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Conserved domains on  [gi|1370512103|ref|XP_011515236|]
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DENN domain-containing protein 3 isoform X6 [Homo sapiens]

Protein Classification

DENN and dDENN domain-containing protein( domain architecture ID 13071475)

protein containing domains DENN, dDENN, and WD40

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
 185-371 1.98e-52

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


:

Pssm-ID: 460461  Cd Length: 186  Bit Score: 182.00  E-value: 1.98e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  185 FVPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEvdsHIKDFAAK-LSLIPSPPPGPLHLVFNM-KSLQIVLPARADP 262
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLPN---PIERFIANlLYEVPFPPPGRTQKLKPLgGTEPILLQRPEDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  263 ESPILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPT 342
Cdd:pfam02141   78 ELPLEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPT 157

                          170       180
                   ....*....|....*....|....*....
gi 1370512103  343 SFLMGCHLDHFEEVSKEADGLVLINIDHG 371
Cdd:pfam02141  158 PFIIGVHSRYFDLLEDPLDDVVLVDLDTG 186
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
 435-497 1.88e-13

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


:

Pssm-ID: 129037  Cd Length: 69  Bit Score: 66.16  E-value: 1.88e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512103   435 NCQIQQTTLQLLVSIFRDVKNHLNY------EHRVFNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKAR 497
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRElrkepgPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1019-1120 5.07e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 52.72  E-value: 5.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1019 HSFKVGTAKVNCMVMADQNQ-VWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLI-VQDGQEapsnVYSCSMDGMVLVW 1096
Cdd:cd00200      3 RTLKGHTGGVTCVAFSPDGKlLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAaSADGTY----LASGSSDKTIRLW 78

                           90       100
                   ....*....|....*....|....
gi 1370512103 1097 NVSTLQVTSRFQLPRGGLTSIRLH 1120
Cdd:cd00200     79 DLETGECVRTLTGHTSYVSSVAFS 102
uDENN super family cl04085
uDENN domain; This region is always found associated with pfam02141. It is predicted to form ...
 108-158 2.13e-04

uDENN domain; This region is always found associated with pfam02141. It is predicted to form an all beta domain.


The actual alignment was detected with superfamily member pfam03456:

Pssm-ID: 470944  Cd Length: 59  Bit Score: 40.29  E-value: 2.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370512103  108 PEDVAvPGGVDLLTLPQLCFPGGVCVATEPKEDCVHFlVLTDVCGNRTYGV 158
Cdd:pfam03456    8 PEDDW-SDPPLPDGIPMFCFPEGLETLSSREPTFFSF-VLTDEDGSRLYGA 56
 
Name Accession Description Interval E-value
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
 185-371 1.98e-52

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


Pssm-ID: 460461  Cd Length: 186  Bit Score: 182.00  E-value: 1.98e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  185 FVPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEvdsHIKDFAAK-LSLIPSPPPGPLHLVFNM-KSLQIVLPARADP 262
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLPN---PIERFIANlLYEVPFPPPGRTQKLKPLgGTEPILLQRPEDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  263 ESPILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPT 342
Cdd:pfam02141   78 ELPLEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPT 157

                          170       180
                   ....*....|....*....|....*....
gi 1370512103  343 SFLMGCHLDHFEEVSKEADGLVLINIDHG 371
Cdd:pfam02141  158 PFIIGVHSRYFDLLEDPLDDVVLVDLDTG 186
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
 186-371 1.14e-49

Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The DENN domain is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214823  Cd Length: 183  Bit Score: 173.92  E-value: 1.14e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103   186 VPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEVDSHIKdfaakLSLIPSPPPGPLHLVFNMKSL-QIVLPARADPES 264
Cdd:smart00799    1 APKCICILSRLPFFELFRKILNELYRLLPSSSNLPLELLIS-----LLLYPVPPPGGSLVLVSLGPGdLIELQRPLDSSL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103   265 PILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPTSF 344
Cdd:smart00799   76 PLIDFSLHELFECLGVENILQLFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQHIYIPILPASLLDVLSAPTPF 155

                           170       180
                    ....*....|....*....|....*...
gi 1370512103   345 LMGCHLDHFEEVSKEADG-LVLINIDHG 371
Cdd:smart00799  156 IIGVHSSYFEEVKELPDEdVVVVDLDTG 183
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
 435-497 1.88e-13

