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Conserved domains on  [gi|1720416528|ref|XP_030110899|]
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protein mono-ADP-ribosyltransferase PARP11 isoform X6 [Mus musculus]

Protein Classification

WWE domain-containing protein( domain architecture ID 12218387)

WWE domain-containing protein similar to Rattus norvegicus zinc finger CCCH-type antiviral protein 1, an antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.76e-18

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.45  E-value: 1.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416528   27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 1720416528  105 SAF 107
Cdd:smart00678  71 YSK 73
PARP super family cl27334
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 140-181 8.40e-05

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.


The actual alignment was detected with superfamily member pfam00644:

Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 41.55  E-value: 8.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416528 140 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRVRVLG 181
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR 47
 
Name Accession Description Interval E-value
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.76e-18

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.45  E-value: 1.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416528   27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 1720416528  105 SAF 107
Cdd:smart00678  71 YSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 29-99 5.08e-18

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: 74.26  E-value: 5.08e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416528  29 WFYLAECGKWHMFQPDTniqcsvsSEDIEKSF-KTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKR 99
Cdd:pfam02825   2 WEWEDDNGGWHPYDPEV-------SSLIEEAYqKGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 140-181 8.40e-05

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: 41.55  E-value: 8.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416528 140 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRVRVLG 181
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR 47
 
Name Accession Description Interval E-value
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.76e-18

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.45  E-value: 1.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416528   27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 1720416528  105 SAF 107
Cdd:smart00678  71 YSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 29-99 5.08e-18

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: 74.26  E-value: 5.08e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416528  29 WFYLAECGKWHMFQPDTniqcsvsSEDIEKSF-KTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKR 99
Cdd:pfam02825   2 WEWEDDNGGWHPYDPEV-------SSLIEEAYqKGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 140-181 8.40e-05

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: 41.55  E-value: 8.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416528 140 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRVRVLG 181
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR 47
 
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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