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Conserved domains on  [gi|32698777|ref|NP_689891|]
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protein DENND6A [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPA super family cl40631
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
270-373 1.21e-16

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.


The actual alignment was detected with superfamily member pfam08616:

Pssm-ID: 454797  Cd Length: 113  Bit Score: 76.17  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777   270 DIFRCFCPVFLHSQMLWELVLLGEPLVVMAPSPS--ESSETVLALVNCISPLKYFSDF----RPYFTIHD-SEFKEYttr 342
Cdd:pfam08616   3 SLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSagEVSEFVLALCNLISGGFVLRGFtnnsFPYVDLSKlDALRKV--- 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 32698777   343 tqapPSVILGVTNPFFAKTLQHWPHIIRIGD 373
Cdd:pfam08616  80 ----PGYIAGVTNPIFENQDQWWDVLCDLDS 106
DENN super family cl11519
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
171-359 1.62e-04

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.


The actual alignment was detected with superfamily member smart00799:

Pssm-ID: 472208  Cd Length: 183  Bit Score: 42.95  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    171 KSLVLISKLPYIHFFHTVLKQIAPEYFEKNE---PYLEAACNDvdrwPAPVPGKTLHLPImgvvmkvriptchdkPGTTQ 247
Cdd:smart00799   3 KCICILSRLPFFELFRKILNELYRLLPSSSNlplELLISLLLY----PVPPPGGSLVLVS---------------LGPGD 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    248 IVQLTQQVDTNISVILPTVHEvdIFRCFCPVFLHSqmLWELVLLGEPLVVMAPSPSESSETVLALVNCISPLKYFSdfrP 327
Cdd:smart00799  64 LIELQRPLDSSLPLIDFSLHE--LFECLGVENILQ--LFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQH---I 136
                          170       180       190
                   ....*....|....*....|....*....|..
gi 32698777    328 YFTIHDSEFKEYTTrtqAPPSVILGVTNPFFA 359
Cdd:smart00799 137 YIPILPASLLDVLS---APTPFIIGVHSSYFE 165
Avl9 super family cl44577
Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It ...
64-201 2.63e-03

Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It has been speculated that Avl9 could play a role in deforming membranes for vesicle fission and/or in recruiting cargo.


The actual alignment was detected with superfamily member pfam09794:

Pssm-ID: 430832 [Multi-domain]  Cd Length: 379  Bit Score: 40.34  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    64 CVCVVGFDLELGQAVEVIYPQHSKLTDREK--TNICYLSFPDS--NSgclgDTQFCFrfrqssgrrvsLHCLLDQFDKDl 139
Cdd:pfam09794   3 GICVVDFHHKRGPEIEFWYPDLDESSDDPSlwKNLPFQALPDGshSF----EEDFSY-----------FTLLYDEPNTG- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32698777   140 pvylkkDPAYFYGYVYFRQV-------RDKTLKRGYFQKSLVLISKLPYIHFFHTVLKQIAPEYFEKNE 201
Cdd:pfam09794  67 ------PLTTLFGISCSRQIkssellkRPADVTRSTVQKAVVVISRLPIFGQIKDKLSIVTNAYFEQGD 129
 
Name Accession Description Interval E-value
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
270-373 1.21e-16

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: 76.17  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777   270 DIFRCFCPVFLHSQMLWELVLLGEPLVVMAPSPS--ESSETVLALVNCISPLKYFSDF----RPYFTIHD-SEFKEYttr 342
Cdd:pfam08616   3 SLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSagEVSEFVLALCNLISGGFVLRGFtnnsFPYVDLSKlDALRKV--- 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 32698777   343 tqapPSVILGVTNPFFAKTLQHWPHIIRIGD 373
Cdd:pfam08616  80 ----PGYIAGVTNPIFENQDQWWDVLCDLDS 106
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
171-359 1.62e-04

