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Conserved domains on  [gi|63252910|ref|NP_001017977|]
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DDB1- and CUL4-associated factor 6 isoform b [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 ...
 43-292 3.03e-22

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: 97.79  E-value: 3.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200  78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200 147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                       250
                ....*....|.
gi 63252910 282 PkdDTARELKT 292
Cdd:cd00200 206 L--STGKCLGT 214
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
289-666 8.11e-08

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: 56.27  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949 406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949 477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  443 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 511
Cdd:PRK14949 557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  512 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 590
Cdd:PRK14949 636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  591 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 663
Cdd:PRK14949 709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                 ...
gi 63252910  664 IPG 666
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 ...
 730-789 1.93e-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: 47.33  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 730 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
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 ...
 43-292 3.03e-22

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: 97.79  E-value: 3.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200  78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200 147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                       250
                ....*....|.
gi 63252910 282 PkdDTARELKT 292
Cdd:cd00200 206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 7.73e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 7.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319 153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319 230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319 296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                       250
                ....*....|....*
gi 63252910 278 YLFDPkdDTARELKT 292
Cdd:COG2319 355 RLWDL--ATGELLRT 367
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 289-666 8.11e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 56.27  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949 406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949 477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  443 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 511
Cdd:PRK14949 557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  512 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 590
Cdd:PRK14949 636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  591 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 663
Cdd:PRK14949 709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                 ...
gi 63252910  664 IPG 666
Cdd:PRK14949 789 SSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 730-789 1.93e-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: 47.33  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 730 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:cd00200 189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.21e-05

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: 41.53  E-value: 4.21e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 63252910     42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 393-649 1.04e-04

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: 45.69  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   393 EVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHStpllSSPDSEQRQSVEASGHHTHHQSdnnneKLSPKPGT 472
Cdd:pfam07263 208 EFDDEGMQSDDPDSIRSERGNSRMSSASVKSKESKGDSEQA----STQDSGDSQSVEYPSRKFFRKS-----RISEEDDR 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   473 GEpvlslhySTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESFVPQS-----SVQPPEGDSETKAPEESSEDV 547
Cdd:pfam07263 279 GE-------LDDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQSqedsqNSQDPSSESSQEADLPSQESS 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   548 TKYQEGVSAENPVENHINITQSDKFTAkplDSNSGERNDLNLDRSCGVP-----EESASSEKAKEPETSDQ--------- 613
Cdd:pfam07263 352 SESQEEVVSESRGDNPDNTSSSEEDQE---DSDSSEEDSLSTFSSSESEsreeqADSESNESLRSSEESPEssedensss 428

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 63252910   614 --------TSTESATNENNTNPEPQFQTEATGPSAHEETSTRDS 649
Cdd:pfam07263 429 qeglqshsASTESQSEESQSEQDSQSEEDDESDSQDSSRSKEDS 472
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.93e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 63252910    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 COG2319
WD40 repeat [General function prediction only];
736-790 8.11e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 63252910 736 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
Cdd:COG2319 263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 750-789 5.07e-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: 35.37  E-value: 5.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 63252910    750 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
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 ...
 43-292 3.03e-22

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: 97.79  E-value: 3.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200  78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200 147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                       250
                ....*....|.
gi 63252910 282 PkdDTARELKT 292
Cdd:cd00200 206 L--STGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 46-275 1.70e-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: 1.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200  88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 125 veqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200 163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63252910 202 PiPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200 230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 7.73e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 7.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319 153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319 230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319 296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                       250
                ....*....|....*
gi 63252910 278 YLFDPkdDTARELKT 292
Cdd:COG2319 355 RLWDL--ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
42-284 4.85e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 4.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI- 120
Cdd:COG2319 195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSP--DGRLLASGSADGTVr 271

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 121 FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPnDPYTFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAI 199
Cdd:COG2319 272 LW-----DLATGELLRtLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF 338

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 200 cPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IY 278
Cdd:COG2319 339 -SPDGKTLASGSDDGTVRLWDLA---------------TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVR 397


                ....*.
gi 63252910 279 LFDPKD 284
Cdd:COG2319 398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-299 1.12e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSP--DGKLLASGSDDGTVR 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 122 YTNVEQDAETNRqcqFTCHygtTYEIMTV---PNDPyTFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAA 194
Cdd:COG2319 188 LWDLATGKLLRT---LTGH---TGAVRSVafsPDGK-LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSV 249

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 195 TSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgnyagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSS 274
Cdd:COG2319 250 RSVAFSPD-GRLLASGSADGTVRLWDL---------------ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSD 308

                       250       260
                ....*....|....*....|....*.
gi 63252910 275 DY-IYLFDPkdDTARELKTPSAEERR 299
Cdd:COG2319 309 DGtVRLWDL--ATGKLLRTLTGHTGA 332
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 42-220 3.03e-15

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: 76.99  E-value: 3.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:cd00200 126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 122 YTNVEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200 203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269

                       170       180
                ....*....|....*....|.
gi 63252910 200 CPPIPyYLAVGCSDSSVRIYD 220
Cdd:cd00200 270 SPDGK-RLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 43-281 6.20e-15

