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Conserved domains on  [gi|119943102|ref|NP_001073315|]
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CREB-binding protein isoform b [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 ...
1304-1611 6.48e-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: 6.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1459 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1514 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1568
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 119943102  1569 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1611
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.70e-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: 1.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1128
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 119943102 1129 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1156
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
549-629 1.10e-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: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   549 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 628
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 119943102   629 E 629
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 2.49e-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: 2.49e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943102 1168 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1240
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1667-1707 7.54e-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: 7.54e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119943102 1667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1707
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 ...
1734-1802 1.54e-24

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.54e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943102  1734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1975-2076 1.58e-19

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: 86.04  E-value: 1.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1975 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 119943102  2044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1242-1273 9.29e-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: 9.29e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119943102 1242 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1273
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-405 4.61e-11

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: 60.48  E-value: 4.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 119943102   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 405
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
PHA03247 super family cl33720
large tegument protein UL36; Provisional
645-987 1.20e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  645 PALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGM 724
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  725 AISPSRMPQPPnmmgahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQ 804
Cdd:PHA03247 2829 PPPTSAQPTAP--------------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRR 2885
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  805 LPCPPVTQSPlHPTPPPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAA 884
Cdd:PHA03247 2886 LARPAVSRST-ESFALPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  885 QAQVTPQPQTPVQPPSVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQ 964
Cdd:PHA03247 2956 SGAVPQPWLGALVPGRVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWP 3030
                         330       340
                  ....*....|....*....|...
gi 119943102  965 AEDTEPDPGESKGEPRSEMMEED 987
Cdd:PHA03247 3031 PDDTEDSDADSLFDSDSERSDLE 3053
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2072-2385 1.53e-05

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2072 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2134
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2135 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2214
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2215 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2291
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2292 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2371
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 119943102  2372 PQLNtPSRSALSSE 2385
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 ...
1304-1611 6.48e-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: 6.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1459 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1514 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1568
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 119943102  1569 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1611
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.70e-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: 1.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1128
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 119943102 1129 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1156
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
549-629 1.10e-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: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   549 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 628
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 119943102   629 E 629
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1046-1154 7.68e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.68e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   1046 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1125
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 119943102   1126 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1154
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 2.49e-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: 2.49e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943102 1168 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1240
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1667-1707 7.54e-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: 7.54e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119943102 1667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1707
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 ...
1734-1802 1.54e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.54e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943102  1734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1154-1193 2.72e-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: 97.01  E-value: 2.72e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 119943102  1154 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1193
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1728-1806 5.12e-24

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 97.44  E-value: 5.12e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   1728 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1803
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 119943102   1804 FCL 1806
Cdd:smart00551   77 KCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1975-2076 1.58e-19

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: 86.04  E-value: 1.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1975 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 119943102  2044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1066-1138 5.01e-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: 5.01e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943102  1066 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1138
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1242-1273 9.29e-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: 9.29e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119943102 1242 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1273
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1663-1705 4.28e-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: 4.28e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 119943102   1663 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHKMV 1705
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1663-1704 1.38e-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: 72.52  E-value: 1.38e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119943102  1663 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHAHKM 1704
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1037-1155 7.69e-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: 7.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1037 TSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYV 1116
Cdd:COG5076   134 KTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFV 210
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119943102 1117 DDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 1155
Cdd:COG5076   211 SDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-405 4.61e-11

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: 60.48  E-value: 4.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 119943102   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 405
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
645-987 1.20e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  645 PALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGM 724
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  725 AISPSRMPQPPnmmgahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQ 804
Cdd:PHA03247 2829 PPPTSAQPTAP--------------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRR 2885
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  805 LPCPPVTQSPlHPTPPPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAA 884
Cdd:PHA03247 2886 LARPAVSRST-ESFALPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  885 QAQVTPQPQTPVQPPSVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQ 964
Cdd:PHA03247 2956 SGAVPQPWLGALVPGRVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWP 3030
                         330       340
                  ....*....|....*....|...
gi 119943102  965 AEDTEPDPGESKGEPRSEMMEED 987
Cdd:PHA03247 3031 PDDTEDSDADSLFDSDSERSDLE 3053
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2028-2070 1.70e-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: 54.97  E-value: 1.70e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 119943102 2028 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2070
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
645-971 1.22e-07

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: 57.47  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   645 PALPaPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVS-----------QGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSV 713
Cdd:pfam03154  204 PSVP-PQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSL 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   714 QMnsmgsvpgmaiSPSRMPQPPNMMGAHTNNMMAQapAQSQFLPQNQFPSSSGAMSVgmgQPPAQTGVSQGQ------VP 787
Cdd:pfam03154  283 QT-----------GPSHMQHPVPPQPFPLTPQSSQ--SQVPPGPSPAAPGQSQQRIH---TPPSQSQLQSQQppreqpLP 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   788 GAALPNPlNMLGPQASQLPCPPVTQSPLHPT----PPPASTAAGMPSLQHTTP-PGMTPPQPAAPTQPSTPVSSSGQTPT 862
Cdd:pfam03154  347 PAPLSMP-HIKPPPTTPIPQLPNPQSHKHPPhlsgPSPFQMNSNLPPPPALKPlSSLSTHHPPSAHPPPLQLMPQSQQLP 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   863 PTPGSVPSATQTQSTPTvqAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVhAQPPGTPLSQAAASIDNRVPTPSSVAS 942
Cdd:pfam03154  426 PPPAQPPVLTQSQSLPP--PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPI-TPPSGPPTSTSSAMPGIQPPSSASVSS 502
                          330       340
                   ....*....|....*....|....*....
gi 119943102   943 AETNSQQPGPDVPVLEMKTETQAEDTEPD 971
Cdd:pfam03154  503 SGPVPAAVSCPLPPVQIKEEALDEAEEPE 531
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
363-402 1.21e-05

