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Conserved domains on  [gi|2169419192|ref|NP_001385654|]
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zinc finger CCCH-type antiviral protein 1 isoform 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 860-969 8.72e-41

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


:

Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 145.93  E-value: 8.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 860 LLFHAACRAHVDYICKNNFEWILHGSRETRYGKGNYFAKEAIYSHKNCSYDIR---NIVMFVARVLVGNVIEGNMTFSSP 936
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2169419192 937 P--------ALYDSCVDTRLNPSVFVIFRKEQIYPEYLIEY 969
Cdd:cd01439    81 PlkpsgvelDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 3.58e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


:

Pssm-ID: 465819  Cd Length: 62  Bit Score: 127.52  E-value: 3.58e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169419192   5 GVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 3.82e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


:

Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.02  E-value: 3.82e-13
                          10        20
                  ....*....|....*....|....*...
gi 2169419192 143 PFFLPEICKSYKGEGRKQTCGQPQPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 685-759 6.90e-12

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 61.54  E-value: 6.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169419192 685 IWYWKNEFNEYIQYGNEspghTSSDINSAYLesffQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHvVRR 759
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE----VSSLIEEAYQ----KGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 860-969 8.72e-41

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 145.93  E-value: 8.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 860 LLFHAACRAHVDYICKNNFEWILHGSRETRYGKGNYFAKEAIYSHKNCSYDIR---NIVMFVARVLVGNVIEGNMTFSSP 936
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2169419192 937 P--------ALYDSCVDTRLNPSVFVIFRKEQIYPEYLIEY 969
Cdd:cd01439    81 PlkpsgvelDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 3.58e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 127.52  E-value: 3.58e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169419192   5 GVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 3.82e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.02  E-value: 3.82e-13
                          10        20
                  ....*....|....*....|....*...
gi 2169419192 143 PFFLPEICKSYKGEGRKQTCGQPQPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 814-969 5.68e-13

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 68.51  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 814 EYVTVSEQFKASMKP-----FKIVRIKRIWNQKLWDAFERKKEKMKNKnemLLFHAACRAHVDYICKNNF-----EWILH 883
Cdd:pfam00644   3 EYQIIEKYFLSTHDPthgypLFILEIFRVQRDGEWERFQPKKKLRNRR---LLWHGSRLTNFLGILSQGLriappEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 884 GsreTRYGKGNYFAKEAIYSHKNCSYDI--RNIVMFVARVLVGNVIE--GNMTFSSPPALYDSCV--------------- 944
Cdd:pfam00644  80 G---YMFGKGIYFADDASKSANYCPPSEahGNGLMLLSEVALGDMNElkKADYAEKLPPGKHSVKglgktapesfvdldg 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419192 945 ------------DTRLNPSVFVIFRKEQIYPEYLIEY 969
Cdd:pfam00644 157 vplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 685-759 6.90e-12

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 61.54  E-value: 6.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169419192 685 IWYWKNEFNEYIQYGNEspghTSSDINSAYLesffQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHvVRR 759
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE----VSSLIEEAYQ----KGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 684-765 9.39e-09

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 52.73  E-value: 9.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192  684 WIWYWKNEFNEYIQYgneSPgHTSSDINSAYL--ESFFQSCPRGvlpfqagsQKYELSFQGMIQTNIASKTQRHvVRRPV 761
Cdd:smart00678   1 YVWEYEGRNGKWWPY---DP-RVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTRK-VRRVT 67


                   ....
gi 2169419192  762 FVSS 765
Cdd:smart00678  68 YSPY 71
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 860-969 8.72e-41

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 145.93  E-value: 8.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 860 LLFHAACRAHVDYICKNNFEWILHGSRETRYGKGNYFAKEAIYSHKNCSYDIR---NIVMFVARVLVGNVIEGNMTFSSP 936
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2169419192 937 P--------ALYDSCVDTRLNPSVFVIFRKEQIYPEYLIEY 969
Cdd:cd01439    81 PlkpsgvelDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 3.58e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 127.52  E-value: 3.58e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169419192   5 GVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 3.82e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.02  E-value: 3.82e-13
                          10        20
                  ....*....|....*....|....*...
gi 2169419192 143 PFFLPEICKSYKGEGRKQTCGQPQPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 814-969 5.68e-13

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 68.51  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 814 EYVTVSEQFKASMKP-----FKIVRIKRIWNQKLWDAFERKKEKMKNKnemLLFHAACRAHVDYICKNNF-----EWILH 883
Cdd:pfam00644   3 EYQIIEKYFLSTHDPthgypLFILEIFRVQRDGEWERFQPKKKLRNRR---LLWHGSRLTNFLGILSQGLriappEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 884 GsreTRYGKGNYFAKEAIYSHKNCSYDI--RNIVMFVARVLVGNVIE--GNMTFSSPPALYDSCV--------------- 944
Cdd:pfam00644  80 G---YMFGKGIYFADDASKSANYCPPSEahGNGLMLLSEVALGDMNElkKADYAEKLPPGKHSVKglgktapesfvdldg 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2169419192 945 ------------DTRLNPSVFVIFRKEQIYPEYLIEY 969
Cdd:pfam00644 157 vplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 685-759 6.90e-12

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 61.54  E-value: 6.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169419192 685 IWYWKNEFNEYIQYGNEspghTSSDINSAYLesffQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHvVRR 759
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE----VSSLIEEAYQ----KGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 684-765 9.39e-09

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 52.73  E-value: 9.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192  684 WIWYWKNEFNEYIQYgneSPgHTSSDINSAYL--ESFFQSCPRGvlpfqagsQKYELSFQGMIQTNIASKTQRHvVRRPV 761
Cdd:smart00678   1 YVWEYEGRNGKWWPY---DP-RVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTRK-VRRVT 67


                   ....
gi 2169419192  762 FVSS 765
Cdd:smart00678  68 YSPY 71
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 805-969 2.14e-04

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 43.74  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 805 FLELNDQDVEYVTVSEQFKASMKP-------------FKIVRIKRIWNQKLWDAF-----ERKKEKMKNKNEMLLFHAAc 866
Cdd:cd01438    18 LLDLAPDDKEYQSVEEEMQSTIREhrdggnaggifnrYNIIRIQKVVNKKLRERYchrqkEIAEENHNHHNERMLFHGS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419192 867 rAHVDYICKNNFEWiLHGSRETRYGKGNYFAKEA------IY---------SHKNCSYDIRNIVMFVARVLVGNVI--EG 929
Cdd:cd01438    97 -PFINAIIHKGFDE-RHAYIGGMFGAGIYFAENSsksnqyVYgigggtgcpTHKDRSCYVCHRQMLFCRVTLGKSFlqFS 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169419192 930 NMTFSSPPALYDSCVDtrlNPSV-------FVIFRKEQIYPEYLIEY 969
Cdd:cd01438   175 AMKMAHAPPGHHSVIG---RPSVnglayaeYVIYRGEQAYPEYLITY 218
 
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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