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 129037  Cd Length: 69  Bit Score: 66.16  E-value: 1.88e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512103   435 NCQIQQTTLQLLVSIFRDVKNHLNY------EHRVFNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKAR 497
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRElrkepgPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1019-1120 5.07e-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: 5.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1019 HSFKVGTAKVNCMVMADQNQ-VWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLI-VQDGQEapsnVYSCSMDGMVLVW 1096
Cdd:cd00200      3 RTLKGHTGGVTCVAFSPDGKlLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAaSADGTY----LASGSSDKTIRLW 78

                           90       100
                   ....*....|....*....|....
gi 1370512103 1097 NVSTLQVTSRFQLPRGGLTSIRLH 1120
Cdd:cd00200     79 DLETGECVRTLTGHTSYVSSVAFS 102
WD40 COG2319
WD40 repeat [General function prediction only];
1004-1117 8.54e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.52  E-value: 8.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1004 GKVTVFNASSWTIhQHSFKVGTAKVNCMVMA-DQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDL-IVQDGQEap 1081
Cdd:COG2319    268 GTVRLWDLATGEL-LRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVaFSPDGKT-- 344

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370512103 1082 snVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSI 1117
Cdd:COG2319    345 --LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV 378
uDENN pfam03456
uDENN domain; This region is always found associated with pfam02141. It is predicted to form ...
 108-158 2.13e-04

uDENN domain; This region is always found associated with pfam02141. It is predicted to form an all beta domain.


Pssm-ID: 460926  Cd Length: 59  Bit Score: 40.29  E-value: 2.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370512103  108 PEDVAvPGGVDLLTLPQLCFPGGVCVATEPKEDCVHFlVLTDVCGNRTYGV 158
Cdd:pfam03456    8 PEDDW-SDPPLPDGIPMFCFPEGLETLSSREPTFFSF-VLTDEDGSRLYGA 56
dDENN pfam03455
dDENN domain; This region is always found associated with pfam02141. It is predicted to form a ...
 464-501 2.26e-04

dDENN domain; This region is always found associated with pfam02141. It is predicted to form a globular domain. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family. This N-terminal region of DENN folds into a longin module, consisting of a central antiparallel beta-sheet layered between helix H1 and helices H2 and H3 (strands S1-S5). Rab35 interacts with dDENN via residues in helix 1 and in the loop S3-S4.


Pssm-ID: 460925  Cd Length: 48  Bit Score: 39.87  E-value: 2.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1370512103  464 FNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKARLNRR 501
Cdd:pfam03455    1 FDKEAFLKSLPSDSRPFLSQFLETQMFNEFIEERLESS 38
 
Name Accession Description Interval E-value
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
 185-371 1.98e-52

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


Pssm-ID: 460461  Cd Length: 186  Bit Score: 182.00  E-value: 1.98e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  185 FVPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEvdsHIKDFAAK-LSLIPSPPPGPLHLVFNM-KSLQIVLPARADP 262
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLPN---PIERFIANlLYEVPFPPPGRTQKLKPLgGTEPILLQRPEDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  263 ESPILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPT 342
Cdd:pfam02141   78 ELPLEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPT 157

                          170       180
                   ....*....|....*....|....*....
gi 1370512103  343 SFLMGCHLDHFEEVSKEADGLVLINIDHG 371
Cdd:pfam02141  158 PFIIGVHSRYFDLLEDPLDDVVLVDLDTG 186
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
 186-371 1.14e-49

Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The DENN domain is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214823  Cd Length: 183  Bit Score: 173.92  E-value: 1.14e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103   186 VPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEVDSHIKdfaakLSLIPSPPPGPLHLVFNMKSL-QIVLPARADPES 264
Cdd:smart00799    1 APKCICILSRLPFFELFRKILNELYRLLPSSSNLPLELLIS-----LLLYPVPPPGGSLVLVSLGPGdLIELQRPLDSSL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103   265 PILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPTSF 344
Cdd:smart00799   76 PLIDFSLHELFECLGVENILQLFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQHIYIPILPASLLDVLSAPTPF 155

                           170       180
                    ....*....|....*....|....*...
gi 1370512103   345 LMGCHLDHFEEVSKEADG-LVLINIDHG 371
Cdd:smart00799  156 IIGVHSSYFEEVKELPDEdVVVVDLDTG 183
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
 435-497 1.88e-13

