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Conserved domains on  [gi|325190525|emb|CCA25024|]
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conserved hypothetical protein [Albugo laibachii Nc14]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
330-848 7.64e-42

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 159.69  E-value: 7.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  330 RRLKVVNGHlQIPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIW 409
Cdd:COG2319    69 ALLATLLGH-TAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  410 ELGSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGrcfcyklpeiplkqsgqyetrqQIaqRLISLnafcLSLRPIYS 489
Cdd:COG2319   148 DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG----------------------TV--RLWDL----ATGKLLRT 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  490 LShfnHHSTRsnkVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVsvlsdpnvsipiqneamqgsE 569
Cdd:COG2319   200 LT---GHTGA---VRSVAF-------------------SPDGKLLASGSADGTVRLWDL--------------------A 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  570 TTHEQAVLNPDEDHSYRlnlvpLEVSPsrsqetnNGsdpheapiastefesitmRRAVlpafdtstpfTSTIDASIprtq 649
Cdd:COG2319   235 TGKLLRTLTGHSGSVRS-----VAFSP-------DG------------------RLLA----------SGSADGTV---- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  650 lqppeRLresmWsingilvpRLSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWsyhptkfsnpnNVNPNl 729
Cdd:COG2319   271 -----RL----W--------DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS-DDGTVRLW-----------DLATG- 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  730 ahKVLFTHEPWTAqdgsgryrriktlAVDTLCWTKDDKRLITlhsvkaeshheiVDWKQRIRIWDPNKGTEVYTLAaids 809
Cdd:COG2319   321 --KLLRTLTGHTG-------------AVRSVAFSPDGKTLAS------------GSDDGTVRLWDLATGELLRTLT---- 369
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 325190525  810 arqhGHVNAVFALDVHPhDWRLAITAGYDGRICLWDISS 848
Cdd:COG2319   370 ----GHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLAT 403
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
1279-1388 8.72e-21

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.


:

Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 89.57  E-value: 8.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHsdDGGIMKlpsesmGVHPLINGCQRVFVHDQCAIASPLCFHRDESWY---NVAKEIRRGRKLECSVCHNK-GAT 1354
Cdd:cd15571     1 CALCPR--SGGALK------GGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLeveGVSKIPKRRKKLKCSICGKRgGAC 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 325190525 1355 IGCCVPECRSVYHWKCALTCGWSLNKS------QFYCPSH 1388
Cdd:cd15571    73 IQCSYPGCPRSFHVSCAIRAGCLFEFEdgpgnfVVYCPKH 112
BROMO smart00297
bromo domain;
1921-2023 6.38e-19

bromo domain;


:

Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 83.87  E-value: 6.38e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525   1921 KNYENLQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEY 1998
Cdd:smart00297    3 KLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENgkYSSVEEFVADFNLMFSNARTY 82
                            90       100
                    ....*....|....*....|....*
gi 325190525   1999 NGKSSEIGLLAMELQQASMKMLTNL 2023
Cdd:smart00297   83 NGPDSEVYKDAKKLEKFFEKKLREL 107
Bromodomain super family cl02556
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1656-1784 1.04e-08

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


The actual alignment was detected with superfamily member cd05529:

Pssm-ID: 445827  Cd Length: 128  Bit Score: 55.42  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1656 SPWELEPLGTRSRQDkqrRDCEREDsvLFRsrrfdgaiQLAMLTEINNimeLSISRDFVDAVDESFL--DYLITIANPIN 1733
Cdd:cd05529     7 SEWELFDPGWEQPHI---RDEERER--LIS--------GLDKLLLSLQ---LEIAEYFEYPVDLRAWypDYWNRVPVPMD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1734 LTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNARTICNTL 1784
Cdd:cd05529    71 LETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWL 121
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
330-848 7.64e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 159.69  E-value: 7.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  330 RRLKVVNGHlQIPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIW 409
Cdd:COG2319    69 ALLATLLGH-TAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  410 ELGSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGrcfcyklpeiplkqsgqyetrqQIaqRLISLnafcLSLRPIYS 489
Cdd:COG2319   148 DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG----------------------TV--RLWDL----ATGKLLRT 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  490 LShfnHHSTRsnkVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVsvlsdpnvsipiqneamqgsE 569
Cdd:COG2319   200 LT---GHTGA---VRSVAF-------------------SPDGKLLASGSADGTVRLWDL--------------------A 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  570 TTHEQAVLNPDEDHSYRlnlvpLEVSPsrsqetnNGsdpheapiastefesitmRRAVlpafdtstpfTSTIDASIprtq 649
Cdd:COG2319   235 TGKLLRTLTGHSGSVRS-----VAFSP-------DG------------------RLLA----------SGSADGTV---- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  650 lqppeRLresmWsingilvpRLSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWsyhptkfsnpnNVNPNl 729
Cdd:COG2319   271 -----RL----W--------DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS-DDGTVRLW-----------DLATG- 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  730 ahKVLFTHEPWTAqdgsgryrriktlAVDTLCWTKDDKRLITlhsvkaeshheiVDWKQRIRIWDPNKGTEVYTLAaids 809
Cdd:COG2319   321 --KLLRTLTGHTG-------------AVRSVAFSPDGKTLAS------------GSDDGTVRLWDLATGELLRTLT---- 369
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 325190525  810 arqhGHVNAVFALDVHPhDWRLAITAGYDGRICLWDISS 848
Cdd:COG2319   370 ----GHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
332-713 1.58e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 135.16  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  332 LKVVNGHLQiPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWEL 411
Cdd:cd00200     2 RRTLKGHTG-GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  412 GSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCYKLPEIPLKQSgqyetrqqiaqrlislnafclslrpiysls 491
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT------------------------------ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  492 hFNHHstrSNKVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVSVLSdpnvsiPIQNeaMQGsett 571
Cdd:cd00200   131 -LRGH---TDWVNSVAF-------------------SPDGTFVASSSQDGTIKLWDLRTGK------CVAT--LTG---- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  572 HEQAV----LNPDE--------DHSYRLnlvpLEVSPSRSQETNNGsdpHEAPIastefesitmrRAVLPAFDTSTPFTS 639
Cdd:cd00200   176 HTGEVnsvaFSPDGekllssssDGTIKL----WDLSTGKCLGTLRG---HENGV-----------NSVAFSPDGYLLASG 237
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325190525  640 TIDASIprtqlqpperlreSMWsingilvpRLSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWS 713
Cdd:cd00200   238 SEDGTI-------------RVW--------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGS-ADGTIRIWD 289
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
1279-1388 8.72e-21

