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Conserved domains on  [gi|332008427|gb|AED95810|]
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WD40/YVTN repeat and Bromo-WDR9-I-like domain-containing protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1548-1677 4.67e-53

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: 182.15  E-value: 4.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427 1548 AETHLHSPWELFDADtkWEQPHIDDEQRNRLLSALTKLETSDKRTQDSFGLRKLNQTVGNSSYSNRFPVPLSLEVIRSRL 1627
Cdd:cd05529     1 LYNPLSSEWELFDPG--WEQPHIRDEERERLISGLDKLLLSLQLEIAEYFEYPVDLRAWYPDYWNRVPVPMDLETIRSRL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 332008427 1628 ENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTLPSS 1677
Cdd:cd05529    79 ENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLRILSSL 128
WD40 COG2319
WD40 repeat [General function prediction only];
238-649 1.73e-50

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 184.73  E-value: 1.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  238 IKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRLP 317
Cdd:COG2319    71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  318 DGLPVSVLRGHTGAVTAIAFSPrPGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknSGPSSSnaqqshqIF 397
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSP-DGK--LLASGSDDGTVRLWDLATGKLLRTL------------TGHTGA-------VR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  398 CCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSgcaagskfsvtdyskdenvpk 477
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDL------------ATGKLLRTLTGHSGSVRSVAFS--------------------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  478 fknswfcHDN--IVTCSRDGSAIIWiprlrRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptPRGVNMIAWSLD 555
Cdd:COG2319   256 -------PDGrlLASGSADGTVRLW-----DLATGELLRTLTGH------------------------SGGVNSVAFSPD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  556 NRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYDiSHYKLVDG 635
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLATGELLRTLT-GHTGAVTS 377
                         410
                  ....*....|....*.
gi 332008427  636 -KFSPDGTSIIL-SDD 649
Cdd:COG2319   378 vAFSPDGRTLASgSAD 393
 
Name Accession Description Interval E-value
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1548-1677 4.67e-53

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: 182.15  E-value: 4.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427 1548 AETHLHSPWELFDADtkWEQPHIDDEQRNRLLSALTKLETSDKRTQDSFGLRKLNQTVGNSSYSNRFPVPLSLEVIRSRL 1627
Cdd:cd05529     1 LYNPLSSEWELFDPG--WEQPHIRDEERERLISGLDKLLLSLQLEIAEYFEYPVDLRAWYPDYWNRVPVPMDLETIRSRL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 332008427 1628 ENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTLPSS 1677
Cdd:cd05529    79 ENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLRILSSL 128
WD40 COG2319
WD40 repeat [General function prediction only];
238-649 1.73e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 184.73  E-value: 1.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  238 IKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRLP 317
Cdd:COG2319    71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  318 DGLPVSVLRGHTGAVTAIAFSPrPGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknSGPSSSnaqqshqIF 397
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSP-DGK--LLASGSDDGTVRLWDLATGKLLRTL------------TGHTGA-------VR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  398 CCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSgcaagskfsvtdyskdenvpk 477
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDL------------ATGKLLRTLTGHSGSVRSVAFS--------------------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  478 fknswfcHDN--IVTCSRDGSAIIWiprlrRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptPRGVNMIAWSLD 555
Cdd:COG2319   256 -------PDGrlLASGSADGTVRLW-----DLATGELLRTLTGH------------------------SGGVNSVAFSPD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  556 NRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYDiSHYKLVDG 635
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLATGELLRTLT-GHTGAVTS 377
                         410
                  ....*....|....*.
gi 332008427  636 -KFSPDGTSIIL-SDD 649
Cdd:COG2319   378 vAFSPDGRTLASgSAD 393
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
237-615 5.96e-50

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: 179.45  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  237 NIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRL 316
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  317 PDGLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWDARGAQFaprIYVPRppspdgknsgpsssnaQQSHQI 396
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSP---DGRILSSSSRDKTIKVWDVETGKC---LTTLR----------------GHTDWV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  397 FCCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSGcaagskfsvtdyskDENvp 476
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDL------------RTGKCVATLTGHTGEVNSVAFSP--------------DGE-- 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  477 kfknswfchdNIVTCSRDGSAIIWIPRLRRSHGkscrwTRAYHLKvppppmppqpprggprqrilptprGVNMIAWSLDN 556
Cdd:cd00200   191 ----------KLLSSSSDGTIKLWDLSTGKCLG-----TLRGHEN------------------------GVNSVAFSPDG 231
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332008427  557 RFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWD 615
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLA-SGSADGTIRIWD 289
BROMO smart00297
bromo domain;
1610-1674 4.23e-09

