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Conserved domains on  [gi|1949290964|gb|KAG0442788|]
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hypothetical protein DMUE_0008 [Dictyocoela muelleri]

Protein Classification

WD40 and DUF2415 superfamily-containing protein( domain architecture ID 1020828)

WD40 and DUF2415 superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF2415 super family cl10524
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
 230-270 7.44e-06

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


The actual alignment was detected with superfamily member pfam10313:

Pssm-ID: 402091  Cd Length: 43  Bit Score: 42.34  E-value: 7.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1949290964 230 GACRNVEFSKTRSL-DLLIFTEHKDYFHIIDTR-NYKKEQIVN 270
Cdd:pfam10313   1 GAFRVCKFSPESGLnDLLVISEHVGRVHLVDLRtGFMNHQVIV 43
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-232 1.21e-05

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 46.17  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964  68 VCLTSKDDFVCVGGIRGNYALKNLKAGNIKCGNVGAT-AVNSIRINDDDMFICV--NKNAIIVLNLKMDYLFDI--PHKW 142
Cdd:cd00200    15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTgPVRDVAASADGTYLASgsSDKTIRLWDLETGECVRTltGHTS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 143 AVNNCELSPNKEFLISVGDSNFVNIIDPkDNFKIVNSTQTISDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLK-KEIF 221
Cdd:cd00200    95 YVSSVAFSPDGRILSSSSRDKTIKVWDV-ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKcVATL 173

                         170
                  ....*....|.
gi 1949290964 222 KSEQSDINGAC 232
Cdd:cd00200   174 TGHTGEVNSVA 184
 
Name Accession Description Interval E-value
DUF2415 pfam10313
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
 230-270 7.44e-06

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


Pssm-ID: 402091  Cd Length: 43  Bit Score: 42.34  E-value: 7.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1949290964 230 GACRNVEFSKTRSL-DLLIFTEHKDYFHIIDTR-NYKKEQIVN 270
Cdd:pfam10313   1 GAFRVCKFSPESGLnDLLVISEHVGRVHLVDLRtGFMNHQVIV 43
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-232 1.21e-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: 46.17  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964  68 VCLTSKDDFVCVGGIRGNYALKNLKAGNIKCGNVGAT-AVNSIRINDDDMFICV--NKNAIIVLNLKMDYLFDI--PHKW 142
Cdd:cd00200    15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTgPVRDVAASADGTYLASgsSDKTIRLWDLETGECVRTltGHTS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 143 AVNNCELSPNKEFLISVGDSNFVNIIDPkDNFKIVNSTQTISDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLK-KEIF 221
Cdd:cd00200    95 YVSSVAFSPDGRILSSSSRDKTIKVWDV-ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKcVATL 173

                         170
                  ....*....|.
gi 1949290964 222 KSEQSDINGAC 232
Cdd:cd00200   174 TGHTGEVNSVA 184
 
Name Accession Description Interval E-value
DUF2415 pfam10313
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
 230-270 7.44e-06

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


Pssm-ID: 402091  Cd Length: 43  Bit Score: 42.34  E-value: 7.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1949290964 230 GACRNVEFSKTRSL-DLLIFTEHKDYFHIIDTR-NYKKEQIVN 270
Cdd:pfam10313   1 GAFRVCKFSPESGLnDLLVISEHVGRVHLVDLRtGFMNHQVIV 43
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-232 1.21e-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: 46.17  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964  68 VCLTSKDDFVCVGGIRGNYALKNLKAGNIKCGNVGAT-AVNSIRINDDDMFICV--NKNAIIVLNLKMDYLFDI--PHKW 142
Cdd:cd00200    15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTgPVRDVAASADGTYLASgsSDKTIRLWDLETGECVRTltGHTS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 143 AVNNCELSPNKEFLISVGDSNFVNIIDPkDNFKIVNSTQTISDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLK-KEIF 221
Cdd:cd00200    95 YVSSVAFSPDGRILSSSSRDKTIKVWDV-ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKcVATL 173

                         170
                  ....*....|.
gi 1949290964 222 KSEQSDINGAC 232
Cdd:cd00200   174 TGHTGEVNSVA 184
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 106-293 6.00e-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: 43.86  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 106 VNSIRINDDDMFICV--NKNAIIVLNLKMDYLFDIP--HKWAVNNCELSPNKEFLISVGDSNFVNIIDPKDNfkivNSTQ 181
Cdd:cd00200    12 VTCVAFSPDGKLLATgsGDGTIKVWDLETGELLRTLkgHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG----ECVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 182 TI---SDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLKkeiFKSEQSDINGACRNVEFSKTrslDLLIFTEHKD-YFHI 257
Cdd:cd00200    88 TLtghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK---CLTTLRGHTDWVNSVAFSPD---GTFVASSSQDgTIKL 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1949290964 258 IDTRNYKKEQIVNIPDKDITGCCFIEDESKIYISTN 293
Cdd:cd00200   162 WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 105-217 1.46e-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: 39.63  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 105 AVNSIRINDDDMFI--CVNKNAIIVLNLKMDYLFDI--PHKWAVNNCELSPNKEFLISVGDSNFVNIIDPkDNFKIVNST 180
Cdd:cd00200   137 WVNSVAFSPDGTFVasSSQDGTIKLWDLRTGKCVATltGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL-STGKCLGTL 215

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1949290964 181 QTISDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLK 217
Cdd:cd00200   216 RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE 252
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 140-302 1.94e-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: 39.24  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 140 HKWAVNNCELSPNKEFLISVGDSNFVNIIDPKDNFKIvnSTQTI-SDSGFKVSWDPTSIYFAVCAQDSYTCVFDIRNLKK 218
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGhTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949290964 219 -EIFKSEQSDINGacrnVEFSKTRSldlLIFTEHKDYFHII-DTRNYKKEQIVNIPDKDITGCCFIEDES---------- 286
Cdd:cd00200    86 vRTLTGHTSYVSS----VAFSPDGR---ILSSSSRDKTIKVwDVETGKCLTTLRGHTDWVNSVAFSPDGTfvasssqdgt 158

                         170
                  ....*....|....*...
gi 1949290964 287 -KIY-ISTNKKIYEYKIH 302
Cdd:cd00200   159 iKLWdLRTGKCVATLTGH 176
 
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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