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Conserved domains on  [gi|47226142|emb|CAG04516|]
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unnamed protein product [Tetraodon nigroviridis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1327-1634 4.61e-99

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: 323.58  E-value: 4.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1327 VNDFLKRQsNPESGDVTIRVVHVSDKVVEVKPGMKSRFVDSGemSESFPYRTKALFAFEDIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKV-LPKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1407 PQPNQRRVYISYLDSVHFFKPRcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPADQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1482 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1537 SIKELEQEEEE-----RKREENSTCS----------ESIDDTKSDSKNAKKKNNKKTSKNKSSLS----RANKKKPGMPN 1597
Cdd:pfam08214  234 LIKEGRWKSVSldqfwEELRFRQEFSlgrlvgfiglEGDYTPGSDDVINPPGLVKSKKQYKMIKSyitgREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 47226142   1598 VSNDLSQKLYATMEKHkevFFVIRLIAGPMANALPPI 1634
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.74e-76

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: 248.51  E-value: 1.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1072 PEELRQALMPTLESLYRQDPESLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWL 1151
Cdd:cd05495    1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                         90       100
                 ....*....|....*....|....*...
gi 47226142 1152 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1179
Cdd:cd05495   81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
609-689 6.58e-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: 163.05  E-value: 6.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    609 GIRKSWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYETANNRAEYYHLLAEKIYKIQKELE 688
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 47226142    689 E 689
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 3.46e-32

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: 120.86  E-value: 3.46e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142 1191 FSPQTLCCYGKqlCTIPRD--AAYFSYQ---NRYHFCEKCFNEIQGETVSLGDDptqPQTSINKDQFEKKKNDTLDPE 1263
Cdd:cd15802    1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
389-456 5.28e-28

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.28e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142    389 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 456
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 8.30e-27

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: 104.57  E-value: 8.30e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 47226142 1690 YTCNECKHHVETRFHCTVCEDYDLCITCYNTKGHEHKMEKL 1730
Cdd:cd02337    1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2166-2289 1.59e-25

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: 102.99  E-value: 1.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   2166 TNQQWAAGGPPMNPQQRPgMMGHMAPQQQPavtqspqqqmnqpqpqpgnrGMMPGLGVSGGPVGlpasiagaaasgNLPQ 2245
Cdd:pfam09030   15 LQQMQGMQRPMMPQQQQQ-QMPGMNPPQQP--------------------GLPQVPGQQPGRPG------------SIAP 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 47226142   2246 GALQELLRTLRSPSSPAQQQQVLNILRSNPALMAAFIRQRAARY 2289
Cdd:pfam09030   62 NALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 105
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1757-1825 2.29e-23

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: 95.53  E-value: 2.29e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226142   1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKSCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1264-1298 9.09e-20

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: 84.14  E-value: 9.09e-20
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 47226142 1264 LFVECLDCGRRMHQICVLHHETIWPSGFVCDGCLK 1298
Cdd:cd15646    6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
COG5076 super family cl34891
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
959-1178 8.50e-16

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: 81.78  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  959 QQPHLDTSSTSLDLKMEVKQQDEEEESEAGSCSKGGKLNSLKTEEKPVKTELKKEECSREGGKGVPMDTSTTTPVVgvKT 1038
Cdd:COG5076   56 MPKEYITSIVDDREPGSMANVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESVTPESGLGSLLMAHLKTSVK--KR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1039 EDRKIevkeevkeeeetsetvaPQAPAKKKIFKPEELRQALMPTLeslyrQDPESLPFRMPVDPQLlcIPDYFDIVKNPM 1118
Cdd:COG5076  134 KTPKI-----------------EDELLYADNKAIAKFKKQLFLRD-----GRFLSSIFLGLPSKRE--YPDYYEIIKSPM 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1119 DLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVM 1178
Cdd:COG5076  190 DLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
PTZ00395 super family cl33180
Sec24-related protein; Provisional
722-1012 2.77e-07

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 56.62  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   722 EVSMVRPAgPNQMvnrmqgPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMVGSRMGQPNVNQLQNQylSQGQFPGAGQ 801
Cdd:PTZ00395  314 QGDLVRGA-PNDK------NSFDRGNEKTYQIYGGFHDGSPNAASAGAPFNGLGNQADGGHINQVHPD--ARGAWAGGPH 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   802 GVGPAQPGIAQPGTQTNMAQSvGAGTAGAPASSVASSNA---NQQANAIPHLSAMRGSSP--SPAHSRSP--------TP 868
Cdd:PTZ00395  385 SNASYNCAAYSNAAQSNAAQS-NAGFSNAGYSNPGNSNPgynNAPNSNTPYNNPPNSNTPysNPPNSNPPysnlpysnTP 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   869 HQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTpshpGLASSSTPHGAQLPRTPVIT 948
Cdd:PTZ00395  464 YSNAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSV----GNPFASRPFGSAPYGGNAAT 539
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142   949 TNTPPLdTSSQQPHLDTSSTsldlkmEVKQQDEEEESEAGSCSKGGKLNSLKTEEK--PVKTELKK 1012
Cdd:PTZ00395  540 TADPNG-IAKREDHPEGGTN------RQKYEQSDEESVESSSSENSSENENEVTDKgeEIYSLLKK 598
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2343-2479 4.61e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2343 AGQPGMNLGQGAAGVSCHAAPEHPPEAPAAAAPGRGFPSAAQQPHEPPATNGPV-PPPPR---TGWPR--PSRVAQQSGP 2416
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPaPAPPAapaAGPPRrlTRPAVASLSE 2793
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47226142  2417 LSPTLAEAAVAAAALQPLPTHAALLPASAFPPPHLPtdtdwfaPPGASEPAPPQYGSSPAPTT 2479
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-------PPTSAQPTAPPPPPGPPPPS 2849
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1327-1634 4.61e-99

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: 323.58  E-value: 4.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1327 VNDFLKRQsNPESGDVTIRVVHVSDKVVEVKPGMKSRFVDSGemSESFPYRTKALFAFEDIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKV-LPKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1407 PQPNQRRVYISYLDSVHFFKPRcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPADQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1482 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1537 SIKELEQEEEE-----RKREENSTCS----------ESIDDTKSDSKNAKKKNNKKTSKNKSSLS----RANKKKPGMPN 1597
Cdd:pfam08214  234 LIKEGRWKSVSldqfwEELRFRQEFSlgrlvgfiglEGDYTPGSDDVINPPGLVKSKKQYKMIKSyitgREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 47226142   1598 VSNDLSQKLYATMEKHkevFFVIRLIAGPMANALPPI 1634
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.74e-76

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: 248.51  E-value: 1.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1072 PEELRQALMPTLESLYRQDPESLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWL 1151
Cdd:cd05495    1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                         90       100
                 ....*....|....*....|....*...
gi 47226142 1152 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1179
Cdd:cd05495   81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
609-689 6.58e-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: 163.05  E-value: 6.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    609 GIRKSWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYETANNRAEYYHLLAEKIYKIQKELE 688
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 47226142    689 E 689
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1069-1177 6.61e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 6.61e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    1069 IFKPEELRQALMPTLESLYRQDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNN 1148
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 47226142    1149 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1177
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 3.46e-32