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: 42.95  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    171 KSLVLISKLPYIHFFHTVLKQIAPEYFEKNE---PYLEAACNDvdrwPAPVPGKTLHLPImgvvmkvriptchdkPGTTQ 247
Cdd:smart00799   3 KCICILSRLPFFELFRKILNELYRLLPSSSNlplELLISLLLY----PVPPPGGSLVLVS---------------LGPGD 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    248 IVQLTQQVDTNISVILPTVHEvdIFRCFCPVFLHSqmLWELVLLGEPLVVMAPSPSESSETVLALVNCISPLKYFSdfrP 327
Cdd:smart00799  64 LIELQRPLDSSLPLIDFSLHE--LFECLGVENILQ--LFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQH---I 136
                          170       180       190
                   ....*....|....*....|....*....|..
gi 32698777    328 YFTIHDSEFKEYTTrtqAPPSVILGVTNPFFA 359
Cdd:smart00799 137 YIPILPASLLDVLS---APTPFIIGVHSSYFE 165
Avl9 pfam09794
Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It ...
64-201 2.63e-03

Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It has been speculated that Avl9 could play a role in deforming membranes for vesicle fission and/or in recruiting cargo.


Pssm-ID: 430832 [Multi-domain]  Cd Length: 379  Bit Score: 40.34  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    64 CVCVVGFDLELGQAVEVIYPQHSKLTDREK--TNICYLSFPDS--NSgclgDTQFCFrfrqssgrrvsLHCLLDQFDKDl 139
Cdd:pfam09794   3 GICVVDFHHKRGPEIEFWYPDLDESSDDPSlwKNLPFQALPDGshSF----EEDFSY-----------FTLLYDEPNTG- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32698777   140 pvylkkDPAYFYGYVYFRQV-------RDKTLKRGYFQKSLVLISKLPYIHFFHTVLKQIAPEYFEKNE 201
Cdd:pfam09794  67 ------PLTTLFGISCSRQIkssellkRPADVTRSTVQKAVVVISRLPIFGQIKDKLSIVTNAYFEQGD 129
 
Name Accession Description Interval E-value
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
270-373 1.21e-16

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: 76.17  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777   270 DIFRCFCPVFLHSQMLWELVLLGEPLVVMAPSPS--ESSETVLALVNCISPLKYFSDF----RPYFTIHD-SEFKEYttr 342
Cdd:pfam08616   3 SLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSagEVSEFVLALCNLISGGFVLRGFtnnsFPYVDLSKlDALRKV--- 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 32698777   343 tqapPSVILGVTNPFFAKTLQHWPHIIRIGD 373
Cdd:pfam08616  80 ----PGYIAGVTNPIFENQDQWWDVLCDLDS 106
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
171-359 1.62e-04

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: 42.95  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    171 KSLVLISKLPYIHFFHTVLKQIAPEYFEKNE---PYLEAACNDvdrwPAPVPGKTLHLPImgvvmkvriptchdkPGTTQ 247
Cdd:smart00799   3 KCICILSRLPFFELFRKILNELYRLLPSSSNlplELLISLLLY----PVPPPGGSLVLVS---------------LGPGD 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    248 IVQLTQQVDTNISVILPTVHEvdIFRCFCPVFLHSqmLWELVLLGEPLVVMAPSPSESSETVLALVNCISPLKYFSdfrP 327
Cdd:smart00799  64 LIELQRPLDSSLPLIDFSLHE--LFECLGVENILQ--LFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQH---I 136
                          170       180       190
                   ....*....|....*....|....*....|..
gi 32698777    328 YFTIHDSEFKEYTTrtqAPPSVILGVTNPFFA 359
Cdd:smart00799 137 YIPILPASLLDVLS---APTPFIIGVHSSYFE 165
Avl9 pfam09794
Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It ...
64-201 2.63e-03

Transport protein Avl9; Avl9 is a protein involved in exocytic transport from the Golgi. It has been speculated that Avl9 could play a role in deforming membranes for vesicle fission and/or in recruiting cargo.


Pssm-ID: 430832 [Multi-domain]  Cd Length: 379  Bit Score: 40.34  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698777    64 CVCVVGFDLELGQAVEVIYPQHSKLTDREK--TNICYLSFPDS--NSgclgDTQFCFrfrqssgrrvsLHCLLDQFDKDl 139
Cdd:pfam09794   3 GICVVDFHHKRGPEIEFWYPDLDESSDDPSlwKNLPFQALPDGshSF----EEDFSY-----------FTLLYDEPNTG- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32698777   140 pvylkkDPAYFYGYVYFRQV-------RDKTLKRGYFQKSLVLISKLPYIHFFHTVLKQIAPEYFEKNE 201
Cdd:pfam09794  67 ------PLTTLFGISCSRQIkssellkRPADVTRSTVQKAVVVISRLPIFGQIKDKLSIVTNAYFEQGD 129
 
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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