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Conserved domains on  [gi|1785364689|ref|XP_004913856|]
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histone acetyltransferase p300 isoform X2 [Xenopus tropicalis]

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 ...
1345-1651 4.79e-96

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: 314.72  E-value: 4.79e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1345 VNDFLRRQNnPEAGEVIIRVVHASDKTVEVKPGMKAKFVDTGEmaESFPYRTKALFAFEEVDGVELCFFGMHVQEYGSDC 1424
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1425 PQPNQRRVYISYLDSVHFFRPKnLRTAVYHEILIGYLEYVKRLGYTAGHIWACPPSEGDDYIFhchPADQKIPK-----P 1499
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1500 KRLQEWYKKMLDKSVSE-------RVIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1554
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1555 SIkeleqeEEERKREENTSNESIEVGK-------------GDSKNAKKKNNKKTSKNKSSLSRGSKK------------- 1608
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEELRFrqefslgrlvgfiGLEGDYTPGSDDVINPPGLVKSKKQYKmiksyitgreyst 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1785364689 1609 KPGMPNVSNDLSQKLYATMEKHkevFFVIRLSAGPAANSLPPI 1651
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1080-1187 1.67e-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: 248.90  E-value: 1.67e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1080 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWL 1159
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1785364689 1160 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1187
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 ...
563-643 1.87e-46

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: 161.89  E-value: 1.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  563 GIRKPWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRAEYYHFLAEKIYKIQKELE 642
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1785364689  643 E 643
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1199-1281 1.13e-31

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: 119.32  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1199 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpkygllaDRYHFCEKCFNEIQGECVSLGDDptqPQTTISKDQFSKRKND 1276
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                   ....*
gi 1785364689 1277 TLDPE 1281
Cdd:cd15802     69 ELDEE 73
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2054-2154 7.79e-30

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: 115.32  E-value: 7.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2054 QSGLPQSQSMQPGMQRSPIMSVPQ-QGQPMNMNPQSGIGQVPGASQTKQGSLPQAALQNLLRTLRSPSSPMQQQQVLNIL 2132
Cdd:pfam09030    8 QWQQQQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVPGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQQQVLNIL 87
                           90       100
                   ....*....|....*....|..
gi 1785364689 2133 HSNPQLLAAFIKQRAAKYASSQ 2154
Cdd:pfam09030   88 KSNPQLMAAFIKQRTAKYQASQ 109
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
347-414 1.93e-28

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.93e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785364689  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
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 ...
1707-1747 1.62e-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: 106.49  E-value: 1.62e-27
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1785364689 1707 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKTHEHKMEKL 1747
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1774-1842 9.63e-24

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


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 96.69  E-value: 9.63e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785364689 1774 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1842
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1282-1316 2.74e-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: 85.68  E-value: 2.74e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1785364689 1282 QYVECLECGRKMHQICVLHNETIWPTGFVCEGCLK 1316
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
761-982 6.76e-09

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.71  E-value: 6.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  761 TAQNQFLSQNQFQASSPVMNTGGMNTGGLNASGMPMPQPgnqNPSSQAPMPNPSHPVSS-PVMPPGAAGNQMHCSSHVQP 839
Cdd:pfam03154  161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQpPNQTQSTAAPHTLIQQTPTL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  840 MHRNSPSPAPSRTPTPHHTPPGLT-PQPTQTPVQ--PILPTAAPISQAPlQHRESPTPPQvtpslsiPTPVMSTADQQIA 916
Cdd:pfam03154  238 HPQRLPSPHPPLQPMTQPPPPSQVsPQPLPQPSLhgQMPPMPHSLQTGP-SHMQHPVPPQ-------PFPLTPQSSQSQV 309
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689  917 TPPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP 375
DUF4175 super family cl44629
Domain of unknown function (DUF4175);
665-809 1.59e-07

Domain of unknown function (DUF4175);


The actual alignment was detected with superfamily member pfam13779:

Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 56.92  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  665 QMNQNQGMAQPqtglstngplPDPNS-MMRANVPNQIMNRMQ--TQTG-MNQFGQMGMQMQSMGQRQQAPLQHPGQMGQT 740
Cdd:pfam13779  533 AQQNPQDLQQP----------DDPNAqEMTQQDLQRMLDRIEelARSGrRAEAQQMLSQLQQMLENLQAGQPQQQQQQGQ 602
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  741 GPMNQMgfqarMQQPGTM---QQTAQNQFLSQNQ-FQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAP 809
Cdd:pfam13779  603 SEMQQA-----MDELGDLlreQQQLLDETFRQLQqQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGA 670
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1870-2183 4.86e-05

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.85  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1870 RMASMQRAGGVGP--QQGLPSPNSAGPATPTGQQPPTPQTPQPPPQPPTQQQPPPPNMPPYSMARAEPARGISQGKAAGQ 1947
Cdd:pfam09606  145 RVGRMQPGGQAGGmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQ 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1948 MTPPTPPQAGAMqqqvqGPPPAAVEMAMQIQRAAETQRQMAKAQIFPRPMMNPHQMQPMNPMQPMGMNPQQgprgQVHME 2027
Cdd:pfam09606  225 ANGGMNPQQMGG-----APNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ----PGAMP 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2028 SGIGPGMQQPQQQQQPPPTQPQPPWVQSGLPQSQSMQPGMQRSPIMSVPQQGQPMNMNPQSGIGQVPGASQTKQG---SL 2104
Cdd:pfam09606  296 NVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPgmmSS 375
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 2105 PQAALQNLLRTLRSPSSPMQQQQVLNILHSNPqllaafiKQRAAKYASSQNAQAAGNVPGMPAQAGLQQVVHSNPGMQG 2183
Cdd:pfam09606  376 PSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-------GSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDS 447
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
2317-2456 7.22e-05

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


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2317 QMSQMPQGMPGDTSSGLQTFPQRLLHQQMgspAQQNPMSPQQHmlPGPAQSPH-LQGQQLPPSLSNQvRSPQPVPSPRPQ 2395
Cdd:pfam09770  217 APAQPPAAPPAQQAQQQQQFPPQIQQQQQ---PQQQPQQPQQH--PGQGHPVTiLQRPQSPQPDPAQ-PSIQPQAQQFHQ 290
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689 2396 SQPPHSSPSPRMQPQP---SPHHVSPQTSSPHPGLVGPGQGNPMDQGHYGSPDP-TAMLSQMAGL 2456
Cdd:pfam09770  291 QPPPVPVQPTQILQNPnrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPiITHPQQLAQL 355
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1345-1651 4.79e-96

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: 314.72  E-value: 4.79e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1345 VNDFLRRQNnPEAGEVIIRVVHASDKTVEVKPGMKAKFVDTGEmaESFPYRTKALFAFEEVDGVELCFFGMHVQEYGSDC 1424
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1425 PQPNQRRVYISYLDSVHFFRPKnLRTAVYHEILIGYLEYVKRLGYTAGHIWACPPSEGDDYIFhchPADQKIPK-----P 1499
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1500 KRLQEWYKKMLDKSVSE-------RVIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1554
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1555 SIkeleqeEEERKREENTSNESIEVGK-------------GDSKNAKKKNNKKTSKNKSSLSRGSKK------------- 1608
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEELRFrqefslgrlvgfiGLEGDYTPGSDDVINPPGLVKSKKQYKmiksyitgreyst 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1785364689 1609 KPGMPNVSNDLSQKLYATMEKHkevFFVIRLSAGPAANSLPPI 1651
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1080-1187 1.67e-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: 248.90  E-value: 1.67e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1080 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWL 1159
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1785364689 1160 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1187
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 ...
563-643 1.87e-46

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: 161.89  E-value: 1.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  563 GIRKPWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRAEYYHFLAEKIYKIQKELE 642
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1785364689  643 E 643
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1077-1185 5.93e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 5.93e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  1077 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNN 1156
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1785364689  1157 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1185
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1199-1281 1.13e-31

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: 119.32  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1199 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpkygllaDRYHFCEKCFNEIQGECVSLGDDptqPQTTISKDQFSKRKND 1276
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                   ....*
gi 1785364689 1277 TLDPE 1281
Cdd:cd15802     69 ELDEE 73
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2054-2154 7.79e-30

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: 115.32  E-value: 7.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2054 QSGLPQSQSMQPGMQRSPIMSVPQ-QGQPMNMNPQSGIGQVPGASQTKQGSLPQAALQNLLRTLRSPSSPMQQQQVLNIL 2132
Cdd:pfam09030    8 QWQQQQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVPGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQQQVLNIL 87
                           90       100
                   ....*....|....*....|..
gi 1785364689 2133 HSNPQLLAAFIKQRAAKYASSQ 2154
Cdd:pfam09030   88 KSNPQLMAAFIKQRTAKYQASQ 109
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
347-414 1.93e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.93e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785364689  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
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 ...
1707-1747 1.62e-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: 106.49  E-value: 1.62e-27
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1785364689 1707 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKTHEHKMEKL 1747
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1774-1842 9.63e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 96.69  E-value: 9.63e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785364689 1774 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1842
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1768-1846 2.13e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.89  E-value: 2.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  1768 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1843
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 1785364689  1844 FCL 1846
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1185-1224 2.49e-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: 94.31  E-value: 2.49e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1785364689 1185 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1224
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
347-417 1.71e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.50  E-value: 1.71e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785364689   347 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 417
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1282-1316 2.74e-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: 85.68  E-value: 2.74e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1785364689 1282 QYVECLECGRKMHQICVLHNETIWPTGFVCEGCLK 1316
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1097-1173 2.95e-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: 84.29  E-value: 2.95e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364689 1097 QDPESLPFRQPVDPqlLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSK 1173
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1703-1745 1.51e-16