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 45.43  E-value: 1.21e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 119943102    363 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGK 402
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2072-2385 1.53e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2072 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2134
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2135 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2214
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2215 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2291
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2292 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2371
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 119943102  2372 PQLNtPSRSALSSE 2385
Cdd:pfam09606  462 SPLN-PQEEQLYRE 474
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
688-1007 2.67e-05

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 49.66  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  688 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPG-MAISPSRMPQPPNMMGAHT-NNMMAQAPAQSQFLPQNQFPSSS 765
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNAVDYSVlVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  766 GAMSVGMGQPPAQTGVSQGQVPGAALPNPLnmlGPQASQLPCppvTQSPLHPTPPPASTAagmPSLQHttpPGMTPPQPA 845
Cdd:COG5665   219 SGRSQHIVQAAKRVGVEWWGDPSLLATPPA---TPATEEKSS---QQPKSQPTSPSGGTT---PPSTN---QLTTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  846 APTQPSTPVSSSGQTPTPTP-------GSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQ 917
Cdd:COG5665   287 STAKAQPQPPTKKQPAKEPPsdtasgnPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTPAtDLA 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  918 PPGTPLSQAAASIDNRVP--------------TPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEM 983
Cdd:COG5665   367 TPVSPTPPETSVDKKVSPdsatsstksekeggTASSPMPPNIAIGAKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSV 446
                         330       340
                  ....*....|....*....|....
gi 119943102  984 MEEDLQGASQVKEETDIAEQKSEP 1007
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAP 470
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
629-762 2.01e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   629 EKRRSRLHKQgILGNQPALPAPGAQPPVIPQ--AQPVRPPNG-------PLSLPVNRMQVSQGMNSFNPMSLGNVQLPQA 699
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPMGSPMGGAmgQPPYYGQGPqqqfngqPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943102   700 PMGPRAASPMNHSVQMNSMGSVPGMAISPS--RMPQPPNMMGAHTNN-----MMAQAPA--QSQFLPQNQFP 762
Cdd:TIGR01628  444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLsqDLPQPQSTASQGGQNkklaqVLASATPqmQKQVLGERLFP 515
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1304-1611 6.48e-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: 6.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1459 KRLQEWYKKMLDKAFAE-------RIIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1514 SIkeleqeEEERKKEESTAASETT---------------EGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKK 1568
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEElrfrqefslgrlvgfIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYST 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 119943102  1569 KPSMPNVSNDLSQKLYATMEKHkevFFVIHLHAGPVINTLPPI 1611
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.70e-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: 1.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1128
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 119943102 1129 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1156
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
549-629 1.10e-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: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   549 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 628
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 119943102   629 E 629
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1046-1154 7.68e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.68e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   1046 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1125
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 119943102   1126 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1154
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 2.49e-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: 2.49e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943102 1168 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKNDTLDPE 1240
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1052-1151 2.83e-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: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1052 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1130
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 119943102 1131 RKTSRVYKFCSKLAEVFEQEI 1151
Cdd:cd04369    79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1072-1149 7.34e-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: 118.15  E-value: 7.34e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943102 1072 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1149
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1667-1707 7.54e-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: 7.54e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119943102 1667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKW 1707
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1051-1151 1.27e-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: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1051 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1130
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|.
gi 119943102 1131 RKTSRVYKFCSKLAEVFEQEI 1151
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1065-1148 1.64e-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: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1065 RQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1144
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                  ....
gi 119943102 1145 EVFE 1148
Cdd:cd05506    93 KIFE 96
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1734-1802 1.54e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.54e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943102  1734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1154-1193 2.72e-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: 97.01  E-value: 2.72e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 119943102  1154 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1193
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1728-1806 5.12e-24

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 97.44  E-value: 5.12e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   1728 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1803
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 119943102   1804 FCL 1806
Cdd:smart00551   77 KCV 79
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1059-1151 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 119943102 1059 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1138
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                          90
                  ....*....|...
gi 119943102 1139 FCSKLAEVFEQEI 1151
Cdd:cd05500    91 MGKRLQAAFEKHL 103
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1054-1153 1.63e-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: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1054 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1132
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                          90       100
                  ....*....|....*....|.
gi 119943102 1133 TSRVYKFCSKLAEVFEQEIDP 1153
Cdd:cd05497    86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1047-1149 3.49e-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: 3.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1047 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKNPMDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 1123
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                          90       100
                  ....*....|....*....|....*.
gi 119943102 1124 NNAWLYNRKTSRVYKFCSKLAEVFEQ 1149
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 ...
1069-1167 8.84e-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: 8.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1069 ESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKFCSKLAEVF 1147
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                          90       100
                  ....*....|....*....|
gi 119943102 1148 EQEIDPVMQSlgYCCGRKYE 1167
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 ...
1072-1148 1.60e-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: 1.60e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119943102 1072 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFE 1148
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1975-2076 1.58e-19

