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Conserved domains on  [gi|134047967|sp|Q9H7D7|]
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RecName: Full=WD repeat-containing protein 26; AltName: Full=CUL4- and DDB1-associated WDR protein 2; AltName: Full=Myocardial ischemic preconditioning up-regulated protein 2

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
347-641 2.96e-49

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.41  E-value: 2.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 347 TQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWqvdpDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDcsE 426
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW----DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG--T 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 427 LWLWNVQTGELRTKMsQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLD-GNLLDSWEG--VRVQCLWCLSDGKTVLAS 503
Cdd:COG2319  186 VRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAtGKLLRTLTGhsGSVRSVAFSPDGRLLASG 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 504 DTHQRIRGYnfeDLTDRNIVQ----EDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIhsCFG 579
Cdd:COG2319  265 SADGTVRLW---DLATGELLRtltgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV--AFS 339
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134047967 580 gHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:COG2319  340 -PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLASGSADGTVRLW 399
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
156-231 1.64e-05

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 42.56  E-value: 1.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047967   156 EHPSATKFRNHVMEGDWDKAENDLNELKPlvhsphaivvrgaleisqTLLGIIVRMKFLLLQQKYLEYLEDGKVLE 231
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKP------------------PLLERNSKLEFELRKQKFLELVRQGKLEE 58
LisH_TPL super family cl39307
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
126-153 2.31e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


The actual alignment was detected with superfamily member pfam17814:

Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.31e-05
                          10        20
                  ....*....|....*....|....*...
gi 134047967  126 DVIRLIGQHLNGLGLNQTVDLLMQESGC 153
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
347-641 2.96e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.41  E-value: 2.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 347 TQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWqvdpDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDcsE 426
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW----DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG--T 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 427 LWLWNVQTGELRTKMsQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLD-GNLLDSWEG--VRVQCLWCLSDGKTVLAS 503
Cdd:COG2319  186 VRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAtGKLLRTLTGhsGSVRSVAFSPDGRLLASG 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 504 DTHQRIRGYnfeDLTDRNIVQ----EDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIhsCFG 579
Cdd:COG2319  265 SADGTVRLW---DLATGELLRtltgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV--AFS 339
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134047967 580 gHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:COG2319  340 -PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
349-641 3.37e-44

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: 159.81  E-value: 3.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 349 QILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPDTHLLKLlktlEGHAYGVSYIAWSPDDNYLVACGPDDCseLW 428
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL----KGHTGPVRDVAASADGTYLASGSSDKT--IR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 429 LWNVQTGELRTKMSQsHEDSLTSVAWNPDGKRFVTGGQrgqfyqcdlDGNLLdSWEGVRVQCL----------WCLS--- 495
Cdd:cd00200   77 LWDLETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSR---------DKTIK-VWDVETGKCLttlrghtdwvNSVAfsp 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 496 DGKTVLASDTHQRIRGYNFEDL-TDRNIVQEDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTI 574
Cdd:cd00200  146 DGTFVASSSQDGTIKLWDLRTGkCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSV 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134047967 575 hsCFGGHNeDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQIPsMMASASDDGTVRIW 641
Cdd:cd00200  226 --AFSPDG-YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGK-RLASGSADGTIRIW 288
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
605-641 4.40e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 4.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 134047967   605 PIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
605-641 2.82e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.82e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 134047967  605 PIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
577-641 6.86e-06

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 49.18  E-value: 6.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134047967 577 CFgghnEDFIASGSEDHKVYIWHKRSEL--------PIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIW 641
Cdd:PTZ00420  85 CF----SEILASGSEDLTIRVWEIPHNDesvkeikdPQCILKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIW 153
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
156-231 1.64e-05

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 42.56  E-value: 1.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047967   156 EHPSATKFRNHVMEGDWDKAENDLNELKPlvhsphaivvrgaleisqTLLGIIVRMKFLLLQQKYLEYLEDGKVLE 231
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKP------------------PLLERNSKLEFELRKQKFLELVRQGKLEE 58
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
126-153 2.31e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.31e-05
                          10        20
                  ....*....|....*....|....*...
gi 134047967  126 DVIRLIGQHLNGLGLNQTVDLLMQESGC 153
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
347-641 2.96e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.41  E-value: 2.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 347 TQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWqvdpDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDcsE 426
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW----DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG--T 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 427 LWLWNVQTGELRTKMsQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLD-GNLLDSWEG--VRVQCLWCLSDGKTVLAS 503
Cdd:COG2319  186 VRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAtGKLLRTLTGhsGSVRSVAFSPDGRLLASG 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 504 DTHQRIRGYnfeDLTDRNIVQ----EDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIhsCFG 579
Cdd:COG2319  265 SADGTVRLW---DLATGELLRtltgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV--AFS 339
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134047967 580 gHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:COG2319  340 -PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLASGSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
348-641 2.01e-46

