UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
|---|---|---|
Q32KR8 | MCGALMERYVAAMVLSAAGDALGYFNGKWEFLQNGEKIHRQLAQLGGLDAIDVERWRVSDDTVMHLATAEALLEAGKVSDLTHLYSLLAKHYQDCMGDMDGRAPGGASVQNAMLLEPDKADGWRIPFNSHEGGCGAAMRAMCIGLRFPHSSQLDSLIQVSIESGRMTHHHPTGYLGALVSALFTAYAVNGKPPQQWGRGLMEVLPEAKKYIVQSGFFVEQNLQHWSYFQDQWEKYLKLRGIWDGKSAPTFPKPFDVKERDQFYSSVSYSGWGGSSGHDAPMIAYDAILAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLR | Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide Binds 2 magnesium ions per subunit. Monomer. Belongs to the ADP-ribosylglycohydrolase family. |
Q54H71 | MFHKFISTLTNKKITQTIMGTINKENIKPAMLLSAFGDACGYKNGIWEFEKSPSRIYEHYEYLGGYKNLKINKKDWRLSDDTIMHIATAIAITRPTNTDNESICKELAKAYIHSMEDMAGRAPGIQTINSVSLMTQTGMRSKVYQWNEIDFSDRAGGCGGSMRSMCIGFKYWSDEQLDTLIELSIESGRITHNNPVGFLGALVSALFASYAIRSIPPKTWPLKLMTEVMPKAREYLEKTSNSSNRNIENYEKGWNYFWNSWKSYLKLRQIPSNPDELKAANDKGIDYPVFPKDYSDYKVRENFYHSISFSGWGGSSGHDSCIIAYDALLGSADNWEEMIKRSVLHGGDNDSTGAIGCCWWGALYGFNGVPECNYEKIEYKSIIEGLAKEISN | Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] Binds 2 magnesium ions per subunit. Monomer. Belongs to the ADP-ribosylglycohydrolase family. |
D3DN83 | MEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDALDVGRWRVSDDTVMHLATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDGRAPGGASVHNAMQLKPGKPNGWRIPFNSHEGGCGAAMRAMCIGLRFPHHSQLDTLIQVSIESGRMTHHHPTGYLGALASALFTAYAVNSRPPLQWGKGLMELLPEAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGESAPTFPESFGVKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLGSKEDTVISL | Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide Binds 2 magnesium ions per subunit. Monomer. Belongs to the ADP-ribosylglycohydrolase family. |
P54923 | MGGGLIERYVAAMVLSAAGDTLGYFNGKWEFIRDGETIHQQLAQMGDLEAIDVARWRVSDDTVMHLATAEALMEAGQSPDLPRLYSLLAKHYRDCMGDMDGRAPGGACMQNAMLLQPNRADGYRIPFNSHEGGCGAAMRAMCIGLRFPHPSQLDLLIQVSIESGRMTHHHPTGYLGSLASALFTAYAVNGKSPWQWGKGLMEVLPEAKKYITQSGYFVKENLQHWSYFEKEWEKYLELRGILDGNSAPVFPQPFGVKERDQFYIDVSYSGWGGSSGHDAPMIAYDALLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFKGVNPANYEKLEYRQRLEEAGRALYSLGSKEDPVLDP | Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide Binds 2 magnesium ions per subunit. Synergistically stimulated by magnesium and dithiothreitol (DTT) in vitro. Monomer. Belongs to the ADP-ribosylglycohydrolase family. |
Q66H27 | MGGGLIERYVAAMVLSAAGDTLGYFNGKWEFLRDGEKIHRQLAQMGDLEAIDVAQWRVSDDTIMHLATAEALMEAGSSPDLPQLYSLLAKHYRDCMGDMDGRAPGGACMQNAMQLDPDRADGWRIPFNSHEGGCGAAMRAMCIGLRFPHPSQLDTLIQVSIESGRMTHHHPTGYLGSLASALFTAYAVNGKSPRQWGKGLMEVLPEAKAYVTQSGYFVKENLQHWSYFEKEWEKYLELRGILDGKSAPVFPKPFGVKERDQFYIEVSYSGWGGSSGHDAPMIAYDALLAAGDSWKELAHRAFFHGGDSDSTATIAGCWWGVMHGFKGVNPSNYEKLEYRQRLEEAGRALYSLGSKEDTILGP | Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein] alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide Binds 2 magnesium ions per subunit. Its activity is synergistically stimulated by magnesium and dithiothreitol (DTT) in vitro. Monomer. Belongs to the ADP-ribosylglycohydrolase family. |
Q5HIW9 | METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLSAKYIIHTVGPQIRRLPVSKMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEAFNRDAE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q99WQ1 | METLKSNKARLEYLINDMRRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNHQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKKTRGYNLPAKYIIHTVGPQIRRLPVSKMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEALNRDAE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q6GJZ1 | METLKSNKARLEYLINDMRRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLPAKYIIHTVGPQIRRLPVSKLNQDLLAKCYLSCLKLADQQSLNHIAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEAFNRDAE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q6GCE6 | METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLPAKYIIHTVGPQIRRLPVSKMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEAFNRDAE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q8NYB7 | METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLPAKYIIHTVGPQIRRLPVSKMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEAFNRDAE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q48YM4 | MPSSFDLLGEMIGLLQTEQLTSSWACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDAYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFSPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGHHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTTIFNTFTSEDKALYDTYLQKENNCE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q8K7D8 | MPSSFDLLGEMIGLLQTEQLTSSWACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDAYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFIPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGHHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTIIFNTFTSEDKALYDTYLQKENNCE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q5XC09 | MPSSFDLLGEMIGLLQTEQLTSSLACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDAYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFIPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGRHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTVIFNTFTSEDKALYDTYLQKENNCE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
Q8P0X2 | MPSSFDLLGEMIGLLQTEQLTSSLACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDAYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFIPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGRHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTIIFNTFTSEDKALYDTYLQKENNCE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress. 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] |
P0DN70 | MPSSFDLLGEMIDLLQTEQLTSYWACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDTYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFIPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGRHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTIIFNTFTSEDKALYDTYLQKENNCE | ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (PubMed:33769608). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L (SpyM50867), by releasing ADP-ribose from the target protein (PubMed:26166706). May be involved in the modulation of the response to host-derived oxidative stress (PubMed:26166706). 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein] Interacts with the lipoylated form of GcvH-L. |
B6HV34 | MSLLQDIVLIITGSASGIGLATATAALSQGAKILGVDVSWAPVSLTEHASYKFIQANLTHEATPKQVVETCIKEFGRIDGLLNIAGIMDQNSSVDSLTDDMWERCIAINLTAPVKLMREVIPIMRQQKSGSIVNVGSKAATSGAASGVAYTASKHGLMGATKNVAWRYKQEGIRCNAVCPGGVPTGIVQASDPTTWDKDALATMSHIHQAHAADRQEGLGVEAEDIANCLLFLVSSQSKRINGAIIPVDNAWSVI | Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). Secondary metabolite biosynthesis; terpenoid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
A0A1Y0BRF7 | MTRGNEKEEAPPQAKILGSFPTGIAPYAELMRVHRLLGFYLNTSPYLVGVAFCASISPTKIPITVLLHRTILLSIWSIFLRSAGCVWDDLIDMDLDSQISRTRTRPLPRGAVSPKNAFLLTVTLFACGGSVLIYLPWPCAVDCLIITFFALLYPFGKRFTDYPQITLVNIGWAIPMAMHSLGLDPLSQMKPTVCMFLFIGLVIIMIDVIYSRQDTEEDLKVGVKSMAVRFRESIELLSYSLLYASTGFLAMAGFFTGLGLSFFVVSVGGHFCGFWVLLKATRVGNSYGVESYAKSAFFLATLFWLFGFVIEYCLRN | Prenytransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). (2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate + diphosphate + H(+) Secondary metabolite biosynthesis; terpenoid biosynthesis. Drastically reduces the production of andrastin A. Belongs to the UbiA prenyltransferase family. |
B6HV35 | MTRRNEKEEVPPQGKILDLFHPGIAPYAELMRIHRLLGFYLNTSPYLVGVAFSASISSTKIPIAVLLHRAMLLSIWSIFLRSAGCVWDDLIDMDLDSQISRTKSRPLPRGAVSPSNALLLTVALFACGGTVLIFLPWACTVDCLIVTFFALSYPFGKRFTDYPQITLMNIGWAVPMAMHSLGLDPLSQMTPTVCMFLFIGSVIIMIDVIYSRQDTEEDLKVGVKSMAVRFRDSIQLLSYSLLCASTGFLAMAGVLTGLGLPFFVLSVGGHFCGFWVLLRATQVGKSSGVESYAKYNMPKQAFRPRPETSCATWLLSTSRNEMGRA | Prenytransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). (2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-carboxylate + diphosphate + H(+) Secondary metabolite biosynthesis; terpenoid biosynthesis. Belongs to the UbiA prenyltransferase family. |
A0A1Y0BRF9 | MEEGMEAPKFKVIIVGGSIAGLTLAHSLSQANIDHVVLEKRASIAPQEGAFIGVWPNGAQILDQLGLYHSLEKLTAPLSRMHLSFPDGYSFSSLLPKTIHEIFKYPIVSLDRQKVLEILFQNYPNKEKIITNQRVSEVRLLGDSASVVTEDGSVFQGDLIVGADGVHSRIRSEMWRLADELHPGMITPQERQTLTVEYACVFGISRAIPGLRSGEHINHYGDKFCVITFHGKDGRVFWFIIQKLDRVYTYPNAPRYSPNDAAELCDKIQDVIIWRDITVGDLWKTKLVSSMTALEEGLFETWSLNRIVILGDSVHKMTPNIGQGANTAIEDVAVLASLINRVVHADALHKPSESCIETMLQKYKTLRYERAKSTYERSRFGARFHTRDNWLKALVGRYVFQYVGGLIENRTSKTLAGGNVIDFLPRPHRLETGCVTRLPKGQGRPQQQWTLLWVSSLVLFLFLPWLRSYLPSATFW | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). Secondary metabolite biosynthesis; terpenoid biosynthesis. Drastically reduces the production of andrastin A. Belongs to the paxM FAD-dependent monooxygenase family. |
B6HV36 | MADSMETHKFKVIIVGGSIAGLTLAHSLSKANIDHIVIEKRAEIAPQEGAFIGVWPNGAQILDQLGLYQSLEELTAPISRMHLSFPDDYSFSSFLPKTIHERFKYPIVSLDRQKVLEILFQNYPDKSNIITNQRVSEVRLLGDSASVVTEDGSVFRGDLIVGADGVHSPLTVEYACVFGISRPIPGLRSGEHINHYGDKFCVITFHGKDGRVFWFIIQKLDRVYTYPNAPRYSPNDAADLCGKMQNVVIWQDITVGDLWKTKVVASMTALEEGIFETWSLNRIVILGDSVHKMTPNIGQGANTAIEDVAVLASLINRMIHADDLNKPSESCIETMLQEYKSLRYEPAKSTYQRSRFGARFHTRDSWLKAVVGRYVFQYVGGLIENRTIKTLAGGDTIDFLPRPDRLETGRVAQFQKSEESPQRQWTLLWVSSLALFLFFPWLGSYLHSTIS | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). Secondary metabolite biosynthesis; terpenoid biosynthesis. Belongs to the paxM FAD-dependent monooxygenase family. |
A0A1Y0BRF5 | MEESSLLSAILDHRDALASVAEFLRILAGICWTLNYFSMLRTSRKDKIPSTGIFPLCNDIGWEFIYAFIYPTASAHWEGGVRVWFLVHCIVIIFIIKYAHNEWDHFPLIQRNLYFLYGVVTIGFAIGQYSFAREVGPDLGFFYGGVLCQTLASLGPIAQILSRNSTRGASLLTWLLRAIATFGGFIKLTIYYLTGNAAGPWFESPMCKFYIGLTLVLDFTYPICYYVIQRQELANAQKEKKEKSK | Terpene cyclase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). Secondary metabolite biosynthesis; terpenoid biosynthesis. Drastically reduces the production of andrastin A. Belongs to the paxB family. |
