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Conserved domains on  [gi|568994536|ref|XP_006521815|]
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histone lysine acetyltransferase CREBBP isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1348-1655 7.86e-94

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


:

Pssm-ID: 400497  Cd Length: 348  Bit Score: 308.56  E-value: 7.86e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1348 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1427
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1428 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1502
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1503 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1557
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1558 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1618
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994536  1619 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1655
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1083-1190 1.73e-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: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1083 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1162
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994536 1163 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1190
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 ...
586-666 1.12e-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: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   586 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 665
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994536   666 E 666
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1202-1284 3.36e-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: 123.55  E-value: 3.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1202 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1279
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994536 1280 TLDPE 1284
Cdd:cd15802    69 ELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-429 1.74e-28

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.74e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 429
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1711-1751 2.41e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


:

Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.80  E-value: 2.41e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994536 1711 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1751
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 ...
1778-1846 3.80e-24

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.84  E-value: 3.80e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994536  1778 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1846
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2019-2120 1.68e-20

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


:

Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 88.74  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2019 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2087
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994536  2088 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2120
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1286-1317 9.45e-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: 9.45e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994536 1286 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1317
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
COG5076 super family cl34891
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
937-1189 7.54e-17

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


The actual alignment was detected with superfamily member COG5076:

Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 84.86  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  937 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 1013
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1014 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1088
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1089 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1168
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994536 1169 RVYKFCSKLAEVFEQEIDPVM 1189
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
PHA03247 super family cl33720
large tegument protein UL36; Provisional
680-1032 9.34e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  680 NQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQ---APMGPRAASPMNHSVQmnsma 756
Cdd:PHA03247 2596 ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRL----- 2670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  757 SVPGMAISPSRMPQPPNMMGThannimaQAPTQNQFLPQNQFPSSsgamsvnsvgmgQPAAQGQVPGAALPnplnmLAPQ 836
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPT-------VGSLTSLADPPPPPPTP------------EPAPHALVSATPLP-----PGPA 2726
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  837 ASQLPCPPvtqSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPT--- 913
Cdd:PHA03247 2727 AARQASPA---LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwd 2803
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  914 ---VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA-----SIDNRVPTPSSVTSAETSSQQPG 985
Cdd:PHA03247 2804 padPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKPAAPARPPV 2883
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994536  986 PDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 1032
Cdd:PHA03247 2884 RRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1966-2356 7.08e-06

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.55  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1966 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 2030
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2031 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2107
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2108 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2184
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2185 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2264
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2265 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2344
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994536  2345 NQVRSPAPVQSP 2356
Cdd:pfam09606  437 PAQQRTIGQDSP 448
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1348-1655 7.86e-94

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


Pssm-ID: 400497  Cd Length: 348  Bit Score: 308.56  E-value: 7.86e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1348 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1427
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1428 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1502
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1503 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1557
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1558 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1618
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994536  1619 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1655
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1083-1190 1.73e-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: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1083 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1162
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994536 1163 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1190
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 ...
586-666 1.12e-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: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   586 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 665
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994536   666 E 666
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1080-1188 7.82e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.82e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   1080 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1159
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 568994536   1160 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1188
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1202-1284 3.36e-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: 123.55  E-value: 3.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1202 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1279
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994536 1280 TLDPE 1284
Cdd:cd15802    69 ELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-429 1.74e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.74e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 429
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1711-1751 2.41e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.80  E-value: 2.41e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994536 1711 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1751
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1188-1227 3.57e-24

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 96.62  E-value: 3.57e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568994536  1188 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1227
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1778-1846 3.80e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.84  E-value: 3.80e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994536  1778 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1846
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1772-1850 1.12e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 96.67  E-value: 1.12e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   1772 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1847
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 568994536   1848 FCL 1850
Cdd:smart00551   77 KCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
362-432 4.42e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 4.42e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568994536    362 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGKaCQVAHCASSRQIISHWKNCTRHDCPVCLPL 432
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2019-2120 1.68e-20

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


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 88.74  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2019 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2087
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994536  2088 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2120
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1100-1172 5.10e-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: 5.10e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994536  1100 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1172
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1286-1317 9.45e-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: 9.45e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994536 1286 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1317
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1707-1749 4.53e-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: 4.53e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568994536   1707 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 1749
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
937-1189 7.54e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 84.86  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  937 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 1013
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1014 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1088
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1089 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1168
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994536 1169 RVYKFCSKLAEVFEQEIDPVM 1189
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1707-1748 8.55e-16

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: 73.29  E-value: 8.55e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568994536  1707 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 1748
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
PHA03247 PHA03247
large tegument protein UL36; Provisional
680-1032 9.34e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  680 NQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQ---APMGPRAASPMNHSVQmnsma 756
Cdd:PHA03247 2596 ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRL----- 2670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  757 SVPGMAISPSRMPQPPNMMGThannimaQAPTQNQFLPQNQFPSSsgamsvnsvgmgQPAAQGQVPGAALPnplnmLAPQ 836
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPT-------VGSLTSLADPPPPPPTP------------EPAPHALVSATPLP-----PGPA 2726
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  837 ASQLPCPPvtqSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPT--- 913
Cdd:PHA03247 2727 AARQASPA---LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwd 2803
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  914 ---VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA-----SIDNRVPTPSSVTSAETSSQQPG 985
Cdd:PHA03247 2804 padPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKPAAPARPPV 2883
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994536  986 PDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 1032
Cdd:PHA03247 2884 RRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2072-2114 1.71e-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: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568994536 2072 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2114
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
725-1111 8.78e-08

