Protein : Qrob_P0747200.2 Q. robur

Protein Identifier  ? Qrob_P0747200.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=2) PTHR15447//PTHR15447:SF12 - POLY [ADP-RIBOSE] POLYMERASE // SUBFAMILY NOT NAMED Code Enzyme  EC:2.4.2.30
Gene Prediction Quality  validated Protein length 

Sequence

Length: 521  
Kegg Orthology  K10798

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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0005634 nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
GO:0003950 NAD+ ADP-ribosyltransferase activity Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
GO:0006471 protein ADP-ribosylation The transfer, from NAD, of ADP-ribose to protein amino acids.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|gmx:548024 9 513 + 505 Gaps:35 66.26 815 72.04 0.0 PARP3 ADPRT-3 PARP-3 PM38 seed maturation protein PM38 (EC:2.4.2.30)
blastp_kegg lcl|gmx:100788978 9 513 + 505 Gaps:35 66.50 812 70.93 0.0 poly [ADP-ribose] polymerase 3-like
blastp_kegg lcl|pmum:103328815 10 513 + 504 Gaps:35 66.46 811 69.76 0.0 poly [ADP-ribose] polymerase 3
blastp_kegg lcl|cam:101514608 12 513 + 502 Gaps:37 66.21 811 72.44 0.0 putative poly [ADP-ribose] polymerase 3-like
blastp_kegg lcl|mtr:MTR_4g053530 8 513 + 506 Gaps:16 63.88 814 72.31 0.0 Poly
blastp_kegg lcl|pper:PRUPE_ppa001509mg 10 513 + 504 Gaps:35 66.46 811 69.39 0.0 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10027891mg 9 513 + 505 Gaps:38 73.98 734 68.69 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_041443 9 513 + 505 Gaps:40 66.54 813 68.58 0.0 Poly [ADP-ribose] polymerase 3 putative
blastp_kegg lcl|cit:102620309 1 513 + 513 Gaps:39 67.07 823 67.39 0.0 poly [ADP-ribose] polymerase 3-like
blastp_kegg lcl|mdm:103441354 9 513 + 505 Gaps:33 66.17 813 67.29 0.0 poly [ADP-ribose] polymerase 3
blastp_pdb 2cr9_A 289 413 + 125 Gaps:7 86.33 139 34.17 7e-11 mol:protein length:139 Poly [ADP-ribose] polymerase-1
blastp_pdb 2riq_A 55 135 + 81 none 50.62 160 30.86 2e-08 mol:protein length:160 Poly [ADP-ribose] polymerase 1
blastp_pdb 2jvn_A 55 135 + 81 none 64.29 126 30.86 3e-08 mol:protein length:126 Poly [ADP-ribose] polymerase 1
blastp_uniprot_sprot sp|Q9SWB4|PARP3_SOYBN 9 513 + 505 Gaps:35 66.26 815 72.04 0.0 Poly [ADP-ribose] polymerase 3 OS Glycine max GN PARP3 PE 2 SV 1
blastp_uniprot_sprot sp|Q1SGF1|PARP3_MEDTR 8 513 + 506 Gaps:31 63.20 799 71.68 0.0 Putative poly [ADP-ribose] polymerase 3 OS Medicago truncatula GN PARP3 PE 3 SV 1
blastp_uniprot_sprot sp|Q9FK91|PARP3_ARATH 9 510 + 502 Gaps:39 65.97 814 64.25 0.0 Poly [ADP-ribose] polymerase 3 OS Arabidopsis thaliana GN PARP3 PE 2 SV 2
blastp_uniprot_sprot sp|Q0E0Q3|PARP3_ORYSJ 12 514 + 503 Gaps:20 62.21 831 53.58 0.0 Poly [ADP-ribose] polymerase 3 OS Oryza sativa subsp. japonica GN PARP3 PE 2 SV 1
blastp_uniprot_sprot sp|Q7EYV7|PARP1_ORYSJ 55 513 + 459 Gaps:56 47.80 977 29.55 5e-54 Poly [ADP-ribose] polymerase 1 OS Oryza sativa subsp. japonica GN PARP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9ZSV1|PARP1_MAIZE 54 513 + 460 Gaps:70 47.76 980 27.35 2e-48 Poly [ADP-ribose] polymerase 1 OS Zea mays GN PARP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9ZP54|PARP1_ARATH 55 513 + 459 Gaps:68 47.10 983 29.81 5e-48 Poly [ADP-ribose] polymerase 1 OS Arabidopsis thaliana GN PARP1 PE 1 SV 2
