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Conserved domains on  [gi|1168720097|ref|NP_001336708|]
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DDB1- and CUL4-associated factor 6 isoform g [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-145 5.06e-08

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 55.03  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720097  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
142-519 1.86e-07

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14949:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 944  Bit Score: 54.73  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 296 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 364
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 365 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 443
Cdd:PRK14949  636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 444 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 516
Cdd:PRK14949  709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                  ...
gi 1168720097 517 IPG 519
Cdd:PRK14949  789 SSG 791
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 583-642 1.12e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 47.71  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 583 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-145 5.06e-08

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: 55.03  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720097  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 142-519 1.86e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 54.73  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 296 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 364
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 365 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 443
Cdd:PRK14949  636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 444 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 516
Cdd:PRK14949  709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                  ...
gi 1168720097 517 IPG 519
Cdd:PRK14949  789 SSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 583-642 1.12e-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: 47.71  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 583 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 1.14e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgn 84
Cdd:COG2319   218 LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSVRSVAFSPD-GRLLASGSADGTVRLWDL---------- 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720097  85 yagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSSDY-IYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   276 -----ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSDDGtVRLWDL--ATGKLLRTLTGHTGA 332
WD40 COG2319
WD40 repeat [General function prediction only];
589-643 6.43e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 6.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720097 589 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 246-502 1.38e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 41.84  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 246 EVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHStpllSSPDSEQRQSVEASGHHTHHQSdnnneKLSPKPGT 325
Cdd:pfam07263 208 EFDDEGMQSDDPDSIRSERGNSRMSSASVKSKESKGDSEQA----STQDSGDSQSVEYPSRKFFRKS-----RISEEDDR 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 326 GEpvlslhySTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESFVPQS-----SVQPPEGDSETKAPEESSEDV 400
Cdd:pfam07263 279 GE-------LDDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQSqedsqNSQDPSSESSQEADLPSQESS 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 401 TKYQEGVSAENPVENHINITQSDKFTAkplDSNSGERNDLNLDRSCGVP-----EESASSEKAKEPETSDQ--------- 466
Cdd:pfam07263 352 SESQEEVVSESRGDNPDNTSSSEEDQE---DSDSSEEDSLSTFSSSESEsreeqADSESNESLRSSEESPEssedensss 428

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1168720097 467 --------TSTESATNENNTNPEPQFQTEATGPSAHEETSTRDS 502
Cdd:pfam07263 429 qeglqshsASTESQSEESQSEQDSQSEEDDESDSQDSSRSKEDS 472
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 603-642 2.92e-03

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: 35.75  E-value: 2.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720097  603 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-145 5.06e-08

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: 55.03  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   5 NDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPPiPYYLAVGCSDSSVRIYDrrmlgtratgn 84
Cdd:cd00200   103 PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD-GTFVASSSQDGTIKLWD----------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168720097  85 yagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFDPkdDTARELKT 145
Cdd:cd00200   164 ----LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWDL--STGKCLGT 214
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 142-519 1.86e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 54.73  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 142 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 216
Cdd:PRK14949  406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 217 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 295
Cdd:PRK14949  477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 296 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 364
Cdd:PRK14949  557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 365 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 443
Cdd:PRK14949  636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 444 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 516
Cdd:PRK14949  709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                  ...
gi 1168720097 517 IPG 519
Cdd:PRK14949  789 SSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-128 9.96e-06

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: 9.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   6 DPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRRMLGTRATgny 85
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSPD-GYLLASGSEDGTIRVWDLRTGECVQT--- 256

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1168720097  86 agrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 128
Cdd:cd00200   257 ------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 583-642 1.12e-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: 47.71  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 583 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200   189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 565-642 9.36e-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: 45.02  E-value: 9.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720097 565 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200     4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 1.14e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgn 84
Cdd:COG2319   218 LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSVRSVAFSPD-GRLLASGSADGTVRLWDL---------- 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720097  85 yagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSSDY-IYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   276 -----ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSDDGtVRLWDL--ATGKLLRTLTGHTGA 332
WD40 COG2319
WD40 repeat [General function prediction only];
9-145 2.03e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.52  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   9 TFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVAICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagr 88
Cdd:COG2319   260 LLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLA------------- 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720097  89 gtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YIYLFDPkdDTARELKT 145
Cdd:COG2319   319 --TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTVRLWDL--ATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 556-643 2.51e-04

