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Conserved domains on  [gi|528516427|ref|XP_005161826|]
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CREB-binding protein isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAT_KAT11 super family cl02120
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1235-1542 7.82e-92

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


The actual alignment was detected with superfamily member pfam08214:

Pssm-ID: 413203  Cd Length: 348  Bit Score: 302.78  E-value: 7.82e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1235 VNKYLKRQNhPEAGEVFVRVVASSDKTVEVKPGMKAKFVDTGEmmEAFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1314
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1315 PFPNTRRVYISYLDSIHFFKPRmLRTAVYHEILIGYLEYVKKLGYVTAHIWACPPSEGDDYIFhchPADQKIPK-----P 1389
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1390 KRLQEWYRKMLDKAFAE-------RILHDYKDIFKQ-----ATEDRL-------------TSANELPYFEGDFWPNVLEE 1444
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1445 SIKELEQEEE--------------------------ERKKEENTAACETPEGTPGdsknakkKNNKKTNKNKSSLSRANK 1498
Cdd:pfam08214  234 LIKEGRWKSVsldqfweelrfrqefslgrlvgfiglEGDYTPGSDDVINPPGLVK-------SKKQYKMIKSYITGREYS 306
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528516427  1499 KKPGMPNVANDLSQKLYATMEKHkevFFVIHLHSGPIVNSLLPI 1542
Cdd:pfam08214  307 TEEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
980-1087 4.48e-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: 247.36  E-value: 4.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  980 PEELRQALMPTLESLYRQDPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1059
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 528516427 1060 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1087
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.92e-47

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


:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 164.59  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   548 GVRKAWHEHVTQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRDEYYHFLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 528516427   628 E 628
Cdd:pfam02172   81 E 81
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1099-1171 8.53e-33

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


:

Pssm-ID: 276805  Cd Length: 73  Bit Score: 122.40  E-value: 8.53e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427 1099 FSPQTLCCYGKqlCTIPRDGT--YYSYQ---NRYHFCEKCFNEIQGDSVTLGDDpaqPQTMISKDQFERKKNDTLDPE 1171
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKRNavYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
325-392 9.01e-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: 107.86  E-value: 9.01e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427   325 HAHKCQRREQAngdvrACALPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 392
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1925-2043 3.78e-27

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: 107.61  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1925 MQPMPQGQWPGgaqpsmpaaqqqvaqqtPQGPQSTLPIQRPAMPQQVA-QPRMMVPTQGPR-----PQAPQRAAGIAPNA 1998
Cdd:pfam09030    1 QPQWAQGQWQQ-----------------QQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGlpqvpGQQPGRPGSIAPNA 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 528516427  1999 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYHAS 2043
Cdd:pfam09030   64 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYQAS 108
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1598-1638 7.83e-27

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


:

Pssm-ID: 239077  Cd Length: 41  Bit Score: 104.18  E-value: 7.83e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528516427 1598 YTCNECKHHVETRWHCTVCEDFDLCINCYNAKGHEHQMVKW 1638
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 ...
1665-1733 9.94e-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: 9.94e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528516427  1665 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1733
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1172-1206 2.15e-19

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: 83.11  E-value: 2.15e-19
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528516427 1172 PFVECKDCGRKMHQICVLHYEVIWPSGFICDNCLK 1206
Cdd:cd15647     6 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
714-903 1.72e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   714 HQQINMNQVPTMN-MSPTRIAPTQGmlgahggnmvtqTPNQTQFMTQPPFPATTnTMNVNMGQPNSQTPVSQQQPNANLP 792
Cdd:pfam03154  163 QQQILQTQPPVLQaQSGAASPPSPP------------PPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQTQSTAAPHT 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   793 LNALGPL--GPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTqaelPIPGQQHPGTP-TG 869
Cdd:pfam03154  230 LIQQTPTlhPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQH----PVPPQPFPLTPqSS 305
                          170       180       190
                   ....*....|....*....|....*....|....
gi 528516427   870 ENRVPTPASAASTelHSQHAVPDVPPNDTKTEEQ 903
Cdd:pfam03154  306 QSQVPPGPSPAAP--GQSQQRIHTPPSQSQLQSQ 337
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1768-1988 2.12e-04

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1768 RAMPQSLPSPPASTAPSTPTSHQQ-----PNTPQTPQPLPNQPTTPNAVVMS-------PTYPNTPRNGQPLPQASQGKP 1835
Cdd:pfam03154  142 RSTSPSIPSPQDNESDSDSSAQQQilqtqPPVLQAQSGAASPPSPPPPGTTQaatagptPSAPSVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1836 GPQASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAvkmarhiEMVAQAQQNYRMTMNGLPMNHQQPRMPGAMQPPmq 1915
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPS-------QVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHP-- 292
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427  1916 lVGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTP---QGPQSTLPIQRPAMPQQVAQPRMMVPTQGPRPQAP 1988
Cdd:pfam03154  293 -VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPsqsQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLP 367
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
81-301 5.43e-04

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427    81 LSELLRPGSSAGMNSVSPQPGGIGPQLGGLGKSPLGQGSPSHPSQTQKPGGTPGTQGNNAGSAGMGFNQGMlnsGMMGQN 160
Cdd:pfam09606  124 LASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQG---PMGGQM 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   161 AGAQGGQVINGALgtvgrgrgvQGMYQGAAMQVASSVGAGGGVGAAAPGGAGSVLAETLTQGAQQMGINAQQAkMGMAGG 240
Cdd:pfam09606  201 PPQMGVPGMPGPA---------DAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQM-QQMPQG 270
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427   241 NSPFGQYQAGGQQLGTNAQNKGALPNSLPPFPTDLKGATVTSVP------NMPQQQQVSVGMVAGQG 301
Cdd:pfam09606  271 VGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQqqqqggNHPAAHQQQMNQSVGQG 337
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1892-2333 2.46e-03

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: 43.07  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1892 MTMNGLPMNHQQPRMpGAMQPPMQLVGPRGQQVMQPMPQGQwpggAQPSMPAAQQQVAQQTPQGPQSTLPIQRpaMPQQV 1971
Cdd:pfam09606  132 MPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP----NQMGPNGGPGQGQAGGMNGGQQGPMGGQ--MPPQM 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1972 AQPRMMVPTQgPRPQAPQRAAGIAPnalqdllrtlkspsspqqqqqvlnilkSNPQLMAAFIKQRtakyhasqpqqqqpq 2051
Cdd:pfam09606  205 GVPGMPGPAD-AGAQMGQQAQANGG---------------------------MNPQQMGGAPNQV--------------- 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2052 qgIHAAQPAMQNMAAMQAVPRPGMAPQQQQQQPTPQGMAALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQG 2131
Cdd:pfam09606  242 --AMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2132 GMPQAHGQfpqaqgtatnytqlrmQQQQLAMqgtgGPMGQLPPMAQMAMDGTPNllhQRNnlllqqQQLPQQQVVLKPPM 2211
Cdd:pfam09606  320 GNHPAAHQ----------------QQMNQSV----GQGGQVVALGGLNHLETWN---PGN------FGGLGANPMQRGQP 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2212 GSQAQPSPMSPQTHLLSGQPQGAHLPGQPmanalsnQVCSPGPVQSPRPPSQQPpphsspsphvQPQPSPQHVPSHtgSP 2291
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQP-------SVPSPQGPGSQPPQSHPG----------GMIPSPALIPSP--SP 431
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 528516427  2292 HPGLTTPMPGSMDQGHLGTPeqsamlpqLNTPNRGGLPSDLN 2333
Cdd:pfam09606  432 QMSQQPAQQRTIGQDSPGGS--------LNTPGQSAVNSPLN 465
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1235-1542 7.82e-92

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: 302.78  E-value: 7.82e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1235 VNKYLKRQNhPEAGEVFVRVVASSDKTVEVKPGMKAKFVDTGEmmEAFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1314
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1315 PFPNTRRVYISYLDSIHFFKPRmLRTAVYHEILIGYLEYVKKLGYVTAHIWACPPSEGDDYIFhchPADQKIPK-----P 1389
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1390 KRLQEWYRKMLDKAFAE-------RILHDYKDIFKQ-----ATEDRL-------------TSANELPYFEGDFWPNVLEE 1444
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1445 SIKELEQEEE--------------------------ERKKEENTAACETPEGTPGdsknakkKNNKKTNKNKSSLSRANK 1498
Cdd:pfam08214  234 LIKEGRWKSVsldqfweelrfrqefslgrlvgfiglEGDYTPGSDDVINPPGLVK-------SKKQYKMIKSYITGREYS 306
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528516427  1499 KKPGMPNVANDLSQKLYATMEKHkevFFVIHLHSGPIVNSLLPI 1542
Cdd:pfam08214  307 TEEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
980-1087 4.48e-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: 247.36  E-value: 4.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  980 PEELRQALMPTLESLYRQDPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1059
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 528516427 1060 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1087
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.92e-47

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 164.59  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   548 GVRKAWHEHVTQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRDEYYHFLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 528516427   628 E 628
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
977-1085 4.35e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.39  E-value: 4.35e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427    977 IFKPEELRQALMPTLESLYRQDPESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1056
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 528516427   1057 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1085
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1099-1171 8.53e-33

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


Pssm-ID: 276805  Cd Length: 73  Bit Score: 122.40  E-value: 8.53e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427 1099 FSPQTLCCYGKqlCTIPRDGT--YYSYQ---NRYHFCEKCFNEIQGDSVTLGDDpaqPQTMISKDQFERKKNDTLDPE 1171
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKRNavYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
325-392 9.01e-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: 107.86  E-value: 9.01e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427   325 HAHKCQRREQAngdvrACALPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 392
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1925-2043 3.78e-27

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: 107.61  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1925 MQPMPQGQWPGgaqpsmpaaqqqvaqqtPQGPQSTLPIQRPAMPQQVA-QPRMMVPTQGPR-----PQAPQRAAGIAPNA 1998
Cdd:pfam09030    1 QPQWAQGQWQQ-----------------QQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGlpqvpGQQPGRPGSIAPNA 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 528516427  1999 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYHAS 2043
Cdd:pfam09030   64 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYQAS 108
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1598-1638 7.83e-27

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


Pssm-ID: 239077  Cd Length: 41  Bit Score: 104.18  E-value: 7.83e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528516427 1598 YTCNECKHHVETRWHCTVCEDFDLCINCYNAKGHEHQMVKW 1638
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 ...
1665-1733 9.94e-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: 9.94e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528516427  1665 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1733
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1659-1737 2.52e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.51  E-value: 2.52e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   1659 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1734
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 528516427   1735 FCL 1737
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1085-1124 1.40e-22

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: 92.38  E-value: 1.40e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 528516427  1085 VMQGLGYCCGRKYEFSPQTLCCYGKQLCTIPRDGTYYSYQ 1124
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
325-395 9.07e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 88.19  E-value: 9.07e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427    325 HAHKCQRREQAngdvraCALPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 395
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1172-1206 2.15e-19

