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Conserved domains on  [gi|533184917|ref|XP_005405506|]
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PREDICTED: zinc finger CCCH-type antiviral protein 1 [Chinchilla lanigera]

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 ...
 779-888 4.37e-40

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: 143.61  E-value: 4.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917 779 LLFYAASRTQVDSICANNFVWTSHGTHENKYGKGNHFSKEAIYSHKNSLYDA---KNIVMFVARVLAGDFIEGNMMYVNP 855
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPkadGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 533184917 856 PPP--------YNSCVDTMLNPSVFVIFQKDQIYPAYLIEY 888
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 9.07e-34

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: 123.66  E-value: 9.07e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533184917    5 TVCCFITKILCAHGGRLSLDELLRKIELSEVQLLEVLKEAGPDRFLVLETGDRAGVTRSVVA 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 2.67e-15

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: 70.19  E-value: 2.67e-15
                          10        20
                  ....*....|....*....|....*...
gi 533184917  143 PFFMPEICKSYKGEGRKQICNQQPPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 592-673 1.67e-12

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 63.51  E-value: 1.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917   592 WIWYWNNESGKWIPYgegsnnqpgSDVDSSYLESFFQS--CPRGVVPFQagvQNYELSFQGMIQTNIVSKTQKiVVRRPT 669
Cdd:smart00678   1 YVWEYEGRNGKWWPY---------DPRVSEDIEEAYAAgkKLCELSICG---FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....
gi 533184917   670 FVSS 673
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 ...
 779-888 4.37e-40

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: 143.61  E-value: 4.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917 779 LLFYAASRTQVDSICANNFVWTSHGTHENKYGKGNHFSKEAIYSHKNSLYDA---KNIVMFVARVLAGDFIEGNMMYVNP 855
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPkadGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 533184917 856 PPP--------YNSCVDTMLNPSVFVIFQKDQIYPAYLIEY 888
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 9.07e-34

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: 123.66  E-value: 9.07e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533184917    5 TVCCFITKILCAHGGRLSLDELLRKIELSEVQLLEVLKEAGPDRFLVLETGDRAGVTRSVVA 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 2.67e-15

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: 70.19  E-value: 2.67e-15
                          10        20
                  ....*....|....*....|....*...
gi 533184917  143 PFFMPEICKSYKGEGRKQICNQQPPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 731-889 1.33e-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: 70.44  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917  731 SLEYASIRDYFKESM-----KNFKIEKIKKIHNPELLNCFERRRlmmTEKKERLLFYAASRTQVDSICANNFV--WTSHG 803
Cdd:pfam00644   1 SEEYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLRiaPPEAP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917  804 THENKYGKGNHF----SKEAIYSHKNSlyDAKNIVMFVARVLAGDFIE-GNMMYVNPPPPYNSCV--------------- 863
Cdd:pfam00644  78 VTGYMFGKGIYFaddaSKSANYCPPSE--AHGNGLMLLSEVALGDMNElKKADYAEKLPPGKHSVkglgktapesfvdld 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 533184917  864 -------------DTMLNPSVFVIFQKDQIYPAYLIEYS 889
Cdd:pfam00644 156 gvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVK 194
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 592-673 1.67e-12

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 63.51  E-value: 1.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917   592 WIWYWNNESGKWIPYgegsnnqpgSDVDSSYLESFFQS--CPRGVVPFQagvQNYELSFQGMIQTNIVSKTQKiVVRRPT 669
Cdd:smart00678   1 YVWEYEGRNGKWWPY---------DPRVSEDIEEAYAAgkKLCELSICG---FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....
gi 533184917   670 FVSS 673
Cdd:smart00678  68 YSPY 71
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 593-667 6.26e-11

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: 58.85  E-value: 6.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533184917  593 IWYWNNESGKWIPYGEGsnnqpgsdvDSSYLESFFQS-CPRGVVPFQAGVQNYELSFQGMIQTNIVSKTQkIVVRR 667
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTT-RPVRR 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 ...
 779-888 4.37e-40

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: 143.61  E-value: 4.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917 779 LLFYAASRTQVDSICANNFVWTSHGTHENKYGKGNHFSKEAIYSHKNSLYDA---KNIVMFVARVLAGDFIEGNMMYVNP 855
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPkadGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 533184917 856 PPP--------YNSCVDTMLNPSVFVIFQKDQIYPAYLIEY 888
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 9.07e-34

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: 123.66  E-value: 9.07e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533184917    5 TVCCFITKILCAHGGRLSLDELLRKIELSEVQLLEVLKEAGPDRFLVLETGDRAGVTRSVVA 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 2.67e-15

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: 70.19  E-value: 2.67e-15
                          10        20
                  ....*....|....*....|....*...
gi 533184917  143 PFFMPEICKSYKGEGRKQICNQQPPCER 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 731-889 1.33e-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: 70.44  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917  731 SLEYASIRDYFKESM-----KNFKIEKIKKIHNPELLNCFERRRlmmTEKKERLLFYAASRTQVDSICANNFV--WTSHG 803
Cdd:pfam00644   1 SEEYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLRiaPPEAP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917  804 THENKYGKGNHF----SKEAIYSHKNSlyDAKNIVMFVARVLAGDFIE-GNMMYVNPPPPYNSCV--------------- 863
Cdd:pfam00644  78 VTGYMFGKGIYFaddaSKSANYCPPSE--AHGNGLMLLSEVALGDMNElKKADYAEKLPPGKHSVkglgktapesfvdld 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 533184917  864 -------------DTMLNPSVFVIFQKDQIYPAYLIEYS 889
Cdd:pfam00644 156 gvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVK 194
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 592-673 1.67e-12

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 63.51  E-value: 1.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533184917   592 WIWYWNNESGKWIPYgegsnnqpgSDVDSSYLESFFQS--CPRGVVPFQagvQNYELSFQGMIQTNIVSKTQKiVVRRPT 669
Cdd:smart00678   1 YVWEYEGRNGKWWPY---------DPRVSEDIEEAYAAgkKLCELSICG---FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....
gi 533184917   670 FVSS 673
Cdd:smart00678  68 YSPY 71
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 593-667 6.26e-11

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: 58.85  E-value: 6.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533184917  593 IWYWNNESGKWIPYGEGsnnqpgsdvDSSYLESFFQS-CPRGVVPFQAGVQNYELSFQGMIQTNIVSKTQkIVVRR 667
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTT-RPVRR 66
 
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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