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Conserved domains on  [gi|237823848]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain. Apc4 contains an N-terminal ...
155-216 3.19e-05

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: 372368  Cd Length: 91  Bit Score: 42.26  E-value: 3.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237823848  155 MKWNPTVpSMVAVCLADGSIAVL----QVTETVKVCATlpsTVAVTSVCWSPKGKQLAVGKQNGTV 216
Cdd:pfam12894   1 LSWCPTM-DLIALATEDGEVLLHrlnwQRVWTLSPPKE---DLEVTSLAWRPDGKLLAVGYSDGTV 62
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
94-265 1.18e-04

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 421866 [Multi-domain]  Cd Length: 289  Bit Score: 43.48  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848  94 PIHHLALSCDNLTLSACMMSSEygsiIAFFDVRTFsneakQQKRPFAYHKllkdagGMVIDMKWNPTvPSMVAVCLADGS 173
Cdd:cd00200   95 YVSSVAFSPDGRILSSSSRDKT----IKVWDVETG-----KCLTTLRGHT------DWVNSVAFSPD-GTFVASSSQDGT 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848 174 IAVLQVtETVKVCATLPS-TVAVTSVCWSPKGKQLAVGKQNGTVVQY-LPTLQEKKVIPCppfyesdHPVRVLDVLWIGT 251
Cdd:cd00200  159 IKLWDL-RTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRG-------HENGVNSVAFSPD 230
                        170
                 ....*....|....
gi 237823848 252 YVFAIVyAAADGTL 265
Cdd:cd00200  231 GYLLAS-GSEDGTI 243
 
Name Accession Description Interval E-value
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain. Apc4 contains an N-terminal ...
155-216 3.19e-05

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: 372368  Cd Length: 91  Bit Score: 42.26  E-value: 3.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237823848  155 MKWNPTVpSMVAVCLADGSIAVL----QVTETVKVCATlpsTVAVTSVCWSPKGKQLAVGKQNGTV 216
Cdd:pfam12894   1 LSWCPTM-DLIALATEDGEVLLHrlnwQRVWTLSPPKE---DLEVTSLAWRPDGKLLAVGYSDGTV 62
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
94-265 1.18e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.48  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848  94 PIHHLALSCDNLTLSACMMSSEygsiIAFFDVRTFsneakQQKRPFAYHKllkdagGMVIDMKWNPTvPSMVAVCLADGS 173
Cdd:cd00200   95 YVSSVAFSPDGRILSSSSRDKT----IKVWDVETG-----KCLTTLRGHT------DWVNSVAFSPD-GTFVASSSQDGT 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848 174 IAVLQVtETVKVCATLPS-TVAVTSVCWSPKGKQLAVGKQNGTVVQY-LPTLQEKKVIPCppfyesdHPVRVLDVLWIGT 251
Cdd:cd00200  159 IKLWDL-RTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRG-------HENGVNSVAFSPD 230
                        170
                 ....*....|....
gi 237823848 252 YVFAIVyAAADGTL 265
Cdd:cd00200  231 GYLLAS-GSEDGTI 243
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
94-216 1.75e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.09  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848  94 PIHHLALSCDNLTLSACmmSSEygSIIAFFDVRTFsneakQQKRPFAYHKllkdagGMVIDMKWNPTvPSMVAVCLADGS 173
Cdd:cd00200  179 EVNSVAFSPDGEKLLSS--SSD--GTIKLWDLSTG-----KCLGTLRGHE------NGVNSVAFSPD-GYLLASGSEDGT 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 237823848 174 IAVLQVtETVKVCATLPS-TVAVTSVCWSPKGKQLAVGKQNGTV 216
Cdd:cd00200  243 IRVWDL-RTGECVQTLSGhTNSVTSLAWSPDGKRLASGSADGTI 285
 
Name Accession Description Interval E-value
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain. Apc4 contains an N-terminal ...
155-216 3.19e-05

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: 372368  Cd Length: 91  Bit Score: 42.26  E-value: 3.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237823848  155 MKWNPTVpSMVAVCLADGSIAVL----QVTETVKVCATlpsTVAVTSVCWSPKGKQLAVGKQNGTV 216
Cdd:pfam12894   1 LSWCPTM-DLIALATEDGEVLLHrlnwQRVWTLSPPKE---DLEVTSLAWRPDGKLLAVGYSDGTV 62
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
94-265 1.18e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.48  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848  94 PIHHLALSCDNLTLSACMMSSEygsiIAFFDVRTFsneakQQKRPFAYHKllkdagGMVIDMKWNPTvPSMVAVCLADGS 173
Cdd:cd00200   95 YVSSVAFSPDGRILSSSSRDKT----IKVWDVETG-----KCLTTLRGHT------DWVNSVAFSPD-GTFVASSSQDGT 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848 174 IAVLQVtETVKVCATLPS-TVAVTSVCWSPKGKQLAVGKQNGTVVQY-LPTLQEKKVIPCppfyesdHPVRVLDVLWIGT 251
Cdd:cd00200  159 IKLWDL-RTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRG-------HENGVNSVAFSPD 230
                        170
                 ....*....|....
gi 237823848 252 YVFAIVyAAADGTL 265
Cdd:cd00200  231 GYLLAS-GSEDGTI 243
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
94-216 1.75e-04

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.09  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237823848  94 PIHHLALSCDNLTLSACmmSSEygSIIAFFDVRTFsneakQQKRPFAYHKllkdagGMVIDMKWNPTvPSMVAVCLADGS 173
Cdd:cd00200  179 EVNSVAFSPDGEKLLSS--SSD--GTIKLWDLSTG-----KCLGTLRGHE------NGVNSVAFSPD-GYLLASGSEDGT 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 237823848 174 IAVLQVtETVKVCATLPS-TVAVTSVCWSPKGKQLAVGKQNGTV 216
Cdd:cd00200  243 IRVWDL-RTGECVQTLSGhTNSVTSLAWSPDGKRLASGSADGTI 285
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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