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 57.75  E-value: 8.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  725 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPG-MAISPSRMPQPPN-MMGTHANNIMAQAPTQNQFLPQNQFPSSS 802
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNaVDYSVLVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  803 GAMSVNSVGMGQPAA--QGQVPGAALPNPLNMLAPQASQlpcppvTQSPLHPTPPPASTAagmPSLQHP--TAPGMTPPQ 878
Cdd:COG5665   219 SGRSQHIVQAAKRVGveWWGDPSLLATPPATPATEEKSS------QQPKSQPTSPSGGTT---PPSTNQltTSNTPTSTA 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  879 PAAPTQPST---PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvHTQ--PP 953
Cdd:COG5665   290 KAQPQPPTKkqpAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTP-ATDlaTP 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  954 GTPlSQAAASIDNRVpTPSSVTSAETSSQQPG-PDVPMLEMKTEVQTDDAEPE---------------PTESKGEPRSEM 1017
Cdd:COG5665   369 VSP-TPPETSVDKKV-SPDSATSSTKSEKEGGtASSPMPPNIAIGAKDDVDATdpsqeakeytknapmTPEADSAPESSV 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1018 MEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPevkveAKEEEENSSNDTASQSTSPSQPRKKIFKPEelrqalmPTLEAL 1097
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAPNAIPPPED-----PSTIGRLSSGDKLANETGPPVIRRDSTPSS-------TADQSI 514
                         410
                  ....*....|....
gi 568994536 1098 YRQDPESLPFRQPV 1111
Cdd:COG5665   515 VGVLAFGLDQRTQA 528
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
466-982 1.82e-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: 56.70  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   466 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPmSIPAGGITTDQQPPNLI 545
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   546 SESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 625
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   626 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPASGAQPPVIPPAQSVRPPNG 705
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   706 P---LPLPVNrmqvsqgmnsfnPMSLGNVQLPQAPMGPRAASPMNHsvQMNSMASVPGMAISPSRMPQPPnmmgthANNI 782
Cdd:pfam03154  339 PpreQPLPPA------------PLSMPHIKPPPTTPIPQLPNPQSH--KHPPHLSGPSPFQMNSNLPPPP------ALKP 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   783 MAQAPTQNqflpqnqfpsssgamsvnsvgmgqpaaqgqvPGAALPNPLNMLaPQASQLPCPPV-----TQSPLHptPPPA 857
Cdd:pfam03154  399 LSSLSTHH-------------------------------PPSAHPPPLQLM-PQSQQLPPPPAqppvlTQSQSL--PPPA 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   858 StaagmpslQHPTaPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVAT 937
Cdd:pfam03154  445 A--------SHPP-TSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLP 515
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 568994536   938 PQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 982
Cdd:pfam03154  516 PVQIKEEALDEAEEPESPPPPPRSPS-----PEPTVVNTPSHASQ 555
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
888-1049 6.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 51.40  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  888 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQpqtpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNR 967
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPA--------VPPPPASAPQQAPAVPLPETTSQLLAARQQLQRA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  968 VPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPrsemMEEDLQGSSQVKEETDTTEQKSEPMEVEEK 1047
Cdd:PRK07994  433 QGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEA----YRWKATNPVEVKKEPVATPKALKKALEHEK 508

                  ..
gi 568994536 1048 KP 1049
Cdd:PRK07994  509 TP 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1966-2356 7.08e-06

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.55  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1966 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 2030
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2031 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2107
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2108 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2184
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2185 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2264
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2265 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2344
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994536  2345 NQVRSPAPVQSP 2356
Cdd:pfam09606  437 PAQQRTIGQDSP 448
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
666-799 4.93e-03

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   666 EKRRSRLHKQgILGNQPALPASG---------AQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQA 736
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPmgspmggamGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994536   737 PMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQP-PNMMGTHANNI------MAQAP--TQNQFLPQNQFP 799
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 ...
1348-1655 7.86e-94

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


Pssm-ID: 400497  Cd Length: 348  Bit Score: 308.56  E-value: 7.86e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1348 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1427
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1428 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1502
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1503 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1557
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1558 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1618
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994536  1619 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1655
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1083-1190 1.73e-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: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1083 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1162
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994536 1163 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1190
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 ...
586-666 1.12e-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: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   586 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 665
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994536   666 E 666
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1080-1188 7.82e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.82e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   1080 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1159
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 568994536   1160 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1188
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1202-1284 3.36e-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: 123.55  E-value: 3.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1202 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1279
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994536 1280 TLDPE 1284
Cdd:cd15802    69 ELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1086-1185 2.88e-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: 2.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1086 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1164
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 568994536 1165 RKTSRVYKFCSKLAEVFEQEI 1185
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 ...
1106-1183 1.04e-30

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


Pssm-ID: 99930  Cd Length: 102  Bit Score: 117.38  E-value: 1.04e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536 1106 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1183
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-429 1.74e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.74e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVC 429
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1711-1751 2.41e-28

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 108.80  E-value: 2.41e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994536 1711 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1751
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1085-1185 1.29e-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: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1085 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1164
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|.
gi 568994536 1165 RKTSRVYKFCSKLAEVFEQEI 1185
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1099-1182 1.67e-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: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1099 RQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1178
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                  ....
gi 568994536 1179 EVFE 1182
Cdd:cd05506    93 KIFE 96
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1188-1227 3.57e-24

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 96.62  E-value: 3.57e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568994536  1188 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1227
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1778-1846 3.80e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 97.84  E-value: 3.80e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994536  1778 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1846
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1093-1185 6.00e-24

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


Pssm-ID: 99932  Cd Length: 103  Bit Score: 98.15  E-value: 6.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1093 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1172
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                          90
                  ....*....|...
gi 568994536 1173 FCSKLAEVFEQEI 1185
Cdd:cd05500    91 MGKRLQAAFEKHL 103
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1772-1850 1.12e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 96.67  E-value: 1.12e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   1772 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1847
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 568994536   1848 FCL 1850
Cdd:smart00551   77 KCV 79
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1088-1187 1.66e-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: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1088 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1166
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                          90       100
                  ....*....|....*....|.
gi 568994536 1167 TSRVYKFCSKLAEVFEQEIDP 1187
Cdd:cd05497    86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1081-1183 3.59e-22