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 89.57  E-value: 8.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHsdDGGIMKlpsesmGVHPLINGCQRVFVHDQCAIASPLCFHRDESWY---NVAKEIRRGRKLECSVCHNK-GAT 1354
Cdd:cd15571     1 CALCPR--SGGALK------GGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLeveGVSKIPKRRKKLKCSICGKRgGAC 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 325190525 1355 IGCCVPECRSVYHWKCALTCGWSLNKS------QFYCPSH 1388
Cdd:cd15571    73 IQCSYPGCPRSFHVSCAIRAGCLFEFEdgpgnfVVYCPKH 112
BROMO smart00297
bromo domain;
1921-2023 6.38e-19

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 83.87  E-value: 6.38e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525   1921 KNYENLQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEY 1998
Cdd:smart00297    3 KLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENgkYSSVEEFVADFNLMFSNARTY 82
                            90       100
                    ....*....|....*....|....*
gi 325190525   1999 NGKSSEIGLLAMELQQASMKMLTNL 2023
Cdd:smart00297   83 NGPDSEVYKDAKKLEKFFEKKLREL 107
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1926-2020 5.45e-18

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: 80.92  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1926 LQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSS 2003
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGFFAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNndYQSIEEFKDDFKLMCENAMKYNKPDT 81
                          90
                  ....*....|....*..
gi 325190525 2004 EIGLLAMELQQASMKML 2020
Cdd:cd05513    82 IYYKAAKKLLHSGMKIL 98
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
1313-1388 1.76e-14

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 70.44  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1313 HDQCAIASP-LCF----HRDESWYNVAKEIRRGRKLECSVCHNK-GATIGCCVPECRSVYHWKCALTCGW------SLNK 1380
Cdd:pfam13771    1 HVVCALWSPeLVQrgndSMGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLlmqfdeDNGT 80

                   ....*...
gi 325190525  1381 SQFYCPSH 1388
Cdd:pfam13771   81 FKSYCKKH 88
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1930-2011 2.39e-12

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: 64.26  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1930 LKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLAR--MSSYRSFSTYFENLRLVFQNAIEYNGKSSEIGL 2007
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKleNGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80

                   ....
gi 325190525  2008 LAME 2011
Cdd:pfam00439   81 AAEK 84
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1656-1784 1.04e-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: 55.42  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1656 SPWELEPLGTRSRQDkqrRDCEREDsvLFRsrrfdgaiQLAMLTEINNimeLSISRDFVDAVDESFL--DYLITIANPIN 1733
Cdd:cd05529     7 SEWELFDPGWEQPHI---RDEERER--LIS--------GLDKLLLSLQ---LEIAEYFEYPVDLRAWypDYWNRVPVPMD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1734 LTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNARTICNTL 1784
Cdd:cd05529    71 LETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWL 121
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1899-2035 1.17e-08

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 59.43  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1899 EILSLEELLQKLTTNQREVVCTKNYEN--LQGLLKK--LHEGLMAADEF--------SIFASPVTDDIAPGYSKRIQDPM 1966
Cdd:COG5076   110 ESVTPESGLGSLLMAHLKTSVKKRKTPkiEDELLYAdnKAIAKFKKQLFlrdgrflsSIFLGLPSKREYPDYYEIIKSPM 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1967 DFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQQASMKMLTNLVDENLQSKRKRR 2035
Cdd:COG5076   190 DLLTIQKKLKNgrYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEEMLELSIKPG 260
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1697-1779 2.70e-08

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: 53.09  E-value: 2.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1697 MLTEINNIMELSISRDFVDAVD-ESFLDYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQ 1775
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDpDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80

                   ....
gi 325190525  1776 NART 1779
Cdd:pfam00439   81 AAEK 84
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
371-410 3.54e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 51.16  E-value: 3.54e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 325190525    371 TGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWE 410
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
372-410 9.38e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 9.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 325190525   372 GYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWE 410
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
378-443 1.28e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 325190525  378 LRGHNGNVTDLAVN-CSDTLLASSSDDKTIRIWELGSG--------APVAVLIGHSSVVNSVRFHPSKNVVLSAS 443
Cdd:PTZ00420   70 LKGHTSSILDLQFNpCFSEILASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDWNPMNYYIMCSS 144
BROMO smart00297
bromo domain;
1693-1780 1.42e-04

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 43.04  E-value: 1.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525   1693 IQLAMLTEINNIMELSISRDFVDAVDESFL-DYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESS 1771
Cdd:smart00297    8 LQELLKAVLDKLDSHPLSWPFLKPVSRKEApDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDS 87

                    ....*....
gi 325190525   1772 TIAQNARTI 1780
Cdd:smart00297   88 EVYKDAKKL 96
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1276-1396 7.90e-04

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1276 LIVCAFCGHSDdgGIMKLPSESMGVHPLingcqrvfvhdqCAIASP-LCFH---RDESWYNVAKEIRRGRKLECSVCHNK 1351
Cdd:COG5141   247 IRCCSFCPSSD--GAFKQTSDGRWGHVI------------CAMFNPeLSFGhllSKDPIDNIASVSSSRWKLGCLICKEF 312
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1352 GAT-IGCCVPECRSVYHWKCALTCGW----SLNKSQF-YCPSHEELDDNAT 1396
Cdd:COG5141   313 GGTcIQCSYFNCTRAYHVTCARRAGYfdlnIYSHNGIsYCIDHEPLCRKHY 363
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1345-1388 1.16e-03