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: 86.04  E-value: 1.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  1975 MPSMPPGQWQQAPLPQQQPmpGLPRPVISMQAQAAVAG---PRMPSVQP--------PRSISPSALQDLLRTLKSPSSPQ 2043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 119943102  2044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1050-1150 2.78e-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: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1050 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMF 1123
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                          90       100
                  ....*....|....*....|....*..
gi 119943102 1124 NNAWLYNRKTSRVYKFCSKLAEVFEQE 1150
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1066-1138 5.01e-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: 5.01e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943102  1066 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1138
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1242-1273 9.29e-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: 9.29e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119943102 1242 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1273
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1241-1275 4.56e-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: 79.26  E-value: 4.56e-18
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119943102 1241 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1275
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 ...
1050-1140 3.24e-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: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1050 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1129
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                          90
                  ....*....|.
gi 119943102 1130 NRKTSRVYKFC 1140
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1663-1705 4.28e-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: 4.28e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 119943102   1663 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHKMV 1705
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1242-1275 4.80e-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: 4.80e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119943102 1242 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1275
Cdd:cd15646     7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1055-1145 1.11e-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: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1055 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1134
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                          90
                  ....*....|.
gi 119943102 1135 RVYKFCSKLAE 1145
Cdd:cd05512    82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1068-1136 1.21e-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: 1.21e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1068 PESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 1136
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1663-1704 1.38e-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: 72.52  E-value: 1.38e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119943102  1663 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHAHKM 1704
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1065-1160 5.05e-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: 5.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1065 RQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1144
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEML 90
                          90
                  ....*....|....*.
gi 119943102 1145 EVFEQEIDPVMQSLGY 1160
Cdd:cd05511    91 ELAEELLAEREEKLTQ 106
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1037-1155 7.69e-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: 7.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1037 TSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYV 1116
Cdd:COG5076   134 KTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFV 210
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119943102 1117 DDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 1155
Cdd:COG5076   211 SDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1085-1138 9.95e-15

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: 9.95e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1138
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1066-1153 1.39e-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: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1066 QDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN------RKTSRvYKF 1139
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                          90
                  ....*....|....*..
gi 119943102 1140 CSKLAEV---FEQEIDP 1153
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1085-1156 2.39e-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: 2.39e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1156
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1667-1703 5.11e-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: 5.11e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119943102 1667 YTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHAHK 1703
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1198-1273 9.29e-14

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: 68.15  E-value: 9.29e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1198 FCEKCFTEIQGENVTLGddpsqpQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHY---DIIWPSGFVCDNC 1273
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNgrrNADETAEYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1053-1138 4.13e-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: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1053 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1132
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSS 81

                  ....*.
gi 119943102 1133 TSRVYK 1138
Cdd:cd05507    82 DHDVYL 87
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1048-1147 1.37e-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: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1048 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1127
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                          90       100
                  ....*....|....*....|
gi 119943102 1128 LYNRKTSRVYKFCSKLAEVF 1147
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1052-1143 2.49e-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: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1052 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1131
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                          90
                  ....*....|..
gi 119943102 1132 KTSRVYKFCSKL 1143
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 ...
1051-1139 1.11e-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: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1051 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKNPMDLSTIKRKLDtgQYQEPWQYVDDVW 1120
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                          90
                  ....*....|....*....
gi 119943102 1121 LMFNNAWLYNRKTSRVYKF 1139
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 ...
1085-1138 2.75e-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: 2.75e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1138
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYK 91
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
363-405 4.61e-11

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: 60.48  E-value: 4.61e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 119943102   363 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 405
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1085-1143 4.95e-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: 4.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 1143
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1084-1152 1.02e-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: 1.02e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1084 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEID 1152
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1052-1151 3.36e-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: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1052 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNA 1126
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                          90       100
                  ....*....|....*....|....*
gi 119943102 1127 WLYNRKTSRVYKFCSKLAEVFEQEI 1151
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1074-1137 4.35e-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: 4.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1074 RQPVD-----PQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 1137
Cdd:cd05518    21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
645-987 1.20e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  645 PALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGM 724
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  725 AISPSRMPQPPnmmgahtnnmmaqaPAQSQFLPqnqfPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPlnmlgPQASQ 804
Cdd:PHA03247 2829 PPPTSAQPTAP--------------PPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR-----PPVRR 2885
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  805 LPCPPVTQSPlHPTPPPASTAAGMPSLQHTTPPgmtppqpaaPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAA 884
Cdd:PHA03247 2886 LARPAVSRST-ESFALPPDQPERPPQPQAPPPP---------QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  885 QAQVTPQPQTPVQPPSVATPQSSQQQPTPvhaqPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDvPVLEMKTETQ 964
Cdd:PHA03247 2956 SGAVPQPWLGALVPGRVAVPRFRVPQPAP----SREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP-PVSLKQTLWP 3030
                         330       340
                  ....*....|....*....|...
gi 119943102  965 AEDTEPDPGESKGEPRSEMMEED 987
Cdd:PHA03247 3031 PDDTEDSDADSLFDSDSERSDLE 3053
PHA03247 PHA03247
large tegument protein UL36; Provisional
645-955 1.60e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.80  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  645 PALPAPGAQPPV-----IPQAQPVRPPNGPlslpvnrmqvSQGMNSFNPMSLGNVQLPQAPMGPRAASPmnhsvqmnsmG 719
Cdd:PHA03247 2551 PPPPLPPAAPPAapdrsVPPPRPAPRPSEP----------AVTSRARRPDAPPQSARPRAPVDDRGDPR----------G 2610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  720 SVPGMAISPS--RMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSV-----GMGQPPAQTGVSQGQVPGAALP 792
Cdd:PHA03247 2611 PAPPSPLPPDthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARP 2690
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  793 NplnmLGPQASQLPCPPvtqSPLHPTPPPASTAAGMPslqhtTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSV--PS 870
Cdd:PHA03247 2691 T----VGSLTSLADPPP---PPPTPEPAPHALVSATP-----LPPGPAAARQASPALPAAPAPPAVPAGPATPGGParPA 2758
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  871 ATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIdNRVPTPSSVASAETNSQQP 950
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL-PPAASPAGPLPPPTSAQPT 2837