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 93.51  E-value: 3.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1081 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKNPMDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 1157
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                          90       100
                  ....*....|....*....|....*.
gi 568994536 1158 NNAWLYNRKTSRVYKFCSKLAEVFEQ 1183
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 ...
1103-1201 9.00e-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: 9.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1103 ESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKFCSKLAEVF 1181
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                          90       100
                  ....*....|....*....|
gi 568994536 1182 EQEIDPVMQSlgYCCGRKYE 1201
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 ...
1106-1182 2.02e-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: 2.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994536 1106 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFE 1182
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
362-432 4.42e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.35  E-value: 4.42e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568994536    362 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGKaCQVAHCASSRQIISHWKNCTRHDCPVCLPL 432
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2019-2120 1.68e-20

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


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 88.74  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2019 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2087
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994536  2088 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2120
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1084-1184 2.83e-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: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1084 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMF 1157
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                          90       100
                  ....*....|....*....|....*..
gi 568994536 1158 NNAWLYNRKTSRVYKFCSKLAEVFEQE 1184
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1100-1172 5.10e-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: 5.10e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994536  1100 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1172
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1286-1317 9.45e-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: 9.45e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994536 1286 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1317
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1285-1319 6.21e-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: 6.21e-18
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568994536 1285 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1319
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 ...
1084-1174 3.30e-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: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1084 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1163
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                          90
                  ....*....|.
gi 568994536 1164 NRKTSRVYKFC 1174
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1707-1749 4.53e-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: 4.53e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568994536   1707 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 1749
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1286-1319 4.88e-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: 4.88e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568994536 1286 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1319
Cdd:cd15646     7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
937-1189 7.54e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 84.86  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  937 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 1013
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1014 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1088
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1089 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1168
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994536 1169 RVYKFCSKLAEVFEQEIDPVM 1189
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1707-1748 8.55e-16

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: 73.29  E-value: 8.55e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568994536  1707 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 1748
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1089-1179 1.13e-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: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1089 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1168
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                          90
                  ....*....|.
gi 568994536 1169 RVYKFCSKLAE 1179
Cdd:cd05512    82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1102-1170 1.23e-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: 1.23e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1102 PESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 1170
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1099-1194 5.14e-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: 5.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1099 RQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1178
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEML 90
                          90
                  ....*....|....*.
gi 568994536 1179 EVFEQEIDPVMQSLGY 1194
Cdd:cd05511    91 ELAEELLAEREEKLTQ 106
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1119-1172 1.03e-14

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 71.95  E-value: 1.03e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1172
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1100-1187 1.42e-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: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1100 QDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN------RKTSRvYKF 1173
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                          90
                  ....*....|....*..
gi 568994536 1174 CSKLAEV---FEQEIDP 1187
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1119-1190 2.43e-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: 2.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1190
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1711-1747 7.68e-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: 67.46  E-value: 7.68e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568994536 1711 YTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHK 1747
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1242-1317 1.28e-13

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


Pssm-ID: 277086  Cd Length: 73  Bit Score: 67.76  E-value: 1.28e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1242 FCEKCFTEIQGENVTLGddpsqpQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHY---DIIWPSGFVCDNC 1317
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNgrrNADETAEYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1087-1172 4.20e-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: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1087 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1166
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSS 81

                  ....*.
gi 568994536 1167 TSRVYK 1172
Cdd:cd05507    82 DHDVYL 87
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1082-1181 1.78e-12

