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Conserved domains on  [gi|514648707|ref|XP_004998720|]
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CBP-A protein [Salpingoeca rosetta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAT_KAT11 super family cl02120
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1278-1456 9.72e-47

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.


The actual alignment was detected with superfamily member pfam08214:

Pssm-ID: 413203  Cd Length: 348  Bit Score: 172.58  E-value: 9.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1278 PESFPYKSKALFVFQRIDGGrDLCFFGLHVQEYGEDCPEPNRRRVYISYLDSVNLFEPKsYRTTVYHELLIGYLYYVAKL 1357
Cdd:pfam08214   42 KPEFTYKEKHFFALSEIDGV-EVIFFGLEVQVYGTVCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1358 GFLHAHIWACPPSPGDDYMFhchP-----PNQRVPTSKRLQAWYRDMLIK--------AKERGVI--------------- 1409
Cdd:pfam08214  120 GYLRAVIWALFTRAQDQYLF---PnssknPKKHVLDGKGLLKWWCKMLDKilveykssAKAKLVIpgkdifktrkylpat 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 514648707  1410 --QDWCDLQQYVDSERLSEARQLPYFDGDFWPNQLEQIVQE-----INKDEEEE 1456
Cdd:pfam08214  197 adPLWLVGHIFHQICDDPARYEIPLFPDDPKPRFLEELIKEgrwksVSLDQFWE 250
Bromodomain super family cl02556
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 980-1086 4.59e-40

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


The actual alignment was detected with superfamily member cd05495:

Pssm-ID: 445827  Cd Length: 108  Bit Score: 144.51  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  980 REELLHHFWPLHEKI-RSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFT 1058
Cdd:cd05495     1 PEELRQALMPTLEKLyKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 514648707 1059 YNGEKSIVGKMAKTLFNLWNAEIEPIMK 1086
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 699-767 3.78e-27

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: 106.32  E-value: 3.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514648707   699 IHRQLTLLLHAYRCRNPN---CQVKFCGDMKRVLKHMASCQKNKSCPYPHCGSSKQLLAHYSSCSNPKCPYC 767
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1098-1172 1.60e-20

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: 87.35  E-value: 1.60e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514648707 1098 FNPPTLYCNGKnlCTIPRE--SKYMSYRTSTLIVNYCPKCWKKLPTGPVKITDENGQEVPveRSQFEEKVNNELEYE 1172
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLDNRYHFCEKCFNEIRGDEITLGDDQGTSIS--KSQFEKKKNDELDEE 73
ZZ super family cl00295
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1584-1626 1.54e-11

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.


The actual alignment was detected with superfamily member cd02337:

Pssm-ID: 412288  Cd Length: 41  Bit Score: 60.65  E-value: 1.54e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 514648707 1584 YVCDLCKHsisAVDSRYHCVGgCEDYDLCKSCYESQGHEHKME 1626
Cdd:cd02337     1 YTCNECKH---HVETRWHCTV-CEDYDLCITCYNTKNHPHKME 39
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1643-1708 2.01e-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: 61.25  E-value: 2.01e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514648707  1643 QQAASLLTHANVCTDAN---CQVKQCSILKRYLQHANTCRRHyRECK--HCRTYWTILRyHASHCREDPCP 1708
Cdd:pfam02135    2 QRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRG-GGCPypHCKRSRQLLR-HAKNCKDEDCP 70
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
 1173-1204 9.72e-10

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: 55.35  E-value: 9.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 514648707 1173 KLIECHVCKRRQHQICELYHEH-FNQPFVCSHC 1204
Cdd:cd15557     5 QFVECKECGRKWHQICVLHNDEiWPNGFICDNC 37
KIX super family cl44390
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 884-957 3.71e-05

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.