                  ....*
gi 119943102  951 GPDVP 955
Cdd:PHA03247 2838 APPPP 2842
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2028-2070 1.70e-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: 54.97  E-value: 1.70e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 119943102 2028 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2070
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 ...
1050-1151 1.73e-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: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1050 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1127
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                          90       100
                  ....*....|....*....|....
gi 119943102 1128 LYNRKTSRVYKFCSKLAEVFEQEI 1151
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 ...
1668-1706 2.00e-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: 2.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119943102 1668 TCNECKHHVE-TRWHCTVCEDYDLCINCYNTKSHA-HKMVK 1706
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHPeHAMLK 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
631-981 1.02e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.11  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  631 RRSRLHKQGILGNQPALPA--------PGAQPPVIPQAQPVRPPN-GPLSLPVNRMQVSQGMNSFNPMSLGNVQ--LPQA 699
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASsppqrprrRAARPTVGSLTSLADPPPpPPTPEPAPHALVSATPLPPGPAAARQASpaLPAA 2738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  700 PMGPRAASPMNHSVQMNSMGSVPGMAISPSrmPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQT 779
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  780 GVSQGQVPGAALPNPlnmlgPQASQLPcPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPstPVSSSGQ 859
Cdd:PHA03247 2817 ALPPAASPAGPLPPP-----TSAQPTA-PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP--PVRRLAR 2888
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  860 TPtptpgsVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAAsidnrVPTPSS 939
Cdd:PHA03247 2889 PA------VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-----AGEPSG 2957
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 119943102  940 VASAETNSQQPGPDVPVLEMKTeTQAEDTEPDPGESKGEPRS 981
Cdd:PHA03247 2958 AVPQPWLGALVPGRVAVPRFRV-PQPAPSREAPASSTPPLTG 2998
PHA03247 PHA03247
large tegument protein UL36; Provisional
644-981 4.26e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  644 QPALPAPGAQPPVIPQAQPVRPPNGPLSLPvnrmqvsqgmnsfnPMSLGNVQLPQAPMGPR--AASPMNHSVQMNSMGSV 721
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDP--------------RGPAPPSPLPPDTHAPDppPPSPSPAANEPDPHPPP 2644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  722 PGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSgamsvgmgqPPAQTGVSQGQVPGAALPNPLNMLGPQ 801
Cdd:PHA03247 2645 TVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA---------RPTVGSLTSLADPPPPPPTPEPAPHAL 2715
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  802 ASQLPCPPVTQS--------PLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPG-----SV 868
Cdd:PHA03247 2716 VSATPLPPGPAAarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslseSR 2795
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  869 PSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAA-----SIDNRVPTPSSVASA 943
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKP 2875
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 119943102  944 ETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRS 981
Cdd:PHA03247 2876 AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
PHA03247 PHA03247
large tegument protein UL36; Provisional
642-979 4.33e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  642 GNQPALPAPGAQPPVIPQAQPvrPPNGPLSLPvnrmqvSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQmnsmgSV 721
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDP--PPPSPSPAA------NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL-----GR 2672
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  722 PGMAISPSRMPQPPNM---MGAHTNNMMAQAP---------AQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQV-PG 788
Cdd:PHA03247 2673 AAQASSPPQRPRRRAArptVGSLTSLADPPPPpptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtPG 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  789 --AALPNPLNMLGPQASQLPCPPVTqsplhpTPPPASTAAGMPSLQHTTPPGMTPPQPAAPtqpstPVSSSGQTPTPTPG 866
Cdd:PHA03247 2753 gpARPARPPTTAGPPAPAPPAAPAA------GPPRRLTRPAVASLSESRESLPSPWDPADP-----PAAVLAPAAALPPA 2821
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  867 SVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvhAQPPGTPLSQAAASIdNRVPTPSSVASAETN 946
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPS--RSPAAKPAAPARPPV-RRLARPAVSRSTESF 2898
                         330       340       350
                  ....*....|....*....|....*....|...
gi 119943102  947 SQQPGPDVPVLEMKTETQAEDTEPDPGESKGEP 979
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1085-1149 6.29e-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: 6.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1149
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
645-971 1.22e-07

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: 57.47  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   645 PALPaPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVS-----------QGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSV 713
Cdd:pfam03154  204 PSVP-PQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSL 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   714 QMnsmgsvpgmaiSPSRMPQPPNMMGAHTNNMMAQapAQSQFLPQNQFPSSSGAMSVgmgQPPAQTGVSQGQ------VP 787
Cdd:pfam03154  283 QT-----------GPSHMQHPVPPQPFPLTPQSSQ--SQVPPGPSPAAPGQSQQRIH---TPPSQSQLQSQQppreqpLP 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   788 GAALPNPlNMLGPQASQLPCPPVTQSPLHPT----PPPASTAAGMPSLQHTTP-PGMTPPQPAAPTQPSTPVSSSGQTPT 862
Cdd:pfam03154  347 PAPLSMP-HIKPPPTTPIPQLPNPQSHKHPPhlsgPSPFQMNSNLPPPPALKPlSSLSTHHPPSAHPPPLQLMPQSQQLP 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   863 PTPGSVPSATQTQSTPTvqAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVhAQPPGTPLSQAAASIDNRVPTPSSVAS 942
Cdd:pfam03154  426 PPPAQPPVLTQSQSLPP--PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPI-TPPSGPPTSTSSAMPGIQPPSSASVSS 502
                          330       340
                   ....*....|....*....|....*....
gi 119943102   943 AETNSQQPGPDVPVLEMKTETQAEDTEPD 971
Cdd:pfam03154  503 SGPVPAAVSCPLPPVQIKEEALDEAEEPE 531
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1085-1149 1.94e-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: 1.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943102 1085 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1149
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
646-985 4.80e-07

