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Conserved domains on  [gi|150170680|ref|NP_001092810|]
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WD repeat-containing protein 35 [Rattus norvegicus]

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 7.22e-10

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQtddsKLRglaapsnlsmnQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATG----KLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSVDGN-RIWgkDLKGIQLCH-----------VTWSA 166
Cdd:COG2319   190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLL---------ASGSADGTvRLW--DLATGKLLRtltghsgsvrsVAFSP 256

                         170
                  ....*....|....*...
gi 150170680  167 DSKILLFGMANGEIHIYD 184
Cdd:COG2319   257 DGRLLASGSADGTVRLWD 274
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 758-929 4.21e-06

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: 49.73  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  758 LAIGLRLKLGDWFRVLQLLKTGSGD-ADDSLLE---------QAHNAIGDYFADRQKWMNAVQYYvkgrnqerlaecyym 827
Cdd:COG2956     1 LLLPVAAALGWYFKGLNYLLNGQPDkAIDLLEEaleldpetvEAHLALGNLYRRRGEYDRAIRIH--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  828 ledyeglENLANSLPENHKLLPEIAQMFVRVGMCEQAVSAFLKC-----NQPKAA---VDTCVHLNQWNKAVELAK--SH 897
Cdd:COG2956    66 -------QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleldpDDAEALrllAEIYEQEGDWEKAIEVLErlLK 138

                         170       180       190
                  ....*....|....*....|....*....|..
gi 150170680  898 SMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956   139 LGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 7.22e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQtddsKLRglaapsnlsmnQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATG----KLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSVDGN-RIWgkDLKGIQLCH-----------VTWSA 166
Cdd:COG2319   190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLL---------ASGSADGTvRLW--DLATGKLLRtltghsgsvrsVAFSP 256

                         170
                  ....*....|....*...
gi 150170680  167 DSKILLFGMANGEIHIYD 184
Cdd:COG2319   257 DGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 18-184 1.66e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   18 KCISWNKDQGFIACGGEDGLLKVLRLETqtddsklrglaapsnLSMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIV 97
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDLRT---------------GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   98 WMLYKGSWYEEMINNRNKsvVRSMSWNADGQkicivyedgAVIVGSVDGN-RIWgkDLKGIQLCH-----------VTWS 165
Cdd:cd00200   204 WDLSTGKCLGTLRGHENG--VNSVAFSPDGY---------LLASGSEDGTiRVW--DLRTGECVQtlsghtnsvtsLAWS 270

                         170
                  ....*....|....*....
gi 150170680  166 ADSKILLFGMANGEIHIYD 184
Cdd:cd00200   271 PDGKRLASGSADGTIRIWD 289
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 758-929 4.21e-06

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: 49.73  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  758 LAIGLRLKLGDWFRVLQLLKTGSGD-ADDSLLE---------QAHNAIGDYFADRQKWMNAVQYYvkgrnqerlaecyym 827
Cdd:COG2956     1 LLLPVAAALGWYFKGLNYLLNGQPDkAIDLLEEaleldpetvEAHLALGNLYRRRGEYDRAIRIH--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  828 ledyeglENLANSLPENHKLLPEIAQMFVRVGMCEQAVSAFLKC-----NQPKAA---VDTCVHLNQWNKAVELAK--SH 897
Cdd:COG2956    66 -------QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleldpDDAEALrllAEIYEQEGDWEKAIEVLErlLK 138

                         170       180       190
                  ....*....|....*....|....*....|..
gi 150170680  898 SMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956   139 LGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 121-184 6.83e-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: 45.73  E-value: 6.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170680   121 MSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQLC--HVTWSADSKILLFGMANGEIHIYD 184
Cdd:pfam12894    1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEDLEvtSLAWRPDGKLLAVGYSDGTVRLLD 66
Clathrin pfam00637
Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are ...
 818-909 8.36e-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: 38.01  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   818 QERLAECYYMLEDYEGLENLANSLpeNHKLLPEIAQMFVRVGMCEQAVSAFLKCNQPKAAVDTCVHLNQWNKAVELAKSH 897
Cdd:pfam00637   45 QTALIELYAKYDDPEELEEFLKKN--NNYDLEKVAKLCEKADLYEEAVILYKKIGNWKEAISLLKKLGDYKDAIEYAVKS 122