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: 83.11  E-value: 2.15e-19
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528516427 1172 PFVECKDCGRKMHQICVLHYEVIWPSGFICDNCLK 1206
Cdd:cd15647     6 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
997-1073 2.48e-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: 2.48e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427   997 QDPESLPFRQPVDPilLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSK 1073
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
903-1086 2.53e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 83.32  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  903 QDYDMaVKTEPSTETEEDTGSLLVKKEEQEGSEAKQEPMEtedkktdlKTETKEEDESKTNGTASSSPSQSRrKIFKPEE 982
Cdd:COG5076    78 DDLEN-VGGITYSPFEKNRPESLRFDEIVFLAIESVTPES--------GLGSLLMAHLKTSVKKRKTPKIED-ELLYADN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  983 LRQALMPTLESLYRQDPESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1062
Cdd:COG5076   148 KAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNG 225
                         170       180
                  ....*....|....*....|....
gi 528516427 1063 KTSRVYKYCSKLAEVFEQEIDPVM 1086
Cdd:COG5076   226 PDSSVYVDAKELEKYFLKLIEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1594-1636 2.92e-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: 74.40  E-value: 2.92e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 528516427   1594 DRFVYTCNEC-KHHVETRWHCTVCEDFDLCINCYNAKGHEHQMV 1636
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1594-1635 7.38e-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: 70.20  E-value: 7.38e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 528516427  1594 DRFVYTCNECKH--HVETRWHCTVCEDFDLCINCYNA-KGHEHQM 1635
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
1998-2040 1.94e-09

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 54.97  E-value: 1.94e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528516427 1998 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2040
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
714-903 1.72e-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: 60.17  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   714 HQQINMNQVPTMN-MSPTRIAPTQGmlgahggnmvtqTPNQTQFMTQPPFPATTnTMNVNMGQPNSQTPVSQQQPNANLP 792
Cdd:pfam03154  163 QQQILQTQPPVLQaQSGAASPPSPP------------PPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQTQSTAAPHT 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   793 LNALGPL--GPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTqaelPIPGQQHPGTP-TG 869
Cdd:pfam03154  230 LIQQTPTlhPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQH----PVPPQPFPLTPqSS 305
                          170       180       190
                   ....*....|....*....|....*....|....
gi 528516427   870 ENRVPTPASAASTelHSQHAVPDVPPNDTKTEEQ 903
Cdd:pfam03154  306 QSQVPPGPSPAAP--GQSQQRIHTPPSQSQLQSQ 337
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1875-2001 1.85e-06

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: 53.27  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1875 KMARHIEMVAQAQQNyRMTMNGLPMNHQqprMPGAM-QPPMQLVGPrgQQVMQPMPQGqWPGGAQpsMPaaqqqvaqqTP 1953
Cdd:TIGR01628  364 KEQRRAHLQDQFMQL-QPRMRQLPMGSP---MGGAMgQPPYYGQGP--QQQFNGQPLG-WPRMSM--MP---------TP 425
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528516427  1954 QGPQSTL-PIQRPAMPQQVAQPRMMVPTQGPRPQAPQRAagiAPNALQD 2001
Cdd:TIGR01628  426 MGPGGPLrPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMY---PPNYQSL 471
PHA03247 PHA03247
large tegument protein UL36; Provisional
758-895 7.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  758 TQPPFPATTNTmnvnmgqPNSQT----PVSQQQPNANLPLNA-LGPLGPALGCPTPPQAPLRATPPPNAtAASTTNLPAA 832
Cdd:PHA03247 2755 ARPARPPTTAG-------PPAPAppaaPAAGPPRRLTRPAVAsLSESRESLPSPWDPADPPAAVLAPAA-ALPPAASPAG 2826
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427  833 LQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTgeNRVPTPASAASTELHSQH------AVPDVPP 895
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV--RRRPPSRSPAAKPAAPARppvrrlARPAVSR 2893
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1768-1988 2.12e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1768 RAMPQSLPSPPASTAPSTPTSHQQ-----PNTPQTPQPLPNQPTTPNAVVMS-------PTYPNTPRNGQPLPQASQGKP 1835
Cdd:pfam03154  142 RSTSPSIPSPQDNESDSDSSAQQQilqtqPPVLQAQSGAASPPSPPPPGTTQaatagptPSAPSVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1836 GPQASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAvkmarhiEMVAQAQQNYRMTMNGLPMNHQQPRMPGAMQPPmq 1915
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPS-------QVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHP-- 292
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427  1916 lVGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTP---QGPQSTLPIQRPAMPQQVAQPRMMVPTQGPRPQAP 1988
Cdd:pfam03154  293 -VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPsqsQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLP 367
PHA03247 PHA03247
large tegument protein UL36; Provisional
1771-1841 3.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427 1771 PQSLPSPPASTAPSTPTSHQQPNTPQTPQPLPNQPTTPNAVVMSPTYPNTPRNGQPLPQASQGKPGPQASP 1841
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP 2975
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
676-854 5.19e-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: 45.18  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   676 NQILNRMQVSQGMNPFSAMsnvpMSQAPMGTRaaspinHQQINMNQVPTMNmsptriaPTQGMLGAHGGNMvtqTPNQTQ 755
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMGGA----MGQPPYYGQ------GPQQQFNGQPLGW-------PRMSMMPTPMGPG---GPLRPN 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   756 FMTQPPFPATTNTMNVNMGQPNSQTPVsQQQPNANlplnalgplgpalGCPTPPQAPLratPPPNataasttnlPAALQP 835
Cdd:TIGR01628  436 GLAPMNAVRAPSRNAQNAAQKPPMQPV-MYPPNYQ-------------SLPLSQDLPQ---PQST---------ASQGGQ 489
                          170
                   ....*....|....*....
gi 528516427   836 STPTPAPAQATPPHMQTQA 854
Cdd:TIGR01628  490 NKKLAQVLASATPQMQKQV 508
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
81-301 5.43e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427    81 LSELLRPGSSAGMNSVSPQPGGIGPQLGGLGKSPLGQGSPSHPSQTQKPGGTPGTQGNNAGSAGMGFNQGMlnsGMMGQN 160
Cdd:pfam09606  124 LASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQG---PMGGQM 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   161 AGAQGGQVINGALgtvgrgrgvQGMYQGAAMQVASSVGAGGGVGAAAPGGAGSVLAETLTQGAQQMGINAQQAkMGMAGG 240
Cdd:pfam09606  201 PPQMGVPGMPGPA---------DAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQM-QQMPQG 270
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427   241 NSPFGQYQAGGQQLGTNAQNKGALPNSLPPFPTDLKGATVTSVP------NMPQQQQVSVGMVAGQG 301
Cdd:pfam09606  271 VGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQqqqqggNHPAAHQQQMNQSVGQG 337
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1892-2333 2.46e-03

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: 43.07  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1892 MTMNGLPMNHQQPRMpGAMQPPMQLVGPRGQQVMQPMPQGQwpggAQPSMPAAQQQVAQQTPQGPQSTLPIQRpaMPQQV 1971
Cdd:pfam09606  132 MPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP----NQMGPNGGPGQGQAGGMNGGQQGPMGGQ--MPPQM 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1972 AQPRMMVPTQgPRPQAPQRAAGIAPnalqdllrtlkspsspqqqqqvlnilkSNPQLMAAFIKQRtakyhasqpqqqqpq 2051
Cdd:pfam09606  205 GVPGMPGPAD-AGAQMGQQAQANGG---------------------------MNPQQMGGAPNQV--------------- 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2052 qgIHAAQPAMQNMAAMQAVPRPGMAPQQQQQQPTPQGMAALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQG 2131
Cdd:pfam09606  242 --AMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2132 GMPQAHGQfpqaqgtatnytqlrmQQQQLAMqgtgGPMGQLPPMAQMAMDGTPNllhQRNnlllqqQQLPQQQVVLKPPM 2211
Cdd:pfam09606  320 GNHPAAHQ----------------QQMNQSV----GQGGQVVALGGLNHLETWN---PGN------FGGLGANPMQRGQP 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2212 GSQAQPSPMSPQTHLLSGQPQGAHLPGQPmanalsnQVCSPGPVQSPRPPSQQPpphsspsphvQPQPSPQHVPSHtgSP 2291
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQP-------SVPSPQGPGSQPPQSHPG----------GMIPSPALIPSP--SP 431
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 528516427  2292 HPGLTTPMPGSMDQGHLGTPeqsamlpqLNTPNRGGLPSDLN 2333
Cdd:pfam09606  432 QMSQQPAQQRTIGQDSPGGS--------LNTPGQSAVNSPLN 465
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1775-2318 2.55e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1775 PSPPASTAPSTPTSHQQPNTPQTP-QPLPNqPTTPNAVVmSPtypnTPRNGQPLPQASQGKPgPQASPLHQQQSPLPQPP 1853
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPAQPTVAwQPVPG-PQTGEPVI-AP----APEGYPQQSQYAQPAV-QYNEPLQQPVQPQQPYY 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1854 QQQPPPQQPPQQQQQPPPMAVKMARHIEMVAQAQQnyrmtmnGLPMNHQQPRMPGAMQPPMQLVGPRGQQVMQPMPQGQW 1933
Cdd:PRK10263  409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVA-------GNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQP 481
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1934 PGGAQPSMPAAQQQVAQQTPQGPQ----STLPIQRPAMPQQVA---QPrMMVPTQGPRPQAPQRAAGIAPNAlqdllrtl 2006
Cdd:PRK10263  482 QPVEQQPVVEPEPVVEETKPARPPlyyfEEVEEKRAREREQLAawyQP-IPEPVKEPEPIKSSLKAPSVAAV-------- 552
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2007 kspsspqqqQQVLNILKSNPqlMAAFIKQRTAKYHASQPQQQQPQQGIHAAQPAMQNMAAM-QAVPRPGMAPQQQQQQPT 2085
Cdd:PRK10263  553 ---------PPVEAAAAVSP--LASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIgPQLPRPKRIRVPTRRELA 621
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2086 PQGM-----------AALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQGGMPQAHGQFPQAQGTATNYTQLR 2154
Cdd:PRK10263  622 SYGIklpsqraaeekAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAAEAELAR 701
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2155 M----QQQQLAMQGTGG--PMG----QLPPMAQMAMDG------TPNLL-HQRNNLLLQQQQLPQQQVVLKPPMGSQAQP 2217
Cdd:PRK10263  702 QfaqtQQQRYSGEQPAGanPFSlddfEFSPMKALLDDGpheplfTPIVEpVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP 781
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2218 -SPMSPQthllsgqpQGAHLPGQPMANALSNQVCSPgPVQSPRPPSQQPPPHSSPSPHVQPQPSPQHVPSHTgSPHPGL- 2295
Cdd:PRK10263  782 qQPVAPQ--------PQYQQPQQPVAPQPQYQQPQQ-PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT-LLHPLLm 851
                         570       580       590
                  ....*....|....*....|....*....|....
gi 528516427 2296 -----------TTPMPgSMDqghLGTPEQSAMLP 2318
Cdd:PRK10263  852 rngdsrplhkpTTPLP-SLD---LLTPPPSEVEP 881
PRK10263 PRK10263
DNA translocase FtsK; Provisional
816-1038 4.12e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  816 TPPPNATAASTT---NLPAALQPSTPTPAPAQATPPHMQTQAEL-PIPGQQHPG---TPTGENRVPTPASAASTELHSQH 888
Cdd:PRK10263  317 TEPVAVAAAATTatqSWAAPVEPVTQTPPVASVDVPPAQPTVAWqPVPGPQTGEpviAPAPEGYPQQSQYAQPAVQYNEP 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  889 --------------------AVPDVPPNDTKTEEQDYDMAVKTEPSTETE---EDTGSLLVKKEEQEGSEAKQEPMETED 945
Cdd:PRK10263  397 lqqpvqpqqpyyapaaeqpaQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwqaEEQQSTFAPQSTYQTEQTYQQPAAQEP 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  946 KKTDLKTETKEEDESKTNGTASSSPSQSRRKIFKP-EELRQALMPTLESLYRQDPEslPFRQPVdPILLGIPDYFDIVKN 1024
Cdd:PRK10263  477 LYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEvEEKRAREREQLAAWYQPIPE--PVKEPE-PIKSSLKAPSVAAVP 553
                         250
                  ....*....|....
gi 528516427 1025 PIDLSTIKRKLDTG 1038
Cdd:PRK10263  554 PVEAAAAVSPLASG 567
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
775-973 4.94e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.06  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  775 QPNSQTPVSQQQPNANLPLNALGP-------------------LGPALGCPTPPQAPLRATPPPNATAASTTNLPAA-LQ 834
Cdd:NF033839  300 QPSPQPEKKEVKPEPETPKPEVKPqlekpkpevkpqpekpkpeVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVkPQ 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  835 PSTPTPA--PAQATP-PHMQTQAELPIPGQQhpgtPTGENRVPTPASAASTELHSQHAVPDVPPNDTKTEEQDYDMAVKT 911
Cdd:NF033839  380 PETPKPEvkPQPEKPkPEVKPQPEKPKPEVK----PQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKP 455
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  912 EPSTETEEDTGSLLVKKEEQEGSEAKQEPM----ETEDKK----TDLKTETKEEDESKTNGTASSSPSQS 973
Cdd:NF033839  456 QPETPKPEVKPQPEKPKPEVKPQPEKPKPDnskpQADDKKpstpNNLSKDKQPSNQASTNEKATNKPKKS 525
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
79-168 8.87e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.14  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   79 KQLSELLRPGSSAGMNSVSPQPG-GIGPQLGGlgksPLGQGSPShPSQTQKPGGTPGTQGNNA--GSAGMGFNQGMLNSG 155
Cdd:cd21118   104 RQAEDIIRHGVDAVHNSWQGSGGhGAYGSQGG----PGVQGHGI-PGGTGGPWASGGNYGTNSlgGSVGQGGNGGPLNYG 178
                          90
                  ....*....|...
gi 528516427  156 MMGQNAGAQGGQV 168
Cdd:cd21118   179 TNSQGAVAQPGYG 191
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1235-1542 7.82e-92