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: 55.54  E-value: 4.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   646 ALPAPGAqPPVIPQAQPV--RPPNGPLSlPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMN---------HSVQ 714
Cdd:pfam03154  197 AGPTPSA-PSVPPQGSPAtsQPPNQTQS-TAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVspqplpqpsLHGQ 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   715 MNSMGSvpGMAISPSRMPQPPNMMGAHTNNMMAQApaQSQFLPQNQFPSSSGAMSVgmgQPPAQTGVSQGQ------VPG 788
Cdd:pfam03154  275 MPPMPH--SLQTGPSHMQHPVPPQPFPLTPQSSQS--QVPPGPSPAAPGQSQQRIH---TPPSQSQLQSQQppreqpLPP 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   789 AALPNPlNMLGPQASQLPCPPVTQSPLHPT----PPPASTAAGMPSLQHTTP-PGMTPPQPAAPTQPSTPVSSSGQTPTP 863
Cdd:pfam03154  348 APLSMP-HIKPPPTTPIPQLPNPQSHKHPPhlsgPSPFQMNSNLPPPPALKPlSSLSTHHPPSAHPPPLQLMPQSQQLPP 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   864 TPGSVPSATQTQSTPTVQAAAqaqvtpqpqtpvqPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASidnrvPTPSSVASA 943
Cdd:pfam03154  427 PPAQPPVLTQSQSLPPPAASH-------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSA 488
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 119943102   944 ETNSQQPGPDVPVLEMKTETQAEDTEPdPGESKGEPRSEMME 985
Cdd:pfam03154  489 MPGIQPPSSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEE 529
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
429-909 7.27e-07

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: 54.77  E-value: 7.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   429 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTdQQPPNLI 508
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-SQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   509 SESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 588
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   589 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPAPGAQ----PPVIPQAQPVR 664
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQrihtPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   665 PPNGPLSLPVnrmqvsqgmnsfnPMSLGNVQLPQAPMGPRAASPMNHsvQMNSMGSVPGMAISPSRMPQPPNMM---GAH 741
Cdd:pfam03154  339 PPREQPLPPA-------------PLSMPHIKPPPTTPIPQLPNPQSH--KHPPHLSGPSPFQMNSNLPPPPALKplsSLS 403
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   742 TNNMMAQAPAQSQFLPQNQFPSSSGAmsvgmgQPPAQTGVSQGQVPGAALPNPlNMLGPQASQLPCPPVTQSPLHPTP-- 819
Cdd:pfam03154  404 THHPPSAHPPPLQLMPQSQQLPPPPA------QPPVLTQSQSLPPPAASHPPT-SGLHQVPSQSPFPQHPFVPGGPPPit 476
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   820 ----PPASTAAGMPSLQhttPPgmtppqpaaptqPSTPVSSSGQTPTPTPGSVPsATQTQSTPTVQAAAQAQVTPQPQTP 895
Cdd:pfam03154  477 ppsgPPTSTSSAMPGIQ---PP------------SSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEEPESPPPPPRSP 540
                          490
                   ....*....|....*
gi 119943102   896 VQPPSVA-TPQSSQQ 909
Cdd:pfam03154  541 SPEPTVVnTPSHASQ 555
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1050-1107 8.63e-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: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102 1050 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKNPMDLSTI-KRKLDTG 1107
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
799-992 1.64e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.45  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  799 GPQASQLPCPPVTQSplHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTP-------VSSSGQTPTPTPGSVPSA 871
Cdd:PRK07764  599 GPPAPASSGPPEEAA--RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEhhpkhvaVPDASDGGDGWPAKAGGA 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  872 TQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPG 951
Cdd:PRK07764  677 APAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 119943102  952 PDVPVLEMKTETQAEDTepdPGESKGEPRSEMMEEDLQGAS 992
Cdd:PRK07764  757 QPPPPPAPAPAAAPAAA---PPPSPPSEEEEMAEDDAPSMD 794
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
776-981 2.79e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.96  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  776 PAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVS 855
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  856 SSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSS-------QQQPTPVHAQPPGTPLSQAAA 928
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPppweelpPEFASPAPAQPDAAPAGWVAE 524
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119943102  929 SIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRS 981
Cdd:PRK12323  525 SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMF 577
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1050-1151 3.41e-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: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102 1050 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1129
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                          90       100
                  ....*....|....*....|..
gi 119943102 1130 NRKTSRVYKFCSKLAEVFEQEI 1151
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1084-1149 4.50e-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: 4.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119943102 1084 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKFCSKLAEVFEQ 1149
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
363-402 1.21e-05

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 45.43  E-value: 1.21e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 119943102    363 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGK 402
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2072-2385 1.53e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2072 ANQPGMQPQPGLQSQP--GMQPQPGMHQQPSLQNLNAMQAGVPRPGVP--------PQQQAMGGLNPQGQ-------ALN 2134
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPgqGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadagaqmgQQAQANGGMNPQQMggapnqvAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2135 IMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQ 2214
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2215 HLPLQGSSMGQMAAQMGQLGqmGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSP---GQPNPMSPQQHMLsgQPQASH 2291
Cdd:pfam09606  325 AHQQQMNQSVGQGGQVVALG--GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMR--QSPQPS 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2292 LPGQQIATSLSNQVRSPAPVQSPRpqsqpphsspsprIQPQPSPhHVSPQTGSPHpglavTMASSIDQGHLGNPEQSAML 2371
Cdd:pfam09606  401 VPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSP-QMSQQPAQQR-----TIGQDSPGGSLNTPGQSAVN 461
                          330
                   ....*....|....
gi 119943102  2372 PQLNtPSRSALSSE 2385
Cdd:pfam09606  462 SPLN-PQEEQLYRE 474
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1669-1700 2.12e-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: 2.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119943102 1669 CNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1700
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKH 36
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
688-1007 2.67e-05

