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Conserved domains on  [gi|568994538|ref|XP_006521816|]
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histone lysine acetyltransferase CREBBP isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1315-1622 7.74e-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: 7.74e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1315 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1395 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1470 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1525 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1585
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994538  1586 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1622
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1050-1157 1.71e-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: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994538 1130 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.10e-47

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


:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.36  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   548 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994538   628 E 628
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1169-1251 3.32e-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: 3.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1169 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994538 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1678-1718 2.38e-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: 2.38e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994538 1678 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1718
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 ...
1745-1813 1.39e-24

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.39e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994538  1745 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1813
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1986-2087 2.83e-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: 87.97  E-value: 2.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1986 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2054
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994538  2055 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2087
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1253-1284 9.33e-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: 9.33e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994538 1253 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1284
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
COG5076 super family cl34891
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
904-1156 7.43e-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: 7.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  904 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 980
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  981 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1055
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1056 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1135
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994538 1136 RVYKFCSKLAEVFEQEIDPVM 1156
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
PHA03247 super family cl33720
large tegument protein UL36; Provisional
649-999 3.33e-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: 69.58  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  649 SGAQPPVIPPA-------QSVrPPNGPLPLPVNRMQVSQgmnSFNPMSLGNVQLPQAPMGPRAASPMnhsvQMNSMASVP 721
Cdd:PHA03247 2548 AGDPPPPLPPAappaapdRSV-PPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRG----PAPPSPLPP 2619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  722 gmaiSPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVN--SVGMGQPAAQAGVSQGQVPGAALP--NPL 797
Cdd:PHA03247 2620 ----DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPQRPRRRAARPtvGSL 2695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  798 NMLA--------------PQASQLPCPPVTQS--------PLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTP 855
Cdd:PHA03247 2696 TSLAdpppppptpepaphALVSATPLPPGPAAarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  856 VSSGQTPTPTPGSVPSAAQTQSTPT------VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA 929
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS 2855
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  930 -----SIDNRVPTPSSVTSAETSSQQPGPDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 999
Cdd:PHA03247 2856 vapggDVRRRPPSRSPAAKPAAPARPPVRRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-404 4.23e-11

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 60.48  E-value: 4.23e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568994538   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 404
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1933-2323 9.71e-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: 51.16  E-value: 9.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1933 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 1997
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1998 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2074
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2075 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2151
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2152 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2231
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2232 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2311
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994538  2312 NQVRSPAPVQSP 2323
Cdd:pfam09606  437 PAQQRTIGQDSP 448
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
146-479 7.27e-04

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   146 ASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPY 225
Cdd:pfam09606   90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSG 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   226 PAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTgttspfgQPFSQTGGQQMGATGVNPQ---LASKQSM 302
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPA-------DAGAQMGQQAQANGGMNPQqmgGAPNQVA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   303 VNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLllhAHKCQRREQANGEVRACSLP 382
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMS---IGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   383 HCRTMKNVLNHMTHCQAGKACQAI--LGSPASGIQNTIGSVGAGQQ---NATSLSNPNPIDPSSMQRAYAALGLPYMNQP 457
Cdd:pfam09606  320 GNHPAAHQQQMNQSVGQGGQVVALggLNHLETWNPGNFGGLGANPMqrgQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQP 399
                          330       340       350
                   ....*....|....*....|....*....|
gi 568994538   458 QTQlQPQVPGQQPAQ--------PPAHQQM 479
Cdd:pfam09606  400 SVP-SPQGPGSQPPQshpggmipSPALIPS 428
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1315-1622 7.74e-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: 7.74e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1315 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1395 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1470 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1525 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1585
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994538  1586 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1622
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1050-1157 1.71e-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: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994538 1130 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.10e-47

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.36  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   548 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994538   628 E 628
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1047-1155 7.71e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.71e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   1047 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1126
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 568994538   1127 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1155
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1169-1251 3.32e-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: 3.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1169 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994538 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1678-1718 2.38e-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: 2.38e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994538 1678 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1718
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 ...
1745-1813 1.39e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.39e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994538  1745 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1813
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1155-1194 2.60e-24

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


Pssm-ID: 399179  Cd Length: 40  Bit Score: 97.01  E-value: 2.60e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568994538  1155 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1194
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1739-1817 4.62e-24

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 97.82  E-value: 4.62e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   1739 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1814
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 568994538   1815 FCL 1817
Cdd:smart00551   77 KCV 79
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1986-2087 2.83e-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: 87.97  E-value: 2.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1986 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2054
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994538  2055 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2087
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1067-1139 5.03e-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: 5.03e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994538  1067 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1139
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1253-1284 9.33e-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: 9.33e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994538 1253 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1284
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1674-1716 4.47e-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: 4.47e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568994538   1674 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 1716
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
904-1156 7.43e-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: 7.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  904 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 980
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  981 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1055
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1056 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1135
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994538 1136 RVYKFCSKLAEVFEQEIDPVM 1156
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1674-1715 4.35e-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: 74.06  E-value: 4.35e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568994538  1674 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 1715
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
PHA03247 PHA03247
large tegument protein UL36; Provisional
649-999 3.33e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.58  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  649 SGAQPPVIPPA-------QSVrPPNGPLPLPVNRMQVSQgmnSFNPMSLGNVQLPQAPMGPRAASPMnhsvQMNSMASVP 721
Cdd:PHA03247 2548 AGDPPPPLPPAappaapdRSV-PPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRG----PAPPSPLPP 2619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  722 gmaiSPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVN--SVGMGQPAAQAGVSQGQVPGAALP--NPL 797
Cdd:PHA03247 2620 ----DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPQRPRRRAARPtvGSL 2695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  798 NMLA--------------PQASQLPCPPVTQS--------PLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTP 855
Cdd:PHA03247 2696 TSLAdpppppptpepaphALVSATPLPPGPAAarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  856 VSSGQTPTPTPGSVPSAAQTQSTPT------VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA 929
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS 2855
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  930 -----SIDNRVPTPSSVTSAETSSQQPGPDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 999
Cdd:PHA03247 2856 vapggDVRRRPPSRSPAAKPAAPARPPVRRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-404 4.23e-11

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 60.48  E-value: 4.23e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568994538   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 404
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
687-1078 1.14e-09

