Biological Process
stringlengths 7
1.01k
| Cellular Component
stringlengths 6
867
| Molecular Function
stringlengths 11
871
| Organism
stringlengths 8
73
| Keywords
stringlengths 1
810
| Sequence 10
stringlengths 5
10
| Sequence
stringlengths 5
1.02k
| Combined
stringlengths 136
3.91k
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adhesion of symbiont to host endothelial cell adhesion of symbiont to host epithelial cell entry into host
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plasma membrane; side of membrane
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host cell surface receptor binding
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Rhizopus delemar
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Cell membrane Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal Virulence
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MKLSIISAAF
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MKLSIISAAFLVAITHAASIKFNVIAPNATDVKVSVNGQQVTLTASDANVPYFTGSAEVGASKTYKYVAGGTEESFDRSLDGITNSTLNDFYNRPVTYANLPQLPWPIEKDPQWTRSGSKADIFDDNYIPSVFFHGDDSQVQNVVKNVPADRISGTLTFIGSNYVYSFQNVSFGIHGAGKKHNNAKQSWNWILSGSDTMGNRNFFKLRHMEEDPTQIRERLYSDILHAMGTYANDATMVRLFINNQGFGTFNMLDDITQFSYINAKFYNGKPPATLGPLYDGASGADFLYHPGNLDGYSSWVANTANPNGEAYEALDPLCKAWNETTYTDNTAIANFEKMFDLDRFMRFMVIEYLTADWDGYWMGQTNDGAYRDPTDNNKWYFLDQDFDGTFGVNLAAPEGNAFLDVSYKDFPSRYPGAVMINNLLQNADKKATFEKYLTETVRVLFNNVTLTNRVLALHNFLLPDLEWDRSIVQQSPGINFGWTFDQVTQNLWQGVTAPNNNGGGAAFGLVEYIAAKAQAVAKEFNISIVSQPVGPPSANGTTAAAPAPAAGNSTGKGGNQSISSSASSNKTSAQSTSGASRSKTAPIVLAISALALLVF
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adhesion of symbiont to host endothelial cell adhesion of symbiont to host epithelial cell entry into host plasma membrane; side of membrane host cell surface receptor binding Rhizopus delemar Cell membrane Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal Virulence MKLSIISAAF MKLSIISAAFLVAITHAASIKFNVIAPNATDVKVSVNGQQVTLTASDANVPYFTGSAEVGASKTYKYVAGGTEESFDRSLDGITNSTLNDFYNRPVTYANLPQLPWPIEKDPQWTRSGSKADIFDDNYIPSVFFHGDDSQVQNVVKNVPADRISGTLTFIGSNYVYSFQNVSFGIHGAGKKHNNAKQSWNWILSGSDTMGNRNFFKLRHMEEDPTQIRERLYSDILHAMGTYANDATMVRLFINNQGFGTFNMLDDITQFSYINAKFYNGKPPATLGPLYDGASGADFLYHPGNLDGYSSWVANTANPNGEAYEALDPLCKAWNETTYTDNTAIANFEKMFDLDRFMRFMVIEYLTADWDGYWMGQTNDGAYRDPTDNNKWYFLDQDFDGTFGVNLAAPEGNAFLDVSYKDFPSRYPGAVMINNLLQNADKKATFEKYLTETVRVLFNNVTLTNRVLALHNFLLPDLEWDRSIVQQSPGINFGWTFDQVTQNLWQGVTAPNNNGGGAAFGLVEYIAAKAQAVAKEFNISIVSQPVGPPSANGTTAAAPAPAAGNSTGKGGNQSISSSASSNKTSAQSTSGASRSKTAPIVLAISALALLVF
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cold acclimation negative regulation of vernalization response positive regulation of transcription by RNA polymerase II positive regulation of vernalization response regulation of photoperiodism, flowering regulation of transcription by RNA polymerase II vernalization response
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nucleus
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DNA-binding transcription factor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding
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Brachypodium distachyon