The actual alignment was detected with superfamily member pfam02172:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 44.02  E-value: 3.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514648707   884 DWRAALKdvKSLRIKLREKVIAALSKCVSPEEKA-GTQDRIKSLGAKIEDQAFHKSQTQKEYFEMLAQRIYQLQK 957
Cdd:pfam02172    5 DWHSRVT--RDLRNHLVHKLVQAIFPTPDQNAMNdGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQK 77
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1278-1456 9.72e-47

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: 172.58  E-value: 9.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1278 PESFPYKSKALFVFQRIDGGrDLCFFGLHVQEYGEDCPEPNRRRVYISYLDSVNLFEPKsYRTTVYHELLIGYLYYVAKL 1357
Cdd:pfam08214   42 KPEFTYKEKHFFALSEIDGV-EVIFFGLEVQVYGTVCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1358 GFLHAHIWACPPSPGDDYMFhchP-----PNQRVPTSKRLQAWYRDMLIK--------AKERGVI--------------- 1409
Cdd:pfam08214  120 GYLRAVIWALFTRAQDQYLF---PnssknPKKHVLDGKGLLKWWCKMLDKilveykssAKAKLVIpgkdifktrkylpat 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 514648707  1410 --QDWCDLQQYVDSERLSEARQLPYFDGDFWPNQLEQIVQE-----INKDEEEE 1456
Cdd:pfam08214  197 adPLWLVGHIFHQICDDPARYEIPLFPDDPKPRFLEELIKEgrwksVSLDQFWE 250
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 980-1086 4.59e-40

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: 144.51  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  980 REELLHHFWPLHEKI-RSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFT 1058
Cdd:cd05495     1 PEELRQALMPTLEKLyKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 514648707 1059 YNGEKSIVGKMAKTLFNLWNAEIEPIMK 1086
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
BROMO smart00297
bromo domain;
987-1084 4.60e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 118.54  E-value: 4.60e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707    987 FWPLHEKIRSHEDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIV 1066
Cdd:smart00297   12 LKAVLDKLDSHPLSWPFLKPVSRKEA--PDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEV 89

                            90
                    ....*....|....*...
gi 514648707   1067 GKMAKTLFNLWNAEIEPI 1084
Cdd:smart00297   90 YKDAKKLEKFFEKKLREL 107
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 699-767 3.78e-27

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: 106.32  E-value: 3.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514648707   699 IHRQLTLLLHAYRCRNPN---CQVKFCGDMKRVLKHMASCQKNKSCPYPHCGSSKQLLAHYSSCSNPKCPYC 767
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1098-1172 1.60e-20

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: 87.35  E-value: 1.60e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514648707 1098 FNPPTLYCNGKnlCTIPRE--SKYMSYRTSTLIVNYCPKCWKKLPTGPVKITDENGQEVPveRSQFEEKVNNELEYE 1172
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLDNRYHFCEKCFNEIRGDEITLGDDQGTSIS--KSQFEKKKNDELDEE 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
698-770 2.30e-20

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 87.04  E-value: 2.30e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514648707    698 VIHRQLTLLLHAYRC--RNPNCQVKFCGDMKRVLKHMASCqKNKSCPYPHCGSSKQLLAHYSSCSNPKCPYCRPI 770
Cdd:smart00551    6 QLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSC-KVRKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 992-1072 2.68e-20

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: 86.98  E-value: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707   992 EKIRSHEDSHPFLEPVDTVALNcsDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAK 1071
Cdd:pfam00439    6 DKLMEHPIAAPFLEPVDPDEYP--DYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAE 83


                   .
gi 514648707  1072 T 1072
Cdd:pfam00439   84 K 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 935-1088 9.09e-20

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 93.72  E-value: 9.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  935 FHKSQTQKEYFeMLAQRIYQLQKAQASRTPTGSAHKLVPKPKKWDREELL--HHFWPLHEKIR-----SHEDSHPFLEPV 1007
Cdd:COG5076    95 RPESLRFDEIV-FLAIESVTPESGLGSLLMAHLKTSVKKRKTPKIEDELLyaDNKAIAKFKKQlflrdGRFLSSIFLGLP 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707 1008 DTvaLNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLWNAEIEPIMKR 1087
Cdd:COG5076   174 SK--REYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEE 251


                  .
gi 514648707 1088 M 1088
Cdd:COG5076   252 M 252
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1084-1123 1.80e-18

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: 80.44  E-value: 1.80e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 514648707  1084 IMKRMGFCCGQELVFNPPTLYCNGKNLCTIPRESKYMSYR 1123
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1584-1626 1.54e-11