B6HV37 | MEKSTLLSAVLKHRDALASVAEFLRILAGICWTLNYFSMLRTSQKDKIPSTGIFPLCNDIGWEFIYAFIYPKASAHWEGGVRVWFLVHCIVIFFIIKNAHNEWDYFPLIQRNLYFLYGIVTIGFAIGQYSFAREVGPDLGFFYGGVLCQTLASLGPIAQILSRNSTRGASLLLRAVATFGGFIKLTIYYLTGNAAGPWFESPMCKFYIGLTLILDFTYPICYYVIRRQELVNDEGDKKKKTKSGKAA | Terpene cyclase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). Secondary metabolite biosynthesis; terpenoid biosynthesis. Belongs to the paxB family. |
A0A1Y0BRF4 | MGFFSSTQPPRPATVPSDEIIPLHFWNTALCMRGTVLDISLKFDDVLDTSKLRSALEELLEMKDWRQLGARLRMNPNGRLEYHIPTRFDASRPAFAMTNAQHETSIADHPLGARIPHATSTPAIFPSPDVLSPLLRSEDAPKNIDDWICSDRPQLSIHIITFSDATLITVTWLHTLTDVMGMALILNAWTALLRGNREAVPKLQGFRLDPLTELGQRTPAEKYMHFNRVFGRKEFWWFIGLNVLDRLWYRQEERRTICIPAASLRNLCQQSSSEICASRGKEEPVPFVSESDVLLGWWVRSLYSALGLRTDQTILVNNALNLRTSLHESFTSNNSAYMGNALCMSPTFLRGHQVADEPLGQIALRIRESVTEQRTPEQVEAMTALQMQTMEQTGYLALVGDPRMMLLSCSNWHKARLFDIDFSSAVLQSSGPSSLQNPQHTGKPCYVNGVQHSANSFRNVLSVIGKDAGGNWWLTGVLRTDAWTHIEKQLHKLGSS | Acetyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. Drastically reduces the production of andrastin A. Belongs to the plant acyltransferase family. |
B6HV38 | MGLFSSTQPPQPTTVPSDEIIPLHFWNTALCMRGTVLDVSLKFDDVLDVSKLRDALNRLLEMEDWRQLGARLRMNVDGKLEYHIPAHFDASRPAFSMTNAQHETSIADHPLGARIPHTTGTPAIFPSPDELSPLLRSADAPKHIDDWTYSDRPQLCIHVITFSDATVITITWLHTLADVMGMTTILNAWTALLQGNREAIPKLQGFRSDPLTQLGQRTPAEKYMHFNRVFGRKEFLWFIGLNIFDRLWYRQEERRTICIPATCLRSLRQQASSEISATSSSEGGTVPFVSESDVLLGWWVRSLYGALGLRTDQTILVNNALNLRTSLHESFMSKDSAYMGNALCMSPTFLQGQQIADEPLGQIALRIRESVAEQRTPEQVEAMTALQMQTMEKTGYLALVGDPRMMLLSCSNWHKARLFDMDFSPAVLQSSAQSSSQNTQKKGKPSYVNGVQHSENSFRNVLSVIGKDAGRNWWLTGVLRTDAWAHVEEQVHKLGSS | Acetyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. Belongs to the plant acyltransferase family. |
A0A1Y0BRG0 | MHPDSQLETAVKNGFDPKSLYSTELTKVNEPARTILEQYSKIPAEKVLQHVKDLKDRAFEVFPYACIGQASFLELSIASSPCYPEMLDRVKKGDRLLDLGCAFGQELRQLIYDGAPSQNLYGTDLRPEFLELGLDLFLDRSFIKSHFIDADVLDDKSALVTQLTGELNIVYISLFLHVFDFETQIKVAKRVLDLLAPKAGSLIVCRVVACRDQAIGNATNARLPYYYHDLASWNRLWERVQEETGLKLKVDNWEQDDALAKKHPLEGIYMLGSSIRRE | Methyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. Drastically reduces the production of andrastin A. Belongs to the class I-like SAM-binding methyltransferase superfamily. |
B6HV39 | MHPDSQLETAVKSGFDPKSLYSTELTKVNEPARTILEKYSKIPADNILQHVKDLRDRAFAFPYACIGQASFLELSIASSPCYPEMLDRVKKGDRLLDLGCAFGQELRQLIYDGAPSQNLYGSDLRPEFLELGLDLFMDRPTIKSRFIDADVLDDKSALVTQLTGELNIVYISLFLHVFDFDTQIKVAKRALELLAPKAGSLIVCRVVACRDQAIGNATNARLPYYYHDLASWNRLWERVQEETGLKLKVDNWEQDDALAKKHPLEGIYMLGSSIRRE | Methyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). Secondary metabolite biosynthesis; terpenoid biosynthesis. Homodimer. Belongs to the class I-like SAM-binding methyltransferase superfamily. |
A8WZU4 | MDPDEVNQALGHYLNDSESGELVVEDSTTVQVTNPEARKTGDKIEVYYSRKTTVVSPTNSDDEEGEFCSDSELLPAQGGHRSRATSFAGRVRAGSDDEMNPKHTVLRYRRKKGGQWREVNAQGTPDKRKDDEDELEVDVKEDRSEQTGIVTKTYEARWKVLKYEHLPEWLQDNEFLRHGHRPPLPSFAECFKSIWSLHTETGNIWTHLIGCVAFFLLACWFLTRPDNHIQFQEKVVFSFFFAGAVSVSDSRSPSTPSRVIRSTSSRYSANSTIWESRCSLSARLFQPKITYIAMVCVLGIGAIVVSLWDKFSESKYRPVRAAVFVGMGCSGVIPTIHYIITDGVHSLFADNSFHWLLLMAFLYLLGAALYATRTPERFFPGKCDIWFQSHQLFHTCVVIAAFVHYYGISEMAFARLNEQCPVR | Probable receptor, which may be involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation. Belongs to the ADIPOR family. |
Q94177 | MNPDEVNRALGHYLNDADSGELVVEDSTTVQVKNPEARKTGDKIEVFYSRKTTVVSPTNSDDEDADFCSDSELLPQQEGHRSRATSFAGRIRAGSDDEAMPKHTILRYRRKKGGQWREINLQGTPDKRKDDEDELEVDVKEDRSEQTGIVTKTYEARWKVLKYEHLPEWLQDNEFLRHGHRPPLPSFSECFKSIWSLHTETGNIWTHLIGCVAFFFLACWFLTRPDNHIQFQEKVVFSFFFAGAVLCLGLSFAFHTLSCHSVNVVKIFCKLDYMGISLLIIGSFIPWIYYGFYCRREPKITYIAMVSVLGIGAIVVSLWDKFSESRFRPIRAAVFVGMGCSGVIPTIHYIITDGVHSLFADNSFHWLLLMAFLYLLGAGLYATRTPERFFPGKCDIWFQSHQLFHTCVVIAAFVHYYGISEMAFARLNEQCPVR | Probable receptor, which may be involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation. Belongs to the ADIPOR family. |
Q9VCY9 | MDSATNLLEQQGSAADVSGGSHPAEVEVTTQARATFGMDAEGHATGEAVTTTTATLRREGSDEDIFEQVQMILRKRRGWGPEDSLSPNDLDILEYDDELVEEDDAGCPLPSTPEDTQLIEAEMTEVLKAGVLSDEIDLGALAHNAAEQAEEFVRKVWEASWKVCHYKNLPKWLQDNDFLHRGHRPPLPSFRACFKSIFRVHTETGNIWTHLLGCIAFIGVALYFISRPSVEIQTQEKIVFGAFFIGAIVCLGFSFAFHTLSCHSVEMGRLFSKLDYCGIALLIMGSFVPWLYYGFYCHYQPKVIYLSVVSILGILSIVVSLWDKFSEPALRPLRAGVFMSFGLSGVIPAIHYSIMEGWFSQMSRASLGWLILMGLLYILGALLYALRVPERWFPGKFDIWGQSHQIFHILVIAAAFVHYHGISEMAMYRVMYSECTVPIEPITF | Adiponectin receptor. In insulin-producing cells, regulates insulin secretion and controls glucose and lipid metabolism. In larval and adult brain, expressed in insulin-producing cells and in neurons of the subesophageal region. Also expressed in lateral neurons of the adult brain (at protein level). In third instar larvae, expressed in central nervous system (CNS), imaginal disk, salivary gland, fat body, gut and malphigian tubules. Expressed throughout development and in adult. Belongs to the ADIPOR family. |
Q09749 | MSESEQLLEKQQDHKWDAATHADKGITIKTGKIAVSSSDIPLRNRKGLLTWDQLEPWQQDNQYIISGYRPPSFSFYLCVKSIFHVHNESVNIWTHLFGAIVFLFFIFKSELILKRDTTTAEDVYVITVFLFSAFTMLGCSTFYHTISNHSDDVSKFGNKLDYLGIVVMIVGSFIPCLHYAFACHANFRTLYIGTIIGIGVIVASTCLLDRFRQPEWRPYRALIFVLMGLFGIFPVIHALKIFSFSEILVRMGLVWLLLQGLFYIVGAVIYALRIPEKWSPGKYDVFGSSHQWFHVCVIIAAFCHFHGVCIAYDYFHERRGCGEM | Probable receptor, which may be involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation. Belongs to the ADIPOR family. |
A1L5A6 | MTTSGALFPSLVPGSRGSSNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSGGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSGGPPASSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGDGASTAASPAQPIQLSDLQSILATMSVPAGPGGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTAEEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNSASPEQQEGDGKDKKDEEEDMSLD | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). Interacts with the proteasomal scaffolding protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts with UBQLN2 and ubiquitin. The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with PSMD1 and ubiquitin. Preferential binding to the proximal subunit of 'Lys-48'-linked diubiquitin allows UCHL5 access to the distal subunit. Ubiquitinated by UBE3C in response to proteotoxic stress. Belongs to the ADRM1 family. |
Q09289 | MAAMFSNTRSVASSSGHIVEFKAGRSRLEAGSGDTMRKVVAEPKKGLVFIKQSNDMLIHFCWKDRETGAVVDDLIIFPDDAEFKAVPGCPDGKVYMLKFKSGDMKLFWIQDSTPDVDKDLVKKVTDALNKPPTSRPAASRSAGSNANTDRQSAGGSLISSSDMNAPLGGIDQGQLMSLIQSLQGGNSDTLPISSVPRGEDASSEADCEPSTNAAEEGSSNPLSLNNPAIQQIFNNLGRSQKKEVAVSLATALSNETVAEVARNHAEELAPHLPTSDDPARELSETVRTPQFRQAADTLGHALQTGQLGPVVAQFGMDEATVGSANQGDIRGFAANLTKAEGGEDAAKTQNSDDDATREPEPKRNRPDNEDMDVD | May function as a proteasomal ubiquitin receptor. May promote the deubiquitinating activity associated with the 26S proteasome. Component of the 19S proteasome regulatory particle complex (By similarity). The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP) (By similarity). Interacts with deubiquitinase ubh-4 (PubMed:23770237). The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with rpn-2 and ubiquitin. Preferential binding to the proximal subunit of K48-linked diubiquitin allows ubh-4 access to the distal subunit. Belongs to the ADRM1 family. |
Q98SH3 | MTTSGALFPSLVPGSRGSSSKYLVEFRAGKMSLKGSTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCTTGRVYVLKFKAGSKRLFFWMQEPKTDKDEEHCRKVNEYLNNPPMPGALGGNASGGHELSALGGEGGLQSLLGNMSHNQLMQLIGPTGLGGLGGLGALTGPGLASLLGSGGFPTSSSSSSSRSQSAAVTPSSTTSSTHVTPAPAVPAAASVTSPSPVPSSGSGTSSATSPTQPIQLSDLQNILATMNVPSGAGGQQVDLATVLTPEIMAPILANAEVQERLMPYLPSGESLPQTAEEIQNTLTSPQFQQALSMFSAALASGQHGPLMSQFGLPAEAIDAANKGDVEAFAKAMQNSVKSDQKEGDSKDKKDEEEDMSLD | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). Belongs to the ADRM1 family. |
Q6NZ09 | MSSGALFPSLVSGSRSSSSKYLVEFRAGKMTLKGSTVTPDKRKGTVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVNQCTTGRVYVLKFKAGSKRLFFWMQEPKTDKDDEYCRKVNEYLNNPPMPGALGSGGGGGHELSALGEGGLQSLLGNMSHNQLMQLIGPTGLGGLGALAGPGLASLLGSGGPATSSSTSSSRSQSAAATPSSGSAARLSSTQAPTTPVTPAATSSGSPTVTPTTPAAQTPSLPAGPASSTQPIQLSDLQSILATMNVPAMPTEGSGVDLASVLTPDVMAPILANPEVQQRLLPYLPSGESLPQSAEEIQNTLTSPQFQQAMSMFSSALASGQLGPLMNQFGLPSEAVDAANKGDVEAFAKAMEGSDSKTDDGDSKDKKDDDEDMSLD | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). Belongs to the ADRM1 family. |
Q8MYI8 | MNRPPQDVEFKAGKAKLTGTTVTSDSRKGYLKFGVTPEGLTCVQWRPRDSSAYEDEFYFAPGESKFIKVPACKTGRMYYLNFSGSDQKEFYWLQEANVEGDAKIEKALKVIESYIPDDDDDEEMVVDTPPPTTTIKQEPPKNPTINEVSLSQPKPTTTPPPSATNLDFIKDLFSNLPTQPKQPQITLGKILTAENLIPFLRENPEIKKDLIQYLPEEYQKDENMINEVLHSAQFLQSIETLDYAIHEGHGPEIVSLLGYEPSIASQRGVEGFLTNIQEGTNKKKNNK | Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme uchl5 at the 26S proteasome and promotes its activity (By similarity). Plays a role in the transition from growth to differentiation (PubMed:16987957). Interacts with the 26S proteasome (By similarity). Interacts with phg2 (PubMed:16987957). Belongs to the ADRM1 family. The gene for this protein is duplicated in strains AX3 and AX4. These strains contain a duplication of a segment of 750 kb of chromosome 2 compared to the corresponding sequence in strain AX2. |
Q6CIF3 | MDKLRLLGSYLRKSPLTSTVSEPGIKISPKQFTFSVRVRDKDRPSKISTTKINEPASKLENTSTVVHNEYLNSLQLPYLARTSLRVSKYDYKRAAQFSNTLKRTLKTQDAHERIFSISSEDVAKLISSLFQVSEDNVSLVAKKRFFERECFTEIPKITEEVLSDIQEFEDYIGLLTHTKFHHKGSSLQDGIIPKLLKNLLHPSNLRIAPLKTASVFNDVIYYYGNKNNFATCRELYAQMKSEGIAPNVQTYNLMLRNLLRNSRLIKQQLPYREAIFYLERMKKENISADVITWNTCYFLLKDNISRAIFLEKMVERGVPLTYHLLYGILEEEDIPFNVIIDFLRENDIPVDTKIIKICHRSLIKRDKFQASWKLMEYARHLNFRVKDPFFLEEYLRQFSEKGRMDMCIMTVNTFKATFEVEPTLHCYDLLFKCLVRQGYSSEFSRVYQMLLINLKEHTGGHVVMNYWIAKCRAIMNSNIKTIPTHDSITRLDALAKRCIWDKRGIKWNCWLEYSEYRNVFRRLGSVPYQSNSRDQLDKHEVAKSSKKKVKYLKKLKETAIRNKQSHDAAYRNDYYSALKNDLINRGIIEEQAK | Required for respiration. |