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 1.16e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 325190525   1345 CSVC---HNKGATIGCCvpECRSVYHWKCA-LTCGWSLNKSQFYCPSH 1388
Cdd:smart00249    2 CSVCgkpDDGGELLQCD--GCDRWYHQTCLgPPLLEEEPDGKWYCPKC 47
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
330-848 7.64e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 159.69  E-value: 7.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  330 RRLKVVNGHlQIPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIW 409
Cdd:COG2319    69 ALLATLLGH-TAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  410 ELGSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGrcfcyklpeiplkqsgqyetrqQIaqRLISLnafcLSLRPIYS 489
Cdd:COG2319   148 DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG----------------------TV--RLWDL----ATGKLLRT 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  490 LShfnHHSTRsnkVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVsvlsdpnvsipiqneamqgsE 569
Cdd:COG2319   200 LT---GHTGA---VRSVAF-------------------SPDGKLLASGSADGTVRLWDL--------------------A 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  570 TTHEQAVLNPDEDHSYRlnlvpLEVSPsrsqetnNGsdpheapiastefesitmRRAVlpafdtstpfTSTIDASIprtq 649
Cdd:COG2319   235 TGKLLRTLTGHSGSVRS-----VAFSP-------DG------------------RLLA----------SGSADGTV---- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  650 lqppeRLresmWsingilvpRLSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWsyhptkfsnpnNVNPNl 729
Cdd:COG2319   271 -----RL----W--------DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS-DDGTVRLW-----------DLATG- 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  730 ahKVLFTHEPWTAqdgsgryrriktlAVDTLCWTKDDKRLITlhsvkaeshheiVDWKQRIRIWDPNKGTEVYTLAaids 809
Cdd:COG2319   321 --KLLRTLTGHTG-------------AVRSVAFSPDGKTLAS------------GSDDGTVRLWDLATGELLRTLT---- 369
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 325190525  810 arqhGHVNAVFALDVHPhDWRLAITAGYDGRICLWDISS 848
Cdd:COG2319   370 ----GHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
351-876 1.17e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.59  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  351 AGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWELGSGAPVAVLIGHSSVVNSV 430
Cdd:COG2319    47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  431 RFHPSKNVVLSASDDGrcfcyklpEIplkqsgqyetrqqiaqRLISLNafclSLRPIYSLShfnHHSTRsnkVLCLAFrc 510
Cdd:COG2319   127 AFSPDGKTLASGSADG--------TV----------------RLWDLA----TGKLLRTLT---GHSGA---VTSVAF-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  511 vedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVsvlsdpnvsipiqneamqgsETTHEQAVLnpdEDHSYRLNLV 590
Cdd:COG2319   171 -----------------SPDGKLLASGSDDGTVRLWDL--------------------ATGKLLRTL---TGHTGAVRSV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  591 plEVSPSRSQetnngsdpheapIAStefesitmrravlpafdtstpftstidASIPRTqlqpperlresmwsingILVPR 670
Cdd:COG2319   211 --AFSPDGKL------------LAS---------------------------GSADGT-----------------VRLWD 232
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  671 LSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWsyhptkfsnpnNVNPNLAHKVLFTHEPWtaqdgsgryr 750
Cdd:COG2319   233 LATGKLLRTLTGHSGSVRSVAFSPDGRLLASGS-ADGTVRLW-----------DLATGELLRTLTGHSGG---------- 290
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  751 riktlaVDTLCWTKDDKRLITlhsvkaeshheiVDWKQRIRIWDPNKGTEVYTLAaidsarqhGHVNAVFALDVHPHDWR 830
Cdd:COG2319   291 ------VNSVAFSPDGKLLAS------------GSDDGTVRLWDLATGKLLRTLT--------GHTGAVRSVAFSPDGKT 344
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 325190525  831 LAiTAGYDGRICLWDISSGRLLKQFINSSTneeciPLLDGGFMPDG 876
Cdd:COG2319   345 LA-SGSDDGTVRLWDLATGELLRTLTGHTG-----AVTSVAFSPDG 384
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
332-713 1.58e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 135.16  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  332 LKVVNGHLQiPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWEL 411
Cdd:cd00200     2 RRTLKGHTG-GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  412 GSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCYKLPEIPLKQSgqyetrqqiaqrlislnafclslrpiysls 491
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT------------------------------ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  492 hFNHHstrSNKVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWDVSVLSdpnvsiPIQNeaMQGsett 571
Cdd:cd00200   131 -LRGH---TDWVNSVAF-------------------SPDGTFVASSSQDGTIKLWDLRTGK------CVAT--LTG---- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  572 HEQAV----LNPDE--------DHSYRLnlvpLEVSPSRSQETNNGsdpHEAPIastefesitmrRAVLPAFDTSTPFTS 639
Cdd:cd00200   176 HTGEVnsvaFSPDGekllssssDGTIKL----WDLSTGKCLGTLRG---HENGV-----------NSVAFSPDGYLLASG 237
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325190525  640 TIDASIprtqlqpperlreSMWsingilvpRLSNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWS 713
Cdd:cd00200   238 SEDGTI-------------RVW--------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGS-ADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
330-547 2.85e-30

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 122.83  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  330 RRLKVVNGHLQiPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIW 409
Cdd:cd00200    84 ECVRTLTGHTS-YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  410 ELGSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCYKLPEIPLKQSGQYETRQQIAQRLISLNAFCLSLRPIYS 489
Cdd:cd00200   163 DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 325190525  490 LSHFNHHSTR--------SNKVLCLAFrcvedeyipiktiltvlirSRCGKFVITGGQDGIGRVWD 547
Cdd:cd00200   243 IRVWDLRTGEcvqtlsghTNSVTSLAW-------------------SPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
329-447 1.45e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 103.18  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  329 FRRLKVVNGHlQIPAYCLTYDNAGKFAITGADDRLIKIWCLQTGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRI 408
Cdd:cd00200   167 GKCVATLTGH-TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 325190525  409 WELGSGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGR 447
Cdd:cd00200   246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
1279-1388 8.72e-21

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 89.57  E-value: 8.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHsdDGGIMKlpsesmGVHPLINGCQRVFVHDQCAIASPLCFHRDESWY---NVAKEIRRGRKLECSVCHNK-GAT 1354
Cdd:cd15571     1 CALCPR--SGGALK------GGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLeveGVSKIPKRRKKLKCSICGKRgGAC 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 325190525 1355 IGCCVPECRSVYHWKCALTCGWSLNKS------QFYCPSH 1388
Cdd:cd15571    73 IQCSYPGCPRSFHVSCAIRAGCLFEFEdgpgnfVVYCPKH 112
BROMO smart00297
bromo domain;
1921-2023 6.38e-19

