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Conserved domains on  [gi|1034591215|ref|XP_016877878|]
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protein mono-ADP-ribosyltransferase PARP16 isoform X12 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 1.41e-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: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215  11 EAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKRAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 1034591215  90 L 90
Cdd:pfam18084  81 L 81
PARP super family cl27334
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 107-204 4.04e-22

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: 90.09  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215 107 LFGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------- 165
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdld 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034591215 166 -IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 204
Cdd:pfam00644 156 gVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
 
Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 1.41e-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: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215  11 EAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKRAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 1034591215  90 L 90
Cdd:pfam18084  81 L 81
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 107-204 4.04e-22

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: 90.09  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215 107 LFGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------- 165
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdld 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034591215 166 -IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 204
Cdd:pfam00644 156 gVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
 
Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 11-90 1.41e-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: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215  11 EAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELL-QSSGDNHKRAWDLVSWI 89
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIKEDEKDIDALREVVSDLPSLEELLlANLNDLDPDVIDLLHWV 80


                  .
gi 1034591215  90 L 90
Cdd:pfam18084  81 L 81
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 107-204 4.04e-22

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: 90.09  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591215 107 LFGEGTYLTSDLSLALIYSP----HGHGWqhsllgPILSCVAVCEV----------IDHPDVKCQTKKKDSKE------- 165
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCPpseaHGNGL------MLLSEVALGDMnelkkadyaeKLPPGKHSVKGLGKTAPesfvdld 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034591215 166 -IDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQ 204
Cdd:pfam00644 156 gVPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
 
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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