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 63.91  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  687 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPG-MAISPSRMPQPPN-MMGTHANNIMAQAPTQNQFLPQNQFPSSS 764
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNaVDYSVLVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  765 GAMSVNSVgmgQPAAQAGVSQGQVPGAALPNPLNMLAPQASQlpcppvTQSPLHPTPPPASTAagmPSLQHP--TAPGMT 842
Cdd:COG5665   219 SGRSQHIV---QAAKRVGVEWWGDPSLLATPPATPATEEKSS------QQPKSQPTSPSGGTT---PPSTNQltTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  843 PPQPAAPTQPST---PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvHTQ- 918
Cdd:COG5665   287 STAKAQPQPPTKkqpAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTP-ATDl 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  919 -PPGTPlSQAAASIDNRVpTPSSVTSAETSSQQPG-PDVPMLEMKTEVQTDDAEPE---------------PTESKGEPR 981
Cdd:COG5665   366 aTPVSP-TPPETSVDKKV-SPDSATSSTKSEKEGGtASSPMPPNIAIGAKDDVDATdpsqeakeytknapmTPEADSAPE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  982 SEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPevkveAKEEEENSSNDTASQSTSPSQPRKKIFKPEelrqalmPTL 1061
Cdd:COG5665   444 SSVRTEASPSAGSDLEPENTTLRDPAPNAIPPPED-----PSTIGRLSSGDKLANETGPPVIRRDSTPSS-------TAD 511
                         410
                  ....*....|....*..
gi 568994538 1062 EALYRQDPESLPFRQPV 1078
Cdd:COG5665   512 QSIVGVLAFGLDQRTQA 528
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2039-2081 1.77e-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: 1.77e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568994538 2039 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2081
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
644-986 2.88e-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: 56.31  E-value: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   644 PALPASGAqPPVIPPAQSVRPPNGPLPLpvnrmqvSQGMNSFNPMSLGNVQLPQAPMgPRAASPMNHSVQMNSMASVPG- 722
Cdd:pfam03154  204 PSVPPQGS-PATSQPPNQTQSTAAPHTL-------IQQTPTLHPQRLPSPHPPLQPM-TQPPPPSQVSPQPLPQPSLHGq 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   723 -------MAISPSRMPQPPNMMGTHANNIMAQAptQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPN 795
Cdd:pfam03154  275 mppmphsLQTGPSHMQHPVPPQPFPLTPQSSQS--QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   796 PlNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPS-LQHPTAPGMTPPQPAAPTQPSTP-----VSSGQTPTPTPGSV 869
Cdd:pfam03154  353 P-HIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnLPPPPALKPLSSLSTHHPPSAHPpplqlMPQSQQLPPPPAQP 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   870 PSAAQTQSTPTVQAAAqaqvtpqpqtpvqPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 949
Cdd:pfam03154  432 PVLTQSQSLPPPAASH-------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSAMPGIQ 493
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994538   950 QPGPDVPMLEMKTEVQTDDAEPePTESKGEPRSEMME 986
Cdd:pfam03154  494 PPSSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEE 529
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
855-1016 7.03e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 51.40  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  855 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQpqtpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNR 934
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPA--------VPPPPASAPQQAPAVPLPETTSQLLAARQQLQRA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  935 VPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPrsemMEEDLQGSSQVKEETDTTEQKSEPMEVEEK 1014
Cdd:PRK07994  433 QGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEA----YRWKATNPVEVKKEPVATPKALKKALEHEK 508

                  ..
gi 568994538 1015 KP 1016
Cdd:PRK07994  509 TP 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1933-2323 9.71e-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: 51.16  E-value: 9.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1933 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 1997
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1998 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2074
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2075 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2151
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2152 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2231
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2232 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2311
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994538  2312 NQVRSPAPVQSP 2323
Cdd:pfam09606  437 PAQQRTIGQDSP 448
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
362-401 1.13e-05

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 45.43  E-value: 1.13e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 568994538    362 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGK 401
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
146-479 7.27e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   146 ASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPY 225
Cdd:pfam09606   90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSG 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   226 PAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTgttspfgQPFSQTGGQQMGATGVNPQ---LASKQSM 302
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPA-------DAGAQMGQQAQANGGMNPQqmgGAPNQVA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   303 VNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLllhAHKCQRREQANGEVRACSLP 382
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMS---IGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   383 HCRTMKNVLNHMTHCQAGKACQAI--LGSPASGIQNTIGSVGAGQQ---NATSLSNPNPIDPSSMQRAYAALGLPYMNQP 457
Cdd:pfam09606  320 GNHPAAHQQQMNQSVGQGGQVVALggLNHLETWNPGNFGGLGANPMqrgQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQP 399
                          330       340       350
                   ....*....|....*....|....*....|
gi 568994538   458 QTQlQPQVPGQQPAQ--------PPAHQQM 479
Cdd:pfam09606  400 SVP-SPQGPGSQPPQshpggmipSPALIPS 428
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
628-761 5.56e-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: 41.72  E-value: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   628 EKRRSRLHKQgILGNQPALPASG---------AQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQA 698
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPmgspmggamGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994538   699 PMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQP-PNMMGTHANNI------MAQAP--TQNQFLPQNQFP 761
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 ...
1315-1622 7.74e-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: 7.74e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1315 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1395 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1470 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1525 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 1585
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994538  1586 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 1622
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1050-1157 1.71e-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: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 568994538 1130 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.10e-47

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.36  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   548 GVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 568994538   628 E 628
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1047-1155 7.71e-35

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 129.71  E-value: 7.71e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   1047 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1126
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 568994538   1127 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 1155
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1169-1251 3.32e-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: 3.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1169 FSPQTLCCYGKqlCTIPRD--AAYYSYQNSSpkygllaDRYHFCEKCFTEIQGENVTLGDDpsqPQTTISKDQFEKKKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                  ....*
gi 568994538 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1053-1152 2.84e-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: 2.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1053 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1131
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 568994538 1132 RKTSRVYKFCSKLAEVFEQEI 1152
Cdd:cd04369    79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1073-1150 9.49e-31

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


Pssm-ID: 99930  Cd Length: 102  Bit Score: 117.76  E-value: 9.49e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994538 1073 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1150
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1678-1718 2.38e-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: 2.38e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994538 1678 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 1718
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1052-1152 1.27e-26

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 105.71  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1052 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1131
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|.
gi 568994538 1132 RKTSRVYKFCSKLAEVFEQEI 1152
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1066-1149 1.65e-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: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1066 RQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1145
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                  ....
gi 568994538 1146 EVFE 1149
Cdd:cd05506    93 KIFE 96
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1745-1813 1.39e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.39e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994538  1745 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1813
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1155-1194 2.60e-24

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


Pssm-ID: 399179  Cd Length: 40  Bit Score: 97.01  E-value: 2.60e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568994538  1155 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 1194
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1739-1817 4.62e-24

