAWLYNRKTSRVYKFCSKLAEVFEQ 1172
Cdd:cd05502    76 KNCYKFNEEDSEVAQAGKELELFFEE 101
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1092-1190 8.93e-22

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 92.52  E-value: 8.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1092 ESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKFCSKLAEVF 1170
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                          90       100
                  ....*....|....*....|
gi 530407637 1171 EQEIDPVMQSlgYCCGRKYE 1190
Cdd:cd05496   100 EEHIKKIISD--WKSALKRN 117
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1095-1171 1.57e-21

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


Pssm-ID: 99931  Cd Length: 102  Bit Score: 91.19  E-value: 1.57e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530407637 1095 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFE 1171
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
363-433 4.56e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 4.56e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530407637    363 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGKaCQVAHCASSRQIISHWKNCTRHDCPVCLPL 433
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1998-2099 8.63e-20

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: 86.81  E-value: 8.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  1998 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2066
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 530407637  2067 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2099
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1073-1173 2.81e-19

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 85.52  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1073 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMF 1146
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                          90       100
                  ....*....|....*....|....*..
gi 530407637 1147 NNAWLYNRKTSRVYKFCSKLAEVFEQE 1173
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1089-1161 5.06e-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: 5.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530407637  1089 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1161
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1265-1296 9.38e-19

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: 81.16  E-value: 9.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530407637 1265 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1296
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1264-1298 7.41e-18

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: 78.87  E-value: 7.41e-18
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530407637 1264 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1298
Cdd:cd15647     6 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1073-1163 3.27e-17

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


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 79.41  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1073 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1152
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                          90
                  ....*....|.
gi 530407637 1153 NRKTSRVYKFC 1163
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1686-1728 4.32e-17

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: 76.71  E-value: 4.32e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530407637   1686 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHKMV 1728
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1265-1298 4.85e-17

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: 76.44  E-value: 4.85e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530407637 1265 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1298
Cdd:cd15646     7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1078-1168 1.12e-15

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


Pssm-ID: 99944  Cd Length: 98  Bit Score: 74.36  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1078 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1157
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                          90
                  ....*....|.
gi 530407637 1158 RVYKFCSKLAE 1168
Cdd:cd05512    82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1091-1159 1.22e-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: 1.22e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1091 PESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 1159
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1686-1727 2.76e-15

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.75  E-value: 2.76e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530407637  1686 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHAHKM 1727
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1088-1183 5.10e-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: 73.07  E-value: 5.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1088 RQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1167
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEML 90
                          90
                  ....*....|....*.
gi 530407637 1168 EVFEQEIDPVMQSLGY 1183
Cdd:cd05511    91 ELAEELLAEREEKLTQ 106
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1060-1178 7.77e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 78.69  E-value: 7.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1060 TSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYV 1139
Cdd:COG5076   134 KTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFV 210
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530407637 1140 DDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 1178
Cdd:COG5076   211 SDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1108-1161 1.01e-14

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 71.95  E-value: 1.01e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1161
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1089-1176 1.41e-14

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


Pssm-ID: 99957  Cd Length: 112  Bit Score: 72.00  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1089 QDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN------RKTSRvYKF 1162
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                          90
                  ....*....|....*..
gi 530407637 1163 CSKLAEV---FEQEIDP 1176
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1108-1179 2.41e-14

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 71.21  E-value: 2.41e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1179
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1690-1726 5.15e-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: 68.23  E-value: 5.15e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530407637 1690 YTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHK 1726
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1221-1296 1.27e-13

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: 67.76  E-value: 1.27e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1221 FCEKCFTEIQGENVTLGddpsqpQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHY---DIIWPSGFVCDNC 1296
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNgrrNADETAEYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1076-1161 4.17e-13

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


Pssm-ID: 99939  Cd Length: 104  Bit Score: 67.39  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1076 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1155
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSS 81

                  ....*.
gi 530407637 1156 TSRVYK 1161
Cdd:cd05507    82 DHDVYL 87
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1071-1170 1.44e-12