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


Pssm-ID: 99937  Cd Length: 97  Bit Score: 65.25  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1082 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1161
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                          90       100
                  ....*....|....*....|
gi 568994536 1162 LYNRKTSRVYKFCSKLAEVF 1181
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1086-1177 2.93e-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: 64.74  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1086 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1165
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                          90
                  ....*....|..
gi 568994536 1166 KTSRVYKFCSKL 1177
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 ...
1085-1173 1.13e-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: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1085 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKNPMDLSTIKRKLDtgQYQEPWQYVDDVW 1154
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                          90
                  ....*....|....*....
gi 568994536 1155 LMFNNAWLYNRKTSRVYKF 1173
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 ...
1119-1172 2.80e-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: 2.80e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1172
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYK 91
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1119-1177 5.83e-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: 61.20  E-value: 5.83e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 1177
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
PHA03247 PHA03247
large tegument protein UL36; Provisional
680-1032 9.34e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  680 NQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQ---APMGPRAASPMNHSVQmnsma 756
Cdd:PHA03247 2596 ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRL----- 2670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  757 SVPGMAISPSRMPQPPNMMGThannimaQAPTQNQFLPQNQFPSSsgamsvnsvgmgQPAAQGQVPGAALPnplnmLAPQ 836
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPT-------VGSLTSLADPPPPPPTP------------EPAPHALVSATPLP-----PGPA 2726
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  837 ASQLPCPPvtqSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPT--- 913
Cdd:PHA03247 2727 AARQASPA---LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwd 2803
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  914 ---VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA-----SIDNRVPTPSSVTSAETSSQQPG 985
Cdd:PHA03247 2804 padPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKPAAPARPPV 2883
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994536  986 PDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 1032
Cdd:PHA03247 2884 RRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1118-1186 1.04e-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: 1.04e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1118 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEID 1186
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1086-1185 3.42e-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: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1086 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNA 1160
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                          90       100
                  ....*....|....*....|....*
gi 568994536 1161 WLYNRKTSRVYKFCSKLAEVFEQEI 1185
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1108-1171 4.43e-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: 4.43e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1108 RQPVD-----PQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 1171
Cdd:cd05518    21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1712-1750 1.37e-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: 55.34  E-value: 1.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994536 1712 TCNECKHHVE-TRWHCTVCEDYDLCINCYNTKSH-THKMVK 1750
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLK 42
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2072-2114 1.71e-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: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568994536 2072 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2114
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 ...
1084-1185 1.76e-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: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1084 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1161
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                          90       100
                  ....*....|....*....|....
gi 568994536 1162 LYNRKTSRVYKFCSKLAEVFEQEI 1185
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
668-1016 5.03e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  668 RRSRLHKQGILGNQPALPAS--------GAQPPVIPPAQSVRPPN-GPLPLPVNRMQVSQgmnsfnpmslgnVQLPQAPM 738
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASSppqrprrrAARPTVGSLTSLADPPPpPPTPEPAPHALVSA------------TPLPPGPA 2726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  739 GPRAASPMNHSVQMN-SMASVPGMAISPSRMPQPPNMMGTHAnnimAQAPTQNQFLPQNQFPSSSGAmsvnsvgmgqPAA 817
Cdd:PHA03247 2727 AARQASPALPAAPAPpAVPAGPATPGGPARPARPPTTAGPPA----PAPPAAPAAGPPRRLTRPAVA----------SLS 2792
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  818 QGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPslqhPTAPGmtppqpaaPTQPSTPVSSGQTP-- 895
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP----PPPPG--------PPPPSLPLGGSVAPgg 2860
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  896 ----TPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQP--PGTPLSQAAASIDNRVP 969
Cdd:PHA03247 2861 dvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPqpPPPPQPQPPPPPPPRPQ 2940
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568994536  970 TPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSE 1016
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