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: 302.78  E-value: 7.82e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1235 VNKYLKRQNhPEAGEVFVRVVASSDKTVEVKPGMKAKFVDTGEmmEAFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 1314
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1315 PFPNTRRVYISYLDSIHFFKPRmLRTAVYHEILIGYLEYVKKLGYVTAHIWACPPSEGDDYIFhchPADQKIPK-----P 1389
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1390 KRLQEWYRKMLDKAFAE-------RILHDYKDIFKQ-----ATEDRL-------------TSANELPYFEGDFWPNVLEE 1444
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1445 SIKELEQEEE--------------------------ERKKEENTAACETPEGTPGdsknakkKNNKKTNKNKSSLSRANK 1498
Cdd:pfam08214  234 LIKEGRWKSVsldqfweelrfrqefslgrlvgfiglEGDYTPGSDDVINPPGLVK-------SKKQYKMIKSYITGREYS 306
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528516427  1499 KKPGMPNVANDLSQKLYATMEKHkevFFVIHLHSGPIVNSLLPI 1542
Cdd:pfam08214  307 TEEGAPESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
980-1087 4.48e-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: 247.36  E-value: 4.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  980 PEELRQALMPTLESLYRQDPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 1059
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 528516427 1060 YNRKTSRVYKYCSKLAEVFEQEIDPVMQ 1087
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
548-628 1.92e-47

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 164.59  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   548 GVRKAWHEHVTQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRDEYYHFLAEKIYKIQKELE 627
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 528516427   628 E 628
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
977-1085 4.35e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 127.39  E-value: 4.35e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427    977 IFKPEELRQALMPTLESLYRQDPESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 1056
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 528516427   1057 AWLYNRKTSRVYKYCSKLAEVFEQEIDPV 1085
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1099-1171 8.53e-33

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


Pssm-ID: 276805  Cd Length: 73  Bit Score: 122.40  E-value: 8.53e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427 1099 FSPQTLCCYGKqlCTIPRDGT--YYSYQ---NRYHFCEKCFNEIQGDSVTLGDDpaqPQTMISKDQFERKKNDTLDPE 1171
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKRNavYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
983-1082 2.51e-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: 116.32  E-value: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  983 LRQALMPTLESLYRQ-DPESLPFRQPVDPilLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1061
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDP--KEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 528516427 1062 RKTSRVYKYCSKLAEVFEQEI 1082
Cdd:cd04369    79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1003-1080 2.23e-28

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


Pssm-ID: 99930  Cd Length: 102  Bit Score: 110.83  E-value: 2.23e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427 1003 PFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1080
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 ...
325-392 9.01e-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: 107.86  E-value: 9.01e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528516427   325 HAHKCQRREQAngdvrACALPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVC 392
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
1925-2043 3.78e-27

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: 107.61  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1925 MQPMPQGQWPGgaqpsmpaaqqqvaqqtPQGPQSTLPIQRPAMPQQVA-QPRMMVPTQGPR-----PQAPQRAAGIAPNA 1998
Cdd:pfam09030    1 QPQWAQGQWQQ-----------------QQPLQQMQGMQRPMMPQQQQqQMPGMNPPQQPGlpqvpGQQPGRPGSIAPNA 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 528516427  1999 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYHAS 2043
Cdd:pfam09030   64 LQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYQAS 108
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
982-1082 7.34e-27

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


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 106.48  E-value: 7.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  982 ELRQALMPTLESLyRQDPESLPFRQPVDpiLLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1061
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVD--KEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|.
gi 528516427 1062 RKTSRVYKYCSKLAEVFEQEI 1082
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1598-1638 7.83e-27

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


Pssm-ID: 239077  Cd Length: 41  Bit Score: 104.18  E-value: 7.83e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528516427 1598 YTCNECKHHVETRWHCTVCEDFDLCINCYNAKGHEHQMVKW 1638
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
996-1079 6.95e-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: 100.87  E-value: 6.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  996 RQDPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLA 1075
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                  ....
gi 528516427 1076 EVFE 1079
Cdd:cd05506    93 KIFE 96
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
990-1082 6.10e-24

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


Pssm-ID: 99932  Cd Length: 103  Bit Score: 98.15  E-value: 6.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  990 TLESLYRQdPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1069
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                          90
                  ....*....|...
gi 528516427 1070 YCSKLAEVFEQEI 1082
Cdd:cd05500    91 MGKRLQAAFEKHL 103
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1665-1733 9.94e-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: 9.94e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528516427  1665 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 1733
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1659-1737 2.52e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.51  E-value: 2.52e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   1659 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 1734
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 528516427   1735 FCL 1737
Cdd:smart00551   77 KCV 79
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
1085-1124 1.40e-22

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: 92.38  E-value: 1.40e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 528516427  1085 VMQGLGYCCGRKYEFSPQTLCCYGKQLCTIPRDGTYYSYQ 1124
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
978-1080 9.93e-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: 91.97  E-value: 9.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  978 FKPEELRQALMPTLEsLYRQDPeSLPFRQPVDPillGIPDYFDIVKNPIDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 1054
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                          90       100
                  ....*....|....*....|....*.
gi 528516427 1055 NNAWLYNRKTSRVYKYCSKLAEVFEQ 1080
Cdd:cd05502    76 KNCYKFNEEDSEVAQAGKELELFFEE 101
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1001-1084 7.39e-21

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


Pssm-ID: 99929  Cd Length: 107  Bit Score: 89.79  E-value: 7.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1001 SLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1080
Cdd:cd05497    23 AWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLFLQ 102

                  ....
gi 528516427 1081 EIDP 1084
Cdd:cd05497   103 KLAQ 106
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
325-395 9.07e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 88.19  E-value: 9.07e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427    325 HAHKCQRREQAngdvraCALPHCRTMKNVLNHMTHCQAGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 395
Cdd:smart00551   16 HARRCKAREAK------CQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1003-1079 9.56e-21

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


Pssm-ID: 99931  Cd Length: 102  Bit Score: 89.27  E-value: 9.56e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427 1003 PFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFE 1079
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1000-1085 3.29e-20

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 88.28  E-value: 3.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1000 ESLPFRQPVDpiLLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKYCSKLAEVF 1078
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99

                  ....*..
gi 528516427 1079 EQEIDPV 1085
Cdd:cd05496   100 EEHIKKI 106
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1172-1206 2.15e-19

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: 83.11  E-value: 2.15e-19
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528516427 1172 PFVECKDCGRKMHQICVLHYEVIWPSGFICDNCLK 1206
Cdd:cd15647     6 PFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
997-1073 2.48e-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: 2.48e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427   997 QDPESLPFRQPVDPilLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSK 1073
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 ...
997-1081 3.14e-19

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 85.14  E-value: 3.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  997 QDPESLPFRQPVDPIllGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAE 1076
Cdd:cd05504    26 KHKDSWPFLRPVSKI--EVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQR 103

                  ....*
gi 528516427 1077 VFEQE 1081
Cdd:cd05504   104 FFIKR 108
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1173-1204 5.00e-18

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: 79.23  E-value: 5.00e-18
                          10        20        30
                  ....*....|....*....|....*....|..
gi 528516427 1173 FVECKDCGRKMHQICVLHYEVIWPSGFICDNC 1204
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1173-1206 4.30e-17

PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277116  Cd Length: 40  Bit Score: 76.44  E-value: 4.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 528516427 1173 FVECKDCGRKMHQICVLHYEVIWPSGFICDNCLK 1206
Cdd:cd15646     7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
903-1086 2.53e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 83.32  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  903 QDYDMaVKTEPSTETEEDTGSLLVKKEEQEGSEAKQEPMEtedkktdlKTETKEEDESKTNGTASSSPSQSRrKIFKPEE 982
Cdd:COG5076    78 DDLEN-VGGITYSPFEKNRPESLRFDEIVFLAIESVTPES--------GLGSLLMAHLKTSVKKRKTPKIED-ELLYADN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  983 LRQALMPTLESLYRQDPESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1062
Cdd:COG5076   148 KAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNG 225
                         170       180
                  ....*....|....*....|....
gi 528516427 1063 KTSRVYKYCSKLAEVFEQEIDPVM 1086
Cdd:COG5076   226 PDSSVYVDAKELEKYFLKLIEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1594-1636 2.92e-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: 74.40  E-value: 2.92e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 528516427   1594 DRFVYTCNEC-KHHVETRWHCTVCEDFDLCINCYNAKGHEHQMV 1636
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1016-1088 4.10e-16