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 65.64  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1071 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1150
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                          90       100
                  ....*....|....*....|
gi 530407637 1151 LYNRKTSRVYKFCSKLAEVF 1170
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1075-1166 2.51e-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: 65.12  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1075 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1154
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                          90
                  ....*....|..
gi 530407637 1155 KTSRVYKFCSKL 1166
Cdd:cd05513    79 PDTIYYKAAKKL 90
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1074-1162 1.12e-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: 63.50  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1074 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKNPMDLSTIKRKLDtgQYQEPWQYVDDVW 1143
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                          90
                  ....*....|....*....
gi 530407637 1144 LMFNNAWLYNRKTSRVYKF 1162
Cdd:cd05521    72 QIPWNARLYNTKGSVIYKY 90
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1108-1161 2.78e-11

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


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 62.26  E-value: 2.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1161
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYK 91
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1108-1166 4.76e-11

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 61.59  E-value: 4.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 1166
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1107-1175 1.03e-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: 60.90  E-value: 1.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1107 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEID 1175
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1075-1174 3.40e-10

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 59.28  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1075 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNA 1149
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                          90       100
                  ....*....|....*....|....*
gi 530407637 1150 WLYNRKTSRVYKFCSKLAEVFEQEI 1174
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1097-1160 4.40e-10

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 58.61  E-value: 4.40e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1097 RQPVD-----PQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 1160
Cdd:cd05518    21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
683-1010 8.70e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.96  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  683 PALPAPGAQPPVIPQAQPVRPPRMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPnmmg 762
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP---- 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  763 ahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQLPCPPVTQSPlHPTP 842
Cdd:PHA03247 2840 ----------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRRLARPAVSRST-ESFA 2899
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  843 PPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPP 922
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  923 SVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQAEDTEPDPGESKGEP 1002
Cdd:PHA03247 2971 RVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWPPDDTEDSDADSLFDS 3045

                  ....*...
gi 530407637 1003 RSEMMEED 1010
Cdd:PHA03247 3046 DSERSDLE 3053
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2051-2093 1.59e-09

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: 55.35  E-value: 1.59e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530407637 2051 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2093
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1073-1174 1.75e-09

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 57.73  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1073 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1150
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                          90       100
                  ....*....|....*....|....
gi 530407637 1151 LYNRKTSRVYKFCSKLAEVFEQEI 1174
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1691-1729 2.02e-09

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


Pssm-ID: 239080  Cd Length: 43  Bit Score: 54.96  E-value: 2.02e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530407637 1691 TCNECKHHVE-TRWHCTVCEDYDLCINCYNTKSHA-HKMVK 1729
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHPeHAMLK 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
680-1002 2.19e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.42  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  680 GNQPALPAPGAQPPVIPQAQPVRP-PRMNSFNPMSLGNVQLPQAPMGPRAASPMNHSV-QMNSMGSVPGMAISPSRMPQP 757
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPsPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRpRRARRLGRAAQASSPPQRPRR 2685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  758 PNM---MGAHTNNMMAQAP---------AQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQV-PG--AALPNPLNMLG 822
Cdd:PHA03247 2686 RAArptVGSLTSLADPPPPpptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtPGgpARPARPPTTAG 2765
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  823 PQASQLPCPPVTqsplhpTPPPASTAAGMPSLQHTTPPGMTPPQPAAPtqpstPVSSSGQTPTPTPGSVPSATQTQSTPT 902
Cdd:PHA03247 2766 PPAPAPPAAPAA------GPPRRLTRPAVASLSESRESLPSPWDPADP-----PAAVLAPAAALPPAASPAGPLPPPTSA 2834
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  903 VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvhAQPPGTPLSQAAASIdNRVPTPSSVASAETNSQQPGPDVPVLEM 982
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPS--RSPAAKPAAPARPPV-RRLARPAVSRSTESFALPPDQPERPPQP 2911
                         330       340
                  ....*....|....*....|
gi 530407637  983 KTETQAEDTEPDPGESKGEP 1002
Cdd:PHA03247 2912 QAPPPPQPQPQPPPPPQPQP 2931
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
467-932 2.69e-09