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Coiled coil DNA-binding Nucleus Reference proteome Transcription Transcription regulation
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MGRGKVQLKR
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MGRGKVQLKRIENKINRQVTFSKRRSGLLKKAHEISVLCDAEVALIIFSTKGKLYEFATDSCMDKILERYERYSYAEKVLVSTESEIQGNWCHEYRKLKAKVETIQKCQKHLMGEDLESLNLKELQQLEQQLESSLKHIRSRKNQLMHESISELQRKERSLQEENKALQKELVEKQKAHTQQAQWEQTHPQTSSSSSSMQREAPPTTNISNRPAAAGERTEEAAGQAQARVGLPPWMVSHISG
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cold acclimation negative regulation of vernalization response positive regulation of transcription by RNA polymerase II positive regulation of vernalization response regulation of photoperiodism, flowering regulation of transcription by RNA polymerase II vernalization response nucleus DNA-binding transcription factor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding Brachypodium distachyon Coiled coil DNA-binding Nucleus Reference proteome Transcription Transcription regulation MGRGKVQLKR MGRGKVQLKRIENKINRQVTFSKRRSGLLKKAHEISVLCDAEVALIIFSTKGKLYEFATDSCMDKILERYERYSYAEKVLVSTESEIQGNWCHEYRKLKAKVETIQKCQKHLMGEDLESLNLKELQQLEQQLESSLKHIRSRKNQLMHESISELQRKERSLQEENKALQKELVEKQKAHTQQAQWEQTHPQTSSSSSSMQREAPPTTNISNRPAAAGERTEEAAGQAQARVGLPPWMVSHISG
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brassinosteroid biosynthetic process brassinosteroid homeostasis microtubule bundle formation skotomorphogenesis sterol metabolic process
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membrane
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heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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Brachypodium distachyon
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Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix
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MVLAVLIGVL
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MVLAVLIGVLVGIVLVSSLLLRWNEVRYSRKQGLPPGTMGWPLFGETTEFLKQGPSFMKARRLRYGSLFRTHILGCPTVVCMDPELNRQMLQQGEGRGFVPGYPQSMLDILGRNNIAAVHGPLHRAMRGSMLALVRPASIRSSLLPKIDAFMRSHLHGWAGDLVDIQDKTKEMALLSALRQIAGITAGPLSDALKTELYTLVLGTISLPINLPGTSYYQGFQARKKLVSMLEKMIAERRSSGLVHNDMLDALLSGNDGTRERLSDEQIIDLIITLIYSGYETMSTTSMMAVKYLSDHPKALEELRKEHFDIRKGKSPEEAIDYNDFKSMTFTRAVIFETLRLATVVNGLLRKTTQDVEMNGYVIPKGWRIYVYTREINYDPCLYPDPMTFNPWRWLEKNMESHPHFMLFGGGGRMCPGKEVGTAEIATFLHYFVTRYRWEEEGTNTILKFPRVEAPNGLHIRVQNY
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brassinosteroid biosynthetic process brassinosteroid homeostasis microtubule bundle formation skotomorphogenesis sterol metabolic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Brachypodium distachyon Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix MVLAVLIGVL MVLAVLIGVLVGIVLVSSLLLRWNEVRYSRKQGLPPGTMGWPLFGETTEFLKQGPSFMKARRLRYGSLFRTHILGCPTVVCMDPELNRQMLQQGEGRGFVPGYPQSMLDILGRNNIAAVHGPLHRAMRGSMLALVRPASIRSSLLPKIDAFMRSHLHGWAGDLVDIQDKTKEMALLSALRQIAGITAGPLSDALKTELYTLVLGTISLPINLPGTSYYQGFQARKKLVSMLEKMIAERRSSGLVHNDMLDALLSGNDGTRERLSDEQIIDLIITLIYSGYETMSTTSMMAVKYLSDHPKALEELRKEHFDIRKGKSPEEAIDYNDFKSMTFTRAVIFETLRLATVVNGLLRKTTQDVEMNGYVIPKGWRIYVYTREINYDPCLYPDPMTFNPWRWLEKNMESHPHFMLFGGGGRMCPGKEVGTAEIATFLHYFVTRYRWEEEGTNTILKFPRVEAPNGLHIRVQNY