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 129037  Cd Length: 69  Bit Score: 66.16  E-value: 1.88e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512103   435 NCQIQQTTLQLLVSIFRDVKNHLNY------EHRVFNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKAR 497
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRElrkepgPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1019-1120 5.07e-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: 5.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1019 HSFKVGTAKVNCMVMADQNQ-VWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLI-VQDGQEapsnVYSCSMDGMVLVW 1096
Cdd:cd00200      3 RTLKGHTGGVTCVAFSPDGKlLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAaSADGTY----LASGSSDKTIRLW 78

                           90       100
                   ....*....|....*....|....
gi 1370512103 1097 NVSTLQVTSRFQLPRGGLTSIRLH 1120
Cdd:cd00200     79 DLETGECVRTLTGHTSYVSSVAFS 102
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 982-1186 1.41e-06

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: 51.57  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  982 GHLDPAEKVE--DAHPKLWCALSEGKVTVFNASS----WTIHQHsfkvgTAKVNCMVMADQNQVWVGS-EDSVIYIINVH 1054
Cdd:cd00200     49 GHTGPVRDVAasADGTYLASGSSDKTIRLWDLETgecvRTLTGH-----TSYVSSVAFSPDGRILSSSsRDKTIKVWDVE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1055 SMSCNKQLTAHCSSVTDLIVQdgqeaPSN--VYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLHGGRLWCCTGNSI 1132
Cdd:cd00200    124 TGKCLTTLRGHTDWVNSVAFS-----PDGtfVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSD 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370512103 1133 MVMKM----NGSLHQELKIEENFkdtstsflAFQLLPEEEQLWAACAGR-SEVYIWSLK 1186
Cdd:cd00200    199 GTIKLwdlsTGKCLGTLRGHENG--------VNSVAFSPDGYLLASGSEdGTIRVWDLR 249
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 981-1134 3.65e-06

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: 50.03  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  981 PGHLDPAEKVeDAHPK---LWCALSEGKVTVFNASSW----TIHQHsfkvgTAKVNCM-VMADQNQVWVGSEDSVIYIIN 1052
Cdd:cd00200    132 RGHTDWVNSV-AFSPDgtfVASSSQDGTIKLWDLRTGkcvaTLTGH-----TGEVNSVaFSPDGEKLLSSSSDGTIKLWD 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1053 VHSMSCNKQLTAHCSSVTDLIVqdgqeAPSN--VYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLHGGRLWCCTG- 1129
Cdd:cd00200    206 LSTGKCLGTLRGHENGVNSVAF-----SPDGylLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGs 280


                   ....*..
gi 1370512103 1130 --NSIMV 1134
Cdd:cd00200    281 adGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
1004-1117 8.54e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.52  E-value: 8.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1004 GKVTVFNASSWTIhQHSFKVGTAKVNCMVMA-DQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDL-IVQDGQEap 1081
Cdd:COG2319    268 GTVRLWDLATGEL-LRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVaFSPDGKT-- 344

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370512103 1082 snVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSI 1117
Cdd:COG2319    345 --LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV 378
WD40 COG2319
WD40 repeat [General function prediction only];
1004-1120 2.22e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.37  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1004 GKVTVFNASSWTIhQHSFKVGTAKVNCMVMA-DQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLIV-QDGQEap 1081
Cdd:COG2319    184 GTVRLWDLATGKL-LRTLTGHTGAVRSVAFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDGRL-- 260

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1370512103 1082 snVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLH 1120
Cdd:COG2319    261 --LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS 297
WD40 COG2319
WD40 repeat [General function prediction only];
997-1187 2.22e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.37  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  997 LWCALSEGKVTVFNASSWTIhQHSFKVGTAKVNCMVMA-DQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDL-IV 1074
Cdd:COG2319    219 LASGSADGTVRLWDLATGKL-LRTLTGHSGSVRSVAFSpDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVaFS 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1075 QDGQeapsNVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLH--GGRL-WCCTGNSIMVMKMNGSlhQELKIEENF 1151
Cdd:COG2319    298 PDGK----LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSpdGKTLaSGSDDGTVRLWDLATG--ELLRTLTGH 371