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 83.87  E-value: 6.38e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525   1921 KNYENLQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEY 1998
Cdd:smart00297    3 KLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENgkYSSVEEFVADFNLMFSNARTY 82
                            90       100
                    ....*....|....*....|....*
gi 325190525   1999 NGKSSEIGLLAMELQQASMKMLTNL 2023
Cdd:smart00297   83 NGPDSEVYKDAKKLEKFFEKKLREL 107
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1926-2020 5.45e-18

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: 80.92  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1926 LQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSS 2003
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGFFAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNndYQSIEEFKDDFKLMCENAMKYNKPDT 81
                          90
                  ....*....|....*..
gi 325190525 2004 EIGLLAMELQQASMKML 2020
Cdd:cd05513    82 IYYKAAKKLLHSGMKIL 98
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1926-2020 6.05e-18

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: 80.88  E-value: 6.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1926 LQGLLKKLHEglMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSS 2003
Cdd:cd04369     5 LRSLLDALKK--LKRDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNgeYKSLEEFEADVRLIFSNAKTYNGPGS 82
                          90
                  ....*....|....*..
gi 325190525 2004 EIGLLAMELQQASMKML 2020
Cdd:cd04369    83 PIYKDAKKLEKLFEKLL 99
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
1279-1388 7.19e-17

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277134  Cd Length: 105  Bit Score: 78.22  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGgimklpsESMGVHPLINGCQRVFVHDQCAIASPLCFHRDE-SWYNVAKEIRRGRKLECSVCHNKGATIGC 1357
Cdd:cd15664     1 CALCGVYGDD-------EPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDgSLQNVHSAVSRGRMMKCELCGKPGATVGC 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 325190525 1358 CVPECRSVYHWKCA--LTCGWSLNKSqFYCPSH 1388
Cdd:cd15664    74 CLKSCPANYHFMCArkAECVFQDDKK-VFCPAH 105
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
416-880 5.17e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 5.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  416 PVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCYKLpeiplkQSGQYETRQQIaqrlislnafclslrpiyslshfnh 495
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL------ETGELLRTLKG------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  496 HStrsnkvlclafrcvedeyIPIKTILTvlirSRCGKFVITGGQDGIGRVWDvsvlsdpnvsipIQNEAMQGSETTHEQA 575
Cdd:cd00200    50 HT------------------GPVRDVAA----SADGTYLASGSSDKTIRLWD------------LETGECVRTLTGHTSY 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  576 VLNPDedhsyrlnlvpleVSPSRsqetnngsdpheaPIAStefesitmrravlpafdtstpfTSTIDASIprtqlqpper 655
Cdd:cd00200    96 VSSVA-------------FSPDG-------------RILS----------------------SSSRDKTI---------- 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  656 lreSMWSINgilvprlsNGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWSYHPTKFSnpnnvnpnlahKVLF 735
Cdd:cd00200   118 ---KVWDVE--------TGKCLTTLRGHTDWVNSVAFSPDGTFVASSS-QDGTIKLWDLRTGKCV-----------ATLT 174
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  736 THEPWtaqdgsgryrriktlaVDTLCWTKDDKRLITLHSVKAeshheivdwkqrIRIWDPNKGTEVYTLaaidsarqHGH 815
Cdd:cd00200   175 GHTGE----------------VNSVAFSPDGEKLLSSSSDGT------------IKLWDLSTGKCLGTL--------RGH 218
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 325190525  816 VNAVFALDVHPHDwRLAITAGYDGRICLWDISSGRLLKQFinSSTNEECIPLldgGFMPDGSGFC 880
Cdd:cd00200   219 ENGVNSVAFSPDG-YLLASGSEDGTIRVWDLRTGECVQTL--SGHTNSVTSL---AWSPDGKRLA 277
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
1279-1388 1.93e-15

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome.


Pssm-ID: 277138  Cd Length: 103  Bit Score: 73.88  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSddggimklpSESMGVHPLINGCQRVFVHDQCAIASPLCFHRDESWYNVAKEIRRGRKLECSVCHNKGATIGCC 1358
Cdd:cd15668     1 CVFCKRG---------PHYKGLGDLFGPYYEVWVHEDCAVWAPGVYLVGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCL 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 325190525 1359 VPECRSVYHWKCALTCGWSLNKSQF--YCPSH 1388
Cdd:cd15668    72 HKGCKAKYHYPCAVESGCQLDEENFslLCPKH 103
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
1279-1388 3.63e-15

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific PHD finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a PHD finger and a non-canonical ePHD finger, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger.


Pssm-ID: 277139 [Multi-domain]  Cd Length: 112  Bit Score: 73.44  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDggimklpsesmgvHPLINGCQRVF----VHDQCAIASPLCFHR---DESWYN-----VAKEIRRGRKLECS 1346
Cdd:cd15669     1 CVLCGRSDD-------------DPDKYGEKLQKdgicAHYFCLLFSSGLPQRgedNEGIYGflpedIRKEVRRASRLRCF 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 325190525 1347 VCHNKGATIGCCVPECRSVYHWKCALTCGwslNKSQF------YCPSH 1388
Cdd:cd15669    68 YCKKKGASIGCAVKGCRRSFHFPCGLENG---CVTQFfgeyrsFCWEH 112
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
1279-1388 6.99e-15

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277143  Cd Length: 116  Bit Score: 72.81  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDggimklpSESMGvhPLINGCQRVFVHDQCAIASPLCFHRDESWYN---------VAKEIRRGRKLECSVCH 1349
Cdd:cd15673     1 CGFCKSGEE-------NKETG--GKLASGEKIAAHHNCMLFSSGLVQYVSPNENdfggfdiedVKKEIKRGRKLKCNLCK 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 325190525 1350 NKGATIGCCVPECRSVYHWKCALTCG--WSLNKSQ----FYCPSH 1388
Cdd:cd15673    72 KTGATIGCDVKQCKKTYHYHCAKKDDakIIERNSQgiyrVYCKNH 116
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
1313-1388 1.76e-14

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 70.44  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1313 HDQCAIASP-LCF----HRDESWYNVAKEIRRGRKLECSVCHNK-GATIGCCVPECRSVYHWKCALTCGW------SLNK 1380
Cdd:pfam13771    1 HVVCALWSPeLVQrgndSMGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLlmqfdeDNGT 80