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brassinosteroid biosynthetic process brassinosteroid homeostasis jasmonic acid mediated signaling pathway leaf shaping response to brassinosteroid sterol metabolic process unidimensional cell growth
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endoplasmic reticulum; membrane
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fatty acid alpha-hydroxylase activity heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen steroid 22-alpha hydroxylase activity
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Brachypodium distachyon
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Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix
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MAAMMASITS
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MAAMMASITSELLFFLPYILLALLTFYTTTVAKCHRWRRTEEKRRCPNLPPGAIGWPFIGETFGYLRAHPATSVGRFMEEHIARYGKIYRSSLFGDRTVVSADAGLNRYILQNEGKLFECSYPRSIGGILGKWSMLVLVGDPHREMRAISLNFLSSLRLRAVLLPEVERHTLLVLRHWPSASPAVFSAQHEAKKFTFNLMAKNIMSMDPGEEETERLRLEYITFMKGVVSAPLNFPGTAYWKALKSRATILGVIERKMEDRLQKMNKEDSSIEEDDLLGWAMKQSNLSKEQILDLLLSLLFAGHETSSMALALAIFFLEGCPKAVQELREEHLEIARRQRLRGECKLSWEDYKDMVFTQCVINETLRLGNVVRFLHRKVIRDVHYKGYDIPSGWKILPVLAAVHLDSSLYEDPSRFNPWRWKGNASGVAQSGNFMPYGGGTRLCAGSELAKLEMAIFLHHLVLNFRWELAEPDQAFVYPFVDFPKGLPIRVHRIAQEEEKSVLTVDI
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brassinosteroid biosynthetic process brassinosteroid homeostasis jasmonic acid mediated signaling pathway leaf shaping response to brassinosteroid sterol metabolic process unidimensional cell growth endoplasmic reticulum; membrane fatty acid alpha-hydroxylase activity heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen steroid 22-alpha hydroxylase activity Brachypodium distachyon Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix MAAMMASITS MAAMMASITSELLFFLPYILLALLTFYTTTVAKCHRWRRTEEKRRCPNLPPGAIGWPFIGETFGYLRAHPATSVGRFMEEHIARYGKIYRSSLFGDRTVVSADAGLNRYILQNEGKLFECSYPRSIGGILGKWSMLVLVGDPHREMRAISLNFLSSLRLRAVLLPEVERHTLLVLRHWPSASPAVFSAQHEAKKFTFNLMAKNIMSMDPGEEETERLRLEYITFMKGVVSAPLNFPGTAYWKALKSRATILGVIERKMEDRLQKMNKEDSSIEEDDLLGWAMKQSNLSKEQILDLLLSLLFAGHETSSMALALAIFFLEGCPKAVQELREEHLEIARRQRLRGECKLSWEDYKDMVFTQCVINETLRLGNVVRFLHRKVIRDVHYKGYDIPSGWKILPVLAAVHLDSSLYEDPSRFNPWRWKGNASGVAQSGNFMPYGGGTRLCAGSELAKLEMAIFLHHLVLNFRWELAEPDQAFVYPFVDFPKGLPIRVHRIAQEEEKSVLTVDI
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defense response proteolysis
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apoplast
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aspartic-type endopeptidase activity
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Glycine max
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Apoplast Aspartyl protease Glycoprotein Hydrolase Plant defense Protease Reference proteome Secreted Signal
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MPPPLPSLCN
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MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK
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defense response proteolysis apoplast aspartic-type endopeptidase activity Glycine max Apoplast Aspartyl protease Glycoprotein Hydrolase Plant defense Protease Reference proteome Secreted Signal MPPPLPSLCN MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK
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lipid metabolic process triglyceride biosynthetic process
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cytoplasm
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diacylglycerol O-acyltransferase activity iron-sulfur cluster binding metal ion binding
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Glycine max
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Alternative splicing Cytoplasm Iron Iron-sulfur Metal-binding Reference proteome Transferase
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MEISGTVLRQ
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MEISGTVLRQVSYVSGYGTHTRSRGLAPRFGVRMGMGSGFCDEGHLRYYQDTKKVLTPKKKLKLLKGFSKLGLASDPEKLAMFYDLQQNLTSDAGDVLLRELEAARAKEKEVKKKRKQEKKAKLKAAKMNCESSSSSSSESSDSDCGCDQVVDMNTFRAGVGVGVGVGVGVVAPAPVEESPLPKTAPIVEDANAHCVAMELCSKNDIYVSSASNGFKNESAVVTSAPQKRIEVCMGNKCKRSGAAALMQEFEKVVGVEGVAVVACKCMGKCKTAPNVKVQNSVDHNSLAQGLDDSVKIPANPLCIGVGLEDVDAIVARYFWESHTDIGMAGAGAATAT
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lipid metabolic process triglyceride biosynthetic process cytoplasm diacylglycerol O-acyltransferase activity iron-sulfur cluster binding metal ion binding Glycine max Alternative splicing Cytoplasm Iron Iron-sulfur Metal-binding Reference proteome Transferase MEISGTVLRQ MEISGTVLRQVSYVSGYGTHTRSRGLAPRFGVRMGMGSGFCDEGHLRYYQDTKKVLTPKKKLKLLKGFSKLGLASDPEKLAMFYDLQQNLTSDAGDVLLRELEAARAKEKEVKKKRKQEKKAKLKAAKMNCESSSSSSSESSDSDCGCDQVVDMNTFRAGVGVGVGVGVGVVAPAPVEESPLPKTAPIVEDANAHCVAMELCSKNDIYVSSASNGFKNESAVVTSAPQKRIEVCMGNKCKRSGAAALMQEFEKVVGVEGVAVVACKCMGKCKTAPNVKVQNSVDHNSLAQGLDDSVKIPANPLCIGVGLEDVDAIVARYFWESHTDIGMAGAGAATAT
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effector-mediated suppression of host innate immune response
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cell septum; cytoplasm; external side of plasma membrane; extracellular region
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metal ion binding
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Gibberella zeae
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Cell membrane Cytoplasm Disulfide bond Glycoprotein GPI-anchor Heme Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal
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MKLSVFTSVL
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MKLSVFTSVLLAGLVAAQQEKLPKCAQPCVDQYTTGGGVAGCGQLDIKCICSNKNFLSGIACCLEKECDAQGKETAVKYAKQICATAGVTDLPDDVTCDKSAASSGTASGTATGATTPTSSDSTNTASATGGSSTVEPNAGAREGAAGFIGVGMAMLLAL
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effector-mediated suppression of host innate immune response cell septum; cytoplasm; external side of plasma membrane; extracellular region metal ion binding Gibberella zeae Cell membrane Cytoplasm Disulfide bond Glycoprotein GPI-anchor Heme Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal MKLSVFTSVL MKLSVFTSVLLAGLVAAQQEKLPKCAQPCVDQYTTGGGVAGCGQLDIKCICSNKNFLSGIACCLEKECDAQGKETAVKYAKQICATAGVTDLPDDVTCDKSAASSGTASGTATGATTPTSSDSTNTASATGGSSTVEPNAGAREGAAGFIGVGMAMLLAL
