Species | Fusarium oxysporum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum | |||||||||||
CAZyme ID | FOC1_g10005690-t38_1-p1 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL42 | 40 | 337 | 3.6e-95 | 0.9493243243243243 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
406346 | BNR_4 | 9.35e-70 | 56 | 333 | 1 | 268 | BNR repeat-containing family member. BNR_4 is a family which carries the unique sequence motif SxDxGxTW which is so characteristic of the repeats of the BNR family, pfam02012. It is unclear whether or not this unit is repeated throughout the sequences of this family, but if it is then the family is likely to be bacterial neuraminidase. |
197314 | TDP2 | 5.69e-50 | 490 | 764 | 1 | 248 | Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains. Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. |
397447 | Exo_endo_phos | 8.38e-09 | 494 | 736 | 2 | 226 | Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12, and Nocturnin. |
197317 | EEP-1 | 1.25e-06 | 599 | 764 | 117 | 252 | Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins. |
197318 | EEP-2 | 0.009 | 599 | 728 | 95 | 233 | Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 768 | 1 | 809 | |
0.0 | 1 | 766 | 1 | 782 | |
4.51e-309 | 1 | 430 | 1 | 430 | |
4.51e-309 | 1 | 430 | 1 | 430 | |
4.51e-309 | 1 | 430 | 1 | 430 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.06e-302 | 20 | 430 | 3 | 413 | Chain A, L-Rhamnose-alpha-1,4-D-glucuronate lyase [Fusarium oxysporum],7ESM_A Chain A, L-rhamnose-alpha-1,4-D-glucuronate lyase [Fusarium oxysporum] |
|
1.75e-301 | 20 | 430 | 3 | 413 | Chain A, L-rhamnose-alpha-1,4-D-glucuronate lyase [Fusarium oxysporum] |
|
2.68e-301 | 20 | 430 | 5 | 415 | Chain A, L-Rhamnose-alpha-1,4-D-glucuronate lyase [Fusarium oxysporum] |
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3.26e-37 | 40 | 308 | 40 | 288 | Glycoside Hydrolase BACINT_00347 [Bacteroides intestinalis DSM 17393] |
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6.65e-36 | 40 | 308 | 35 | 283 | Glycoside Hydrolase BACCELL_00856 [Bacteroides cellulosilyticus DSM 14838] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.74e-12 | 102 | 279 | 150 | 371 | Ulvan lyase, short isoform OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_107 PE=1 SV=1 |
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3.31e-10 | 102 | 279 | 150 | 371 | Ulvan lyase, short isoform OS=Pseudoalteromonas sp. (strain PLSV) OX=1547444 GN=PLSV_3875 PE=1 SV=1 |
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6.49e-10 | 102 | 306 | 136 | 377 | Ulvan lyase, long isoform OS=Glaciecola sp. (strain KUL10) OX=2161813 GN=ullA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000236 | 0.999730 | CS pos: 19-20. Pr: 0.9746 |
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