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: 62.86  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   467 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTdQQPPNLI 546
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-SQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   547 SESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 626
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   627 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPAPGAQ----PPVIPQAQPVR 702
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQrihtPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   703 PPRMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMM---GAHTNNMMAQAPAQSQFL 779
Cdd:pfam03154  339 PPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKplsSLSTHHPPSAHPPPLQLM 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   780 PQNQFPSSSGAmsvgmgQPPAQTGVSQGQVPGAALPNPlNMLGPQASQLPCPPVTQSPLHPTP------PPASTAAGMPS 853
Cdd:pfam03154  419 PQSQQLPPPPA------QPPVLTQSQSLPPPAASHPPT-SGLHQVPSQSPFPQHPFVPGGPPPitppsgPPTSTSSAMPG 491
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   854 LQhttPPgmtppqpaaptqPSTPVSSSGQTPTPTPGSVPsATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVA-TPQSSQQ 932
Cdd:pfam03154  492 IQ---PP------------SSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEEPESPPPPPRSPSPEPTVVnTPSHASQ 555
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
673-1008 3.21e-09

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: 62.48  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   673 LHKQGILGNQPALPAPgaQPPVIPQAQPVrPPRMNSFNPMSLGNVQLPQAPMG-PRAASP--MNHSVQMNSMGSVPGMai 749
Cdd:pfam03154  230 LIQQTPTLHPQRLPSP--HPPLQPMTQPP-PPSQVSPQPLPQPSLHGQMPPMPhSLQTGPshMQHPVPPQPFPLTPQS-- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   750 SPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSS----GAMSVGMGQPPAQTGVSQgqvpgaaLPNPLNMLGPQA 825
Cdd:pfam03154  305 SQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQplppAPLSMPHIKPPPTTPIPQ-------LPNPQSHKHPPH 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   826 SQLPCPpvTQSPLHPTPPPASTAagMPSLQHTTPPGMTPPQPAaptqpstpVSSSGQTPTPTPGSVPSATQTQSTPTVQA 905
Cdd:pfam03154  378 LSGPSP--FQMNSNLPPPPALKP--LSSLSTHHPPSAHPPPLQ--------LMPQSQQLPPPPAQPPVLTQSQSLPPPAA 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   906 AAqaqvtpqpqtpvqPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASidnrvPTPSSVASAETNSQQPGPDVPVLEMKTE 985
Cdd:pfam03154  446 SH-------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSAMPGIQPPSSASVSSSGPVP 507
                          330       340
                   ....*....|....*....|...
gi 530407637   986 TQAEDTEPdPGESKGEPRSEMME 1008
Cdd:pfam03154  508 AAVSCPLP-PVQIKEEALDEAEE 529
PHA03247 PHA03247
large tegument protein UL36; Provisional
683-1004 2.50e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  683 PALPAP------GAQPPVIPQAQPVRPPRMNSFNPMSLGNVQ-------LPQAPMGPRAASPMNHSVQMNSMGSVPGMAI 749
Cdd:PHA03247 2686 RAARPTvgsltsLADPPPPPPTPEPAPHALVSATPLPPGPAAarqaspaLPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  750 SPSrmPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLgPQASQLP 829
Cdd:PHA03247 2766 PPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-PTAPPPP 2842
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  830 CPPVTQsplhPTPPPASTAAGMPsLQHTTPPGMTPPQPAAPTQPstPVSSSGQTPtptpgsVPSATQTQSTPTVQAAAQA 909
Cdd:PHA03247 2843 PGPPPP----SLPLGGSVAPGGD-VRRRPPSRSPAAKPAAPARP--PVRRLARPA------VSRSTESFALPPDQPERPP 2909
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  910 QVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAAsidnrVPTPSSVASAETNSQQPGPDVPVLEMKTeTQAE 989
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-----AGEPSGAVPQPWLGALVPGRVAVPRFRV-PQPA 2983
                         330
                  ....*....|....*
gi 530407637  990 DTEPDPGESKGEPRS 1004
Cdd:PHA03247 2984 PSREAPASSTPPLTG 2998
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1108-1172 6.35e-08