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sterol biosynthetic process
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endoplasmic reticulum membrane
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heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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Gibberella zeae
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Endoplasmic reticulum Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix
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MGLLQELAGH
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MGLLQELAGHPLAQQFQELPLGQQVGIGFAVFLVLSVVLNVLNQLLFRNPNEPPMVFHWFPFVGSTITYGMDPPTFFRENRAKHGDVFTFILLGKKTTVAVGPAGNDFILNGKLKDVCAEEIYTVLTTPVFGKDVVYDCPNAKLMEQKKFMKIALTTEAFRSYVPIISSEVRDYFKRSPDFKGKSGIADIPKKMAEITIFTASHALQGSAIRSKFDESLAALYHDLDMGFTPINFMLHWAPLPWNRKRDHAQRTVAKIYMDTIKERRAKGNNESEHDMMKHLMNSTYKNGIRVPDHEVAHMMIALLMAGQHSSSSTSSWIMLRLAQYPHIMEELYQEQVKNLGADLPPLTYEDLAKLPLNQAIVKETLRLHAPIHSIMRAVKSPMPVPGTKYVIPTSHTLLAAPGVSATDSAFFPNPDEWDPHRWEADSPNFPRMASKGEDEEKIDYGYGLVSKGSASPYLPFGAGRHRCIGEHFANAQLQTIVAEVVREFKFRNVDGGHTLIDTDYASLFSRPLEPANIHWERRQ
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sterol biosynthetic process endoplasmic reticulum membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Gibberella zeae Endoplasmic reticulum Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix MGLLQELAGH MGLLQELAGHPLAQQFQELPLGQQVGIGFAVFLVLSVVLNVLNQLLFRNPNEPPMVFHWFPFVGSTITYGMDPPTFFRENRAKHGDVFTFILLGKKTTVAVGPAGNDFILNGKLKDVCAEEIYTVLTTPVFGKDVVYDCPNAKLMEQKKFMKIALTTEAFRSYVPIISSEVRDYFKRSPDFKGKSGIADIPKKMAEITIFTASHALQGSAIRSKFDESLAALYHDLDMGFTPINFMLHWAPLPWNRKRDHAQRTVAKIYMDTIKERRAKGNNESEHDMMKHLMNSTYKNGIRVPDHEVAHMMIALLMAGQHSSSSTSSWIMLRLAQYPHIMEELYQEQVKNLGADLPPLTYEDLAKLPLNQAIVKETLRLHAPIHSIMRAVKSPMPVPGTKYVIPTSHTLLAAPGVSATDSAFFPNPDEWDPHRWEADSPNFPRMASKGEDEEKIDYGYGLVSKGSASPYLPFGAGRHRCIGEHFANAQLQTIVAEVVREFKFRNVDGGHTLIDTDYASLFSRPLEPANIHWERRQ
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effector-mediated suppression of host innate immune response
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cell septum; cytoplasm; external side of plasma membrane; extracellular region; fungal-type cell wall
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metal ion binding
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Gibberella zeae
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Cell membrane Cell wall Cytoplasm Disulfide bond Glycoprotein GPI-anchor Heme Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal
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MKYSVAFVAL
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MKYSVAFVALAAVAAQAQSLADVPKCAIPCLDKAIASETSCDKTDLACVCKGFSAVRSKATSCVIDECGTDVAINEVLPATENLCKNPPKESEAKSTAEEEKPTTTAAATSTLVVVTTSAEVVETTAAATTTVAPIIPTTAAEEPATSTPAAATPTKGPEQANGAAGLKGLGALAMAAFAALAL