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: 60.65  E-value: 1.54e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 514648707 1584 YVCDLCKHsisAVDSRYHCVGgCEDYDLCKSCYESQGHEHKME 1626
Cdd:cd02337     1 YTCNECKH---HVETRWHCTV-CEDYDLCITCYNTKNHPHKME 39
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1643-1708 2.01e-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: 61.25  E-value: 2.01e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514648707  1643 QQAASLLTHANVCTDAN---CQVKQCSILKRYLQHANTCRRHyRECK--HCRTYWTILRyHASHCREDPCP 1708
Cdd:pfam02135    2 QRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRG-GGCPypHCKRSRQLLR-HAKNCKDEDCP 70
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1643-1713 1.33e-10

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 59.30  E-value: 1.33e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514648707   1643 QQAASLLTHANVCT--DANCQVKQCSILKRYLQHANTCR-RH--YRECKHCRTYWtilrYHASHCREDPCPMPQCS 1713
Cdd:smart00551    8 QRWLELLVHARRCKarEAKCQYPNCKTMKKLLRHMDSCKvRKckYGYCASCKQLW----QHSKHCKDSNCPVCKCV 79
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
 1173-1204 9.72e-10

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: 55.35  E-value: 9.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 514648707 1173 KLIECHVCKRRQHQICELYHEH-FNQPFVCSHC 1204
Cdd:cd15557     5 QFVECKECGRKWHQICVLHNDEiWPNGFICDNC 37
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1581-1625 9.77e-08

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: 50.17  E-value: 9.77e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 514648707  1581 SEGYVCDLCKHSISaVDSRYHCVGgCEDYDLCKSCY-ESQGHEHKM 1625
Cdd:pfam00569    2 HKVYTCNGCSNDPS-IGVRYHCLR-CSDYDLCQSCFqTHKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1584-1626 3.28e-07

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: 48.59  E-value: 3.28e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 514648707   1584 YVCDLCKHSISAVdsRYHCVGgCEDYDLCKSCYESQGHEHKME 1626
Cdd:smart00291    5 YSCDTCGKPIVGV--RYHCLV-CPDYDLCQSCFAKGSAGGEHS 44
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 884-957 3.71e-05

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: 44.02  E-value: 3.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514648707   884 DWRAALKdvKSLRIKLREKVIAALSKCVSPEEKA-GTQDRIKSLGAKIEDQAFHKSQTQKEYFEMLAQRIYQLQK 957
Cdd:pfam02172    5 DWHSRVT--RDLRNHLVHKLVQAIFPTPDQNAMNdGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQK 77
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1278-1456 9.72e-47

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: 172.58  E-value: 9.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1278 PESFPYKSKALFVFQRIDGGrDLCFFGLHVQEYGEDCPEPNRRRVYISYLDSVNLFEPKsYRTTVYHELLIGYLYYVAKL 1357
Cdd:pfam08214   42 KPEFTYKEKHFFALSEIDGV-EVIFFGLEVQVYGTVCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  1358 GFLHAHIWACPPSPGDDYMFhchP-----PNQRVPTSKRLQAWYRDMLIK--------AKERGVI--------------- 1409
Cdd:pfam08214  120 GYLRAVIWALFTRAQDQYLF---PnssknPKKHVLDGKGLLKWWCKMLDKilveykssAKAKLVIpgkdifktrkylpat 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 514648707  1410 --QDWCDLQQYVDSERLSEARQLPYFDGDFWPNQLEQIVQE-----INKDEEEE 1456
Cdd:pfam08214  197 adPLWLVGHIFHQICDDPARYEIPLFPDDPKPRFLEELIKEgrwksVSLDQFWE 250
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 980-1086 4.59e-40

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: 144.51  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  980 REELLHHFWPLHEKI-RSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFT 1058
Cdd:cd05495     1 PEELRQALMPTLEKLyKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 514648707 1059 YNGEKSIVGKMAKTLFNLWNAEIEPIMK 1086
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 993-1080 3.03e-31

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: 118.97  E-value: 3.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  993 KIRSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKT 1072
Cdd:cd05506    11 KLMKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKE 90


