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Conserved domains on  [gi|1958667082|ref|XP_038944801|]
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E3 ubiquitin-protein ligase DZIP3 isoform X8 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HEPN_DZIP3 pfam18738
DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, ...
 419-564 9.62e-43

DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, Ankyrin, CARD, NACHT ATPase, DEATH and LRR in various animal lineages.


:

Pssm-ID: 436703  Cd Length: 144  Bit Score: 151.62  E-value: 9.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 419 PTLLKKELLIHKNVLEpyynHLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPRKGWDMEPPSSDLS 498
Cdd:pfam18738   1 PGTLHKVLAKNKVKLQ----GLRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958667082 499 KSADILRLCKYRDILLSEILMNGLSETQFNSIWKKVSDILLRLGMK--QDDIDKVKENPIENISLDYH 564
Cdd:pfam18738  77 KEADIVRIKYYRNEVYGHASSASVSDADFNDYWKDISDALVRLGGAlyQDAIDDLKTECMDPELEEHY 144
TTC3_DZIP3_dom super family cl41160
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
 252-336 9.78e-15

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


The actual alignment was detected with superfamily member pfam19179:

Pssm-ID: 465988  Cd Length: 116  Bit Score: 70.74  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 252 ICSYLDCERSCEADILKNT-NYKGFFQLMCSKSCCIYFHKICWKKFKNLKYPGESDQSFSGQKCLKDGCAGDMVRMLQCD 330
Cdd:pfam19179  29 VCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSDKNDKDFLQESCLTPDCRGQICKIVIFG 108


                  ....*.
gi 1958667082 331 VPGIVK 336
Cdd:pfam19179 109 STGLVK 114
 
Name Accession Description Interval E-value
HEPN_DZIP3 pfam18738
DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, ...
 419-564 9.62e-43

DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, Ankyrin, CARD, NACHT ATPase, DEATH and LRR in various animal lineages.


Pssm-ID: 436703  Cd Length: 144  Bit Score: 151.62  E-value: 9.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 419 PTLLKKELLIHKNVLEpyynHLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPRKGWDMEPPSSDLS 498
Cdd:pfam18738   1 PGTLHKVLAKNKVKLQ----GLRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958667082 499 KSADILRLCKYRDILLSEILMNGLSETQFNSIWKKVSDILLRLGMK--QDDIDKVKENPIENISLDYH 564
Cdd:pfam18738  77 KEADIVRIKYYRNEVYGHASSASVSDADFNDYWKDISDALVRLGGAlyQDAIDDLKTECMDPELEEHY 144
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
 252-336 9.78e-15

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


Pssm-ID: 465988  Cd Length: 116  Bit Score: 70.74  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 252 ICSYLDCERSCEADILKNT-NYKGFFQLMCSKSCCIYFHKICWKKFKNLKYPGESDQSFSGQKCLKDGCAGDMVRMLQCD 330
Cdd:pfam19179  29 VCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSDKNDKDFLQESCLTPDCRGQICKIVIFG 108


                  ....*.
gi 1958667082 331 VPGIVK 336
Cdd:pfam19179 109 STGLVK 114
 
Name Accession Description Interval E-value
HEPN_DZIP3 pfam18738
DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, ...
 419-564 9.62e-43

DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, Ankyrin, CARD, NACHT ATPase, DEATH and LRR in various animal lineages.


Pssm-ID: 436703  Cd Length: 144  Bit Score: 151.62  E-value: 9.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 419 PTLLKKELLIHKNVLEpyynHLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPRKGWDMEPPSSDLS 498
Cdd:pfam18738   1 PGTLHKVLAKNKVKLQ----GLRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958667082 499 KSADILRLCKYRDILLSEILMNGLSETQFNSIWKKVSDILLRLGMK--QDDIDKVKENPIENISLDYH 564
Cdd:pfam18738  77 KEADIVRIKYYRNEVYGHASSASVSDADFNDYWKDISDALVRLGGAlyQDAIDDLKTECMDPELEEHY 144
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
 252-336 9.78e-15

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


Pssm-ID: 465988  Cd Length: 116  Bit Score: 70.74  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667082 252 ICSYLDCERSCEADILKNT-NYKGFFQLMCSKSCCIYFHKICWKKFKNLKYPGESDQSFSGQKCLKDGCAGDMVRMLQCD 330
Cdd:pfam19179  29 VCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSDKNDKDFLQESCLTPDCRGQICKIVIFG 108


                  ....*.
gi 1958667082 331 VPGIVK 336
Cdd:pfam19179 109 STGLVK 114
 
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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