                           90
                   ....*....|..
gi 150170680   898 SMKEIGSLLARY 909
Cdd:pfam00637  123 SNPELWEELLEA 134
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 7.22e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQtddsKLRglaapsnlsmnQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATG----KLL-----------RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSVDGN-RIWgkDLKGIQLCH-----------VTWSA 166
Cdd:COG2319   190 DLATGKLLRTL--TGHTGAVRSVAFSPDGKLL---------ASGSADGTvRLW--DLATGKLLRtltghsgsvrsVAFSP 256

                         170
                  ....*....|....*...
gi 150170680  167 DSKILLFGMANGEIHIYD 184
Cdd:COG2319   257 DGRLLASGSADGTVRLWD 274
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 1.22e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQtddsKLRglaapsnlsmnQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDLATG----KLL-----------RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMinNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVD-GNRIWGKDLKGIQLCHVTWSADSKILLFGMAN 177
Cdd:COG2319   274 DLATGELLRTL--TGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351


                  ....*..
gi 150170680  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 ...
 18-184 1.66e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   18 KCISWNKDQGFIACGGEDGLLKVLRLETqtddsklrglaapsnLSMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIV 97
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDLRT---------------GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   98 WMLYKGSWYEEMINNRNKsvVRSMSWNADGQkicivyedgAVIVGSVDGN-RIWgkDLKGIQLCH-----------VTWS 165
Cdd:cd00200   204 WDLSTGKCLGTLRGHENG--VNSVAFSPDGY---------LLASGSEDGTiRVW--DLRTGECVQtlsghtnsvtsLAWS 270

                         170
                  ....*....|....*....
gi 150170680  166 ADSKILLFGMANGEIHIYD 184
Cdd:cd00200   271 PDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-184 4.09e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   17 LKCISWNKDQGFIACGGEDGLLKVLRLETQTDDSKLRG-----------------LAAPSNLSMN----------QNLEG 69
Cdd:cd00200    54 VRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGhtsyvssvafspdgrilSSSSRDKTIKvwdvetgkclTTLRG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   70 HSGAVQVVTWNEQYQKLTTSDQNGLIIVWMLykGSWYEEMINNRNKSVVRSMSWNADGQKICivyedgaviVGSVDGN-R 148
Cdd:cd00200   134 HTDWVNSVAFSPDGTFVASSSQDGTIKLWDL--RTGKCVATLTGHTGEVNSVAFSPDGEKLL---------SSSSDGTiK 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 150170680  149 IWgkDLKGIQL-----------CHVTWSADSKILLFGMANGEIHIYD 184
Cdd:cd00200   203 LW--DLSTGKClgtlrghengvNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-184 5.75e-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: 52.72  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQTDDSKlrglaapsnlsmnqnLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRT---------------LKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMINnrNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIwGKDLKGIQ--LCHVTWSADSKILLFGMA 176
Cdd:cd00200    79 DLETGECVRTLTG--HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC-LTTLRGHTdwVNSVAFSPDGTFVASSSQ 155


                  ....*...
gi 150170680  177 NGEIHIYD 184
Cdd:cd00200   156 DGTIKLWD 163
WD40 COG2319
WD40 repeat [General function prediction only];
19-184 7.60e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.99  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   19 CISWNKDQGFIACGGEDGLLKVLRLETQtddsKLRGLaapsnlsmnqnLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVW 98
Cdd:COG2319   251 SVAFSPDGRLLASGSADGTVRLWDLATG----ELLRT-----------LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   99 MLYKGSWYEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSVDGN-RIWgkDLKGIQLCH-----------VTWSA 166
Cdd:COG2319   316 DLATGKLLRTL--TGHTGAVRSVAFSPDGKTL---------ASGSDDGTvRLW--DLATGELLRtltghtgavtsVAFSP 382

                         170
                  ....*....|....*...
gi 150170680  167 DSKILLFGMANGEIHIYD 184
Cdd:COG2319   383 DGRTLASGSADGTVRLWD 400
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 758-929 4.21e-06

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: 49.73  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  758 LAIGLRLKLGDWFRVLQLLKTGSGD-ADDSLLE---------QAHNAIGDYFADRQKWMNAVQYYvkgrnqerlaecyym 827
Cdd:COG2956     1 LLLPVAAALGWYFKGLNYLLNGQPDkAIDLLEEaleldpetvEAHLALGNLYRRRGEYDRAIRIH--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  828 ledyeglENLANSLPENHKLLPEIAQMFVRVGMCEQAVSAFLKC-----NQPKAA---VDTCVHLNQWNKAVELAK--SH 897
Cdd:COG2956    66 -------QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLleldpDDAEALrllAEIYEQEGDWEKAIEVLErlLK 138