                  ....*...
gi 514648707 1073 LFNLWNAE 1080
Cdd:cd05506    91 LLKIFETR 98
BROMO smart00297
bromo domain;
987-1084 4.60e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 118.54  E-value: 4.60e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707    987 FWPLHEKIRSHEDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIV 1066
Cdd:smart00297   12 LKAVLDKLDSHPLSWPFLKPVSRKEA--PDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEV 89

                            90
                    ....*....|....*...
gi 514648707   1067 GKMAKTLFNLWNAEIEPI 1084
Cdd:smart00297   90 YKDAKKLEKFFEKKLREL 107
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 990-1081 3.37e-30

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


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 115.93  E-value: 3.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  990 LHEKIRSH--EDSHPFLEPVDtvALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVG 1067
Cdd:cd04369     8 LLDALKKLkrDLSEPFLEPVD--PKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGPGSPIY 85

                          90
                  ....*....|....
gi 514648707 1068 KMAKTLFNLWNAEI 1081
Cdd:cd04369    86 KDAKKLEKLFEKLL 99
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 990-1074 8.79e-30

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: 114.72  E-value: 8.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  990 LHEKIRSHE---DSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIV 1066
Cdd:cd05500     9 LLSSIRSLKrlkDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPV 88


                  ....*...
gi 514648707 1067 GKMAKTLF 1074
Cdd:cd05500    89 SQMGKRLQ 96
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 982-1073 6.31e-29

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: 112.26  E-value: 6.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  982 ELLHHFWPLHEKIRSHEDSHPFLEPVDTvaLNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNG 1061
Cdd:cd05509     1 PLYTQLKKVLDSLKNHKSAWPFLEPVDK--EEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNG 78

                          90
                  ....*....|..
gi 514648707 1062 EKSIVGKMAKTL 1073
Cdd:cd05509    79 PDTEYYKCANKL 90
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 699-767 3.78e-27

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: 106.32  E-value: 3.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514648707   699 IHRQLTLLLHAYRCRNPN---CQVKFCGDMKRVLKHMASCQKNKSCPYPHCGSSKQLLAHYSSCSNPKCPYC 767
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 1001-1073 2.35e-26

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: 105.05  E-value: 2.35e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514648707 1001 HPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05498    22 WPFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKL 94
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 993-1078 9.38e-26

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: 103.13  E-value: 9.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  993 KIRSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKT 1072
Cdd:cd05499    14 KPKHSAYNWPFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQ 93


                  ....*.
gi 514648707 1073 LFNLWN 1078
Cdd:cd05499    94 LEEVFN 99
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 997-1073 1.32e-21

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: 91.71  E-value: 1.32e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514648707  997 HEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05497    20 HKFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTL 96
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 996-1073 1.01e-20

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: 89.27  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  996 SHEDSHPFLEPVDTVALNcsdYYDIIKQPMDLGTIGKKLKAGD---YKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKT 1072
Cdd:cd05502    18 CHELSLPFHEPVSPSVPN---YYKIIKTPMDLSLIRKKLQPKSpqhYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKE 94


                  .
gi 514648707 1073 L 1073
Cdd:cd05502    95 L 95
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 998-1086 1.36e-20

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: 89.05  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  998 EDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYN-GEKSIVGKMAKTLFNL 1076
Cdd:cd05496    21 EDSEPFRQPVDLLKY--PDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSAL 98

                          90
                  ....*....|
gi 514648707 1077 WNAEIEPIMK 1086
Cdd:cd05496    99 FEEHIKKIIS 108
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1098-1172 1.60e-20

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: 87.35  E-value: 1.60e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514648707 1098 FNPPTLYCNGKnlCTIPRE--SKYMSYRTSTLIVNYCPKCWKKLPTGPVKITDENGQEVPveRSQFEEKVNNELEYE 1172
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLDNRYHFCEKCFNEIRGDEITLGDDQGTSIS--KSQFEKKKNDELDEE 73
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 990-1076 1.91e-20

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: 88.48  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  990 LHEKIRSHEDSHPFLEPVDtvALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKM 1069
Cdd:cd05511     8 IVNELKNLPDSWPFHTPVN--KKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKK 85


                  ....*..
gi 514648707 1070 AKTLFNL 1076
Cdd:cd05511    86 AKEMLEL 92
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
698-770 2.30e-20