810-1021 1.94e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 60.00  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  810 VGMGQPAAQGQVPGAALPNplnMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSlqHPTAPGMTPPQPAAPTQPSTPV 889
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASS---GPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAS--AAPAPGVAAPEHHPKHVAVPDA 662
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  890 SSGqtPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVP 969
Cdd:PRK07764  663 SDG--GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994536  970 TPSSVTSAETSSQQPGPDVPMLEmktEVQTDDAEPEPTESKGEPRSEMMEED 1021
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPA---PAPAAAPAAAPPPSPPSEEEEMAEDD 789
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1119-1183 6.40e-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: 6.40e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1183
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
725-1111 8.78e-08

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 57.75  E-value: 8.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  725 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPG-MAISPSRMPQPPN-MMGTHANNIMAQAPTQNQFLPQNQFPSSS 802
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNaVDYSVLVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  803 GAMSVNSVGMGQPAA--QGQVPGAALPNPLNMLAPQASQlpcppvTQSPLHPTPPPASTAagmPSLQHP--TAPGMTPPQ 878
Cdd:COG5665   219 SGRSQHIVQAAKRVGveWWGDPSLLATPPATPATEEKSS------QQPKSQPTSPSGGTT---PPSTNQltTSNTPTSTA 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  879 PAAPTQPST---PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvHTQ--PP 953
Cdd:COG5665   290 KAQPQPPTKkqpAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTP-ATDlaTP 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  954 GTPlSQAAASIDNRVpTPSSVTSAETSSQQPG-PDVPMLEMKTEVQTDDAEPE---------------PTESKGEPRSEM 1017
Cdd:COG5665   369 VSP-TPPETSVDKKV-SPDSATSSTKSEKEGGtASSPMPPNIAIGAKDDVDATdpsqeakeytknapmTPEADSAPESSV 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1018 MEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPevkveAKEEEENSSNDTASQSTSPSQPRKKIFKPEelrqalmPTLEAL 1097
Cdd:COG5665   447 RTEASPSAGSDLEPENTTLRDPAPNAIPPPED-----PSTIGRLSSGDKLANETGPPVIRRDSTPSS-------TADQSI 514
                         410
                  ....*....|....
gi 568994536 1098 YRQDPESLPFRQPV 1111
Cdd:COG5665   515 VGVLAFGLDQRTQA 528
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
466-982 1.82e-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: 56.70  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   466 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPmSIPAGGITTDQQPPNLI 545
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   546 SESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 625
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   626 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPASGAQPPVIPPAQSVRPPNG 705
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   706 P---LPLPVNrmqvsqgmnsfnPMSLGNVQLPQAPMGPRAASPMNHsvQMNSMASVPGMAISPSRMPQPPnmmgthANNI 782
Cdd:pfam03154  339 PpreQPLPPA------------PLSMPHIKPPPTTPIPQLPNPQSH--KHPPHLSGPSPFQMNSNLPPPP------ALKP 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   783 MAQAPTQNqflpqnqfpsssgamsvnsvgmgqpaaqgqvPGAALPNPLNMLaPQASQLPCPPV-----TQSPLHptPPPA 857
Cdd:pfam03154  399 LSSLSTHH-------------------------------PPSAHPPPLQLM-PQSQQLPPPPAqppvlTQSQSL--PPPA 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   858 StaagmpslQHPTaPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVAT 937
Cdd:pfam03154  445 A--------SHPP-TSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLP 515
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 568994536   938 PQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 982
Cdd:pfam03154  516 PVQIKEEALDEAEEPESPPPPPRSPS-----PEPTVVNTPSHASQ 555
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1119-1183 2.07e-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: 2.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994536 1119 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1183
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
682-1019 5.46e-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: 55.16  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   682 PALPASGAqPPVIPPAQSVRPPNGPLPLpvnrmqvSQGMNSFNPMSLGNVQLPQAPMgPRAASPMNHSVQMNSMASVPG- 760
Cdd:pfam03154  204 PSVPPQGS-PATSQPPNQTQSTAAPHTL-------IQQTPTLHPQRLPSPHPPLQPM-TQPPPPSQVSPQPLPQPSLHGq 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   761 -------MAISPSRMPQPPNMMGTHANNIMAQAptQNQFLPQNQFPSSSGAM-----SVNSVGMGQPAAQGQVPGAALPN 828
Cdd:pfam03154  275 mppmphsLQTGPSHMQHPVPPQPFPLTPQSSQS--QVPPGPSPAAPGQSQQRihtppSQSQLQSQQPPREQPLPPAPLSM 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   829 PlNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPS-LQHPTAPGMTPPQPAAPTQPSTP-----VSSGQTPTPTPGSV 902
Cdd:pfam03154  353 P-HIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnLPPPPALKPLSSLSTHHPPSAHPpplqlMPQSQQLPPPPAQP 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   903 PSAAQTQSTPTVQAAAqaqvtpqpqtpvqPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 982
Cdd:pfam03154  432 PVLTQSQSLPPPAASH-------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSAMPGIQ 493
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994536   983 QPGPDVPMLEMKTEVQTDDAEPePTESKGEPRSEMME 1019
Cdd:pfam03154  494 PPSSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEE 529
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1084-1141 8.96e-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: 8.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536 1084 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKNPMDLSTI-KRKLDTG 1141
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1084-1185 3.47e-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: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536 1084 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1163
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                          90       100
                  ....*....|....*....|..
gi 568994536 1164 NRKTSRVYKFCSKLAEVFEQEI 1185
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1118-1183 4.58e-06