                   ....*...
gi 325190525  1381 SQFYCPSH 1388
Cdd:pfam13771   81 FKSYCKKH 88
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
1279-1388 1.99e-14

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277136  Cd Length: 105  Bit Score: 71.18  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGgimklpsESMGVHPLINGCQRVFVHDQCAIASplcfhrDE-------SWYNVAKEIRRGRKLECSVCHNK 1351
Cdd:cd15666     1 CVLCGGEGDG-------DTDGPGRLLNLDVDKWVHLNCALWS------YEvyetqngALMNVEEALRRALTTTCSHCGRT 67
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 325190525 1352 GATIGCCVPECRSVYHWKCALTCGWSLNKSQ-FYCPSH 1388
Cdd:cd15666    68 GATVPCFKPRCANVYHLPCAIKDGCMFFKDKtMLCPSH 105
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
1279-1372 5.89e-14

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .


Pssm-ID: 277180  Cd Length: 115  Bit Score: 69.99  E-value: 5.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGGIMKLpsesmgvhpLINGCQRVFVHDQCAIASP--LCFHRDE------SWYNVAKEIRRGRKLECSVCHN 1350
Cdd:cd15710     1 CGFCRSNREKECGQL---------LISENQKVAAHHKCMLFSSalVSSHSDSenlggfSIEDVQKEIKRGTKLMCSLCHC 71
                          90       100
                  ....*....|....*....|..
gi 325190525 1351 KGATIGCCVPECRSVYHWKCAL 1372
Cdd:cd15710    72 PGATIGCDVKTCHRTYHYYCAL 93
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
1308-1391 9.44e-13

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277163  Cd Length: 113  Bit Score: 66.56  E-value: 9.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1308 QRVFVHDQCAIASPLCFHRDE-SWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCAL--TCGWsLNKSQFY 1384
Cdd:cd15693    25 QNEWTHVNCALWSAEVFEDDDgSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRakNCVF-LEDKKVY 103

                  ....*..
gi 325190525 1385 CPSHEEL 1391
Cdd:cd15693   104 CQRHKDL 110
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1930-2011 2.39e-12

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: 64.26  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1930 LKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLAR--MSSYRSFSTYFENLRLVFQNAIEYNGKSSEIGL 2007
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKleNGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80

                   ....
gi 325190525  2008 LAME 2011
Cdd:pfam00439   81 AAEK 84
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
1279-1372 1.43e-11

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 63.38  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGGIMKLPSEsmgvhplingcQRVFVHDQCAIAS----------PLCFHRDESWYNVAKEIRRGRKLECSVC 1348
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQE-----------QNIAAHQNCLLYSsgfveseeynPLNLDRRFDVESVLNEIKRGKRLKCNFC 69
                          90       100
                  ....*....|....*....|....
gi 325190525 1349 HNKGATIGCCVPECRSVYHWKCAL 1372
Cdd:cd15712    70 RKKGATVGCEERACRRSYHYFCAL 93
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
1279-1388 2.86e-11

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277164  Cd Length: 105  Bit Score: 61.98  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGgimklPSESMGvhPLINGCQRVFVHDQCAIASPLCFHR-DESWYNVAKEIRRGRKLECSVCHNKGATIGC 1357
Cdd:cd15694     1 CALCLKYGDA-----DSKDAG--RLLYIGQNEWTHVNCAIWSAEVFEEnDGSLKNVHAAVARGRQMRCEHCQKIGATVGC 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 325190525 1358 CVPECRSVYHWKCALT--CGWSLNKSQFyCPSH 1388
Cdd:cd15694    74 CLSACLSNFHFMCARAsrCCFQDDKKVF-CQKH 105
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1921-2023 7.94e-11

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: 60.65  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1921 KNYENLQGLLKKLHEGLMAADefsiFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEY 1998
Cdd:cd05509     1 PLYTQLKKVLDSLKNHKSAWP----FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENgyYVTLEEFVADLKLIFDNCRLY 76
                          90       100
                  ....*....|....*....|....*
gi 325190525 1999 NGKSSEIGLLAMELQQASMKMLTNL 2023
Cdd:cd05509    77 NGPDTEYYKCANKLEKFFWKKLKEL 101
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1944-2018 1.20e-10

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: 60.46  E-value: 1.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325190525 1944 SIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQQASMK 2018
Cdd:cd05507    22 SVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENgtIRSTAEFQRDVLLMFQNAIMYNSSDHDVYLMAVEMQREVMS 98
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
1306-1388 1.81e-10

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277135  Cd Length: 90  Bit Score: 59.26  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1306 GCQRVFVHDQCAIASP-LCFHRDESWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCALTCGWSLNKSQF- 1383
Cdd:cd15665     5 NLGEVYAHHCCAAWSEgVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCFQDIKTLt 84

                  ....*.
gi 325190525 1384 -YCPSH 1388
Cdd:cd15665    85 lFCPEH 90
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1946-2005 4.75e-10

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: 58.32  E-value: 4.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325190525 1946 FASPVTDDIAPGYSKRIQDPMDFGTMLARMS--SYRSFSTYFENLRLVFQNAIEYNGKSSEI 2005
Cdd:cd05505    21 FREPVTADEAEDYKKVITNPMDLQTMQTKCScgSYSSVQEFLDDMKLVFSNAEKYYENGSYV 82
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1926-2001 4.92e-10

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: 58.18  E-value: 4.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325190525 1926 LQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGK 2001
Cdd:cd05512     2 LEVLLRKTLDQLQEKDTAEIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESqrYRTLEDFEADFNLIINNCLAYNAK 79
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
1279-1388 1.30e-09

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.