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 87.04  E-value: 2.30e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514648707    698 VIHRQLTLLLHAYRC--RNPNCQVKFCGDMKRVLKHMASCqKNKSCPYPHCGSSKQLLAHYSSCSNPKCPYCRPI 770
Cdd:smart00551    6 QLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSC-KVRKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 979-1068 2.60e-20

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 88.22  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  979 DREELLHHFWPLHE---KIRSHEDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRN 1055
Cdd:cd05504     6 GRHHGPLNLSALEQllvEIVKHKDSWPFLRPVSKIEV--PDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSN 83

                          90
                  ....*....|...
gi 514648707 1056 AFTYNGEKSIVGK 1068
Cdd:cd05504    84 CFLYNPEHTSVYK 96
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 992-1072 2.68e-20

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: 86.98  E-value: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707   992 EKIRSHEDSHPFLEPVDTVALNcsDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAK 1071
Cdd:pfam00439    6 DKLMEHPIAAPFLEPVDPDEYP--DYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAE 83


                   .
gi 514648707  1072 T 1072
Cdd:pfam00439   84 K 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 935-1088 9.09e-20

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 93.72  E-value: 9.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  935 FHKSQTQKEYFeMLAQRIYQLQKAQASRTPTGSAHKLVPKPKKWDREELL--HHFWPLHEKIR-----SHEDSHPFLEPV 1007
Cdd:COG5076    95 RPESLRFDEIV-FLAIESVTPESGLGSLLMAHLKTSVKKRKTPKIEDELLyaDNKAIAKFKKQlflrdGRFLSSIFLGLP 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707 1008 DTvaLNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLWNAEIEPIMKR 1087
Cdd:COG5076   174 SK--REYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEE 251


                  .
gi 514648707 1088 M 1088
Cdd:COG5076   252 M 252
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1084-1123 1.80e-18

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: 80.44  E-value: 1.80e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 514648707  1084 IMKRMGFCCGQELVFNPPTLYCNGKNLCTIPRESKYMSYR 1123
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 994-1073 2.39e-18

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: 82.04  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  994 IRSHEDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05503    12 MEAHEDAWPFLEPVNTKLV--PGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNM 89
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 980-1064 4.05e-18

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: 81.72  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  980 REELLHHFWPLHEKIRSH-EDSHPFLEPVDTValNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFT 1058
Cdd:cd05510     5 QEEFYESLDKVLNELKTYtEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLL 82


                  ....*.
gi 514648707 1059 YNGEKS 1064
Cdd:cd05510    83 YNSDPS 88
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 987-1079 1.83e-12

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: 65.44  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  987 FWPLHEKIRSHED------SHPFLE-PVDTVAlncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTY 1059
Cdd:cd05520     5 LWQLYDTIRNARNnqgqllAEPFLKlPSKRKY---PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRY 81

                          90       100
                  ....*....|....*....|
gi 514648707 1060 NGEKSIVGKMAKTLFNLWNA 1079
Cdd:cd05520    82 NVPNSRIYKDAEKLQKLMQA 101
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 981-1072 2.17e-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: 64.87  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  981 EELLHhfwplheKIRSHEDSHPFLEPVDtvALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYN 1060
Cdd:cd05505     6 EEILS-------KILKYRFSWPFREPVT--ADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76

                          90
                  ....*....|...
gi 514648707 1061 GEKS-IVGKMAKT 1072
Cdd:cd05505    77 ENGSyVLSCMRKT 89
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 1016-1073 4.61e-12

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: 64.25  E-value: 4.61e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05515    38 DYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYKDALTL 95
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1584-1626 1.54e-11

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: 60.65  E-value: 1.54e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 514648707 1584 YVCDLCKHsisAVDSRYHCVGgCEDYDLCKSCYESQGHEHKME 1626
Cdd:cd02337     1 YTCNECKH---HVETRWHCTV-CEDYDLCITCYNTKNHPHKME 39
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 1016-1073 1.79e-11

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: 62.79  E-value: 1.79e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05525    40 DYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRL 97
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1643-1708 2.01e-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: 61.25  E-value: 2.01e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514648707  1643 QQAASLLTHANVCTDAN---CQVKQCSILKRYLQHANTCRRHyRECK--HCRTYWTILRyHASHCREDPCP 1708
Cdd:pfam02135    2 QRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRG-GGCPypHCKRSRQLLR-HAKNCKDEDCP 70
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1016-1077 4.11e-11