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: 75.17  E-value: 1.51e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1785364689  1703 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKTHEHKME 1745
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1078-1186 1.24e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1078 FKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNA 1157
Cdd:COG5076    143 LYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNC 220
                           90       100
                   ....*....|....*....|....*....
gi 1785364689 1158 WLYNRKTSRVYKYCSKLAEVFEQEIDPVM 1186
Cdd:COG5076    221 KLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1703-1744 2.35e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.75  E-value: 2.35e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1785364689 1703 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNT-KTHEHKM 1744
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2108-2150 2.10e-14

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: 69.22  E-value: 2.10e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1785364689 2108 ALQNLLRTLRSPSSPMQQQQVLNILHSNPQLLAAFIKQRAAKY 2150
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
761-982 6.76e-09

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: 61.71  E-value: 6.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  761 TAQNQFLSQNQFQASSPVMNTGGMNTGGLNASGMPMPQPgnqNPSSQAPMPNPSHPVSS-PVMPPGAAGNQMHCSSHVQP 839
Cdd:pfam03154  161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQpPNQTQSTAAPHTLIQQTPTL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  840 MHRNSPSPAPSRTPTPHHTPPGLT-PQPTQTPVQ--PILPTAAPISQAPlQHRESPTPPQvtpslsiPTPVMSTADQQIA 916
Cdd:pfam03154  238 HPQRLPSPHPPLQPMTQPPPPSQVsPQPLPQPSLhgQMPPMPHSLQTGP-SHMQHPVPPQ-------PFPLTPQSSQSQV 309
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689  917 TPPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP 375
PHA03247 PHA03247
large tegument protein UL36; Provisional
777-982 4.73e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 4.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  777 PVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPH 856
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  857 HTPPGLTPQPTQ-TPVQPILPTAAPISQ----------APLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQ 925
Cdd:PHA03247  2822 ASPAGPLPPPTSaQPTAPPPPPGPPPPSlplggsvapgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689  926 QFSSQQQPLPRPPSQPSLTTPVATPT--APPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:PHA03247  2902 PDQPERPPQPQAPPPPQPQPQPPPPPqpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
DUF4175 pfam13779
Domain of unknown function (DUF4175);
665-809 1.59e-07

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 56.92  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  665 QMNQNQGMAQPqtglstngplPDPNS-MMRANVPNQIMNRMQ--TQTG-MNQFGQMGMQMQSMGQRQQAPLQHPGQMGQT 740
Cdd:pfam13779  533 AQQNPQDLQQP----------DDPNAqEMTQQDLQRMLDRIEelARSGrRAEAQQMLSQLQQMLENLQAGQPQQQQQQGQ 602
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  741 GPMNQMgfqarMQQPGTM---QQTAQNQFLSQNQ-FQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAP 809
Cdd:pfam13779  603 SEMQQA-----MDELGDLlreQQQLLDETFRQLQqQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGA 670
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
795-956 2.80e-06

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 468188 [Multi-domain]  Cd Length: 1552  Bit Score: 53.02  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  795 PMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPaPSRTPTphhtppglTPQPTQtPVQPI 874
Cdd:NF033804   854 PAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTP-PVKTPD--------QPEPSK-PEEPT 923
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  875 LPTAAPISQAPLQ--HRESPTPPQVTPSLSIPT-PVMSTADqqiatppsqqpsqqfssqqqPLPRPPSQPsltTPVATPT 951
Cdd:NF033804   924 YETEKPLEPAPVApsYENEPTPPVKTPDQPEPSkPVEPTYD--------------------PLPTPPVAP---TPKQLPT 980

                   ....*
gi 1785364689  952 APPLP 956
Cdd:NF033804   981 PPAVP 985
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
703-841 1.59e-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: 50.19  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  703 RMQTQTGMNQFgQMGMQMQSMGQRQQAPLQHPGQMGQTGPMN-----QMGFQARMQ---QPGTMQQTAQNQFLSQNQFQA 774
Cdd:TIGR01628  375 FMQLQPRMRQL-PMGSPMGGAMGQPPYYGQGPQQQFNGQPLGwprmsMMPTPMGPGgplRPNGLAPMNAVRAPSRNAQNA 453
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  775 SS--PVMNTGGMNTGGLNASGMPMPQPgNQNPSSQAPMPNPSHPVSSpvMPPG----AAGNQMHcsSHVQPMH 841
Cdd:TIGR01628  454 AQkpPMQPVMYPPNYQSLPLSQDLPQP-QSTASQGGQNKKLAQVLAS--ATPQmqkqVLGERLF--PLVEAIE 521
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1870-2183 4.86e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.85  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1870 RMASMQRAGGVGP--QQGLPSPNSAGPATPTGQQPPTPQTPQPPPQPPTQQQPPPPNMPPYSMARAEPARGISQGKAAGQ 1947
Cdd:pfam09606  145 RVGRMQPGGQAGGmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQ 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1948 MTPPTPPQAGAMqqqvqGPPPAAVEMAMQIQRAAETQRQMAKAQIFPRPMMNPHQMQPMNPMQPMGMNPQQgprgQVHME 2027
Cdd:pfam09606  225 ANGGMNPQQMGG-----APNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ----PGAMP 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2028 SGIGPGMQQPQQQQQPPPTQPQPPWVQSGLPQSQSMQPGMQRSPIMSVPQQGQPMNMNPQSGIGQVPGASQTKQG---SL 2104
Cdd:pfam09606  296 NVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPgmmSS 375
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 2105 PQAALQNLLRTLRSPSSPMQQQQVLNILHSNPqllaafiKQRAAKYASSQNAQAAGNVPGMPAQAGLQQVVHSNPGMQG 2183
Cdd:pfam09606  376 PSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-------GSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDS 447
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
2317-2456 7.22e-05

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: 48.49  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2317 QMSQMPQGMPGDTSSGLQTFPQRLLHQQMgspAQQNPMSPQQHmlPGPAQSPH-LQGQQLPPSLSNQvRSPQPVPSPRPQ 2395
Cdd:pfam09770  217 APAQPPAAPPAQQAQQQQQFPPQIQQQQQ---PQQQPQQPQQH--PGQGHPVTiLQRPQSPQPDPAQ-PSIQPQAQQFHQ 290
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689 2396 SQPPHSSPSPRMQPQP---SPHHVSPQTSSPHPGLVGPGQGNPMDQGHYGSPDP-TAMLSQMAGL 2456
Cdd:pfam09770  291 QPPPVPVQPTQILQNPnrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPiITHPQQLAQL 355
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1959-2129 1.45e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 47.11  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1959 MQQQVQGPPPAAVEMAMQI-QRAAETQRQMAKAQIFPRPMMNPHQMQPMNPMQPM-GMNPQQGPRGQVHMeSGIGPGMQQ 2036
Cdd:TIGR01628  346 MHGRMLGGKPLYVALAQRKeQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYyGQGPQQQFNGQPLG-WPRMSMMPT 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2037 PQQQQQPPPTQPQPPWVQSGLPQSQSmQPGMQRSPIMSVPQQgqpmnmnPQSGIGQVPGASQTKQGSLPQAALQNLLRTL 2116
Cdd:TIGR01628  425 PMGPGGPLRPNGLAPMNAVRAPSRNA-QNAAQKPPMQPVMYP-------PNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
                          170
                   ....*....|...
gi 1785364689 2117 RSPSSPMQQQQVL 2129
Cdd:TIGR01628  497 LASATPQMQKQVL 509
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
2303-2413 4.27e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2303 RFQHHIQMQQGSMGQMSQMPQGMPGDTSSGLQTFPQRLLHQQMGS-----PAQQNPMSPQQHMLPGPAQSPHLQGQQLPP 2377
Cdd:TIGR01628  367 RRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGqplgwPRMSMMPTPMGPGGPLRPNGLAPMNAVRAP 446
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1785364689 2378 SLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSP 2413
Cdd:TIGR01628  447 SRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
838-966 7.32e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.47  E-value: 7.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689   838 QPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPslsiptPVMSTADQQIAT 917
Cdd:smart00818   37 HQIIPVSQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQ------PFQPQPLQPPQP 110
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1785364689   918 PPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPT 966
Cdd:smart00818  111 QQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATDKT 159
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1345-1651 4.79e-96