Pssm-ID: 277167  Cd Length: 105  Bit Score: 57.36  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCgHSDDGGIMKLPSEsmgvhpLINGCQRVFVHDQCAIASPLCFHRDE-SWYNVAKEIRRGRKLECSVCHNKGATIGC 1357
Cdd:cd15697     1 CCFC-HEEGDGLTDGPAR------LLNLDLDLWVHLNCALWSTEVYETQAgALINVELALRRGLQMKCVFCHKTGATSGC 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 325190525 1358 CVPECRSVYHWKCALTCGWSLNKSQ-FYCPSH 1388
Cdd:cd15697    74 HRLRCTNVYHFTCAIKAQCMFFKDKtMLCPMH 105
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1930-2015 6.94e-09

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: 55.40  E-value: 6.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1930 LKKLHEGLMaadefsiFASPVtDDIA---PGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSE 2004
Cdd:cd05500    16 LKRLKDARP-------FLVPV-DPVKlniPHYPTIIKKPMDLGTIERKLKSnvYTSVEEFTADFNLMVDNCLTFNGPEHP 87
                          90
                  ....*....|.
gi 325190525 2005 IGLLAMELQQA 2015
Cdd:cd05500    88 VSQMGKRLQAA 98
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1656-1784 1.04e-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: 55.42  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1656 SPWELEPLGTRSRQDkqrRDCEREDsvLFRsrrfdgaiQLAMLTEINNimeLSISRDFVDAVDESFL--DYLITIANPIN 1733
Cdd:cd05529     7 SEWELFDPGWEQPHI---RDEERER--LIS--------GLDKLLLSLQ---LEIAEYFEYPVDLRAWypDYWNRVPVPMD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1734 LTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNARTICNTL 1784
Cdd:cd05529    71 LETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWL 121
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1925-2026 1.07e-08

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: 55.06  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1925 NLQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSSYRSFST--YFENLRLVFQNAIEYNGKS 2002
Cdd:cd05528     3 ELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAkdFLKDIDLIVTNALEYNPDR 82
                          90       100
                  ....*....|....*....|....*...
gi 325190525 2003 SEIGLL----AMELQQASMKMLTNLVDE 2026
Cdd:cd05528    83 DPADKLirsrACELRDEVHAMIEAELDP 110
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1899-2035 1.17e-08

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 59.43  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1899 EILSLEELLQKLTTNQREVVCTKNYEN--LQGLLKK--LHEGLMAADEF--------SIFASPVTDDIAPGYSKRIQDPM 1966
Cdd:COG5076   110 ESVTPESGLGSLLMAHLKTSVKKRKTPkiEDELLYAdnKAIAKFKKQLFlrdgrflsSIFLGLPSKREYPDYYEIIKSPM 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1967 DFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQQASMKMLTNLVDENLQSKRKRR 2035
Cdd:COG5076   190 DLLTIQKKLKNgrYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEEMLELSIKPG 260
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1946-2006 1.45e-08

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: 54.30  E-value: 1.45e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325190525 1946 FASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIG 2006
Cdd:cd05503    21 FLEPVNTKLVPGYRKIIKKPMDFSTIREKLESgqYKTLEEFAEDVRLVFDNCETFNEDDSEVG 83
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1929-2012 1.54e-08

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: 54.26  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1929 LLKKLheglmAADEFS-IFASPVtDDIA---PGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKS 2002
Cdd:cd05506     8 LLRKL-----MKHKWGwVFNAPV-DVVAlglPDYFDIIKKPMDLGTVKKKLEKgeYSSPEEFAADVRLTFANAMRYNPPG 81
                          90
                  ....*....|
gi 325190525 2003 SEIGLLAMEL 2012
Cdd:cd05506    82 NDVHTMAKEL 91
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
1311-1388 2.47e-08

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes.


Pssm-ID: 277170  Cd Length: 104  Bit Score: 53.73  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1311 FVHDQCAIASPLCFHRDESWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCALTCGWSLNKSQFY--CPSH 1388
Cdd:cd15700    25 WVHEACAVWTTGVYLVAGKLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSlrCPKH 104
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1697-1779 2.70e-08

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: 53.09  E-value: 2.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1697 MLTEINNIMELSISRDFVDAVD-ESFLDYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQ 1775
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDpDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80

                   ....
gi 325190525  1776 NART 1779
Cdd:pfam00439   81 AAEK 84
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
371-410 3.54e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 51.16  E-value: 3.54e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 325190525    371 TGYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWE 410
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1946-2013 6.23e-08

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: 52.78  E-value: 6.23e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1946 FASPVTDDIAPGYSKRIQDPMDFGTMLAR--MSSYRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQ 2013
Cdd:cd05504    33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKlnMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQ 102
WD40 pfam00400
WD domain, G-beta repeat;
372-410 9.38e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 9.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 325190525   372 GYLQYTLRGHNGNVTDLAVNCSDTLLASSSDDKTIRIWE 410
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1926-2019 1.30e-07

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: 51.88  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1926 LQGLLKKLHEGLMAADEFSIFASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSS 2003
Cdd:cd05511     1 LSFILDEIVNELKNLPDSWPFHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKhkYQSREEFLEDIELIVDNSVLYNGPDS 80
                          90
                  ....*....|....*..
gi 325190525 2004 EIGLLAME-LQQASMKM 2019
Cdd:cd05511    81 VYTKKAKEmLELAEELL 97
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
1279-1389 1.54e-07

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.


Pssm-ID: 277168  Cd Length: 107  Bit Score: 51.59  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSDDGGimklpseSMGVHPLINGCQRVFVHDQCAIASPLCFH-RDESWYNVAKEIRRGRKLECSVCHNKGATIGC 1357
Cdd:cd15698     1 CCFCHEEGDGA-------TDGPARLLNLDLDLWVHLNCALWSTEVYEtQGGALMNVEVALHRGLLTKCSLCQKTGATNSC 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 325190525 1358 CVPECRSVYHWKCAL--TCGWSLNKSQFyCPSHE 1389
Cdd:cd15698    74 NRLRCPNVYHFACAIraKCMFFKDKTML-CPMHK 106
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
673-713 3.12e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.46  E-value: 3.12e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 325190525    673 NGEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWS 713
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGS-DDGTIKLWD 40
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
1307-1388 4.01e-07

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.