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: 76.22  E-value: 4.10e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVMQG 1088
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLSG 111
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
981-1071 4.85e-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: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  981 EELRQALMPTLESLYRQDPESLPFRQPVDPIllGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1060
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                          90
                  ....*....|.
gi 528516427 1061 NRKTSRVYKYC 1071
Cdd:cd05510    84 NSDPSHPLRRH 94
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1594-1635 7.38e-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: 70.20  E-value: 7.38e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 528516427  1594 DRFVYTCNECKH--HVETRWHCTVCEDFDLCINCYNA-KGHEHQM 1635
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1016-1069 1.45e-14

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 71.57  E-value: 1.45e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 1069
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
986-1076 3.76e-14

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


Pssm-ID: 99944  Cd Length: 98  Bit Score: 70.12  E-value: 3.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  986 ALMPTLESLYRQDPESLpFRQPVDpiLLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 1065
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                          90
                  ....*....|.
gi 528516427 1066 RVYKYCSKLAE 1076
Cdd:cd05512    82 IFYRAAVRLRD 92
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1598-1638 5.04e-14

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 68.23  E-value: 5.04e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 528516427 1598 YTCNEC-KHHVETRWHCTVCEDFDLCINCYNA--KGH--EHQMVKW 1638
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKgkKGHppDHSFTEI 46
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
999-1067 8.50e-14

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: 68.94  E-value: 8.50e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427  999 PESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 1067
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
996-1081 1.52e-13

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: 68.83  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  996 RQDPESLPFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSR-------VY 1068
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90
                          90
                  ....*....|...
gi 528516427 1069 KYCSKLAEVFEQE 1081
Cdd:cd05511    91 ELAEELLAEREEK 103
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
982-1084 1.80e-13

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: 68.54  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  982 ELRQALMPTLESLYRqDPESLPFRQPVDPilLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 1061
Cdd:cd05528     3 ELRLFLRDVLKRLAS-DKRFNAFTKPVDE--EEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 528516427 1062 ------RKTSRvYKYCSKLAEV---FEQEIDP 1084
Cdd:cd05528    80 pdrdpaDKLIR-SRACELRDEVhamIEAELDP 110
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
982-1070 3.15e-13

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


Pssm-ID: 99952  Cd Length: 106  Bit Score: 67.73  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  982 ELRQALMPTLESLYRQDPES----LPFRQpVDPILLGIPDYFDIVKNPIDLSTIKRKLDtgQYQEPWQYVDDVWLMFNNA 1057
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieiHPIFN-VLPLRKDYPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNA 77
                          90
                  ....*....|...
gi 528516427 1058 WLYNRKTSRVYKY 1070
Cdd:cd05521    78 RLYNTKGSVIYKY 90
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1129-1204 2.66e-12

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


Pssm-ID: 277086  Cd Length: 73  Bit Score: 63.91  E-value: 2.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427 1129 FCEKCFNEIQGDSVTLGddpaqpQTMISKDQFERKKNDTLDPEPFVECKDCGRKMHQICVLHYEVIWPSG---FICDNC 1204
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADEtaeYVCPLC 73
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
984-1081 4.08e-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: 64.69  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  984 RQALMPTLESLYRQdPESLPFRQPVDpiLLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRk 1063
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPVT--EDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNS- 80
                          90
                  ....*....|....*...
gi 528516427 1064 tsrvYKYCSKLAEVFEQE 1081
Cdd:cd05507    81 ----SDHDVYLMAVEMQR 94
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1016-1074 2.22e-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: 62.36  E-value: 2.22e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKL 1074
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1016-1074 3.18e-11

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


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 61.87  E-value: 3.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKL 1074
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
979-1078 3.91e-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: 61.40  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  979 KPEELRQALMPtleslYRqdpESLPFRQPVDPIllGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1058
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                          90       100
                  ....*....|....*....|
gi 528516427 1059 LYNRKTSRVYKYCSKLAEVF 1078
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
983-1074 6.79e-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: 60.89  E-value: 6.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  983 LRQALMPTLESLYRQDPESLpFRQPVDPILlgIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 1062
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                          90
                  ....*....|..
gi 528516427 1063 KTSRVYKYCSKL 1074
Cdd:cd05513    79 PDTIYYKAAKKL 90
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1016-1082 7.94e-11

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: 60.82  E-value: 7.94e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEI 1082
Cdd:cd05519    37 PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1003-1083 3.94e-10

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


Pssm-ID: 99947  Cd Length: 107  Bit Score: 58.98  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1003 PFRQ-PVDPILlgiPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQE 1081
Cdd:cd05516    27 VFIQlPSRKEL---PEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSA 103

                  ..
gi 528516427 1082 ID 1083
Cdd:cd05516   104 RQ 105
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1016-1068 7.48e-10

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


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 58.23  E-value: 7.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 1068
Cdd:cd05518    37 PDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
1998-2040 1.94e-09

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 54.97  E-value: 1.94e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528516427 1998 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 2040
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1010-1080 5.45e-09

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: 55.86  E-value: 5.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427 1010 PILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1080
Cdd:cd05525    33 PSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1599-1637 5.62e-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: 53.80  E-value: 5.62e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528516427 1599 TCNECKHHVE-TRWHCTVCEDFDLCINCYNAKGH-EHQMVK 1637
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLK 42
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
714-903 1.72e-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: 60.17  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   714 HQQINMNQVPTMN-MSPTRIAPTQGmlgahggnmvtqTPNQTQFMTQPPFPATTnTMNVNMGQPNSQTPVSQQQPNANLP 792
Cdd:pfam03154  163 QQQILQTQPPVLQaQSGAASPPSPP------------PPGTTQAATAGPTPSAP-SVPPQGSPATSQPPNQTQSTAAPHT 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   793 LNALGPL--GPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTqaelPIPGQQHPGTP-TG 869
Cdd:pfam03154  230 LIQQTPTlhPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQH----PVPPQPFPLTPqSS 305
                          170       180       190
                   ....*....|....*....|....*....|....
gi 528516427   870 ENRVPTPASAASTelHSQHAVPDVPPNDTKTEEQ 903
Cdd:pfam03154  306 QSQVPPGPSPAAP--GQSQQRIHTPPSQSQLQSQ 337
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
981-1082 1.90e-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: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  981 EELRQALMPTLESLYRQDPESL--PFRQPVDpILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 1058
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                          90       100
                  ....*....|....*....|....
gi 528516427 1059 LYNRKTSRVYKYCSKLAEVFEQEI 1082
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1016-1080 2.27e-08

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


Pssm-ID: 99948  Cd Length: 103  Bit Score: 53.98  E-value: 2.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528516427 1016 PDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQ 1080
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1875-2001 1.85e-06

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: 53.27  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1875 KMARHIEMVAQAQQNyRMTMNGLPMNHQqprMPGAM-QPPMQLVGPrgQQVMQPMPQGqWPGGAQpsMPaaqqqvaqqTP 1953
Cdd:TIGR01628  364 KEQRRAHLQDQFMQL-QPRMRQLPMGSP---MGGAMgQPPYYGQGP--QQQFNGQPLG-WPRMSM--MP---------TP 425
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 528516427  1954 QGPQSTL-PIQRPAMPQQVAQPRMMVPTQGPRPQAPQRAagiAPNALQD 2001
Cdd:TIGR01628  426 MGPGGPLrPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMY---PPNYQSL 471
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
668-926 2.41e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 52.65  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   668 PVPMPNVPNQILNRMQVSQGMNPFSAMSNVPMSQAPM----------GTRAASPINHQQINMNQVP-TMNMSPTRIAP-T 735
Cdd:pfam17823  173 PAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatGHPAAGTALAAVGNSSPAAgTVTAAVGTVTPaA 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   736 QGMLGAHGGNMVT--QTPNQTQFMTQPPFPAT---TNTMNVN----MGqPNSQTPVSQ---QQPnanlPLNALGPLGPAL 803
Cdd:pfam17823  253 LATLAAAAGTVASaaGTINMGDPHARRLSPAKhmpSDTMARNpaapMG-AQAQGPIIQvstDQP----VHNTAGEPTPSP 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   804 GCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAP-------AQATPPHMQTQAELPIPGQQHPGTPTGENRVPTP 876
Cdd:pfam17823  328 SNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLhtsmipeVEATSPTTQPSPLLPTQGAAGPGILLAPEQVATE 407
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528516427   877 ASA--ASTELHSQHA-VPDVPPNDT-KTEEQDYDMAVKTEPSTETEEDTGSLLV 926
Cdd:pfam17823  408 ATAgtASAGPTPRSSgDPKTLAMAScQLSTQGQYLVVTTDPLTPALVDKMFLLV 461
PHA03247 PHA03247
large tegument protein UL36; Provisional
758-895 7.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  758 TQPPFPATTNTmnvnmgqPNSQT----PVSQQQPNANLPLNA-LGPLGPALGCPTPPQAPLRATPPPNAtAASTTNLPAA 832
Cdd:PHA03247 2755 ARPARPPTTAG-------PPAPAppaaPAAGPPRRLTRPAVAsLSESRESLPSPWDPADPPAAVLAPAA-ALPPAASPAG 2826
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427  833 LQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTgeNRVPTPASAASTELHSQH------AVPDVPP 895
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV--RRRPPSRSPAAKPAAPARppvrrlARPAVSR 2893
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
642-975 1.04e-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: 51.07  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   642 TSMTATGQQPSALNQPNVMGPRPQNGPVPMPNVPNQILNRMQVSQGMNPfsaMSNVPMSQAPMGTRAASPINhqqinmnq 721
Cdd:pfam05109  446 TGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSP---RDNGTESKAPDMTSPTSAVT-------- 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   722 VPTmnmsPTRIAPTQGMlgahggnmVTQTPNQTQfmtqPPFPATTNTMNVNMGQPNSQTP---VSQQQPNANLPlnALGP 798
Cdd:pfam05109  515 TPT----PNATSPTPAV--------TTPTPNATS----PTLGKTSPTSAVTTPTPNATSPtpaVTTPTPNATIP--TLGK 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   799 LGP--ALGCPTP-----------PQA-------------PLRATPPPNATAASTT------------------NLPAALQ 834
Cdd:pfam05109  577 TSPtsAVTTPTPnatsptvgetsPQAnttnhtlggtsstPVVTSPPKNATSAVTTgqhnitssstssmslrpsSISETLS 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   835 PST---------------PTPA-------PAQATPPHMQTQAELPIPGQQHPGTPTGEnrvptpaSAASTELHSQHAVPD 892
Cdd:pfam05109  657 PSTsdnstshmplltsahPTGGenitqvtPASTSTHHVSTSSPAPRPGTTSQASGPGN-------SSTSTKPGEVNVTKG 729
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   893 VPPNDTKTEE--QDYDMAVKTEPST--ETEEDTGSllvKKEEQEGSEAKQEPmeTEDKKTDLKTEtkeedESKTNGTASS 968
Cdd:pfam05109  730 TPPKNATSPQapSGQKTAVPTVTSTggKANSTTGG---KHTTGHGARTSTEP--TTDYGGDSTTP-----RTRYNATTYL 799