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: 314.72  E-value: 4.79e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1345 VNDFLRRQNnPEAGEVIIRVVHASDKTVEVKPGMKAKFVDTGEmaESFPYRTKALFAFEEVDGVELCFFGMHVQEYGSDC 1424
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1425 PQPNQRRVYISYLDSVHFFRPKnLRTAVYHEILIGYLEYVKRLGYTAGHIWACPPSEGDDYIFhchPADQKIPK-----P 1499
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1500 KRLQEWYKKMLDKSVSE-------RVIHDYKDIFKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1554
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1555 SIkeleqeEEERKREENTSNESIEVGK-------------GDSKNAKKKNNKKTSKNKSSLSRGSKK------------- 1608
Cdd:pfam08214  234 LI------KEGRWKSVSLDQFWEELRFrqefslgrlvgfiGLEGDYTPGSDDVINPPGLVKSKKQYKmiksyitgreyst 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1785364689 1609 KPGMPNVSNDLSQKLYATMEKHkevFFVIRLSAGPAANSLPPI 1651
Cdd:pfam08214  308 EEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1080-1187 1.67e-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: 248.90  E-value: 1.67e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1080 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWL 1159
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1785364689 1160 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1187
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 ...
563-643 1.87e-46

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: 161.89  E-value: 1.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  563 GIRKPWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRAEYYHFLAEKIYKIQKELE 642
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1785364689  643 E 643
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
1077-1185 5.93e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.01  E-value: 5.93e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  1077 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNN 1156
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1785364689  1157 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1185
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1199-1281 1.13e-31

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: 119.32  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1199 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpkygllaDRYHFCEKCFNEIQGECVSLGDDptqPQTTISKDQFSKRKND 1276
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68

                   ....*
gi 1785364689 1277 TLDPE 1281
Cdd:cd15802     69 ELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1083-1182 1.00e-30

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


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 117.47  E-value: 1.00e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1083 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYN 1161
Cdd:cd04369      1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                           90       100
                   ....*....|....*....|.
gi 1785364689 1162 RKTSRVYKYCSKLAEVFEQEI 1182
Cdd:cd04369     79 GPGSPIYKDAKKLEKLFEKLL 99
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
2054-2154 7.79e-30

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: 115.32  E-value: 7.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2054 QSGLPQSQSMQPGMQRSPIMSVPQ-QGQPMNMNPQSGIGQVPGASQTKQGSLPQAALQNLLRTLRSPSSPMQQQQVLNIL 2132
Cdd:pfam09030    8 QWQQQQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVPGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQQQVLNIL 87
                           90       100
                   ....*....|....*....|..
gi 1785364689 2133 HSNPQLLAAFIKQRAAKYASSQ 2154
Cdd:pfam09030   88 KSNPQLMAAFIKQRTAKYQASQ 109
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1103-1180 1.23e-29

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: 114.68  E-value: 1.23e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785364689 1103 PFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1180
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 ...
347-414 1.93e-28

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.17  E-value: 1.93e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785364689  347 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 414
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 ...
1707-1747 1.62e-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: 106.49  E-value: 1.62e-27
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1785364689 1707 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKTHEHKMEKL 1747
Cdd:cd02337      1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1082-1182 1.23e-26

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


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 105.71  E-value: 1.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1082 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYN 1161
Cdd:cd05509      1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                           90       100
                   ....*....|....*....|.
gi 1785364689 1162 RKTSRVYKYCSKLAEVFEQEI 1182
Cdd:cd05509     78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1096-1179 3.91e-25

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: 101.64  E-value: 3.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1096 RQDPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLA 1175
Cdd:cd05506     13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                   ....
gi 1785364689 1176 EVFE 1179
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 ...
1774-1842 9.63e-24

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


Pssm-ID: 460457  Cd Length: 72  Bit Score: 96.69  E-value: 9.63e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785364689 1774 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1842
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1768-1846 2.13e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.89  E-value: 2.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  1768 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1843
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 1785364689  1844 FCL 1846
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1185-1224 2.49e-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: 94.31  E-value: 2.49e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1785364689 1185 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1224
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1090-1182 4.74e-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: 95.84  E-value: 4.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1090 TLEALYRQdPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYK 1169
Cdd:cd05500     12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                           90
                   ....*....|...
gi 1785364689 1170 YCSKLAEVFEQEI 1182
Cdd:cd05500     91 MGKRLQAAFEKHL 103
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1085-1184 6.32e-23

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: 95.57  E-value: 6.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1085 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRK 1163
Cdd:cd05497      7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                           90       100
                   ....*....|....*....|.
gi 1785364689 1164 TSRVYKYCSKLAEVFEQEIDP 1184
Cdd:cd05497     86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1078-1180 2.86e-22

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


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 93.89  E-value: 2.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1078 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFEIVKTPMDLSTIKRKLD---TGQYQEPWQYVEDIWLMF 1154
Cdd:cd05502      1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                           90       100
                   ....*....|....*....|....*.
gi 1785364689 1155 NNAWLYNRKTSRVYKYCSKLAEVFEQ 1180
Cdd:cd05502     76 KNCYKFNEEDSEVAQAGKELELFFEE 101
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1100-1188 3.85e-22

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 93.68  E-value: 3.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1100 ESLPFRQPVDpqLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYN-RKTSRVYKYCSKLAEVF 1178
Cdd:cd05496     22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                           90
                   ....*....|
gi 1785364689 1179 EQEIDPVMQS 1188
Cdd:cd05496    100 EEHIKKIISD 109
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
347-417 1.71e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.50  E-value: 1.71e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785364689   347 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 417
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1282-1316 2.74e-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: 85.68  E-value: 2.74e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1785364689 1282 QYVECLECGRKMHQICVLHNETIWPTGFVCEGCLK 1316
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1103-1179 1.51e-19

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: 85.80  E-value: 1.51e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364689 1103 PFRQPVDPQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFE 1179
Cdd:cd05499     23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1097-1173 2.95e-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: 84.29  E-value: 2.95e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364689 1097 QDPESLPFRQPVDPqlLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSK 1173
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 ...
1081-1181 8.38e-19

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 83.98  E-value: 8.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1081 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMF 1154
Cdd:cd05504      4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                           90       100
                   ....*....|....*....|....*..
gi 1785364689 1155 NNAWLYNRKTSRVYKYCSKLAEVFEQE 1181
Cdd:cd05504     82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1703-1745 1.51e-16

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: 75.17  E-value: 1.51e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1785364689  1703 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKTHEHKME 1745
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1282-1314 1.68e-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: 75.00  E-value: 1.68e-16
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1785364689 1282 QYVECLECGRKMHQICVLHNETIWPTGFVCEGC 1314
Cdd:cd15557      5 QFVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1081-1171 5.66e-16

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: 75.94  E-value: 5.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1081 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLY 1160
Cdd:cd05510      6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                           90
                   ....*....|.
gi 1785364689 1161 NRKTSRVYKYC 1171
Cdd:cd05510     84 NSDPSHPLRRH 94
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1099-1167 5.98e-16

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: 75.49  E-value: 5.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1099 PESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRV 1167
Cdd:cd05503     16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1086-1176 1.20e-15

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


Pssm-ID: 99944  Cd Length: 98  Bit Score: 74.36  E-value: 1.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1086 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTS 1165
Cdd:cd05512      5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                           90
                   ....*....|.
gi 1785364689 1166 RVYKYCSKLAE 1176
Cdd:cd05512     82 IFYRAAVRLRD 92
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1078-1186 1.24e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1078 FKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNA 1157
Cdd:COG5076    143 LYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNC 220
                           90       100
                   ....*....|....*....|....*....
gi 1785364689 1158 WLYNRKTSRVYKYCSKLAEVFEQEIDPVM 1186
Cdd:COG5076    221 KLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1703-1744 2.35e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.75  E-value: 2.35e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1785364689 1703 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNT-KTHEHKM 1744
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1097-1184 3.39e-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: 3.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1097 QDPESLPFRQPVDPQllGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYN------RKTSRvYKY 1170
Cdd:cd05528     17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                           90
                   ....*....|....*..
gi 1785364689 1171 CSKLAEV---FEQEIDP 1184
Cdd:cd05528     94 CELRDEVhamIEAELDP 110
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1096-1181 4.56e-15

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 73.45  E-value: 4.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1096 RQDPESLPFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSR-------VY 1168
Cdd:cd05511     13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90
                           90
                   ....*....|...
gi 1785364689 1169 KYCSKLAEVFEQE 1181
Cdd:cd05511     91 ELAEELLAEREEK 103
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1283-1316 1.54e-14

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: 69.63  E-value: 1.54e-14
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1785364689 1283 YVECLECGRKMHQICVLHNETIWPTGFVCEGCLK 1316
Cdd:cd15647      7 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2108-2150 2.10e-14

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: 69.22  E-value: 2.10e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1785364689 2108 ALQNLLRTLRSPSSPMQQQQVLNILHSNPQLLAAFIKQRAAKY 2150
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1116-1169 7.42e-14

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 69.64  E-value: 7.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYK 1169
Cdd:cd05515     37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1707-1743 1.32e-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: 67.07  E-value: 1.32e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1785364689 1707 YTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKTHEHK 1743
Cdd:cd02249      1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1116-1187 2.35e-13

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: 68.51  E-value: 2.35e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1187
Cdd:cd05524     39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1239-1314 5.51e-13