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 49.66  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  688 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPG-MAISPSRMPQPPNMMGAHT-NNMMAQAPAQSQFLPQNQFPSSS 765
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNAVDYSVlVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  766 GAMSVGMGQPPAQTGVSQGQVPGAALPNPLnmlGPQASQLPCppvTQSPLHPTPPPASTAagmPSLQHttpPGMTPPQPA 845
Cdd:COG5665   219 SGRSQHIVQAAKRVGVEWWGDPSLLATPPA---TPATEEKSS---QQPKSQPTSPSGGTT---PPSTN---QLTTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  846 APTQPSTPVSSSGQTPTPTP-------GSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQ 917
Cdd:COG5665   287 STAKAQPQPPTKKQPAKEPPsdtasgnPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTPAtDLA 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  918 PPGTPLSQAAASIDNRVP--------------TPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEM 983
Cdd:COG5665   367 TPVSPTPPETSVDKKVSPdsatsstksekeggTASSPMPPNIAIGAKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSV 446
                         330       340
                  ....*....|....*....|....
gi 119943102  984 MEEDLQGASQVKEETDIAEQKSEP 1007
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAP 470
PHA03379 PHA03379
EBNA-3A; Provisional
631-827 8.80e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 48.13  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  631 RRSRLHKQGilgnQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNV--------QLP-QAPM 701
Cdd:PHA03379  591 RLARLRAEA----QPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVpamqpqyfDLPlQQPI 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  702 GPRAASPMNHSvqmnSMGSVPGM-AISPSRMPQP---PNMMGAHTNNMMAQAPAQSQFLP-QNQFPSSSGAMSVgmgqpp 776
Cdd:PHA03379  667 SQGAPLAPLRA----SMGPVPPVpATQPQYFDIPltePINQGASAAHFLPQQPMEGPLVPeRWMFQGATLSQSV------ 736
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119943102  777 aQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPV------TQSPLHPTPPPASTAAG 827
Cdd:PHA03379  737 -RPGVAQSQYFDLPLTQPINHGAPAAHFLHQPPMegpwvpEQWMFQGAPPSQGTDVV 792
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
837-976 1.24e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.17  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  837 PGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATP-QSSQQQPTPVH 915
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlQRAQGATKAKK 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943102  916 AQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESK 976
Cdd:PRK07994  441 SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALK 501
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1668-1704 1.28e-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: 41.42  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 119943102 1668 TCNECK--HHVETRWHCTVCEDYDLCINCY----NTKSH--AHKM 1704
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHnsLHIM 46
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1667-1706 1.81e-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: 41.26  E-value: 1.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 119943102 1667 YTCNECKHH--VETRWHCTVC--EDYDLCINC-YNTKSH--AHKMVK 1706
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
629-762 2.01e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   629 EKRRSRLHKQgILGNQPALPAPGAQPPVIPQ--AQPVRPPNG-------PLSLPVNRMQVSQGMNSFNPMSLGNVQLPQA 699
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPMGSPMGGAmgQPPYYGQGPqqqfngqPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943102   700 PMGPRAASPMNHSVQMNSMGSVPGMAISPS--RMPQPPNMMGAHTNN-----MMAQAPA--QSQFLPQNQFP 762
Cdd:TIGR01628  444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLsqDLPQPQSTASQGGQNkklaqVLASATPqmQKQVLGERLFP 515
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
864-979 2.23e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.40  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  864 TPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASA 943
Cdd:PRK07994  363 APLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSE 442
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 119943102  944 ETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEP 979
Cdd:PRK07994  443 PAAASRARPVNSALERLASVRPAPSALEKAPAKKEA 478
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2074-2150 2.66e-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: 45.34  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  2074 QPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMG---GLNPQgQALNIMNPGHNPNMASMNPQ 2150
Cdd:pfam07271  168 RIGFPMQPNMGMRPGFNQMPGMPPNQMRPGFNQMPGMPPRPGFPNPMPNMQprpGFRPQ-PGPMGNRPGGGFPHPGTPMG 246
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1667-1695 2.80e-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: 40.74  E-value: 2.80e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119943102 1667 YTCNECKHHV--ETRWHCTVCEDYDLCINCY 1695
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
802-943 3.09e-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: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   802 ASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPpgmtppqpaAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQ 881
Cdd:pfam17823  111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAP---------RAAACRANASAAPRAAIAAASAPHAASPAPRTAASS 181
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943102   882 AAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTP-LSQAAASIDNRVPTPSSVASA 943
Cdd:pfam17823  182 TTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPaAGTALAAVGNSSPAAGTVTAA 244
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
769-970 5.04e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  769 SVGMGQPPAqtGVSQGQVPGAAlpnplnmlgPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPpgmtppqpAAPT 848
Cdd:PRK07003  361 AVTGGGAPG--GGVPARVAGAV---------PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA--------AAAT 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  849 QPSTPVSSSGQTPTPT----PGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSvATPQSSQQQPTPVHAQPPGTPLS 924
Cdd:PRK07003  422 RAEAPPAAPAPPATADrgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSA-SAPASDAPPDAAFEPAPRAAAPS 500
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 119943102  925 QAAAsidNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEP 970
Cdd:PRK07003  501 AATP---AAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
800-989 6.76e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 45.08  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  800 PQASQLPcPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPvsSSGQTPTPTPGSVPSATQTQSTPT 879
Cdd:PRK08691  388 ETAAKKP-QPRPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWEDAP--DEAQTAAGTAQTSAKSIQTASEAE 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  880 VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPV-HAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPD-VPVL 957
Cdd:PRK08691  465 TPPENQVSKNKAADNETDAPLSEVPSENPIQATPNdEAVETETFAHEAPAEPFYGYGFPDNDCPPEDGAEIPPPDwEHAA 544
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 119943102  958 EMKTETQAEDTEPDPGESKG-----EPRSEMMEEDLQ 989
Cdd:PRK08691  545 PADTAGGGADEEAEAGGIGGnntpsAPPPEFSTENWA 581
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
852-960 6.91e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  852 TPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASID 931
Cdd:PRK07764  407 AAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPA 486
                          90       100
                  ....*....|....*....|....*....
gi 119943102  932 NRVPTPSSVASAETNSQQPGPDVPVLEMK 960
Cdd:PRK07764  487 APAPAAAPAAPAAPAAPAGADDAATLRER 515
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
757-1007 7.45e-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: 44.57  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   757 PQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNP--LNMLGPQAsQLPCPPVTQSPLHPTPPPASTAAGMPSLQHT 834
Cdd:pfam17823  100 PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALpsEAFSAPRA-AACRANASAAPRAAIAAASAPHAASPAPRTA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   835 TPPGMTPPQPAAPTQPSTPVSSSG-QTPTPTPGSVPSATQTqSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP 913
Cdd:pfam17823  179 ASSTTAASSTTAASSAPTTAASSApATLTPARGISTAATAT-GHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   914 VHAQppgtPLSQAAASID-----NRVPTPSSVASAETNSQQPGPDV------PVLEMKTETQAEDTEPDPGESKGEPRSE 982
Cdd:pfam17823  258 AAAG----TVASAAGTINmgdphARRLSPAKHMPSDTMARNPAAPMgaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTLE 333
                          250       260
                   ....*....|....*....|....*
gi 119943102   983 MMEEDLQGASQVKEETDIAEQKSEP 1007
Cdd:pfam17823  334 PNTPKSVASTNLAVVTTTKAQAKEP 358
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
637-839 1.43e-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: 43.87  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   637 KQGILGNQPALPAPGAQPPViPQAQPVRPPngplslpvnrmQVSQGMnsfnpMSLGNV-------------QLPQAPMGP 703
Cdd:pfam09770  159 DASLWGVAPKKAAAPAPAPQ-PAAQPASLP-----------APSRKM-----MSLEEVeaamraqakkpaqQPAPAPAQP 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   704 RAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQ 783
Cdd:pfam09770  222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQ 301
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119943102   784 gqvpgaALPNPlNMLGPQ---ASQLPCPPVTQSPLHPTPPPASTAAGMPSLqHTTPPGM 839
Cdd:pfam09770  302 ------ILQNP-NRLSAArvgYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI-ITHPQQL 352
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
751-948 1.55e-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: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   751 AQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPnplnmlgPQASQLPCPPVT---QSP-LHPT--PPPAST 824
Cdd:pfam03154  176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQP-------PNQTQSTAAPHTliqQTPtLHPQrlPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   825 AAGMPSlqhTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATP 904
Cdd:pfam03154  249 LQPMTQ---PPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRI 325
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 119943102   905 QSSQQQPTPVHAQPP-GTPLSQAAASIDNRVPTPSSVASAETNSQ 948
Cdd:pfam03154  326 HTPPSQSQLQSQQPPrEQPLPPAPLSMPHIKPPPTTPIPQLPNPQ 370
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
765-886 1.58e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  765 SGAMSVGMGQPPAQTGVSQGQVPGAALPnplnmlGPQASQLPCPPVTQSPlHPTPPPASTAAGMPSLQHTTPPGmtpPQP 844
Cdd:PRK07764  388 AGGAGAPAAAAPSAAAAAPAAAPAPAAA------APAAAAAPAPAAAPQP-APAPAPAPAPPSPAGNAPAGGAP---SPP 457
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119943102  845 AAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQA 886
Cdd:PRK07764  458 PAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAA 499
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1668-1700 1.94e-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: 1.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119943102 1668 TCNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1700
Cdd:cd02344     2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKH 36
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
1667-1696 2.38e-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: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119943102 1667 YTCNEC-KHHVETRWHCTVCEDYDLCINCYN 1696
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ 31
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
649-950 3.13e-03