                   ....*..
gi 528516427   969 SPSQSRR 975
Cdd:pfam05109  800 PPSTSSK 806
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
981-1082 1.42e-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: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  981 EELRQALMPTLESLYRqdPESLPFRQPVDpiLLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 1060
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                          90       100
                  ....*....|....*....|..
gi 528516427 1061 NRKTSRVYKYCSKLAEVFEQEI 1082
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
763-923 2.02e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.87  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  763 PATTNTMNVNMGQPNSQTPVSQQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPPNATAASTTNLP-----AALQPST 837
Cdd:PRK12323  374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASArgpggAPAPAPA 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  838 PTPAPAQATPPHMqtqAELPIPGQQHPGTPTGENRVPTPASAASTELHSQHAVPDVP---PNDTKTEEQDYDMAVKTEPS 914
Cdd:PRK12323  454 PAAAPAAAARPAA---AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFAspaPAQPDAAPAGWVAESIPDPA 530

                  ....*....
gi 528516427  915 TETEEDTGS 923
Cdd:PRK12323  531 TADPDDAFE 539
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
748-904 2.83e-05

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 48.89  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   748 TQTPNQTQFMTQPPFPATTNTMNvnmgQPNSQtpvSQQQPNANLPLNALGPLGPAlGCPTPPQAPLRATPPPNATAASTT 827
Cdd:pfam05539  175 SKTTSWPTEVSHPTYPSQVTPQS----QPATQ---GHQTATANQRLSSTEPVGTQ-GTTTSSNPEPQTEPPPSQRGPSGS 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   828 N--LPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQH------PGTPTGENRVPTPASAASTELHSQHAVPDVPPNDTK 899
Cdd:pfam05539  247 PqhPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHstatppPTTKRQETGRPTPRPTATTQSGSSPPHSSPPGVQAN 326

                   ....*
gi 528516427   900 TEEQD 904
Cdd:pfam05539  327 PTTQN 331
PHA03378 PHA03378
EBNA-3B; Provisional
653-895 3.06e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 49.68  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  653 ALNQPNVMGPRPQNGPVPMPNVPNQILNRMQVSQGMNPFSAMSN--VPMSQAPMG--TRAASPINH--QQINMNQVPtMN 726
Cdd:PHA03378  554 ASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWpvPHPSQTPEPptTQSHIPETSapRQWPMPLRP-IP 632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  727 MSPTRIAPTQ----GMLGAHGGNMVTQTPNQTQFMTQPPFPATTNTMNVNMGQPNSQTPVSQQQPNAnlplnALGPLGPA 802
Cdd:PHA03378  633 MRPLRMQPITfnvlVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPR-----APTPMRPP 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  803 LGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPaQATPPHMQTQAELPIPGQQHPGTPTGENRVPTPASAAST 882
Cdd:PHA03378  708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP-AAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP 786
                         250
                  ....*....|...
gi 528516427  883 ELHSQHAVPDVPP 895
Cdd:PHA03378  787 QQRPRGAPTPQPP 799
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
981-1038 3.20e-05

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


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 45.13  E-value: 3.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528516427  981 EELRQALMPtLESLYRQDPeSLPFRQPVDPILLGIPDYFDIVKNPIDLSTI-KRKLDTG 1038
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
689-914 3.61e-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: 49.14  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   689 NPFSAMSNVPMSQAPMGTRAASPINHQQI----------NMNQVPTMNMSPTRIAPTQGMLG---------AHGGNMVTQ 749
Cdd:pfam05109  411 NATTTTHKVIFSKAPESTTTSPTLNTTGFaapntttglpSSTHVPTNLTAPASTGPTVSTADvtsptpagtTSGASPVTP 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   750 TPNQTQFMTQPPFP-ATTNTMNVNMGQPNSQTP---VSQQQPNANLPlnALGPLGP--ALGCPTP---PQAPLRATPPPN 820
Cdd:pfam05109  491 SPSPRDNGTESKAPdMTSPTSAVTTPTPNATSPtpaVTTPTPNATSP--TLGKTSPtsAVTTPTPnatSPTPAVTTPTPN 568
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   821 A----------TAASTTNLPAALQPSTPTPAPAQATPPH-MQTQAELPI----PGQQHPGTPTGENRVpTPASAASTELH 885
Cdd:pfam05109  569 AtiptlgktspTSAVTTPTPNATSPTVGETSPQANTTNHtLGGTSSTPVvtspPKNATSAVTTGQHNI-TSSSTSSMSLR 647
                          250       260
                   ....*....|....*....|....*....
gi 528516427   886 SQHAVPDVPPNDTKTEEQDYDMAVKTEPS 914
Cdd:pfam05109  648 PSSISETLSPSTSDNSTSHMPLLTSAHPT 676
PHA03247 PHA03247
large tegument protein UL36; Provisional
760-912 4.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  760 PPFPATTNTMNVNMGQPNSQTPVSQQQPNANLPLNALGP-----LGPALGCPTPPQAPLR-ATPPPNATAASTTNLPAal 833
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrLGRAAQASSPPQRPRRrAARPTVGSLTSLADPPP-- 2703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  834 QPSTPTPAP-----AQATPPHMQ---------TQAELPIPGQQHPGTPTGENRVPTPASAASTELHSQHAVPDVPPNDTK 899
Cdd:PHA03247 2704 PPPTPEPAPhalvsATPLPPGPAaarqaspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783
                         170
                  ....*....|...
gi 528516427  900 TEEQDYDMAVKTE 912
Cdd:PHA03247 2784 TRPAVASLSESRE 2796
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1598-1637 5.89e-05

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: 42.42  E-value: 5.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528516427 1598 YTCNECKHH--VETRWHCTVC--EDFDLCINCYNAKG-HE--HQMVK 1637
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCVVKGEsHQedHWLVK 47
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1015-1080 9.09e-05

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


Pssm-ID: 99933  Cd Length: 102  Bit Score: 43.57  E-value: 9.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427 1015 IPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKYCSKLAEVFEQ 1080
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
PRK13042 PRK13042
superantigen-like protein SSL4; Reviewed;
795-927 9.33e-05

superantigen-like protein SSL4; Reviewed;


Pssm-ID: 183854 [Multi-domain]  Cd Length: 291  Bit Score: 46.93  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  795 ALGPLGPALGCPTPPQAplRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPgqqHPGTPTGENrVP 874
Cdd:PRK13042   12 ALGLLTTGVITTTTQAA--NATTPSSTKVEAPQSTPPSTKVEAPQSKPNATTPPSTKVEAPQQTP---NATTPSSTK-VE 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528516427  875 TPASAASTELhsqhavpdvpPNDTKTEEQDYdMAVKTEPSTETEEDTGSLLVK 927
Cdd:PRK13042   86 TPQSPTTKQV----------PTEINPKFKDL-RAYYTKPSLEFKNEIGIILKK 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
643-903 1.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  643 SMTATGQQPSALNQPNV-MGPRPQNGPVPMPNVPNQIlnrMQVSQGMNPFSAMSNVPMSQAPMGTRAASPINHQQINMNQ 721
Cdd:PHA03247 2581 AVTSRARRPDAPPQSARpRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA 2657
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  722 VPtmNMSPTRIAPTQGMlgahggnmVTQTPNQTQFMTQPPFPATTNTMnVNMGQPNSQTPVSQQQPNANLPLNALgPLGP 801
Cdd:PHA03247 2658 PG--RVSRPRRARRLGR--------AAQASSPPQRPRRRAARPTVGSL-TSLADPPPPPPTPEPAPHALVSATPL-PPGP 2725
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  802 ALGCPTPPQAPLRATPPPNATAASTtnlpaalqPSTPTPAPAQATP--PHMQTQAELPIPGQQHPGT-PTGENRVPTPAS 878
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPAT--------PGGPARPARPPTTagPPAPAPPAAPAAGPPRRLTrPAVASLSESRES 2797
                         250       260
                  ....*....|....*....|....*
gi 528516427  879 AASTELHSQHAVPDVPPNDTKTEEQ 903
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAA 2822
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
801-902 1.15e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  801 PALGCPTPPQAPLRATPPPN--ATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTGEnRVPTPAS 878
Cdd:PRK07764  394 PAAAAPSAAAAAPAAAPAPAaaAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ-PAPAPAA 472
                          90       100
                  ....*....|....*....|....
gi 528516427  879 AASTELHSQHAVPDVPPNDTKTEE 902
Cdd:PRK07764  473 APEPTAAPAPAPPAAPAPAAAPAA 496
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1598-1626 1.52e-04

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


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 41.12  E-value: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 528516427 1598 YTCNECKHHV--ETRWHCTVCEDFDLCINCY 1626
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1768-1988 2.12e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1768 RAMPQSLPSPPASTAPSTPTSHQQ-----PNTPQTPQPLPNQPTTPNAVVMS-------PTYPNTPRNGQPLPQASQGKP 1835
Cdd:pfam03154  142 RSTSPSIPSPQDNESDSDSSAQQQilqtqPPVLQAQSGAASPPSPPPPGTTQaatagptPSAPSVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1836 GPQASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAvkmarhiEMVAQAQQNYRMTMNGLPMNHQQPRMPGAMQPPmq 1915
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPS-------QVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHP-- 292
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427  1916 lVGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTP---QGPQSTLPIQRPAMPQQVAQPRMMVPTQGPRPQAP 1988
Cdd:pfam03154  293 -VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPsqsQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLP 367
PHA03369 PHA03369
capsid maturational protease; Provisional
823-962 2.66e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 46.15  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  823 AASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTGE-NRVPTPASAASTELHSQhAVPDVPPNDTKTE 901
Cdd:PHA03369  347 ILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVpARSPMTAYPPVPQFCGD-PGLVSPYNPQSPG 425
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427  902 EQDYDMAVKTEPSTETE-----EDTGSLLVKKEEQEGSEAKQEPMETEDKKTDLKT-----ETKEEDESKT 962
Cdd:PHA03369  426 TSYGPEPVGPVPPQPTNpyvmpISMANMVYPGHPQEHGHERKRKRGGELKEELIETlklvkKLKEEQESLA 496
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
651-919 2.85e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   651 PSALNQPNVMGPRPqngpvPMPNVPNQILNRMQVSQGMNPFSAMSNVPMSQAPMGTRAASPINHQQiNMNQVPTMNMSPT 730
Cdd:pfam03154  263 PQPLPQPSLHGQMP-----PMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQ-RIHTPPSQSQLQS 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   731 RIAPTQGMLGAHGGNMVTQTPNQTQFMTQPPFPATTN-----------TMNVNMGQPNSQTPVS----QQQPNANLPLNA 795
Cdd:pfam03154  337 QQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKhpphlsgpspfQMNSNLPPPPALKPLSslstHHPPSAHPPPLQ 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   796 LGPLGPALgcPTPPQAPLRAT------------PPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQH 863
Cdd:pfam03154  417 LMPQSQQL--PPPPAQPPVLTqsqslpppaashPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427   864 PGTPTGENRVPTPASAASTelhsqhavpdVPPndtkteeqdydMAVKTEPSTETEE 919
Cdd:pfam03154  495 PSSASVSSSGPVPAAVSCP----------LPP-----------VQIKEEALDEAEE 529
PHA03247 PHA03247
large tegument protein UL36; Provisional
1771-1841 3.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528516427 1771 PQSLPSPPASTAPSTPTSHQQPNTPQTPQPLPNQPTTPNAVVMSPTYPNTPRNGQPLPQASQGKPGPQASP 1841
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP 2975
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
1600-1637 3.48e-04