blastp_uniprot_sprot sp|P09874|PARP1_HUMAN 55 504 + 450 Gaps:63 48.22 1014 26.79 2e-31 Poly [ADP-ribose] polymerase 1 OS Homo sapiens GN PARP1 PE 1 SV 4
blastp_uniprot_sprot sp|Q9R152|PARP1_CRIGR 55 504 + 450 Gaps:60 48.17 1013 25.82 2e-31 Poly [ADP-ribose] polymerase 1 OS Cricetulus griseus GN PARP1 PE 2 SV 3
blastp_uniprot_sprot sp|P18493|PARP1_BOVIN 55 504 + 450 Gaps:62 48.03 1016 26.84 8e-30 Poly [ADP-ribose] polymerase 1 OS Bos taurus GN PARP1 PE 2 SV 2
rpsblast_cdd gnl|CDD|178669 10 514 + 505 Gaps:39 66.75 815 68.38 0.0 PLN03122 PLN03122 Poly [ADP-ribose] polymerase Provisional.
rpsblast_cdd gnl|CDD|178670 19 513 + 495 Gaps:81 52.19 981 28.12 2e-59 PLN03123 PLN03123 poly [ADP-ribose] polymerase Provisional.
rpsblast_cdd gnl|CDD|153428 311 415 + 105 Gaps:5 98.08 104 37.25 6e-29 cd08001 WGR_PARP1_like 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.
rpsblast_cdd gnl|CDD|197868 314 402 + 89 Gaps:5 100.00 84 30.95 3e-18 smart00773 WGR 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.
rpsblast_cdd gnl|CDD|191934 82 135 + 54 Gaps:1 100.00 55 41.82 2e-16 pfam08063 PADR1 PADR1 (NUC008) domain. This domain is found in poly(ADP-ribose)-synthetases. The function of this domain is unknown.
rpsblast_cdd gnl|CDD|203245 315 402 + 88 Gaps:5 100.00 83 32.53 1e-12 pfam05406 WGR WGR domain. This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator 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 Rhizobium radiobacter ych and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.
rpsblast_cdd gnl|CDD|153426 310 414 + 105 Gaps:6 99.02 102 27.72 4e-10 cd07997 WGR_PARP WGR domain of poly(ADP-ribose) polymerases. 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 and histones. Higher eukaryotes contain several PARPs 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. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However it is now known that it plays important roles in many cellular processes including maintenance of genomic stability transcriptional regulation energy metabolism cell death and survival among others.

13 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 169 259 91 G3DSA:3.40.50.10190 none none IPR001357
Pfam 83 135 53 PF08063 none PADR1 (NUC008) domain IPR012982
PANTHER 8 515 508 PTHR15447 none none none
SUPERFAMILY 284 413 130 SSF142921 none none IPR008893
ProSiteProfiles 168 260 93 PS50172 none BRCT domain profile. IPR001357
Pfam 170 247 78 PF00533 none BRCA1 C Terminus (BRCT) domain IPR001357
SUPERFAMILY 435 514 80 SSF47587 none none IPR004102
SMART 170 250 81 SM00292 none breast cancer carboxy-terminal domain IPR001357
Pfam 317 397 81 PF05406 none WGR domain IPR008893
Coils 465 486 22 Coil none none none
PANTHER 8 515 508 PTHR15447:SF12 none none none
SUPERFAMILY 153 271 119 SSF52113 none none IPR001357
SMART 319 402 84 SM00773 none Proposed nucleic acid binding domain IPR008893

0 Localization

0 Qtllist

0 Targeting