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Conserved domains on  [gi|1063705831|ref|NP_001323748|]
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uncharacterized protein AT2G35510 [Arabidopsis thaliana]

Protein Classification

PARP domain-containing protein( domain architecture ID 713042)

Poly(ADP-ribose) polymerase (PARP) domain-containing protein similar to Dictyostelium discoideum poly [ADP-ribose] polymerase DDB_G0278045

EC:  2.4.2.30
Gene Ontology:  GO:0003950|GO:0070403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PARP super family cl27334
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 316-400 1.10e-06

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: 48.87  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705831 316 KKHRGDANIRYAWVPAKKEVLSAVMMHGL-------GVGGAfikksMYGVGVHAANCPYFSARYC-DIDDNGVRHMVLCR 387
Cdd:pfam00644  41 QPKKKLRNRRLLWHGSRLTNFLGILSQGLriappeaPVTGY-----MFGKGIYFADDASKSANYCpPSEAHGNGLMLLSE 115

                          90
                  ....*....|...
gi 1063705831 388 VIMGNMEPLRGDN 400
Cdd:pfam00644 116 VALGDMNELKKAD 128
 
Name Accession Description Interval E-value
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 316-400 1.10e-06

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: 48.87  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705831 316 KKHRGDANIRYAWVPAKKEVLSAVMMHGL-------GVGGAfikksMYGVGVHAANCPYFSARYC-DIDDNGVRHMVLCR 387
Cdd:pfam00644  41 QPKKKLRNRRLLWHGSRLTNFLGILSQGLriappeaPVTGY-----MFGKGIYFADDASKSANYCpPSEAHGNGLMLLSE 115

                          90
                  ....*....|...
gi 1063705831 388 VIMGNMEPLRGDN 400
Cdd:pfam00644 116 VALGDMNELKKAD 128
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 355-442 3.19e-04

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: 40.38  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705831 355 MYGVGVHAANCPYFSARYCDIDDNGVRH--MVLCRVIMGnmeplrgdntqYFTGGEE----------------YDNGVDD 416
Cdd:cd01439    30 MYGKGSYFAKNASYSHQYSKKSPKADGLkeMFLARVLTG-----------DYTQGHPgyrrpplkpsgveldrYDSCVDN 98

                          90       100
                  ....*....|....*....|....*.
gi 1063705831 417 VESPKHYLIWNmnmNTHIYPEFVVSF 442
Cdd:cd01439    99 VSNPSIFVIFS---DVQAYPEYLITY 121
 
Name Accession Description Interval E-value
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 316-400 1.10e-06

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: 48.87  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705831 316 KKHRGDANIRYAWVPAKKEVLSAVMMHGL-------GVGGAfikksMYGVGVHAANCPYFSARYC-DIDDNGVRHMVLCR 387
Cdd:pfam00644  41 QPKKKLRNRRLLWHGSRLTNFLGILSQGLriappeaPVTGY-----MFGKGIYFADDASKSANYCpPSEAHGNGLMLLSE 115

                          90
                  ....*....|...
gi 1063705831 388 VIMGNMEPLRGDN 400
Cdd:pfam00644 116 VALGDMNELKKAD 128
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 355-442 3.19e-04

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: 40.38  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705831 355 MYGVGVHAANCPYFSARYCDIDDNGVRH--MVLCRVIMGnmeplrgdntqYFTGGEE----------------YDNGVDD 416
Cdd:cd01439    30 MYGKGSYFAKNASYSHQYSKKSPKADGLkeMFLARVLTG-----------DYTQGHPgyrrpplkpsgveldrYDSCVDN 98

                          90       100
                  ....*....|....*....|....*.
gi 1063705831 417 VESPKHYLIWNmnmNTHIYPEFVVSF 442
Cdd:cd01439    99 VSNPSIFVIFS---DVQAYPEYLITY 121
 
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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