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: 76.22  E-value: 6.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIF 121
Cdd:cd00200  43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKtIKV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 122 YtnveqDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSV 197
Cdd:cd00200 120 W-----DVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSV 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 198 AICpPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY- 276
Cdd:cd00200 184 AFS-PDGEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGt 242


                ....*
gi 63252910 277 IYLFD 281
Cdd:cd00200 243 IRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 41-170 8.31e-13

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: 69.67  E-value: 8.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI 120
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 63252910 121 -FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFD 170
Cdd:cd00200 244 rVW-----DLRTGECVQtLSGHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 289-666 8.11e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 56.27  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949 406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949 477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  443 EQRQSVEASGHHTHHQSDNNNEKLSPkPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-----------GS 511
Cdd:PRK14949 557 VAFSSESYNALSDDEQHSANVQSAQS-AAEAQPSSQSLSPISAVTTAAASLADDDILDAVLAARDSLlsdldalspkeGD 635

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  512 HCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINI-TQSDKFTAKPLDSNsgerndlNLD 590
Cdd:PRK14949 636 GKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAaLASGSAPAPPPVPD-------PYD 708

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  591 RSCGV--PE-ESASSEKAKEPETSDQTSTESATNENNTN----PEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVL 663
Cdd:PRK14949 709 RPPWEeaPEvASANDGPNNAAEGNLSESVEDASNSELQAveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLL 788


                 ...
gi 63252910  664 IPG 666
Cdd:PRK14949 789 SSG 791
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 730-789 1.93e-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: 47.33  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 730 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:cd00200 189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.21e-05

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: 41.53  E-value: 4.21e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 63252910     42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 393-649 1.04e-04

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: 45.69  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   393 EVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHStpllSSPDSEQRQSVEASGHHTHHQSdnnneKLSPKPGT 472
Cdd:pfam07263 208 EFDDEGMQSDDPDSIRSERGNSRMSSASVKSKESKGDSEQA----STQDSGDSQSVEYPSRKFFRKS-----RISEEDDR 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   473 GEpvlslhySTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESFVPQS-----SVQPPEGDSETKAPEESSEDV 547
Cdd:pfam07263 279 GE-------LDDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQSqedsqNSQDPSSESSQEADLPSQESS 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910   548 TKYQEGVSAENPVENHINITQSDKFTAkplDSNSGERNDLNLDRSCGVP-----EESASSEKAKEPETSDQ--------- 613
Cdd:pfam07263 352 SESQEEVVSESRGDNPDNTSSSEEDQE---DSDSSEEDSLSTFSSSESEsreeqADSESNESLRSSEESPEssedensss 428

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 63252910   614 --------TSTESATNENNTNPEPQFQTEATGPSAHEETSTRDS 649
Cdd:pfam07263 429 qeglqshsASTESQSEESQSEQDSQSEEDDESDSQDSSRSKEDS 472
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 712-789 1.64e-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: 44.63  E-value: 1.64e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63252910 712 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:cd00200   4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.93e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 63252910    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 703-790 4.27e-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: 43.09  E-value: 4.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910 703 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 781
Cdd:cd00200 121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                ....*....
gi 63252910 782 DYDIKIWSP 790
Cdd:cd00200 198 DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
736-790 8.11e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 63252910 736 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
Cdd:COG2319 263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 732-789 9.15e-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: 42.32  E-value: 9.15e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 63252910 732 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:cd00200  64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
PRK08581 PRK08581
amidase domain-containing protein;
375-634 1.07e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.47  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  375 TSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSP--TESPHSTPLLSSPDSEqrqSVEASG 452
Cdd:PRK08581  19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQdnNDKKFSTIDSSTSDSN---NIIDFI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  453 HHTHHQSDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWS-SIASSSRGIGSHCKSEGQEESFVPQSSVQPP 531
Cdd:PRK08581  96 YKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEkSTNDSNKNSDSSIKNDTDTQSSKQDKADNQK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252910  532 EGDSETKAPEESSEDVTKYQEgvsaENPVENHINITQSDKFTAKPLDSNSGERNDLNLDrscGVPEEsaSSEKAKEPETS 611
Cdd:PRK08581 176 APSSNNTKPSTSNKQPNSPKP----TQPNQSNSQPASDDTANQKSSSKDNQSMSDSALD---SILDQ--YSEDAKKTQKD 246

                        250       260
                 ....*....|....*....|...
gi 63252910  612 DQTSTESATNENNTNPEPQFQTE 634
Cdd:PRK08581 247 YASQSKKDKTETSNTKNPQLPTQ 269
WD40 COG2319
WD40 repeat [General function prediction only];
732-790 1.61e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 63252910 732 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
Cdd:COG2319 343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 736-790 1.66e-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: 41.17  E-value: 1.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 63252910 736 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
Cdd:cd00200 111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 732-789 3.42e-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: 40.40  E-value: 3.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 63252910 732 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
732-790 4.50e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 4.50e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 63252910 732 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
Cdd:COG2319 301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 750-789 5.07e-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: 35.37  E-value: 5.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 63252910    750 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 789
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
736-790 8.84e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 8.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 63252910 736 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 790
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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