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Conserved domains on  [gi|109081532|ref|XP_001109120|]
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protein mono-ADP-ribosyltransferase PARP16 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 102-273 2.75e-48

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: 160.19  E-value: 2.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  102 KAEFEKIQKLTGAPHTPVPA-PDFLFEIEYFDPAN--AKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSL-- 176
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHGyPLFILEIFRVQRDGewERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVtg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  177 --FGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------ 234
Cdd:pfam00644  81 ymFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdl 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 109081532  235 --IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 273
Cdd:pfam00644 155 dgVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 7.34e-31

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


:

Pssm-ID: 465641  Cd Length: 81  Bit Score: 111.51  E-value: 7.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532   11 EAAGRDLLAADLRCSLFASALKSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKWAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 109081532   90 L 90
Cdd:pfam18084  81 L 81
 
Name Accession Description Interval E-value
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 102-273 2.75e-48

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: 160.19  E-value: 2.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  102 KAEFEKIQKLTGAPHTPVPA-PDFLFEIEYFDPAN--AKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSL-- 176
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHGyPLFILEIFRVQRDGewERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVtg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  177 --FGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------ 234
Cdd:pfam00644  81 ymFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdl 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 109081532  235 --IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 273
Cdd:pfam00644 155 dgVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 7.34e-31

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


Pssm-ID: 465641  Cd Length: 81  Bit Score: 111.51  E-value: 7.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532   11 EAAGRDLLAADLRCSLFASALKSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKWAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 109081532   90 L 90
Cdd:pfam18084  81 L 81
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 150-259 2.06e-03

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses 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: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 37.92  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532 150 AFHGSRLENFHSIIHNGLH-----CHLNKTSlFGEGTYLTSDLSLALIYSpHGHGWQHSLlgpILSCVAVCEvIDHPDVK 224
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRpasygVLLNGGM-FGKGIYSAPNISKSNGYS-VGCDGQHVF---QNGKPKVCG-RELCVFG 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 109081532 225 CQTKKKDSKEiDRRRARIKHSEGGDIPPKYFVVTN 259
Cdd:cd01341   76 FLTLGVMSGA-TEESSRVLFPRNFRGATGAEVVDL 109
 
Name Accession Description Interval E-value
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 102-273 2.75e-48

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: 160.19  E-value: 2.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  102 KAEFEKIQKLTGAPHTPVPA-PDFLFEIEYFDPAN--AKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSL-- 176
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHGyPLFILEIFRVQRDGewERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVtg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532  177 --FGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------ 234
Cdd:pfam00644  81 ymFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdl 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 109081532  235 --IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 273
Cdd:pfam00644 155 dgVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 7.34e-31

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


Pssm-ID: 465641  Cd Length: 81  Bit Score: 111.51  E-value: 7.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532   11 EAAGRDLLAADLRCSLFASALKSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKWAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 109081532   90 L 90
Cdd:pfam18084  81 L 81
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 150-259 2.06e-03

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses 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: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 37.92  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109081532 150 AFHGSRLENFHSIIHNGLH-----CHLNKTSlFGEGTYLTSDLSLALIYSpHGHGWQHSLlgpILSCVAVCEvIDHPDVK 224
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRpasygVLLNGGM-FGKGIYSAPNISKSNGYS-VGCDGQHVF---QNGKPKVCG-RELCVFG 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 109081532 225 CQTKKKDSKEiDRRRARIKHSEGGDIPPKYFVVTN 259
Cdd:cd01341   76 FLTLGVMSGA-TEESSRVLFPRNFRGATGAEVVDL 109
 
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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