D6W407 | MNTLRCLTQALSKSGREAPKLYQKVIFPGLFREGIPIANVKKVDEKIIDSPTSTSVNGEAKKIVRHGVKYEREQVKEYLSSLPTLTLSRKQIRDDYDEERAKRMYMFSKQTNSSNKFQKLLTAKSQEFTRELLTLLIDCTSNEKNSGPERFTRKFLKFSNDEIPPLPDFSKNPQLFENYIGILSHTKFNFRSSSKLNGIVRKMLRHLLHPTNKTTLPLRSAQVYNDSIYFFSEHFDFASCREIFAQMKAEGTKPNTITFNLLLRNVVKNSHIRKTKHPDDEVLFYLRSMRNHGVFADVITWTTCYNFLRDEVSRQLYIVQMGEHLGNFNVNFVYTVLRNGDYRAEDCLKVLAANSLPISRKTFYLCIERLLNEEQLETASKLLDYGFQHLKSNFKLDSEAMNHFMRVFANKGRSDLAFLCYNTCRKIYKIKPDSQTFEMLFKALVRNGNTKNFGAVLQYIKDLKVSEGFGLRTSYWRTKADSIFKFGSPNTLSEKSIEKARKLLGNLIASEGEFSWKIWKESDSSQKKILRFLGCIPTTLRCTNTAQDHQKPTNLPSNISQKKREYRNRVKAIATKAALEKRMAYIKDNDVAFKKELVKRRIVGEV | Required for respiration. Stabilizes the mitochondrial bicistronic mRNA encoding ATP6 and ATP8, 2 subunits of the proton-translocating ATP synthase. Present with 1760 molecules/cell in log phase SD medium. |
Q53463 | MKFNVKMLSVTLGLFTSHAFAHTVYENARIYTVNDRQPTASVLVVDQGKIVYVGGNDGAKPFKATATELVDLEGKTVLPGFIESHAHPATVAVMEAGDFVYVDGARTLSQILSQLKAYLVAHPKANYLLAQGFNVASLGLPQGALPTAADLDTVSESVPIVVYDSGMHAGWANSAALNVAHVDANTPDPIPGKHYFERDNKGNPTGFMHESAMHNVVDAQQFNAVENVAEKLQPILKTYHSLGFTAITDVGDTFSTTVAAIARLNEQGKLKVYYQRGYFYDAAKSTEQNIASLKGLREKYHQGNLSINLYKLFMDGTIEMDSGAMYQPYPNGNVVEPFLSQKQINDNVAAALKAGFSVHVHAIGDKAQQSILDAFAANKKINPQLARVIAHNQVFEPQGVQKFAAMKDNLFLQTTPNWAVMYEKDETKTKIGQDAYHHQFLLGQAAREGVAVTSALTILRIPLMR | Involved in the control of extracellular enzymes production. Stimulates PEL, PEH, CEL, and PRT production. Belongs to the metallo-dependent hydrolases superfamily. |
Q9T199 | MTSYYYSRSLANVNKLADNTKAAARKLLDWSESNGIEVLIYETIRTKEQQAANVNSGASQTMRSYHLVGQALDFVMAKGKTVDWGAYRSDKGKKFVAKAKSLGFEWGGDWSGFVDNPHLQFNYKGYGTDTFGKGASTSNSSKPSADTNTNSLGLVDYMNLNKLDSSFANRKKLATSYGIKNYSGTATQNTTLLAKLKAGKPHTPASKNTYYTENPRKVKTLVQCDLYKSVDFTTKNQTGGTFPPGTVFTISGMGKTKGGTPRLKTKSGYYLTANTKFVKKI | Cell wall lytic enzyme. Hydrolyzes the link between L-alanine and D-glutamate residues in certain bacterial cell-wall glycopeptides. Expressed at about 20 minutes after infection. Belongs to the peptidase M15C family. |
Q37979 | MALTEAWLIEKANRKLNAGGMYKITSDKTRNVIKKMAKEGIYLCVAQGYRSTAEQNALYAQGRTKPGAIVTNAKGGQSNHNYGVAVDLCLYTNDGKDVIWESTTSRWKKVVAAMKAEGFKWGGDWKSFKDYPHFELCDAVSGEKIPAATQNTNTNSNRYEGKVIDSAPLLPKMDFKSSPFRMYKVGTEFLVYDHNQYWYKTYIDDKLYYMYKSFCDVVAKKDAKGRIKVRIKSAKDLRIPVWNNIKLNSGKIKWYAPNVKLAWYNYRRGYLELWYPNDGWYYTAEYFLK | Cell wall lytic enzyme. Hydrolyzes the link between L-alanine and D-glutamate residues in certain bacterial cell-wall glycopeptides. Expressed at about 20 minutes after infection. Belongs to the peptidase M15C family. |
Q53462 | MGQEPKGIESRKIQDGHVRKKVGRQQGLWVRTTKKEKFSRMSRDANV | Involved in the control of extracellular enzymes production. Stimulates PEL, PEH, CEL, and PRT production. |
Q6BZQ0 | MKLATAFTILTAVLAAPLAAPAPAPDAAPAAVPEGPAAAAYSSILSVVAKQSKKFKHHKRDLDEKDQFIVVFDSSATVDQIASEIQKLDSLVDEDSSNGITSALDLPVYTDGSGFLGFVGKFNSTIVDKLKESSVLTVEPDTIVSLPEIPASSNAKRAIQTTPVTQWGLSRISHKKAQTGNYAYVRETVGKHPTVSYVVDSGIRTTHSEFGGRAVWGANFADTQNADLLGHGTHVAGTVGGKTYGVDANTKLVAVKVFAGRSAALSVINQGFTWALNDYISKRDTLPRGVLNFSGGGPKSASQDALWSRATQEGLLVAIAAGNDAVDACNDSPGNIGGSTSGIITVGSIDSSDKISVWSGGQGSNYGTCVDVFAPGSDIISASYQSDSGTLVYSGTSMACPHVAGLASYYLSINDEVLTPAQVEALITESNTGVLPTTNLKGSPNAVAYNGVGI | Major secreted protein that belongs to the subtilisin family serine proteases. Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. The protease activity is completely inhibited by the serine inhibitor PMSF but is not affected by thiol group inhibitors and in the presence of dithiothreitol (PubMed:6750031). In the presence of high concentrations of o-phenanthroline the protease activity is only partially inhibited (PubMed:6750031). The pro-region plays an inhibitory role and may provide a mechanism for preventing premature activation in the secretory pathway (PubMed:2649495). Optimum pH is 9.0-10.0. Optimum temperature is 40 degrees Celsius. Proper secretion requires TSR1. Expression is subject to at least 3 different regulatory controls, carbon, sulfur and nitrogen repression (PubMed:870075). Intracellular cysteine and ammonia appear to be the metabolic signals for sulfur and nitrogen repression (PubMed:870075). Moreover, pH regulates expression independently from other metabolic signals, with highest levels of AEP mRNA at pH 6.5 (PubMed:8842151, PubMed:9308186). The transcriptional activator RIM101 and the Rim pathway are required for the alkaline induction of gene expression (PubMed:9199331, PubMed:11861549). Two major upstream activation sequences (UASs) are essential for promoter activity under conditions of repression or full induction. The distal UAS (UAS1) is located at position -790 to -778, whereas the proximal UAS (UAS2) localizes at positions -148 to -124 (PubMed:8264600, PubMed:10206713). The pro-region is removed through cleavage by XPR6 after Lys156-Arg157, which yields mature active XPR2. The 10 consecutive -X-Ala- or -X-Pro- dipeptides located over 100 amino acids upstream of the N-terminal of mature XPR2 are subject to dipeptidyl aminopeptidase (DPAPase)-processing (PubMed:9353927). DPAPase activity is not necessary for XPR6 cleavage and for secretion of mature active XPR2 (PubMed:9353927). N-glycosylated. Glycosylation within the pro-region has no effect on secretion and maturation at 18 degrees Celsius, but is required for secretion at 28 degrees Celsius (PubMed:1995632). The pro-region inhibits protease activity (PubMed:2649495) and plays an additional essential role in the proper folding of the protein into a conformation compatible with secretion (PubMed:1995632, PubMed:1634541). Its complex processing and high level of secretion make XPR2 the perfect model to study the secretion pathway. Belongs to the peptidase S8 family. Strain CLIB 122 / E 150 has a defective XPR2 sequence (xpr2-322) which lacks the N-terminus (positions 1 to 34). |
P07164 | MTSEQYSVKLTPDFDNPKWIGRHKHMFNFLDVNHNGRISLDEMVYKASDIVINNLGATPEQAKRHKDAVEAFFGGAGMKYGVETEWPEYIEGWKRLASEELKRYSKNQITLIRLWGDALFDIIDKDQNGAISLDEWKAYTKSDGIIQSSEDCEETFRVCDIDESGQLDVDEMTRQHLGFWYTMDPACEKLYGGAVP | Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light. The reduction of the disulfide bond is necessary to regenerate aequorin from apoaequorin. Aequorin is used as an intracellular Ca(2+) indicator. Aequorin has a number of advantages over other Ca(2+) indicators, for example, low leakage rate from cells, lack of intracellular compartmentalization or sequestration and it does not disrupt cell functions or embryo development. Belongs to the aequorin family. Was originally thought to have an internal disulfide bond. Aequorin entry |
P02592 | MTSKQYSVKLTSDFDNPRWIGRHKHMFNFLDVNHNGKISLDEMVYKASDIVINNLGATPEQAKRHKDAVEAFFGGAGMKYGVETDWPAYIEGWKKLATDELEKYAKNEPTLIRIWGDALFDIVDKDQNGAITLDEWKAYTKAAGIIQSSEDCEETFRVCDIDESGQLDVDEMTRQHLGFWYTMDPACEKLYGGAVP | Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light. The reduction of the disulfide bond is necessary to regenerate aequorin from apoaequorin. Belongs to the aequorin family. Was originally thought to have an internal disulfide bond. |
A7RFL3 | MKSVIAVLVLSLVLVNFTQAAKDDRWKACRMKCYTESKLCMNNDSKCFDSQSCNSCIQQVYSPCFNRCQEMLRRREAFKRMFAFDEEN | Probable neuropeptide. Is expressed in the ectodermal cells of gastrulae and planulae. Is also noticeable in the endoderm in late planulae. In the primary polyps, is expressed in both ectoderm (sensory neurons) and endoderm (ganglions). Is not expressed in nematocytes. Is strongly and equally detected in planulae, in primary polyps (9d), and in both adult females and males (at protein level) (PubMed:33060291). Transcripts are expressed early in development in ectodermal cells of the gastrula, then increases in early planula and by the late planula spreads in expression to endodermal cells. In primary polyps, they are expressed in ectodermal sensory cells and multiple endodermal ganglion cells that send their processes in different directions all around the body (PubMed:33060291). Extended N-terminus. |
P0DQS0 | MLVNARAIRQSIGIVVAQCRRDLESNRTLDYRTRMRTSLILVAMVMVSVLLPYTYGSSCDSFCTEQANKCLTGCEGFVGCMECTNFAGHCREQCRKRSVKRRKEIRARFTKEPTEES | Expressed in endodermal ganglion neurons, apparently bipolar and following mesentery folds (observed in both planulae and primary polyps). It not expressed in nematocytes. The mature peptide may be cleaved at a dibasic residue site and be shorter than the sequence shown (possibly residues 1-94). |
Q06305 | MKKLKITGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQEVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGSASSTWCYPTNPATGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTSIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAINDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSPTTSLSQSVRPTVPAHSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLPTMQNNLAKVLRPVRAGITGDFSAESQFAGNIEIGAPVPVAAASHSSRARNLSAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
Q06303 | MKKLKITGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQEVCGDKYRPVNREEAQSIKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGSASSTWCYPTNPATGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTSIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAINDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPAHSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLPTMQNNLAKVLRPVRAGITGDFSAESQFAGNIEIGAPVPVAAASHSSRARNLSAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