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


Pssm-ID: 277086  Cd Length: 73  Bit Score: 66.22  E-value: 5.51e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1239 FCEKCFNEIQGECVSLGddptqpQTTISKDQFSKRKNDTLDPEQYVECLECGRKMHQICVLHNE---TIWPTGFVCEGC 1314
Cdd:cd15614      1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGrrnADETAEYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1084-1181 1.77e-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: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1084 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRk 1163
Cdd:cd05507      5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNS- 80
                           90
                   ....*....|....*...
gi 1785364689 1164 tsrvYKYCSKLAEVFEQE 1181
Cdd:cd05507     81 ----SDHDVYLMAVEMQR 94
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1079-1178 1.14e-11

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: 63.32  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1079 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAW 1158
Cdd:cd05505      4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                           90       100
                   ....*....|....*....|
gi 1785364689 1159 LYNRKTSRVYKYCSKLAEVF 1178
Cdd:cd05505     74 KYYENGSYVLSCMRKTEQCC 93
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1115-1183 1.43e-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: 63.22  E-value: 1.43e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1115 IPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEID 1183
Cdd:cd05516     37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1083-1174 2.88e-11

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: 62.04  E-value: 2.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1083 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNR 1162
Cdd:cd05513      2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                           90
                   ....*....|..
gi 1785364689 1163 KTSRVYKYCSKL 1174
Cdd:cd05513     79 PDTIYYKAAKKL 90
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1116-1174 8.49e-11

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


Pssm-ID: 99951  Cd Length: 103  Bit Score: 60.82  E-value: 8.49e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKL 1174
Cdd:cd05520     37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1082-1170 1.86e-10

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: 60.03  E-value: 1.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1082 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFEIVKTPMDLSTIKRKLDtgQYQEPWQYVEDIW 1151
Cdd:cd05521      1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                           90
                   ....*....|....*....
gi 1785364689 1152 LMFNNAWLYNRKTSRVYKY 1170
Cdd:cd05521     72 QIPWNARLYNTKGSVIYKY 90
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1083-1182 4.99e-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: 58.51  E-value: 4.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1083 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNA 1157
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                           90       100
                   ....*....|....*....|....*
gi 1785364689 1158 WLYNRKTSRVYKYCSKLAEVFEQEI 1182
Cdd:cd05519     79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1116-1174 1.11e-09

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: 57.64  E-value: 1.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKL 1174
Cdd:cd05522     38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1708-1747 3.82e-09

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 54.19  E-value: 3.82e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1785364689 1708 TCNECKHHVE-TRWHCTVCEDYDLCITCYNTKTH-EHKMEKL 1747
Cdd:cd02340      2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLKI 43
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1105-1168 4.43e-09

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: 55.91  E-value: 4.43e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1105 RQPVD-----PQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVY 1168
Cdd:cd05518     21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
761-982 6.76e-09

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: 61.71  E-value: 6.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  761 TAQNQFLSQNQFQASSPVMNTGGMNTGGLNASGMPMPQPgnqNPSSQAPMPNPSHPVSS-PVMPPGAAGNQMHCSSHVQP 839
Cdd:pfam03154  161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQpPNQTQSTAAPHTLIQQTPTL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  840 MHRNSPSPAPSRTPTPHHTPPGLT-PQPTQTPVQ--PILPTAAPISQAPlQHRESPTPPQvtpslsiPTPVMSTADQQIA 916
Cdd:pfam03154  238 HPQRLPSPHPPLQPMTQPPPPSQVsPQPLPQPSLhgQMPPMPHSLQTGP-SHMQHPVPPQ-------PFPLTPQSSQSQV 309
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689  917 TPPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP 375
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1081-1182 1.69e-08

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 55.04  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1081 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAW 1158
Cdd:cd05529     23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                           90       100
                   ....*....|....*....|....
gi 1785364689 1159 LYNRKTSRVYKYCSKLAEVFEQEI 1182
Cdd:cd05529    102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
638-973 2.44e-08

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: 59.78  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  638 QKELEEKRRTRLQKQHLIPTPPGMPPTQMNQnQGMAQPQTGLSTNGPLPDPNSMMranVPNQIMNRMQTQTGMNQFGQMG 717
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSPPPPGTTQ-AATAGPTPSAPSVPPQGSPATSQ---PPNQTQSTAAPHTLIQQTPTLH 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  718 MQ--------MQSMGQR---QQAPLQHPGQMGQTGPMNQMGFQ-----ARMQQPGTMQQTAQNQFLSQNQFQASSPVMNT 781
Cdd:pfam03154  239 PQrlpsphppLQPMTQPpppSQVSPQPLPQPSLHGQMPPMPHSlqtgpSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAP 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  782 G---GMNTGGLNASGMPMPQPGNQNPSSQAPMPNP--SHPVSSPVMPPGAAgnqmhcSSHVQPMHRNSPSP--APSRTPT 854
Cdd:pfam03154  319 GqsqQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNP------QSHKHPPHLSGPSPfqMNSNLPP 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  855 P-----------HH-----------------------TPPGLTPQPTQTPVQPILPTAAPISQAPLQ-----HRESPT-P 894
Cdd:pfam03154  393 PpalkplsslstHHppsahppplqlmpqsqqlppppaQPPVLTQSQSLPPPAASHPPTSGLHQVPSQspfpqHPFVPGgP 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  895 PQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPRPPSQPSLTTPVAT--PTAPPlPMQLQPSTPPTAnLDCP 972
Cdd:pfam03154  473 PPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAeePESPP-PPPRSPSPEPTV-VNTP 550

                   .
gi 1785364689  973 S 973
Cdd:pfam03154  551 S 551
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1116-1180 4.63e-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: 4.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1180
Cdd:cd05525     39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
777-982 4.73e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 4.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  777 PVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPH 856
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  857 HTPPGLTPQPTQ-TPVQPILPTAAPISQ----------APLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQ 925
Cdd:PHA03247  2822 ASPAGPLPPPTSaQPTAPPPPPGPPPPSlplggsvapgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689  926 QFSSQQQPLPRPPSQPSLTTPVATPT--APPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:PHA03247  2902 PDQPERPPQPQAPPPPQPQPQPPPPPqpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1116-1180 9.65e-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: 52.06  E-value: 9.65e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689 1116 PDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1180
Cdd:cd05517     37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
787-982 1.07e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  787 GGLNASGMPMPQPgnqnpssQAPMPNPSHPVSSPVMPPGAAGNQmhcsshvqpmhrnSPSPAPSRTPTPHHTPPG-LTPQ 865
Cdd:PHA03247  2693 GSLTSLADPPPPP-------PTPEPAPHALVSATPLPPGPAAAR-------------QASPALPAAPAPPAVPAGpATPG 2752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  866 PTQTPVQPILPtAAPISQAPLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPRPPSQPSLTT 945
Cdd:PHA03247  2753 GPARPARPPTT-AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1785364689  946 PVATPTAPPLPMQLQPSTPPTANLDCP----SSNPPSTNSP 982
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPggdvRRRPPSRSPA 2872
PHA03247 PHA03247
large tegument protein UL36; Provisional
797-982 1.54e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  797 PQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAgnqmhcSSHVQPMHRNSPSPAPSRTPTPHHT-PPGLTPQPTQTPVQPiL 875
Cdd:PHA03247  2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHP------PPTVPPPERPRDDPAPGRVSRPRRArRLGRAAQASSPPQRP-R 2684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  876 PTAAPISQAPLQHRESPTPPQVTP-------SLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLP---RPPSQPSLT- 944
Cdd:PHA03247  2685 RRAARPTVGSLTSLADPPPPPPTPepaphalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggpARPARPPTTa 2764
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1785364689  945 -----TPVATPTAPPLPmqlQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:PHA03247  2765 gppapAPPAAPAAGPPR---RLTRPAVASLSESRESLPSPWDP 2804
DUF4175 pfam13779
Domain of unknown function (DUF4175);
665-809 1.59e-07

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 56.92  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  665 QMNQNQGMAQPqtglstngplPDPNS-MMRANVPNQIMNRMQ--TQTG-MNQFGQMGMQMQSMGQRQQAPLQHPGQMGQT 740
Cdd:pfam13779  533 AQQNPQDLQQP----------DDPNAqEMTQQDLQRMLDRIEelARSGrRAEAQQMLSQLQQMLENLQAGQPQQQQQQGQ 602
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  741 GPMNQMgfqarMQQPGTM---QQTAQNQFLSQNQ-FQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAP 809
Cdd:pfam13779  603 SEMQQA-----MDELGDLlreQQQLLDETFRQLQqQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGA 670
PHA03247 PHA03247
large tegument protein UL36; Provisional
773-982 4.05e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  773 QASSPVMNTGGMNTGGLNASGMPMPQPgnqnPSSQAPMPNPSHPVSSPVMPPGAA---GNQMHCSSHV----QPMHRNSP 845
Cdd:PHA03247  2485 EARFPFAAGAAPDPGGGGPPDPDAPPA----PSRLAPAILPDEPVGEPVHPRMLTwirGLEELASDDAgdppPPLPPAAP 2560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  846 SPAPSRT-PTPHHTP-------------PGLTPQPT--QTPVQPILPTAAPISQAPLQhrESPTPPQVTPSLSIPTPVMS 909
Cdd:PHA03247  2561 PAAPDRSvPPPRPAPrpsepavtsrarrPDAPPQSArpRAPVDDRGDPRGPAPPSPLP--PDTHAPDPPPPSPSPAANEP 2638
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  910 TADQQIATPPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSP 982
Cdd:PHA03247  2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPA 2711
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1115-1180 4.82e-07