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 97.82  E-value: 4.62e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   1739 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1814
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 568994538   1815 FCL 1817
Cdd:smart00551   77 KCV 79
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1060-1152 5.92e-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: 5.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1060 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1139
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                          90
                  ....*....|...
gi 568994538 1140 FCSKLAEVFEQEI 1152
Cdd:cd05500    91 MGKRLQAAFEKHL 103
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1055-1154 1.64e-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: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1055 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1133
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                          90       100
                  ....*....|....*....|.
gi 568994538 1134 TSRVYKFCSKLAEVFEQEIDP 1154
Cdd:cd05497    86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1048-1150 3.24e-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: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1048 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKNPMDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 1124
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                          90       100
                  ....*....|....*....|....*.
gi 568994538 1125 NNAWLYNRKTSRVYKFCSKLAEVFEQ 1150
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 ...
1070-1168 8.87e-22

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 92.52  E-value: 8.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1070 ESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKFCSKLAEVF 1148
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                          90       100
                  ....*....|....*....|
gi 568994538 1149 EQEIDPVMQSlgYCCGRKYE 1168
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 ...
1073-1149 2.00e-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: 2.00e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994538 1073 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFE 1149
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1986-2087 2.83e-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: 87.97  E-value: 2.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1986 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 2054
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 568994538  2055 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 2087
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1051-1151 2.79e-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: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1051 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMF 1124
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                          90       100
                  ....*....|....*....|....*..
gi 568994538 1125 NNAWLYNRKTSRVYKFCSKLAEVFEQE 1151
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1067-1139 5.03e-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: 5.03e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994538  1067 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1139
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1253-1284 9.33e-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: 9.33e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568994538 1253 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNC 1284
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1252-1286 3.99e-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: 79.64  E-value: 3.99e-18
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568994538 1252 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1286
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 ...
1051-1141 3.25e-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: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1051 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1130
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                          90
                  ....*....|.
gi 568994538 1131 NRKTSRVYKFC 1141
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1674-1716 4.47e-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: 4.47e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568994538   1674 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 1716
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1253-1286 4.82e-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: 4.82e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568994538 1253 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 1286
Cdd:cd15646     7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
904-1156 7.43e-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: 7.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  904 TPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVtSAETSSQQPGPDVP-MLEMKTEVQTDDAEP--EPTESKGEP 980
Cdd:COG5076     3 FDEVSYSQLGRPSVLKEEFGNELLRLVDNDSSPFPNAP-EEEGSKNLFQKQLKrMPKEYITSIVDDREPgsMANVNDDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  981 RSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENSSNDTASQSTSPSQPRKKIfKPEELRQ 1055
Cdd:COG5076    82 NVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAHLKTSVKKRKTPKIEDELL-YADNKAI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1056 ALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1135
Cdd:COG5076   151 AKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDS 228
                         250       260
                  ....*....|....*....|.
gi 568994538 1136 RVYKFCSKLAEVFEQEIDPVM 1156
Cdd:COG5076   229 SVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1674-1715 4.35e-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: 74.06  E-value: 4.35e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568994538  1674 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 1715
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1056-1146 1.12e-15

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


Pssm-ID: 99944  Cd Length: 98  Bit Score: 74.36  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1056 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1135
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                          90
                  ....*....|.
gi 568994538 1136 RVYKFCSKLAE 1146
Cdd:cd05512    82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1069-1137 1.22e-15

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 74.33  E-value: 1.22e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1069 PESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 1137
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1066-1161 5.07e-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: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1066 RQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 1145
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEML 90
                          90
                  ....*....|....*.
gi 568994538 1146 EVFEQEIDPVMQSLGY 1161
Cdd:cd05511    91 ELAEELLAEREEKLTQ 106
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1086-1139 1.02e-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: 1.02e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1139
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1067-1154 1.40e-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: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1067 QDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN------RKTSRvYKF 1140
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                          90
                  ....*....|....*..
gi 568994538 1141 CSKLAEV---FEQEIDP 1154
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1086-1157 2.40e-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: 2.40e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQ 1157
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1678-1714 7.57e-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: 7.57e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568994538 1678 YTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHK 1714
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1209-1284 9.33e-14

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


Pssm-ID: 277086  Cd Length: 73  Bit Score: 68.15  E-value: 9.33e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1209 FCEKCFTEIQGENVTLGddpsqpQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHY---DIIWPSGFVCDNC 1284
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNgrrNADETAEYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1054-1139 4.14e-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: 4.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1054 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 1133
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSS 81

                  ....*.
gi 568994538 1134 TSRVYK 1139
Cdd:cd05507    82 DHDVYL 87
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1049-1148 1.61e-12

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


Pssm-ID: 99937  Cd Length: 97  Bit Score: 65.64  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1049 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1128
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                          90       100
                  ....*....|....*....|
gi 568994538 1129 LYNRKTSRVYKFCSKLAEVF 1148
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1053-1144 2.89e-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: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1053 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1132
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                          90
                  ....*....|..
gi 568994538 1133 KTSRVYKFCSKL 1144
Cdd:cd05513    79 PDTIYYKAAKKL 90
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1052-1140 1.12e-11

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


Pssm-ID: 99952  Cd Length: 106  Bit Score: 63.50  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1052 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKNPMDLSTIKRKLDtgQYQEPWQYVDDVW 1121
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                          90
                  ....*....|....*....
gi 568994538 1122 LMFNNAWLYNRKTSRVYKF 1140
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 ...
1086-1139 2.77e-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: 2.77e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1139
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYK 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
649-999 3.33e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.58  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  649 SGAQPPVIPPA-------QSVrPPNGPLPLPVNRMQVSQgmnSFNPMSLGNVQLPQAPMGPRAASPMnhsvQMNSMASVP 721
Cdd:PHA03247 2548 AGDPPPPLPPAappaapdRSV-PPPRPAPRPSEPAVTSR---ARRPDAPPQSARPRAPVDDRGDPRG----PAPPSPLPP 2619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  722 gmaiSPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVN--SVGMGQPAAQAGVSQGQVPGAALP--NPL 797
Cdd:PHA03247 2620 ----DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPQRPRRRAARPtvGSL 2695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  798 NMLA--------------PQASQLPCPPVTQS--------PLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTP 855
Cdd:PHA03247 2696 TSLAdpppppptpepaphALVSATPLPPGPAAarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  856 VSSGQTPTPTPGSVPSAAQTQSTPT------VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAA 929
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS 2855
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  930 -----SIDNRVPTPSSVTSAETSSQQPGPDV--PMLEMKTEVQT---DDAEPEPTESKGEPRSEMMEEDLQGSSQVKEET 999
Cdd:PHA03247 2856 vapggDVRRRPPSRSPAAKPAAPARPPVRRLarPAVSRSTESFAlppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
362-404 4.23e-11