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: 40.13  E-value: 3.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528516427 1600 CNECKHH--VETRWHCTVCEDFDLCINCYNAKGH--EHQMVK 1637
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHdlEHRFYR 44
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
640-974 5.19e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   640 NQTSMTATGQQPSALNQPNVMGPRPQnGPVPMPNVPnqilnrmqvSQGMNPFSAMSNVPMSQAPMGTRAASPInhqQINM 719
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPREQPLPP-APLSMPHIK---------PPPTTPIPQLPNPQSHKHPPHLSGPSPF---QMNS 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   720 NQVPTMNMSPTRIAPTQGMLGAHGGNMvtQTPNQTQFMTQPPFPATTNTMNVNMGQPNSQTPvsqqqpnanlPLNALGPL 799
Cdd:pfam03154  389 NLPPPPALKPLSSLSTHHPPSAHPPPL--QLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP----------PTSGLHQV 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   800 GPALGCPTPPQAPLRATP--PPNATAASTTNLPAALQP--------STPTPAPAQATPPHMQTQAElPIPGQQHPGTPTG 869
Cdd:pfam03154  457 PSQSPFPQHPFVPGGPPPitPPSGPPTSTSSAMPGIQPpssasvssSGPVPAAVSCPLPPVQIKEE-ALDEAEEPESPPP 535
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   870 ENRVPTP-ASAASTELHSQHAVpdvppNDTKTEEQDYDMAVKTE------PSTETEEDTGSLLVKKEEQEGSEAKQEPME 942
Cdd:pfam03154  536 PPRSPSPePTVVNTPSHASQSA-----RFYKHLDRGYNSCARTDlyfmplAGSKLAKKREEALEKAKREAEQKAREEKER 610
                          330       340       350
                   ....*....|....*....|....*....|..
gi 528516427   943 TEDKKTDLKTETKEEDESKTNGTASSSPSQSR 974
Cdd:pfam03154  611 EKEKEKEREREREREREAERAAKASSSSHEGR 642
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
676-854 5.19e-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: 45.18  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   676 NQILNRMQVSQGMNPFSAMsnvpMSQAPMGTRaaspinHQQINMNQVPTMNmsptriaPTQGMLGAHGGNMvtqTPNQTQ 755
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMGGA----MGQPPYYGQ------GPQQQFNGQPLGW-------PRMSMMPTPMGPG---GPLRPN 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   756 FMTQPPFPATTNTMNVNMGQPNSQTPVsQQQPNANlplnalgplgpalGCPTPPQAPLratPPPNataasttnlPAALQP 835
Cdd:TIGR01628  436 GLAPMNAVRAPSRNAQNAAQKPPMQPV-MYPPNYQ-------------SLPLSQDLPQ---PQST---------ASQGGQ 489
                          170
                   ....*....|....*....
gi 528516427   836 STPTPAPAQATPPHMQTQA 854
Cdd:TIGR01628  490 NKKLAQVLASATPQMQKQV 508
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1599-1638 5.36e-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: 39.88  E-value: 5.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 528516427 1599 TCNECK--HHVETRWHCTVCEDFDLCINCY--NAKGHEHQMVKW 1638
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkGRETKRHNSLHI 45
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
81-301 5.43e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427    81 LSELLRPGSSAGMNSVSPQPGGIGPQLGGLGKSPLGQGSPSHPSQTQKPGGTPGTQGNNAGSAGMGFNQGMlnsGMMGQN 160
Cdd:pfam09606  124 LASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQG---PMGGQM 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   161 AGAQGGQVINGALgtvgrgrgvQGMYQGAAMQVASSVGAGGGVGAAAPGGAGSVLAETLTQGAQQMGINAQQAkMGMAGG 240
Cdd:pfam09606  201 PPQMGVPGMPGPA---------DAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQM-QQMPQG 270
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427   241 NSPFGQYQAGGQQLGTNAQNKGALPNSLPPFPTDLKGATVTSVP------NMPQQQQVSVGMVAGQG 301
Cdd:pfam09606  271 VGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQqqqqggNHPAAHQQQMNQSVGQG 337
PHA03247 PHA03247
large tegument protein UL36; Provisional
1758-1841 6.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1758 MRRRMATMQGRAMPQSLPSPPAS--TAPSTPTSHQQPNTPQTPQPLPNQPTTPNAVVMSPTYPNTPRNGQPLPQasQGKP 1835
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP--PPRP 2939

                  ....*.
gi 528516427 1836 GPQASP 1841
Cdd:PHA03247 2940 QPPLAP 2945
PHA02682 PHA02682
ORF080 virion core protein; Provisional
773-892 6.22e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.08  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  773 MGQPNSQTPVSQQ----QPNANLPLNALGPLGPALGCPTP----PQAPLRATPPPNATAASTTNLPAAlQPST------- 837
Cdd:PHA02682   73 MQRPSGQSPLAPSpacaAPAPACPACAPAAPAPAVTCPAPapacPPATAPTCPPPAVCPAPARPAPAC-PPSTrqcppap 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528516427  838 --PTPAPAQATPPHMqTQAELPIPGQQHPGTPTGENrvptpASAASTELHSQhaVPD 892
Cdd:PHA02682  152 plPTPKPAPAAKPIF-LHNQLPPPDYPAASCPTIET-----APAASPVLEPR--IPD 200
PRK10856 PRK10856
cytoskeleton protein RodZ;
1763-1841 6.74e-04

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 44.25  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1763 ATMQGRAMPQSLP------------SPPASTAPSTPTSHQQPNTPQTPQPL----------PNQPTTPNAVVMSPTYPNT 1820
Cdd:PRK10856  151 SAELSQNSGQSVPldtstttdpattPAPAAPVDTTPTNSQTPAVATAPAPAvdpqqnavvaPSQANVDTAATPAPAAPAT 230
                          90       100
                  ....*....|....*....|.
gi 528516427 1821 PRNGQPLPQASQGKPGPQASP 1841
Cdd:PRK10856  231 PDGAAPLPTDQAGVSTPAADP 251
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
640-895 6.91e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   640 NQTSMTATGQQPSALNQPNVMgpRPQNGPVPMPNVPNQilnrmqvsqgmNPFSAMSNVPMSQAPMGTRAASPINHQQINM 719
Cdd:pfam03154  154 NESDSDSSAQQQILQTQPPVL--QAQSGAASPPSPPPP-----------GTTQAATAGPTPSAPSVPPQGSPATSQPPNQ 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   720 NQVP---------TMNMSPTRI----APTQGMlgahggnmvTQTPNQTQFMTQPPFPATTNTMNVNMGQPNSQTPVSQQQ 786
Cdd:pfam03154  221 TQSTaaphtliqqTPTLHPQRLpsphPPLQPM---------TQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQH 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   787 PNANLPLNALGPLGPALGCPTP-PQAPLRA-----TPPPNATAASTTnlPAALQPSTPTPAPAqatpPHMQTQAELPIP- 859
Cdd:pfam03154  292 PVPPQPFPLTPQSSQSQVPPGPsPAAPGQSqqrihTPPSQSQLQSQQ--PPREQPLPPAPLSM----PHIKPPPTTPIPq 365
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 528516427   860 -----GQQHPGTPTG-------ENRVPTPASAASTELHSQHAVPDVPP 895
Cdd:pfam03154  366 lpnpqSHKHPPHLSGpspfqmnSNLPPPPALKPLSSLSTHHPPSAHPP 413
PHA03378 PHA03378
EBNA-3B; Provisional
664-868 7.27e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  664 PQNGPVPMPNVPNQILnRMQVSqgmnPFsamsNVPMSQAPMGTRAASPINHQQiNMNQVPTMNMSPTRIAPTQgMLGAHG 743
Cdd:PHA03378  621 PRQWPMPLRPIPMRPL-RMQPI----TF----NVLVFPTPHQPPQVEITPYKP-TWTQIGHIPYQPSPTGANT-MLPIQW 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  744 GNMVTQTPNQTQFMTQPPFPATTNtmnvnMGQPNSQTpvSQQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPpnaTA 823
Cdd:PHA03378  690 APGTMQPPPRAPTPMRPPAAPPGR-----AQRPAAAT--GRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP---AA 759
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 528516427  824 ASTTNLPAALQPSTPTPAPA-QATPPHMQTQAELPIPGQQHPGTPT 868
Cdd:PHA03378  760 APGRARPPAAAPGAPTPQPPpQAPPAPQQRPRGAPTPQPPPQAGPT 805
PHA03247 PHA03247
large tegument protein UL36; Provisional
1769-1997 8.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1769 AMPQSLPSPPASTAPSTPTSHQQPNTPQTPQPlPNQPTTPNAVVMSPTYPNTPRNGQPLPQASQGKPGPQ---------- 1838
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAG-PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdpadppaavl 2812
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1839 ------------ASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAVKMARH-----------------IEMVAQAQQN 1889
Cdd:PHA03247 2813 apaaalppaaspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRppsrspaakpaaparppVRRLARPAVS 2892
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1890 YRMTMNGLPMNHQQ-PRMPGAMQPPmqLVGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTPQGPQSTlPIQRPAMP 1968
Cdd:PHA03247 2893 RSTESFALPPDQPErPPQPQAPPPP--QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ-PWLGALVP 2969
                         250       260
                  ....*....|....*....|....*....
gi 528516427 1969 QQVAQPRMMVPTqgPRPQAPQRAAGIAPN 1997
Cdd:PHA03247 2970 GRVAVPRFRVPQ--PAPSREAPASSTPPL 2996
PHA03247 PHA03247
large tegument protein UL36; Provisional
662-895 1.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  662 PRPQNGPVPMPNVPnqilnrmQVSQGMNPFSAMSNVPmsqAPMGTRAASPINHQQINMNQVPTMNMSPTRIA-PTQGMLG 740
Cdd:PHA03247 2712 PHALVSATPLPPGP-------AAARQASPALPAAPAP---PAVPAGPATPGGPARPARPPTTAGPPAPAPPAaPAAGPPR 2781
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  741 AHGGNMVTQTPNQTQFMTQPPFPA--TTNTMNVNMGQPNSQTPVS-QQQPNANLPLNALGPLGP-----ALGCPTPPQAP 812
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPAdpPAAVLAPAAALPPAASPAGpLPPPTSAQPTAPPPPPGPpppslPLGGSVAPGGD 2861
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  813 LRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQ-QHPGTPTGENRVPTPASAASTElhSQHAVP 891
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQpQAPPPPQPQPQPPPPPQPQPPP--PPPPRP 2939

                  ....
gi 528516427  892 DVPP 895
Cdd:PHA03247 2940 QPPL 2943
PHA03291 PHA03291
envelope glycoprotein I; Provisional
799-883 1.40e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.40  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  799 LGPA-LGCPTPPQAPLRATPPPNATAASttnlPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTGENRVPTPA 877
Cdd:PHA03291  197 LGPAdVFVPATPRPTPRTTASPETTPTP----STTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANA 272