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: 50.12  E-value: 4.82e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689 1115 IPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLYNRKTSRVyKYCSKLAEVFEQ 1180
Cdd:cd05501     30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
718-887 5.29e-07

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: 55.43  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  718 MQMQSMGQRQQAPLQHPgqmgqtgpmnqmgfqarmQQPGTmQQTAQNQFLSQNQFQASSPVMNTGGMNTGGLNASGMPMP 797
Cdd:pfam09770  203 MRAQAKKPAQQPAPAPA------------------QPPAA-PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPV 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  798 QPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMhcsshvQPMH--RNSPSPAPSRTPTPHHTPPGLTPQPTQ--TPVQP 873
Cdd:pfam09770  264 TILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPV------QPTQilQNPNRLSAARVGYPQNPQPGVQPAPAHqaHRQQG 337
                          170
                   ....*....|....
gi 1785364689  874 ILPTAAPISQAPLQ 887
Cdd:pfam09770  338 SFGRQAPIITHPQQ 351
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1709-1746 1.83e-06

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: 46.68  E-value: 1.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1785364689 1709 CNECKHH--VETRWHCTVCEDYDLCITCYNTKTH--EHKMEK 1746
Cdd:cd02339      3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHdlEHRFYR 44
PHA02682 PHA02682
ORF080 virion core protein; Provisional
795-905 2.38e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 51.79  E-value: 2.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  795 PMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNqmhcsshvqpmhrnspSPAPSRTPTPHHTPPGLTPQPTQTPVQPI 874
Cdd:PHA02682    89 AAPAPACPACAPAAPAPAVTCPAPAPACPPATAPT----------------CPPPAVCPAPARPAPACPPSTRQCPPAPP 152
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1785364689  875 LPTAAPISQA-PLQHRESPTPPQVtPSLSIPT 905
Cdd:PHA02682   153 LPTPKPAPAAkPIFLHNQLPPPDY-PAASCPT 183
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
795-956 2.80e-06

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 468188 [Multi-domain]  Cd Length: 1552  Bit Score: 53.02  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  795 PMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPaPSRTPTphhtppglTPQPTQtPVQPI 874
Cdd:NF033804   854 PAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTP-PVKTPD--------QPEPSK-PEEPT 923
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  875 LPTAAPISQAPLQ--HRESPTPPQVTPSLSIPT-PVMSTADqqiatppsqqpsqqfssqqqPLPRPPSQPsltTPVATPT 951
Cdd:NF033804   924 YETEKPLEPAPVApsYENEPTPPVKTPDQPEPSkPVEPTYD--------------------PLPTPPVAP---TPKQLPT 980

                   ....*
gi 1785364689  952 APPLP 956
Cdd:NF033804   981 PPAVP 985
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
797-977 3.24e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.57  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  797 PQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQM----------HCSSHVQPMHRNSPSPAPSRTPTPHHTPPGLTPQP 866
Cdd:PRK12323   392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRspapealaaaRQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRP 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  867 TQTPVQPILPTAAPISQAplqhreSPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPRPPSQPSLTTP 946
Cdd:PRK12323   472 VAAAAAAAPARAAPAAAP------APADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAP 545
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1785364689  947 VATPtAPPLPMQLQPSTPPTANLDCPSSNPP 977
Cdd:PRK12323   546 AAAP-APRAAAATEPVVAPRPPRASASGLPD 575
PRK10263 PRK10263
DNA translocase FtsK; Provisional
809-983 3.27e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.78  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  809 PMPNpSHPVSSPVMPPGAAGNQMHC-SSHVQPMHRNSPSPAPSR-----------TPTPHHTPPGLTPQPTQTPVQPILP 876
Cdd:PRK10263   309 PLLN-GAPITEPVAVAAAATTATQSwAAPVEPVTQTPPVASVDVppaqptvawqpVPGPQTGEPVIAPAPEGYPQQSQYA 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  877 TAAPISQAPLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLP-RPPSQPSLTTPvaTPTAPPL 955
Cdd:PRK10263   388 QPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwQAEEQQSTFAP--QSTYQTE 465
                          170       180
                   ....*....|....*....|....*...
gi 1785364689  956 PMQLQPSTPPTANLDCPSSNPPSTNSPE 983
Cdd:PRK10263   466 QTYQQPAAQEPLYQQPQPVEQQPVVEPE 493
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1081-1138 5.12e-06

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: 47.44  E-value: 5.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 1081 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFEIVKTPMDLSTI-KRKLDTG 1138
Cdd:cd05494      3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
663-982 5.98e-06

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 51.93  E-value: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  663 PTQMNQNQGMAQpqtGLSTNGPLPDPNSMMRANVPNQimnrMQTQTGMNQFGQMGMQMQSMGQRQQaplQHPGQMGQTGP 742
Cdd:pfam09606  140 PSQMSRVGRMQP---GGQAGGMMQPSSGQPGSGTPNQ----MGPNGGPGQGQAGGMNGGQQGPMGG---QMPPQMGVPGM 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  743 MNQMGFQARM--QQPGTMQQTAQNQFLSQNQF-QASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQ--APMPNPSHPV 817
Cdd:pfam09606  210 PGPADAGAQMgqQAQANGGMNPQQMGGAPNQVaMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQggPGQPMGPPGQ 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  818 SSPVMPP--GAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQhrESPTPP 895
Cdd:pfam09606  290 QPGAMPNvmSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLG--ANPMQR 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  896 QVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQqplPRPPSQPSLTTPVATPTAPPlpmQLQPSTPPTANLDCPSSN 975
Cdd:pfam09606  368 GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPS---PQGPGSQPPQSHPGGMIPSP---ALIPSPSPQMSQQPAQQR 441

                   ....*..
gi 1785364689  976 PPSTNSP 982
Cdd:pfam09606  442 TIGQDSP 448
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1081-1182 1.46e-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: 45.84  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1081 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFEIVKTPMDLSTIKRKLDTGQYQEPWQYVEDIWLMFNNAWLY 1160
Cdd:cd05508      2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                           90       100
                   ....*....|....*....|..
gi 1785364689 1161 NRKTSRVYKYCSKLAEVFEQEI 1182
Cdd:cd05508     78 NGGDHKLTQAAKAIVKICEQEM 99
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
703-841 1.59e-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: 50.19  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  703 RMQTQTGMNQFgQMGMQMQSMGQRQQAPLQHPGQMGQTGPMN-----QMGFQARMQ---QPGTMQQTAQNQFLSQNQFQA 774
Cdd:TIGR01628  375 FMQLQPRMRQL-PMGSPMGGAMGQPPYYGQGPQQQFNGQPLGwprmsMMPTPMGPGgplRPNGLAPMNAVRAPSRNAQNA 453
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  775 SS--PVMNTGGMNTGGLNASGMPMPQPgNQNPSSQAPMPNPSHPVSSpvMPPG----AAGNQMHcsSHVQPMH 841
Cdd:TIGR01628  454 AQkpPMQPVMYPPNYQSLPLSQDLPQP-QSTASQGGQNKKLAQVLAS--ATPQmqkqVLGERLF--PLVEAIE 521
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
789-985 1.73e-05

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: 50.30  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  789 LNASGMPMPQPGNQNPSSQAPMPNPSHPVSS-------PVMPPGAAGNqmhcSSHVQPMhrnSPSPAP----SRTPTPHH 857
Cdd:pfam05109  434 LNTTGFAAPNTTTGLPSSTHVPTNLTAPASTgptvstaDVTSPTPAGT----TSGASPV---TPSPSPrdngTESKAPDM 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  858 TPPG---LTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPSLSIPTPVmstadqqiatppsqqpsqqfssqqqpl 934
Cdd:pfam05109  507 TSPTsavTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--------------------------- 559
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785364689  935 prppsqPSLTTPVATPTAPPLPmqlqpSTPPTANLDCPSSNPPSTNSPEVS 985
Cdd:pfam05109  560 ------PAVTTPTPNATIPTLG-----KTSPTSAVTTPTPNATSPTVGETS 599
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
786-986 2.03e-05