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 60.48  E-value: 4.23e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568994538   362 HAHKCQRREQAngevrACSLPHCRTMKNVLNHMTHCQAGKACQ 404
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCP 47
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1086-1144 5.75e-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: 5.75e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 1144
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1085-1153 1.03e-10

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 60.90  E-value: 1.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1085 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEID 1153
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1053-1152 3.38e-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: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1053 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNA 1127
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                          90       100
                  ....*....|....*....|....*
gi 568994538 1128 WLYNRKTSRVYKFCSKLAEVFEQEI 1152
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1075-1138 4.37e-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: 4.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1075 RQPVD-----PQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 1138
Cdd:cd05518    21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
687-1078 1.14e-09

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


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 63.91  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  687 PMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPG-MAISPSRMPQPPN-MMGTHANNIMAQAPTQNQFLPQNQFPSSS 764
Cdd:COG5665   139 GADSLQASSEMALWGPRRVALVVRDGASNPVAVVVTtMIAVPSAPAAPPNaVDYSVLVPIAAQDPAASVSTPQAFNASAT 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  765 GAMSVNSVgmgQPAAQAGVSQGQVPGAALPNPLNMLAPQASQlpcppvTQSPLHPTPPPASTAagmPSLQHP--TAPGMT 842
Cdd:COG5665   219 SGRSQHIV---QAAKRVGVEWWGDPSLLATPPATPATEEKSS------QQPKSQPTSPSGGTT---PPSTNQltTSNTPT 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  843 PPQPAAPTQPST---PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPvHTQ- 918
Cdd:COG5665   287 STAKAQPQPPTKkqpAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTPSSVPSTPAEKDTP-ATDl 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  919 -PPGTPlSQAAASIDNRVpTPSSVTSAETSSQQPG-PDVPMLEMKTEVQTDDAEPE---------------PTESKGEPR 981
Cdd:COG5665   366 aTPVSP-TPPETSVDKKV-SPDSATSSTKSEKEGGtASSPMPPNIAIGAKDDVDATdpsqeakeytknapmTPEADSAPE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  982 SEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPevkveAKEEEENSSNDTASQSTSPSQPRKKIFKPEelrqalmPTL 1061
Cdd:COG5665   444 SSVRTEASPSAGSDLEPENTTLRDPAPNAIPPPED-----PSTIGRLSSGDKLANETGPPVIRRDSTPSS-------TAD 511
                         410
                  ....*....|....*..
gi 568994538 1062 EALYRQDPESLPFRQPV 1078
Cdd:COG5665   512 QSIVGVLAFGLDQRTQA 528
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1679-1717 1.36e-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: 1.36e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568994538 1679 TCNECKHHVE-TRWHCTVCEDYDLCINCYNTKSH-THKMVK 1717
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLK 42
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1051-1152 1.74e-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: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1051 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1128
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                          90       100
                  ....*....|....*....|....
gi 568994538 1129 LYNRKTSRVYKFCSKLAEVFEQEI 1152
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2039-2081 1.77e-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: 1.77e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568994538 2039 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2081
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
PHA03247 PHA03247
large tegument protein UL36; Provisional
630-983 1.88e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.34  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  630 RRSRLHKQGILGNQPALPAS--------GAQPPVIPPAQSVRPPN-GPLPLPVNRMQVSQGMNSFNPMSlGNVQLPQAPM 700
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASSppqrprrrAARPTVGSLTSLADPPPpPPTPEPAPHALVSATPLPPGPAA-ARQASPALPA 2737
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  701 GPRAASPmnhsvqmnsmASVPGMAISPSRMPQPPNMMGTHAnnimAQAPTQNQFLPQNQFPSSsgamsvnsvgmgqPAAQ 780
Cdd:PHA03247 2738 APAPPAV----------PAGPATPGGPARPARPPTTAGPPA----PAPPAAPAAGPPRRLTRP-------------AVAS 2790
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  781 AGVSQGQVPGAalPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPslqhPTAPGmtppqpaaPTQPSTPVSSGQ 860
Cdd:PHA03247 2791 LSESRESLPSP--WDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP----PPPPG--------PPPPSLPLGGSV 2856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  861 TP------TPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQP--PGTPLSQAAASID 932
Cdd:PHA03247 2857 APggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPqpPPPPQPQPPPPPP 2936
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568994538  933 NRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSE 983
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
777-988 2.73e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  777 PAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPvtqsplhPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPV 856
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP-------AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  857 SSGqtPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVP 936
Cdd:PRK07764  663 SDG--GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568994538  937 TPSSVTSAETSSQQPGPDVPMLEmktEVQTDDAEPEPTESKGEPRSEMMEED 988
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 ...
1086-1150 6.31e-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: 6.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1150
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1086-1150 2.02e-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: 2.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994538 1086 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 1150
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