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: 61.67  E-value: 4.11e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLW 1077
Cdd:cd05516    39 EYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 100
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 1016-1073 4.21e-11

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: 61.69  E-value: 4.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05518    38 DYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVYEDANIL 95
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 992-1065 8.35e-11

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: 60.49  E-value: 8.35e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514648707  992 EKIRSHEDSHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSI 1065
Cdd:cd05512    11 DQLQEKDTAEIFSEPVDLSEV--PDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTI 82
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1131-1204 1.00e-10

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: 59.29  E-value: 1.00e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1131 YCPKCWKKLPTGPVKITdengqEVPVERSQFEEKVNNELEYEKLIECHVCKRRQHQICELYHEHFNQ----PFVCSHC 1204
Cdd:cd15614     1 WCSPCYNELKGENILIG-----GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNAdetaEYVCPLC 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1643-1713 1.33e-10

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 59.30  E-value: 1.33e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514648707   1643 QQAASLLTHANVCT--DANCQVKQCSILKRYLQHANTCR-RH--YRECKHCRTYWtilrYHASHCREDPCPMPQCS 1713
Cdd:smart00551    8 QRWLELLVHARRCKarEAKCQYPNCKTMKKLLRHMDSCKvRKckYGYCASCKQLW----QHSKHCKDSNCPVCKCV 79
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 1016-1066 1.84e-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: 59.66  E-value: 1.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIV 1066
Cdd:cd05519    38 DYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYNQEGSIV 88
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 1002-1073 2.62e-10

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: 59.68  E-value: 2.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514648707 1002 PFLEPVDtvALNCSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGK----MAKTL 1073
Cdd:cd05528    23 AFTKPVD--EEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNPDRDPADKlirsRACEL 96
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
 1173-1204 9.72e-10

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: 55.35  E-value: 9.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 514648707 1173 KLIECHVCKRRQHQICELYHEH-FNQPFVCSHC 1204
Cdd:cd15557     5 QFVECKECGRKWHQICVLHNDEiWPNGFICDNC 37
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 999-1075 1.38e-09

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: 57.03  E-value: 1.38e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514648707  999 DSHPFLE-PV-DTVALNcsdYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFN 1075
Cdd:cd05513    17 DPHGFFAfPVtDFIAPG---YSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYYKAAKKLLH 92
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 993-1085 2.81e-09

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: 56.22  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  993 KIRSHEDSHPFLEPV-DTVAlncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAK 1071
Cdd:cd05507    14 TLASHRYASVFLKPVtEDIA---PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSSDHDVYLMAV 90

                          90
                  ....*....|....
gi 514648707 1072 TLFNLWNAEIEPIM 1085
Cdd:cd05507    91 EMQREVMSQIQQLL 104
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 1016-1085 3.70e-09

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: 56.19  E-value: 3.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLWNAEIEPIM 1085
Cdd:cd05524    40 EYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVL 109
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1016-1073 1.22e-08

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: 54.64  E-value: 1.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKagDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTL 1073
Cdd:cd05521    39 DYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALIL 94
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 1016-1079 1.36e-08

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: 54.37  E-value: 1.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLWNA 1079
Cdd:cd05517    38 DYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 970-1064 1.89e-08

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: 54.17  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  970 KLVPKPKKWDREELLHHFwplhEKIRSHEDsHPflepvdtvalncsDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDM 1049
Cdd:cd05522    11 KGLRKERDENGRLLTLHF----EKLPDKAR-EP-------------EYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDL 72

                          90
                  ....*....|....*
gi 514648707 1050 RLMFRNAFTYNGEKS 1064
Cdd:cd05522    73 NLMFENAKLYNENDS 87
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1584-1627 3.63e-08

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: 51.28  E-value: 3.63e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 514648707 1584 YVCDLCKHSISAVdsRYHCVGgCEDYDLCKSCYESQGHEHKMEQ 1627
Cdd:cd02249     1 YSCDGCLKPIVGV--RYHCLV-CEDFDLCSSCYAKGKKGHPPDH 41
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 980-1076 5.20e-08