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: 50.30  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  786 TGGLNASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPpgaagnqmhcSSHVQPMHRNSPSPAPS-RTPTPHHTPPGL-T 863
Cdd:pfam05109  507 TSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSP----------TSAVTTPTPNATSPTPAvTTPTPNATIPTLgK 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  864 PQPTQTPVQPilptaAPISQAPLQHRESPTPPQVTPSL--SIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPRPPSQP 941
Cdd:pfam05109  577 TSPTSAVTTP-----TPNATSPTVGETSPQANTTNHTLggTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSI 651
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1785364689  942 SLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSPEVSS 986
Cdd:pfam05109  652 SETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVST 696
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
779-913 4.12e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 49.00  E-value: 4.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  779 MNTGGMNTGGLNASGMPMPQpgnqnpssQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPmhrnSPSPAPSRTPTPHHT 858
Cdd:PRK14971   357 IQLAQLTQKGDDASGGRGPK--------QHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAA----QPSAPQSATQPAGTP 424
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785364689  859 PPGLTPQPTQTPVQPilPTAAPISQAPLQHRES-PTPPQVTPSLSIPT--PVMSTADQ 913
Cdd:PRK14971   425 PTVSVDPPAAVPVNP--PSTAPQAVRPAQFKEEkKIPVSKVSSLGPSTlrPIQEKAEQ 480
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1870-2183 4.86e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.85  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1870 RMASMQRAGGVGP--QQGLPSPNSAGPATPTGQQPPTPQTPQPPPQPPTQQQPPPPNMPPYSMARAEPARGISQGKAAGQ 1947
Cdd:pfam09606  145 RVGRMQPGGQAGGmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQ 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1948 MTPPTPPQAGAMqqqvqGPPPAAVEMAMQIQRAAETQRQMAKAQIFPRPMMNPHQMQPMNPMQPMGMNPQQgprgQVHME 2027
Cdd:pfam09606  225 ANGGMNPQQMGG-----APNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ----PGAMP 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2028 SGIGPGMQQPQQQQQPPPTQPQPPWVQSGLPQSQSMQPGMQRSPIMSVPQQGQPMNMNPQSGIGQVPGASQTKQG---SL 2104
Cdd:pfam09606  296 NVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPgmmSS 375
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689 2105 PQAALQNLLRTLRSPSSPMQQQQVLNILHSNPqllaafiKQRAAKYASSQNAQAAGNVPGMPAQAGLQQVVHSNPGMQG 2183
Cdd:pfam09606  376 PSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-------GSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDS 447
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
797-899 6.02e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 48.27  E-value: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  797 PQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNqmhcsshvqpmhrNSPSPAPSRTPTPhhTPPGLTPQPTQTPVQPILP 876
Cdd:PRK14950   362 PVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAA-------------ANIPPKEPVRETA--TPPPVPPRPVAPPVPHTPE 426
                           90       100
                   ....*....|....*....|...
gi 1785364689  877 TAAPISQAPLQHRESPTPPQVTP 899
Cdd:PRK14950   427 SAPKLTRAAIPVDEKPKYTPPAP 449
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
2317-2456 7.22e-05

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: 48.49  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2317 QMSQMPQGMPGDTSSGLQTFPQRLLHQQMgspAQQNPMSPQQHmlPGPAQSPH-LQGQQLPPSLSNQvRSPQPVPSPRPQ 2395
Cdd:pfam09770  217 APAQPPAAPPAQQAQQQQQFPPQIQQQQQ---PQQQPQQPQQH--PGQGHPVTiLQRPQSPQPDPAQ-PSIQPQAQQFHQ 290
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689 2396 SQPPHSSPSPRMQPQP---SPHHVSPQTSSPHPGLVGPGQGNPMDQGHYGSPDP-TAMLSQMAGL 2456
Cdd:pfam09770  291 QPPPVPVQPTQILQNPnrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPiITHPQQLAQL 355
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
813-969 9.70e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.94  E-value: 9.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  813 PSHPVSSPVMPPGAAGNQMHCSSHVQPmhrnsPSPAPSRTPTPHHTPPglTPQPTQTPVQPILPTAAPISQAP---LQHR 889
Cdd:PRK07994   361 PAAPLPEPEVPPQSAAPAASAQATAAP-----TAAVAPPQAPAVPPPP--ASAPQQAPAVPLPETTSQLLAARqqlQRAQ 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  890 ESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPR-PPSQPSL--TTPVATPTAPPLPMQLQPSTPPT 966
Cdd:PRK07994   434 GATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRwKATNPVEvkKEPVATPKALKKALEHEKTPELA 513

                   ...
gi 1785364689  967 ANL 969
Cdd:PRK07994   514 AKL 516
PHA03247 PHA03247
large tegument protein UL36; Provisional
786-967 1.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  786 TGGLNASGMPMpqpgNQNPSSQAPMPNPSHPVSSPVMppGAAGNQMHCSSHVQPMhrnsPSPAPSRTPTPHHTPPgltPQ 865
Cdd:PHA03247  2852 LGGSVAPGGDV----RRRPPSRSPAAKPAAPARPPVR--RLARPAVSRSTESFAL----PPDQPERPPQPQAPPP---PQ 2918
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  866 PTQTPVQPILPTAAPISQAPLQHRESPTP---PQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLPRPPSQPS 942
Cdd:PHA03247  2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTdpaGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
                          170       180
                   ....*....|....*....|....*
gi 1785364689  943 LTTPVATPTAPPLPMQLQPSTPPTA 967
Cdd:PHA03247  2999 HSLSRVSSWASSLALHEETDPPPVS 3023
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
791-986 1.24e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  791 ASGMPMPQPGNQNPSSQAPMPNPSHPVSS-PVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPHHTPPG-------- 861
Cdd:PHA03307    98 ASPAREGSPTPPGPSSPDPPPPTPPPASPpPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSrqaalpls 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  862 LTPQPTQTPVQPI--LPTAAPisQAPLQHRESPTPPQVTPSLSIPTPV---------------MSTADQQIATPPSQQPS 924
Cdd:PHA03307   178 SPEETARAPSSPPaePPPSTP--PAAASPRPPRRSSPISASASSPAPApgrsaaddagasssdSSSSESSGCGWGPENEC 255
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785364689  925 QQFSSQQQPLPRPP---SQPSLTTPVATPTAPPLPMQLQPSTPPTANLDCPSSNPPSTNSPEVSS 986
Cdd:PHA03307   256 PLPRPAPITLPTRIweaSGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSS 320
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1959-2129 1.45e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 47.11  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1959 MQQQVQGPPPAAVEMAMQI-QRAAETQRQMAKAQIFPRPMMNPHQMQPMNPMQPM-GMNPQQGPRGQVHMeSGIGPGMQQ 2036
Cdd:TIGR01628  346 MHGRMLGGKPLYVALAQRKeQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYyGQGPQQQFNGQPLG-WPRMSMMPT 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2037 PQQQQQPPPTQPQPPWVQSGLPQSQSmQPGMQRSPIMSVPQQgqpmnmnPQSGIGQVPGASQTKQGSLPQAALQNLLRTL 2116
Cdd:TIGR01628  425 PMGPGGPLRPNGLAPMNAVRAPSRNA-QNAAQKPPMQPVMYP-------PNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
                          170
                   ....*....|...
gi 1785364689 2117 RSPSSPMQQQQVL 2129
Cdd:TIGR01628  497 LASATPQMQKQVL 509
PHA02682 PHA02682
ORF080 virion core protein; Provisional
807-986 1.90e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 46.01  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  807 QAPMPNPSHPVsspvmPPGAagnqmhcssHVQPMHRNSPSPAPSRTPTPHHTPPGLTPQPT-QTPVQPILPTAAPISQAP 885
Cdd:PHA02682    31 QATIPAPAAPC-----PPDA---------DVDPLDKYSVKEAGRYYQSRLKANSACMQRPSgQSPLAPSPACAAPAPACP 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  886 lqhreSPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSQQQPLP----RPPSQPSLTTPVATPTAPPLpmQLQP 961
Cdd:PHA02682    97 -----ACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPpstrQCPPAPPLPTPKPAPAAKPI--FLHN 169
                          170       180
                   ....*....|....*....|....*
gi 1785364689  962 STPPTanlDCPSSNPPSTNSPEVSS 986
Cdd:PHA02682   170 QLPPP---DYPAASCPTIETAPAAS 191
PHA03378 PHA03378
EBNA-3B; Provisional
786-965 1.92e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  786 TGGLNASGMPMPQPGNQNPSSQAPMPNPshpvsspvmPPGAAgnqmhcsshvqPMHRNSPSPAPSRTPTPHHTPPGLTPq 865
Cdd:PHA03378   678 PTGANTMLPIQWAPGTMQPPPRAPTPMR---------PPAAP-----------PGRAQRPAAATGRARPPAAAPGRARP- 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  866 PTQTPVQPILPTAAPISQAPLQHRESPT-PPQVTPSLSIPTP---VMSTADQQiatppsqqpsqqfsSQQQPLPRPPsqp 941
Cdd:PHA03378   737 PAAAPGRARPPAAAPGRARPPAAAPGRArPPAAAPGAPTPQPppqAPPAPQQR--------------PRGAPTPQPP--- 799
                          170       180
                   ....*....|....*....|....
gi 1785364689  942 slttpvatPTAPPLPMQLQPSTPP 965
Cdd:PHA03378   800 --------PQAGPTSMQLMPRAAP 815
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
791-952 2.44e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.38  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  791 ASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTP 870
Cdd:PRK07003   392 GASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPP 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  871 VQPIlPTAAPISQAPLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQqpsqqfssqqqplPRPPSQPSLTTPVATP 950
Cdd:PRK07003   472 ADSG-SASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA-------------PAAAAPPAPEARPPTP 537

                   ..
gi 1785364689  951 TA 952
Cdd:PRK07003   538 AA 539
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
609-831 2.49e-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: 46.54  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  609 ARKVEGDMYESANSRAEYYHFLAEKIYKIQkelEEKRRTRLQKQhliptppgmpPTQMNQNQGMAQPQTGLstngplPDP 688
Cdd:pfam09606   22 AREMENHVFAKARTKDEYLGTVARLILHVR---DMSKKAAQQQQ----------PQGGQGNGGMGGGQQGM------PDP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  689 NSMMRANVPNQIMNRMQTQTGMNQFGQMGMQMQSMGQrqQAPLQHPGQMGQTgPMNQMGFQARMQQPGTMQQTAQNQFLS 768
Cdd:pfam09606   83 INALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGT--ASNLLASLGRPQM-PMGGAGFPSQMSRVGRMQPGGQAGGMM 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364689  769 QNQFQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQM 831
Cdd:pfam09606  160 QPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQ 222
TALPID3 pfam15324
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ...
792-981 3.04e-04

Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.