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: 120.86  E-value: 3.46e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142 1191 FSPQTLCCYGKqlCTIPRD--AAYFSYQ---NRYHFCEKCFNEIQGETVSLGDDptqPQTSINKDQFEKKKNDTLDPE 1263
Cdd:cd15802    1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
389-456 5.28e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.28e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142    389 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 456
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 8.30e-27

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: 104.57  E-value: 8.30e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 47226142 1690 YTCNECKHHVETRFHCTVCEDYDLCITCYNTKGHEHKMEKL 1730
Cdd:cd02337    1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2166-2289 1.59e-25

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: 102.99  E-value: 1.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   2166 TNQQWAAGGPPMNPQQRPgMMGHMAPQQQPavtqspqqqmnqpqpqpgnrGMMPGLGVSGGPVGlpasiagaaasgNLPQ 2245
Cdd:pfam09030   15 LQQMQGMQRPMMPQQQQQ-QMPGMNPPQQP--------------------GLPQVPGQQPGRPG------------SIAP 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 47226142   2246 GALQELLRTLRSPSSPAQQQQVLNILRSNPALMAAFIRQRAARY 2289
Cdd:pfam09030   62 NALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 105
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1757-1825 2.29e-23

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: 95.53  E-value: 2.29e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226142   1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKSCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1751-1829 4.22e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.12  E-value: 4.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    1751 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKSCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1826
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 47226142    1827 FCL 1829
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1177-1216 5.82e-23

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: 93.54  E-value: 5.82e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 47226142   1177 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDAAYFSYQ 1216
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
389-459 3.33e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.73  E-value: 3.33e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47226142     389 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 459
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1264-1298 9.09e-20

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: 84.14  E-value: 9.09e-20
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 47226142 1264 LFVECLDCGRRMHQICVLHHETIWPSGFVCDGCLK 1298
Cdd:cd15646    6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1089-1165 1.06e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 85.44  E-value: 1.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47226142   1089 QDPESLPFRMPVDPqlLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSK 1165
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1686-1728 7.37e-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: 76.32  E-value: 7.37e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 47226142    1686 DRFVYTCNEC-KHHVETRFHCTVCEDYDLCITCYNTKGHEHKME 1728
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2247-2289 4.51e-16

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: 73.84  E-value: 4.51e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 47226142 2247 ALQELLRTLRSPSSPAQQQQVLNILRSNPALMAAFIRQRAARY 2289
Cdd:cd20910    1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
959-1178 8.50e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.78  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  959 QQPHLDTSSTSLDLKMEVKQQDEEEESEAGSCSKGGKLNSLKTEEKPVKTELKKEECSREGGKGVPMDTSTTTPVVgvKT 1038
Cdd:COG5076   56 MPKEYITSIVDDREPGSMANVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESVTPESGLGSLLMAHLKTSVK--KR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1039 EDRKIevkeevkeeeetsetvaPQAPAKKKIFKPEELRQALMPTLeslyrQDPESLPFRMPVDPQLlcIPDYFDIVKNPM 1118
Cdd:COG5076  134 KTPKI-----------------EDELLYADNKAIAKFKKQLFLRD-----GRFLSSIFLGLPSKRE--YPDYYEIIKSPM 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1119 DLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVM 1178
Cdd:COG5076  190 DLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1686-1727 6.62e-14

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: 67.89  E-value: 6.62e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 47226142   1686 DRFVYTCNECKH--HVETRFHCTVCEDYDLCITCYNT-KGHEHKM 1727
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
PTZ00395 PTZ00395
Sec24-related protein; Provisional
722-1012 2.77e-07

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 56.62  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   722 EVSMVRPAgPNQMvnrmqgPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMVGSRMGQPNVNQLQNQylSQGQFPGAGQ 801
Cdd:PTZ00395  314 QGDLVRGA-PNDK------NSFDRGNEKTYQIYGGFHDGSPNAASAGAPFNGLGNQADGGHINQVHPD--ARGAWAGGPH 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   802 GVGPAQPGIAQPGTQTNMAQSvGAGTAGAPASSVASSNA---NQQANAIPHLSAMRGSSP--SPAHSRSP--------TP 868
Cdd:PTZ00395  385 SNASYNCAAYSNAAQSNAAQS-NAGFSNAGYSNPGNSNPgynNAPNSNTPYNNPPNSNTPysNPPNSNPPysnlpysnTP 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   869 HQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTpshpGLASSSTPHGAQLPRTPVIT 948
Cdd:PTZ00395  464 YSNAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSV----GNPFASRPFGSAPYGGNAAT 539
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142   949 TNTPPLdTSSQQPHLDTSSTsldlkmEVKQQDEEEESEAGSCSKGGKLNSLKTEEK--PVKTELKK 1012
Cdd:PTZ00395  540 TADPNG-IAKREDHPEGGTN------RQKYEQSDEESVESSSSENSSENENEVTDKgeEIYSLLKK 598
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
698-943 9.55e-07

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: 54.24  E-value: 9.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    698 QGLALGPASMGQPPIGLPPNGPLPEVSMVRPAG---PNQMVNRMQGPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMV 774
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    775 GSR-MGQPNVNQL-----QNQYLSQGQFPGAGQGvGPAQP------------------------------------GIAQ 812
Cdd:pfam09606  245 QQQpQQQGQQSQLgmginQMQQMPQGVGGGAGQG-GPGQPmgppgqqpgampnvmsigdqnnyqqqqtrqqqqqqgGNHP 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    813 PGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIP-HLSAMRGSSPSPAHSRSPTPHQTPPRLAGSQ----TPQPHTPS 887
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGlGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQfmrqSPQPSVPS 403
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47226142    888 ------------APQLAPPPGAQQNH---LGQGPGSNKSLQQQhmGPAGS-TTPSHPGLASSSTPHGAQLPR 943
Cdd:pfam09606  404 pqgpgsqppqshPGGMIPSPALIPSPspqMSQQPAQQRTIGQD--SPGGSlNTPGQSAVNSPLNPQEEQLYR 473
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
734-904 2.17e-05

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: 49.81  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    734 MVNRMQGPGMNQFNQMGmQSMGQRstpplPMGATGNQMgMVGsrmGQPNVNQLQNQYLSQGQFPGAGQGVGPAQPGiaQP 813
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMG-GAMGQP-----PYYGQGPQQ-QFN---GQPLGWPRMSMMPTPMGPGGPLRPNGLAPMN--AV 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    814 GTQTNMAQsvgagtagapassvassNANQQANAIPHLSAmrgssPSPAHSRSPTPHQTPPRLAGSQTPQPHTPSAPQLAp 893
Cdd:TIGR01628  444 RAPSRNAQ-----------------NAAQKPPMQPVMYP-----PNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASA- 500
                          170
                   ....*....|.
gi 47226142    894 PPGAQQNHLGQ 904
Cdd:TIGR01628  501 TPQMQKQVLGE 511
PHA03247 PHA03247
large tegument protein UL36; Provisional
2343-2479 4.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2343 AGQPGMNLGQGAAGVSCHAAPEHPPEAPAAAAPGRGFPSAAQQPHEPPATNGPV-PPPPR---TGWPR--PSRVAQQSGP 2416
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPaPAPPAapaAGPPRrlTRPAVASLSE 2793
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47226142  2417 LSPTLAEAAVAAAALQPLPTHAALLPASAFPPPHLPtdtdwfaPPGASEPAPPQYGSSPAPTT 2479
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-------PPTSAQPTAPPPPPGPPPPS 2849
PPE COG5651
PPE-repeat protein [Function unknown];
757-970 4.37e-03

