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Conserved domains on  [gi|568911186|ref|XP_006497067|]
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DDB1- and CUL4-associated factor 6 isoform X2 [Mus musculus]

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 4.03e-23

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 421866 [Multi-domain]  Cd Length: 289  Bit Score: 100.49  E-value: 4.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctDDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 123 TNIEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 203 vPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlsnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 568911186 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
824-883 1.52e-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: 421866 [Multi-domain]  Cd Length: 289  Bit Score: 47.71  E-value: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 824 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
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 4.03e-23

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 100.49  E-value: 4.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctDDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 123 TNIEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 203 vPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlsnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 568911186 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-281 2.51e-17

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 85.91  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  42 KLEATLNVHDGCVNTICWNDTGEYILSGSD-DTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPCtDDKQIVSCSGDGVI 120
Cdd:COG2319  146 KLIRTLEGHSESVTSLAFSPDGKLLASGSSlDGTIKLWDLRTGKPLSTL-AGHTDPVSSLAFSPD-GGLLIASGSSDGTI 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 121 FYTNIEqdaeTNRQCQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDILINCrraatsvAIC 200
Cdd:COG2319  224 RLWDLS----TGKLLRSTLSGHSDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLS-------VAF 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 201 PPVPYYLAVGCSDSSVRIYDRRMLGTRATGNYAGrgttgmvarfipshlsnKSCRVTSLCYSEDGQEILVSYSSD-YIYL 279
Cdd:COG2319  293 SPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKG-----------------HEGPVSSLSFSPDGSLLVSGGSDDgTIRL 355

                 ..
gi 568911186 280 FD 281
Cdd:COG2319  356 WD 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
824-883 1.52e-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: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 824 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
42-77 2.76e-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: 41.91  E-value: 2.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568911186    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.25e-04

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 38.88  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568911186   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
844-883 3.56e-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: 36.14  E-value: 3.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568911186   844 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
802-883 7.90e-03

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 39.69  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 802 LVKMVYKGHRNSRTMikeANFWGANFVMSGSDCGHIFIWD-RHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIK 880
Cdd:COG2319  233 LLRSTLSGHSDSVVS---SFSPDGSLLASGSSDGTIRLWDlRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVR 309

                 ...
gi 568911186 881 IWS 883
Cdd:COG2319  310 LWD 312
 
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 4.03e-23

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 100.49  E-value: 4.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctDDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 123 TNIEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 203 vPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlsnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 568911186 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 5.30e-18

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: 85.46  E-value: 5.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctDDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 125 ieqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200  163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911186 202 PvPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLSnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200  230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-281 2.51e-17

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 85.91  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  42 KLEATLNVHDGCVNTICWNDTGEYILSGSD-DTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPCtDDKQIVSCSGDGVI 120
Cdd:COG2319  146 KLIRTLEGHSESVTSLAFSPDGKLLASGSSlDGTIKLWDLRTGKPLSTL-AGHTDPVSSLAFSPD-GGLLIASGSSDGTI 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 121 FYTNIEqdaeTNRQCQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDILINCrraatsvAIC 200
Cdd:COG2319  224 RLWDLS----TGKLLRSTLSGHSDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLS-------VAF 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 201 PPVPYYLAVGCSDSSVRIYDRRMLGTRATGNYAGrgttgmvarfipshlsnKSCRVTSLCYSEDGQEILVSYSSD-YIYL 279
Cdd:COG2319  293 SPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKG-----------------HEGPVSSLSFSPDGSLLVSGGSDDgTIRL 355

                 ..
gi 568911186 280 FD 281
Cdd:COG2319  356 WD 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
42-220 5.24e-16

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 79.69  E-value: 5.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctDDKQIVSCSGDGVIF 121
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 122 YTNIEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200  203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269
                        170       180
                 ....*....|....*....|.
gi 568911186 200 CPPVPyYLAVGCSDSSVRIYD 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 ...
43-292 4.21e-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: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctDDKQIVSCSGDGVIfy 122
Cdd:cd00200   43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKTI-- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 123 tnIEQDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSVA 198
Cdd:cd00200  118 --KVWDVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSVA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 199 ICPPvPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLSnkscRVTSLCYSEDGQeILVSYSSDY-I 277
Cdd:cd00200  185 FSPD-GEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGtI 243
                        250
                 ....*....|....*
gi 568911186 278 YLFDpkDDTARELKT 292
Cdd:cd00200  244 RVWD--LRTGECVQT 256
WD40 COG2319
WD40 repeat [General function prediction only];
46-285 3.39e-14

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 76.28  E-value: 3.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKL-VISNPYSRKVLTTIRSGHRANIFSAKFLPCTDDKQIVSCSG-DGVIFYT 123
Cdd:COG2319   60 LLRGHEDSITSIAFSPDGELLLSGSSDGTIkLWDLDNGEKLIKSLEGLHDSSVSKLALSSPDGNSILLASSSlDGTVKLW 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 124 NIEQDAETNRqcQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDILincrraaTSVAICPPV 203
Cdd:COG2319  140 DLSTPGKLIR--TLEGHSESVTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPV-------SSLAFSPDG 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 204 PYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVarfIPSHLSNKSCRVTSlCYSEDGQEILVSYSSDYIYLFDPK 283
Cdd:COG2319  211 GLLIASGSSDGTIRLWD---------------LSTGKL---LRSTLSGHSDSVVS-SFSPDGSLLASGSSDGTIRLWDLR 271