644-986 2.88e-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: 56.31  E-value: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   644 PALPASGAqPPVIPPAQSVRPPNGPLPLpvnrmqvSQGMNSFNPMSLGNVQLPQAPMgPRAASPMNHSVQMNSMASVPG- 722
Cdd:pfam03154  204 PSVPPQGS-PATSQPPNQTQSTAAPHTL-------IQQTPTLHPQRLPSPHPPLQPM-TQPPPPSQVSPQPLPQPSLHGq 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   723 -------MAISPSRMPQPPNMMGTHANNIMAQAptQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPN 795
Cdd:pfam03154  275 mppmphsLQTGPSHMQHPVPPQPFPLTPQSSQS--QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   796 PlNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPS-LQHPTAPGMTPPQPAAPTQPSTP-----VSSGQTPTPTPGSV 869
Cdd:pfam03154  353 P-HIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnLPPPPALKPLSSLSTHHPPSAHPpplqlMPQSQQLPPPPAQP 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   870 PSAAQTQSTPTVQAAAqaqvtpqpqtpvqPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 949
Cdd:pfam03154  432 PVLTQSQSLPPPAASH-------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSAMPGIQ 493
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568994538   950 QPGPDVPMLEMKTEVQTDDAEPePTESKGEPRSEMME 986
Cdd:pfam03154  494 PPSSASVSSSGPVPAAVSCPLP-PVQIKEEALDEAEE 529
PHA03247 PHA03247
large tegument protein UL36; Provisional
644-914 6.12e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  644 PALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSfnPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGM 723
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  724 AISPSRMPQPPnmmGTHANNIMAQAPTQNQFLPQNQF----PSSSGAmsvnsvgmGQPAAQAGVSQGQVPGAALPNPLNM 799
Cdd:PHA03247 2829 PPPTSAQPTAP---PPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPA--------AKPAAPARPPVRRLARPAVSRSTES 2897
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  800 LAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGS-------VPSA 872
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlvpgrvaVPRF 2977
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568994538  873 AQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP 914
Cdd:PHA03247 2978 RVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDP 3019
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1051-1108 8.75e-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: 8.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538 1051 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKNPMDLSTI-KRKLDTG 1108
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
428-949 9.24e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.39  E-value: 9.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   428 ATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPmSIPAGGITTDQQPPNLI 507
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   508 SESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVrkgwhehvtQDLRSHLVHKLVQaifPTPDPAALKDRRM 587
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP---------QPLPQPSLHGQMP---PMPHSLQTGPSHM 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   588 EnlvayakkvegdmyesansrdeyyHLLAEKIYKIQKELEEKrrsrlhkQGILGNQPALPASGAQPPVIPPAQSVRPPNG 667
Cdd:pfam03154  290 Q------------------------HPVPPQPFPLTPQSSQS-------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   668 P---LPLPVNrmqvsqgmnsfnPMSLGNVQLPQAPMGPRAASPMNHsvQMNSMASVPGMAISPSRMPQPPnmmgthANNI 744
Cdd:pfam03154  339 PpreQPLPPA------------PLSMPHIKPPPTTPIPQLPNPQSH--KHPPHLSGPSPFQMNSNLPPPP------ALKP 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   745 MAQAPTQNqflpqnqfpsssgamsvnsvgmgqpaaqagvsqgqvPGAALPNPLNMLaPQASQLPCPPV-----TQSPLHp 819
Cdd:pfam03154  399 LSSLSTHH------------------------------------PPSAHPPPLQLM-PQSQQLPPPPAqppvlTQSQSL- 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   820 tPPPAStaagmpslQHPTaPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQP 899
Cdd:pfam03154  441 -PPPAA--------SHPP-TSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAV 510
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 568994538   900 PSVATPQSSQQQPTPVHTQPPGTPLSQAAASidnrvPTPSSVTSAETSSQ 949
Cdd:pfam03154  511 SCPLPPVQIKEEALDEAEEPESPPPPPRSPS-----PEPTVVNTPSHASQ 555
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1051-1152 3.42e-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: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538 1051 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1130
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                          90       100
                  ....*....|....*....|..
gi 568994538 1131 NRKTSRVYKFCSKLAEVFEQEI 1152
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1085-1150 4.52e-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: 4.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568994538 1085 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKFCSKLAEVFEQ 1150
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
761-1008 5.28e-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: 51.50  E-value: 5.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   761 PSSSG--AMSVNSVGMGQPAAQAGVSQGQVPGAALPNP--LNMLAPQAsQLPCPPVTQSPLHPTPPPASTAAGMPSLQHP 836
Cdd:pfam17823  100 PATREgaADGAASRALAAAASSSPSSAAQSLPAAIAALpsEAFSAPRA-AACRANASAAPRAAIAAASAPHAASPAPRTA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   837 TAPGMTPPQPAAPTQPSTP--VSSGQTPTPTPGSVPSAAQTqSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP 914
Cdd:pfam17823  179 ASSTTAASSTTAASSAPTTaaSSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   915 VHTQPpgtpLSQAAASID-----NRVPTPSSVTSAETSSQQPGPDV------PMLEMKTEVQTDDAEPEPTESKGEPRSE 983
Cdd:pfam17823  258 AAAGT----VASAAGTINmgdphARRLSPAKHMPSDTMARNPAAPMgaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTLE 333
                          250       260
                   ....*....|....*....|....*
gi 568994538   984 MMEEDLQGSSQVKEETDTTEQKSEP 1008
Cdd:pfam17823  334 PNTPKSVASTNLAVVTTTKAQAKEP 358
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
855-1016 7.03e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 51.40  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  855 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQpqtpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNR 934
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPA--------VPPPPASAPQQAPAVPLPETTSQLLAARQQLQRA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  935 VPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPrsemMEEDLQGSSQVKEETDTTEQKSEPMEVEEK 1014
Cdd:PRK07994  433 QGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEA----YRWKATNPVEVKKEPVATPKALKKALEHEK 508