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 47.42  E-value: 4.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568994536 1118 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKFCSKLAEVFEQ 1183
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
888-1049 6.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 51.40  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  888 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQpqtpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNR 967
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPA--------VPPPPASAPQQAPAVPLPETTSQLLAARQQLQRA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  968 VPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPrsemMEEDLQGSSQVKEETDTTEQKSEPMEVEEK 1047
Cdd:PRK07994  433 QGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEA----YRWKATNPVEVKKEPVATPKALKKALEHEK 508

                  ..
gi 568994536 1048 KP 1049
Cdd:PRK07994  509 TP 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1966-2356 7.08e-06

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.55  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  1966 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 2030
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2031 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2107
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2108 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2184
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2185 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2264
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  2265 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2344
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994536  2345 NQVRSPAPVQSP 2356
Cdd:pfam09606  437 PAQQRTIGQDSP 448
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
799-1041 7.55e-06

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: 51.11  E-value: 7.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   799 PSSSGAMSVNSVGMGQPAAQGQVPGAALPNPlnmlapqASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQ 878
Cdd:pfam17823  115 LAAAASSSPSSAAQSLPAAIAALPSEAFSAP-------RAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASS 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   879 PAAPTQPSTP--VSSGQTPTPTPGSVPSAAQTqSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPpgtp 956
Cdd:pfam17823  188 TTAASSAPTTaaSSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGT---- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   957 LSQAAASID-----NRVPTPSSVTSAETSSQQPGPDV------PMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGS 1025
Cdd:pfam17823  263 VASAAGTINmgdphARRLSPAKHMPSDTMARNPAAPMgaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVAS 342
                          250
                   ....*....|....*.
gi 568994536  1026 SQVKEETDTTEQKSEP 1041
Cdd:pfam17823  343 TNLAVVTTTKAQAKEP 358
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
602-919 1.02e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.16  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   602 HLVHKLVQAIFPTPDPAALKDRRMENLVayakkvegdmYESANSRDEYYHLLAEKIYKIqKELEEKRRsrlhkqgilgnQ 681
Cdd:pfam09606    2 SVVNKIEEALQQNGQTSTKNAREMENHV----------FAKARTKDEYLGTVARLILHV-RDMSKKAA-----------Q 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   682 PALPASGAQPPVIPPAQSVRPPngplplPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPR-------------------- 741
Cdd:pfam09606   60 QQQPQGGQGNGGMGGGQQGMPD------PINALQNLAGQGTRPQMMGPMGPGPGGPMGQQmggpgtasnllaslgrpqmp 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   742 -----AASPMNHSVQMNSMASVPGM--AISPSRMPQPPNMMGTHANNIMAQAPTQN---QFLPQNQFPSSSGAMSVNSVG 811
Cdd:pfam09606  134 mggagFPSQMSRVGRMQPGGQAGGMmqPSSGQPGSGTPNQMGPNGGPGQGQAGGMNggqQGPMGGQMPPQMGVPGMPGPA 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   812 MGQPAAQGQVPGAALPNPLNML-----APQASQLPCPPVTQSPLHPTP-PPASTAAGMPSLQHPTAPGMTPPQPAAPTQP 885
Cdd:pfam09606  214 DAGAQMGQQAQANGGMNPQQMGgapnqVAMQQQQPQQQGQQSQLGMGInQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGA 293
                          330       340       350
                   ....*....|....*....|....*....|....
gi 568994536   886 STPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQ 919
Cdd:pfam09606  294 MPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ 327
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1713-1744 2.16e-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: 2.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568994536 1713 CNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1744
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKH 36
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
786-1013 3.80e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  786 APTQNQFLPQNQFPSSSGAmsvnSVGMGQPAAQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPS 865
Cdd:PRK07764  602 APASSGPPEEAARPAAPAA----PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  866 lqhPTAPGMtppqpaaptqpSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAqvtPQPQTPVQPPSVATPQSSQQQP 945
Cdd:PRK07764  678 ---PAAPPP-----------APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPA---AQPPQAAQGASAPSPAADDPVP 740
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536  946 TPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEmktevqtDDAEPEPTESKGEP 1013
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE-------DDAPSMDDEDRRDA 801
PHA03247 PHA03247
large tegument protein UL36; Provisional
682-947 8.48e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  682 PALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGM 761
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  762 AISPSRMPQPPNmmgthannimaqaptqnqflPQNQFPSSSGAMSvNSVGMGQPAAQGQVPGAALPNPLNMLAPQASQLP 841
Cdd:PHA03247 2829 PPPTSAQPTAPP--------------------PPPGPPPPSLPLG-GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA 2887
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  842 CPPVTQS-------PLHPTPPPASTAAGMPSLQ-------HPTAPGMTPPQPAAPTQPST-----PVSSGQTPTPTPGS- 901
Cdd:PHA03247 2888 RPAVSRStesfalpPDQPERPPQPQAPPPPQPQpqpppppQPQPPPPPPPRPQPPLAPTTdpagaGEPSGAVPQPWLGAl 2967
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994536  902 ------VPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP 947
Cdd:PHA03247 2968 vpgrvaVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDP 3019
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
800-983 1.52e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   800 SSSGAMSVNSVGMGQPAAQGQVPgAALPNPLNMLAPQAS---------QLPCPPVTQS---PLHPTPPPAS--TAAGMPS 865
Cdd:pfam05109  427 STTTSPTLNTTGFAAPNTTTGLP-SSTHVPTNLTAPASTgptvstadvTSPTPAGTTSgasPVTPSPSPRDngTESKAPD 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   866 LQHPTApgmtpPQPAAPTQPSTPVSSGQTPTPTPGS------VPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQ 939
Cdd:pfam05109  506 MTSPTS-----AVTTPTPNATSPTPAVTTPTPNATSptlgktSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPT 580
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568994536   940 SSQQQPTPVHTQPPGTPLSQAAASIDNRV----------PTPSSVTSAETSSQQ 983
Cdd:pfam05109  581 SAVTTPTPNATSPTVGETSPQANTTNHTLggtsstpvvtSPPKNATSAVTTGQH 634
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
832-994 1.57e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  832 MLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGmtppqpaaptQPSTPVSSGQTPTPTPGSVPS-AAQTQS 910
Cdd:PRK07764  362 MLLPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAA----------AAPAAAPAPAAAAPAAAAAPApAAAPQP 431
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  911 TPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPM 990
Cdd:PRK07764  432 APAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAAT 511