                  ....*.
gi 528516427  878 SAASTE 883
Cdd:PHA03291  273 TPAPEA 278
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
801-987 1.66e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  801 PALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPhMQTQAELPIPgqqhpgtptgenrvPTPASAA 880
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQ-QAPAVPLPET--------------TSQLLAA 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  881 STELHSQHAVPDVPPNDTKTeeqdydmAVKTEPSTETEEDTGSLLVKKEEQEGSEAKQEPMETEdkktdlktETKEEDES 960
Cdd:PRK07994  426 RQQLQRAQGATKAKKSEPAA-------ASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWK--------ATNPVEVK 490
                         170       180
                  ....*....|....*....|....*..
gi 528516427  961 KTNGTAssspsqsrrkifkPEELRQAL 987
Cdd:PRK07994  491 KEPVAT-------------PKALKKAL 504
PHA03321 PHA03321
tegument protein VP11/12; Provisional
804-921 1.68e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.79  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  804 GCPTPP-QAPLR---ATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGT----PTGENRVPT 875
Cdd:PHA03321  412 GVPSEHyEASLRllsSRQPPGAPAPRRDNDPPPPPRARPGSTPACARRARAQRARDAGPEYVDPLGAlrrlPAGAAPPPE 491
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528516427  876 PASAASTELHSQH---AVPDVPPNDTKTEEQDYDMAVKTEPSTETEEDT 921
Cdd:PHA03321  492 PAAAPSPATYYTRmggGPPRLPPRNRATETLRPDWGPPAAAPPEQMEDP 540
PHA03193 PHA03193
tegument protein VP11/12; Provisional
751-919 1.80e-03

tegument protein VP11/12; Provisional


Pssm-ID: 177555  Cd Length: 594  Bit Score: 43.55  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  751 PNQTQFMTQPPFPATTNTMNVNMGQPNSQTPVSQQQpnANLPLNALGPLgpalgcPTPPQAPLRATPPPNATAASTTN-L 829
Cdd:PHA03193  430 GGDSQIGCLHDSPFQRKRAMPEDGGEIHEALANNGQ--AIFPECFSGDL------PPIAQALLSADELPNDTTASTSNeM 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  830 PAALQPSTPTPApAQATPPHMQTQAelpipGQQHPGTPTgenRVPTpASAASTELHSQHAVPDVPPNDTKTEEQDY---D 906
Cdd:PHA03193  502 KGDAECPAAQDA-AAILPASFQIEN-----GGAADGSGL---AIPA-AMCDATAVESPSTVAETPPERLLAAESGPrckA 571
                         170
                  ....*....|...
gi 528516427  907 MAVKTEPSTETEE 919
Cdd:PHA03193  572 TAKHKGGSSKVEE 584
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
800-906 2.08e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  800 GPALGC----PTPPQAPLRATPPPnATAASTTNLPAALQPS-TPTPA-PAQATPPHMQTQAELPIPGQQHPGTPTGENRV 873
Cdd:PRK14959  388 GPASGGaatiPTPGTQGPQGTAPA-AGMTPSSAAPATPAPSaAPSPRvPWDDAPPAPPRSGIPPRPAPRMPEASPVPGAP 466
                          90       100       110
                  ....*....|....*....|....*....|...
gi 528516427  874 PTPASAASTElhSQHAVPDVPPNDTKTEEQDYD 906
Cdd:PRK14959  467 DSVASASDAP--PTLGDPSDTAEHTPSGPRTWD 497
PHA03247 PHA03247
large tegument protein UL36; Provisional
1758-2000 2.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1758 MRRRMATMQGRAMPQSLPSPPAS----TAPSTPTSHQQPNTPQTPQPLPNQPTTPnAVVMSPTYPNTPRNgQPLPQASQG 1833
Cdd:PHA03247 2688 ARPTVGSLTSLADPPPPPPTPEPaphaLVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPAR-PARPPTTAG 2765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1834 KPGPqASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAVKMARHIEMVAQAQQNYRMTMNGLP-----MNHQQPRMPG 1908
Cdd:PHA03247 2766 PPAP-APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPpptsaQPTAPPPPPG 2844
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1909 AMQPPMQL---VGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTPQGPQS----TLPIQRPAMPQQVAQPRMMVPTQ 1981
Cdd:PHA03247 2845 PPPPSLPLggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESfalpPDQPERPPQPQAPPPPQPQPQPP 2924
                         250       260
                  ....*....|....*....|
gi 528516427 1982 -GPRPQAPQRAAGIAPNALQ 2000
Cdd:PHA03247 2925 pPPQPQPPPPPPPRPQPPLA 2944
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1892-2333 2.46e-03

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: 43.07  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1892 MTMNGLPMNHQQPRMpGAMQPPMQLVGPRGQQVMQPMPQGQwpggAQPSMPAAQQQVAQQTPQGPQSTLPIQRpaMPQQV 1971
Cdd:pfam09606  132 MPMGGAGFPSQMSRV-GRMQPGGQAGGMMQPSSGQPGSGTP----NQMGPNGGPGQGQAGGMNGGQQGPMGGQ--MPPQM 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  1972 AQPRMMVPTQgPRPQAPQRAAGIAPnalqdllrtlkspsspqqqqqvlnilkSNPQLMAAFIKQRtakyhasqpqqqqpq 2051
Cdd:pfam09606  205 GVPGMPGPAD-AGAQMGQQAQANGG---------------------------MNPQQMGGAPNQV--------------- 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2052 qgIHAAQPAMQNMAAMQAVPRPGMAPQQQQQQPTPQGMAALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQG 2131
Cdd:pfam09606  242 --AMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2132 GMPQAHGQfpqaqgtatnytqlrmQQQQLAMqgtgGPMGQLPPMAQMAMDGTPNllhQRNnlllqqQQLPQQQVVLKPPM 2211
Cdd:pfam09606  320 GNHPAAHQ----------------QQMNQSV----GQGGQVVALGGLNHLETWN---PGN------FGGLGANPMQRGQP 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  2212 GSQAQPSPMSPQTHLLSGQPQGAHLPGQPmanalsnQVCSPGPVQSPRPPSQQPpphsspsphvQPQPSPQHVPSHtgSP 2291
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQP-------SVPSPQGPGSQPPQSHPG----------GMIPSPALIPSP--SP 431
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 528516427  2292 HPGLTTPMPGSMDQGHLGTPeqsamlpqLNTPNRGGLPSDLN 2333
Cdd:pfam09606  432 QMSQQPAQQRTIGQDSPGGS--------LNTPGQSAVNSPLN 465
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1775-2318 2.55e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1775 PSPPASTAPSTPTSHQQPNTPQTP-QPLPNqPTTPNAVVmSPtypnTPRNGQPLPQASQGKPgPQASPLHQQQSPLPQPP 1853
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPAQPTVAwQPVPG-PQTGEPVI-AP----APEGYPQQSQYAQPAV-QYNEPLQQPVQPQQPYY 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1854 QQQPPPQQPPQQQQQPPPMAVKMARHIEMVAQAQQnyrmtmnGLPMNHQQPRMPGAMQPPMQLVGPRGQQVMQPMPQGQW 1933
Cdd:PRK10263  409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVA-------GNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQP 481
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1934 PGGAQPSMPAAQQQVAQQTPQGPQ----STLPIQRPAMPQQVA---QPrMMVPTQGPRPQAPQRAAGIAPNAlqdllrtl 2006
Cdd:PRK10263  482 QPVEQQPVVEPEPVVEETKPARPPlyyfEEVEEKRAREREQLAawyQP-IPEPVKEPEPIKSSLKAPSVAAV-------- 552
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2007 kspsspqqqQQVLNILKSNPqlMAAFIKQRTAKYHASQPQQQQPQQGIHAAQPAMQNMAAM-QAVPRPGMAPQQQQQQPT 2085
Cdd:PRK10263  553 ---------PPVEAAAAVSP--LASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIgPQLPRPKRIRVPTRRELA 621
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2086 PQGM-----------AALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQGGMPQAHGQFPQAQGTATNYTQLR 2154
Cdd:PRK10263  622 SYGIklpsqraaeekAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAAEAELAR 701
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2155 M----QQQQLAMQGTGG--PMG----QLPPMAQMAMDG------TPNLL-HQRNNLLLQQQQLPQQQVVLKPPMGSQAQP 2217
Cdd:PRK10263  702 QfaqtQQQRYSGEQPAGanPFSlddfEFSPMKALLDDGpheplfTPIVEpVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP 781
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2218 -SPMSPQthllsgqpQGAHLPGQPMANALSNQVCSPgPVQSPRPPSQQPPPHSSPSPHVQPQPSPQHVPSHTgSPHPGL- 2295
Cdd:PRK10263  782 qQPVAPQ--------PQYQQPQQPVAPQPQYQQPQQ-PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT-LLHPLLm 851
                         570       580       590
                  ....*....|....*....|....*....|....
gi 528516427 2296 -----------TTPMPgSMDqghLGTPEQSAMLP 2318
Cdd:PRK10263  852 rngdsrplhkpTTPLP-SLD---LLTPPPSEVEP 881
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
775-884 2.71e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  775 QPNSQTPVSQQQPNANLPLNALGPlgPALGCPTPPQAPLRATPPPNATAASTTnlPAALQPSTPTPAPAQATPPHMQTQA 854
Cdd:PRK14951  383 RPEAAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPAAAPPAPVAAPAAAA--PAAAPAAAPAAVALAPAPPAQAAPE 458
                          90       100       110
                  ....*....|....*....|....*....|
gi 528516427  855 ELPIPGQQHPGTPTGENRVPTPASAASTEL 884
Cdd:PRK14951  459 TVAIPVRVAPEPAVASAAPAPAAAPAAARL 488
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
753-879 3.27e-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: 42.49  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   753 QTQFM-TQPPFPATT--NTMNVNMGQPnsqtPVSQQQPNANLPLNALG-PLGPALGCPTPPQAPLRAT--PPPNATAAST 826
Cdd:TIGR01628  372 QDQFMqLQPRMRQLPmgSPMGGAMGQP----PYYGQGPQQQFNGQPLGwPRMSMMPTPMGPGGPLRPNglAPMNAVRAPS 447
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528516427   827 TNLPAALQPstPTPAPAQATPPHMQTQAELPIPgqQHPGTPTGENRVPTPASA 879
Cdd:TIGR01628  448 RNAQNAAQK--PPMQPVMYPPNYQSLPLSQDLP--QPQSTASQGGQNKKLAQV 496
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
1598-1631 3.41e-03