                 ..
gi 568911186 284 DD 285
Cdd:COG2319  272 SS 273
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
41-170 3.87e-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: 70.83  E-value: 3.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctDDKQIVSCSGDGVI 120
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568911186 121 -FYtnieqDAETNRQCQ-FTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFD 170
Cdd:cd00200  244 rVW-----DLRTGECVQtLSGHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
38-294 4.40e-13

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 72.43  E-value: 4.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  38 IQRLKLEATLNVHDGCVNTICWNDTGE-YILSGSDDTKLVISNPYSRKVLTTIRSGHRANIFSAkFLPctDDKQIVSCSG 116
Cdd:COG2319  185 LRTGKPLSTLAGHTDPVSSLAFSPDGGlLIASGSSDGTIRLWDLSTGKLLRSTLSGHSDSVVSS-FSP--DGSLLASGSS 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 117 DGVIFYTNIEQDaetnrQCQFTCHYGTTYEI--MTVPNDPYTFLSCGEDGTVrwfdtRIKTSCTKEDCKDDILINCRRAA 194
Cdd:COG2319  262 DGTIRLWDLRSS-----SSLLRTLSGHSSSVlsVAFSPDGKLLASGSSDGTV-----RLWDLETGKLLSSLTLKGHEGPV 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 195 TSVAICPPVPYYLAVGCSDSSVRIYDRRMLGTRAT---------------GNYAGRGTTGMVAR-------FIPSHLSNK 252
Cdd:COG2319  332 SSLSFSPDGSLLVSGGSDDGTIRLWDLRTGKPLKTleghsnvlsvsfspdGRVVSSGSTDGTVRlwdlstgSLLRNLDGH 411
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568911186 253 SCRVTSLCYSEDGQEILVSYSSDYIYLFDPKDDTARELKTPS 294
Cdd:COG2319  412 TSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSLKSVSFSPD 453
WD40 COG2319
WD40 repeat [General function prediction only];
39-299 1.71e-12

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 70.89  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186  39 QRLKLEATLNVHDGCVNTICW--NDTGEYILSGSD-DTKLVISNPYSRKVLTTIRSGHRANIFSAKFLPctDDKQIVSCS 115
Cdd:COG2319   97 GEKLIKSLEGLHDSSVSKLALssPDGNSILLASSSlDGTVKLWDLSTPGKLIRTLEGHSESVTSLAFSP--DGKLLASGS 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 116 G-DGVIFYTNIEQDAETnrqCQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKE-DCKDDILINCrra 193
Cdd:COG2319  175 SlDGTIKLWDLRTGKPL---STLAGHTDPVSSLAFSPDGGLLIASGSSDGTIRLWDLSTGKLLRSTlSGHSDSVVSS--- 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 194 atsvaiCPPVPYYLAVGCSDSSVRIYDRRMLGTRAtgnyagrgttgmvaRFIPSHLSnkscRVTSLCYSEDGQEILVSYS 273
Cdd:COG2319  249 ------FSPDGSLLASGSSDGTIRLWDLRSSSSLL--------------RTLSGHSS----SVLSVAFSPDGKLLASGSS 304
                        250       260
                 ....*....|....*....|....*.
gi 568911186 274 SDYIYLFDPKDDTARELKTPSAEERR 299
Cdd:COG2319  305 DGTVRLWDLETGKLLSSLTLKGHEGP 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
824-883 1.52e-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: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 824 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
42-77 2.76e-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: 41.91  E-value: 2.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568911186    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
806-883 1.26e-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: 45.02  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911186 806 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:cd00200    4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.25e-04

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 38.88  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568911186   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
797-884 3.38e-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: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 797 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 875
Cdd:cd00200  121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197

                 ....*....
gi 568911186 876 DYDIKIWSP 884
Cdd:cd00200  198 DGTIKLWDL 206
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
826-883 7.44e-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: 7.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568911186 826 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:cd00200   64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
830-884 1.27e-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: 41.94  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568911186 830 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 884
Cdd:cd00200  111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
826-883 2.83e-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: 2.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568911186 826 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:cd00200  232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
844-883 3.56e-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: 36.14  E-value: 3.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568911186   844 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 883
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
802-883 7.90e-03

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 39.69  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911186 802 LVKMVYKGHRNSRTMikeANFWGANFVMSGSDCGHIFIWD-RHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIK 880
Cdd:COG2319  233 LLRSTLSGHSDSVVS---SFSPDGSLLASGSSDGTIRLWDlRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVR 309

                 ...
gi 568911186 881 IWS 883
Cdd:COG2319  310 LWD 312
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
82-120 9.63e-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: 34.60  E-value: 9.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568911186    82 SRKVLTTIRsGHRANIFSAKFLPctDDKQIVSCSGDGVI 120
Cdd:smart00320   1 SGELLKTLK-GHTGPVTSVAFSP--DGKYLASGSDDGTI 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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