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 42.19  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  757 RSTPPLPMGATGNQMGMVGSRMGQPNVNQlqnQYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVA 836
Cdd:COG5651  167 FTQPPPTITNPGGLLGAQNAGSGNTSSNP---GFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAA 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  837 SSNANQQANAIPHLSAMRGSSPSPAHSrSPTPHQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQH 916
Cdd:COG5651  244 AAAAAAAAGAGASAALASLAATLLNAS-SLGLAATAASSAATNLGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGAT 322
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 47226142  917 MGPAGSTTPSHPGLASSSTPHGAQLPRTPVITTNTPPLDTSSQQPHLDTSSTSL 970
Cdd:COG5651  323 GAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAG 376
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1327-1634 4.61e-99

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: 323.58  E-value: 4.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1327 VNDFLKRQsNPESGDVTIRVVHVSDKVVEVKPGMKSRFVDSGemSESFPYRTKALFAFEDIDGVDVCFFGMHVQEYGSDC 1406
Cdd:pfam08214    1 LNDFLAKV-LPKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1407 PQPNQRRVYISYLDSVHFFKPRcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPADQKIPK-----P 1481
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1482 KRLQEWYKKMLDKAVSE-------RIVHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1536
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   1537 SIKELEQEEEE-----RKREENSTCS----------ESIDDTKSDSKNAKKKNNKKTSKNKSSLS----RANKKKPGMPN 1597
Cdd:pfam08214  234 LIKEGRWKSVSldqfwEELRFRQEFSlgrlvgfiglEGDYTPGSDDVINPPGLVKSKKQYKMIKSyitgREYSTEEGAPE 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 47226142   1598 VSNDLSQKLYATMEKHkevFFVIRLIAGPMANALPPI 1634
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1072-1179 1.74e-76

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: 248.51  E-value: 1.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1072 PEELRQALMPTLESLYRQDPESLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWL 1151
Cdd:cd05495    1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                         90       100
                 ....*....|....*....|....*...
gi 47226142 1152 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1179
Cdd:cd05495   81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
609-689 6.58e-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: 163.05  E-value: 6.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    609 GIRKSWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYETANNRAEYYHLLAEKIYKIQKELE 688
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 47226142    689 E 689
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1069-1177 6.61e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 6.61e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    1069 IFKPEELRQALMPTLESLYRQDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNN 1148
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 47226142    1149 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1177
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1191-1263 3.46e-32

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: 120.86  E-value: 3.46e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142 1191 FSPQTLCCYGKqlCTIPRD--AAYFSYQ---NRYHFCEKCFNEIQGETVSLGDDptqPQTSINKDQFEKKKNDTLDPE 1263
Cdd:cd15802    1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1075-1174 2.26e-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: 119.40  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1075 LRQALMPTLESLYRQ-DPESLPFRMPVDPQLLciPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYN 1153
Cdd:cd04369    1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                         90       100
                 ....*....|....*....|.
gi 47226142 1154 RKTSRVYKYCSKLAEVFEQEI 1174
Cdd:cd04369   79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1095-1172 2.03e-28

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: 111.22  E-value: 2.03e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142 1095 PFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1172
Cdd:cd05498   23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
389-456 5.28e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 108.63  E-value: 5.28e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142    389 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 456
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1690-1730 8.30e-27

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: 104.57  E-value: 8.30e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 47226142 1690 YTCNECKHHVETRFHCTVCEDYDLCITCYNTKGHEHKMEKL 1730
Cdd:cd02337    1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1074-1174 9.19e-27

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: 106.10  E-value: 9.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1074 ELRQALMPTLESLyRQDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYN 1153
Cdd:cd05509    1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                         90       100
                 ....*....|....*....|.
gi 47226142 1154 RKTSRVYKYCSKLAEVFEQEI 1174
Cdd:cd05509   78 GPDTEYYKCANKLEKFFWKKL 98
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2166-2289 1.59e-25

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: 102.99  E-value: 1.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   2166 TNQQWAAGGPPMNPQQRPgMMGHMAPQQQPavtqspqqqmnqpqpqpgnrGMMPGLGVSGGPVGlpasiagaaasgNLPQ 2245
Cdd:pfam09030   15 LQQMQGMQRPMMPQQQQQ-QMPGMNPPQQP--------------------GLPQVPGQQPGRPG------------SIAP 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 47226142   2246 GALQELLRTLRSPSSPAQQQQVLNILRSNPALMAAFIRQRAARY 2289
Cdd:pfam09030   62 NALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 105
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1088-1171 4.77e-24

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: 98.56  E-value: 4.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1088 RQDPESLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLA 1167
Cdd:cd05506   13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                 ....
gi 47226142 1168 EVFE 1171
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 ...
1757-1825 2.29e-23

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: 95.53  E-value: 2.29e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226142   1757 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKSCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1825
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1082-1174 2.38e-23

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: 96.61  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1082 TLESLYRQdPESLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYK 1161
Cdd:cd05500   12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                         90
                 ....*....|...
gi 47226142 1162 YCSKLAEVFEQEI 1174
Cdd:cd05500   91 MGKRLQAAFEKHL 103
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1751-1829 4.22e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.12  E-value: 4.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    1751 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKSCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1826
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 47226142    1827 FCL 1829
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1177-1216 5.82e-23

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: 93.54  E-value: 5.82e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 47226142   1177 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDAAYFSYQ 1216
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1093-1176 5.92e-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: 92.87  E-value: 5.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1093 SLPFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1172
Cdd:cd05497   23 AWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLFLQ 102

                 ....
gi 47226142 1173 EIDP 1176
Cdd:cd05497  103 KLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1070-1172 3.04e-21

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: 90.81  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1070 FKPEELRQALMPTLEsLYRQDPeSLPFRMPVDPQllcIPDYFDIVKNPMDLSTIKRKLD---TGQYQDPWQYVDDIWLMF 1146
Cdd:cd05502    1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSPS---VPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                         90       100
                 ....*....|....*....|....*.
gi 47226142 1147 NNAWLYNRKTSRVYKYCSKLAEVFEQ 1172
Cdd:cd05502   76 KNCYKFNEEDSEVAQAGKELELFFEE 101
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
389-459 3.33e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.73  E-value: 3.33e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47226142     389 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 459
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1092-1180 4.09e-21

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: 90.98  E-value: 4.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1092 ESLPFRMPVDpqLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYN-RKTSRVYKYCSKLAEVF 1170
Cdd:cd05496   22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                         90
                 ....*....|
gi 47226142 1171 EQEIDPVMQS 1180
Cdd:cd05496  100 EEHIKKIISD 109
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1095-1171 7.09e-20

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: 86.57  E-value: 7.09e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47226142 1095 PFRMPVDPQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFE 1171
Cdd:cd05499   23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1264-1298 9.09e-20

