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Conserved domains on  [gi|56243599|ref|NP_065830|]
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WD repeat-containing protein 35 isoform 2 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 18610525)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 3.11e-10

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETqtddAKLRglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:COG2319  125 SVAFSPDGKTLASGSADGTVRLWDLAT----GKLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMinNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIwGKDLKG--IQLSHVTWSADSKVLLFGMA 176
Cdd:COG2319  190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL-LRTLTGhsGSVRSVAFSPDGRLLASGSA 266


                 ....*...
gi 56243599  177 NGEIHIYD 184
Cdd:COG2319  267 DGTVRLWD 274
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 821-929 5.68e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 46.26  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  821 LAECYYMLEDYEG----LENLAISLPENHKLLPEIAQMFVRVGMCEQAVTAFLKC--SQPKAA------VDTCVHLNQWN 888
Cdd:COG2956   48 LGNLYRRRGEYDRairiHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAealrllAEIYEQEGDWE 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56243599  889 KAVELAKN--HSMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956  128 KAIEVLERllKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 679-870 4.51e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  679 IEDNP-HPRLWRLLAEAALQKLDLYTAEQAFVRC--KDYQGIKFVKRLGKLLSESmkqaevvgyfGRFEEAERTYLEMDR 755
Cdd:COG2956   69 LERDPdRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAEALRLLAEIYEQE----------GDWEKAIEVLERLLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  756 RD---------LAiGLRLKLGDWFRVLQLLKTGSGDADDSLleQANNAIGDYFADRQKWLNAVQYYVQGRNQ-------- 818
Cdd:COG2956  139 LGpenahayceLA-ELYLEQGDYDEAIEALEKALKLDPDCA--RALLLLAELYLEQGDYEEAIAALERALEQdpdylpal 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56243599  819 ERLAECYYMLEDYEGLENL---AISLPENHKLLPEIAQMFVRVGMCEQAVTAFLK 870
Cdd:COG2956  216 PRLAELYEKLGDPEEALELlrkALELDPSDDLLLALADLLERKEGLEAALALLER 270
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 3.11e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETqtddAKLRglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:COG2319  125 SVAFSPDGKTLASGSADGTVRLWDLAT----GKLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMinNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIwGKDLKG--IQLSHVTWSADSKVLLFGMA 176
Cdd:COG2319  190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL-LRTLTGhsGSVRSVAFSPDGRLLASGSA 266


                 ....*...
gi 56243599  177 NGEIHIYD 184
Cdd:COG2319  267 DGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-184 2.25e-09

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: 60.04  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETqtddaklrglaapsnLSMNQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:cd00200  140 SVAFSPDGTFVASSSQDGTIKLWDLRT---------------GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMINNRNKsvVRSMSWNADGQkicivyedgAVIVGSVDGN-RIWgkDLKGIQLSH-----------VTWSA 166
Cdd:cd00200  205 DLSTGKCLGTLRGHENG--VNSVAFSPDGY---------LLASGSEDGTiRVW--DLRTGECVQtlsghtnsvtsLAWSP 271

                        170
                 ....*....|....*...
gi 56243599  167 DSKVLLFGMANGEIHIYD 184
Cdd:cd00200  272 DGKRLASGSADGTIRIWD 289
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 121-184 8.71e-06

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 45.35  E-value: 8.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56243599    121 MSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQL--SHVTWSADSKVLLFGMANGEIHIYD 184
Cdd:pfam12894    1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEDLevTSLAWRPDGKLLAVGYSDGTVRLLD 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 821-929 5.68e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 46.26  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  821 LAECYYMLEDYEG----LENLAISLPENHKLLPEIAQMFVRVGMCEQAVTAFLKC--SQPKAA------VDTCVHLNQWN 888
Cdd:COG2956   48 LGNLYRRRGEYDRairiHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAealrllAEIYEQEGDWE 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56243599  889 KAVELAKN--HSMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956  128 KAIEVLERllKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 679-870 4.51e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  679 IEDNP-HPRLWRLLAEAALQKLDLYTAEQAFVRC--KDYQGIKFVKRLGKLLSESmkqaevvgyfGRFEEAERTYLEMDR 755
Cdd:COG2956   69 LERDPdRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAEALRLLAEIYEQE----------GDWEKAIEVLERLLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  756 RD---------LAiGLRLKLGDWFRVLQLLKTGSGDADDSLleQANNAIGDYFADRQKWLNAVQYYVQGRNQ-------- 818
Cdd:COG2956  139 LGpenahayceLA-ELYLEQGDYDEAIEALEKALKLDPDCA--RALLLLAELYLEQGDYEEAIAALERALEQdpdylpal 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56243599  819 ERLAECYYMLEDYEGLENL---AISLPENHKLLPEIAQMFVRVGMCEQAVTAFLK 870
Cdd:COG2956  216 PRLAELYEKLGDPEEALELlrkALELDPSDDLLLALADLLERKEGLEAALALLER 270
Clathrin pfam00637
Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are ...
 818-909 4.64e-03

Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are composed of multiple alpha helical repeats. They occur in the arm region of the Clathrin heavy chain.


Pssm-ID: 459884 [Multi-domain]  Cd Length: 142  Bit Score: 38.78  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599    818 QERLAECYYMLEDYEGLENLAISLpeNHKLLPEIAQMFVRVGMCEQAVTAFLKCSQPKAAVDTCVHLNQWNKAVELAKNH 897
Cdd:pfam00637   45 QTALIELYAKYDDPEELEEFLKKN--NNYDLEKVAKLCEKADLYEEAVILYKKIGNWKEAISLLKKLGDYKDAIEYAVKS 122

                           90
                   ....*....|..
gi 56243599    898 SMKEIGSLLARY 909
Cdd:pfam00637  123 SNPELWEELLEA 134
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 3.11e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETqtddAKLRglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:COG2319  125 SVAFSPDGKTLASGSADGTVRLWDLAT----GKLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMinNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIwGKDLKG--IQLSHVTWSADSKVLLFGMA 176
Cdd:COG2319  190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL-LRTLTGhsGSVRSVAFSPDGRLLASGSA 266


                 ....*...
gi 56243599  177 NGEIHIYD 184
Cdd:COG2319  267 DGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-184 2.25e-09

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: 60.04  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETqtddaklrglaapsnLSMNQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:cd00200  140 SVAFSPDGTFVASSSQDGTIKLWDLRT---------------GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMINNRNKsvVRSMSWNADGQkicivyedgAVIVGSVDGN-RIWgkDLKGIQLSH-----------VTWSA 166
Cdd:cd00200  205 DLSTGKCLGTLRGHENG--VNSVAFSPDGY---------LLASGSEDGTiRVW--DLRTGECVQtlsghtnsvtsLAWSP 271

                        170
                 ....*....|....*...
gi 56243599  167 DSKVLLFGMANGEIHIYD 184
Cdd:cd00200  272 DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 3.57e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETQtddaKLRglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATG----KLL-----------RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMinNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVD-GNRIWGKDLKGIQLSHVTWSADSKVLLFGMAN 177
Cdd:COG2319  274 DLATGELLRTL--TGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351


                 ....*..
gi 56243599  178 GEIHIYD 184
Cdd:COG2319  352 GTVRLWD 358
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-319 8.94e-09

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: 58.12  E-value: 8.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   19 CVSWNKEQGFIACGGEDGLLKVLKLETQTDDaklrglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVW 98
Cdd:cd00200   14 CVAFSPDGKLLATGSGDGTIKVWDLETGELL---------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   99 MLYKGSWIEEMINnrNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIwGKDLKGIQ--LSHVTWSADSKVLLFGMA 176
Cdd:cd00200   79 DLETGECVRTLTG--HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC-LTTLRGHTdwVNSVAFSPDGTFVASSSQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  177 NGEIHIYDNQGnfmikmkLSClvnvtgaisiagIHWYHGTEGYVE-----PDCPCLAVCFDNGR------------CQIM 239
Cdd:cd00200  156 DGTIKLWDLRT-------GKC------------VATLTGHTGEVNsvafsPDGEKLLSSSSDGTiklwdlstgkclGTLR 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  240 RHENdqnpvlidtgmYVVGIQWNHMGSVLAVAgfqkaamqDKDVNIVQFYTPFGEHLGTLKVPGKEISALSWEGGGLKIA 319
Cdd:cd00200  217 GHEN-----------GVNSVAFSPDGYLLASG--------SEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLA 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 65-184 7.81e-07