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 169.32  E-value: 2.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 348 QQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPdthlLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDcsEL 427
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLAT----GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADG--TV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 428 WLWNVQTGELRTKMSqSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLD-GNLLDSWEG--VRVQCLWCLSDGKTVLASD 504
Cdd:COG2319  145 RLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGhtGAVRSVAFSPDGKLLASGS 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 505 THQRIRGYnfeDLTDRNIVQE----DHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIhsCFGG 580
Cdd:COG2319  224 ADGTVRLW---DLATGKLLRTltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSV--AFSP 298
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134047967 581 hNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:COG2319  299 -DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD-GKTLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
349-641 3.37e-44

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: 159.81  E-value: 3.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 349 QILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPDTHLLKLlktlEGHAYGVSYIAWSPDDNYLVACGPDDCseLW 428
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL----KGHTGPVRDVAASADGTYLASGSSDKT--IR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 429 LWNVQTGELRTKMSQsHEDSLTSVAWNPDGKRFVTGGQrgqfyqcdlDGNLLdSWEGVRVQCL----------WCLS--- 495
Cdd:cd00200   77 LWDLETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSR---------DKTIK-VWDVETGKCLttlrghtdwvNSVAfsp 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 496 DGKTVLASDTHQRIRGYNFEDL-TDRNIVQEDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTI 574
Cdd:cd00200  146 DGTFVASSSQDGTIKLWDLRTGkCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSV 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134047967 575 hsCFGGHNeDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQIPsMMASASDDGTVRIW 641
Cdd:cd00200  226 --AFSPDG-YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGK-RLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
351-641 1.95e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 1.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 351 LTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWqvdpDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDdcSELWLW 430
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLL----DAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD--GTVRLW 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 431 NVQTGELRTKmSQSHEDSLTSVAWNPDGKRFVTGGQrgqfyqcdlDGnlldsweGVRvqcLWCLSDGKTVlasdthQRIR 510
Cdd:COG2319  106 DLATGLLLRT-LTGHTGAVRSVAFSPDGKTLASGSA---------DG-------TVR---LWDLATGKLL------RTLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 511 GYnfedltdrnivqeDHPIMSFTISKNGRLallnvatqgvhlwdlqdrvlvrkyqgvtqgfytihscfgghnedfIASGS 590
Cdd:COG2319  160 GH-------------SGAVTSVAFSPDGKL---------------------------------------------LASGS 181
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 134047967 591 EDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:COG2319  182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD-GKLLASGSADGTVRLW 231
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
345-466 3.66e-19

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.16  E-value: 3.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 345 CYTQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWqvdpDTHLLKLLKTLEGHAYGVSYIAWSPdDNYLVACGPDDC 424
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW----DLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDG 241
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 134047967 425 SeLWLWNVQTGELrTKMSQSHEDSLTSVAWNPDGKRFVTGGQ 466
Cdd:cd00200  242 T-IRVWDLRTGEC-VQTLSGHTNSVTSLAWSPDGKRLASGSA 281
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
351-478 7.80e-09

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 55.06  E-value: 7.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 351 LTEHCNEVWFCKFSNDGTKLA-TGSKDTTVIIWQVDPDTHLLKLLKTLEGHAYGVSyiaWSPDDNYLV-ACGPDDCSELW 428
Cdd:COG0823   26 LTNSPGIDTSPAWSPDGRRIAfTSDRGGGPQIYVVDADGGEPRRLTFGGGYNASPS---WSPDGKRLAfVSRSDGRFDIY 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 134047967 429 LWNVQTGELRTkmsqsHEDSLTSVAWNPDGKRFV---TGGQRGQFYQCDLDGN 478
Cdd:COG0823  103 VLDLDGGAPRR-----LTDGPGSPSWSPDGRRIVfssDRGGRPDLYVVDLDGR 150
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
605-641 4.40e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 4.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 134047967   605 PIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
605-641 2.82e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.82e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 134047967  605 PIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
577-641 6.86e-06

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 49.18  E-value: 6.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134047967 577 CFgghnEDFIASGSEDHKVYIWHKRSEL--------PIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIW 641
Cdd:PTZ00420  85 CF----SEILASGSEDLTIRVWEIPHNDesvkeikdPQCILKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIW 153
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
349-382 1.38e-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: 42.30  E-value: 1.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 134047967   349 QILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIW 382
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
156-231 1.64e-05

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 42.56  E-value: 1.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047967   156 EHPSATKFRNHVMEGDWDKAENDLNELKPlvhsphaivvrgaleisqTLLGIIVRMKFLLLQQKYLEYLEDGKVLE 231
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKP------------------PLLERNSKLEFELRKQKFLELVRQGKLEE 58
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
126-153 2.31e-05