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: 84.14  E-value: 9.09e-20
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 47226142 1264 LFVECLDCGRRMHQICVLHHETIWPSGFVCDGCLK 1298
Cdd:cd15646    6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1089-1165 1.06e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 85.44  E-value: 1.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47226142   1089 QDPESLPFRMPVDPqlLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSK 1165
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1089-1173 1.97e-18

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: 83.21  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1089 QDPESLPFRMPVdpQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAE 1168
Cdd:cd05504   26 KHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQR 103

                 ....*
gi 47226142 1169 VFEQE 1173
Cdd:cd05504  104 FFIKR 108
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1073-1163 2.32e-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: 79.79  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1073 EELRQALMPTLESLYRQDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLY 1152
Cdd:cd05510    6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKRE--APDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                         90
                 ....*....|.
gi 47226142 1153 NRKTSRVYKYC 1163
Cdd:cd05510   84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1686-1728 7.37e-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: 76.32  E-value: 7.37e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 47226142    1686 DRFVYTCNEC-KHHVETRFHCTVCEDYDLCITCYNTKGHEHKME 1728
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1265-1296 2.61e-16

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: 74.23  E-value: 2.61e-16
                         10        20        30
                 ....*....|....*....|....*....|..
gi 47226142 1265 FVECLDCGRRMHQICVLHHETIWPSGFVCDGC 1296
Cdd:cd15557    6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2247-2289 4.51e-16

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: 73.84  E-value: 4.51e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 47226142 2247 ALQELLRTLRSPSSPAQQQQVLNILRSNPALMAAFIRQRAARY 2289
Cdd:cd20910    1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
959-1178 8.50e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.78  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  959 QQPHLDTSSTSLDLKMEVKQQDEEEESEAGSCSKGGKLNSLKTEEKPVKTELKKEECSREGGKGVPMDTSTTTPVVgvKT 1038
Cdd:COG5076   56 MPKEYITSIVDDREPGSMANVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESVTPESGLGSLLMAHLKTSVK--KR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1039 EDRKIevkeevkeeeetsetvaPQAPAKKKIFKPEELRQALMPTLeslyrQDPESLPFRMPVDPQLlcIPDYFDIVKNPM 1118
Cdd:COG5076  134 KTPKI-----------------EDELLYADNKAIAKFKKQLFLRD-----GRFLSSIFLGLPSKRE--YPDYYEIIKSPM 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1119 DLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVM 1178
Cdd:COG5076  190 DLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1093-1161 1.34e-15

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 74.65  E-value: 1.34e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1093 SLPF-RMPVDPQLlciPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYK 1161
Cdd:cd05515   24 SLIFmRLPSKSEY---PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1265-1298 1.90e-15

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: 71.94  E-value: 1.90e-15
                         10        20        30
                 ....*....|....*....|....*....|....
gi 47226142 1265 FVECLDCGRRMHQICVLHHETIWPSGFVCDGCLK 1298
Cdd:cd15647    7 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1091-1159 1.95e-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: 73.95  E-value: 1.95e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47226142 1091 PESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRV 1159
Cdd:cd05503   16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1088-1173 2.21e-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: 74.22  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1088 RQDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSR-------VY 1160
Cdd:cd05511   13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90
                         90
                 ....*....|...
gi 47226142 1161 KYCSKLAEVFEQE 1173
Cdd:cd05511   91 ELAEELLAEREEK 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1108-1179 3.76e-15

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: 73.52  E-value: 3.76e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1179
Cdd:cd05524   39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1074-1176 3.97e-15

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: 73.55  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1074 ELRQALMPTLESLYRqDPESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYN 1153
Cdd:cd05528    3 ELRLFLRDVLKRLAS-DKRFNAFTKPVDEEE--VPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 47226142 1154 ------RKTSRvYKYCSKLAEV---FEQEIDP 1176
Cdd:cd05528   80 pdrdpaDKLIR-SRACELRDEVhamIEAELDP 110
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1078-1168 1.06e-14

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: 71.66  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1078 ALMPTLESLYRQDPESLpFRMPVDpqLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTS 1157
Cdd:cd05512    5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                         90
                 ....*....|.
gi 47226142 1158 RVYKYCSKLAE 1168
Cdd:cd05512   82 IFYRAAVRLRD 92
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1686-1727 6.62e-14

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: 67.89  E-value: 6.62e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 47226142   1686 DRFVYTCNECKH--HVETRFHCTVCEDYDLCITCYNT-KGHEHKM 1727
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1690-1730 5.24e-13

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: 65.15  E-value: 5.24e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 47226142 1690 YTCNEC-KHHVETRFHCTVCEDYDLCITCYNT--KGH--EHKMEKL 1730
Cdd:cd02249    1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKgkKGHppDHSFTEI 46
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1074-1162 8.34e-13

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: 66.58  E-value: 8.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1074 ELRQALMPTLESLYRQDPES----------LPFRMPvdpqllcIPDYFDIVKNPMDLSTIKRKLDtgQYQDPWQYVDDIW 1143
Cdd:cd05521    1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                         90
                 ....*....|....*....
gi 47226142 1144 LMFNNAWLYNRKTSRVYKY 1162
Cdd:cd05521   72 QIPWNARLYNTKGSVIYKY 90
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1075-1166 9.01e-13

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: 66.28  E-value: 9.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1075 LRQALMPTLESLYRQDPESLpFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNR 1154
Cdd:cd05513    2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                         90
                 ....*....|..
gi 47226142 1155 KTSRVYKYCSKL 1166
Cdd:cd05513   79 PDTIYYKAAKKL 90
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1076-1173 1.46e-12

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: 65.85  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1076 RQALMPTLESLYRQdPESLPFRMPVdpQLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRk 1155
Cdd:cd05507    5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNS- 80
                         90
                 ....*....|....*...
gi 47226142 1156 tsrvYKYCSKLAEVFEQE 1173
Cdd:cd05507   81 ----SDHDVYLMAVEMQR 94
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1108-1166 2.85e-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: 65.05  E-value: 2.85e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKL 1166
Cdd:cd05520   37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1221-1296 3.14e-12

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: 63.91  E-value: 3.14e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47226142 1221 FCEKCFNEIQGETVSLGddptqpQTSINKDQFEKKKNDTLDPELFVECLDCGRRMHQICVLHHETIWPSG---FVCDGC 1296
Cdd:cd15614    1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADEtaeYVCPLC 73
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1093-1166 3.36e-12

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: 64.95  E-value: 3.36e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226142 1093 SLPF-RMPvDPQLLciPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKL 1166
Cdd:cd05522   25 TLHFeKLP-DKARE--PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1071-1170 5.63e-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: 64.09  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1071 KPEELRQALMPtleslYRqdpESLPFRMPVDPQLlcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAW 1150
Cdd:cd05505    4 KCEEILSKILK-----YR---FSWPFREPVTADE--AEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                         90       100
                 ....*....|....*....|
gi 47226142 1151 LYNRKTSRVYKYCSKLAEVF 1170
Cdd:cd05505   74 KYYENGSYVLSCMRKTEQCC 93
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1107-1175 5.07e-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: 5.07e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47226142 1107 IPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEID 1175
Cdd:cd05516   37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1108-1174 1.95e-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: 1.95e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEI 1174
Cdd:cd05519   37 PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1108-1160 4.51e-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: 59.00  E-value: 4.51e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVY 1160
Cdd:cd05518   37 PDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1691-1730 1.00e-08