                         170       180       190
                  ....*....|....*....|....*....|..
gi 150170680  898 SMKEIGSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956   139 LGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 121-184 6.83e-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: 45.73  E-value: 6.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170680   121 MSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQLC--HVTWSADSKILLFGMANGEIHIYD 184
Cdd:pfam12894    1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEDLEvtSLAWRPDGKLLAVGYSDGTVRLLD 66
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 67-184 1.05e-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: 48.87  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   67 LEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVWMLYKGswyEEMINNRNKSV-VRSMSWNADGQKICIVYEDGAVivgsvd 145
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG---ELLRTLKGHTGpVRDVAASADGTYLASGSSDKTI------ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 150170680  146 gnRIWgkDLKGIQLCH-----------VTWSADSKILLFGMANGEIHIYD 184
Cdd:cd00200    76 --RLW--DLETGECVRtltghtsyvssVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
20-184 1.69e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   20 ISWNKDQGFIACGGEDGLLKVLRLETQTddsklrglaapsnlsMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVWM 99
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWDLATGL---------------LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  100 LYKGSWYEEMinNRNKSVVRSMSWNADGQKIcivyedgavIVGSVDGN-RIW----GKDLKGIQ-----LCHVTWSADSK 169
Cdd:COG2319   149 LATGKLLRTL--TGHSGAVTSVAFSPDGKLL---------ASGSDDGTvRLWdlatGKLLRTLTghtgaVRSVAFSPDGK 217

                         170
                  ....*....|....*
gi 150170680  170 ILLFGMANGEIHIYD 184
Cdd:COG2319   218 LLASGSADGTVRLWD 232
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 741-929 2.48e-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: 44.33  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  741 GRFEEAERMY---LDMDRRDLAIGLRL-----KLGDWFRVLQLLKTGSGDADDSllEQAHNAIGDYFADRQKWMNAVQYY 812
Cdd:COG2956    90 GLLDRAEELLeklLELDPDDAEALRLLaeiyeQEGDWEKAIEVLERLLKLGPEN--AHAYCELAELYLEQGDYDEAIEAL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  813 VKG--------RNQERLAECYYMLEDYEG----LENLANSLPENHKLLPEIAQmfvrvgmceqavsAFLKCNQPKAAvdt 880
Cdd:COG2956   168 EKAlkldpdcaRALLLLAELYLEQGDYEEaiaaLERALEQDPDYLPALPRLAE-------------LYEKLGDPEEA--- 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 150170680  881 cvhLNQWNKAVELAKSHsmkeigSLLARYASHLLEKNKTLDAIELYRKA 929
Cdd:COG2956   232 ---LELLRKALELDPSD------DLLLALADLLERKEGLEAALALLERQ 271
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 679-870 5.46e-03

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: 40.10  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  679 IEDNP-HPRLWRLLAEAALQKLDLYTAQQAFVRC--KDYQGIKFVKRLGNLQSESMKQAEVIAYFGRFEEA--ERMYLDM 753
Cdd:COG2956    69 LERDPdRAEALLELAQDYLKAGLLDRAEELLEKLleLDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLgpENAHAYC 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680  754 DRRDLAiglrLKLGDWFRVLQLLKTGSGDADDSLleQAHNAIGDYFADRQKWMNAVQYYVKGRNQ--------ERLAECY 825
Cdd:COG2956   149 ELAELY----LEQGDYDEAIEALEKALKLDPDCA--RALLLLAELYLEQGDYEEAIAALERALEQdpdylpalPRLAELY 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 150170680  826 YMLEDYEGLENLANSLPENHKLLPE---IAQMFVRVGMCEQAVSAFLK 870
Cdd:COG2956   223 EKLGDPEEALELLRKALELDPSDDLllaLADLLERKEGLEAALALLER 270
Clathrin pfam00637
Region in Clathrin and VPS; Each region is about 140 amino acids long. The regions are ...
 818-909 8.36e-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: 38.01  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170680   818 QERLAECYYMLEDYEGLENLANSLpeNHKLLPEIAQMFVRVGMCEQAVSAFLKCNQPKAAVDTCVHLNQWNKAVELAKSH 897
Cdd:pfam00637   45 QTALIELYAKYDDPEELEEFLKKN--NNYDLEKVAKLCEKADLYEEAVILYKKIGNWKEAISLLKKLGDYKDAIEYAVKS 122

                           90
                   ....*....|..
gi 150170680   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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