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: 52.34  E-value: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   65 QTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVWMLYKGSWIEEMINnrNKSVVRSMSWNADGQKICIVYEDGAVIVGSV 144
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG--HTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56243599  145 DGN---RIWGKDLKGIqlSHVTWSADSKVLLFGMANGEIHIYD 184
Cdd:cd00200   81 ETGecvRTLTGHTSYV--SSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
65-184 1.89e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   65 QTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVWMLYKGSWIEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSV 144
Cdd:COG2319  114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL--TGHSGAVTSVAFSPDGKLL---------ASGSD 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 56243599  145 DGN-RIW----GKDLKGIQ-----LSHVTWSADSKVLLFGMANGEIHIYD 184
Cdd:COG2319  183 DGTvRLWdlatGKLLRTLTghtgaVRSVAFSPDGKLLASGSADGTVRLWD 232
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 121-184 8.71e-06

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 45.35  E-value: 8.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56243599    121 MSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQL--SHVTWSADSKVLLFGMANGEIHIYD 184
Cdd:pfam12894    1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEDLevTSLAWRPDGKLLAVGYSDGTVRLLD 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 821-929 5.68e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 46.26  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  821 LAECYYMLEDYEG----LENLAISLPENHKLLPEIAQMFVRVGMCEQAVTAFLKC--SQPKAA------VDTCVHLNQWN 888
Cdd:COG2956   48 LGNLYRRRGEYDRairiHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAealrllAEIYEQEGDWE 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56243599  889 KAVELAKN--HSMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956  128 KAIEVLERllKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
WD40 COG2319
WD40 repeat [General function prediction only];
47-184 2.16e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.90  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   47 TDDAKLRGLAAPSNLSMNQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVWMLYKGSWIEEMinNRNKSVVRSMSWNAD 126
Cdd:COG2319   54 GAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTL--TGHTGAVRSVAFSPD 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56243599  127 GQKIcivyedgavIVGSVDGN-RIW----GKDLKGIQ-----LSHVTWSADSKVLLFGMANGEIHIYD 184
Cdd:COG2319  132 GKTL---------ASGSADGTvRLWdlatGKLLRTLTghsgaVTSVAFSPDGKLLASGSDDGTVRLWD 190
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 679-870 4.51e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  679 IEDNP-HPRLWRLLAEAALQKLDLYTAEQAFVRC--KDYQGIKFVKRLGKLLSESmkqaevvgyfGRFEEAERTYLEMDR 755
Cdd:COG2956   69 LERDPdRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAEALRLLAEIYEQE----------GDWEKAIEVLERLLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599  756 RD---------LAiGLRLKLGDWFRVLQLLKTGSGDADDSLleQANNAIGDYFADRQKWLNAVQYYVQGRNQ-------- 818
Cdd:COG2956  139 LGpenahayceLA-ELYLEQGDYDEAIEALEKALKLDPDCA--RALLLLAELYLEQGDYEEAIAALERALEQdpdylpal 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56243599  819 ERLAECYYMLEDYEGLENL---AISLPENHKLLPEIAQMFVRVGMCEQAVTAFLK 870
Cdd:COG2956  216 PRLAELYEKLGDPEEALELlrkALELDPSDDLLLALADLLERKEGLEAALALLER 270
WD40 COG2319
WD40 repeat [General function prediction only];
28-150 2.33e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599   28 FIACGGEDGLLKVLKLETqtddAKLRglaapsnlsmnQTLEGHSGSVQVVTWNEQYQKLTTSDENGLIIVWMLYKGSWIE 107
Cdd:COG2319  302 LLASGSDDGTVRLWDLAT----GKLL-----------RTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR 366

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 56243599  108 EMINNRNKsvVRSMSWNADGQKIcivyedgavIVGSVDGN-RIW 150
Cdd:COG2319  367 TLTGHTGA--VTSVAFSPDGRTL---------ASGSADGTvRLW 399
Clathrin pfam00637
Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are ...
 818-909 4.64e-03

Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are composed of multiple alpha helical repeats. They occur in the arm region of the Clathrin heavy chain.


Pssm-ID: 459884 [Multi-domain]  Cd Length: 142  Bit Score: 38.78  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56243599    818 QERLAECYYMLEDYEGLENLAISLpeNHKLLPEIAQMFVRVGMCEQAVTAFLKCSQPKAAVDTCVHLNQWNKAVELAKNH 897
Cdd:pfam00637   45 QTALIELYAKYDDPEELEEFLKKN--NNYDLEKVAKLCEKADLYEEAVILYKKIGNWKEAISLLKKLGDYKDAIEYAVKS 122

                           90
                   ....*....|..
gi 56243599    898 SMKEIGSLLARY 909
Cdd:pfam00637  123 SNPELWEELLEA 134
 
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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