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effector-mediated suppression of host innate immune response cell septum; cytoplasm; external side of plasma membrane; extracellular region; fungal-type cell wall metal ion binding Gibberella zeae Cell membrane Cell wall Cytoplasm Disulfide bond Glycoprotein GPI-anchor Heme Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal MKYSVAFVAL MKYSVAFVALAAVAAQAQSLADVPKCAIPCLDKAIASETSCDKTDLACVCKGFSAVRSKATSCVIDECGTDVAINEVLPATENLCKNPPKESEAKSTAEEEKPTTTAAATSTLVVVTTSAEVVETTAAATTTVAPIIPTTAAEEPATSTPAAATPTKGPEQANGAAGLKGLGALAMAAFAALAL
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xylan catabolic process
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extracellular region
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endo-1,4-beta-xylanase activity
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Gibberella zeae
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Carbohydrate metabolism Glycosidase Hydrolase Polysaccharide degradation Reference proteome Secreted Signal Virulence Xylan degradation
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MVSFTYLLAA
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MVSFTYLLAAVSAVTGAVAAPNPTKVDAQPPSGLLEKRTSPTTGVNNGFYFSFWTDTPSAVTYTNGNGGQFSMNWNGNRGNHVGGKGWNPGAARTIKYSGDYRPNGNSYLAVYGWTRNPLVEYYIVENFGTYNPSSGAQKKGEINIDGSIYDIAVSTRNCAPSIEGDCKTFQQYWSVRRNKRSSGSVNTGAHFNAWAQAGLRLGSHDYQILAVEGYQSSGQATMTVSG
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xylan catabolic process extracellular region endo-1,4-beta-xylanase activity Gibberella zeae Carbohydrate metabolism Glycosidase Hydrolase Polysaccharide degradation Reference proteome Secreted Signal Virulence Xylan degradation MVSFTYLLAA MVSFTYLLAAVSAVTGAVAAPNPTKVDAQPPSGLLEKRTSPTTGVNNGFYFSFWTDTPSAVTYTNGNGGQFSMNWNGNRGNHVGGKGWNPGAARTIKYSGDYRPNGNSYLAVYGWTRNPLVEYYIVENFGTYNPSSGAQKKGEINIDGSIYDIAVSTRNCAPSIEGDCKTFQQYWSVRRNKRSSGSVNTGAHFNAWAQAGLRLGSHDYQILAVEGYQSSGQATMTVSG
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sterol biosynthetic process
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endoplasmic reticulum membrane
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heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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Gibberella zeae
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Endoplasmic reticulum Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix
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MFHLLIYPLW
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MFHLLIYPLWVLVALFAVIIANLLYQQLPRRPDEPPLVFHWFPFFGNAVAYGLDPCGFFEKCREKHGDVFTFILFGRKIVACLGVDGNDFVLNSRLQDANAEEVYGPLTIPVFGSDVVYDCPNSKLMEQKKFVKFGLTQKALESHVQLIEREVLDYVETDPSFSGRTSTIDVPKAMAEITIFTASRSLQGEEVRRKLTAEFAALYHDLDLGFRPVNFLFPWLPLPHNRKRDAAHIKMREVYMDIINDRRKGGIRTEDGTDMIANLMGCTYKNGQPVPDKEIAHMMITLLMAGQHSSSSASSWIVLHLASSPDITEELYQEQLVNLSVNGALPPLQYSDLDKLPLLQNVVKETLRVHSSIHSILRKVKRPMQVPNSPYTITTDKVIMASPTVTAMSEEYFENAKTWNPHRWDNRAKEEVDTEDVIDYGYGAVSKGTKSPYLPFGAGRHRCIGEKFAYVNLGVIVATLVRNFRLSTIDGRPGVPETDYTSLFSRPAQPAFIRWERRKKI