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: 53.03  E-value: 1.00e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 47226142 1691 TCNECKHHVE-TRFHCTVCEDYDLCITCYNTKGH-EHKMEKL 1730
Cdd:cd02340    2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLKI 43
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1108-1172 3.91e-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: 53.21  E-value: 3.91e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1172
Cdd:cd05517   37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1108-1172 5.26e-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: 53.16  E-value: 5.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226142 1108 PDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1172
Cdd:cd05525   39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1073-1174 1.04e-07

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: 52.72  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1073 EELRQALMPTLESLYRQDPESL--PFRMPVDPQLLcIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAW 1150
Cdd:cd05529   23 DEERERLISGLDKLLLSLQLEIaeYFEYPVDLRAW-YPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                         90       100
                 ....*....|....*....|....
gi 47226142 1151 LYNRKTSRVYKYCSKLAEVFEQEI 1174
Cdd:cd05529  102 TFNEPNSEIAKKAKRLSDWLLRIL 125
PTZ00395 PTZ00395
Sec24-related protein; Provisional
722-1012 2.77e-07

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 56.62  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   722 EVSMVRPAgPNQMvnrmqgPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMVGSRMGQPNVNQLQNQylSQGQFPGAGQ 801
Cdd:PTZ00395  314 QGDLVRGA-PNDK------NSFDRGNEKTYQIYGGFHDGSPNAASAGAPFNGLGNQADGGHINQVHPD--ARGAWAGGPH 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   802 GVGPAQPGIAQPGTQTNMAQSvGAGTAGAPASSVASSNA---NQQANAIPHLSAMRGSSP--SPAHSRSP--------TP 868
Cdd:PTZ00395  385 SNASYNCAAYSNAAQSNAAQS-NAGFSNAGYSNPGNSNPgynNAPNSNTPYNNPPNSNTPysNPPNSNPPysnlpysnTP 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   869 HQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTpshpGLASSSTPHGAQLPRTPVIT 948
Cdd:PTZ00395  464 YSNAPLSNAPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSV----GNPFASRPFGSAPYGGNAAT 539
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142   949 TNTPPLdTSSQQPHLDTSSTsldlkmEVKQQDEEEESEAGSCSKGGKLNSLKTEEK--PVKTELKK 1012
Cdd:PTZ00395  540 TADPNG-IAKREDHPEGGTN------RQKYEQSDEESVESSSSENSSENENEVTDKgeEIYSLLKK 598
PHA03247 PHA03247
large tegument protein UL36; Provisional
700-989 2.82e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   700 LALGPASMGQ--PPIGLPPNGPLPEVSMVRPAGPNQMVNR--MQGPGMNQFNQMGMQSMGQRSTPP--LPMGATGNQMGM 773
Cdd:PHA03247 2721 LPPGPAAARQasPALPAAPAPPAVPAGPATPGGPARPARPptTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRESLPS 2800
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   774 VGSRMGQPNVNQLQNQYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIP----H 849
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPaapaR 2880
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   850 LSAMRGSSPSPAHS------------RSPTPH-------QTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNK 910
Cdd:PHA03247 2881 PPVRRLARPAVSRStesfalppdqpeRPPQPQappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   911 SLQQQHMGP---------AGSTTPSHPGLASS-STPHGAQLPRTPVIttntppldTSSQQPHLDTSSTSLDLKMEVKQQD 980
Cdd:PHA03247 2961 QPWLGALVPgrvavprfrVPQPAPSREAPASStPPLTGHSLSRVSSW--------ASSLALHEETDPPPVSLKQTLWPPD 3032

                  ....*....
gi 47226142   981 EEEESEAGS 989
Cdd:PHA03247 3033 DTEDSDADS 3041
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
800-1024 5.94e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.18  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   800 GQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQ-QANAIPHLSAMRGSSPSPAHSRSP-------TPHQT 871
Cdd:PHA03307   41 GQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANEsRSTPTWSLSTLAPASPAREGSPTPpgpsspdPPPPT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   872 PPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSlqqqhMGPAGSTTPSHPGLASSSTPHGAQLPRTPVIT--T 949
Cdd:PHA03307  121 PPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA-----AVASDAASSRQAALPLSSPEETARAPSSPPAEppP 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   950 NTPPLDTSSQQPHLDT-------SSTSLDLKMEVKQQDEEEESEAGSCSKGGKLNSLKTEEKPVKTELKKEECSREGGKG 1022
Cdd:PHA03307  196 STPPAAASPRPPRRSSpisasasSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW 275

                  ..
gi 47226142  1023 VP 1024
Cdd:PHA03307  276 NG 277
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
698-943 9.55e-07

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: 54.24  E-value: 9.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    698 QGLALGPASMGQPPIGLPPNGPLPEVSMVRPAG---PNQMVNRMQGPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMV 774
Cdd:pfam09606  165 QPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    775 GSR-MGQPNVNQL-----QNQYLSQGQFPGAGQGvGPAQP------------------------------------GIAQ 812
Cdd:pfam09606  245 QQQpQQQGQQSQLgmginQMQQMPQGVGGGAGQG-GPGQPmgppgqqpgampnvmsigdqnnyqqqqtrqqqqqqgGNHP 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    813 PGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIP-HLSAMRGSSPSPAHSRSPTPHQTPPRLAGSQ----TPQPHTPS 887
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGlGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQfmrqSPQPSVPS 403
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47226142    888 ------------APQLAPPPGAQQNH---LGQGPGSNKSLQQQhmGPAGS-TTPSHPGLASSSTPHGAQLPR 943
Cdd:pfam09606  404 pqgpgsqppqshPGGMIPSPALIPSPspqMSQQPAQQRTIGQD--SPGGSlNTPGQSAVNSPLNPQEEQLYR 473
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1107-1172 7.90e-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: 46.65  E-value: 7.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142 1107 IPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLYNRKTSRVyKYCSKLAEVFEQ 1172
Cdd:cd05501   30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
797-987 8.99e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.14  E-value: 8.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   797 PGAGQGVGPAQPGIAQPGTQTNM----------AQSVGAGTAGAPASSVASSNANQQAN-----AIPHLSAMRGSSPSPA 861
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARpaapaapaapAAPAPAGAAAAPAEASAAPAPGVAAPehhpkHVAVPDASDGGDGWPA 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   862 HSRSPTPHQTPPRLAGSQTPQPHTPSAPQLAPPPGAQqnhlGQGPGSNKSLQQQHMGPAGSTTPshpglaSSSTPHGAQL 941
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT----PPAGQADDPAAQPPQAAQGASAP------SPAADDPVPL 741
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 47226142   942 PRTPVITTNTPPLDTSSQQPHLDTSSTSLDLKMEVKQQDEEEESEA 987
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1692-1729 1.65e-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: 43.99  E-value: 1.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 47226142 1692 CNECKHH--VETRFHCTVCEDYDLCITCYNTKGH--EHKMEK 1729
Cdd:cd02339    3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHdlEHRFYR 44
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
696-925 1.78e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    696 QKQGLALGPASMGQPPIGLPPNGPLPEvsmvrPAGPNQMVNRMQG-----PGMNQFNQMGMQSMgqrstPPLPMGATgnq 770
Cdd:pfam09606  141 SQMSRVGRMQPGGQAGGMMQPSSGQPG-----SGTPNQMGPNGGPgqgqaGGMNGGQQGPMGGQ-----MPPQMGVP--- 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    771 mGMVGSRMGQpnvNQLQNQYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVgAGTAGAPASSVASSNANQQANAIPhl 850
Cdd:pfam09606  208 -GMPGPADAG---AQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQ-LGMGINQMQQMPQGVGGGAGQGGP-- 280
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226142    851 samrgSSPSPAHSRSptPHQTPPRLAGSQtpQPHTPSAPQLAPPPGAQQNHLGQGPGSnkslQQQHMGPAGSTTP 925
Cdd:pfam09606  281 -----GQPMGPPGQQ--PGAMPNVMSIGD--QNNYQQQQTRQQQQQQGGNHPAAHQQQ----MNQSVGQGGQVVA 342
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1073-1130 2.00e-05