Q06306 | MQKLKITGLSLIISGLLMAQRHAAEPVYPDQLRLFSLGQEVCGDKYRPITREEAQSVKSNIVNMMGQWQISGLANGWVIMGPVYNGEIKPGSASNTWCYPVNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCEGYRCGEKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAINDSYTPQSAYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLAADGKAPRALSARRGEQGLRLAIPLECRKSSPGLASATSA | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
P09166 | MKALKITGLSLIISATLAAQTNAAEPIYPDQLRLFSLGEDVCGTDYRPINREEAQSVRNNIVAMMGQWQISGLANNWVILGPGYNGEIKPGKASTTWCYPTRPATAEIPVLPAFNIPDGDAVDVQWRMVHDSANFIKPVSYLAHYLGYAWVGGDHSQFVGDDMDVIQEGDDWVLRGNDGGKCDGYRCNEKSSIRVSNFAYTLDPGSFSHGDVTQSERTLVHTVVGWATNISDTPQSGYDVTLNYTTMSNWSKTNTYGLSEKVSTKNKFKWPLVGETEVSIEIAANQSWASQNGGAVTTALSQSVRPVVPARSRVPVKIELYKANISYPYEFKADMSYDLTFNGFLRWGGNAWHTHPEDRPTLSHTFAIGPFKDKASSIRYQWDKRYLPGEMKWWDWNWAIQQNGLATMQDSLARVLRPVRASITGDFRAESQFAGNIEIGTPVPLGSDSKVRRTRSVDGANTGLKLDIPLDAQELAELGFENVTLSVTPARN | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter (By similarity). Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. Was originally thought to originate from A.sobria. |
P09167 | MQKIKLTGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane. Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
Q08676 | MMNRIITANLANLASSLMLAQVLGWHEPVYPDQVKWAGLGTGVCASGYRPLTRDEAMSIKGNLVSRMGQWQITGLADRWVIMGPGYNGEIKQGTAGETWCYPNSPVSGEIPTLSDWNIPAGDEVDVQWRLVHDNDYFIKPVSYLAHYLGYAWVGGNHSPYVGEDMDVTRVGDGWLIKGNNDGGCSGYRCGEKSSIKVSNFSYTLEPDSFSHGQVTESGKQLVKTITANATNYTDLPQQVVVTLKYDKATNWSKTDTYSLSEKVTTKNKFQWPLVGETELAIEIAASQSWASQKGGSTTETVSVEARPTVPPHSSLPVRVALYKSNISYPYEFKAEVNYDLTMKGFLRWGGNAWYTHPDNRPTWEHTFRLGPFRGQGEQHPLPVDKRYIPGEVKWWDWNWTISEYGLSTMQNNLGRVLRPIRSAVTGDFYAESQFAGDIEIGQPQTRSAKAAQLRSASAEEVALTSVDLDSEALANEGFGNVSLTIVPVQ | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
Q06304 | MMNRIITANLAFLASSLMLAQVQAAEPVYPDQVKWAGLGTGVCASGYRPLTRDEAMSIKGNLVSRMGQWQITGLADRWVIMGPGYNGEIKQGTAGETWCYPNSPVSGEIPTLSDWNIPAGDEVDVQWRLVHDNDYFIKPVSYLAHYLGYAWVGGNHSPYVGEDMDVTRVGDGWLIKGNNDGGCSGYRCGEKSSIKVSNFSYTLEPDSFSHGQVTESGKQLVKTITANATNYTDLPQQVVVTLKYDKATNWSKTDTYSLSEKVTTKNKFQWPLVGETELAIEIAASQSWASQKGGSTTETVSVEARPTVPPHSSLPVRVALYKSNISYPYEFKAEVNYDLTMKGFLRWGGNAWYTHPDNRPTWEHTLLLGPFRGQGEQHPLPVDKRYIPGEVKWWDWNWTISEYGLSTMQNNLGRVLRPIRSAVTGDFYAESQFAGDIEIGQPQTRSAKAAQLRSASAEEVALTSVDLDSEALANEGFGNVSLTIVPVQ | Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane (By similarity). Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family. |
P09165 | MMIKRHLPQPRHRERPGALCGSGVPAPAARHPTAVPGGQDQFGSATHHGSDGQTHTGPQIR | Regulation of the expression of aerolysin. |
A0A073CEA3 | MLKFSMEFCYPQPDVKTLIVGTLGPKETSSEQTLNYLITQWQAEQISVTSHLFDTFTELKEALLQDRVDLALVPHAYERVNDFYMEPSLKLGFVFTYPTPIYGLAKRKNEELVWENCTLVTHPAPFPLLPYLLPGYPHQKNIKVEFVNSTSAAAIQVKQGLADLAITNENALKENDLEFIAEYGKIEMSWSIFHKKGTVHRE | In vivo, involved in the biosynthesis of 2-carboxy-6-hydroxyoctahydroindole (Choi) present in the nonribosomal glycopeptides aeruginoside 126A and B. AerD is an unusual prephenate decarboxylase that avoids the typical aromatization of the cyclohexadienol ring of prephenate. AerD catalyzes the protonation at C8 followed by decarboxylation to produce the dihydro-4-hydroxyphenylpyruvate regioisomer A258 (H2HPP A258)(3-(4-hydroxycyclohexa- 1,5-dienyl)-2-oxopropanoic acid), which is able to undergo a nonenzymatic isomerization to produce dihydro-4-hydroxyphenylpyruvate regioisomer A295 (H2HPP A295)(3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoic acid). H(+) + prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 kcat is 245 min(-1) for decarboxylase activity with prephenate as substrate. Cells lacking this gene are unable to produce aeruginoside 126A and B. Belongs to the prephenate decarboxylase family. |
Q39184 | MQSSVYRDKASSIAMILETQRNVEFPHRIVDKRPRKRPRLTWDAAPPLLPPPPPPTVFQPPLYYGPEFASGLVPNFVYPNMFYNGLPRQGSPPWRPDDKDGHYVFVVGDTLTPRYQILSKMGEGTFGQVLECFDNKNKEVVAIKVIRSINKYREAAMIEIDVLQRLTRHDVGGSRCVQIRNWFDYRNHICIVFEKLGPSLYDFLRKNSYRSFPIDLVRELGRQLLESVAYMHDLRLIHTDLKPENILLVSSEYIKIPDYKFLSRPTKDGSYFKNLPKSSAIKLIDFGSTTFEHQDHNYIVSTRHYRAPEVILGVGWNYPCDLWSIGCILVELCSGEALFQTHENLEHLAMMERVLGPLPPHMVLRADRRSEKYFRRGAKLDWPEGATSRDSLKAVWKLPRLPNLIMQHVDHSAGDLIDLLQGLLRYDPTERFKAREALNHPFFTRSREQSIPPFNPNPHPFLYNQKN | Activator of yeast transcription factor, STE12. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] A number of isoforms are produced. According to EST sequences. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. |
P51567 | MEMERVHEFPHTHMDRRPRKRARLGWDVLPQATKAQVGMFCGQEIGNISSFASSGAPSDNSSSLCVKGVARNGSPPWREDDKDGHYIFELGDDLTPRYKIYSKMGEGTFGQVLECWDRERKEMVAVKIVRGVKKYREAAMIEIEMLQQLGKHDKGGNRCVQIRNWFDYRNHICIVFEKLGSSLYDFLRKNNYRSFPIDLVREIGWQLLECVAFMHDLRMIHTDLKPENILLVSSDYVKIPEYKGSRLQRDVCYKRVPKSSAIKVIDFGSTTYERQDQTYIVSTRHYRAPEVILGLGWSYPCDVWSVGCIIVELCTGEALFQTHENLEHLAMMERVLGPFPQQMLKKVDRHSEKYVRRGRLDWPDGATSRDSLKAVLKLPRLQNLIMQHVDHSAGELINMVQGLLRFDPSERITAREALRHPFFARRR | ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] A number of isoforms are produced. According to EST sequences. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. |
Q39185 | MIANGFESMDKERVRKRPRMTWDEAPAEPEAKRAVIKGHGSDGRILSPPLRDDDRDGHYVFSLRDNLTPRYKILSKMGEGTFGRVLECWDRDTKEYVAIKIIRSIKKYRDAAMIEIDVLQKLVKSDKGRTRCVQMKNWFDYRNHICIVFEKLGPSLFDFLKRNKYSAFPLALVRDFGCQLLESVAYMHELQLVHTDLKPENILLVSSENVKLPDNKRSAANETHFRCLPKSSAIKLIDFGSTVCDNRIHHSIVQTRHYRSPEVILGLGWSYQCDLWSIGCILFELCTGEALFQTHDNLEHLAMMERALGPLPEHMTRKASRGAEKYFRRGCRLNWPEGANSRESIRAVKRLDRLKDMVSKHVDNTRSRFADLLYGLLAYDPSERLTANEALDHPFFKSSS | ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] A number of isoforms are produced. According to EST sequences. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. |
A2R797 | MLISGSSAALCALALPFAAAKSLWSDSPGNYSSFITTAFPLGNGRLGAMPIGSYDKEIVNLNVDSLWRGGPFESPTYSGGNPNVSKAGALPGIREWIFQNGTGNVSALLGEYPYYGSYQVLANLTIDMGELSDIDGYRRNLDLDSAVYSDHFSTGETYIEREAFCSYPDNVCVYRLSSNSSLPEITFGLENQLTSPAPNVSCHGNSISLYGQTYPVIGMIYNARVTVVVPGSSNTTDLCSSSTVKVPEGEKEVFLVFAADTNYEASNGNSKASFSFKGENPYMKVLQTATNAAKKSYSALKSSHVKDYQGVFNKFTLTLPDPNGSADRPTTELLSSYSQPGDPYVENLLFDYGRYLFISSSRPGSLPPNLQGLWTESYSPAWSGDYHANINLQMNHWAVDQTGLGELTEPLWTYMAETWMPRGAETAELLYGTSEGWVTHDEMNTFGHTAMKDVAQWADYPATNAWMSHHVWDHFDYSQDSAWYRETGYPILKGAAQFWLSQLVKDEYFKDGTLVVNPCNSPEHGPTLTPQTFGCTHYQQLIWELFDHVLQGWTASGDDDTSFKNAITSKFSTLDPGIHIGSWGQIQEWKLDIDVKNDTHRHLSNLYGWYPGYIISSVHGSNKTITDAVETTLYSRGTGVEDSNTGWAKVWRSACWALLNVTDEAYSELSLAIQDNFAENGFDMYSGSPPFQIDANFGLVGAMVQMLIRDSDRSSADASAGKTQDVLLGPAIPAAWGGGSVGGLRLRGGGVVSFSWNDSGVVDSCKADLSARGSDVSQVKFYVAGGRAIDCSS | Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose (By similarity). an alpha-L-fucoside + H2O = an alcohol + L-fucose Belongs to the glycosyl hydrolase 95 family. |
Q2USL3 | MRSLVLLGMSSLATANSLWSSKAASWDTTNEAYTLGNGKLGVMPFGEPGAEKLNLNHDELWEGGPFEVNGYRGGNPNSSMTEILSEVRDEIWKKGTGNDSRLHGDTDGYGSFHSLANLTIAIDGIDKVSDYTRSLDLGTGIHTTTYSTGKGKYTTDVYCSYPAQVCIYKLNSTATLSKVTIYFDQLVEESSLWNATCDSDFARLRGVTQEGPPRGMTYDTIARSSIPGRCDSSTGKLAINARNSSSLTIVIGAGTDFDGTKGTAATDYTFKGEDPAEYVEKITSSALSQSESKLRTEHIEDYSGLMSAFTLDLPDTQDSTGTELSTLITNYNANKTDGDPYLEKLLFDYGRHLFISSSRANSLPPNLQGVWSPTKNAAWSGDYHANINLQMNLWGAEATGLGELTVAVFNYMEQNWMPRGAETAELLYGGAGWVTHDEMNIFGHTGSLVVNPCTSPEQGPTTFGCTHWQQLIHQVYENAIQGAEIAGETDSTLLKDIKDQLPRLDKGLHIGTWGQIKEWKLPDSYDYEKEGNEHRHLSHLVGWYPGWSLSSYFNGYNNATIQSAVNTSLISRGVGLYTNAGWEKVWRSACWARLNNTEKAHYELRLTIDQNIGQSGLSLYSGGDTPSGAFQIDANFGYLGAVLSMLVVDMPLDSTHSEDDVRTVVLGPAIPAAWAGGSVKGLRLRGGGSVDFSWDSEGLVDKASATGVSSNVRIVNVEGTVLV | Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose (By similarity). an alpha-L-fucoside + H2O = an alcohol + L-fucose Belongs to the glycosyl hydrolase 95 family. |
Q1HFQ8 | MRKTTLFLAVTFATSNAQGRALRSSSPATYGTTDGSDYILKTGYLIGNGKLGVIPFGPPDTEKLNLNVDSLWSGGPFEVENYTGGNPSSPIYDALPGIRERIFENGTGGMEELLGSGNHYGSSRVLGNITIALDGVEAYSKYKRTLDLSDGVHRTSFTIANRTTAALKSSIFCSYPDQVCVYHLESASDARLPKVTISIENLLVNQSLLQTSCESEAKRAVLRHSGVTQAGPPEGMKYAAVAEVVNPRSSVTTCLGEGALQISSRKKQLTIIIGAATNYDQKAGNAKSGWSFKNAKDPASIVDGIASAAGWKGYQRLLDRHVKDYKKLMGDFSLELPDTTDSASKDTSELIEKYSYASATGNPYLENLLLDYARHLLVSSSRPNSLPANLQGRWTESLTPSWSADYHANINLQMNYWLADQTGLGETQHALWNYMADTWVPRGTETARLLYNASGWVVHNEINIFGFTAMKEDAGWANYPAAAAWMMQHVWDNFDYTHDTAWLVSQGYALLKGIASFWLSSLQEDKFFNDGSLVVNPCNSPETGPTTFGCTHYQQLIHQVFETVLAAQEYIHESDTKFVDSVASALERLDTGLHLSSWGGLKEWKLPDSYGYDNMSTHRHLSHLAGWYPGYSISSFAHGYRNKTIQDAVKETLTARGMGNAADANAGWAKVWRAACWARLNDSSMAYDELRYAIDENFVGNGLSMYWGASPPFQIDANFGFAGAVLSMLVVDLPTPRSDPGQRTVVLGPAIPSAWGGGRAKGLRLRGGAKVDFGWDKRGVVNWVNIVKRGKGTSRVKLVNKEGDILAEM | Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside. an alpha-L-fucoside + H2O = an alcohol + L-fucose Belongs to the glycosyl hydrolase 95 family. |
Q8NB23 | MGAAGSDGRCCVRSGRAGTGGAGSKWVVMDLWTGGAGSRRAVLGPDGRWVRWAVLGSVRMGGARSKWAAPDPMGGAGFGPDWRVRVWTGGAGSKWGCSAGSGRAVLGPNGRWVPWAVLGSVRTGGAGSKWAALGPMGGTGSGRAVLGLDGRCSIQMGAAGSGRAVLGSVRTGGAGSKWAVLGSAGDRWAWRHRYGAQGRWSALSEGPCAPRARCSSCPRIAPGLLRVSSRVIPFRWVTSKPTFSSCFLPRRTRC | Ubiquitously expressed. Product of a dubious CDS prediction. May be a long non-coding RNA. |