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: 42.64  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   649 APGAQPPVIPQAQPVRPPNGPlslPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISP 728
Cdd:pfam17823  152 ANASAAPRAAIAAASAPHAAS---PAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTAL 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   729 SRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAAL-PNPLNMLGPQASQLPC 807
Cdd:pfam17823  229 AAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMaRNPAAPMGAQAQGPII 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   808 PPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPaaptqpSTPVSSSGQTPTPTPGSVPsATQTQSTPTVQAaaqaq 887
Cdd:pfam17823  309 QVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNL------AVVTTTKAQAKEPSASPVP-VLHTSMIPEVEA----- 376
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943102   888 vtpqpqtpvqppsvaTPQSSQQQPTPV--HAQPPGTPL------SQAAASIDNRVPTPSS---VASAETNSQQP 950
Cdd:pfam17823  377 ---------------TSPTTQPSPLLPtqGAAGPGILLapeqvaTEATAGTASAGPTPRSsgdPKTLAMASCQL 435
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
762-972 3.27e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  762 PSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQ-ASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMT 840
Cdd:PRK07003  374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKaAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKA 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  841 PPQ----PAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSV-------ATPQSSQQ 909
Cdd:PRK07003  454 NARasadSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRedapaaaAPPAPEAR 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  910 QPTPVHAQPPGTPlSQAAASID------NRV-----------PTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDP 972
Cdd:PRK07003  534 PPTPAAAAPAARA-GGAAAALDvlrnagMRVssdrgaraaaaAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNG 612
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
673-955 3.39e-03