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 55.75  E-value: 4.23e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332008427   1610 YSNRFPVPLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTL 1674
Cdd:smart00297   40 YYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKL 104
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
318-360 3.90e-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: 50.77  E-value: 3.90e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 332008427    318 DGLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWD 360
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP---DGKYLASGSDDGTIKLWD 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1617-1661 1.17e-07

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: 50.77  E-value: 1.17e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 332008427  1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAA 1661
Cdd:pfam00439   36 PMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
WD40 pfam00400
WD domain, G-beta repeat;
319-360 2.83e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.11  E-value: 2.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 332008427   319 GLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWD 360
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSP---DGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
250-455 7.09e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.77  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  250 CAI-LDRSGRYVITGSDDRLVKVWSMDTayCLASCRGHEGDITDLAVSSN------NIFI----ASASNDCVIRVWRLPD 318
Cdd:PLN00181  487 CAIgFDRDGEFFATAGVNKKIKIFECES--IIKDGRDIHYPVVELASRSKlsgicwNSYIksqvASSNFEGVVQVWDVAR 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  319 GLPVSVLRGHTGAVTAIAFSPrpGSPYQLLSSSDDGTCRIWDArgaqfapriyvprppspdgkNSGPSSSNAQQSHQIFC 398
Cdd:PLN00181  565 SQLVTEMKEHEKRVWSIDYSS--ADPTLLASGSDDGSVKLWSI--------------------NQGVSIGTIKTKANICC 622
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332008427  399 CAF-NASGSVFVTGSSDTLARVYsvwsanktntdDPEQPNHEMDVLAGHENDVNYVQF 455
Cdd:PLN00181  623 VQFpSESGRSLAFGSADHKVYYY-----------DLRNPKLPLCTMIGHSKTVSYVRF 669
 
Name Accession Description Interval E-value
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1548-1677 4.67e-53

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: 182.15  E-value: 4.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427 1548 AETHLHSPWELFDADtkWEQPHIDDEQRNRLLSALTKLETSDKRTQDSFGLRKLNQTVGNSSYSNRFPVPLSLEVIRSRL 1627
Cdd:cd05529     1 LYNPLSSEWELFDPG--WEQPHIRDEERERLISGLDKLLLSLQLEIAEYFEYPVDLRAWYPDYWNRVPVPMDLETIRSRL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 332008427 1628 ENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTLPSS 1677
Cdd:cd05529    79 ENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLRILSSL 128
WD40 COG2319
WD40 repeat [General function prediction only];
238-649 1.73e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 184.73  E-value: 1.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  238 IKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRLP 317
Cdd:COG2319    71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  318 DGLPVSVLRGHTGAVTAIAFSPrPGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknSGPSSSnaqqshqIF 397
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSP-DGK--LLASGSDDGTVRLWDLATGKLLRTL------------TGHTGA-------VR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  398 CCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSgcaagskfsvtdyskdenvpk 477
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDL------------ATGKLLRTLTGHSGSVRSVAFS--------------------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  478 fknswfcHDN--IVTCSRDGSAIIWiprlrRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptPRGVNMIAWSLD 555
Cdd:COG2319   256 -------PDGrlLASGSADGTVRLW-----DLATGELLRTLTGH------------------------SGGVNSVAFSPD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  556 NRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYDiSHYKLVDG 635
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDLATGELLRTLT-GHTGAVTS 377
                         410
                  ....*....|....*.
gi 332008427  636 -KFSPDGTSIIL-SDD 649
Cdd:COG2319   378 vAFSPDGRTLASgSAD 393
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
237-615 5.96e-50