Pssm-ID: 277166  Cd Length: 90  Bit Score: 49.94  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1307 CQRVFVHDQCAIASPLCFHRDE-SWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCALTCGWSLNKSQFY- 1384
Cdd:cd15696     6 CGECWAHLRCAEWSLGVCQGEEqLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLl 85

                  ....*
gi 325190525 1385 -CPSH 1388
Cdd:cd15696    86 lCPTH 90
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
1279-1388 5.07e-07

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277141  Cd Length: 112  Bit Score: 50.13  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCghSDDGGIMKlpsesmgvhPLINGCQrvFVHDQCAIASP----LCFHRDESWYNVAKeIRRGRK-LECSVCHNK-G 1352
Cdd:cd15671     1 CVLC--PKKGGAMK---------STKSGTK--WVHVSCALWIPevsiGCPEKMEPITKISH-IPMSRWaLVCVLCKEKtG 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 325190525 1353 ATIGCCVPECRSVYHWKCALTCGWSLN----------KSQFYCPSH 1388
Cdd:cd15671    67 ACIQCSVKSCKTAFHVTCAFQHGLEMKtilededdevKFKSYCPKH 112
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1924-2019 5.79e-07

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: 49.59  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1924 ENLQGLLKKLHEGLMaadefSIFASPVTDDI--APGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYN 1999
Cdd:cd05499     7 EVLKELMKPKHSAYN-----WPFLDPVDPVAlnIPNYFSIIKKPMDLGTISKKLQNgqYQSAKEFERDVRLIFKNCYTFN 81
                          90       100
                  ....*....|....*....|.
gi 325190525 2000 GKSSEIGLLAMELQQA-SMKM 2019
Cdd:cd05499    82 PEGTDVYMMGHQLEEVfNDKW 102
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
1333-1372 5.92e-07

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.


Pssm-ID: 277181  Cd Length: 118  Bit Score: 50.08  E-value: 5.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 325190525 1333 VAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCAL 1372
Cdd:cd15711    57 VIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGV 96
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
1311-1388 6.36e-07

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain.


Pssm-ID: 277169  Cd Length: 103  Bit Score: 49.53  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1311 FVHDQCAIASPLCFHRDESWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCALTCGWSLNKSQF--YCPSH 1388
Cdd:cd15699    24 WVHEGCILWANGIYLVCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEENFsvRCPKH 103
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1946-2023 9.16e-07

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: 49.34  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1946 FASPVtDDIA---PGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQQASMKML 2020
Cdd:cd05497    26 FQQPV-DAVKlnlPDYHKIIKTPMDLGTIKKRLENnyYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLFLQKL 104

                  ...
gi 325190525 2021 TNL 2023
Cdd:cd05497   105 AQM 107
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
413-452 3.91e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.38  E-value: 3.91e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 325190525    413 SGAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCYK 452
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
674-713 5.17e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 5.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 325190525   674 GEPVAYMRGHTGPITNILFSNDGTQIATASiKDGTARIWS 713
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGS-DDGTVKVWD 39
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1923-2025 6.64e-06

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: 47.05  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1923 YENLQGLLKKLHeglmAADEFSI-FASPVTDDIAPGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYN 1999
Cdd:cd05510     9 YESLDKVLNELK----TYTEHSTpFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNlqYKSKAEFVDDLNLIWKNCLLYN 84
                          90       100
                  ....*....|....*....|....*..
gi 325190525 2000 GKSSE-IGLLAMELQQASMKMLTNLVD 2025
Cdd:cd05510    85 SDPSHpLRRHANFMKKKAEHLLKLIPD 111
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1927-2013 8.71e-06

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: 46.50  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1927 QGLLKKLHEGLMAADEFsIFASPVtDDIA---PGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGK 2001
Cdd:cd05498     6 SGILKELFSKKHKAYAW-PFYKPV-DPEAlglHDYHDIIKHPMDLSTIKKKLDNreYADAQEFAADVRLMFSNCYKYNPP 83
                          90
                  ....*....|..
gi 325190525 2002 SSEIGLLAMELQ 2013
Cdd:cd05498    84 DHPVHAMARKLQ 95
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
1279-1388 1.20e-05

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 46.18  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525  1279 CAFCGHSddGGIMKLPSESMgvhplingcqrvFVHDQCAIASP----LCFHRDESWY--NVAKEIRrgrKLECSVCHNK- 1351
Cdd:pfam13832    3 CCLCPLR--GGALKQTSDGR------------WVHVLCAIFVPevrfGNVATMEPIDvsRIPPERW---KLKCVFCKKRs 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 325190525  1352 GATIGCCVPECRSVYHWKCALTCG-------WSLNKSQFYCPSH 1388
Cdd:pfam13832   66 GACIQCSKGRCTTAFHVTCAQAAGvymepedWPNVVVIAYCQKH 109
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
1307-1388 1.32e-05

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.


Pssm-ID: 277165  Cd Length: 90  Bit Score: 45.68  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1307 CQRVFVHDQCAIASPLCFHRD-ESWYNVAKEIRRGRKLECSVCHNKGATIGCCVPECRSVYHWKCALTCG--WSLNKSQF 1383
Cdd:cd15695     6 CGECWVHHWCAAWSAGVKQHEgDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGsfQSMKTLLL 85

                  ....*
gi 325190525 1384 YCPSH 1388
Cdd:cd15695    86 LCPEH 90
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1697-1782 1.51e-05

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: 46.10  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1697 MLTEI-NNIMELSISRDFVDAVDESFL-DYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIA 1774
Cdd:cd05511     4 ILDEIvNELKNLPDSWPFHTPVNKKKVpDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYT 83

                  ....*...
gi 325190525 1775 QNARTICN 1782
Cdd:cd05511    84 KKAKEMLE 91
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1697-1780 1.64e-05

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: 45.44  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1697 MLTEINNIMElSISRDFVDAVDESFL-DYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQ 1775
Cdd:cd04369     8 LLDALKKLKR-DLSEPFLEPVDPKEApDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGPGSPIYK 86

                  ....*
gi 325190525 1776 NARTI 1780
Cdd:cd04369    87 DAKKL 91
WD40 pfam00400
WD domain, G-beta repeat;
414-451 3.05e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 3.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 325190525   414 GAPVAVLIGHSSVVNSVRFHPSKNVVLSASDDGRCFCY 451
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1946-2013 6.23e-05