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1370512103 1152 KDTSTSfLAFqlLPEEEQLWAACAGRSeVYIWSLKD 1187
Cdd:COG2319    372 TGAVTS-VAF--SPDGRTLASGSADGT-VRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1002-1097 2.24e-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: 47.71  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1002 SEGKVTVFNASSWTiHQHSFKVGTAKVNCmVMADQNQVWV--GSEDSVIYIINVHSMSCNKQLTAHCSSVTDL-IVQDGQ 1078
Cdd:cd00200    197 SDGTIKLWDLSTGK-CLGTLRGHENGVNS-VAFSPDGYLLasGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLaWSPDGK 274

                           90
                   ....*....|....*....
gi 1370512103 1079 EapsnVYSCSMDGMVLVWN 1097
Cdd:cd00200    275 R----LASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1004-1120 3.63e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.60  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1004 GKVTVFNASSWTIhQHSFKVGTAKVNCMVM-ADQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLIV-QDGQeap 1081
Cdd:COG2319    142 GTVRLWDLATGKL-LRTLTGHSGAVTSVAFsPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDGK--- 217

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1370512103 1082 sNVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLH 1120
Cdd:COG2319    218 -LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS 255
uDENN pfam03456
uDENN domain; This region is always found associated with pfam02141. It is predicted to form ...
 108-158 2.13e-04

uDENN domain; This region is always found associated with pfam02141. It is predicted to form an all beta domain.


Pssm-ID: 460926  Cd Length: 59  Bit Score: 40.29  E-value: 2.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370512103  108 PEDVAvPGGVDLLTLPQLCFPGGVCVATEPKEDCVHFlVLTDVCGNRTYGV 158
Cdd:pfam03456    8 PEDDW-SDPPLPDGIPMFCFPEGLETLSSREPTFFSF-VLTDEDGSRLYGA 56
dDENN pfam03455
dDENN domain; This region is always found associated with pfam02141. It is predicted to form a ...
 464-501 2.26e-04

dDENN domain; This region is always found associated with pfam02141. It is predicted to form a globular domain. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family. This N-terminal region of DENN folds into a longin module, consisting of a central antiparallel beta-sheet layered between helix H1 and helices H2 and H3 (strands S1-S5). Rab35 interacts with dDENN via residues in helix 1 and in the loop S3-S4.


Pssm-ID: 460925  Cd Length: 48  Bit Score: 39.87  E-value: 2.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1370512103  464 FNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKARLNRR 501
Cdd:pfam03455    1 FDKEAFLKSLPSDSRPFLSQFLETQMFNEFIEERLESS 38
WD40 COG2319
WD40 repeat [General function prediction only];
1000-1117 6.37e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.75  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103 1000 ALSEGKVTVFNASSwTIHQHSFKVGTAKVNCMVM-ADQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLIV-QDG 1077
Cdd:COG2319     96 ASADGTVRLWDLAT-GLLLRTLTGHTGAVRSVAFsPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFsPDG 174

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370512103 1078 QeapsNVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSI 1117
Cdd:COG2319    175 K----LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV 210
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
 283-377 4.50e-03

Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque of the spindle pole body. In Aspergillus nidulans the protein member is necessary for stabilization of the polarity axes during septation. and in S. cerevisiae it functions as a polarization-specific docking factor.


Pssm-ID: 400783  Cd Length: 113  Bit Score: 38.04  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512103  283 VLQILTCILTEQRIVFFSSDW----------ALLTLVTECFMAYlYPLQWQHPFVPIlsdQMLDFVMAPTSFLMGCHLDH 352
Cdd:pfam08616   15 IILLINALLTSKRIIFLSYQRsagevsefvlALCNLISGGFVLR-GFTNNSFPYVDL---SKLDALRKVPGYIAGVTNPI 90

                           90       100
                   ....*....|....*....|....*
gi 1370512103  353 FEEVSKEADglVLINIDHGSITYSK 377
Cdd:pfam08616   91 FENQDQWWD--VLCDLDSGSVKLSK 113
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1058-1132 4.87e-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: 40.40  E-value: 4.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370512103 1058 CNKQLTAHCSSVTDLIVQDGQEapsNVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIrlhggrLWCCTGNSI 1132
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDGK---LLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDV------AASADGTYL 66
 
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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