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Conserved domains on  [gi|922581987|ref|NP_001300471|]
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Poly [ADP-ribose] polymerase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADP_ribosyl super family cl00283
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 11-81 3.56e-24

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.


The actual alignment was detected with superfamily member cd01437:

Pssm-ID: 444809 [Multi-domain]  Cd Length: 347  Bit Score: 92.72  E-value: 3.56e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581987  11 LPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLGLTYMQlqgKQDVDYHLLYNEFIVYDVDQIQLKYLVRVK 81
Cdd:cd01437  280 LPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPS---GHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 11-81 3.56e-24

Poly(ADP-ribose) polymerase (parp) catalytic domain 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. Poly(ADP-ribose)-like 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 through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 92.72  E-value: 3.56e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581987  11 LPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLGLTYMQlqgKQDVDYHLLYNEFIVYDVDQIQLKYLVRVK 81
Cdd:cd01437  280 LPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPS---GHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 11-86 2.07e-12

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 60.62  E-value: 2.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581987  11 LPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLG--LTYMQLQGKqdvdyhLLYNEFIVYDVDQIQLKYLVRVKMHHAR 86
Cdd:PLN03124 571 LPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGkpVESPYSKGS------LEYNEYIVYNVDQIRMRYVLQVKFNYKR 642
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 11-82 9.48e-10

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: 52.34  E-value: 9.48e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581987   11 LPAGFQSVQGLGRQCPReigSYNHPDGytIPLGltymQLQGKQDVDYHLLYNEFIVYDVDQIQLKYLVRVKM 82
Cdd:pfam00644 133 LPPGKHSVKGLGKTAPE---SFVDLDG--VPLG----KLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 11-81 3.56e-24

Poly(ADP-ribose) polymerase (parp) catalytic domain 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. Poly(ADP-ribose)-like 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 through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 92.72  E-value: 3.56e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581987  11 LPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLGLTYMQlqgKQDVDYHLLYNEFIVYDVDQIQLKYLVRVK 81
Cdd:cd01437  280 LPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPS---GHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 11-86 2.07e-12

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 60.62  E-value: 2.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581987  11 LPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLG--LTYMQLQGKqdvdyhLLYNEFIVYDVDQIQLKYLVRVKMHHAR 86
Cdd:PLN03124 571 LPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGkpVESPYSKGS------LEYNEYIVYNVDQIRMRYVLQVKFNYKR 642
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 12-86 1.55e-11

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 58.26  E-value: 1.55e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581987  12 PAGFQSVQGLGRQCPREIGSYNHPDGYTIPLGltymQLQGKQDVDYHLLYNEFIVYDVDQIQLKYLVRVKMHHAR 86
Cdd:PLN03123 911 PRGKHSTKGLGKTVPQESEFVKWRDDVVVPCG----KPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVRFKHKR 981
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 11-82 9.48e-10

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: 52.34  E-value: 9.48e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581987   11 LPAGFQSVQGLGRQCPReigSYNHPDGytIPLGltymQLQGKQDVDYHLLYNEFIVYDVDQIQLKYLVRVKM 82
Cdd:pfam00644 133 LPPGKHSVKGLGKTAPE---SFVDLDG--VPLG----KLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 18-81 8.23e-08

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 47.87  E-value: 8.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581987  18 VQGLGRQCPREIGSYNHPDGYTIPLGltymQLQGKQDVDYHLLYNEFIVYDVDQIQLKYLVRVK 81
Cdd:PLN03122 744 VKGLGRKKTDESEHFKWRDDITVPCG----RLIPSEHKDSPLEYNEYAVYDPKQVSIRFLVGVK 803
 
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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