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Conserved domains on  [gi|1886450762|gb|KAF6276348|]
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zinc finger CCCH-type containing, antiviral 1 [Rhinolophus ferrumequinum]

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 ...
 902-1011 4.39e-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: 144.00  E-value: 4.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  902 RLFCAVGRANVEYICANNFEWTLHGTSETKYGKGNYFTKDAICAHSNCQCDLKS---IVMFVARVLVGESIEGHKSYTSP 978
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1886450762  979 PAP--------YDSCVDTRLNPSVFVIFQKDQIYPEYVIEY 1011
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 1.05e-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: 126.36  E-value: 1.05e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886450762    5 EVCCFITKILCAHGGRMALDALLDEIVLSEAQLCEVLEAAGPNRFVILETGGGAGVTRSVVA 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 4.56e-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: 69.42  E-value: 4.56e-15
                           10        20
                   ....*....|....*....|....*...
gi 1886450762  143 PFFMPEICKSYKGEGRRQICSQQPPCER 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 ...
 725-799 3.85e-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: 62.31  E-value: 3.85e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886450762  725 IWYWKNEFDEWVEYGKKkgnqqistvDSSYLESFFLL-YPRGIVTFQVGSQNYELSFQGMIQTNVESKTQRGvVRR 799
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-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 ...
 902-1011 4.39e-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: 144.00  E-value: 4.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  902 RLFCAVGRANVEYICANNFEWTLHGTSETKYGKGNYFTKDAICAHSNCQCDLKS---IVMFVARVLVGESIEGHKSYTSP 978
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1886450762  979 PAP--------YDSCVDTRLNPSVFVIFQKDQIYPEYVIEY 1011
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 1.05e-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: 126.36  E-value: 1.05e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886450762    5 EVCCFITKILCAHGGRMALDALLDEIVLSEAQLCEVLEAAGPNRFVILETGGGAGVTRSVVA 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 4.56e-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: 69.42  E-value: 4.56e-15
                           10        20
                   ....*....|....*....|....*...
gi 1886450762  143 PFFMPEICKSYKGEGRRQICSQQPPCER 170
Cdd:pfam18633    1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 856-1011 4.28e-14

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: 71.98  E-value: 4.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  856 EYANISEHFKATM-----KNASIAKIKKIKNVELLNAFERKKmkmKNRNEKRLFCAVGRANVEYICANNFE--WTLHGTS 928
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLRiaPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  929 ETKYGKGNYFTKDAICAHSNC--QCDLKSIVMFVARVLVGESIEGHKS--YTSPPAPYDSCV------------------ 986
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCppSEAHGNGLMLLSEVALGDMNELKKAdyAEKLPPGKHSVKglgktapesfvdldgvpl 159

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1886450762  987 ---------DTRLNPSVFVIFQKDQIYPEYVIEY 1011
Cdd:pfam00644  160 gklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 725-799 3.85e-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: 62.31  E-value: 3.85e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886450762  725 IWYWKNEFDEWVEYGKKkgnqqistvDSSYLESFFLL-YPRGIVTFQVGSQNYELSFQGMIQTNVESKTQRGvVRR 799
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 724-804 6.99e-08

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 50.42  E-value: 6.99e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762   724 WIWYWKNEFDEWVEYgkkkgnqqiSTVDSSYLESFFLLYPR--GIVTFqvgSQNYELSFQGMIQTNVESKTQRgVVRRPV 801
Cdd:smart00678    1 YVWEYEGRNGKWWPY---------DPRVSEDIEEAYAAGKKlcELSIC---GFPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                    ...
gi 1886450762   802 FVS 804
Cdd:smart00678   68 YSP 70
 
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 ...
 902-1011 4.39e-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: 144.00  E-value: 4.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  902 RLFCAVGRANVEYICANNFEWTLHGTSETKYGKGNYFTKDAICAHSNCQCDLKS---IVMFVARVLVGESIEGHKSYTSP 978
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1886450762  979 PAP--------YDSCVDTRLNPSVFVIFQKDQIYPEYVIEY 1011
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 1.05e-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: 126.36  E-value: 1.05e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886450762    5 EVCCFITKILCAHGGRMALDALLDEIVLSEAQLCEVLEAAGPNRFVILETGGGAGVTRSVVA 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 4.56e-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: 69.42  E-value: 4.56e-15
                           10        20
                   ....*....|....*....|....*...
gi 1886450762  143 PFFMPEICKSYKGEGRRQICSQQPPCER 170
Cdd:pfam18633    1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 856-1011 4.28e-14

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: 71.98  E-value: 4.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  856 EYANISEHFKATM-----KNASIAKIKKIKNVELLNAFERKKmkmKNRNEKRLFCAVGRANVEYICANNFE--WTLHGTS 928
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLRiaPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762  929 ETKYGKGNYFTKDAICAHSNC--QCDLKSIVMFVARVLVGESIEGHKS--YTSPPAPYDSCV------------------ 986
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCppSEAHGNGLMLLSEVALGDMNELKKAdyAEKLPPGKHSVKglgktapesfvdldgvpl 159

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1886450762  987 ---------DTRLNPSVFVIFQKDQIYPEYVIEY 1011
Cdd:pfam00644  160 gklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 725-799 3.85e-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: 62.31  E-value: 3.85e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886450762  725 IWYWKNEFDEWVEYGKKkgnqqistvDSSYLESFFLL-YPRGIVTFQVGSQNYELSFQGMIQTNVESKTQRGvVRR 799
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 724-804 6.99e-08

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 50.42  E-value: 6.99e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886450762   724 WIWYWKNEFDEWVEYgkkkgnqqiSTVDSSYLESFFLLYPR--GIVTFqvgSQNYELSFQGMIQTNVESKTQRgVVRRPV 801
Cdd:smart00678    1 YVWEYEGRNGKWWPY---------DPRVSEDIEEAYAAGKKlcELSIC---GFPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                    ...
gi 1886450762   802 FVS 804
Cdd:smart00678   68 YSP 70
 
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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