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: 45.90  E-value: 2.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47226142 1073 EELRQALMPtLESLYRQDPeSLPFRMPVDPQLLCIPDYFDIVKNPMDLSTI-KRKLDTG 1130
Cdd:cd05494    3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
734-904 2.17e-05

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: 49.81  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    734 MVNRMQGPGMNQFNQMGmQSMGQRstpplPMGATGNQMgMVGsrmGQPNVNQLQNQYLSQGQFPGAGQGVGPAQPGiaQP 813
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMG-GAMGQP-----PYYGQGPQQ-QFN---GQPLGWPRMSMMPTPMGPGGPLRPNGLAPMN--AV 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    814 GTQTNMAQsvgagtagapassvassNANQQANAIPHLSAmrgssPSPAHSRSPTPHQTPPRLAGSQTPQPHTPSAPQLAp 893
Cdd:TIGR01628  444 RAPSRNAQ-----------------NAAQKPPMQPVMYP-----PNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASA- 500
                          170
                   ....*....|.
gi 47226142    894 PPGAQQNHLGQ 904
Cdd:TIGR01628  501 TPQMQKQVLGE 511
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
804-961 7.65e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 7.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   804 GPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNAnqqanaiPHLSAMRGSSPSPAHSRSPTPHQTPPRLAGSQTPQp 883
Cdd:PHA03307  296 PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS-------SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK- 367
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142   884 htpsAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTPSHPGLASSSTPHGAQlpRTPVITTNTPPLDTSSQQP 961
Cdd:PHA03307  368 ----RPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG--AASGAFYARYPLLTPSGEP 439
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1073-1174 8.39e-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: 43.53  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142 1073 EELRQALMPTLESLYRqdPESLPFRMPVDpqLLCIPDYFDIVKNPMDLSTIKRKLDTGQYQDPWQYVDDIWLMFNNAWLY 1152
Cdd:cd05508    2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                         90       100
                 ....*....|....*....|..
gi 47226142 1153 NRKTSRVYKYCSKLAEVFEQEI 1174
Cdd:cd05508   78 NGGDHKLTQAAKAIVKICEQEM 99
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1690-1718 1.12e-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: 41.89  E-value: 1.12e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 47226142 1690 YTCNECKHHV--ETRFHCTVCEDYDLCITCY 1718
Cdd:cd02335    1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
708-929 1.12e-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: 47.70  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    708 GQPPIGLPPNGPLPEVSMVRPAGPNQMvnRMQGPGMNQfNQMGMQSMGQrstpplpmgatGNQMGMVGSRMGQPNVNQLQ 787
Cdd:pfam09606  106 PGGPMGQQMGGPGTASNLLASLGRPQM--PMGGAGFPS-QMSRVGRMQP-----------GGQAGGMMQPSSGQPGSGTP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    788 NQYLSQGQfPGAGQGVGPAQPGIAQPGTQtnMAQSVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPT 867
Cdd:pfam09606  172 NQMGPNGG-PGQGQAGGMNGGQQGPMGGQ--MPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQP 248
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142    868 PHQTPPRLAGSQTPQPHTPS-----------APQLAPPPGAQQNHLGQGPGS---NKSLQQQHMGPAGSTTPSHPG 929
Cdd:pfam09606  249 QQQGQQSQLGMGINQMQQMPqgvgggagqggPGQPMGPPGQQPGAMPNVMSIgdqNNYQQQQTRQQQQQQGGNHPA 324
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1691-1727 1.27e-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: 41.81  E-value: 1.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 47226142 1691 TCNECK--HHVETRFHCTVCEDYDLCITCY----NTKGHE--HKM 1727
Cdd:cd02345    2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNslHIM 46
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
802-946 2.29e-04

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 46.57  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    802 GVGPAQPGIAQPGTQTNMAQSVGagtaGAPASSVASSnanQQANAiphlsAMRGSSPSPAHSRSPTPHQTP-PRLAGSQT 880
Cdd:pfam09770  164 GVAPKKAAAPAPAPQPAAQPASL----PAPSRKMMSL---EEVEA-----AMRAQAKKPAQQPAPAPAQPPaAPPAQQAQ 231
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47226142    881 PQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTPSHPGLASSSTPHGAQLPRTPV 946
Cdd:pfam09770  232 QQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPV 297
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
789-960 3.16e-04

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 46.18  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    789 QYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVgagtagaPASSVASSNANQQANAIPhlsamrgssPSPAHSRSPTP 868
Cdd:pfam09770  202 AMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQF-------PPQIQQQQQPQQQPQQPQ---------QHPGQGHPVTI 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    869 HQTPPrlagSQTPQPHTPSA-------PQLAPPPGAQQNHLGQGPgsNKSLQQQHMGPAGSTTPSHPGLASSSTPHGAQL 941
Cdd:pfam09770  266 LQRPQ----SPQPDPAQPSIqpqaqqfHQQPPPVPVQPTQILQNP--NRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSF 339
                          170
                   ....*....|....*....
gi 47226142    942 PRTPVITTNTPPLDTSSQQ 960
Cdd:pfam09770  340 GRQAPIITHPQQLAQLSEE 358
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
695-987 3.67e-04

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: 45.91  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    695 LQKQGLALGPASMGQPPIGLPPNGPLPEVSMVRPAGPNQMVNRMQGPGMNQFNQMGMQSMgQRSTPPLPMGATGNqmgMV 774
Cdd:pfam03154  230 LIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHM-QHPVPPQPFPLTPQ---SS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    775 GSRMGQPNVNQLQNQYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQAnaiPHLSAmr 854
Cdd:pfam03154  306 QSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP---PHLSG-- 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    855 gssPSPAHSRSPTPhqTPPRLAG-SQTPQPHTPSA--PQLAPPPGAQQnhLGQGPGSNKSL-QQQHMGPAGSTTPshPGL 930
Cdd:pfam03154  381 ---PSPFQMNSNLP--PPPALKPlSSLSTHHPPSAhpPPLQLMPQSQQ--LPPPPAQPPVLtQSQSLPPPAASHP--PTS 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    931 ASSSTPHGAQLPRTPVIT-------------TNTPPLDTSSQQPHLDTSSTSLDL---------KMEVKQQ--DEEEESE 986
Cdd:pfam03154  452 GLHQVPSQSPFPQHPFVPggpppitppsgppTSTSSAMPGIQPPSSASVSSSGPVpaavscplpPVQIKEEalDEAEEPE 531