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 41.61  E-value: 2.31e-05
                          10        20
                  ....*....|....*....|....*...
gi 134047967  126 DVIRLIGQHLNGLGLNQTVDLLMQESGC 153
Cdd:pfam17814   3 DVVRLILQFLKENGLHRTLQALQTESGV 30
WD40 COG2319
WD40 repeat [General function prediction only];
349-385 3.64e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 3.64e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 134047967 349 QILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVD 385
Cdd:COG2319  366 RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 pfam00400
WD domain, G-beta repeat;
348-382 4.03e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 4.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 134047967  348 QQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIW 382
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
605-641 9.38e-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: 44.63  E-value: 9.38e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 134047967 605 PIAELTGHTRTVNCVSWNPQiPSMMASASDDGTVRIW 641
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPD-GKLLATGSGDGTIKVW 36
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
586-641 9.66e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.85  E-value: 9.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 134047967 586 IASGSEDHKVYIWHKRS-ELPIAELTGHTRTVNCVSWNPQipSMMASASDDGTVRIW 641
Cdd:PLN00181 633 LAFGSADHKVYYYDLRNpKLPLCTMIGHSKTVSYVRFVDS--STLVSSSTDNTLKLW 687
PTZ00421 PTZ00421
coronin; Provisional
366-493 1.17e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.27  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 366 DGTKLATGSKDTTVIIWQVDPDTHLLKLLK---TLEGHAYGVSYIAWSPD-DNYLVACGPDdcSELWLWNVQTGELRTKM 441
Cdd:PTZ00421  87 DPQKLFTASEDGTIMGWGIPEEGLTQNISDpivHLQGHTKKVGIVSFHPSaMNVLASAGAD--MVVNVWDVERGKAVEVI 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 134047967 442 SqSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCD-LDGNLLDSWE---GVRVQ-CLWC 493
Cdd:PTZ00421 165 K-CHSDQITSLEWNLDGSLLCTTSKDKKLNIIDpRDGTIVSSVEahaSAKSQrCLWA 220
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
362-459 1.43e-04

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 45.03  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967  362 KFSNDGTKLATGSKDTTviIW----------QVDPDthllkllktleGHAYGVSYIAWSPDDNYLV--ACGPDDCSELWL 429
Cdd:COG4946   395 VWSPDGKKIAFTDNRGR--LWvvdlasgkvrKVDTD-----------GYGDGISDLAWSPDSKWLAysKPGPNQLSQIFL 461
                          90       100       110
                  ....*....|....*....|....*....|
gi 134047967  430 WNVQTGELrTKMSQSHEDSlTSVAWNPDGK 459
Cdd:COG4946   462 YDVETGKT-VQLTDGRYDD-GSPAFSPDGK 489
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
577-641 2.91e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.92  E-value: 2.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047967 577 CFGGHNEDFIASGSEDHKVYIWH-KRSELpIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIW 641
Cdd:PLN00181 539 CWNSYIKSQVASSNFEGVVQVWDvARSQL-VTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLW 603
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
407-463 3.07e-04

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 42.26  E-value: 3.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 134047967  407 IAWSPDDNYLVACGPDDCS-ELWLWNVQTgelRTKMSQSHEDSLTSVAWNPDGKRFVT 463
Cdd:pfam08662 106 IFWSPFGRLVLLAGFGNLAgDIEFWDVVN---KKKIATAEASNATLCEWSPDGRYFLT 160
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
349-383 3.05e-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: 40.01  E-value: 3.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 134047967 349 QILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQ 383
Cdd:cd00200  255 QTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
363-459 4.27e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.41  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967  363 FSNDGTKLA-----TGSKDttviIWQVDPDTHLLKLLKTLEGHAYgVSYIAWSPDDNYLVACgpDDCSELWLWNVQTGEL 437
Cdd:COG4946   350 WSPDGKSIAyfsdaSGEYE----LYIAPADGSGEPKQLTLGDLGR-VFNPVWSPDGKKIAFT--DNRGRLWVVDLASGKV 422
                          90       100
                  ....*....|....*....|..
gi 134047967  438 RTKMSQSHEDSLTSVAWNPDGK 459
Cdd:COG4946   423 RKVDTDGYGDGISDLAWSPDSK 444
PTZ00420 PTZ00420
coronin; Provisional
605-641 6.19e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 39.55  E-value: 6.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 134047967 605 PIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIW 641
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVW 102
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
425-539 7.68e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 37.73  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047967 425 SELWLWNVQTGELRTKMSQSHEDslTSVAWNPDGKRFV---TGGQRGQFYQCDLDGN---LLDSWEGVRVQCLWcLSDGK 498
Cdd:COG0823   11 SDIYVVDLDGGEPRRLTNSPGID--TSPAWSPDGRRIAftsDRGGGPQIYVVDADGGeprRLTFGGGYNASPSW-SPDGK 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 134047967 499 TVL---ASDTHQRIRGYNFEDLTDRNIVQEDHpimSFTISKNGR 539
Cdd:COG0823   88 RLAfvsRSDGRFDIYVLDLDGGAPRRLTDGPG---SPSWSPDGR 128
 
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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