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CAZyme Information: P170DRAFT_456659-t37_1-p1
You are here: Home > Sequence: P170DRAFT_456659-t37_1-p1
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Aspergillus steynii | |||||||||||
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| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii | |||||||||||
| CAZyme ID | P170DRAFT_456659-t37_1-p1 | |||||||||||
| CAZy Family | GH71 | |||||||||||
| CAZyme Description | phospholipase D/nuclease | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT59 | 35 | 535 | 1.3e-138 | 0.995049504950495 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 399229 | Tyr-DNA_phospho | 0.0 | 669 | 1124 | 1 | 433 | Tyrosyl-DNA phosphodiesterase. Covalent intermediates between topoisomerase I and DNA can become dead-end complexes that lead to cell death. Tyrosyl-DNA phosphodiesterase can hydrolyze the bond between topoisomerase I and DNA. |
| 398537 | DIE2_ALG10 | 1.42e-139 | 36 | 535 | 1 | 383 | DIE2/ALG10 family. The ALG10 protein from Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum. This protein has been characterized in rat as potassium channel regulator 1. |
| 197290 | PLDc_yTdp1_1 | 1.66e-71 | 668 | 844 | 1 | 166 | Catalytic domain, repeat 1, of yeast tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 1, of yeast tyrosyl-DNA phosphodiesterase (yTdp1, EC 3.1.4.-). yTdp1 is involved in the repair of topoisomerase I DNA lesions by hydrolyzing the topoisomerase from the 3'-end of the DNA during double-strand break repair. Unlike human Tdp1 whose substrate-binding pocket can accommodate a fairly large topoisomerase I peptide fragment, yTdp1 has a preference for substrates containing one to four amino acid residues. The monomeric yTdp1 contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, yTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. |
| 197222 | PLDc_Tdp1_2 | 7.62e-48 | 892 | 1077 | 1 | 182 | Catalytic domain, repeat 2, of tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 2, of Tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-), which exists in eukaryotes but not in prokaryotes. Tdp1 acts as an important DNA repair enzyme that removes stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is a monomeric protein that contains two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Thus, this family represents a distinct class within the PLD superfamily. Like other PLD enzymes, Tdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. |
| 197291 | PLDc_mTdp1_2 | 1.10e-39 | 869 | 1078 | 3 | 191 | Catalytic domain, repeat 2, of metazoan tyrosyl-DNA phosphodiesterase. Catalytic domain, repeat 2, of metazoan tyrosyl-DNA phosphodiesterase (Tdp1, EC 3.1.4.-). Human Tdp1 (hTdp1) acts as an important DNA repair enzyme with a preference for single-stranded or blunt-ended duplex oligonucleotides. It can remove stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is therefore a potential molecular target for new anti-cancer drugs. hTdp1 has been shown to associate with additional proteins, such as XRCC1, to form a multi-enzyme complex. These additional proteins may be involved in recognizing 3'-phoshotyrosyl DNA in vivo. hTdp1 is a monomeric protein containing two copies of a variant HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which consists of the highly conserved histidine and lysine residues, but lacks the aspartate residue that is well conserved in other phospholipase D (PLD, EC 3.1.4.4) enzymes. Like other PLD enzymes, hTdp1 may utilize a common two-step general acid/base catalytic mechanism, involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 3.40e-295 | 1 | 605 | 1 | 608 | |
| 1.94e-294 | 1 | 605 | 1 | 608 | |
| 2.21e-293 | 1 | 605 | 1 | 608 | |
| 4.31e-290 | 1 | 605 | 1 | 625 | |
| 6.10e-290 | 1 | 605 | 1 | 625 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 8.36e-66 | 668 | 1150 | 14 | 458 | Crystal structure of Tdp1 catalytic domain in complex with compound XZ519 [Homo sapiens],6MJ5_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ519 [Homo sapiens] |
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| 8.58e-66 | 668 | 1150 | 15 | 459 | Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT0911 from cocktail soak [Homo sapiens],6DHU_B Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT0911 from cocktail soak [Homo sapiens],6DIE_A Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment benzene-1,2,4-tricarboxylic acid from single soak [Homo sapiens],6DIE_B Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment benzene-1,2,4-tricarboxylic acid from single soak [Homo sapiens],6DIH_A Crystal structure of Tdp1 catalytic domain in complex with Sigma Aldrich compound PH004941 [Homo sapiens],6DIH_B Crystal structure of Tdp1 catalytic domain in complex with Sigma Aldrich compound PH004941 [Homo sapiens],6DIM_A Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT1982 from cocktail soak [Homo sapiens],6DIM_B Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT1982 from cocktail soak [Homo sapiens],6DJD_A Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT1982 (single soak) [Homo sapiens],6DJD_B Crystal structure of Tdp1 catalytic domain in complex with Zenobia fragment ZT1982 (single soak) [Homo sapiens],6DJE_A Crystal structure of Tdp1 catalytic domain in complex with Sigma Aldrich compound CDS010292 [Homo sapiens],6DJE_B Crystal structure of Tdp1 catalytic domain in complex with Sigma Aldrich compound CDS010292 [Homo