                   .
gi 47226142    987 A 987
Cdd:pfam03154  532 S 532
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
827-952 4.40e-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: 45.68  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    827 TAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPTPHQTP---PRLAGSQTPQPH--TPSAPQLAPPPGAQQnh 901
Cdd:pfam05109  445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPspsPRDNGTESKAPDmtSPTSAVTTPTPNATS-- 522
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 47226142    902 lgQGPGSNKSLQQQHMGPAGSTTPShpglASSSTPHGAQLPRTPVITTNTP 952
Cdd:pfam05109  523 --PTPAVTTPTPNATSPTLGKTSPT----SAVTTPTPNATSPTPAVTTPTP 567
PHA03247 PHA03247
large tegument protein UL36; Provisional
2343-2479 4.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2343 AGQPGMNLGQGAAGVSCHAAPEHPPEAPAAAAPGRGFPSAAQQPHEPPATNGPV-PPPPR---TGWPR--PSRVAQQSGP 2416
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPaPAPPAapaAGPPRrlTRPAVASLSE 2793
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47226142  2417 LSPTLAEAAVAAAALQPLPTHAALLPASAFPPPHLPtdtdwfaPPGASEPAPPQYGSSPAPTT 2479
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-------PPTSAQPTAPPPPPGPPPPS 2849
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2312-2481 6.24e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2312 QGAAGAMPPIGGPGAIQIGNLDAQQTASVNQAGQPGMNLGQGAAGVSCHAAPEHPPEAPAAAAPGRGFPSAAQQPHEPPA 2391
Cdd:PRK07764  626 APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP 705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2392 TNGPVPPPPRTGWPRPSRVAQQSGPLSPtlaeaavAAAALQPLPthaallpasafPPPHLPTDTDWFAPPGASEPAPPQY 2471
Cdd:PRK07764  706 AATPPAGQADDPAAQPPQAAQGASAPSP-------AADDPVPLP-----------PEPDDPPDPAGAPAQPPPPPAPAPA 767
                         170
                  ....*....|
gi 47226142  2472 GSSPAPTTPT 2481
Cdd:PRK07764  768 AAPAAAPPPS 777
PHA03247 PHA03247
large tegument protein UL36; Provisional
708-963 6.95e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   708 GQPPIGLPPNGPLPEVSMVRPAGPNqmvnrmqgpGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMVGSRMGQPNVNQLQ 787
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPS---------PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQA 2676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   788 NQYLSQGQFPGAGQGVGPAQpGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPT 867
Cdd:PHA03247 2677 SSPPQRPRRRAARPTVGSLT-SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA 2755
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   868 PHQTPPRLAGSQTPQPhtPSAPQLAPPPGAQQNHLGQGPGSNKSL--QQQHMGPAGSTTPSHPGLASSSTPHGAqLPRTP 945
Cdd:PHA03247 2756 RPARPPTTAGPPAPAP--PAAPAAGPPRRLTRPAVASLSESRESLpsPWDPADPPAAVLAPAAALPPAASPAGP-LPPPT 2832
                         250
                  ....*....|....*...
gi 47226142   946 VITTNTPPLDTSSQQPHL 963
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSL 2850
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
795-898 7.51e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   795 QFPGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPTPHQTPP- 873
Cdd:PRK07764  395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAp 474
                          90       100
                  ....*....|....*....|....*
gi 47226142   874 RLAGSQTPQPHTPSAPQLAPPPGAQ 898
Cdd:PRK07764  475 EPTAAPAPAPPAAPAPAAAPAAPAA 499
PHA03247 PHA03247
large tegument protein UL36; Provisional
2380-2482 1.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2380 PSAAQQPHEPPATNGPVPPP-PRTGWPRPS-----RVAQQSGPLSPTLAEAAVAAAALQPLPTHA----ALLPASAFPPP 2449
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSlPLGGSVAPGgdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRStesfALPPDQPERPP 2909
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 47226142  2450 H-----LPTDTDWFAPPGASEPAPPQYGSSPAPTTPTA 2482
Cdd:PHA03247 2910 QpqappPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTT 2947
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
798-899 1.36e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   798 GAGQGVGPAqPGIAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPTPHQTPPRLAG 877
Cdd:PRK12323  367 QSGGGAGPA-TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPG 445
                          90       100
                  ....*....|....*....|...
gi 47226142   878 SQT-PQPHTPSAPQLAPPPGAQQ 899
Cdd:PRK12323  446 GAPaPAPAPAAAPAAAARPAAAG 468
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1691-1726 1.73e-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: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 47226142 1691 TCNECKHHV--ETRFHCTVCEDYDLCITCYNTKGHEHK 1726
Cdd:cd02344    2 TCDGCQMFPinGPRFKCRNCDDFDFCENCFKTRKHNTR 39
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
797-958 2.00e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   797 PGAGQGVG----PAQPG-IAQPGTQTNMAQSVGAGTAGAPASSVASSNANQQAnaiphlSAMRGSSPSPAHSRSPTPHQT 871
Cdd:PRK07003  362 VTGGGAPGggvpARVAGaVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKA------AAAAAATRAEAPPAAPAPPAT 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   872 PPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQqqhMGPAGSTTPshPGLASSSTPHGAQLPRTPVITTNT 951
Cdd:PRK07003  436 ADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSA---SAPASDAPP--DAAFEPAPRAAAPSAATPAAVPDA 510