Pssm-ID: 434634 [Multi-domain]  Cd Length: 1288  Bit Score: 46.42  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  792 SGMpMPQPGNQNPSSQAPMPNPSHPVSSP-VMPPGAAGNQMHCSSHV-------------------------QPMHRNSP 845
Cdd:pfam15324  890 SGM-FPQQAQADPDASVSESEPSEPSTSDiVEAAGGGGLQLFVDAGVpvdsemirhfvnealaetiaimlgdREAQREPP 968
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  846 SPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQhresptppqvTPSLSiptPVMSTADQQiatppsqqpSQ 925
Cdd:pfam15324  969 VAASVPGDLPTKETLLPTPVPTPQPTPPCSPPSPLKEPSPVK----------TPDSS---PCVSEHDFF---------PV 1026
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364689  926 QFSSQQQPLPRPPSQPSLTTPVATPTA-PPLPMQLQPSTPPTANLDCPSSNPPSTNS 981
Cdd:pfam15324 1027 KEIPPEKGADTGPAVSLVITPTVTPIAtPPPAATPTPPLSENSIDKLKSPSPELPKP 1083
PRK10263 PRK10263
DNA translocase FtsK; Provisional
795-986 3.30e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  795 PMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGA--AGNQMHCSSHVQPMHRNSPSPA---PSRTPTPHHTPPGLT--PQPT 867
Cdd:PRK10263   382 QQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEqpAQQPYYAPAPEQPAQQPYYAPApeqPVAGNAWQAEEQQSTfaPQST 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  868 QTPVQPILptaAPISQAPLQHRESPTPPQVTPSlsiPTPVMStadqqiATPPSQQPSQQFSSQQQPLPRPPSQ-PSLTTP 946
Cdd:PRK10263   462 YQTEQTYQ---QPAAQEPLYQQPQPVEQQPVVE---PEPVVE------ETKPARPPLYYFEEVEEKRAREREQlAAWYQP 529
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1785364689  947 VATPTAPPLPmqLQPSTPPTAnldcPSSNPPSTNSPEVSS 986
Cdd:PRK10263   530 IPEPVKEPEP--IKSSLKAPS----VAAVPPVEAAAAVSP 563
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1947-2444 3.38e-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: 46.15  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1947 QMTPPTPPQAGAMQQQVQGPPpaaVEMAMQIQRAAETQRQMAKAQiFPRPMMNPHQMQPMNPMQPM--GMNPQQGPRGQV 2024
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGP---GTASNLLASLGRPQMPMGGAG-FPSQMSRVGRMQPGGQAGGMmqPSSGQPGSGTPN 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2025 HMESGIGPGMQqpqqqqqppptqpqppwvQSGLPQSQSMQPGMQRSPimsvPQQGQPMNMNPQSGIGQVPGASQTKQGSL 2104
Cdd:pfam09606  173 QMGPNGGPGQG------------------QAGGMNGGQQGPMGGQMP----PQMGVPGMPGPADAGAQMGQQAQANGGMN 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2105 PQAALQNllrtlrSPSSPMQQQQvlnilhsnpqllaafikqrAAKYASSQNAQAAGNVPGMPAQAGLQQVVHSNPGmqgm 2184
Cdd:pfam09606  231 PQQMGGA------PNQVAMQQQQ-------------------PQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPG---- 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2185 NPMQAIGPRPGMPQqpqapqqqppqqsplpqqamAGINPQGQPLNINPGGispqfreiilrrqqimqqqqqQQQQQQQQq 2264
Cdd:pfam09606  282 QPMGPPGQQPGAMP--------------------NVMSIGDQNNYQQQQT---------------------RQQQQQQG- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2265 qqqqqqqqqgagpgmVNHNQFQQHQVMsgytqqqqqqqrfqhhIQMQQGsmGQMSQMPQGMPGDTSsglqtFPQRLLHQQ 2344
Cdd:pfam09606  320 ---------------GNHPAAHQQQMN----------------QSVGQG--GQVVALGGLNHLETW-----NPGNFGGLG 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2345 MGSPAQQNP-MSPQQHMLPGPAQSPHLQGQQLPPSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSP 2423
Cdd:pfam09606  362 ANPMQRGQPgMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQR 441
                          490       500
                   ....*....|....*....|..
gi 1785364689 2424 HPGLVGPGQG-NPMDQGHYGSP 2444
Cdd:pfam09606  442 TIGQDSPGGSlNTPGQSAVNSP 463
PHA03247 PHA03247
large tegument protein UL36; Provisional
787-982 3.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  787 GGLNASGMPMPQPGnqnpssQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSR--------------- 851
Cdd:PHA03247   264 GADRAPETARGATG------PPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGdaeeeddedgamevv 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  852 TPTPHHT---PPGLTPQ--PTQTPvqpilPTAAPISQAPLQHRESPTPPqvtpslsiptpvmsTADQQIATPPSQQPSQQ 926
Cdd:PHA03247   338 SPLPRPRqhyPLGFPKRrrPTWTP-----PSSLEDLSAGRHHPKRASLP--------------TRKRRSARHAATPFARG 398
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689  927 FSSQQQPLPRPPSQPSLTTPVATPTAPPLPmqLQPSTPPtanldcPSSNPPSTNSP 982
Cdd:PHA03247   399 PGGDDQTRPAAPVPASVPTPAPTPVPASAP--PPPATPL------PSAEPGSDDGP 446
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1708-1744 3.67e-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: 40.27  E-value: 3.67e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1785364689 1708 TCNECK--HHVETRWHCTVCEDYDLCITCY----NTKTHE--HKM 1744
Cdd:cd02345      2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNslHIM 46
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1707-1735 3.89e-04

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


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 40.35  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1785364689 1707 YTCNECKHHV--ETRWHCTVCEDYDLCITCY 1735
Cdd:cd02335      1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1707-1746 4.15e-04

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 40.11  E-value: 4.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1785364689 1707 YTCNECKHH--VETRWHCTVC--EDYDLCITC-YNTKTHE--HKMEK 1746
Cdd:cd02341      1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHQedHWLVK 47
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
2303-2413 4.27e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2303 RFQHHIQMQQGSMGQMSQMPQGMPGDTSSGLQTFPQRLLHQQMGS-----PAQQNPMSPQQHMLPGPAQSPHLQGQQLPP 2377
Cdd:TIGR01628  367 RRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGqplgwPRMSMMPTPMGPGGPLRPNGLAPMNAVRAP 446
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1785364689 2378 SLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSP 2413
Cdd:TIGR01628  447 SRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
838-966 7.32e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.47  E-value: 7.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689   838 QPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPslsiptPVMSTADQQIAT 917
Cdd:smart00818   37 HQIIPVSQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQ------PFQPQPLQPPQP 110
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1785364689   918 PPSQQPSQQFSSQQQPLPRPPSQPSLTTPVATPTAPPLPMQLQPSTPPT 966
Cdd:smart00818  111 QQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATDKT 159
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1917-2147 1.01e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 44.64  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1917 QQQPPPPNMPPYSMARAEPAR----------------------GISQGKAAgqmTPPTPPQAGAMQQQVQGPPPAA---- 1970
Cdd:pfam09770  121 SSLPQYQYASQQSQQPSKPVRtgyekykepepipdlqvdaslwGVAPKKAA---APAPAPQPAAQPASLPAPSRKMmsle 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 1971 -VEMAMQIQRAAETQRQMAKAQIFPrpmmnphQMQPMNPMQPMGMNPQQGPRGQVHMESGIGPGMQQPQQQQQPPPTQPQ 2049
Cdd:pfam09770  198 eVEAAMRAQAKKPAQQPAPAPAQPP-------AAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQ 270
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689 2050 PPWVQSGLPQSQSMQPGMQRSPimsVPQQGQPMNM--NPQSGIGQVPGASQTKQGSLPQAALQNLLRTLRSPSSPMQ--- 2124
Cdd:pfam09770  271 SPQPDPAQPSIQPQAQQFHQQP---PPVPVQPTQIlqNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPiit 347
                          250       260
                   ....*....|....*....|....
gi 1785364689 2125 -QQQVLNIlhsNPQLLAAFIKQRA 2147
Cdd:pfam09770  348 hPQQLAQL---SEEEKAAYLDEEA 368
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
783-912 1.21e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  783 GMNTGGlnASGMPMPQPGNQNPSSQAPMPNPSHP-VSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPSRTPTPHHTPPG 861
Cdd:PRK07764   384 RLGVAG--GAGAPAAAAPSAAAAAPAAAPAPAAAaPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785364689  862 LTPQPTQTPVQPILPTAAPiSQAPLQHRESPTPPQVTPSLSIPTPVMSTAD 912
Cdd:PRK07764   462 PSAQPAPAPAAAPEPTAAP-APAPPAAPAPAAAPAAPAAPAAPAGADDAAT 511
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1708-1745 1.87e-03