G5EGL9 | MRLWQWSIAVAICLVMVTEARLRRHHRKRRFVSSNFDEFYCGESAHAQSQFEEERESNSSKVSSVHSTQFNWGLDNTICIKLQNVVHVLKYERLEQRYPIENSYTFSVPLIDTNCKCHCYGFGTNDVCNVEKYADDRNCTTSSEFPTCYTKYHPAVEPLDCPVTSIPAKACCDIKLKPRDGRMFRAVKLQQPINDMIISHSIFANNSGKMMKVLGPDEFRINLLKGKEQFELTEYHRISVQLVASSPQQQLREGMYYFPEENHNDLREGKINEITESDLDKLGWYRRVGNDWQVATSGLLLRNAHKVVIKNCKGQVHMDQFSGTKNFVLRGTQYNDTYNERRVSDNNFVRSVKVDESSREITIVHEHGTAAQVSLKTDTRPNLTKSQSLLANFTGSITLDHDGNRMLNVTFFGVKGTVHIKMYVNDRKLIATFACTAQFGTSLKDDGSRISLPSTINQAQWVCILPDEQPTKSEICKWIPYEEKAMRTPRQEQSWSKGHSPCSQAECNSLKSGVSDLFPWIMNFDYFMAHGGDFTEWLKIGIHIVIAVGLLLLLILLFTKCLVPLACCSLSIPFKNRNKKKKKKNSSDY | Required for cell fusion events during development including the fusion of anchor cells (AC), vulval A and vulval D rings, and late epidermal seam cells (PubMed:17488621). Required for amphid sheath cell fusion induced by entry into dauer stage (PubMed:21350017). Expressed in amphid sheath cells. First expressed in embryonic hyp5 cells and then during larval development in pharyngeal muscles, uterine rings, head and tail neurons, sheath cells of chemo-sensory neurons, and in male neurons. Expressed in AC, vulval D rings and uterine seam cells in cell fusion events during development. Egg laying defective phenotype. AC fail to fuse in the majority of worms (PubMed:17488621). RNAi-mediated knockdown in a daf-7 e1372 mutant background causes a severe defect in amphid sheath cell fusion induced by entry into dauer stage (PubMed:21350017). Belongs to the EFF/AFF cell fusogen family. |
E9PBM3 | MAAQSSLYNDDRNLLRIREKERRNQEAHQEKEAFPEKIPLFGEPYKTAKGDELSSRIQNMLGNYEEVKEFLSTKSHTHRLDASENRLGKPKYPLIPDKGSSIPSSSFHTSVHHQSIHTPASGPLSVGNISHNPKMAQPRTEPMPSLHAKSCGPPDSQHLTQDRLGQEGFGSSHHKKGDRRADGDHCASVTDSAPERELSPLISLPSPVPPLSPIHSNQQTLPRTQGSSKVHGSSNNSKGYCPAKSPKDLAVKVHDKETPQDSLVAPAQPPSQTFPPPSLPSKSVAMQQKPTAYVRPMDGQDQAPSESPELKPLPEDYRQQTFEKTDLKVPAKAKLTKLKMPSQSVEQTYSNEVHCVEEILKEMTHSWPPPLTAIHTPSTAEPSKFPFPTKDSQHVSSVTQNQKQYDTSSKTHSNSQQGTSSMLEDDLQLSDSEDSDSEQTPEKPPSSSAPPSAPQSLPEPVASAHSSSAESESTSDSDSSSDSESESSSSDSEENEPLETPAPEPEPPTTNKWQLDNWLTKVSQPAAPPEGPRSTEPPRRHPESKGSSDSATSQEHSESKDPPPKSSSKAPRAPPEAPHPGKRSCQKSPAQQEPPQRQTVGTKQPKKPVKASARAGSRTSLQGEREPGLLPYGSRDQTSKDKPKVKTKGRPRAAASNEPKPAVPPSSEKKKHKSSLPAPSKALSGPEPAKDNVEDRTPEHFALVPLTESQGPPHSGSGSRTSGCRQAVVVQEDSRKDRLPLPLRDTKLLSPLRDTPPPQSLMVKITLDLLSRIPQPPGKGSRQRKAEDKQPPAGKKHSSEKRSSDSSSKLAKKRKGEAERDCDNKKIRLEKEIKSQSSSSSSSHKESSKTKPSRPSSQSSKKEMLPPPPVSSSSQKPAKPALKRSRREADTCGQDPPKSASSTKSNHKDSSIPKQRRVEGKGSRSSSEHKGSSGDTANPFPVPSLPNGNSKPGKPQVKFDKQQADLHMREAKKMKQKAELMTDRVGKAFKYLEAVLSFIECGIATESESQSSKSAYSVYSETVDLIKFIMSLKSFSDATAPTQEKIFAVLCMRCQSILNMAMFRCKKDIAIKYSRTLNKHFESSSKVAQAPSPCIASTGTPSPLSPMPSPASSVGSQSSAGSVGSSGVAATISTPVTIQNMTSSYVTITSHVLTAFDLWEQAEALTRKNKEFFARLSTNVCTLALNSSLVDLVHYTRQGFQQLQELTKTP | Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1. The result is a rogue activator protein. Belongs to the AF4 family. |
O88573 | MAAHSSLYNEDRNLLRIREKERRNQEAHQEKEAFPEKAPLFPEPYKTAKGDELSSRIQTMLGDYEEMKEFLSSKSHPHRLDGSEDRPGKPRYPLGHDRGNGAASSSLRTHVYHQPIHTSAPGSRPVGNISHSPKMAQPRMEPSLHTKIYDGPRLTQDHLSQGHCSRKCDRRAEGDSAPERKLSPLISSLPSPVPPLSPVHSRLQGTSKAHSSGVSSKSCCVAKSSKDLVAKAQDKETPHDGLVAVTSLGSAPPQPPCQTFPPPPLPSKSAAMQQKPTAYVRPMDGQDQAPSESPELKLPLEDYGQQSFEKPDLKVPAKAKLTRLRMPSQSVEQPYSNEVHCVEEILKEMTHSWPPPLTAIHTPSTAEPSRFPFPTKDPLHVSPATQSQKQYDTPSKTHPNPQQGTSMLEDDLQLSDSEDSDTEQATEKPPSPPAPPSAPQTLPEPVASAHSSSGESESSESDSSSDSESESSSSDSEEEEENEPLETRAPEPEPPTTNKWQLDNWLTKVNQPSVPLDGRGSTESPQWRQESKGVAEGSSDQQHPDSKDPLPKSSSKTLRGPSEGPSLGRGAVRNPPLNRNPHLGKPWAANNPGNPPRLRPGRAQASSQAESEVGPLPYGSKEQTSKDRPKVKTKGRPRAVGSREPKPEVPAPTPQAAVPRPKPPVPTPSEKRKHKSSTAPSKAPSAPQPPKDSAGDRNPEHSALVSLTQSQGPSHSSRGSSGSVRTSGCRQAVIAQGDGCKDKLLLPLRDTKLLSPLRDSPPPTSLVVKITLDLLTRIPQPLGKGSRPRKAEDKQLSAGKKQDSETKSCDSSSRVTKKRKVTQKKSTVTRDTNWISRRASSSSSHTESSRTKAPRSSSENSRKEMLPPASASSVSSSSSSQKPSRPAQKRPRPDEDTCSQEPPRSASSTKSSSTDPPAPKHRKVQARGSEHKGSSGDAANAANPFPVPSLPNGNAKPGKPQVKSDRQQADFHMKEAKKLKCKAETMVDKAGKAFKYLEAVLSFIECGMASESESSAKSAYAVYSETIDLIRYVMSLKCFSDNTMPAQEKIFAVLCLRCQSLLNMAMFRCKKDTVMKYSRTLSEHFKSTSKVAQAPSPCTARSTGVPSPLSPMPSPASSVGSQSSAGSSMGSVGVTATVSTPVSIQNMTSSYVTITSHVLTAFSLWEQAEALTRKNKEFFAQLSTKVRVLALNSSLVDLVHYTRQGLQRLKQSPKGP | Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Belongs to the AF4 family. |
Q9UNA5 | MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEDDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGNYDEMKNLLTNHSNQNHLVGIPKNSVPQNPNNKNEPSFFPEQKNRIIPPHQDNTHPSAPMPPPSVVILNSTLIHSNRKSKPEWSRDSHNPSTVLASQASGQPNKMQTLTQDQSQAKLEDFFVYPAEQPQIGEVEESNPSAKEDSNPNSSGEDAFKEIFQSNSPEESEFAVQAPGSPLVASSLLAPSSGLSVQNFPPGLYCKTSMGQQKPTAYVRPMDGQDQAPDISPTLKPSIEFENSFGNLSFGTLLDGKPSAASSKTKLPKFTILQTSEVSLPSDPSCVEEILREMTHSWPTPLTSMHTAGHSEQSTFSIPGQESQHLTPGFTLQKWNDPTTRASTKSVSFKSMLEDDLKLSSDEDDLEPVKTLTTQCTATELYQAVEKAKPRNNPVNPPLATPQPPPAVQASGGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPMETISLPPPIIQPMEVQMKVKTNASQVPAEPKERPLLSLIREKARPRPTQKIPETKALKHKLSTTSETVSQRTIGKKQPKKVEKNTSTDEFTWPKPNITSSTPKEKESVELHDPPRGRNKATAHKPAPRKEPRPNIPLAPEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCIISGGNTAKSKEICGASLTLSTLMSSSGSNNNLSISNEEPTFSPIPVMQTEILSPLRDHENLKNLWVKIDLDLLSRVPGHSSLHAAPAKPDHKETATKPKRQTAVTAVEKPAPKGKRKHKPIEVAEKIPEKKQRLEEATTICLLPPCISPAPPHKPPNTRENNSSRRANRRKEEKLFPPPLSPLPEDPPRRRNVSGNNGPFGQDKNIAMTGQITSTKPKRTEGKFCATFKGISVNEGDTPKKASSATITVTNTAIATATVTATAIVTTTVTATATATATTTTTTTTISTITSTITTGLMDSSHLEMTSWAALPLLSSSSTNVRRPKLTFDDSVHNADYYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVAQIPSPWVSNGKNTPSPVSLNNVSPINAMGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRENKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL | RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. When splicing is inhibited, accumulates in enlarged speckles. Additional isoforms seem to exist. Brain (most abundant in hippocampus and amygdala), placenta and lung. The disease is caused by variants affecting the gene represented in this entry. It is caused either by silencing of the AFF2 gene as a consequence of a CCG expansion located upstream of this gene or by deletion within the gene. Loss of AFF2 expression is correlated with FRAXE CCG(N) expansion. Normal individuals have 6-35 copies of the repeat, whereas cytogenetically positive, developmentally delayed males have more than 200 copies and show methylation of the associated CPG island. Belongs to the AF4 family. |
B1ATW0 | MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSFGSLLDGKPSAVSSKTKLPKFTILQTSEVSLTSDPSCVEEILRESQHLTPGFTLQKWSDPSSRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTANELYQAVEKAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPTETISLPPPIIQPVEVQVKVKPNPSQAVAVPKERPLLSLIREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCITSKSKETSNASLTLSTLTNGNSNNLSTSNEETAFSPPPAMQTELLSPLRDHENPKNLWVKIDLDLLSRVPGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKNISMAGQITSSKPKRSEGKFCATFKGISINEGDAPKKAASATVTVANMALATATATATVPAIVTATVTATATTTATATTTTTTTTISSITPTITSGLMDSSHLEMTSWAALPLLSSSSANVRRPKLTFDDSVHNADFYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVTQIPSPWVGNGKNTPSPVSLNNVSPINSVGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRDNKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL | RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus. Highly expressed in the hippocampus, the piriform cortex, Purkinje cells and the cingulate gyrus. Expressed before day 7 in the embryo and reached its highest levels at 10.5-11.5 days. In the embryo at day 11, expression is more specific in the roof of the hind brain and the lateral ventricle of the brain. Belongs to the AF4 family. |
Q7YQM2 | MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEDDLFSSGFDLFGEPYKTNKGDALANRVQNTLGNYDEMKDLLTNHSNQNHLVGIPKNSVPQNPNNKNEPSFFPEQKNRIIPPHQDNTHPSAPMPPPSVVILNSTLIHSNRKSKPEWSRDSHNPSTVLASQASGQPNKMQTLTQDQSQAKLEDFFVYPAEQPQIGEAEESNPSAKEDSNPNSSGEDAFKEIFQSNSPEESEFAVQAPGSPLVASSLLAPSSGLSVQNFPPGLYCKTSMGQQKPTAYVRPMDGQDQAPDISPTLKPSIEFENSFGNLSFGTLLDGKPSAASSKTKLPKFTILQTSEVSLPSDPSCVEEILRESQHLTPGFTLQKWNDPTTRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTATELYQAVEKAKPRNNPVNPPLATPQPPPAVQASGGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPMETISLPPPIIQPMEVQMKVKTNASQVPAEPKERPLLSLIREKARPRPTQKIPETKALKHKLSTTSETVSQRTIGKKQPKKVEKNTSIDEFTWPKPNITSSTPKEKESVELHDPPRGRNKATAHKPAPRKEPRPNIPLAPEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCIISGGNTAKSKEICGASLTLSTLMSSSGSNNNLSISNEEPTFSPIPVMQTEMLSPLRDHENLKNLWVKIDLDLLSRVPGHNSLHAAPAKPDHKETATKPKRQTALTAVEKPAPKGKRKHKPTEVAEKIPEKKQRLEEATTICLLPPCISPAPPHKPPNTRENNSSRRANRRKEEKLFPPPLSPLPEDPPRRRNVSGNNGPFGQDKNIAMTGQITSTKPKRTEGKFCATFKGISVNEGDTPKKASSATITVTNTAIATATVTATAIVTTTVTATATATATTTTTTTTISTITSTITTGLMDSSHLEMTSWAALPLLSSSSTNVRRPKLTFDDSVHNADYYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVAQIPSPWVGNGKNTPSPVSLNNVSPINAMGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRENKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL | RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure (By similarity). Belongs to the AF4 family. |
Q7YQM1 | MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKTNKGDALANRVQNTLGNYDEMKDLLTNHSNQNHLVGIPKNSVPQNPNNKNEPSFFPEQKNRIIPPHQDNTHPSAPMPPPSVVILNSTLIHSNRKSKPEWSRDSHNPSTVLASQASGQPNKMQTLTQDQSQARLEDFFVYPAEQPQIGEVEESNPSAKEDSNPKSSGEDAFKEIFQSNSPEESEFAVQAPGSPLVASSLLAPSSGLSVQNFPPGLYCKTSMGQQKPTAYVRPMDGQDQAPDISPTLKPSIEFENSFGNLSFGTLLDGKPSAASSKTKLPKFTILQTSEVSLPSDPSCVEEILRESQHLTPGFTLQKWNDPTTRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTATELYQAVEKAKPRNNPVNPPLATPQPPPAVQASGGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPMETISLPPPIIQPMEVQMKVKTNASQVPAEPKERPLLSLIREKARPRPTQKIPETKALKHKLSTTSETVSQRTIGKKQPKKVEKNTSIDEFTWPKPNITSSTPKEKESVELHDPPRGRNKATAHKPAPRKEPRPNIPLAPEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCIISGGNTAKSKEICGASLTLSTLMNSSGSNNNLSISNEEPTFSPIPVMQTEMLSPLRDHENLKNLWVKIDLDLLSRVPGHNSLHAAPAKPDHKETATKPKRQTAVTAVEKPAPKGKRKHKPTEVAEKIPEKKQRLEEATTICLLPPCISPAPPHKPPNTRENNSSRRANRRKEEKLFPPPLSPLPEDPPRRRNVSGNNGPFGQDKNIAMTGQITSTKPKRNEGKFCATFKGISVNEGDTPKKASSATMTITNTAVATATVTATAIVTTTVTATATATATTTTTTTTISTITSTITTGLMDSSHLEMTSWAALPLLSSSSTNVRRPKLTFDDSVHNADYYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVAQIPSPWVGNGKNTPSPVSLNNVSPINAMGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRENKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL | RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure (By similarity). Belongs to the AF4 family. |