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


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 52.78  E-value: 6.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1172
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1108-1172 1.88e-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: 51.29  E-value: 1.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530407637 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1172
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1073-1130 8.72e-07

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


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 49.75  E-value: 8.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530407637 1073 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKNPMDLSTI-KRKLDTG 1130
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
822-1015 1.59e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  822 GPQASQLPCPPVTQSplHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTP-------VSSSGQTPTPTPGSVPSA 894
Cdd:PRK07764  599 GPPAPASSGPPEEAA--RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEhhpkhvaVPDASDGGDGWPAKAGGA 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  895 TQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPG 974
Cdd:PRK07764  677 APAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 530407637  975 PDVPVLEMKTETQAEDTepdPGESKGEPRSEMMEEDLQGAS 1015
Cdd:PRK07764  757 QPPPPPAPAPAAAPAAA---PPPSPPSEEEEMAEDDAPSMD 794
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
799-1004 2.44e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.96  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  799 PAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVS 878
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  879 SSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSS-------QQQPTPVHAQPPGTPLSQAAA 951
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPppweelpPEFASPAPAQPDAAPAGWVAE 524
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530407637  952 SIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRS 1004
Cdd:PRK12323  525 SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMF 577
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1073-1174 3.44e-06

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


Pssm-ID: 99940  Cd Length: 99  Bit Score: 47.76  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637 1073 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1152
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                          90       100
                  ....*....|....*....|..
gi 530407637 1153 NRKTSRVYKFCSKLAEVFEQEI 1174
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1107-1172 4.55e-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: 47.42  E-value: 4.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530407637 1107 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKFCSKLAEVFEQ 1172
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2095-2408 1.03e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.16  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2095 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2157
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2158 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2237
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2238 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2314
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2315 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2394
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 530407637  2395 PQLNtPSRSALSSE 2408
Cdd:pfam09606  462 SPLN-PQEEQLYRE 474
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
711-1030 1.95e-05

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 50.05  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  711 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPG-MAISPSRMPQPPNMMGAHT-NNMMAQAPAQSQFLPQNQFPSSS 788
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNAVDYSVlVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  789 GAMSVGMGQPPAQTGVSQGQVPGAALPNPLnmlGPQASQLPCppvTQSPLHPTPPPASTAagmPSLQHttpPGMTPPQPA 868
Cdd:COG5665   219 SGRSQHIVQAAKRVGVEWWGDPSLLATPPA---TPATEEKSS---QQPKSQPTSPSGGTT---PPSTN---QLTTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  869 APTQPSTPVSSSGQTPTPTP-------GSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQ 940
Cdd:COG5665   287 STAKAQPQPPTKKQPAKEPPsdtasgnPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTPAtDLA 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  941 PPGTPLSQAAASIDNRVP--------------TPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEM 1006
Cdd:COG5665   367 TPVSPTPPETSVDKKVSPdsatsstksekeggTASSPMPPNIAIGAKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSV 446
                         330       340
                  ....*....|....*....|....
gi 530407637 1007 MEEDLQGASQVKEETDIAEQKSEP 1030
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAP 470
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1692-1723 2.14e-05

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


Pssm-ID: 239079  Cd Length: 45  Bit Score: 43.60  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530407637 1692 CNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1723
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKH 36
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
860-999 1.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.17  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  860 PGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATP-QSSQQQPTPVH 938
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlQRAQGATKAKK 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530407637  939 AQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESK 999
Cdd:PRK07994  441 SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALK 501
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2097-2173 2.04e-04