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 38.10  E-value: 1.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1785364689 1708 TCNECKHHVET--RWHCTVCEDYDLCITCYNTK--THEHKME 1745
Cdd:cd02338      2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGvtTERHLFD 43
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
823-972 2.33e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  823 PPGAAGNQMhcSSHVQPMHRNS-PSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPSL 901
Cdd:PRK14951   366 PAAAAEAAA--PAEKKTPARPEaAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785364689  902 SIPTPVMSTADQQiatppsqqpsqqfssqqqplPRPPSQPSLTTP-VATPTAPPLPMQLQPSTPPTANLDCP 972
Cdd:PRK14951   444 AVALAPAPPAQAA--------------------PETVAIPVRVAPePAVASAAPAPAAAPAAARLTPTEEGD 495
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
655-824 2.63e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.10  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  655 IPTPPGMPPTQMNQNQGMAQPQTGLStngpLPDPNSMMRANVPN---QIMNRMQTQTGMNQ--FGQMGMQMQSMGQRQQA 729
Cdd:pfam09770  170 AAAPAPAPQPAAQPASLPAPSRKMMS----LEEVEAAMRAQAKKpaqQPAPAPAQPPAAPPaqQAQQQQQFPPQIQQQQQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  730 PLQHPGQMGQ-TGPMNQMGFQARMQQPGTMQQTAQNQFLSQNQFQASSPVMNTGGM---NTGGLNASGMPMPQPGNQNPS 805
Cdd:pfam09770  246 PQQQPQQPQQhPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQilqNPNRLSAARVGYPQNPQPGVQ 325
                          170
                   ....*....|....*....
gi 1785364689  806 SQAPMPNPSHPVSSPVMPP 824
Cdd:pfam09770  326 PAPAHQAHRQQGSFGRQAP 344
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
771-906 3.56e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.55  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  771 QFQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHRNSPSPAPS 850
Cdd:PRK07994   362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKS 441
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364689  851 RTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPSLSIPTP 906
Cdd:PRK07994   442 EPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATP 497
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
804-965 3.94e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.72  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  804 PSSQAPMPNPSHPVSSPVMPPGAAGNQMHCSSHVQPMHR-NSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPIS 882
Cdd:pfam09770  166 APKKAAAPAPAPQPAAQPASLPAPSRKMMSLEEVEAAMRaQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  883 QAPLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPSQQPSQQFSSqqqplPRPPSQPS--LTTPVATPTAP-PLPMQL 959
Cdd:pfam09770  246 PQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQP-----PPVPVQPTqiLQNPNRLSAARvGYPQNP 320

                   ....*.
gi 1785364689  960 QPSTPP 965
Cdd:pfam09770  321 QPGVQP 326
PHA03378 PHA03378
EBNA-3B; Provisional
681-982 4.47e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  681 TNGPLPDPNSmmraNVPNQIMNRMQTQTGMNQFGQMGMQMQSMGQRqqaPLQHPgqmgQTGPMNQMGFQAR-MQQPGTMQ 759
Cdd:PHA03378   438 TEQPRATPHS----QAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQ---PLPHP----QVTPVILHQPPAQgVQAHGSML 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  760 QtaqnqFLSQNQFQASSPVMNTggmntggLNASGMPMPQPGNQNPSS-------QAPMPNPSHPVSSPVMPPGAAGnqmh 832
Cdd:PHA03378   507 D-----LLEKDDEDMEQRVMAT-------LLPPSPPQPRAGRRAPCVytedldiESDEPASTEPVHDQLLPAPGLG---- 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  833 cSSHVQPMhrNSPSPAPSRTPTPHHT-PPGLTPQPTQTPVQPILPTAAPISQAPLQH----RESPTPPQVTPSLSIPTPV 907
Cdd:PHA03378   571 -PLQIQPL--TSPTTSQLASSAPSYAqTPWPVPHPSQTPEPPTTQSHIPETSAPRQWpmplRPIPMRPLRMQPITFNVLV 647
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364689  908 MSTADQqiatpPSQQPSQQFSSQQQPLPRPPSQPSLTTPVAT--PTAPPLPMQLQPSTPPTANldcPSSNPPSTNSP 982
Cdd:PHA03378   648 FPTPHQ-----PPQVEITPYKPTWTQIGHIPYQPSPTGANTMlpIQWAPGTMQPPPRAPTPMR---PPAAPPGRAQR 716
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
760-889 4.92e-03

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  760 QTAQNQFlsqNQFQASSPVMNTGGMNTGGLNASGMPMPQPGNQNPS------SQAPMPNPSHPVSS--PVMPPGAAGNQM 831
Cdd:TIGR01628  369 AHLQDQF---MQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGqplgwpRMSMMPTPMGPGGPlrPNGLAPMNAVRA 445
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  832 HCSSHVQPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQ--PILPTAAPISQAPLQHR 889
Cdd:TIGR01628  446 PSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQggQNKKLAQVLASATPQMQ 505
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
805-905 5.45e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.18  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  805 SSQAPMPNPSHPVSSPVMPPGAAGnqmhcsshvQPMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQA 884
Cdd:PRK12270    34 ADYGPGSTAAPTAAAAAAAAAASA---------PAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAA 104
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1785364689  885 PLQHRESPTPPQVTP--------------SLSIPT 905
Cdd:PRK12270   105 AAAPAAAAVEDEVTPlrgaaaavaknmdaSLEVPT 139
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1708-1743 5.64e-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: 36.79  E-value: 5.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1785364689 1708 TCNECKHH--VETRWHCTVCEDYDLCITCYNTKTHEHK 1743
Cdd:cd02344      2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKHNTR 39
PHA03247 PHA03247
large tegument protein UL36; Provisional
839-982 6.94e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  839 PMHRNSPSPAPSRTPTPHHTPPGLTPQPTQTPVQPILPTAAPISQAPLQHresPTPPQV-----------------TPSL 901
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGE---PVHPRMltwirgleelasddagdPPPP 2554
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  902 SIPTPVMSTADQQIATppsqqpsqqfssqqqplPRP---PSQPSLTTPVATPTAPPlpmqlQPSTP--PTANLDCPSSNP 976
Cdd:PHA03247  2555 LPPAAPPAAPDRSVPP-----------------PRPaprPSEPAVTSRARRPDAPP-----QSARPraPVDDRGDPRGPA 2612

                   ....*.
gi 1785364689  977 PSTNSP 982
Cdd:PHA03247  2613 PPSPLP 2618
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
837-913 8.46e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  837 VQPMHRNSPSPAPSR-TPTPHHTPPGLTPQPT-QTPVQPILPTAAPISQAPLQHRESPTPPQV--TPSLSIPTPVMSTAD 912
Cdd:PRK14950   366 PQPAKPTAAAPSPVRpTPAPSTRPKAAAAANIpPKEPVRETATPPPVPPRPVAPPVPHTPESApkLTRAAIPVDEKPKYT 445

                   .
gi 1785364689  913 Q 913
Cdd:PRK14950   446 P 446
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
775-986 9.01e-03

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: 41.44  E-value: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  775 SSPVMNTGGMNTgglnasgmpmpqpgnqnPSSQAPMPNPSHpVSSPVMPPGAAGNQMhcsshvqpmhrnspSPAPSRTPT 854
Cdd:pfam05109  430 TSPTLNTTGFAA-----------------PNTTTGLPSSTH-VPTNLTAPASTGPTV--------------STADVTSPT 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364689  855 PHHTPPGLTP-QPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPSLSIPTPVMSTADQQIATPPsqqpsqqfssqqqp 933
Cdd:pfam05109  478 PAGTTSGASPvTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTS-------------- 543
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689  934 lprPPSQPSLTTPVATPTAPPLpmqlqpsTPPTANLDCPS---SNPPS---TNSPEVSS 986
Cdd:pfam05109  544 ---PTSAVTTPTPNATSPTPAV-------TTPTPNATIPTlgkTSPTSavtTPTPNATS 592
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
838-906 9.97e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 41.10  E-value: 9.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364689  838 QPMHRNSPSPAPSRTPTPHHTPPglTPQPTQTPVQPILPTAAPISQAPLQHRESPTPPQVTPSLSIPTP 906
Cdd:PRK14948   517 ASNTAKTPPPPQKSPPPPAPTPP--LPQPTATAPPPTPPPPPPTATQASSNAPAQIPADSSPPPPIPEE 583
 
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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