Q8IWJ5 | MDSFDLALLQEWDLESLCVYEPDRNALRRKERERRNQETQQDDGTFNSSYSLFSEPYKTNKGDELSNRIQNTLGNYDEMKDFLTDRSNQSHLVGVPKPGVPQTPVNKIDEHFVADSRAQNQPSSICSTTTSTPAAVPVQQSKRGTMGWQKAGHPPSDGQQRATQQGSLRTLLGDGVGRQQPRAKQVCNVEVGLQTQERPPAMAAKHSSSGHCVQNFPPSLASKPSLVQQKPTAYVRPMDGQDQAPDESPKLKSSSETSVHCTSYRGVPASKPEPARAKAKLSKFSIPKQGEESRSGETNSCVEEIIREMTWLPPLSAIQAPGKVEPTKFPFPNKDSQLVSSGHNNPKKGDAEPESPDNGTSNTSMLEDDLKLSSDEEENEQQAAQRTALRALSDSAVVQQPNCRTSVPSSKGSSSSSSSGSSSSSSDSESSSGSDSETESSSSESEGSKPPHFSSPEAEPASSNKWQLDKWLNKVNPHKPPILIQNESHGSESNQYYNPVKEDVQDCGKVPDVCQPSLREKEIKSTCKEEQRPRTANKAPGSKGVKQKSPPAAVAVAVSAAAPPPAVPCAPAENAPAPARRSAGKKPTRRTERTSAGDGANCHRPEEPAAADALGTSVVVPPEPTKTRPCGNNRASHRKELRSSVTCEKRRTRGLSRIVPKSKEFIETESSSSSSSSDSDLESEQEEYPLSKAQTVAASASSGNDQRLKEAAANGGSGPRAPVGSINARTTSDIAKELEEQFYTLVPFGRNELLSPLKDSDEIRSLWVKIDLTLLSRIPEHLPQEPGVLSAPATKDSESAPPSHTSDTPAEKALPKSKRKRKCDNEDDYREIKKSQGEKDSSSRLATSTSNTLSANHCNMNINSVAIPINKNEKMLRSPISPLSDASKHKYTSEDLTSSSRPNGNSLFTSASSSKKPKADSQLQPHGGDLTKAAHNNSENIPLHKSRPQTKPWSPGSNGHRDCKRQKLVFDDMPRSADYFMQEAKRMKHKADAMVEKFGKALNYAEAALSFIECGNAMEQGPMESKSPYTMYSETVELIRYAMRLKTHSGPNATPEDKQLAALCYRCLALLYWRMFRLKRDHAVKYSKALIDYFKNSSKAAQAPSPWGASGKSTGTPSPMSPNPSPASSVGSQGSLSNASALSPSTIVSIPQRIHQMAANHVSITNSILHSYDYWEMADNLAKENREFFNDLDLLMGPVTLHSSMEHLVQYSQQGLHWLRNSAHLS | Putative transcription activator that may function in lymphoid development and oncogenesis. Binds, in vitro, to double-stranded DNA. Preferentially expressed in lymphoid tissues, highest levels being found in the thymus. The disease is caused by variants affecting the gene represented in this entry. Belongs to the AF4 family. |
Q80WS6 | MDSFDLALLQEWDLESLWGEDILSQRNDSLVLEVQASASRCRSVYEPDRNALRRKERERRSQETQQDSGSFNSGYSLFSEPYKTNKGDELSNRIQNTLGNYDEMKDFLTDRSNQSHLVGVPKPGVPQTPVNKIDEHFGAESRAQPQPSTVCSTASSTPAAVPVQQGKRGAMGWQKAGHPPSDGQQRAAQQGSLRTLLGDGVGRQQTRAKQVCNMETGLQTQERPPAMAAKHGGSGHCVQNFPPSLASKPSLVQQKPTAYVRPMDGQDQAPDESPKLKSSTETAVHCTAYRGVPANKPESARAKAKLAKFSIPKQAEESRSGENNSCVEEIIREMTWLPPLSAIQAPAKVEPSKFPFPNKDSQLVSSGHSNPKKADAEPGSPDNGASNTSTLEDDLKLSSDDEEGEQQAAQRTALRALADSSVVQQTNCRGSAPSSKGGGSSSSSGGSSSSSDSESTSGSDSETESSSSSSESEGSKPPHCSSPEAEPASSNKWQLDKWLNKVNPHKPPILIQNESHGPERNQYYTPPVKDEGQDCGKLPEICQASLRDKELKTTCKEEQRPRTANKAPGSKSVKQKSPPAAVAVTAAALPPAVPSAPTESAPAPTRRSAGKKPTRRTERTSAGDGANCHRPEEPVAPDTLGASVVGPLEPPKTRPCGNNRTGHRKELRSSVTCEKRRTRGLSRIVPKSKEFIETESSSSSSSSDSDLESEQEEYVLSKAPTTTGSEQRLKEAASSNNNSNSNSSTSRASVGSINARTTSDIAKELEEQFYTLVPFGRNELLSPLKDSDEVRSLWVKIDLTLLSRIPEHLSQEPGVLSAPSAKDTDSAPASHALDAPAEKTLPKSKRKRKCDNEDDYREIKKVQGRKESASRLAASTNNTLSGNHCNVNVNSLAIPINKNEKMLRSPTSPLSDTCKHKYASEDLTSSSRPHGNGLLTSASSNKEPKAESQLQTIAGDLTKASHNSSENGTLHSKSRPQTEPWSPGSNGHRDCKRQKLIFDDMPRSADYFMREAKRMKHKADAMVEKFGKALNYAEAALSFIECGNAMEQGPMESKSPYTMYSETVELIRYAMRLKTHSGPNATPEDKQLAALCYRCLALLYWRMFRLKRDHAVKYSKALIDYFKNSSKAAQAPSPWGSSGKSTGSPSPMSPNPSPASSVGSQGSLSSSSGLSPSTIVSIPQRIHQMAANHVSITNSILHSYDYWEMADNLAKENREFFNDLDLLMGPVTLHSSMEHLVQYSQQGLHWLRSSVHLS | Putative transcription activator that may function in lymphoid development and oncogenesis. Highest levels found in lymphoid tissues, lower levels in brain and lung. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the AF4 family. |
Q9P0E4 | MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPKLVAIPKPTVPPSADEKSNPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRTSAGSSSGTNSSGQRHDRESYNNSGSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLNSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSTQSFPPSLMSKSNSMLQKPTAYVRPMDGQESMEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSQPLDASASGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGTGEQKRYNPSKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQGYKKEGREQGTGNSYTDTSGPKETSSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKAEKAAAEEPRGGLKIESETPVDLASSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSTSKSSQKSREIIETDTSSSDSDESESLPPSSQTPKYPESNRTPVKPSSVEEEDSFFRQRMFSPMEEKELLSPLSEPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHTREAQKQASEKVSNKGKRKHKNEDDNRASESKKPKTEDKNSAGHKPSSNRESSKQSAAKEKDLLPSPAGPVPSKDPKTEHGSRKRTISQSSSLKSSSNSNKETSGSSKNSSSTSKQKKTEGKTSSSSKEVKEKAPSSSSNCPPSAPTLDSSKPRRTKLVFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSETVDLIKYTMKLKNYLAPDATAADKRLTVLCLRCESLLYLRLFKLKKENALKYSKTLTEHLKNSYNNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGNYSSGASSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLVRYTRQGLHWLRQDAKLIS | Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. Interacts with ELL3; the interaction is direct (By similarity). Interacts with ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation. Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL. Associates to transcriptionally active chromatin but not at snRNA genes. Ubiquitously expressed. Strongly expressed in heart, placenta, skeletal muscle, pancreas and to a lower extent in brain. Expressed in fetal heart, lung, brain and to a lower extent liver. A chromosomal aberration involving AFF4 is found in acute lymphoblastic leukemia (ALL). Insertion ins(5;11)(q31;q13q23) that forms a KMT2A/MLL1-AFF4 fusion protein. The disease is caused by variants affecting the gene represented in this entry. Belongs to the AF4 family. Contaminating sequence. Potential poly-A sequence. |
Q8CCH3 | MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDYIGDRSIPKLVAIPKPAVPTTTDEKANPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSALQSGHSSQRSGAGGSGASSSGQRHDRDSYSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLSSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRGPFSSGQHSSQSFPPSLMSKSSSMLQKPTAYVRPMDGQESVEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSRPLDASVSGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGPGEQKRYSTAKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQAYKKEGREQGTASNYTDPGGTKETSSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKPEKSAAEEPRGGLKIESETPVDMAASMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSASKPSQKSREIIETDTSSSDSDGSESLPPSSQTPKYPESNRTPVKPSSVEEEDSFFRQRMFSPMEEKELLSPLSEPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHSREVQKQASEKASNKGKRKHKNDDDTRASESKKPKTEDKNSSGHKPSSSRESSKQSSTKEKDLLPSPAGPILSKDSKTEHGSRKRTVSQSSSLKSSGTSSKENSGSSSKSSSSSTAKQKKTEGKGPSSSKEAKEKAPNSSSNCPPSTPTSESSKPRRTKLAFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSDTVELIKYTMKLKNYLAPDATAADKRLTVLCLRCQSLLYLRLFKLKKENALKYSKTLTEHLKNSYSNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGSYSSGGSSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLARYTRQGLHWLRQDAKLIS | Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression (By similarity). Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation (By similarity). Interacts with ELL3; the interaction is direct. Associates to transcriptionally active chromatin but not at snRNA genes. Highly expressed in testis by Sertoli cells, and at low levels in other tissues. Expressed throughout embryogenesis with maximum expression at 10.5 and 12.5 dpc. Mice are infertile with azoospermia. Spermatogenesis is arrested at the level of spermiogenesis. Belongs to the AF4 family. |
B3MLB7 | MAQQQQQQHNHQTSNNNNNNSSILLLQQQQLHQEQLQQYNNNLYSQNYNMEEYERRKRREREKIERQQGIQIDDRETSLFGEPRRLTEADADITAALGEFGDARVYINQSTVGISRHTPGAGNPRLQAPLQPPPKSLGHSPSYTGSTGSASASANSAVPSQQQQQQHYNGTGGRFLPPAASKRSSSGAGQQPLPQEKDISKMISEMADNFRVTPLTSIAATPHAPVRENYNLNGPNKNKYMDDIISSPLSQPSSLMTPLFAPIAPIASPPQTSQLPLGGATSLTGSSEAVLGLAPLQQLPPTPPKAASAITSPAAAKPLKTEKNHTLEKQDSCLENDLELSESEDEQPKKEGRSAGNSSNSSESDSSESGSESSSKNDAQPLPNHKLHHQQQQQLQQQPLQQQQHQQQQQQQILLQQQQQQRPQQLTANGKSEKKKYKHAIIAGGSNTITGLLTSSGFGSGGNGGPGGNSCGPGSGASASAGTMSSGGSSSNKTPSPTESNKWTLSRFFPKPANQTNTESATPGNVSMKVPGILPGGAQIIPEPIEVSTAIVKNEKIHDDPMDMDDGEEDDDDEDQQQQQQQQLHYRADLSVTPVSVKKEAIDGVSELGLAAIPKNQIKRESSEALHASRLSDSGTSGSSSSSSSSSESAPGGEVVPMPGPGETLQIPGGAAITSVMRVPPTLTQKAPSSTSVTLMPILPLPMSPKQRQKKQRKKKTSTPIVNSSDEDEPAPKHPGLDYTAVSAHSQSTATAPAKKRGRPRKQQQQSGGSGNLSSASAGSSSQTKGPTLTAAKKPLCKALPAMGGARKRDHSSQSSSNGNTPTKKMATPMSVSAPPKTASVHRDSSSSDDDSSSSGGSSSKSSSSSSSSDDTEEAQNTNCRIVKLNKTGAGAVAAKVLLGSGSSSALSSGSEAEDQARSQAGSGKALAQQMPPYKPQVMSQHSQQLSSSECSSSSGDRGGTGAGSSSSGEEDEARHEKERERKPKSDKNKISTLTRIFNPKEGGAKKQGQVVIMDLQEEQQQGKLDAATQSSQIPATAPAVKPRMTPTQQLQQQHAQSQQMLGTSLASPARTTTPHLTSLICKIDLSKLSRERIMRLKKLTPAQQNGHLTPKGQAASAVQMPNGYANDAVPAAKVKPEHPVKPEPDADYEAKFKPGSVKQEFQLKQERDRDRERERERDREQPPGRRRKRSSSSSSSPYKEKKRKKEKTDQLQICKELLPSNNHERIPNHDRLSYDKLQLLHEDAAAAAAASGVGAAPNGSPRKNLLAMSPLPPPPISTAIAIVPPITCNEAVQTTPPLTTSTSPQAASAVTEPAPPAVAVPPAPVTRLIYRSYFDREEAHPSADLRRNNQFLQEAVNRKHAADAEPDSFNQVTLYLEAVVYFLLTADAMERCSSEATYTMYKDTLSLIKFISFKFRPQHSANGQTKTHMAKVAILSLRCQSLISLKLYNLRRANCRDIIASLTDFFRTGRGDIVNGNTPSSISPSNSVGSQGSGSNTPPGRIVPRDIHNQLSKQNEYLSYVHSAHELWDQADHSVRKGNHTDFFRELDHENGPLTLHSTMHEVFRYVQAGLKTLRDAVSHTAHPTQ | Has a role in transcriptional regulation. Acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth. Essential for regulation of the cytoskeleton and cell growth but not for cell proliferation or growth rate. Required specifically for the microtubule-based basal transport of lipid droplets. Plays a partially redundant function downstream of Raf in cell fate specification in the developing eye. Pair-rule protein that regulates embryonic cellularization, gastrulation and segmentation (By similarity). Belongs to the AF4 family. |