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: 44.20  E-value: 6.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325190525 1946 FASPVTDDIaPGYSKRIQDPMDFGTMLARM-----SSYRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQ 2013
Cdd:cd05502    25 FHEPVSPSV-PNYYKIIKTPMDLSLIRKKLqpkspQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELE 96
PTZ00420 PTZ00420
coronin; Provisional
378-443 1.28e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 325190525  378 LRGHNGNVTDLAVN-CSDTLLASSSDDKTIRIWELGSG--------APVAVLIGHSSVVNSVRFHPSKNVVLSAS 443
Cdd:PTZ00420   70 LKGHTSSILDLQFNpCFSEILASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDWNPMNYYIMCSS 144
BROMO smart00297
bromo domain;
1693-1780 1.42e-04

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 43.04  E-value: 1.42e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525   1693 IQLAMLTEINNIMELSISRDFVDAVDESFL-DYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESS 1771
Cdd:smart00297    8 LQELLKAVLDKLDSHPLSWPFLKPVSRKEApDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDS 87

                    ....*....
gi 325190525   1772 TIAQNARTI 1780
Cdd:smart00297   88 EVYKDAKKL 96
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1710-1792 2.46e-04

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: 42.16  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1710 SRDFVDAVDES-FLDYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNArticNTLighv 1788
Cdd:cd05509    19 AWPFLEPVDKEeAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCA----NKL---- 90

                  ....
gi 325190525 1789 QRFF 1792
Cdd:cd05509    91 EKFF 94
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
813-845 3.69e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.99  E-value: 3.69e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 325190525    813 HGHVNAVFALDVHPHDWRLAiTAGYDGRICLWD 845
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLA-SGSDDGTIKLWD 40
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1956-2015 4.18e-04

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: 41.61  E-value: 4.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325190525 1956 PGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEYNGKSSEIGLLAMELQQA 2015
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTgyYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKA 100
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1924-2005 7.53e-04

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: 40.89  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1924 ENLQGLLKKLHEGLMAADEFSI-FASPVTDDI--APGYSKRIQDPMDFGTMLARMSS--YRSFSTYFENLRLVFQNAIEY 1998
Cdd:cd05495     2 EELRQALMPTLEKLYKQDPESLpFRQPVDPKLlgIPDYFDIVKNPMDLSTIRRKLDTgqYQDPWQYVDDVWLMFDNAWLY 81

                  ....*..
gi 325190525 1999 NGKSSEI 2005
Cdd:cd05495    82 NRKTSRV 88
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1276-1396 7.90e-04

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1276 LIVCAFCGHSDdgGIMKLPSESMGVHPLingcqrvfvhdqCAIASP-LCFH---RDESWYNVAKEIRRGRKLECSVCHNK 1351
Cdd:COG5141   247 IRCCSFCPSSD--GAFKQTSDGRWGHVI------------CAMFNPeLSFGhllSKDPIDNIASVSSSRWKLGCLICKEF 312
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 325190525 1352 GAT-IGCCVPECRSVYHWKCALTCGW----SLNKSQF-YCPSHEELDDNAT 1396
Cdd:COG5141   313 GGTcIQCSYFNCTRAYHVTCARRAGYfdlnIYSHNGIsYCIDHEPLCRKHY 363
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1946-2005 8.34e-04

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: 41.29  E-value: 8.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325190525 1946 FASPVTDDIAPGYSKRIQDPMDFGTMLARMS--SYRSFSTYFENLRLVFQNAIEYN-GKSSEI 2005
Cdd:cd05496    26 FRQPVDLLKYPDYRDIIDTPMDLGTVKETLFggNYDDPMEFAKDVRLIFSNSKSYTpNKRSRI 88
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1345-1388 1.16e-03

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 1.16e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 325190525   1345 CSVC---HNKGATIGCCvpECRSVYHWKCA-LTCGWSLNKSQFYCPSH 1388
Cdd:smart00249    2 CSVCgkpDDGGELLQCD--GCDRWYHQTCLgPPLLEEEPDGKWYCPKC 47
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1714-1767 1.72e-03

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: 40.10  E-value: 1.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 325190525 1714 VDAVDESFLDYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYN 1767
Cdd:cd05497    30 VDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYN 83
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
1343-1388 2.39e-03

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277174  Cd Length: 118  Bit Score: 40.05  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 325190525 1343 LECSVCHNK-GATIGCCVPECRSVYHWKCALTCGWSLN---------KSQFYCPSH 1388
Cdd:cd15704    59 LVCSLCNEKvGASIQCSVKNCRTAFHVTCAFDRGLEMKtilaendevKFKSYCPKH 114
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1344-1388 2.78e-03

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 37.31  E-value: 2.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 325190525 1344 ECSVCHNKGATIGCCVPECRSVYHWKCA-LTcgwSLNKSQFYCPSH 1388
Cdd:cd15568     1 ECFRCGDGGDLVLCDFKGCPKVYHLSCLgLE---KPPGGKWICPWH 43
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1719-1777 3.50e-03

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: 38.86  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 325190525 1719 ESFLDYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNA 1777
Cdd:cd05520    34 RKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDA 92
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1723-1780 4.49e-03

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: 38.95  E-value: 4.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 325190525 1723 DYLITIANPINLTQLRERLRLGYYRQVEALLADAKLLANNCELYNVESSTIAQNARTI 1780
Cdd:cd05516    39 EYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVL 96
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
1279-1388 5.56e-03

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.


Pssm-ID: 277177 [Multi-domain]  Cd Length: 113  Bit Score: 38.73  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325190525 1279 CAFCGHSddGGIMKlpSESMGVHplingcqrvFVHDQCAIASPL----CFHRDESWYNVAkEIRRGR-KLECSVCHNK-G 1352
Cdd:cd15707     1 CILCPNK--GGAMK--STRSGTK---------WAHVSCALWIPEvsigCVEKMEPITKIS-SIPASRwALICVLCRERtG 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 325190525 1353 ATIGCCVPECRSVYHWKCALTCGWSLN-----------KSQFYCPSH 1388
Cdd:cd15707    67 ACIQCSVKTCKTAYHVTCGFQHGLEMKtildeesedgvKLRSYCQKH 113
WD40 pfam00400
WD domain, G-beta repeat;
813-845 5.83e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 5.83e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 325190525   813 HGHVNAVFALDVHPHDwRLAITAGYDGRICLWD 845
Cdd:pfam00400    8 EGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
 
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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