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Conserved domains on  [gi|125630384|ref|NP_766633|]
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zinc finger CCCH-type antiviral protein 1 isoform 2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 2.74e-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: 2.74e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125630384    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 4.61e-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: 63.64  E-value: 4.61e-13
                          10        20
                  ....*....|....*....|....*...
gi 125630384  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 3.53e-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: 61.93  E-value: 3.53e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125630384  685 IWYWKNEFNEYIQYGNEspghTSSDINSAYLesffQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHvVRR 759
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE----VSSLIEEAYQ----KGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
 
Name Accession Description Interval E-value
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 2.74e-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: 2.74e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125630384    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 4.61e-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: 63.64  E-value: 4.61e-13
                          10        20
                  ....*....|....*....|....*...
gi 125630384  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 3.53e-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: 61.93  E-value: 3.53e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125630384  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 5.09e-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: 53.50  E-value: 5.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630384   684 WIWYWKNEFNEYIQYgneSPgHTSSDINSAYL--ESFFQSCPRGvlpfqagsQKYELSFQGMIQTNIASKTQRHvVRRPV 761
Cdd:smart00678   1 YVWEYEGRNGKWWPY---DP-RVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTRK-VRRVT 67


                   ....
gi 125630384   762 FVSS 765
Cdd:smart00678  68 YSPY 71
 
Name Accession Description Interval E-value
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 2.74e-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: 2.74e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125630384    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 4.61e-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: 63.64  E-value: 4.61e-13
                          10        20
                  ....*....|....*....|....*...
gi 125630384  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 3.53e-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: 61.93  E-value: 3.53e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125630384  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 5.09e-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: 53.50  E-value: 5.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630384   684 WIWYWKNEFNEYIQYgneSPgHTSSDINSAYL--ESFFQSCPRGvlpfqagsQKYELSFQGMIQTNIASKTQRHvVRRPV 761
Cdd:smart00678   1 YVWEYEGRNGKWWPY---DP-RVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTRK-VRRVT 67


                   ....
gi 125630384   762 FVSS 765
Cdd:smart00678  68 YSPY 71
 
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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