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: 43.48  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 556 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 634
Cdd:cd00200   121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                  ....*....
gi 1168720097 635 DYDIKIWSP 643
Cdd:cd00200   198 DGTIKLWDL 206
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 585-642 5.54e-04

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: 42.71  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720097 585 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200    64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
9-152 5.90e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   9 TFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAATSVAICPpipyYLAVGCSDSSVRIYDRRmlgtratgn 84
Cdd:COG2319   176 LLASGSDDGTVRLWDLAtgklLRT-----------LTGHTGAVRSVAFSPdg-kLLASGSADGTVRLWDLA--------- 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720097  85 yagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YIYLFDPkdDTARELKTPSAEERR 152
Cdd:COG2319   235 ------TGKLLRTLTGHSG----SVRSVAFSPDGR-LLASGSADgTVRLWDL--ATGELLRTLTGHSGG 290
WD40 COG2319
WD40 repeat [General function prediction only];
589-643 6.43e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 6.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720097 589 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 589-643 9.43e-04

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: 41.94  E-value: 9.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720097 589 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:cd00200   111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 COG2319
WD40 repeat [General function prediction only];
585-643 1.28e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720097 585 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:COG2319   343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 246-502 1.38e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 41.84  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 246 EVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHStpllSSPDSEQRQSVEASGHHTHHQSdnnneKLSPKPGT 325
Cdd:pfam07263 208 EFDDEGMQSDDPDSIRSERGNSRMSSASVKSKESKGDSEQA----STQDSGDSQSVEYPSRKFFRKS-----RISEEDDR 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 326 GEpvlslhySTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESFVPQS-----SVQPPEGDSETKAPEESSEDV 400
Cdd:pfam07263 279 GE-------LDDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQSqedsqNSQDPSSESSQEADLPSQESS 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 401 TKYQEGVSAENPVENHINITQSDKFTAkplDSNSGERNDLNLDRSCGVP-----EESASSEKAKEPETSDQ--------- 466
Cdd:pfam07263 352 SESQEEVVSESRGDNPDNTSSSEEDQE---DSDSSEEDSLSTFSSSESEsreeqADSESNESLRSSEESPEssedensss 428

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1168720097 467 --------TSTESATNENNTNPEPQFQTEATGPSAHEETSTRDS 502
Cdd:pfam07263 429 qeglqshsASTESQSEESQSEQDSQSEEDDESDSQDSSRSKEDS 472
PRK08581 PRK08581
amidase domain-containing protein;
228-487 1.94e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 41.31  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 228 TSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSP--TESPHSTPLLSSPDSEqrqSVEASG 305
Cdd:PRK08581   19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQdnNDKKFSTIDSSTSDSN---NIIDFI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 306 HHTHHQSDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWS-SIASSSRGIGSHCKSEGQEESFVPQSSVQPP 384
Cdd:PRK08581   96 YKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEkSTNDSNKNSDSSIKNDTDTQSSKQDKADNQK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097 385 EGDSETKAPEESSEDVTKYQEgvsaENPVENHINITQSDKFTAKPLDSNSGERNDLNLDrscGVPEEsaSSEKAKEPETS 464
Cdd:PRK08581  176 APSSNNTKPSTSNKQPNSPKP----TQPNQSNSQPASDDTANQKSSSKDNQSMSDSALD---SILDQ--YSEDAKKTQKD 246

                         250       260
                  ....*....|....*....|...
gi 1168720097 465 DQTSTESATNENNTNPEPQFQTE 487
Cdd:PRK08581  247 YASQSKKDKTETSNTKNPQLPTQ 269
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 585-642 2.11e-03

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: 40.78  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720097 585 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:cd00200   232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 603-642 2.92e-03

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: 35.75  E-value: 2.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1168720097  603 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 642
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
585-643 3.58e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720097 585 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:COG2319   301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
9-137 6.13e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720097   9 TFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAIcPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagr 88
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLA------------- 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1168720097  89 gtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IYLFDPKD 137
Cdd:COG2319   361 --TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
589-643 7.05e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720097 589 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 643
Cdd:COG2319   221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275
 
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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