                  ..
gi 568994538 1015 KP 1016
Cdd:PRK07994  509 TP 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1933-2323 9.71e-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: 51.16  E-value: 9.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1933 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSMPpgQWQQA 1997
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTASNL--LASLG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  1998 PIPQQQPMPGMPRP---VMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFI 2074
Cdd:pfam09606  129 RPQMPMGGAGFPSQmsrVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2075 KQRTAKYVANQPGMQP---QPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPgh 2151
Cdd:pfam09606  209 MPGPADAGAQMGQQAQangGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2152 NPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNsaslaggmAGHSQFQQPQGPGGYAPAMQQQRMQQhLPIQGSS 2231
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--------AHQQQMNQSVGQGGQVVALGGLNHLE-TWNPGNF 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  2232 MGQMAAPMGQlGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS 2311
Cdd:pfam09606  358 GGLGANPMQR-GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
                          410
                   ....*....|..
gi 568994538  2312 NQVRSPAPVQSP 2323
Cdd:pfam09606  437 PAQQRTIGQDSP 448
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
362-401 1.13e-05

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 45.43  E-value: 1.13e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 568994538    362 HAHKCQRREQAngevraCSLPHCRTMKNVLNHMTHCQAGK 401
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK 49
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1680-1711 2.13e-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: 2.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568994538 1680 CNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 1711
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKH 36
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
775-980 3.84e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  775 GQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTppqpaaPTQPST 854
Cdd:PRK07764  622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAA------PAAPAG 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  855 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAqvtpqpqtpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNR 934
Cdd:PRK07764  696 AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGA-------------SAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP 762
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568994538  935 VPTPSSVTSAETSSQQPGPDVPMLEmktevqtDDAEPEPTESKGEP 980
Cdd:PRK07764  763 APAPAAAPAAAPPPSPPSEEEEMAE-------DDAPSMDDEDRRDA 801
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
564-886 6.55e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.47  E-value: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   564 HLVHKLVQAIFPTPDPAALKDRRMENLVayakkvegdmYESANSRDEYYHLLAEKIYKIqKELEEKRRsrlhkqgilgnQ 643
Cdd:pfam09606    2 SVVNKIEEALQQNGQTSTKNAREMENHV----------FAKARTKDEYLGTVARLILHV-RDMSKKAA-----------Q 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   644 PALPASGAQPPVIPPAQSVRPPngplplPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPR-------------------- 703
Cdd:pfam09606   60 QQQPQGGQGNGGMGGGQQGMPD------PINALQNLAGQGTRPQMMGPMGPGPGGPMGQQmggpgtasnllaslgrpqmp 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   704 -----AASPMNHSVQMNSMASVPGM--AISPSRMPQPPNMMGTHANNIMAQAPTQN---QFLPQNQFPSSSGAMsvnsvG 773
Cdd:pfam09606  134 mggagFPSQMSRVGRMQPGGQAGGMmqPSSGQPGSGTPNQMGPNGGPGQGQAGGMNggqQGPMGGQMPPQMGVP-----G 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   774 MGQPAAQAGVSQGQVPGAALPNPLNML-----APQASQLPCPPVTQSPLHPTP-PPASTAAGMPSLQHPTAPGMTPPQPA 847
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGMNPQQMGgapnqVAMQQQQPQQQGQQSQLGMGInQMQQMPQGVGGGAGQGGPGQPMGPPG 288
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568994538   848 APTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQ 886
Cdd:pfam09606  289 QQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ 327
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
776-981 9.03e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.95  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  776 QPAAQAGvSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQhptAPGMTPPQPAAPTQPSTP 855
Cdd:PRK12323  364 RPGQSGG-GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAA---APARRSPAPEALAAARQA 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  856 VSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPlSQAAASIDNRV 935
Cdd:PRK12323  440 SARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA-SPAPAQPDAAP 518
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568994538  936 PTPSSVTSAETSSQQPGPDVPMLE---MKTEVQTDDAEPEPTESKGEPR 981
Cdd:PRK12323  519 AGWVAESIPDPATADPDDAFETLApapAAAPAPRAAAATEPVVAPRPPR 567
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1679-1718 1.59e-04

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


Pssm-ID: 239085  Cd Length: 49  Bit Score: 41.42  E-value: 1.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568994538 1679 TCNECK--HHVETRWHCTVCEDYDLCINCY--NTKSHTHKMVKW 1718
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkGRETKRHNSLHI 45
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
823-961 1.63e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  823 PASTAAGMPSLQHPTAPGmtppqpaaptQPSTPVSSGQTPTPTPGSVPS-AAQTQSTPTVQAAAQAQVTPQPQTPVQPPS 901
Cdd:PRK07764  386 GVAGGAGAPAAAAPSAAA----------AAPAAAPAPAAAAPAAAAAPApAAAPQPAPAPAPAPAPPSPAGNAPAGGAPS 455
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  902 VATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMK 961
Cdd:PRK07764  456 PPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER 515
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1678-1717 1.70e-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: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568994538 1678 YTCNECKHH--VETRWHCTVC--EDYDLCINC-YNTKSH--THKMVK 1717
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1678-1706 2.82e-04

