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Conserved domains on  [gi|564344724|ref|XP_006235736|]
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Z-DNA-binding protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
z-alpha super family cl02659
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 10-68 1.12e-14

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


The actual alignment was detected with superfamily member smart00550:

Pssm-ID: 295419  Cd Length: 68  Bit Score: 68.52  E-value: 1.12e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564344724    10 TGDNLEQKILQVLSDAGSP-VQIDQLLKKLQVPKKILNQVLYRLKKEGRVSSPA--PATWSL 68
Cdd:smart00550   3 TQDSLEEKILEFLENSGDEtSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGgtPPLWKL 64
z-alpha super family cl02659
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 85-149 6.57e-14

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


The actual alignment was detected with superfamily member smart00550:

Pssm-ID: 295419  Cd Length: 68  Bit Score: 66.21  E-value: 6.57e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564344724    85 SAAQPSLEERILRFLETKGPQ--RALHIAKALGMTTaKEVNPILYSMRNKHLLTVSDT--QMWTIYRSS 149
Cdd:smart00550   1 SLTQDSLEEKILEFLENSGDEtsTALQLAKNLGLPK-KEVNRVLYSLEKKGKVCKQGGtpPLWKLTDKA 68
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 184-204 7.84e-05

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


:

Pssm-ID: 463679  Cd Length: 21  Bit Score: 39.25  E-value: 7.84e-05
                          10        20
                  ....*....|....*....|.
gi 564344724  184 SLISISNSKAIQIGHGNVMSR 204
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMSI 21
 
Name Accession Description Interval E-value
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 10-68 1.12e-14

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.


Pssm-ID: 128823  Cd Length: 68  Bit Score: 68.52  E-value: 1.12e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564344724    10 TGDNLEQKILQVLSDAGSP-VQIDQLLKKLQVPKKILNQVLYRLKKEGRVSSPA--PATWSL 68
Cdd:smart00550   3 TQDSLEEKILEFLENSGDEtSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGgtPPLWKL 64
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 85-149 6.57e-14

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.


Pssm-ID: 128823  Cd Length: 68  Bit Score: 66.21  E-value: 6.57e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564344724    85 SAAQPSLEERILRFLETKGPQ--RALHIAKALGMTTaKEVNPILYSMRNKHLLTVSDT--QMWTIYRSS 149
Cdd:smart00550   1 SLTQDSLEEKILEFLENSGDEtsTALQLAKNLGLPK-KEVNRVLYSLEKKGKVCKQGGtpPLWKLTDKA 68
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 184-204 7.84e-05

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


Pssm-ID: 463679  Cd Length: 21  Bit Score: 39.25  E-value: 7.84e-05
                          10        20
                  ....*....|....*....|.
gi 564344724  184 SLISISNSKAIQIGHGNVMSR 204
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMSI 21
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 13-68 2.88e-04

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 39.03  E-value: 2.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564344724   13 NLEQKILQVL--SDAGSPVQIDQLLKKLQVPKKILNQVLYRLKKEGRVSSPA--PATWSL 68
Cdd:pfam02295   4 ECAEKILELLenLGEGKAATAIALERGLSTPKREINRVLYDLERKGDVYREDgtPPRWFL 63
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 90-140 1.98e-03

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 36.72  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564344724   90 SLEERILRFLETKGPQR-ALHIAKALGMTT-AKEVNPILYSMRNKHLLTVSDT 140
Cdd:pfam02295   4 ECAEKILELLENLGEGKaATAIALERGLSTpKREINRVLYDLERKGDVYREDG 56
 
Name Accession Description Interval E-value
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 10-68 1.12e-14

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.


Pssm-ID: 128823  Cd Length: 68  Bit Score: 68.52  E-value: 1.12e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564344724    10 TGDNLEQKILQVLSDAGSP-VQIDQLLKKLQVPKKILNQVLYRLKKEGRVSSPA--PATWSL 68
Cdd:smart00550   3 TQDSLEEKILEFLENSGDEtSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGgtPPLWKL 64
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 85-149 6.57e-14

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.


Pssm-ID: 128823  Cd Length: 68  Bit Score: 66.21  E-value: 6.57e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564344724    85 SAAQPSLEERILRFLETKGPQ--RALHIAKALGMTTaKEVNPILYSMRNKHLLTVSDT--QMWTIYRSS 149
Cdd:smart00550   1 SLTQDSLEEKILEFLENSGDEtsTALQLAKNLGLPK-KEVNRVLYSLEKKGKVCKQGGtpPLWKLTDKA 68
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 184-204 7.84e-05

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


Pssm-ID: 463679  Cd Length: 21  Bit Score: 39.25  E-value: 7.84e-05
                          10        20
                  ....*....|....*....|.
gi 564344724  184 SLISISNSKAIQIGHGNVMSR 204
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMSI 21
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 13-68 2.88e-04

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 39.03  E-value: 2.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564344724   13 NLEQKILQVL--SDAGSPVQIDQLLKKLQVPKKILNQVLYRLKKEGRVSSPA--PATWSL 68
Cdd:pfam02295   4 ECAEKILELLenLGEGKAATAIALERGLSTPKREINRVLYDLERKGDVYREDgtPPRWFL 63
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 90-140 1.98e-03

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 36.72  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564344724   90 SLEERILRFLETKGPQR-ALHIAKALGMTT-AKEVNPILYSMRNKHLLTVSDT 140
Cdd:pfam02295   4 ECAEKILELLENLGEGKaATAIALERGLSTpKREINRVLYDLERKGDVYREDG 56
 
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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