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Conserved domains on  [gi|2217347035|ref|XP_047305211|]
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E3 ubiquitin-protein ligase DZIP3 isoform X3 [Homo sapiens]

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, ...
418-563 6.36e-42

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: 150.07  E-value: 6.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  418 PPLLKKELLIHKNVLESyynhLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPKKGWNMEPPSSDIS 497
Cdd:pfam18738    1 PGTLHKVLAKNKVKLQG----LRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217347035  498 KSADILRLCKYRDILLSEILMNGLTESQFNSIWKKVSDILLRLGMM--QEDIDKVKENPIENISLDYH 563
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 ...
224-335 1.31e-14

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: 71.12  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  224 DEDLPTTFKDLLNNFIKTTESNIMKQTICSYLDCERSCEADILKNT-SYKGFFQLMCSKSCCVYFHKICWKKFKNLKYPG 302
Cdd:pfam19179    2 EETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSD 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217347035  303 ENDQSFSGKKCLKEGCTGDMVRMLQCDVPGIVK 335
Cdd:pfam19179   82 KNDKDFLQESCLTPDCRGQICKIVIFGSTGLVK 114
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
748-939 5.53e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  748 KERLARQRQLYKLhyqcedfKRQLRTVTFRWQENQMQIKKKDKIIASLNQQVAFGINKVSKLQRQIHAKDNEIKNLKEQL 827
Cdd:COG4942     20 DAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  828 SMKRSQWEMEKHNLESTMKTY-----VSKLN--------AETSRALTAEVYFLQCRRDFG------LLHLEQTEKECLNQ 888
Cdd:COG4942     93 AELRAELEAQKEELAELLRALyrlgrQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeelradLAELAALRAELEAE 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217347035  889 LARVTHMAASNLESLQ-LKAAVDSWNAIVADVRNKIAFLRTQYNEQINKVKQ 939
Cdd:COG4942    173 RAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
 
Name Accession Description Interval E-value
HEPN_DZIP3 pfam18738
DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, ...
418-563 6.36e-42

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: 150.07  E-value: 6.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  418 PPLLKKELLIHKNVLESyynhLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPKKGWNMEPPSSDIS 497
Cdd:pfam18738    1 PGTLHKVLAKNKVKLQG----LRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217347035  498 KSADILRLCKYRDILLSEILMNGLTESQFNSIWKKVSDILLRLGMM--QEDIDKVKENPIENISLDYH 563
Cdd:pfam18738   77 KEADIVRIKYYRNEVYGHASSASVSDADFNDYWKDISDALVRLGGAlyQDAIDDLKTECMDPELEEHY 144
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
224-335 1.31e-14

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: 71.12  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  224 DEDLPTTFKDLLNNFIKTTESNIMKQTICSYLDCERSCEADILKNT-SYKGFFQLMCSKSCCVYFHKICWKKFKNLKYPG 302
Cdd:pfam19179    2 EETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSD 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217347035  303 ENDQSFSGKKCLKEGCTGDMVRMLQCDVPGIVK 335
Cdd:pfam19179   82 KNDKDFLQESCLTPDCRGQICKIVIFGSTGLVK 114
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
748-939 5.53e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  748 KERLARQRQLYKLhyqcedfKRQLRTVTFRWQENQMQIKKKDKIIASLNQQVAFGINKVSKLQRQIHAKDNEIKNLKEQL 827
Cdd:COG4942     20 DAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  828 SMKRSQWEMEKHNLESTMKTY-----VSKLN--------AETSRALTAEVYFLQCRRDFG------LLHLEQTEKECLNQ 888
Cdd:COG4942     93 AELRAELEAQKEELAELLRALyrlgrQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeelradLAELAALRAELEAE 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217347035  889 LARVTHMAASNLESLQ-LKAAVDSWNAIVADVRNKIAFLRTQYNEQINKVKQ 939
Cdd:COG4942    173 RAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
 
Name Accession Description Interval E-value
HEPN_DZIP3 pfam18738
DZIP3/ hRUL138-like HEPN; DZIP3/ hRUL138-like HEPN nuclease. Fusion to TPR, Zn-ribbon, RING, ...
418-563 6.36e-42

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: 150.07  E-value: 6.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  418 PPLLKKELLIHKNVLESyynhLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPKKGWNMEPPSSDIS 497
Cdd:pfam18738    1 PGTLHKVLAKNKVKLQG----LRKKVLNPSQWDKLYPPSGSSVSSQDFDITLLYLLLRNICGLTPPSTGWDNLPPATDTS 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217347035  498 KSADILRLCKYRDILLSEILMNGLTESQFNSIWKKVSDILLRLGMM--QEDIDKVKENPIENISLDYH 563
Cdd:pfam18738   77 KEADIVRIKYYRNEVYGHASSASVSDADFNDYWKDISDALVRLGGAlyQDAIDDLKTECMDPELEEHY 144
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
224-335 1.31e-14

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: 71.12  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  224 DEDLPTTFKDLLNNFIKTTESNIMKQTICSYLDCERSCEADILKNT-SYKGFFQLMCSKSCCVYFHKICWKKFKNLKYPG 302
Cdd:pfam19179    2 EETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDpDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFSD 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217347035  303 ENDQSFSGKKCLKEGCTGDMVRMLQCDVPGIVK 335
Cdd:pfam19179   82 KNDKDFLQESCLTPDCRGQICKIVIFGSTGLVK 114
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
748-939 5.53e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  748 KERLARQRQLYKLhyqcedfKRQLRTVTFRWQENQMQIKKKDKIIASLNQQVAFGINKVSKLQRQIHAKDNEIKNLKEQL 827
Cdd:COG4942     20 DAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217347035  828 SMKRSQWEMEKHNLESTMKTY-----VSKLN--------AETSRALTAEVYFLQCRRDFG------LLHLEQTEKECLNQ 888
Cdd:COG4942     93 AELRAELEAQKEELAELLRALyrlgrQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeelradLAELAALRAELEAE 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217347035  889 LARVTHMAASNLESLQ-LKAAVDSWNAIVADVRNKIAFLRTQYNEQINKVKQ 939
Cdd:COG4942    173 RAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
 
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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