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: 179.45  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  237 NIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRL 316
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  317 PDGLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWDARGAQFaprIYVPRppspdgknsgpsssnaQQSHQI 396
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSP---DGRILSSSSRDKTIKVWDVETGKC---LTTLR----------------GHTDWV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  397 FCCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSGcaagskfsvtdyskDENvp 476
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDL------------RTGKCVATLTGHTGEVNSVAFSP--------------DGE-- 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  477 kfknswfchdNIVTCSRDGSAIIWIPRLRRSHGkscrwTRAYHLKvppppmppqpprggprqrilptprGVNMIAWSLDN 556
Cdd:cd00200   191 ----------KLLSSSSDGTIKLWDLSTGKCLG-----TLRGHEN------------------------GVNSVAFSPDG 231
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332008427  557 RFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWD 615
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLA-SGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
236-616 3.29e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.18  E-value: 3.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  236 QNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWR 315
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  316 LPDGLPVSVLRGHTGAVTAIAFSPRpGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknSGPSSSnaqqshq 395
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSPD-GK--LLASGSADGTVRLWDLATGKLLRTL------------TGHSGS------- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  396 IFCCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSGcaagskfsvtdyskDENV 475
Cdd:COG2319   249 VRSVAFSPDGRLLASGSADGTVRLWDL------------ATGELLRTLTGHSGGVNSVAFSP--------------DGKL 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  476 pkfknswfchdnIVTCSRDGSAIIWiprlRRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptpRGVNMIAWSLD 555
Cdd:COG2319   303 ------------LASGSDDGTVRLW----DLATGKLLRTLTGHT-------------------------GAVRSVAFSPD 341
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332008427  556 NRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDI 616
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLA-SGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
240-660 2.15e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 158.15  E-value: 2.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  240 RLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRLPDG 319
Cdd:COG2319    31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  320 LPVSVLRGHTGAVTAIAFSPRpGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknSGPSSSnaqqshqIFCC 399
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPD-GK--TLASGSADGTVRLWDLATGKLLRTL------------TGHSGA-------VTSV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  400 AFNASGSVFVTGSSDTLARVYSVWSANKTNTddpeqpnhemdvLAGHENDVNYVQFSgcaAGSKFsvtdyskdenvpkfk 479
Cdd:COG2319   169 AFSPDGKLLASGSDDGTVRLWDLATGKLLRT------------LTGHTGAVRSVAFS---PDGKL--------------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  480 nswfchdnIVTCSRDGSAIIWiprlrRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptPRGVNMIAWSLDNRFV 559
Cdd:COG2319   219 --------LASGSADGTVRLW-----DLATGKLLRTLTGH------------------------SGSVRSVAFSPDGRLL 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  560 LAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYDISHYKLVDGKFSP 639
Cdd:COG2319   262 ASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLA-SGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP 340
                         410       420
                  ....*....|....*....|...
gi 332008427  640 DGTSIILSDDVGQLYI--LSTGQ 660
Cdd:COG2319   341 DGKTLASGSDDGTVRLwdLATGE 363
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
232-500 1.19e-39

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: 149.41  E-value: 1.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  232 VQKMQNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVI 311
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTI 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  312 RVWRLPDGLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWDARGAQFapriyvprppspdgKNSGPSSSNAq 391
Cdd:cd00200   160 KLWDLRTGKCVATLTGHTGEVNSVAFSP---DGEKLLSSSSDGTIKLWDLSTGKC--------------LGTLRGHENG- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  392 qshqIFCCAFNASGSVFVTGSSDTLARVYSVWSANktntddpeqpnhEMDVLAGHENDVNYVQFsgcaagskfsvtdySK 471
Cdd:cd00200   222 ----VNSVAFSPDGYLLASGSEDGTIRVWDLRTGE------------CVQTLSGHTNSVTSLAW--------------SP 271
                         250       260
                  ....*....|....*....|....*....
gi 332008427  472 DENVpkfknswfchdnIVTCSRDGSAIIW 500
Cdd:cd00200   272 DGKR------------LASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
238-575 3.56e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 151.60  E-value: 3.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  238 IKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWRLP 317
Cdd:COG2319   155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  318 DGLPVSVLRGHTGAVTAIAFSPRpGSpyQLLSSSDDGTCRIWDARGAQFAPRIyvprppspdgknsgpsssnAQQSHQIF 397
Cdd:COG2319   235 TGKLLRTLTGHSGSVRSVAFSPD-GR--LLASGSADGTVRLWDLATGELLRTL-------------------TGHSGGVN 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  398 CCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVQFSgcAAGSKfsvtdyskdenvpk 477
Cdd:COG2319   293 SVAFSPDGKLLASGSDDGTVRLWDL------------ATGKLLRTLTGHTGAVRSVAFS--PDGKT-------------- 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  478 fknswfchdnIVTCSRDGSAIIWiprlrRSHGKSCRWTRAYHlkvppppmppqpprggprqrilptPRGVNMIAWSLDNR 557
Cdd:COG2319   345 ----------LASGSDDGTVRLW-----DLATGELLRTLTGH------------------------TGAVTSVAFSPDGR 385
                         330
                  ....*....|....*...
gi 332008427  558 FVLAAIMDCRICVWNASD 575
Cdd:COG2319   386 TLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
236-363 2.09e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.79  E-value: 2.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  236 QNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWR 315
Cdd:COG2319   279 ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWD 358
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 332008427  316 LPDGLPVSVLRGHTGAVTAIAFSPRpGSpyQLLSSSDDGTCRIWDARG 363
Cdd:COG2319   359 LATGELLRTLTGHTGAVTSVAFSPD-GR--TLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
393-660 7.39e-19