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


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 40.74  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568994538 1678 YTCNECKHHV--ETRWHCTVCEDYDLCINCY 1706
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
839-977 3.25e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.01  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  839 PGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQ--SSQQQPTPVH 916
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlqRAQGATKAKK 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568994538  917 TQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESK 977
Cdd:PRK07994  441 SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALK 501
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
797-980 4.20e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  797 LNMLAPQasqlPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGmtppqpAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQ 876
Cdd:PRK07003  353 LRMLAFE----PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVG------ASAVPAVTAVTGAAGAALAPKAAAAAAATR 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  877 STPTVQAAAQAQV-----TPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPS-SVTSAETSSQQ 950
Cdd:PRK07003  423 AEAPPAAPAPPATadrgdDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFePAPRAAAPSAA 502
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568994538  951 PGPDVPMLEMKTEVQTDD-----AEPEPTESKGEP 980
Cdd:PRK07003  503 TPAAVPDARAPAAASREDapaaaAPPAPEARPPTP 537
PRK10263 PRK10263
DNA translocase FtsK; Provisional
801-1082 5.26e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  801 APQASQLPCPPVTQSPLHPTPPPASTaagMPSLQHPTAPGMtppqpaaptqpstpvssgQTPTPTPGSVPSAAQTQSTPT 880
Cdd:PRK10263  329 ATQSWAAPVEPVTQTPPVASVDVPPA---QPTVAWQPVPGP------------------QTGEPVIAPAPEGYPQQSQYA 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  881 VQAAAQaqvtpqpqtpvqppsvatpQSSQQQPTPVHtQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEM 960
Cdd:PRK10263  388 QPAVQY-------------------NEPLQQPVQPQ-QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAW 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  961 KTEVQTDDAEPEPTESKGEPRSE-MMEEDLQGSSQVKEETDTTEqkSEPmEVEEkkpevkveakeeeenssndtasqsTS 1039
Cdd:PRK10263  448 QAEEQQSTFAPQSTYQTEQTYQQpAAQEPLYQQPQPVEQQPVVE--PEP-VVEE------------------------TK 500
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568994538 1040 PSQPRKKIFKP-EELRQALMPTLEALYRQDPESLPFRQPVDPQL 1082
Cdd:PRK10263  501 PARPPLYYFEEvEEKRAREREQLAAWYQPIPEPVKEPEPIKSSL 544
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
762-950 5.55e-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: 45.29  E-value: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   762 SSSGAMSVNSVGMGQPAAQAGVSqgqvpgAALPNPLNMLAPQAS---------QLPCPPVTQS---PLHPTPPPAS--TA 827
Cdd:pfam05109  427 STTTSPTLNTTGFAAPNTTTGLP------SSTHVPTNLTAPASTgptvstadvTSPTPAGTTSgasPVTPSPSPRDngTE 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   828 AGMPSLQHPTApgmtpPQPAAPTQPSTPVSSGQTPTPTPGS------VPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPS 901
Cdd:pfam05109  501 SKAPDMTSPTS-----AVTTPTPNATSPTPAVTTPTPNATSptlgktSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLG 575
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568994538   902 VATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRV----------PTPSSVTSAETSSQQ 950
Cdd:pfam05109  576 KTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLggtsstpvvtSPPKNATSAVTTGQH 634
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
775-887 6.32e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  775 GQPAAQAGVSQGQVPGAALPnplnmlAPQASQLPCPPVTQSPlHPTPPPAStaagmpslQHPTAPGMTPPQPAAPTQPST 854
Cdd:PRK07764  396 AAAPSAAAAAPAAAPAPAAA------APAAAAAPAPAAAPQP-APAPAPAP--------APPSPAGNAPAGGAPSPPPAA 460
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568994538  855 PVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQA 887
Cdd:PRK07764  461 APSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAA 493
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
146-479 7.27e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   146 ASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPY 225
Cdd:pfam09606   90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSG 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   226 PAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTgttspfgQPFSQTGGQQMGATGVNPQ---LASKQSM 302
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPA-------DAGAQMGQQAQANGGMNPQqmgGAPNQVA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   303 VNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLllhAHKCQRREQANGEVRACSLP 382
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMS---IGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   383 HCRTMKNVLNHMTHCQAGKACQAI--LGSPASGIQNTIGSVGAGQQ---NATSLSNPNPIDPSSMQRAYAALGLPYMNQP 457
Cdd:pfam09606  320 GNHPAAHQQQMNQSVGQGGQVVALggLNHLETWNPGNFGGLGANPMqrgQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQP 399
                          330       340       350
                   ....*....|....*....|....*....|
gi 568994538   458 QTQlQPQVPGQQPAQ--------PPAHQQM 479
Cdd:pfam09606  400 SVP-SPQGPGSQPPQshpggmipSPALIPS 428
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
778-982 7.35e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.84  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  778 AAQAGVSQGQVPGAAlPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPgmtppqpaapTQPSTPVS 857
Cdd:PRK07003  366 GAPGGGVPARVAGAV-PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP----------PAAPAPPA 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  858 SG---QTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTpvqppSVATPQSSQQQPTPVHTQPPGTPLSQAAAsidNR 934
Cdd:PRK07003  435 TAdrgDDAADGDAPVPAKANARASADSRCDERDAQPPADSG-----SASAPASDAPPDAAFEPAPRAAAPSAATP---AA 506
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568994538  935 VPTPSSVTSAETssqqpgPDVPmlEMKTEVQTDDAEPEPTESKGEPRS 982
Cdd:PRK07003  507 VPDARAPAAASR------EDAP--AAAAPPAPEARPPTPAAAAPAARA 546
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
773-887 7.67e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  773 GMGQPAAQAGVSQGQVPGAALPNPLNMlAPQASQLPCPPVTQSPlHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQP 852
Cdd:PRK07764  389 GGAGAPAAAAPSAAAAAPAAAPAPAAA-APAAAAAPAPAAAPQP-APAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568994538  853 STPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQA 887
Cdd:PRK07764  467 APAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
761-983 1.21e-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: 44.05  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   761 PSSSGAMSVnSVGMGQPAAQAGVSQGQV---PGAALPNPLNMLAPQASQLPCPPvtqSPLHPTPPPASTAAgmPSLQHPt 837
Cdd:pfam08580  430 PGSSPPSSV-IMTPVNKGSKTPSSRRGSsfdFGSSSERVINSKLRRESKLPQIA---STLKQTKRPSKIPR--ASPNHS- 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   838 apgmtppqpaapTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPT---- 913
Cdd:pfam08580  503 ------------GFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTNTNDLDVGHNFKPLTLTTPSPTPSrssr 570
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994538   914 PVHTQPPGTPLSQAA-ASIDNRVPTPSSVTSAETSSQ-----QPGPDVPML-EMKTevqtddaePEPTESKGEPRSE 983
Cdd:pfam08580  571 SSSTLPPVSPLSRDKsRSPAPTCRSVSRASRRRASRKptrigSPNSRTSLLdEPPY--------PKLTLSKGLPRTP 639
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
778-956 1.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.07  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  778 AAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQhpTAPGMTPPQPAAPTQPSTPVS 857
Cdd:PRK07003  357 AFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPK--AAAAAAATRAEAPPAAPAPPA 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  858 SG---QTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTP------VHTQPPGTPLSQAA 928
Cdd:PRK07003  435 TAdrgDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPraaapsAATPAAVPDARAPA 514
                         170       180
                  ....*....|....*....|....*...
gi 568994538  929 ASIDNRVPTPSSVTSAETSSQQPGPDVP 956
Cdd:PRK07003  515 AASREDAPAAAAPPAPEARPPTPAAAAP 542
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1679-1714 1.69e-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: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568994538 1679 TCNECKHH--VETRWHCTVCEDYDLCINCYNTKSHTHK 1714
Cdd:cd02344     2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKHNTR 39
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1679-1712 2.02e-03

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 38.10  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568994538 1679 TCNECKHHVET--RWHCTVCEDYDLCINCYNTKSHT 1712
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 ...
1678-1707 2.39e-03