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


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 45.73  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  2097 QPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMG---GLNPQgQALNIMNPGHNPNMASMNPQ 2173
Cdd:pfam07271  168 RIGFPMQPNMGMRPGFNQMPGMPPNQMRPGFNQMPGMPPRPGFPNPMPNMQprpGFRPQ-PGPMGNRPGGGFPHPGTPMG 246
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1691-1727 2.07e-04

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


Pssm-ID: 239085  Cd Length: 49  Bit Score: 41.04  E-value: 2.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530407637 1691 TCNECK--HHVETRWHCTVCEDYDLCINCY----NTKSH--AHKM 1727
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHnsLHIM 46
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
887-1002 2.19e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.40  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  887 TPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASA 966
Cdd:PRK07994  363 APLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSE 442
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530407637  967 ETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEP 1002
Cdd:PRK07994  443 PAAASRARPVNSALERLASVRPAPSALEKAPAKKEA 478
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1690-1729 2.36e-04

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


Pssm-ID: 239081  Cd Length: 48  Bit Score: 40.88  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530407637 1690 YTCNECKHH--VETRWHCTVC--EDYDLCINC-YNTKSH--AHKMVK 1729
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
825-966 2.61e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.11  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   825 ASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPpgmtppqpaAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQ 904
Cdd:pfam17823  111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAP---------RAAACRANASAAPRAAIAAASAPHAASPAPRTAASS 181
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530407637   905 AAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTP-LSQAAASIDNRVPTPSSVASA 966
Cdd:pfam17823  182 TTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPaAGTALAAVGNSSPAAGTVTAA 244
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1690-1718 3.62e-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: 40.35  E-value: 3.62e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 530407637 1690 YTCNECKHHV--ETRWHCTVCEDYDLCINCY 1718
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
792-993 4.34e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  792 SVGMGQPPAqtGVSQGQVPGAAlpnplnmlgPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPpgmtppqpAAPT 871
Cdd:PRK07003  361 AVTGGGAPG--GGVPARVAGAV---------PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA--------AAAT 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  872 QPSTPVSSSGQTPTPT----PGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSvATPQSSQQQPTPVHAQPPGTPLS 947
Cdd:PRK07003  422 RAEAPPAAPAPPATADrgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSA-SAPASDAPPDAAFEPAPRAAAPS 500
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 530407637  948 QAAAsidNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEP 993
Cdd:PRK07003  501 AATP---AAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
680-1034 5.79e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  680 GNQPALPAPGAQPPVIPQAQPVRPPRMnsfnpmslGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPN 759
Cdd:PRK07764  384 RLGVAGGAGAPAAAAPSAAAAAPAAAP--------APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPS 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  760 MMGAHTNNMMAQ-APAQSQFLPQNQFPSSSGAM-SVGMGQPPAQTGVSQGQVPGAAL----PNPLNMLG----------- 822
Cdd:PRK07764  456 PPPAAAPSAQPApAPAAAPEPTAAPAPAPPAAPaPAAAPAAPAAPAAPAGADDAATLrerwPEILAAVPkrsrktwaill 535
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  823 PQASQLPcppVTQSPL---HPTPPPAS---------------------------TAAGMP-SLQHTTPPGMTPPQPAAPT 871
Cdd:PRK07764  536 PEATVLG---VRGDTLvlgFSTGGLARrfaspgnaevlvtalaeelggdwqveaVVGPAPgAAGGEGPPAPASSGPPEEA 612
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  872 QPSTPVSSSGQTPTPTPGSVPSATQTQST--------PTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPG 943
Cdd:PRK07764  613 ARPAAPAAPAAPAAPAPAGAAAAPAEASAapapgvaaPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA 692
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  944 TPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAE-------DTEPDPGESKGEPRSEMMEEDLQGASQ 1016
Cdd:PRK07764  693 PAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvplppepDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
                         410
                  ....*....|....*...
gi 530407637 1017 VKEETDIAEQksEPMEVD 1034
Cdd:PRK07764  773 APPPSPPSEE--EEMAED 788