                  ....
gi 568994536  991 LEMK 994
Cdd:PRK07764  512 LRER 515
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1711-1750 1.72e-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: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568994536 1711 YTCNECKHH--VETRWHCTVC--EDYDLCINC-YNTKSH--THKMVK 1750
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1712-1751 2.23e-04

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


Pssm-ID: 239085  Cd Length: 49  Bit Score: 41.04  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568994536 1712 TCNECK--HHVETRWHCTVCEDYDLCINCY--NTKSHTHKMVKW 1751
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkGRETKRHNSLHI 45
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
813-1014 2.58e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  813 GQPAAQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQhptAPGMTPPQPAAPTQPSTPVSSG 892
Cdd:PRK12323  367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAA---APARRSPAPEALAAARQASARG 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  893 QTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPlSQAAASIDNRVPTPS 972
Cdd:PRK12323  444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA-SPAPAQPDAAPAGWV 522
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568994536  973 SVTSAETSSQQPGPDVPMLE---MKTEVQTDDAEPEPTESKGEPR 1014
Cdd:PRK12323  523 AESIPDPATADPDDAFETLApapAAAPAPRAAAATEPVVAPRPPR 567
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1711-1739 3.06e-04

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


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 40.35  E-value: 3.06e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568994536 1711 YTCNECKHHV--ETRWHCTVCEDYDLCINCY 1739
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
811-989 3.28e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.00  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  811 GMGQPAAQGQVPGAAlPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPslqhPTAPGMTPPQPAAPTQPSTPvS 890
Cdd:PRK07003  370 GGVPARVAGAVPAPG-ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATR----AEAPPAAPAPPATADRGDDA-A 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  891 SGQTPTPTPGSVPSAAQTQSTP-TVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASiDNRVP 969
Cdd:PRK07003  444 DGDAPVPAKANARASADSRCDErDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS-REDAP 522
                         170       180
                  ....*....|....*....|
gi 568994536  970 TPSSVTSAETSSQQPGPDVP 989
Cdd:PRK07003  523 AAAAPPAPEARPPTPAAAAP 542
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
872-1010 3.50e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.01  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  872 PGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQ--SSQQQPTPVH 949
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlqRAQGATKAKK 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568994536  950 TQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESK 1010
Cdd:PRK07994  441 SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALK 501
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
810-969 3.55e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  810 VGMGQPAAQGQVPGAALPnplnmlAPQASQLPCPPVTQSPLHPTPPPASTAAGMPslQHPTAPGMTPPQPAAPTQPSTPV 889
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAA------APAAAPAPAAAAPAAAAAPAPAAAPQPAPAP--APAPAPPSPAGNAPAGGAPSPPP 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  890 SSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAqvtpqpqtpvqppsvatPQSSQQQPTPVHTQPPGtplsQAAASIDNRVP 969
Cdd:PRK07764  459 AAAPSAQPAPAPAAAPEPTAAPAPAPPAAPA-----------------PAAAPAAPAAPAAPAGA----DDAATLRERWP 517
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
830-1013 3.79e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.00  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  830 LNMLAPQasqlPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGmtppqpAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQ 909
Cdd:PRK07003  353 LRMLAFE----PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVG------ASAVPAVTAVTGAAGAALAPKAAAAAAATR 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  910 STPTVQAAAQAQV-----TPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPS-SVTSAETSSQQ 983
Cdd:PRK07003  423 AEAPPAAPAPPATadrgdDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFePAPRAAAPSAA 502
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568994536  984 PGPDVPMLEMKTEVQTDD-----AEPEPTESKGEP 1013
Cdd:PRK07003  503 TPAAVPDARAPAAASREDapaaaAPPAPEARPPTP 537
PRK10263 PRK10263
DNA translocase FtsK; Provisional
834-1115 4.11e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  834 APQASQLPCPPVTQSPLHPTPPPASTaagMPSLQHPTAPGMtppqpaaptqpstpvssgQTPTPTPGSVPSAAQTQSTPT 913
Cdd:PRK10263  329 ATQSWAAPVEPVTQTPPVASVDVPPA---QPTVAWQPVPGP------------------QTGEPVIAPAPEGYPQQSQYA 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  914 VQAAAQaqvtpqpqtpvqppsvatpQSSQQQPTPVHtQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEM 993
Cdd:PRK10263  388 QPAVQY-------------------NEPLQQPVQPQ-QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAW 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  994 KTEVQTDDAEPEPTESKGEPRSE-MMEEDLQGSSQVKEETDTTEqkSEPmEVEEkkpevkveakeeeenssndtasqsTS 1072
Cdd:PRK10263  448 QAEEQQSTFAPQSTYQTEQTYQQpAAQEPLYQQPQPVEQQPVVE--PEP-VVEE------------------------TK 500
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568994536 1073 PSQPRKKIFKP-EELRQALMPTLEALYRQDPESLPFRQPVDPQL 1115
Cdd:PRK10263  501 PARPPLYYFEEvEEKRAREREQLAAWYQPIPEPVKEPEPIKSSL 544
PHA03378 PHA03378
EBNA-3B; Provisional
695-984 1.31e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  695 PPAQSVRPPNGPLPLPVNRM------QVSQGMNSFNPMSLGNVQLPQAPMGP--RAASPMNHSVQMNSMASVPgMAISPS 766
Cdd:PHA03378  558 PVHDQLLPAPGLGPLQIQPLtspttsQLASSAPSYAQTPWPVPHPSQTPEPPttQSHIPETSAPRQWPMPLRP-IPMRPL 636
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  767 RMP-------------QPPNMMGTHANNIMAQAPTqnqfLPQNQFPSSSGAMSVNSVGMGQ----PAAQGQVPGAALPnP 829
Cdd:PHA03378  637 RMQpitfnvlvfptphQPPQVEITPYKPTWTQIGH----IPYQPSPTGANTMLPIQWAPGTmqppPRAPTPMRPPAAP-P 711
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  830 LNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTApgmtppqpaaptqpSTPVSSGQTPTPTPGSVPSAAQTQ 909
Cdd:PHA03378  712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGR--------------ARPPAAAPGRARPPAAAPGAPTPQ 777
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568994536  910 STPTVQAAAQaqvtpqpqtpVQPPSVATPQSSQQQ-PTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQP 984
Cdd:PHA03378  778 PPPQAPPAPQ----------QRPRGAPTPQPPPQAgPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKP 843
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1712-1747 1.72e-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: 38.33  E-value: 1.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568994536 1712 TCNECKHH--VETRWHCTVCEDYDLCINCYNTKSHTHK 1747
Cdd:cd02344     2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKHNTR 39
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
822-954 2.49e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  822 PGAALPNPlnmlAPQASQLPCPPVTQSPLhPTPPPASTAAGMPslqHPTAPGMTPPQPAAPTQPSTPVSSGQ---TPTPT 898
Cdd:PRK14951  366 PAAAAEAA----APAEKKTPARPEAAAPA-AAPVAQAAAAPAP---AAAPAAAASAPAAPPAAAPPAPVAAPaaaAPAAA 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568994536  899 PGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSS-QQQPTPVHTQPPG 954
Cdd:PRK14951  438 PAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAaAPAAARLTPTEEG 494
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1712-1745 2.67e-03

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 37.71  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568994536 1712 TCNECKHHVET--RWHCTVCEDYDLCINCYNTKSHT 1745
Cdd:cd02338     2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGVTT 37
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
1711-1740 3.00e-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: 3.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568994536 1711 YTCNEC-KHHVETRWHCTVCEDYDLCINCYN 1740
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ 31
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
830-965 3.62e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  830 LNMLA--PQASQLPCPPVTQSPlhPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSgqtPTPTPGSVPSAAQ 907
Cdd:PRK14951  359 LRLLAfkPAAAAEAAAPAEKKT--PARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAA---APPAPVAAPAAAA 433
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568994536  908 TQSTPTVqAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASID 965
Cdd:PRK14951  434 PAAAPAA-APAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
679-896 3.83e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  679 GNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNrmqvSQGMNSFNPMSLGNVQLPQApmGPRAASPMNHSVQMNSMASV 758
Cdd:PRK12323  368 SGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAA----PPAAPAAAPAAAAAARAVAA--APARRSPAPEALAAARQASA 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  759 PGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVnsvgmgqPAAQGQVPGAALPNPLNMLAP--- 835
Cdd:PRK12323  442 RGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA-------PADDDPPPWEELPPEFASPAPaqp 514
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994536  836 -------QASQLPCPPVTQ-SPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPT 896
Cdd:PRK12323  515 daapagwVAESIPDPATADpDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPA 583
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
666-799 4.93e-03