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sterol biosynthetic process endoplasmic reticulum membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Gibberella zeae Endoplasmic reticulum Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix MFHLLIYPLW MFHLLIYPLWVLVALFAVIIANLLYQQLPRRPDEPPLVFHWFPFFGNAVAYGLDPCGFFEKCREKHGDVFTFILFGRKIVACLGVDGNDFVLNSRLQDANAEEVYGPLTIPVFGSDVVYDCPNSKLMEQKKFVKFGLTQKALESHVQLIEREVLDYVETDPSFSGRTSTIDVPKAMAEITIFTASRSLQGEEVRRKLTAEFAALYHDLDLGFRPVNFLFPWLPLPHNRKRDAAHIKMREVYMDIINDRRKGGIRTEDGTDMIANLMGCTYKNGQPVPDKEIAHMMITLLMAGQHSSSSASSWIVLHLASSPDITEELYQEQLVNLSVNGALPPLQYSDLDKLPLLQNVVKETLRVHSSIHSILRKVKRPMQVPNSPYTITTDKVIMASPTVTAMSEEYFENAKTWNPHRWDNRAKEEVDTEDVIDYGYGAVSKGTKSPYLPFGAGRHRCIGEKFAYVNLGVIVATLVRNFRLSTIDGRPGVPETDYTSLFSRPAQPAFIRWERRKKI
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autophagy phosphorylation protein transport regulation of autophagy
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phagophore assembly site membrane
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ATP binding protein serine kinase activity protein serine/threonine kinase activity
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Gibberella zeae
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ATP-binding Autophagy Cytoplasm Kinase Membrane Nucleotide-binding Protein transport Reference proteome Serine/threonine-protein kinase Transferase Transport
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MAGPQESSTS
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MAGPQESSTSSGSRKSGSRAVGQFNIGSEIGKGSFAQVYLGWHKETKAAVAIKSVELERLNKKLRENLYSEIQILKTLRHPHIVALHDCIESTSHINLIMEYCELGDLSLFIKKREKLATHPATHDMARKYPSMPNSGLHEVVIRHFLKQLTSALEFLRSKNYVHRDVKPQNLLLLPSQPFRDQRSRPVMQASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMSTGRPPFRARNHVELLRKIEAAEDVIKFPREVSITPELKALIRSLLKRSPVERLSFENFFTHQVVTSEIPGLVEDDIPKSLRQESRDPRSAFQSGSPSLSSRSPRQTGHQSPTEALVSRSPRDQQPRSPQVGSPGGSRYARRSNESQRTTGNSPREGGEGLGIRRPVAQHAMTAPVQQVAYDSVTGRNRASPPTSLLDQVRRNRALSNPPITEEERAAQDVALEREYVVVERRHVEVNALADELAANEKLGDASQRSGPITRRYTQQGAPTSTTGAISTPYSRNALATQPRHDRKSSYEKSLSASPGSASSAISKAIQDASLRLFGFKVPPLRASPKGPSPPLYQAFPTYPTPQAPVGLLGDGRNVQGTDEDGKAAQTIEELATRSDCVYGFAEVKYKQLVPLAPSADHILGGLEPEQLVNEEDGLTVEAIVALSEEALVLYVKSLTLLARAMDIASLWWSKKSRGDTGTGLSAAAAQTVVQRINAVVQWVRQRFNEVLEKSEIVRLKLTEAQKQLPDDHPSHPSNHGTESIASSAGSPTKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLSGCEISYITAIRMLEAVLDNDEGSGSETRRLSTGKEAEREAVKEVSGGELDSDEEAHVRKRRLAAVRKKQQMIAEANSKTNLVYQQAVRRRSGDMTPRSVPSHASS
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autophagy phosphorylation protein transport regulation of autophagy phagophore assembly site membrane ATP binding protein serine kinase activity protein serine/threonine kinase activity Gibberella zeae ATP-binding Autophagy Cytoplasm Kinase Membrane Nucleotide-binding Protein transport Reference proteome Serine/threonine-protein kinase Transferase Transport MAGPQESSTS MAGPQESSTSSGSRKSGSRAVGQFNIGSEIGKGSFAQVYLGWHKETKAAVAIKSVELERLNKKLRENLYSEIQILKTLRHPHIVALHDCIESTSHINLIMEYCELGDLSLFIKKREKLATHPATHDMARKYPSMPNSGLHEVVIRHFLKQLTSALEFLRSKNYVHRDVKPQNLLLLPSQPFRDQRSRPVMQASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMSTGRPPFRARNHVELLRKIEAAEDVIKFPREVSITPELKALIRSLLKRSPVERLSFENFFTHQVVTSEIPGLVEDDIPKSLRQESRDPRSAFQSGSPSLSSRSPRQTGHQSPTEALVSRSPRDQQPRSPQVGSPGGSRYARRSNESQRTTGNSPREGGEGLGIRRPVAQHAMTAPVQQVAYDSVTGRNRASPPTSLLDQVRRNRALSNPPITEEERAAQDVALEREYVVVERRHVEVNALADELAANEKLGDASQRSGPITRRYTQQGAPTSTTGAISTPYSRNALATQPRHDRKSSYEKSLSASPGSASSAISKAIQDASLRLFGFKVPPLRASPKGPSPPLYQAFPTYPTPQAPVGLLGDGRNVQGTDEDGKAAQTIEELATRSDCVYGFAEVKYKQLVPLAPSADHILGGLEPEQLVNEEDGLTVEAIVALSEEALVLYVKSLTLLARAMDIASLWWSKKSRGDTGTGLSAAAAQTVVQRINAVVQWVRQRFNEVLEKSEIVRLKLTEAQKQLPDDHPSHPSNHGTESIASSAGSPTKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLSGCEISYITAIRMLEAVLDNDEGSGSETRRLSTGKEAEREAVKEVSGGELDSDEEAHVRKRRLAAVRKKQQMIAEANSKTNLVYQQAVRRRSGDMTPRSVPSHASS