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
823-1012 5.81e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 45.08  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  823 PQASQLPcPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPvsSSGQTPTPTPGSVPSATQTQSTPT 902
Cdd:PRK08691  388 ETAAKKP-QPRPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWEDAP--DEAQTAAGTAQTSAKSIQTASEAE 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  903 VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPD-VPVL 980
Cdd:PRK08691  465 TPPENQVSKNKAADNETDAPLSEVPSENPIQATPNdEAVETETFAHEAPAEPFYGYGFPDNDCPPEDGAEIPPPDwEHAA 544
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530407637  981 EMKTETQAEDTEPDPGESKG-----EPRSEMMEEDLQ 1012
Cdd:PRK08691  545 PADTAGGGADEEAEAGGIGGnntpsAPPPEFSTENWA 581
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
780-1030 6.68e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.95  E-value: 6.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   780 PQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNP--LNMLGPQAsQLPCPPVTQSPLHPTPPPASTAAGMPSLQHT 857
Cdd:pfam17823  100 PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALpsEAFSAPRA-AACRANASAAPRAAIAAASAPHAASPAPRTA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   858 TPPGMTPPQPAAPTQPSTPVSSSG-QTPTPTPGSVPSATQTqSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP 936
Cdd:pfam17823  179 ASSTTAASSTTAASSAPTTAASSApATLTPARGISTAATAT-GHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   937 VHAQppgtPLSQAAASID-----NRVPTPSSVASAETNSQQPGPDV------PVLEMKTETQAEDTEPDPGESKGEPRSE 1005
Cdd:pfam17823  258 AAAG----TVASAAGTINmgdphARRLSPAKHMPSDTMARNPAAPMgaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTLE 333
                          250       260
                   ....*....|....*....|....*
gi 530407637  1006 MMEEDLQGASQVKEETDIAEQKSEP 1030
Cdd:pfam17823  334 PNTPKSVASTNLAVVTTTKAQAKEP 358
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
774-971 1.38e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   774 AQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPnplnmlgPQASQLPCPPVT---QSP-LHPT--PPPAST 847
Cdd:pfam03154  176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQP-------PNQTQSTAAPHTliqQTPtLHPQrlPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   848 AAGMPSlqhTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATP 927
Cdd:pfam03154  249 LQPMTQ---PPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRI 325
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 530407637   928 QSSQQQPTPVHAQPP-GTPLSQAAASIDNRVPTPSSVASAETNSQ 971
Cdd:pfam03154  326 HTPPSQSQLQSQQPPrEQPLPPAPLSMPHIKPPPTTPIPQLPNPQ 370
PHA03378 PHA03378
EBNA-3B; Provisional
682-887 1.86e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  682 QPALPAPGAQPPviPQAQPVR---------PPRMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPS 752
Cdd:PHA03378  695 QPPPRAPTPMRP--PAAPPGRaqrpaaatgRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG 772
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  753 R-MPQPPNMMGAHTNNMMAQAPAqsqflPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVpgAALPNPLNMLGPQASQLPCP 831
Cdd:PHA03378  773 ApTPQPPPQAPPAPQQRPRGAPT-----PQPPPQAGPTSMQLMPRAAPGQQGPTKQIL--RQLLTGGVKRGRPSLKKPAA 845
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530407637  832 PVTQSPLHPTPPPAS-TAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPT 887
Cdd:PHA03378  846 LERQAAAGPTPSPGSgTSDKIVQAPVFYPPVLQPIQVMRQLGSVRAAAASTVTQAPT 902
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1691-1723 1.96e-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: 37.95  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530407637 1691 TCNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1723
Cdd:cd02344     2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKH 36
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
676-952 2.91e-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: 43.07  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   676 QGILGNQPALPAPGAQPPVIPQAQPVRP----PRMNSFNPMSLGNVQLPQAPMGPRAASPM---NHSVQMNSMGSVPGMA 748
Cdd:pfam09606  144 SRVGRMQPGGQAGGMMQPSSGQPGSGTPnqmgPNGGPGQGQAGGMNGGQQGPMGGQMPPQMgvpGMPGPADAGAQMGQQA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   749 ISPSRMPqPPNMMGAHTNNMMAQAPAQSQfLPQNQFPSSSGAMS-----VGMGQP---PAQTGVSQGQVPGA-------- 812
Cdd:pfam09606  224 QANGGMN-PQQMGGAPNQVAMQQQQPQQQ-GQQSQLGMGINQMQqmpqgVGGGAGqggPGQPMGPPGQQPGAmpnvmsig 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   813 -----------------------ALPNPLNMLGPQASQLPCPPvTQSPLHPTPPPASTAAGMPSLQHTtPPGMTPPQPAA 869
Cdd:pfam09606  302 dqnnyqqqqtrqqqqqqggnhpaAHQQQMNQSVGQGGQVVALG-GLNHLETWNPGNFGGLGANPMQRG-QPGMMSSPSPV 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   870 PTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQA 949
Cdd:pfam09606  380 PGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSA 459