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: 88.93  E-value: 7.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  393 SHQIFCCAFNASGSVFVTGSSDTLARVYSVwsanktntddpeQPNHEMDVLAGHENDVNYVqfsgcaagskfsvtdyskd 472
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL------------ETGELLRTLKGHTGPVRDV------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  473 envpkfknSWFCHDN-IVTCSRDGSAIIWIPRlrrshGKSCRWTRAYHLKvppppmppqpprggprqrilptprGVNMIA 551
Cdd:cd00200    58 --------AASADGTyLASGSSDKTIRLWDLE-----TGECVRTLTGHTS------------------------YVSSVA 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  552 WSLDNRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYDiSHYK 631
Cdd:cd00200   101 FSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVA-SSSQDGTIKLWDLRTGKCVATLT-GHTG 178
                         250       260       270
                  ....*....|....*....|....*....|..
gi 332008427  632 LVDG-KFSPDGTSIILSDDVGQLYI--LSTGQ 660
Cdd:cd00200   179 EVNSvAFSPDGEKLLSSSSDGTIKLwdLSTGK 210
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
236-315 4.14e-17

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: 83.92  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  236 QNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDTAYCLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVWR 315
Cdd:cd00200   210 KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
BROMO smart00297
bromo domain;
1610-1674 4.23e-09

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 55.75  E-value: 4.23e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332008427   1610 YSNRFPVPLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTL 1674
Cdd:smart00297   40 YYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKL 104
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
318-360 3.90e-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: 50.77  E-value: 3.90e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 332008427    318 DGLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWD 360
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP---DGKYLASGSDDGTIKLWD 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1617-1661 1.17e-07

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: 50.77  E-value: 1.17e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 332008427  1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAA 1661
Cdd:pfam00439   36 PMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
WD40 pfam00400
WD domain, G-beta repeat;
319-360 2.83e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.11  E-value: 2.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 332008427   319 GLPVSVLRGHTGAVTAIAFSPrpgSPYQLLSSSDDGTCRIWD 360
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSP---DGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
279-314 5.66e-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: 47.31  E-value: 5.66e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 332008427    279 CLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVW 314
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
279-314 2.14e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 2.14e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 332008427   279 CLASCRGHEGDITDLAVSSNNIFIASASNDCVIRVW 314
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1617-1674 3.15e-06

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: 47.37  E-value: 3.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332008427 1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTL 1674
Cdd:cd04369    42 PMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGPGSPIYKDAKKLEKLFEKLL 99
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
234-273 4.10e-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: 45.00  E-value: 4.10e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 332008427    234 KMQNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWS 273
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
235-273 6.79e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 6.79e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 332008427   235 MQNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWS 273
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
578-660 2.23e-05

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: 48.10  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  578 LVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGIPIQIYdISHY-KLVDGKFSPDGTSIILS--DDVGQLY 654
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLA-TGSGDGTIKVWDLETGELLRTL-KGHTgPVRDVAASADGTYLASGssDKTIRLW 78

                  ....*.
gi 332008427  655 ILSTGQ 660
Cdd:cd00200    79 DLETGE 84
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1617-1674 3.34e-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: 44.59  E-value: 3.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332008427 1617 PLSLEVIRSRLE---NNYYRSVEALRHDVSVMLSNAETFFGRNKSVAAKISNLSNWFDRTL 1674
Cdd:cd05502    43 PMDLSLIRKKLQpksPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELELFFEEQL 103
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1573-1674 5.12e-05