                  ....*..
gi 47226142   952 PPLDTSS 958
Cdd:PRK07003  511 RAPAAAS 517
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
2380-2483 2.33e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.38  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2380 PSAAQQPHEPPATNGPVPPPPRTGWPRPSRVAQQSGPLSPtlaeaavAAAALQPLPTHAALlpaSAFPPPHLPTDTdwfa 2459
Cdd:PLN03209  324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQP-------KAVVPRPLSPYTAY---EDLKPPTSPIPT---- 389
                          90       100
                  ....*....|....*....|....
gi 47226142  2460 PPGASEPAPPQYGSSPAPTTPTAS 2483
Cdd:PLN03209  390 PPSSSPASSKSVDAVAKPAEPDVV 413
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
823-942 2.46e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   823 VGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPTPHQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHL 902
Cdd:PRK07764  386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 47226142   903 GQGPGSNKSLQQQHMGPAGSTTPSHPGLASSSTPHGAQLP 942
Cdd:PRK07764  466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
779-962 3.10e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    779 GQPNVNQLQNQYLSQGQFPGAGQ------GVGPAQPGIA-QPGTQTNMAQSVGAGTAGAPASSVASSNANQQANAIPHLS 851
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTtqaataGPTPSAPSVPpQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    852 AMRGSSPSPAHSRSPTPHQtPPRLAGSQTPQPHT----------PSAPQlaPPPGAQQNHLGQGPGSNKSLQQQHMGPAG 921
Cdd:pfam03154  249 LQPMTQPPPPSQVSPQPLP-QPSLHGQMPPMPHSlqtgpshmqhPVPPQ--PFPLTPQSSQSQVPPGPSPAAPGQSQQRI 325
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 47226142    922 STTPSHPGLASSSTPHGAQLPRTPVI--------TTNTPPLDTSSQQPH 962
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSmphikpppTTPIPQLPNPQSHKH 374
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
797-890 3.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.74  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   797 PGAGQGVGPAQPGIAQPGTQ-----TNMAQSVGAGTAGAPASSVASSNANQQANAIPHLS--------AMRGSSPSPAHS 863
Cdd:PRK14959  387 EGPASGGAATIPTPGTQGPQgtapaAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSgipprpapRMPEASPVPGAP 466
                          90       100
                  ....*....|....*....|....*...
gi 47226142   864 RS-PTPHQTPPRLAGSQTPQPHTPSAPQ 890
Cdd:PRK14959  467 DSvASASDAPPTLGDPSDTAEHTPSGPR 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
2313-2481 4.19e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2313 GAAGAMPPIGGPGAIQIGNLDAQQTASVNQAGQPGMNLGQGAAGVSCHAAPEHPPEAPAaaapgrgfPSAAQQPHEPPAT 2392
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP--------AAKPAAPARPPVR 2884
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  2393 NGPVPPPPRTGWPRPSRVAQQSGPLSPTLAEAAVAAAALQPLPTHAALLPASAFPPPHLPTDTDWFAPPGASEPAP-PQY 2471
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPqPWL 2964
                         170       180
                  ....*....|....*....|....
gi 47226142  2472 G--------------SSPAPTTPT 2481
Cdd:PHA03247 2965 GalvpgrvavprfrvPQPAPSREA 2988
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
822-944 4.23e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.36  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   822 SVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSSPSPAHSRSPT--------PHQTP-PRLAGSQTPQphTPSAPQLA 892
Cdd:PRK14959  372 RPSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSsaapatpaPSAAPsPRVPWDDAPP--APPRSGIP 449
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 47226142   893 PPPGAQQNHLGQGPGSNKSLQQqhmgpAGSTTPSHpGLASSSTPHGAQLPRT 944
Cdd:PRK14959  450 PRPAPRMPEASPVPGAPDSVAS-----ASDAPPTL-GDPSDTAEHTPSGPRT 495
PPE COG5651
PPE-repeat protein [Function unknown];
757-970 4.37e-03

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 42.19  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  757 RSTPPLPMGATGNQMGMVGSRMGQPNVNQlqnQYLSQGQFPGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVA 836
Cdd:COG5651  167 FTQPPPTITNPGGLLGAQNAGSGNTSSNP---GFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAA 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142  837 SSNANQQANAIPHLSAMRGSSPSPAHSrSPTPHQTPPRLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQH 916
Cdd:COG5651  244 AAAAAAAAGAGASAALASLAATLLNAS-SLGLAATAASSAATNLGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGAT 322
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 47226142  917 MGPAGSTTPSHPGLASSSTPHGAQLPRTPVITTNTPPLDTSSQQPHLDTSSTSL 970
Cdd:COG5651  323 GAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAG 376
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
1690-1723 4.91e-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: 36.91  E-value: 4.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 47226142 1690 YTCNEC-KHHVETRFHCTVCEDYDLCITCYNtKGH 1723
Cdd:cd02336    1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ-EGR 34
PHA03377 PHA03377
EBNA-3C; Provisional
703-936 5.21e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 42.35  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   703 GPASMGQPPIGLPPNGPlpEVSMVRPAGPNQMVNRMQGPGMNQFNQMGMQSMGQR-----STPPLPMGATGNQMGMVGSR 777
Cdd:PHA03377  561 GPPKASPPVMAPPSTGP--RVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHekqppSSAPRDMAPSVVRMFLRERL 638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   778 MGQPNVNQLQNQYlsqgQFPGAGQGVGPAQPGIAQPGTQTnmaQSVGAGTAGAPASSVASS--NANQQANAIPHLSAMrg 855
Cdd:PHA03377  639 LEQSTGPKPKSFW----EMRAGRDGSGIQQEPSSRRQPAT---QSTPPRPSWLPSVFVLPSvdAGRAQPSEESHLSSM-- 709
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   856 sSPSpahsrSPTPHQTPPRLAGSQTPQpHTPSAPQLAPPPGAQQNHLG-QGPGSNKSLQQQHMGP-------AGSTTPSH 927
Cdd:PHA03377  710 -SPT-----QPISHEEQPRYEDPDDPL-DLSLHPDQAPPPSHQAPYSGhEEPQAQQAPYPGYWEPrppqapyLGYQEPQA 782

                  ....*....
gi 47226142   928 PGLASSSTP 936
Cdd:PHA03377  783 QGVQVSSYP 791
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
797-941 6.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   797 PGAGQGVGPAQPGIAQPGTQTNMAQSVGAGTAGAPASSVAS---SNANQQANAIPHLSAMRGSSPSPAHSRSPTPHQTPP 873
Cdd:PRK07764  365 PSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAApaaAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSP 444
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47226142   874 RLAGSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTTPSHPGLASSSTPHGAQL 941
Cdd:PRK07764  445 AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1691-1721 7.65e-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: 7.65e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 47226142 1691 TCNECKHHVET--RFHCTVCEDYDLCITCYNTK 1721
Cdd:cd02338    2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSG 34
Androgen_recep pfam02166
Androgen receptor;
801-935 7.87e-03

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 41.45  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142    801 QGVGPAQPGIAQ----PGTQTNMAQSVGAGTAGAPASSvASSNANQQANAIPHLSAMRGSSPspAHSRSPTPHQTpprLA 876
Cdd:pfam02166   30 QNPGPRHPEAAGgaapPGARLQHQQQQQQQVPQQPQQQ-ESSPRQPQASVQPQQAGDDGSPP--AHNRGPAGYLA---LE 103
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47226142    877 GSQTPQPHTPSAPQLAPPPGAQQNHLGQGPGSNKSLQQQHMGPAGSTT-------------PSHPGLASSST 935
Cdd:pfam02166  104 DDEQPQPSQAQPAAECCPENGCVPEPGAAAAAGKGLPQQAVAPAAPDDddsaapstlsllgPSFPGLSGCSA 175
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
703-899 7.89e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   703 GPASMGQPPIGLPPNGPLPEVSMVRPAGPNQMVNRMQGPGMNQFNQMGMQSMGQRSTPPLPMGATGNQMGMVGSRMGQPn 782
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG- 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226142   783 vnqlqnqylsqgQFPGAGQGVGPAQPGIAQPGTQTnmAQSVGAGTAGAPASSVASSNANQQANAIPHLSAMRGSS-PSPA 861
Cdd:PRK07764  669 ------------WPAKAGGAAPAAPPPAPAPAAPA--APAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASaPSPA 734
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47226142   862 HSRSPTPHQTP-PRLAGSQTPQPHTPSAPQLAPPPGAQQ 899
Cdd:PRK07764  735 ADDPVPLPPEPdDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
 
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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