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


Pssm-ID: 239076  Cd Length: 45  Bit Score: 37.68  E-value: 2.39e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568994538 1678 YTCNEC-KHHVETRWHCTVCEDYDLCINCYN 1707
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ 31
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
789-921 2.67e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  789 PGAALPNPlnmlAPQASQLPCPPVTQSPLhPTPPPASTAAGMPslqHPTAPGMTPPQPAAPTQPSTPVSSGQ---TPTPT 865
Cdd:PRK14951  366 PAAAAEAA----APAEKKTPARPEAAAPA-AAPVAQAAAAPAP---AAAPAAAASAPAAPPAAAPPAPVAAPaaaAPAAA 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568994538  866 PGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSS-QQQPTPVHTQPPG 921
Cdd:PRK14951  438 PAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAaAPAAARLTPTEEG 494
PHA03379 PHA03379
EBNA-3A; Provisional
630-829 3.34e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 42.74  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  630 RRSRLHKQGilgnQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNV--------QLP-QAPM 700
Cdd:PHA03379  591 RLARLRAEA----QPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVpamqpqyfDLPlQQPI 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  701 GPRAASPMNHSvqmnSMASVPGM-AISPSRMPQP---PNMMGTHANNIMAQAPTQNQFLP-QNQFPSSSGAMSVnsvgmg 775
Cdd:PHA03379  667 SQGAPLAPLRA----SMGPVPPVpATQPQYFDIPltePINQGASAAHFLPQQPMEGPLVPeRWMFQGATLSQSV------ 736
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  776 qpaaQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPV------TQSPLHPTPPPASTAAG 829
Cdd:PHA03379  737 ----RPGVAQSQYFDLPLTQPINHGAPAAHFLHQPPMegpwvpEQWMFQGAPPSQGTDVV 792
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
797-932 3.78e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  797 LNMLA--PQASQLPCPPVTQSPlhPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSgqtPTPTPGSVPSAAQ 874
Cdd:PRK14951  359 LRLLAfkPAAAAEAAAPAEKKT--PARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAA---APPAPVAAPAAAA 433
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568994538  875 TQSTPTVqAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASID 932
Cdd:PRK14951  434 PAAAPAA-APAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
PRK10263 PRK10263
DNA translocase FtsK; Provisional
436-946 4.10e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  436 PIDPSsMQRAYAALGLPYMNQPQTQLQPqVPGQQPAQP---------PAHQQMRTLNALGNNPMSIPAGGITTDQQPPNL 506
Cdd:PRK10263  336 PVEPV-TQTPPVASVDVPPAQPTVAWQP-VPGPQTGEPviapapegyPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAE 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  507 ISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGvrkgWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRR 586
Cdd:PRK10263  414 QPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQST----FAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPV 489
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  587 MENlvayakkvEGDMYESANSRDEYYHLlaekiykiqKELEEKR---RSRLHK------QGILGNQPALP-ASGAQPPVI 656
Cdd:PRK10263  490 VEP--------EPVVEETKPARPPLYYF---------EEVEEKRareREQLAAwyqpipEPVKEPEPIKSsLKAPSVAAV 552
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  657 PPAQSVrPPNGPLPLPVNRMQVSQGMNS------FNPMSlGNVQLPQAP--MGPRAASPMNHSVQMNSMASVPGMAISPS 728
Cdd:PRK10263  553 PPVEAA-AAVSPLASGVKKATLATGAAAtvaapvFSLAN-SGGPRPQVKegIGPQLPRPKRIRVPTRRELASYGIKLPSQ 630
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  729 RMPQ------------------PPNMMGTHANNIMAQ-APTQNQ-FLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQ--- 785
Cdd:PRK10263  631 RAAEekareaqrnqydsgdqynDDEIDAMQQDELARQfAQTQQQrYGEQYQHDVPVNAEDADAAAEAELARQFAQTQqqr 710
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  786 --GQVPGAALPNPLNML--APQASQL---PCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSS 858
Cdd:PRK10263  711 ysGEQPAGANPFSLDDFefSPMKALLddgPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQ 790
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  859 GQTPTPTPGSVPSAAQTQStptvqaaaqaQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQP------------------- 919
Cdd:PRK10263  791 YQQPQQPVAPQPQYQQPQQ----------PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPqdtllhpllmrngdsrplh 860
                         570       580
                  ....*....|....*....|....*...
gi 568994538  920 -PGTPLsqaaASIDNRVPTPSSVTSAET 946
Cdd:PRK10263  861 kPTTPL----PSLDLLTPPPSEVEPVDT 884
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
644-952 4.72e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  644 PALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMS---LGNVQLPQAPMGPRAASPMNHSVQMNSMASV 720
Cdd:PHA03307  108 PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPaagASPAAVASDAASSRQAALPLSSPEETARAPS 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  721 PGMAISPSRMPQPPNMMGTHANNIMAQAPTQnqfLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNML 800
Cdd:PHA03307  188 SPPAEPPPSTPPAAASPRPPRRSSPISASAS---SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  801 APQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGmtppqpaAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPT 880
Cdd:PHA03307  265 LPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG-------SGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994538  881 VQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVH-----TQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPG 952
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRapsspAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRP 414
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
628-761 5.56e-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: 41.72  E-value: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   628 EKRRSRLHKQgILGNQPALPASG---------AQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQA 698
Cdd:TIGR01628  365 EQRRAHLQDQ-FMQLQPRMRQLPmgspmggamGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994538   699 PMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQP-PNMMGTHANNI------MAQAP--TQNQFLPQNQFP 761
Cdd:TIGR01628  444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPqPQSTASQGGQNkklaqvLASATpqMQKQVLGERLFP 515
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
761-956 6.43e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.66  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  761 PSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLA-------PQASQLPCPPVTQSPLHPTPPPASTAAGMPSL 833
Cdd:COG3469    14 GASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASgsagsgtGTTAASSTAATSSTTSTTATATAAAAAATSTS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  834 QHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPT 913
Cdd:COG3469    94 ATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTT 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568994538  914 PVHTQPPGTPLSQAAASIDnrvPTPSSVTSAETSSQQPGPDVP 956
Cdd:COG3469   174 SASTTPSATTTATATTASG---ATTPSATTTATTTGPPTPGLP 213
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
819-1013 6.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  819 PTPPPASTAAGMPSLQ-HPTAPGmtppqpaaptQPSTPVSSGQTPTPTPGSVPSAAQTQST--PTVQAAAQAQVTPQPQT 895
Cdd:PRK07764  597 GEGPPAPASSGPPEEAaRPAAPA----------APAAPAAPAPAGAAAAPAEASAAPAPGVaaPEHHPKHVAVPDASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  896 PVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTevQTDDAEPEPTE 975
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSP--AADDPVPLPPE 744
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568994538  976 SKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEE 1013
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
801-983 7.31e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 7.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   801 APQASQLPCPPVTQSPlHPTPPPASTAAGMPSLQHPTAPgmTPPQPAAPTQPSTPVSsgQTPTPTPGSVPSAAQTQSTPT 880
Cdd:pfam03154  162 AQQQILQTQPPVLQAQ-SGAASPPSPPPPGTTQAATAGP--TPSAPSVPPQGSPATS--QPPNQTQSTAAPHTLIQQTPT 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538   881 V--QAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPT-PSSVTSAETSSQQPGPDVPM 957
Cdd:pfam03154  237 LhpQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPqPFPLTPQSSQSQVPPGPSPA 316
                          170       180
                   ....*....|....*....|....*.
gi 568994538   958 LEMKTEVQTDDAEPEPTESKGEPRSE 983
Cdd:pfam03154  317 APGQSQQRIHTPPSQSQLQSQQPPRE 342
PHA03247 PHA03247
large tegument protein UL36; Provisional
810-953 7.44e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  810 PPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPV-----------------SSGQTPTPTPGSVPSA 872
Cdd:PHA03247 2483 PAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirgleelasdDAGDPPPPLPPAAPPA 2562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994538  873 AQTQSTPTVQAAAQAQVTPQPQTPV---QPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDnrvPTPSSVTSAETSSQ 949
Cdd:PHA03247 2563 APDRSVPPPRPAPRPSEPAVTSRARrpdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD---PPPPSPSPAANEPD 2639

                  ....
gi 568994538  950 QPGP 953
Cdd:PHA03247 2640 PHPP 2643
 
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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