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: 43.84  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427 1573 EQRNRLLSALTKLetsdKRTQDSFGLR------KLNQtvgnSSYSNRFPVPLSLEVIRSRLENNYYRSVEALRHDVSVML 1646
Cdd:cd05500     4 HQHKFLLSSIRSL----KRLKDARPFLvpvdpvKLNI----PHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMV 75
                          90       100
                  ....*....|....*....|....*...
gi 332008427 1647 SNAETFFGRNKSVAAKISNLSNWFDRTL 1674
Cdd:cd05500    76 DNCLTFNGPEHPVSQMGKRLQAAFEKHL 103
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
250-455 7.09e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.77  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  250 CAI-LDRSGRYVITGSDDRLVKVWSMDTayCLASCRGHEGDITDLAVSSN------NIFI----ASASNDCVIRVWRLPD 318
Cdd:PLN00181  487 CAIgFDRDGEFFATAGVNKKIKIFECES--IIKDGRDIHYPVVELASRSKlsgicwNSYIksqvASSNFEGVVQVWDVAR 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  319 GLPVSVLRGHTGAVTAIAFSPrpGSPYQLLSSSDDGTCRIWDArgaqfapriyvprppspdgkNSGPSSSNAQQSHQIFC 398
Cdd:PLN00181  565 SQLVTEMKEHEKRVWSIDYSS--ADPTLLASGSDDGSVKLWSI--------------------NQGVSIGTIKTKANICC 622
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332008427  399 CAF-NASGSVFVTGSSDTLARVYsvwsanktntdDPEQPNHEMDVLAGHENDVNYVQF 455
Cdd:PLN00181  623 VQFpSESGRSLAFGSADHKVYYY-----------DLRNPKLPLCTMIGHSKTVSYVRF 669
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1617-1653 1.96e-04

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: 42.33  E-value: 1.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 332008427 1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFF 1653
Cdd:cd05520    46 PISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYN 82
WD40 COG2319
WD40 repeat [General function prediction only];
232-276 2.85e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 2.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 332008427  232 VQKMQNIKRLRGHRNAVYCAILDRSGRYVITGSDDRLVKVWSMDT 276
Cdd:COG2319   359 LATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1617-1652 3.38e-04

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 41.56  E-value: 3.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332008427 1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETF 1652
Cdd:cd05519    46 PIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTY 81
PTZ00420 PTZ00420
coronin; Provisional
284-377 3.72e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 45.33  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  284 RGHEGDITDLavSSNNIF---IASASNDCVIRVWRLPDG--------LPVSVLRGHTGAVTAIAFSPRpgSPYQLLSSSD 352
Cdd:PTZ00420   71 KGHTSSILDL--QFNPCFseiLASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDWNPM--NYYIMCSSGF 146
                          90       100
                  ....*....|....*....|....*
gi 332008427  353 DGTCRIWDARGAQFAPRIYVPRPPS 377
Cdd:PTZ00420  147 DSFVNIWDIENEKRAFQINMPKKLS 171
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
575-615 4.28e-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: 39.22  E-value: 4.28e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 332008427    575 DGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWD 615
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLA-SGSDDGTIKLWD 40
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1617-1652 4.91e-04

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 41.14  E-value: 4.91e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332008427 1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETF 1652
Cdd:cd05515    46 PIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKY 81
WD40 COG2319
WD40 repeat [General function prediction only];
541-661 1.41e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008427  541 LPTPRGVNMIAWSLDNRFVLAAIMDCRICVWNASDGSLVHSLTGHTASTYVMDVHPFNPRIAmSAGYDGKTIVWDIWEGI 620
Cdd:COG2319    33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLA-SASADGTVRLWDLATGL 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 332008427  621 PIQIYDISHYKLVDGKFSPDGTSIILSDDVGQLYILSTGQG 661
Cdd:COG2319   112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG 152
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1607-1659 1.72e-03

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: 39.68  E-value: 1.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332008427 1607 NSSYSNRFPVPLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFGRNKSV 1659
Cdd:cd05525    38 NPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPI 90
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1617-1666 2.40e-03

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


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 39.15  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332008427 1617 PLSLEVIRSRLENNYYRSVEALRHDVSVMLSNAETFFgRNKSVAAKISNL 1666
Cdd:cd05522    47 PISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN-ENDSQEYKDAVL 95
 
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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