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poly [ADP-ribose] polymerase 3 isoform X2 [Oryza sativa Japonica Group]
PLN03122 family protein( domain architecture ID 11477447)
PLN03122 family protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||||||||
PLN03122 | PLN03122 | Poly [ADP-ribose] polymerase; Provisional |
27-862 | 0e+00 | ||||||||||||
Poly [ADP-ribose] polymerase; Provisional : Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 1442.29 E-value: 0e+00
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Name | Accession | Description | Interval | E-value | ||||||||||||
PLN03122 | PLN03122 | Poly [ADP-ribose] polymerase; Provisional |
27-862 | 0e+00 | ||||||||||||
Poly [ADP-ribose] polymerase; Provisional Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 1442.29 E-value: 0e+00
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parp_like | cd01437 | Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
492-850 | 1.12e-94 | ||||||||||||
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: 301.11 E-value: 1.12e-94
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PARP | pfam00644 | Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
645-851 | 2.80e-52 | ||||||||||||
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: 180.99 E-value: 2.80e-52
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WGR | smart00773 | Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
370-451 | 4.34e-21 | ||||||||||||
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain. Pssm-ID: 214814 Cd Length: 84 Bit Score: 88.11 E-value: 4.34e-21
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Name | Accession | Description | Interval | E-value | ||||||||||||
PLN03122 | PLN03122 | Poly [ADP-ribose] polymerase; Provisional |
27-862 | 0e+00 | ||||||||||||
Poly [ADP-ribose] polymerase; Provisional Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 1442.29 E-value: 0e+00
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PLN03123 | PLN03123 | poly [ADP-ribose] polymerase; Provisional |
22-851 | 1.43e-138 | ||||||||||||
poly [ADP-ribose] polymerase; Provisional Pssm-ID: 215590 [Multi-domain] Cd Length: 981 Bit Score: 436.53 E-value: 1.43e-138
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parp_like | cd01437 | Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
492-850 | 1.12e-94 | ||||||||||||
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: 301.11 E-value: 1.12e-94
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PARP | pfam00644 | Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
645-851 | 2.80e-52 | ||||||||||||
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: 180.99 E-value: 2.80e-52
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PLN03124 | PLN03124 | poly [ADP-ribose] polymerase; Provisional |
494-851 | 4.93e-40 | ||||||||||||
poly [ADP-ribose] polymerase; Provisional Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 157.69 E-value: 4.93e-40
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PARP_reg | pfam02877 | Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ... |
493-631 | 1.27e-29 | ||||||||||||
Poly(ADP-ribose) polymerase, regulatory 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: 460732 [Multi-domain] Cd Length: 135 Bit Score: 114.16 E-value: 1.27e-29
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WGR_PARP1_like | cd08001 | WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ... |
365-472 | 5.85e-22 | ||||||||||||
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging. Pssm-ID: 153428 [Multi-domain] Cd Length: 104 Bit Score: 91.50 E-value: 5.85e-22
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BRCT_PARP1 | cd17747 | BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
229-304 | 9.57e-22 | ||||||||||||
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 89.51 E-value: 9.57e-22
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WGR | smart00773 | Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
370-451 | 4.34e-21 | ||||||||||||
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain. Pssm-ID: 214814 Cd Length: 84 Bit Score: 88.11 E-value: 4.34e-21
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PADR1 | pfam08063 | PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of ... |
140-191 | 3.74e-17 | ||||||||||||
PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of this domain is unknown. Pssm-ID: 462349 [Multi-domain] Cd Length: 53 Bit Score: 75.69 E-value: 3.74e-17
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BRCT_Rev1 | cd17719 | BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
228-314 | 1.45e-08 | ||||||||||||
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light. Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 52.57 E-value: 1.45e-08
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BRCT_2 | pfam16589 | BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
227-314 | 3.39e-08 | ||||||||||||
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown. Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 51.60 E-value: 3.39e-08
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BRCT | smart00292 | breast cancer carboxy-terminal domain; |
226-303 | 6.16e-08 | ||||||||||||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 50.45 E-value: 6.16e-08
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BRCT | pfam00533 | BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
226-303 | 9.18e-08 | ||||||||||||
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants. Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 49.98 E-value: 9.18e-08
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WGR | pfam05406 | WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
375-455 | 6.77e-06 | ||||||||||||
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain. Pssm-ID: 398851 Cd Length: 79 Bit Score: 44.92 E-value: 6.77e-06
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BRCT | cd00027 | C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
234-302 | 2.25e-05 | ||||||||||||
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage. Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 43.12 E-value: 2.25e-05
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BRCT_p53bp1_rpt1 | cd17745 | first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ... |
228-307 | 4.92e-04 | ||||||||||||
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain. Pssm-ID: 349376 [Multi-domain] Cd Length: 99 Bit Score: 39.99 E-value: 4.92e-04
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BRCT_TopBP1_rpt2_like | cd17731 | second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
227-306 | 1.72e-03 | ||||||||||||
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain. Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 37.90 E-value: 1.72e-03
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Blast search parameters | ||||
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