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   666 EKRRSRLHKQgILGNQPALPASG---------AQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQA 736
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPmgspmggamGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994536   737 PMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQP-PNMMGTHANNI------MAQAP--TQNQFLPQNQFP 799
Cdd:TIGR01628  444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPqPQSTASQGGQNkklaqvLASATpqMQKQVLGERLFP 515
PHA03379 PHA03379
EBNA-3A; Provisional
668-862 5.13e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 42.35  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  668 RRSRLHKQGilgnQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNV--------QLP-QAPM 738
Cdd:PHA03379  591 RLARLRAEA----QPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVpamqpqyfDLPlQQPI 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  739 GPRAASPMNHSvqmnSMASVPGM-AISPSRMPQP---PNMMGTHANNIMAQAPTQNQFLP-QNQFPSSSGAMSVNSvgmg 813
Cdd:PHA03379  667 SQGAPLAPLRA----SMGPVPPVpATQPQYFDIPltePINQGASAAHFLPQQPMEGPLVPeRWMFQGATLSQSVRP---- 738
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568994536  814 qPAAQGQVPGAALPNPLNMLAPQASQLPCPPV------TQSPLHPTPPPASTAAG 862
Cdd:PHA03379  739 -GVAQSQYFDLPLTQPINHGAPAAHFLHQPPMegpwvpEQWMFQGAPPSQGTDVV 792
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
852-1046 6.19e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  852 PTPPPASTAAGMPSLQ-HPTAPGmtppqpaaptQPSTPVSSGQTPTPTPGSVPSAAQTQST--PTVQAAAQAQVTPQPQT 928
Cdd:PRK07764  597 GEGPPAPASSGPPEEAaRPAAPA----------APAAPAAPAPAGAAAAPAEASAAPAPGVaaPEHHPKHVAVPDASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  929 PVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTevQTDDAEPEPTE 1008
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSP--AADDPVPLPPE 744
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568994536 1009 SKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEE 1046
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
834-1016 6.48e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   834 APQASQLPCPPVTQSPlHPTPPPASTAAGMPSLQHPTAPgmTPPQPAAPTQPSTPVSsgQTPTPTPGSVPSAAQTQSTPT 913
Cdd:pfam03154  162 AQQQILQTQPPVLQAQ-SGAASPPSPPPPGTTQAATAGP--TPSAPSVPPQGSPATS--QPPNQTQSTAAPHTLIQQTPT 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   914 V--QAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPT-PSSVTSAETSSQQPGPDVPM 990
Cdd:pfam03154  237 LhpQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPA 316
                          170       180
                   ....*....|....*....|....*.
gi 568994536   991 LEMKTEVQTDDAEPEPTESKGEPRSE 1016
Cdd:pfam03154  317 APGQSQQRIHTPPSQSQLQSQQPPRE 342
PHA03247 PHA03247
large tegument protein UL36; Provisional
843-986 6.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  843 PPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPV-----------------SSGQTPTPTPGSVPSA 905
Cdd:PHA03247 2483 PAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirgleelasdDAGDPPPPLPPAAPPA 2562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  906 AQTQSTPTVQAAAQAQVTPQPQTPV---QPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDnrvPTPSSVTSAETSSQ 982
Cdd:PHA03247 2563 APDRSVPPPRPAPRPSEPAVTSRARrpdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD---PPPPSPSPAANEPD 2639

                  ....
gi 568994536  983 QPGP 986
Cdd:PHA03247 2640 PHPP 2643
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
843-989 8.35e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  843 PPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQV 922
Cdd:COG3469    70 AATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTT 149
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994536  923 TPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDnrvPTPSSVTSAETSSQQPGPDVP 989
Cdd:COG3469   150 TTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASG---ATTPSATTTATTTGPPTPGLP 213
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
682-985 8.48e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  682 PALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMS---LGNVQLPQAPMGPRAASPMNHSVQMNSMASV 758
Cdd:PHA03307  108 PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPaagASPAAVASDAASSRQAALPLSSPEETARAPS 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  759 PGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQ--FLPQNQFPSSSGAMSVNSVGMGQPAAQGQVPGAALPNPLNMLAPQ 836
Cdd:PHA03307  188 SPPAEPPPSTPPAAASPRPPRRSSPISASASSPapAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  837 ASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGmtppqpaAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQA 916
Cdd:PHA03307  268 RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG-------SGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAA 340
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994536  917 AAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVH-----TQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPG 985
Cdd:PHA03307  341 VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRapsspAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRP 414
PHA02682 PHA02682
ORF080 virion core protein; Provisional
805-918 9.80e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 40.61  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536  805 MSVNSVGMGQPAAQGQV-PGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPAsTAAGMPSLQHPTAPGMTPPQPAAPT 883
Cdd:PHA02682   66 LKANSACMQRPSGQSPLaPSPACAAPAPACPACAPAAPAPAVTCPAPAPACPPA-TAPTCPPPAVCPAPARPAPACPPST 144
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568994536  884 QPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAA 918
Cdd:PHA02682  145 RQCPPAPPLPTPKPAPAAKPIFLHNQLPPPDYPAA 179
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
799-1016 9.81e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 41.35  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   799 PSSSGAMSVnSVGMGQPAAQGQ--------VPGAALPNPLNMLAPQASQLPCPPvtqSPLHPTPPPASTAAgmPSLQHPt 870
Cdd:pfam08580  430 PGSSPPSSV-IMTPVNKGSKTPssrrgssfDFGSSSERVINSKLRRESKLPQIA---STLKQTKRPSKIPR--ASPNHS- 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994536   871 apgmtppqpaapTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPT---- 946
Cdd:pfam08580  503 ------------GFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTNTNDLDVGHNFKPLTLTTPSPTPSrssr 570
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994536   947 PVHTQPPGTPLSQAA-ASIDNRVPTPSSVTSAETSSQ-----QPGPDVPML-EMKTevqtddaePEPTESKGEPRSE 1016
Cdd:pfam08580  571 SSSTLPPVSPLSRDKsRSPAPTCRSVSRASRRRASRKptrigSPNSRTSLLdEPPY--------PKLTLSKGLPRTP 639
 
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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