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 53.49  E-value: 5.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707  980 REELLHHFWPLHEKIRSHEDShPFLEPVDTVALNcSDYYDIIKQPMDLGTIGKKLKAGDYKDP----WeycdDMRLMFRN 1055
Cdd:cd05529    26 RERLISGLDKLLLSLQLEIAE-YFEYPVDLRAWY-PDYWNRVPVPMDLETIRSRLENRYYRSLealrH----DVRLILSN 99

                          90       100
                  ....*....|....*....|.
gi 514648707 1056 AFTYNGEKSIVGKMAKTLFNL 1076
Cdd:cd05529   100 AETFNEPNSEIAKKAKRLSDW 120
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1581-1625 9.77e-08

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: 50.17  E-value: 9.77e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 514648707  1581 SEGYVCDLCKHSISaVDSRYHCVGgCEDYDLCKSCY-ESQGHEHKM 1625
Cdd:pfam00569    2 HKVYTCNGCSNDPS-IGVRYHCLR-CSDYDLCQSCFqTHKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1584-1626 3.28e-07

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: 48.59  E-value: 3.28e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 514648707   1584 YVCDLCKHSISAVdsRYHCVGgCEDYDLCKSCYESQGHEHKME 1626
Cdd:smart00291    5 YSCDTCGKPIVGV--RYHCLV-CPDYDLCQSCFAKGSAGGEHS 44
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 992-1030 4.46e-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: 50.52  E-value: 4.46e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 514648707  992 EKIRSHEDSHPFLEPVDTVALNCSDYYDIIKQPMDLGTI 1030
Cdd:cd05494    13 KRHRRNEDAWPFLEPVNPPRRGAPDYRDVIKRPMSFGTK 51
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1585-1625 1.44e-05

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: 43.79  E-value: 1.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 514648707 1585 VCDLCKHSIsaVDSRYHCVGgCEDYDLCKSCYESQGH-EHKM 1625
Cdd:cd02340     2 ICDGCQGPI--VGVRYKCLV-CPDYDLCESCEAKGVHpEHAM 40
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 884-957 3.71e-05

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: 44.02  E-value: 3.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514648707   884 DWRAALKdvKSLRIKLREKVIAALSKCVSPEEKA-GTQDRIKSLGAKIEDQAFHKSQTQKEYFEMLAQRIYQLQK 957
Cdd:pfam02172    5 DWHSRVT--RDLRNHLVHKLVQAIFPTPDQNAMNdGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQK 77
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 1000-1081 5.99e-05

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


Pssm-ID: 99940  Cd Length: 99  Bit Score: 43.91  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514648707 1000 SHPFLEPVDTVALncSDYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIVGKMAKTLFNLWNA 1079
Cdd:cd05508    20 AEPFLKPVDLEQF--PDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGGDHKLTQAAKAIVKICEQ 97


                  ..
gi 514648707 1080 EI 1081
Cdd:cd05508    98 EM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 1016-1073 1.23e-04

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: 43.19  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514648707 1016 DYYDIIKQPMDLGTIGKKLKAGDYKDPWEYCDDMRLMFRNAFTYNGEKSIvGKMAKTL 1073
Cdd:cd05501    32 DYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDF-GQVGITL 88
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1586-1619 6.52e-03

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 36.56  E-value: 6.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 514648707 1586 CDLCKHSISAvDSRYHCVGgCEDYDLCKSCYESQ 1619
Cdd:cd02338     3 CDGCGKSNFT-GRRYKCLI-CYDYDLCADCYDSG 34
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1584-1622 7.11e-03

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: 36.50  E-value: 7.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 514648707 1584 YVCDLCKHSISAVdSRYHCVGgCEDYDLCKSCYeSQGHE 1622
Cdd:cd02335     1 YHCDYCSKDITGT-IRIKCAE-CPDFDLCLECF-SAGAE 36
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1585-1622 7.13e-03

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: 36.28  E-value: 7.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 514648707 1585 VCDLC-KHSISAVdsRYHCvGGCEDYDLCKSCYESQGHE 1622
Cdd:cd02339     2 ICDTCrKQGIIGI--RWKC-AECPNYDLCTTCYHGDKHD 37
 
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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