B3NAM7 | MAQQQQQQLQQQQQHHTSSINNNNNSILLLQQQQPQQQQQLDQLQQYNNNLYSQNYNMEEYERRKRREREKIERQQGIQIDDRETSLFGEPRRVTEGDAEITAALGEFFEARVYINNQTVGISRSAPGAGNPRLQPNMPPQGKSLGHSPSSASASAAAGPTSASATTALPGQQQQHYQQQQRPPTYVKQADNKPPYNGRGGYPGQPMKNDIPSSSGMAPPRGPPRSSSSNSNSSSATNNASSGGVPASTPLGPPLSTQMPNGREKSFLGPPAPALHNGTGGRFVPPAASKRPGVGQQPPPPEKDVNKIISDIANIFTVQPLTLIAATPHAPTRENYNLLAPNKQKYAMDIPSSPPSAEPSSLMTPLFAPIASPIAPLVTTPPQASQLPLGGATSGTILAGEALAPLHQLPPTPPKAASGVTSPGPGKPLKTEKNHSLEKQDSCLENDLELSESEDEQRKKEGRSAGNSSNSSESDSSESGSESSSKNDPQHHPNHQQHHHQLQQQQQQQQQQASMQQQQVLQQQQQHRPQPLTSNGAQNKKFRHEIIARGSNTITGLLSSSGFGSGGSVGPAGLNSSAAMGAGSGSGGTLSSGGSSSNKTPSPTESNKWNLSRFFHKPANQTNSENVSPGNVSMKVPGILPGGAQIIPESIDVTTAIVKNEKIHDDHMAMEDGEEEDDDEEQQLRYGGGLSVTPVAVKKEAIDAVSEMALGAIPKTQIKRESAEALLSARLSDSGTSASGSSSSSSSSSDSAVGGEVVPKLGLGEILQLPGVPAAITTVMRVQPTQSQKAPPSNSVTLTPILPLPTSPKQRQKKPRKKKAVTSAPILDSSDDDEPPPKHPGLDHTAVSVQTPPAADTVKKGRGRPRKQQQSGGSGNLSSASAGSSSQTKGPTLTAAKKPLAKTPLAMSRARKREHSSQSSSNGNTPTKKVATPQLVAAPLKPTSVTAGSSSSDEDSSSSAESSSKSSSSSSSSDDTETQNTNCRIVKLNKTGAVQKKALLGSGSSSPSSSGSEPEDQTTRSQVGSGQALAQQLPPYKQLPISQHSQHLSSSECSSSSGGCTAVCSSSSGEEDEGRREKERERKPKSDKNKISTLTRIFNPKEGGAKKQGQVVIVDLQEEQQQGKLDAAAQPPPPQAPPAAPAAIMAKPRMTPTQQQQLGAGLASPARTTTPHLTSLICKIDLSKLSRERIMRLKKLTPAQQNGHLTPKDQATNAVHVPNGYAGDTNPATKVKHEHPVKPEPELDAGYEAKFKPGNVKQEFQLKQERDRDRERERERERERDREREQPPGRRRKRSSSSSSSPYKEKKRKKEKADQLQIGKELLPVPVLLPSNNHERMPNHDRLSYDKLQLLHEDAAAVIGDVSAANGSPTKKMMVMSPLPPPPTVTVAPATCNEAVQTTPPSATTASATAPPVPATRLIYRSYFDRDVEHPSDDPRKNNQFLQEAISRKHAADLERDSFNQVTLYLEAVVYFLLTADAMERCSSEQATNTMYKDTLSLIKFISTKFRPYQQQSTTNIQHETHNKVAILSLRCQSLISLKLYKLRRKDCRAVINSLADFFRVGRGDIANGNTPSSISPSNSVGSQGSGSNTPPGRIVPPDIHNMLCKENEFLSYLNSAHELWDQADRLVRTGNHIDFIRELDHENGPLTLHSTMHEVFRYVQAGLKTLRDAVSHPTHQSQ | Has a role in transcriptional regulation. Acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth. Essential for regulation of the cytoskeleton and cell growth but not for cell proliferation or growth rate. Required specifically for the microtubule-based basal transport of lipid droplets. Plays a partially redundant function downstream of Raf in cell fate specification in the developing eye. Pair-rule protein that regulates embryonic cellularization, gastrulation and segmentation (By similarity). Belongs to the AF4 family. |
Q4WE86 | MTTFFSLTTAAAVLTLARGSNALVRPGNVGKLPALGWNTWNAFGCDIDATKIMTAANEVVNLGLKDLGYEYINIDDCWSVKSGRDASTQRIIPDPDKFPDGISGVADQIHDLGLKIGIYSSAGLTTCAGYPASLGYEDIDAQTFAEWGIDYLKYDNCGVPSNWTDTYTYCVPDPGSKATNGTCPDNKNPAPAGYDWRTSLTAERYRRMRDALVSVDRTILYSLCEWGQANVNDWGNETGNSWRTTGDITPSWPRIAAIANENSFLMNHVDFWGYPDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDSISQDHLAILSNKILLKFHQDPVIGRPAQPYKWGYNPDWTFDPAHPAEYWSGASSVLGGTLVLMLNSEDTTQRRTAVWKEVPELKDVLGRQGKRRIGFRVTDVWTGKDLGCVRDHYSVELESHDVAALVVGRAC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
A2QEJ9 | MRWLLTSSALLVPAAALVRPDGVGRTPALGWNSWNAYSCDIDADKIVTAANEVVNLGLKDLGYEYINIDDCWSVKSGRNTTTKRIIPDPDKFPNGISGVADQVHALGLKLGIYSSAGLTTCAGYPASLGYEEIDAQSFAEWGIDYLKYDNCGVPTNLTDQYTYCVPDSTDGSNYPNGTCVNLTDAAPQGYDWATSTTAKRYQRMRDALLSVNRTILYSLCDWGQADVNAWGNATGNSWRMSGDITATWSRIAEIANENSFLMNYANFWGYPDPDMLEVGNGNLTLPENRAHFALWAMMKAPLIIGTPLDSIDTSHLTILSNKPLLTFHQDAVIGRPAYPYKWGYNPDWTFDPEHPAEYWSGPTSSGEVFVLMLNSEGEVKTRSAVWEEVPELKDRGTKKNSKEKKGFKVTDAWTGKDLGCVKDKYEVKLQAHDVAVLVVGGQC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
Q9Y865 | MRWLLTSSALLVPAAALVRPDGVGLTPALGWNSWNAYSCDIDADKIVTAANEVVNLGLKDLGYEYINIDDCWSVKSGRNTTTKRIIPDPDKFPNGISGVADQVHALGLKLGIYSSAGLTTCAGYPASLGYEEIDAQSFAEWGIDYLKYDNCGVPTNLTDQYTYCVPDSTDGSNYPNGTCVNLTDAAPQGYDWATSTTAKRYQRMRDALLSVNRTILYSLCDWGQADVNAWGNATGNSWRMSGDITATWSRIAEIANENSFLMNYANFWGYPDPDMLEVGNGNLTLPENRAHFALWAMMKAPLIIGTPLDSIDTSHLTILSNKPLLTFHQDAVIGRPAYPYKWGYNPDWTFDPEHPAEYWSGPTSSGEVFVLMLNSEGEVKTRSAVWEEVPELKDRGTKKNSKEKKGFKVTDAWTGKDLGCVKDKYEVKLQAHDVAVLVVGGQC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Expression on xylan is very high, whereas elevated expression levels are also detected on galactose and xylose. Belongs to the glycosyl hydrolase 27 family. |
Q2UJ97 | MQRYISLSVSLSLLSGANALVRPDGVGRLPALGWNTWNAFGCDIDASKVLTAAEETINLGLKDAGYEYINIDDCWSVKSGRDPNTKRIIPDSAKFPDGISGVASKIHDLGLKVGIYSSAGTETCAGYPASLGYEKIDAESFAEWGIDYLKYDNCGVPTNWTDTYTHCVPDNSNGSKFPNGTCPDISNPAPTAYDWSSSNTAQRYNAMRDALLGVNRTILYSLCEWGQADVNTWGNGTGNSWRTTGDITPDWSRIVEIANENSFLMNYADFWGYPDPDMLEVGNGNLTLEENRAHFALWAAMKSPLIIGTALDSINEEHLAILKNKPLLSFHQDPVIGRPAYPYKWGYNPDWTFDPAHPAEYWSGPSSTLGGTLVLMFNSEDSAKHRTAVWSEIPELKDSAEKGSGYRVTEIWTGEDLGCVKDQYDVELQSHDIAALVVGESC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
Q1HFR2 | MIEFLALITLISRANALMRPDGVGRLPALGWSSWNAHECDINATVILTAAAQVVKLGLKDLGYEYINIDDCWSIKTHRDPTTNRMIPDADRFPDGIASVASQIHELGLKVGIYSSAGETTCAGYPASLGYEDIDAETFAEWEIDYLKYDDCGVPDNWKDPYTFCVPDTANNAGPFPNGTCPSLPNPAPANYNWSTSPSAERFRRMLDALNTQDRTILYSLCNWGNAAVNTWGAEIGNSWRMSGDISPGRGEVGPDRTRIAVWERIAEITNEMSFLVREYAEFWGWPDADMLEVGNGEGGMTVAENRAHFALWAAMRSPLLIGTKLDTIRQEHLKILKNPTLLTFHQDPIINRPAYPYKWGYNADYTFDAAHPAEYWSGPSPALEGTLVVMLNSENVTSTRMAVWSEVPELQNQDQGDAFEVMDGWTGEDLGCIKEKYEVELDAHDAAVLVVGNAC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
A1D0A3 | MTTFLSLTTAAAVLTLARGSNALVRPGNVGKLPALGWNSWNAFGCDIDAAKIMTAANEVVNLGLKDLGYEYINIDDCWSVKSGRDASTQRMVPDPEKFPDGISGLADQIHDLGLKVGIYSSAGLTTCAGYPASLGYEDIDAQTFAEWGIDYLKYDNCGVPSNWTDAYTYCVPDPGSKSTNGTCPDNKNPAPAGYDWRTSLTAERYRRMRDALVSVDRTILYSLCNWGQADVNDWGNETGNSWRTTGDITPSWPRIAAIANENSFLMNYVDFWGYPDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDSISQDHLAILSNKILLKFHQDPVVGRPAHPYKWGYNPDWTFDPAHPAEYWSGASSVLGGTLVLMLNSEDTKQRRTAVWKEIPELKDVLGRQGKRRTGFRVTDVWTGKDLGCVRDHYSVELESHDVAALVVGRAC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
O94221 | MLTSLSLTALALLPSANALVRKDGVGRLPALGWNSWNAFGCDVDSTKIMTAANEMVHLGLKDLGYEYVNIDDCWSVKNTRNSTTQRIIPDTQKFPDGISGVADQVHQLGLKIGIYSSAGETTCAGYPASLGYEKVDAEAFAEWGIDYLKYDNCGVPSNWTDQYSSCVPDGSNEPANGTCPGLSNPAPAGYDWTKSNTFTRYTMMRDALLGQTRTILYSLCDWGQADVNTWGNETGNSWRMSGDISANWARIAQIANENTFRMNYVGFWGHPDPDMLEVGNGDLTAAENRAHFALWAIMKSPLIIGTALDGISDANLAVLKNKYLIEFNQDPIIGRSAHPYKWGYNPDWTFDPAHPAEYWSGPSSTLKGTLVLMLNSENSTSTRTAVWKEIPELKGHNAYRVTDAWSGKDLGCVKKQYSASLASHDVAVLVVKEAC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
A7XZT2 | MLHRATTTAAAAAAAALLLCPVQALVRPDGVGKLPALGWNSWNAFGCDIDEEKILTAANQIVNLGLKDLGYEYVNIDDCWSVKSGRNATTGRIMPDLTKFPDGISGLAEKIHNLGLKIGIYSSAGWTTCAGYPASLGNETIDAETFAEWGIDYLKYDNCGVPPDWQDQYSYCVPDSGDPATNPNGTCPNLQNPAPAVYDWRTSKTAERYRRMRDALLGVQDKRTILFSLCDWGQADVNEWGAETGNSWRMSGDISPNWPRISTIANLNSFELNSVDFWGHNDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDKIDQDHLSILSNKYLLTFHQDPQIGRPAYPYKWGYNPDWTFDPGHPAEYWSGPTSSGDVLVLMLNTESGPANRTAVWSEVPELKGRNNNNNSSSTGFQVTDAWTGSSLGCVQGGYSVELESHDVAVLVVSGEC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
B8NWY6 | MFGSPKRAALAAASLLAIFGNGPSVMAQETSSNNAVVADGKTFALNGENVSYRFRVNETTGDLVSDHFGGSITGDLFPGFGAEALGGWVGLAGRFRREFPDHGRGDFRIPAVRIRQEAGYTVTDLQYQSYSVIPGKPALPGLPSTFGSEEDVTTLVVHLYDNYSSIAVDLSYSIFPKYDAIVRSANVTNKGTQNITVEALSSFSFDFPYEDLEMISLRGDWAREAHRQRRKVEYGLQGFGSSTGFSSHLHNPFLAIVHPSTTESQGEAWGFNLVYTGSFSVDVEKGSQGLTRALLGFNPSQLSWQLGAGETLTSPECVSVYSSDGIGGMSRSFHRLYRNHLIKSKFATSDRPPLLNSWEGLYFDYNESTIYRLAEESAALGVKLFVMDDGWFGDKYPRVSDNAGLGDWVPNPDRFPDGLTPLVEDVTKLKAGNSSTDLRFGLWVEPEMANPNSTLYHEHPDWVLHAGQYPRTLQRNQLVLNLALPEVQDYIIDEITNILNSSAISYVKWDFNRAMHETPSPSNDHEYILGMYRVFDTLTTRFPDVLWEGCASGGGRFDPGVLEYFPQIWTSDNTDALMRITIQLGTSLAYPPSAMGAHLSAVPNAQTGRTIPVKFRGHVAMMGGSFGLELDPAELQEDEKAEVPGLIALAEKVNPIILTGDMWRLRLPEESNWPAVLFISEDGNQAVLFYFQLGPNVNHATPWLRLQGLDPKATYSVDGNGSYSGATLMNMGLQYKFESDYDSKVVFLQKQ | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Homotetramer. Belongs to the glycosyl hydrolase 36 family. |
Q9UUZ4 | MIGSSHAVVALGLFTLYGHSAAAPAIGASNSQTIVTNGTSFALNGDNVSYRFHVNSSTGDLISDHFGGVVSGTIPSPVEPAVNGWVGMPGRIRREFPDQGRGDFRIPAVRIRESAGYTVSDLQYVSHEVIEGKYALPGLPATFGDAQDATTLVVHLYDNYSSVAADLSYSIFPKYDAIVRSVNVTNQGPGNITIEALASISIDFPYEDLDMVSLRGDWAREANVQRSKVQYGVQGFGSSTGYSSHLHNPFLAIVDPATTESQGEAWGFNLVYTGSFSAQVEKGSQGFTRALLGFNPDQLSWNLGPGETLTSPECVAVYSDKGLGSVSRKFHRLYRNHLMKSKFATSDRPVLLNSWEGVYFDYNQSSIETLAEESAALGVHLFVMDDGWFGDKYPRVSDNAGLGDWMPNPARFPDGLTPVVQDITNLTVNGTESTKLRFGIWVEPEMVNPNSTLYHEHPEWALHAGPYPRTERRNQLVLNLALPAVQDFIIDFMTNLLQDTGISYVKWDNNRGIHETPSPSTDHQYMLGLYRVFDTLTTRFPDVLWEGCASGGGRFDAGMLQYVPQIWTSDNTDAIDRITIQFGTSLAYPPSAMGAHLSAVPNAQTGRTVPFTFRAHVAMMGGSFGLELDPATVEGDEIVPELLALAEKVNPIILNGDLYRLRLPQDSQWPAALFVSQDGAQAVLFYFQVQPNVNHAVPWVRLQGLDPKADYTVDGDQTYSGATLMNLGLQYSFDTEYGSKVVFLERQ | Involved in galactomannan degradation. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Homotetramer. Belongs to the glycosyl hydrolase 36 family. |
Q2TW69 | MFGSPKRAALAAASLLAVFGNGPSVMAQETSSNNAVVADGKTFALNGENVSYRFRVNETTGDLVSDHFGGSITGNLFPGFGAEALGGWVGLAGRFRREFPDHGRGDFRIPAVRIRQEAGYTVTDLQYQSYSVIPGKPALPGLPSTFGSEEDVTTLVVHLYDNYSSIAVDLSYSIFPKYDAIVRSANVTNKGTQNITVEALSSFSFDFPYEDLEMISLRGDWAREAHRQRRKVEYGLQGFGSSTGFSSHLHNPFLAIVHPSTTESQGEAWGFNLVYTGSFSVDVEKGSQGLTRALLGFNPSQLSWQLGAGETLTSPECVSVYSSDGIGGMSRSFHRLYRNHLIKSKFATSDRPPLLNSWEGLYFDYNESTIYRLAEESAALGVKLFVMDDGWFGDKYPRVSDNAGLGDWVPNPDRFPDGLTPLVEDVTKLKAGNSSTDLRFGLWVEPEMANPNSTLYHEHPDWVLHAGQYPRTLQRNQLVLNLALPEVQDYIIDEITNILNSSAISYVKWDFNRAMHETPSPSNDHEYILGMYRVFDTLTTRFPDVLWEGCASGGGRFDPGVLEYFPQIWTSDNTDALMRITIQLGTSLAYPPSAMGAHLSAVPNAQTGRTIPVKFRGHVAMMGGSFGLELDPAELQEDEKAEVPGLIALAEKVNPIILTGDMWRLRLPEESNWPAVLFISEDGNQAVLFYFQLGPNVNHATPWLRLQGLDPKATYSVDGNGSYSGATLMNMGLQYKFESDYDSKVVFLQKQ | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Homotetramer. Belongs to the glycosyl hydrolase 36 family. |
Q0CVH2 | MVAFMNSATFVAGLFTLWSRPIWATPASNTNAVVVNGTAFTLNGDHVSYRFHVDDATGDLFSDHFGPRVSGNFPTEIVSQVNGWVNTIGRVRREFPDQGRGDFRIPAIRIRQTAGYTVSELLYRSHTVIPGKPALPGLPATFGSEEDVTTLVVHLYDEISEVAADLSYSIFPKYDAVVRSVNVTNQGAGNITIETLASLSVDFPYEDLDMVYLRGDWAREAHSERRKVEYGTQGFDSSAGYSSHLHNPFLAIMNPATTESQGETWGFSLVYSGSFAVNVERGSQGFTRALLGLNPGQLSWVLRPGESLVSPECVAVYSADGIGGMSRLLHRLYRNHLIKSKFAVSDRPVLLNSWEGLGFNYNETTVYQLATEAAELGVKLFVLDDGWFGDKYPRTADNAGLGDWVPNPDRFPHGLPHEVDRITALHPGNDTSTNLRFGLWFEPEMVNPNSSLYHQHPDWALHAGSYPRTLTRNQLVLNMALPEVQDYVIKSVSDILDSADISYVKWDNNRGIHETPSPSTDHQYMLGMYRVFDNLTTKYPNVLWEGCASGGGRFDPGVLQYFPQIWTSDDTDALERITIQMGTSLAYPPSAMGAHLSAVPNQQTGRTLPITFRAHVAMMGGSFGLELNPAHMPDDERDAVPGLIALAERVNPIVLTGDMYRLSPHDSQWPAVLFISPDGEQAVLFYFQTSPRVDNSIPRVKMQGLDPQAVYSVDGDAEYSGATLMNVGLQFPFDSDVGSKVVFFQRL | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Homotetramer. Belongs to the glycosyl hydrolase 36 family. |