sapiens],6DJF_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ502 [Homo sapiens],6DJF_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ502 [Homo sapiens],6DJG_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ503 [Homo sapiens],6DJG_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ503 [Homo sapiens],6DJH_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ515 [Homo sapiens],6DJH_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ515 [Homo sapiens],6DJI_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ522 [Homo sapiens],6DJI_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ522 [Homo sapiens],6DJJ_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ532 [Homo sapiens],6DJJ_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ532 [Homo sapiens],6MYZ_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ520 [Homo sapiens],6MYZ_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ520 [Homo sapiens],6MZ0_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ530 [Homo sapiens],6MZ0_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ530 [Homo sapiens],6N0D_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ575 [Homo sapiens],6N0D_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ575 [Homo sapiens],6N0N_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ574 [Homo sapiens],6N0N_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ574 [Homo sapiens],6N0O_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ523 [Homo sapiens],6N0O_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ523 [Homo sapiens],6N0R_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ572 [Homo sapiens],6N0R_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ572 [Homo sapiens],6N17_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ577 [Homo sapiens],6N17_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ577 [Homo sapiens],6N19_A Crystal structure of Tdp1 catalytic domain in complex with compound XZ578 [Homo sapiens],6N19_B Crystal structure of Tdp1 catalytic domain in complex with compound XZ578 [Homo sapiens],6W4R_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W4R_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7J_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7J_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7K_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7K_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7L_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],6W7L_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens] |
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| 1.49e-65 | 668 | 1150 | 37 | 481 | human Tyrosyl DNA phosphodiesterase [Homo sapiens],1QZQ_B human Tyrosyl DNA phosphodiesterase [Homo sapiens] |
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| 2.55e-64 | 668 | 1150 | 39 | 483 | Chain A, Tyrosyl-DNA Phosphodiesterase [Homo sapiens],1MU7_B Chain B, Tyrosyl-DNA Phosphodiesterase [Homo sapiens],1MU9_A Chain A, Tyrosyl-DNA Phosphodiesterase [Homo sapiens],1MU9_B Chain B, Tyrosyl-DNA Phosphodiesterase [Homo sapiens],1NOP_A Chain A, tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1NOP_B Chain B, tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RFF_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RFF_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RFI_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RFI_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RG1_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RG1_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RG2_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RG2_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RGT_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RGT_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RGU_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RGU_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RH0_A Chain A, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],1RH0_B Chain B, Tyrosyl-DNA phosphodiesterase 1 [Homo sapiens],5NW9_A Crystal structure of the complex of Tdp1 with duplex DNA [Homo sapiens],5NW9_B Crystal structure of the complex of Tdp1 with duplex DNA [Homo sapiens],5NWA_A Crystal structure of the complex of Tdp1 with duplex DNA [Homo sapiens],5NWA_B Crystal structure of the complex of Tdp1 with duplex DNA [Homo sapiens] |
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| 2.90e-62 | 668 | 1150 | 18 | 462 | Chain A, TYROSYL-DNA PHOSPHODIESTERASE [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.07e-279 | 1 | 605 | 1 | 614 | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=alg10 PE=3 SV=1 |
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| 7.67e-259 | 1 | 605 | 1 | 608 | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=alg10 PE=3 SV=1 |
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| 5.43e-99 | 21 | 605 | 53 | 660 | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=ALG10 PE=3 SV=1 |
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| 1.01e-86 | 28 | 605 | 67 | 722 | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ALG10 PE=3 SV=1 |
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| 1.45e-76 | 28 | 605 | 61 | 771 | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alg-10 PE=3 SV=3 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.051201 | 0.948766 | CS pos: 34-35. Pr: 0.8773 |
TMHMM Annotations download full data without filtering help
| Start | End |
|---|---|
| 13 | 30 |
| 65 | 87 |
| 131 | 153 |
| 180 | 197 |
| 261 | 283 |
| 307 | 329 |
| 349 | 371 |
| 400 | 422 |
| 501 | 523 |