                   ...
gi 530407637   950 AAS 952
Cdd:pfam09606  460 VNS 462
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
785-995 2.94e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  785 PSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQ-ASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMT 863
Cdd:PRK07003  374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKaAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKA 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  864 PPQ----PAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSV-------ATPQSSQQ 932
Cdd:PRK07003  454 NARasadSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRedapaaaAPPAPEAR 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  933 QPTPVHAQPPGTPlSQAAASID------NRV-----------PTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDP 995
Cdd:PRK07003  534 PPTPAAAAPAARA-GGAAAALDvlrnagMRVssdrgaraaaaAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNG 612
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
1690-1719 2.98e-03

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


Pssm-ID: 239076  Cd Length: 45  Bit Score: 37.68  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 530407637 1690 YTCNEC-KHHVETRWHCTVCEDYDLCINCYN 1719
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ 31
PHA03378 PHA03378
EBNA-3B; Provisional
685-961 3.30e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  685 LPAPGAQPPVIpqaQPVRPPRMNSFNPMSLGNVQLP-------QAPMGP--RAASPMNHSVQMNSMGSVPGMAISPSRMP 755
Cdd:PHA03378  564 LPAPGLGPLQI---QPLTSPTTSQLASSAPSYAQTPwpvphpsQTPEPPttQSHIPETSAPRQWPMPLRPIPMRPLRMQP 640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  756 QPPNMMGAHTNNMMAQAP--------AQSQFLPQNQFPSSSGAM-----SVGMGQPPAQtgvSQGQVPGAALPnPLNMLG 822
Cdd:PHA03378  641 ITFNVLVFPTPHQPPQVEitpykptwTQIGHIPYQPSPTGANTMlpiqwAPGTMQPPPR---APTPMRPPAAP-PGRAQR 716
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  823 PQASQLPCPPVTQSPLHPTPPPASTAAGMPSlqhTTPPGMTPPQPAAPTQPSTPVSSSGQ-TPTPTPGSVPSATQT-QST 900
Cdd:PHA03378  717 PAAATGRARPPAAAPGRARPPAAAPGRARPP---AAAPGRARPPAAAPGRARPPAAAPGApTPQPPPQAPPAPQQRpRGA 793
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530407637  901 PTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNR---VPTPS 961
Cdd:PHA03378  794 PTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQaaaGPTPS 857
PHA03247 PHA03247
large tegument protein UL36; Provisional
684-993 4.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  684 ALPAPGAQPPVI----PQAQPVrPPRM----NSFNPMSLGNVQLPQAPMGPRAASPmnhsvqmnsmgsVPGMAISPSRMP 755
Cdd:PHA03247 2508 APPAPSRLAPAIlpdePVGEPV-HPRMltwiRGLEELASDDAGDPPPPLPPAAPPA------------APDRSVPPPRPA 2574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  756 QPPNMMGAHTNNMMAQAPaqsqflPQNQFPSSSGAMSvgmGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQ 835
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAP------PQSARPRAPVDDR---GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT 2645
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  836 SPLHPTPPPAStAAGMPSLQHTTPPGMTPPQPAAPTQPST---------PVSSSGQTPTPTPGSVPSATQTQS---TPTV 903
Cdd:PHA03247 2646 VPPPERPRDDP-APGRVSRPRRARRLGRAAQASSPPQRPRrraarptvgSLTSLADPPPPPPTPEPAPHALVSatpLPPG 2724
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  904 QAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQA-----AASIDNRVPTPSSVASAETNSQQPGPDVP 978