Q1HFQ9 | MFRSTATVAAATAMGLLTATGHGSLAIAQGTTGSNAVVVDGTNFALNGASMSYVFHANSTTGDLVSDHFGATISGAIPAPKEPAVNGWVGMPGRIRREFPDQGRGDFRIPAVRIRQTAGYTVSDLQYQGHEVVDGKPALPGLPATFGEAGDVTTLVVHLYDNYSAVAADLSYSVFPEFDAVVRSVNVTNKGKGNITIENLASLSVDFPLEDLDLVSLRGDWAREANRERRRVEYGIQGFGSSTGYSSHLHNPFFALVHPSTTESQGEAWGFNLVYTGSFSAQVEKGSQGLTRALIGFNPDQLSWNLGPGETLTSPECVSVYSKDGIGGMSRKFHRLYRKHLIRSKFATSDRPPLLNSWEGVYFDFNQSSIETLAEQSAALGIRLFVMDDGWFGDKYPRTSDNAGLGDWTPNPDRFPNGLEPVVEEITNLTVNDTSAEKLRFGIWVEPEMVNPNSSLYREHPDWALHAGAYARTERRNQLVLNLALPEVQEYIIDFMTDLLNSADISYIKWDNNRGIHEAPSPSTDHEYMLGVYRVFDTLTARFPDVLWEGCASGGGRFDAGVLHYFPQIWTSDNTDGVDRVTIQFGTSLAYPPSAMGAHLSAVPNHQTGRTVPLEFRAHVAMMGGSFGLELDPATLQDDPDVPELIQMAEKVNPLVLNGDLYRLRLPEESQWPAALFVAEDGSQAVLFYFQLSPNVNHAAPWVRLQGLDPEASYTVDGDKTYTGATLMNLGLQYTFDTEYGSKVVFLERQ | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside, raffinose, locust bean gum and gum guar. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Optimum pH is 3.5. Optimum temperature is 52 degrees Celsius. Homotetramer. Belongs to the glycosyl hydrolase 36 family. |
B0YEK2 | MEFIVSLLLLSPALVAGSLHSRIDNGLARTPQMGWNSYNYYSCSPNEAIIRSNAKALVDLGLAELGYRYVTTDCGWSVADRLPNGTLTWNETLFPSGFPAMGEYLHELGLLFGVYGDSGTKLCGSPPDQVGSLYHEEQDAKTFAEWGADSLKYDNCYSDAATNYPNVNYEPSTSPRPRYEIMSSALARVGRPILFQICEWGIDFPALWAPALGNSWRIGNDIIPAWRSIFRTLNQAVPNTDFAGPGQWADLDMLYVGNGVFSLPEEQTHFSLWAILKSPLTIGAALKDDDTSISQASLEVLKQKDVIGFNQDALGVSASLKRRWSDEGYEVWSGPLSGNRTVVAVINWRNESRDLTLDLPDVGLQYAQVARNIWGKTVVRDVRTSYTAGVAGHGTILLELQGTLPSGLYPAKIFAKSTGQRSTFESIYAATTSANYELAITFSRPSTETVTITTSSGQTVSISGKSGRIALTAGSNTITIQHKTPIESIQITPPTGTYYANTVFNVTGSAKHTTCGSGCSPVGSKIGYLSPTSNAYTSISTTTAGSKYLAIDYINNEVAFSSSWGWGSNSRNLTVSVNDGAPVRLEVPLSGRHSELYSPGKGWWDTATLGVLTSGWKKGENKVVFGNEGGEDGFQTYAADFVGVRVLD | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
B8N7Z0 | MLPKIFYLSLLPAALGHPHLQPRLDNGLARTPQMGWNTYNHYSCSPNETIVRSNAQALVDLGLASLGYRYVTTDCGWTVADRLSDGSLTWNETLFPEGFPALGKYLHDLDLLFGVYQDSGIKLCGSPPDNVGNYEDQDARTFASWEVDSLKYDNCYSDAATGYPNVNYEPSTSPQPRFANMSRALAAQNRSMVFQVCEWGIDFPARWAPALGHSWRIGNDIIPHWRAIYRTLNQAVPQTSFAGPGQWPDLDMLFVGNDILSIPEEQTHFSLWAILKSPLTIGAALKDDETSINDESLQILKQADIIGYNQDSLGVSASLRRRWTEEGYEVWSGPLSGGRTVAALINWRNESRDLTLDLPDIGLQYAGTVKNIWDGTTAQNVKTSYTAKVQGHGTILLELQDTTASGQYPGDTFATSTGSSTTFESIYGVTTSFRYNITVKLSEASSSSDVKIQSTASNKTITAQVSASGTEASAQIPLLAGSSNSITIVSPQSVDAITITPPNGTYFPNTAFTTIGDADTVSCGAGYCQPVGSKIGNISTNGTARAVIPATAGTKYLAIDYINNDVAFDSAWDWGSNSRNLTVSVNGNKPVRIEVPLSGQHSELFGPGKGWWDTATIGVLTEGWKDGDNDVVIGNEGGESGFTSYGPDFVGLRVL | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
A4DA70 | MEFIVSLLLLSPALVAGSLHSRIDNGLARTPQMGWNSYNYYSCSPNEAIIRSNAKALVDLGLAELGYRYVTTDCGWSVADRLPNGTLTWNETLFPSGFPAMGEYLHELGLLFGVYGDSGTKLCGSPPDQVGSLYHEEQDAKTFAEWGADSLKYDNCYSDAATNYPNVNYEPSTSPRPRYEIMSSALARVGRPILFQICEWGIDFPALWAPALGNSWRIGNDIIPAWRSIFRTLNQAVPNTDFAGPGQWADLDMLYVGNGVFSLPEEQTHFSLWAILKSPLTIGAALKDDDTSISQASLEVLKQKDVIGFNQDALGVSASLKRRWSDEGYEVWSGPLSGNRTVVAVINWRNESRDLTLDLPDVGLQYAQVARNIWGKTVVRDVRTSYTAGVAGHGTILLELQGTLPSGLYPAKIFAKSTGQRSTFESIYAATTSANYELAITFSRPSTETVTITTSSGQTVSISGKSGRIALTAGSNTITIQHKTPIESIQITPPTGTYYANTVFNVTGSAKHTTCGSGCSPVGSKIGYLSPTSNAYTSISTTTAGSKYLAIDYINNEVAFSSSWGWGSNSRNLTVSVNDGAPVRLEVPLSGRHSELYSPGKGWWDTATLGVLTSGWKKGENKVVFGNEGGEDGFQTYAADFVGVRVLD | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
A2R2S6 | MLLHFILYAALSSVVTSVSLQPRLQDGLALTPQMGWNTYNHYSCSPNETIVQSNAQALVDLGLSSLGYRYVTTDCGWTVADRLPDGSLTWNDTLFPQGFPAMGDFLHDLGLLFGVYQDSGILLCGSPPNETGSLYHEEQDARTFASWNVDSLKYDNCYSDAATGYPNVNYAPSTSPEPRFANMSHALLQQNRTILFQICEWGISFPANWAPALGHSWRIGNDIIPDWRTIFRIINQAAPQTDVAGPGQWPDLDMLEVGNNIFSLPEEQTHFSLWAILKSPLIIGAALKDELTAINDASLAVLKQKDVIAFNQDALGKSASLRRRWTEEGYEVWSGPLSNGRTVAAVINWHNESKDLTLDLPDVGLQHAGTVKNIWDGTTARDVLTSYTATVAGHGTMLLELQNTTAVGVYPRGVFGVSSGQTTTFQNIYAVTTSAKYIISVYFSQPASSTETITIGSNANQSMISAQVPASSTLVSAEIPLTAGSSNTITINTSIPIDAIHVTPPNGTYYPCTNFTLAGSTTLTTCGSGYCQPVGSKVGYISPSGTAKATISATTSGSKYLEIDWINNDIAFDSSWGWGSNSRNLTVTVNSEDPVRIEVPLSGRHSELFGPGLGWWDTSTLGLLTSGWKEGLNEVVVGNVGGDEGFQSYGADFVGIRVLD | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
Q2UI87 | MLPKIFYLSLLPAALGHPHLQPRLDNGLARTPQMGWNTYNHYSCSPNETIVRSNAQALVDLGLASLGYRYVTTDCGWTVADRLSDGSLTWNETLFPKGFPALGKYLHDLDLLFGVYQDSGIKLCGSPPDNVGSLYHEDQDARTFASWEVDSLKYDNCYSDAATGYPNVNYEPSTSPQPRFANMSRALAAQNRSMVFQVCEWGIDFPARWAPALGHSWRIGNDIIPHWRAIYRTLNQAVPQTSFAGPGQWPDLDMLFVGNDILSIPEEQTHFSLWAILKSPLTIGAALKDDNTSINDESLQILKQEEVIGYNQDSLGVSASLRRRWTEEGYEVWSGPLSGGRTVAALINWKDEARELTLDLPDIGLQFAGTVKNIWDGTTAQNVKTSYTAKVQSHGTILLELQDTTASGQYPTDTFATSTDSSTTFESIYGVTTSFRYNITVKLSEASSSGDVNIQSTASNKTITAQVSASGTEASAQIPLLAGSSNSITIVSPQSVDAITITPPNGTYFPNTAFTTTGDADTVSCGAGYCQPVGSKIGNISTNGTARAVIPATAGTKYLAIDYINNDVAFDSAWDWGSNSRNLTVSVNGNKPVRIEVPLSGQHSELFGPGKGWWDTATIGVLTEGWKDGDNDVVIGNEGGESGFTSYGPDFVGLRVL | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
Q0CVX4 | MASVIALSLLLPAAFAADHSPLRARLQDGLARTPQMGWNTYNHYNCYPDEEIFRSNAKALVDFGLADLGYRYATIDCGWTLTERLANGSLTWNATRFPSGFPAIADYLHDLGLLFGVYGDAGIKLCGPSDEHEEQDAQTFAAWGADSLKYDNCFSEASLGYPNVEYAPSSPLKPRYEVMSNALQKLDRPILFQICEWGIDFPALWAPALGHSWRIGNDIIPAWRSVFRTLNQAVPQTDFAGPGQWPDLDMLMVGNGVYSVPEEETHFSLWAILKSPLIIGSALKDATTEINSESLRILKQKAVIGYNQDKLGVSASLRRRWTDQGYEVWSGPLSNGRTVAAVINWRGEARDLTLDLPDIGLQSAGLVKNIWAGSTSRNVQTSYTARVEGHGTMLLELRDTVPAGVYPKKIFGSSRGQGTVFKSVYAGSTSENYTLAINFAKTIPSASKITVQVGANRQKLSIAVPPSRQQVTATIPLVAGSNNTITISHSHPITAIQVTSPNGTYYPATQFSLTGAARHETCGEGFCQPVGSKVSYLSPNSTARGVIPASAGTKYVEIDYINNEVAFSSSWGWGANSRNLTISLNGGEPVRLEVPLSGRHSELFGPGKGWWDTATLGVSVDGWKEGDNEVVVGNVNGEKGFQPYAADFVGLRVFD | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Belongs to the glycosyl hydrolase 27 family. |
Q1HFR9 | MRALVPMVVAATALASPAPALKPRLDDGLARTPQMGWNTYNQYNCFPNESIVHENAQALVDTGLADLGYRYVTIDCGWGVEDRLPNGTITWNPELFPQGFPAMGQYLHDLGLLFGVYGDSGILLCGSPPNITGSLYYEDIDARTFAEWGADSLKYDNCYSDAATNYPNVNYAPSTSPHPRFANMSRYIQAQDRDILFQVCEWGIDFPALWAPEIGHSWRIGNDIIPHWRSIFRTLNQAVPQTDFAGPGQWPDLDMLLVGLDGVLTVPEEQTHFSLWSILKSPLTIGAAIPGMRAESLEILSNADVIAFNQDALGVSAALRRRWSDEGYEVWSGPLEGGRTIAAVINWRDEDREITLDLPDIGLQYAETLQNVWADETVNGVKTSYSSVVEAHGVMLVQLAETVEEGVYPADVFAATNRDVTTFSDVYAITSSPNFVLNITLTEVTAAATNITIITDSSRRPISTSIPAGSSSISTSVSLIAGSNNTITIRNAPPLSSITLSPPEPTYYTGAQDFTLTSPAGAYTCPDAYCLPAGSKIVDLSTESAATAHINSSTSGSKYLEIDYINNEVAFDSSWGWGANSRNLTIKVNDNNPVRLEVPLSGRHSELFGPGLGWWDSGRLGVLTDGWIKGTNELVLSNEGGEGGFTKYAPDVVGIAVYD | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside but not on raffinose, locust bean gum and gum guar. Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Optimum pH is 5.0. Optimum temperature is 52 degrees Celsius. Belongs to the glycosyl hydrolase 27 family. |
P33889 | AYPGSHISGPNGFXMDVK | Lectin that binds galactose, galactose-containing sugars and gentiobiose. It is strongly mitogenic for human T-lymphocytes and induces the release of interleukin-1 beta and tumor necrosis factor alpha from cultured mononuclear cells. It has a strong hemagglutininating activity. Homodimer. The production of this lecting varies with seasons being higher in late spring. N-glycosylated. An isoform with Ala-1 missing is found in 20% of the samples. |
P15312 | MKMMSTRALALGAAAVLAFAAATAHAQRCGEQGSNMECPNNLCCSQYGYCGMGGDYCGKGCQNGACYTSKRCGTQAGGKTCPNNHCCSQWGYCGFGAEYCGAGCQGGPCRADIKCGSQAGGKLCPNNLCCSQWGYCGLGSEFCGEGCQGGACSTDKPCGKAAGGKVCTNNYCCSKWGSCGIGPGYCGAGCQSGGCDGVFAEAIAANSTLVAE | Carbohydrate binding. In roots. Localized to the coleorhiza, outer cell layers of the radicles, and the root caps of the developing embryo. Later found in the root tip and root cap. |
Q9XFF4 | MTMTSTTTKAMAMAAAVLAAAAVAATNAQTCGKQNDGMICPHNLCCSQFGYCGLGRDYCGTGCQSGACCSSQRCGSQGGGATCSNNQCCSQYGYCGFGSEYCGSGCQNGPCRADIKCGRNANGELCPNNMCCSQWGYCGLGSEFCGNGCQSGACCPEKRCGKQAGGDKCPNNFCCSAGGYCGLGGNYCGSGCQSGGCYKGGDGMAAILANNQSVSFEGIIESVAELV | N-acetyl-D-glucosamine binding lectin. Confined to root caps, several cell layers at the periphery of the coleorhiza and radicle, and in all cell layers of the coleoptile. |
Q9SYR1 | MMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSEPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNYGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNANSAANRIPNKGVIGNIISRAFGHDDFAVRSSSIGFYKRYCDMLGVSYGHDLKYWFDNTPSSEFQRIQMRVAA | Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties. Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Monomer and homodimer. Zinc favors dimerization. Active in the monomeric form but probably inactive in the dimeric form. The interaction with glycans on the mammalian TCR and MHC molecules of the T-cell and antigen-presenting cell, respectively, is inhibited by oligomers of GlcNAc. Rhizomes and inflorescence with immature seeds. Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains. |
Q1LX48 | MARVVKVFRTLRNHWKKSTFAVCVLSYGGHWLYGNHCDSVLRREACIEARAFGQQLIGPQEILKKATVILNPAACKGKANQLFEKNAAPILHLAGVEVKIVKTDYEGQAKKLMELMEQTDMLIIAGGDGTLQEVITGLLRRADEEIFSKTPIGFIPLGSSNSLSQSLHLVSDNKVQHITSATLSILKGETVPLDVLQIKGEKEQPVFALLGLRWGAFRDVATSISKYWYLGPLKTRAAHWFSSLKQWPQVHVASLSYLAPVPRPPDLPDEIPQRPNLLYRIYRRLQNYWNPPLEEPPKEPEPEQWESKDVSTLELTVLTHNKNPVKRRVDDSMLISLDPESLTAGQFITEGTNKSVDPMEPIENAVQIEASAARLELPEEGAGFYDIDNQEYEAMSVEVRLLPRKLRFFCSAERREQLAEAQ | Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (By similarity). Phosphorylates ceramide but not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex. Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. Belongs to the AGK family. |
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