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   673 PVNRMQVSQGMNSFNPMSLGNVQLPQaPMGPRAASPMNHSVQMNSMGSVPGMAISPsrMPQPPNMMGAHTNNMMAQAPAQ 752
Cdd:pfam09606  142 QMSRVGRMQPGGQAGGMMQPSSGQPG-SGTPNQMGPNGGPGQGQAGGMNGGQQGPM--GGQMPPQMGVPGMPGPADAGAQ 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   753 SQFLPQNQFPSSSGAMSVGMGQPP---AQTGVSQGQVPGAALPNPLNML--GPQASQLPCPPVTQSPLHPTPPPASTAAG 827
Cdd:pfam09606  219 MGQQAQANGGMNPQQMGGAPNQVAmqqQQPQQQGQQSQLGMGINQMQQMpqGVGGGAGQGGPGQPMGPPGQQPGAMPNVM 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   828 MPSL------QHTTPPGMTPPQPAAPTQPSTPVSSSGQTP--TPTPGSVPSATQTQST-------PTVQAAAQAQVTPQP 892
Cdd:pfam09606  299 SIGDqnnyqqQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGqvVALGGLNHLETWNPGNfgglganPMQRGQPGMMSSPSP 378
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943102   893 QTPVQPPSVATPQSSQQQPTPvHAQPPGTPLSQAAAS-IDNRVPTPSSVASaetNSQQPGPDVP 955
Cdd:pfam09606  379 VPGQQVRQVTPNQFMRQSPQP-SVPSPQGPGSQPPQShPGGMIPSPALIPS---PSPQMSQQPA 438
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1668-1699 3.71e-03

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 37.33  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119943102 1668 TCNECKHHVET--RWHCTVCEDYDLCINCYNTKS 1699
Cdd:cd02338     2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGV 35
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
800-935 4.83e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  800 PQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPgmtppqpaAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPT 879
Cdd:PRK07764  394 PAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQP--------APAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119943102  880 VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGtplsQAAASIDNRVP 935
Cdd:PRK07764  466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA----DDAATLRERWP 517
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
638-929 6.08e-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: 41.92  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   638 QGILGNQPALPAPGAQPPVIPQAQPVRP-----PNGPLSLPVNRMQVSQG--MNSFNPMSLG---------------NVQ 695
Cdd:pfam09606  144 SRVGRMQPGGQAGGMMQPSSGQPGSGTPnqmgpNGGPGQGQAGGMNGGQQgpMGGQMPPQMGvpgmpgpadagaqmgQQA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   696 LPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRM-PQPPNMMGAHTNNMMAQA-PAQSQFLPQNQFPSSSGAMSVGMG 773
Cdd:pfam09606  224 QANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMgINQMQQMPQGVGGGAGQGgPGQPMGPPGQQPGAMPNVMSIGDQ 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   774 QPPAQTGV-----SQGQVPGAALPNPLNMLGPQASQLPCPPvTQSPLHPTPPPASTAAGMPSLQHTtPPGMTPPQPAAPT 848
Cdd:pfam09606  304 NNYQQQQTrqqqqQQGGNHPAAHQQQMNQSVGQGGQVVALG-GLNHLETWNPGNFGGLGANPMQRG-QPGMMSSPSPVPG 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   849 QPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAA 928
Cdd:pfam09606  382 QQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVN 461

                   .
gi 119943102   929 S 929
Cdd:pfam09606  462 S 462
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
642-1011 6.39e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  642 GNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGmnsfnpmslgnvqlPQAPMGPRAASPMNHSVQMNSMGSV 721
Cdd:PRK07764  390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQ--------------PAPAPAPAPAPPSPAGNAPAGGAPS 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  722 PGMAISPSRMPQPpnmmgahtnnmmAQAPAQSQFLPQNQFPSSSGAmSVGMGQPPAQTGVSQGQVPGAAL----PNPLNM 797
Cdd:PRK07764  456 PPPAAAPSAQPAP------------APAAAPEPTAAPAPAPPAAPA-PAAAPAAPAAPAAPAGADDAATLrerwPEILAA 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  798 LG-----------PQASQLPcppVTQSPL---HPTPPPAS---------------------------TAAGMP-SLQHTT 835
Cdd:PRK07764  523 VPkrsrktwaillPEATVLG---VRGDTLvlgFSTGGLARrfaspgnaevlvtalaeelggdwqveaVVGPAPgAAGGEG 599
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  836 PPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQST--------PTVQAAAQAQVTPQPQTPVQPPSVATPQSS 907
Cdd:PRK07764  600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAapapgvaaPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102  908 QQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAE-------DTEPDPGESKGEPR 980
Cdd:PRK07764  680 APPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvplppepDDPPDPAGAPAQPP 759
                         410       420       430
                  ....*....|....*....|....*....|.
gi 119943102  981 SEMMEEDLQGASQVKEETDIAEQksEPMEVD 1011
Cdd:PRK07764  760 PPPAPAPAAAPAAAPPPSPPSEE--EEMAED 788
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
808-982 7.22e-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: 41.68  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   808 PPVTQSPLHPTPPPASTAAGMPSLQHTTPPgmtppqPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTV--QAAAQ 885
Cdd:pfam03154  171 PPVLQAQSGAASPPSPPPPGTTQAATAGPT------PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLhpQRLPS 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943102   886 AQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPT-PSSVASAETNSQQPGPDVPVLEMKTETQ 964
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
                          170
                   ....*....|....*...
gi 119943102   965 AEDTEPDPGESKGEPRSE 982
Cdd:pfam03154  325 IHTPPSQSQLQSQQPPRE 342
 
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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