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAppaapAAGPPRRLTRPAVASLSESRESLPSPWDP 2804
                         330
                  ....*....|....*
gi 530407637  979 VLEMKTETQAEDTEP 993
Cdd:PHA03247 2805 ADPPAAVLAPAAALP 2819
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
680-910 4.63e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  680 GNQPALPAPGAQPPVIPQAQPVRPPRMNSFNPMSLGNVQL-PQAPMGPRAASPMnhsvqmnsmgsVPGMAISPSRMPQPP 758
Cdd:PRK07003  365 GGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGaAGAALAPKAAAAA-----------AATRAEAPPAAPAPP 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  759 NMMGAHTNNMMAQAPAQS----------QFLPQNQFPSSSGAMSVG--MGQPPA---QTGVSQGQVPGAALPNPLNMLGP 823
Cdd:PRK07003  434 ATADRGDDAADGDAPVPAkanarasadsRCDERDAQPPADSGSASApaSDAPPDaafEPAPRAAAPSAATPAAVPDARAP 513
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637  824 QASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHT---------------------TPPGMTPPQPAAPTQPSTPVSSSGQ 882
Cdd:PRK07003  514 AAASREDAPAAAAPPAPEARPPTPAAAAPAARAGgaaaaldvlrnagmrvssdrgARAAAAAKPAAAPAAAPKPAAPRVA 593
                         250       260       270
                  ....*....|....*....|....*....|
gi 530407637  883 TPTPTPGSVPSATQTQSTPTVQA--AAQAQ 910
Cdd:PRK07003  594 VQVPTPRARAATGDAPPNGAARAeqAAESR 623
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1691-1722 5.23e-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: 36.94  E-value: 5.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530407637 1691 TCNECKHHVET--RWHCTVCEDYDLCINCYNTKS 1722
Cdd:cd02338     2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGV 35
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
831-1005 6.48e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   831 PPVTQSPLHPTPPPASTAAGMPSLQHTTPPgmtppqPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTV--QAAAQ 908
Cdd:pfam03154  171 PPVLQAQSGAASPPSPPPPGTTQAATAGPT------PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLhpQRLPS 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   909 AQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPT-PSSVASAETNSQQPGPDVPVLEMKTETQ 987
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
                          170
                   ....*....|....*...
gi 530407637   988 AEDTEPDPGESKGEPRSE 1005
Cdd:pfam03154  325 IHTPPSQSQLQSQQPPRE 342
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
686-862 6.49e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.95  E-value: 6.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   686 PAPGAQPPVIPQAQPVRPPrmnsfnpmslGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPpnmmgaht 765
Cdd:pfam09770  208 KKPAQQPAPAPAQPPAAPP----------AQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRP-------- 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407637   766 nnmmaqapaQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQgqvpgaALPNPlNMLGPQ---ASQLPCPPVTQSPLHPTP 842
Cdd:pfam09770  270 ---------QSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQ------ILQNP-NRLSAArvgYPQNPQPGVQPAPAHQAH 333
                          170       180
                   ....*....|....*....|
gi 530407637   843 PPASTAAGMPSLqHTTPPGM 862
Cdd:pfam09770  334 RQQGSFGRQAPI-ITHPQQL 352
 
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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