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


Pssm-ID: 239076  Cd Length: 45  Bit Score: 37.30  E-value: 3.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528516427 1598 YTCNEC-KHHVETRWHCTVCEDFDLCINCYNaKGH 1631
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ-EGR 34
PHA03378 PHA03378
EBNA-3B; Provisional
656-992 3.65e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  656 QPNVMGPRPQNGPV-PMPNVPNQIlnrmQVSQGMNPFSAMSNVPMSQAPMGTRAASPINHQQINMNQVPTmnmSPTRIAP 734
Cdd:PHA03378  634 RPLRMQPITFNVLVfPTPHQPPQV----EITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPR---APTPMRP 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  735 TQGMLGAhggnmvtQTPNQTQFMTQPPFPATTNTMNVNMGQPNSQTPVSQQQPNANLPLNALGPLGPalgcptPPQAPLR 814
Cdd:PHA03378  707 PAAPPGR-------AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP------PAAAPGA 773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  815 ATPPPNATAAsttnlPAALQ----PSTPTPAPaQATPPHMQTQAELPiPGQQHPGTP------TGENRVPTPASAASTEL 884
Cdd:PHA03378  774 PTPQPPPQAP-----PAPQQrprgAPTPQPPP-QAGPTSMQLMPRAA-PGQQGPTKQilrqllTGGVKRGRPSLKKPAAL 846
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  885 HSQHAVPDVPPNDTKTEEQDYDMAVKTEPSTETEEDTGSLLVKK-----------EEQEGSEAKQEPMETEDKKTDLKTE 953
Cdd:PHA03378  847 ERQAAAGPTPSPGSGTSDKIVQAPVFYPPVLQPIQVMRQLGSVRaaaastvtqapTEYTGERRGVGPMHPTDIPPSKRAK 926
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 528516427  954 TKEEDESKtngTASSSPSQSRRKIFkpEELRQALMPTLE 992
Cdd:PHA03378  927 TDAYVESQ---PPHGGQSHSFSVIW--ENVSQGQQQTLE 960
PRK10263 PRK10263
DNA translocase FtsK; Provisional
816-1038 4.12e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  816 TPPPNATAASTT---NLPAALQPSTPTPAPAQATPPHMQTQAEL-PIPGQQHPG---TPTGENRVPTPASAASTELHSQH 888
Cdd:PRK10263  317 TEPVAVAAAATTatqSWAAPVEPVTQTPPVASVDVPPAQPTVAWqPVPGPQTGEpviAPAPEGYPQQSQYAQPAVQYNEP 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  889 --------------------AVPDVPPNDTKTEEQDYDMAVKTEPSTETE---EDTGSLLVKKEEQEGSEAKQEPMETED 945
Cdd:PRK10263  397 lqqpvqpqqpyyapaaeqpaQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwqaEEQQSTFAPQSTYQTEQTYQQPAAQEP 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  946 KKTDLKTETKEEDESKTNGTASSSPSQSRRKIFKP-EELRQALMPTLESLYRQDPEslPFRQPVdPILLGIPDYFDIVKN 1024
Cdd:PRK10263  477 LYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEvEEKRAREREQLAAWYQPIPE--PVKEPE-PIKSSLKAPSVAAVP 553
                         250
                  ....*....|....
gi 528516427 1025 PIDLSTIKRKLDTG 1038
Cdd:PRK10263  554 PVEAAAAVSPLASG 567
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
774-881 4.19e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  774 GQPNSQTPVSQQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPS---TPTPAPAQATPPHM 850
Cdd:PRK07764  397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAaapSAQPAPAPAAAPEP 476
                          90       100       110
                  ....*....|....*....|....*....|.
gi 528516427  851 QTQAElpiPGQQHPGTPTGENRVPTPASAAS 881
Cdd:PRK07764  477 TAAPA---PAPPAAPAPAAAPAAPAAPAAPA 504
PHA03247 PHA03247
large tegument protein UL36; Provisional
662-893 4.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  662 PRPQNGPVPMPNvpnqilNRMQVSQGMNPFSAMSNVPMSQAPMGTRAASPINHQQINMNQVPTMNMSPtriaPTqgmlga 741
Cdd:PHA03247 2769 PAPPAAPAAGPP------RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP----PT------ 2832
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  742 hggnmvtqTPNQTQFMTQPPFPATTNTM--NVNMGQPNSQTPVSQQQP-----NANLPLNALGplGPALGCPT-----PP 809
Cdd:PHA03247 2833 --------SAQPTAPPPPPGPPPPSLPLggSVAPGGDVRRRPPSRSPAakpaaPARPPVRRLA--RPAVSRSTesfalPP 2902
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  810 QAPLRATPPPNATAAsttnLPAALQPSTPTPAPAQATPPHMQTQAElPIPGQQHPGTPTG-------------------- 869
Cdd:PHA03247 2903 DQPERPPQPQAPPPP----QPQPQPPPPPQPQPPPPPPPRPQPPLA-PTTDPAGAGEPSGavpqpwlgalvpgrvavprf 2977
                         250       260
                  ....*....|....*....|....*..
gi 528516427  870 ---ENRVPTPASAASTELHSQHAVPDV 893
Cdd:PHA03247 2978 rvpQPAPSREAPASSTPPLTGHSLSRV 3004
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
775-973 4.94e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.06  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  775 QPNSQTPVSQQQPNANLPLNALGP-------------------LGPALGCPTPPQAPLRATPPPNATAASTTNLPAA-LQ 834
Cdd:NF033839  300 QPSPQPEKKEVKPEPETPKPEVKPqlekpkpevkpqpekpkpeVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVkPQ 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  835 PSTPTPA--PAQATP-PHMQTQAELPIPGQQhpgtPTGENRVPTPASAASTELHSQHAVPDVPPNDTKTEEQDYDMAVKT 911
Cdd:NF033839  380 PETPKPEvkPQPEKPkPEVKPQPEKPKPEVK----PQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKP 455
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  912 EPSTETEEDTGSLLVKKEEQEGSEAKQEPM----ETEDKK----TDLKTETKEEDESKTNGTASSSPSQS 973
Cdd:NF033839  456 QPETPKPEVKPQPEKPKPEVKPQPEKPKPDnskpQADDKKpstpNNLSKDKQPSNQASTNEKATNKPKKS 525
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
783-942 5.11e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   783 SQQQPNANLPLNALGPLGPALGCPTPPQAPLR---ATPPPNATAASTTNLPAALQP---------------STPTPAPAQ 844
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQaatAGPTPSAPSVPPQGSPATSQPpnqtqstaaphtliqQTPTLHPQR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   845 ATPPHMQ-TQAELPIPGQQHPGTPTGENRV-----PTPASAASTELHSQHAVPDVPPNDTKTEEQDydmAVKTEPSTETE 918
Cdd:pfam03154  242 LPSPHPPlQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQS---QVPPGPSPAAP 318
                          170       180
                   ....*....|....*....|....
gi 528516427   919 EDTGSLLVKKEEQEGSEAKQEPME 942
Cdd:pfam03154  319 GQSQQRIHTPPSQSQLQSQQPPRE 342
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
776-921 5.44e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.77  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  776 PNSQTPVSQQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPPNATAASttnlpAALQPSTPTPAPAQATPPHMQTQAE 855
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQA-----PAVPLPETTSQLLAARQQLQRAQGA 435
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528516427  856 LPiPGQQHPGTPTgenrVPTPASAASTELHSQHAVPDVPPNDTKTEEqDYDMAVKTEPSTETEEDT 921
Cdd:PRK07994  436 TK-AKKSEPAAAS----RARPVNSALERLASVRPAPSALEKAPAKKE-AYRWKATNPVEVKKEPVA 495
PHA03247 PHA03247
large tegument protein UL36; Provisional
1775-2323 6.01e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1775 PSPPASTAPSTPTSHQQPNTPQ-TPQP-------------LPNQPTTPNAVVMSPTYPNTPRNGQPLPQASQGKPGPQAS 1840
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRpAPRPsepavtsrarrpdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1841 PLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAVKMARHIEMVAQAQQNyrmtmnglPMNHQQPRMPGAMQPPMQLVGPR 1920
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP--------PQRPRRRAARPTVGSLTSLADPP 2702
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 1921 GQQVM-QPMPQGQWPGGAQPSMPAAQQQVAQQTPQGPQSTLPIQRPAMPQQVAQPrmmvptqgPRPQAPQRAAGIAPnal 1999
Cdd:PHA03247 2703 PPPPTpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP--------ARPPTTAGPPAPAP--- 2771
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2000 qdllrtlkspsspqqqqqvlnilksnpqlmaafikqrtakyhasqpqqqqpqqgihaaqPAMQNMAAMQAVPRPGMAPQQ 2079
Cdd:PHA03247 2772 -----------------------------------------------------------PAAPAAGPPRRLTRPAVASLS 2792
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2080 QQQQPTPQGMAALGPQGQLMNPAPANNPqlqemyrrqllrhqqqqqQQQQQGGMPQAHGQFPQAQGTATNYTQlrmqqQQ 2159
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPP------------------AASPAGPLPPPTSAQPTAPPPPPGPPP-----PS 2849
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2160 LAMQGTGGPMGQL----PPMAQMAMDGTPNllHQRNNLLLQQQQLPQQQVVLKPPMGSQAQPSPMSPQTHLLSGQPQGAH 2235
Cdd:PHA03247 2850 LPLGGSVAPGGDVrrrpPSRSPAAKPAAPA--RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427 2236 LPGQPmanalsnqvcspgpvqsprppsqqppphSSPSPHVQPQPSPQHVPSHTGSPHPGLTTPMPGSMDQGHLGTPEQSA 2315
Cdd:PHA03247 2928 QPQPP----------------------------PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979

                  ....*...
gi 528516427 2316 MLPQLNTP 2323
Cdd:PHA03247 2980 PQPAPSRE 2987
PRK10856 PRK10856
cytoskeleton protein RodZ;
776-881 7.42e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 41.17  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  776 PNSQTPVSQQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAe 855
Cdd:PRK10856  156 QNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGA- 234
                          90       100
                  ....*....|....*....|....*.
gi 528516427  856 lpipgqqhPGTPTGENRVPTPASAAS 881
Cdd:PRK10856  235 --------APLPTDQAGVSTPAADPN 252
PRK10856 PRK10856
cytoskeleton protein RodZ;
807-890 7.88e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.78  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  807 TPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQ--ATPPHMQTQAELPIPGQQHPGTPTGENRVPTPASAASTEL 884
Cdd:PRK10856  169 TTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQnaVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPA 248

                  ....*.
gi 528516427  885 HSQHAV 890
Cdd:PRK10856  249 ADPNAL 254
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
79-168 8.87e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.14  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427   79 KQLSELLRPGSSAGMNSVSPQPG-GIGPQLGGlgksPLGQGSPShPSQTQKPGGTPGTQGNNA--GSAGMGFNQGMLNSG 155
Cdd:cd21118   104 RQAEDIIRHGVDAVHNSWQGSGGhGAYGSQGG----PGVQGHGI-PGGTGGPWASGGNYGTNSlgGSVGQGGNGGPLNYG 178
                          90
                  ....*....|...
gi 528516427  156 MMGQNAGAQGGQV 168
Cdd:cd21118   179 TNSQGAVAQPGYG 191
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
806-904 9.94e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.24  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528516427  806 PTPPQAPLRATPPPNATAASTTNLPAAlqPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTGENRVPTPASAAS---- 881
Cdd:PRK14951  395 AQAAAAPAPAAAPAAAASAPAAPPAAA--PPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPepav 472
                          90       100
                  ....*....|....*....|...
gi 528516427  882 TELHSQHAVPDVPPNDTKTEEQD 904
Cdd:PRK14951  473 ASAAPAPAAAPAAARLTPTEEGD 495
 
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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