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lipid droplet disassembly lipid transport macroautophagy
|
autophagosome membrane; cytoplasmic vesicle membrane; endoplasmic reticulum membrane; Golgi membrane; phagophore assembly site membrane; vacuolar membrane
|
guanyl-nucleotide exchange factor activity
|
Gibberella zeae
|
Autophagy Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Lipid transport Membrane Reference proteome Transmembrane Transmembrane helix Transport
|
MASNIFSRIK
|
MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTATNISPRLRQFMGSQSKERLDALDIANRLMRKENYLIAMINKDILDLSLPVPFLRGRQMFSKTMEWYLQYCILDMAFNELGQVQQDFLRPDRRRLLSQKLRQRFLFAGFLNLLFAPVVLAYVVIVYFFTYYYEYQKDPKQAAARKYTSLAEWKFRQFNELPHIFYERLHMSYPFATRYIDQFPKRITEAVARTIAFMSGAITAILAIGSVLDSELFLNFEITKDRPVIFYLGVFAAIWATTRGMVSEETLVFNPEYALRNVIEYTRYVPDHWKNKLHSSEVKQEFSELYKMKVVIFLEEMMGIVTTPMLLLFSLPRCSDQIVDFFREFTIHVDGLGYVCSFAVFDFQKGPGNTGPQGPRPDVREDYYSTKHGKMAASYYGFLDNYAANPKTGIPGHLPPGPKPSFHPPPSFPGIGSPTLAADMQGSHIGRTGTETGRARSRAPGGRGPRIGVMPQPSPMASMLLDQHHQPPGGNMVARSLHASRYPRGYRGESQIIEETEASSIRRNGEDDELYEPGGALGESVWETSPARGVTRENSAANTEDPEAGVLGLIYQLQQTQRPRRGGGMV
|
lipid droplet disassembly lipid transport macroautophagy autophagosome membrane; cytoplasmic vesicle membrane; endoplasmic reticulum membrane; Golgi membrane; phagophore assembly site membrane; vacuolar membrane guanyl-nucleotide exchange factor activity Gibberella zeae Autophagy Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Lipid transport Membrane Reference proteome Transmembrane Transmembrane helix Transport MASNIFSRIK MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTATNISPRLRQFMGSQSKERLDALDIANRLMRKENYLIAMINKDILDLSLPVPFLRGRQMFSKTMEWYLQYCILDMAFNELGQVQQDFLRPDRRRLLSQKLRQRFLFAGFLNLLFAPVVLAYVVIVYFFTYYYEYQKDPKQAAARKYTSLAEWKFRQFNELPHIFYERLHMSYPFATRYIDQFPKRITEAVARTIAFMSGAITAILAIGSVLDSELFLNFEITKDRPVIFYLGVFAAIWATTRGMVSEETLVFNPEYALRNVIEYTRYVPDHWKNKLHSSEVKQEFSELYKMKVVIFLEEMMGIVTTPMLLLFSLPRCSDQIVDFFREFTIHVDGLGYVCSFAVFDFQKGPGNTGPQGPRPDVREDYYSTKHGKMAASYYGFLDNYAANPKTGIPGHLPPGPKPSFHPPPSFPGIGSPTLAADMQGSHIGRTGTETGRARSRAPGGRGPRIGVMPQPSPMASMLLDQHHQPPGGNMVARSLHASRYPRGYRGESQIIEETEASSIRRNGEDDELYEPGGALGESVWETSPARGVTRENSAANTEDPEAGVLGLIYQLQQTQRPRRGGGMV
|
alkaloid metabolic process
|
endoplasmic reticulum membrane
|
heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
|
Catharanthus roseus
|
Alkaloid metabolism Endoplasmic reticulum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix
|
MEFHESSPFV
|
MEFHESSPFVFITRGFIFIAISIAVLRRIISKKTKTLPPGPWKLPLIGNLHQFLGSVPYQILRDLAQKNGPLMHLQLGEVSAIVAASPQMAKEITKTLDLQFADRPVIQALRIVTYDYLDISFNAYGKYWRQLRKIFVQELLTSKRVRSFCSIREDEFSNLVKTINSANGKSINLSKLMTSCTNSIINKVAFGKVRYEREVFIDLINQILALAGGFKLVDLFPSYKILHVLEGTERKLWEIRGKIDKILDKVIDEHRENSSRTGKGNGCNGQEDIVDILLRIEEGGDLDLDIPFGNNNIKALLFDIIAGGTETSSTAVDWAMSEMMRNPHVMSKAQKEIREAFNGKEKIEENDIQNLKYLKLVIQETLRLHPPAPLLMRQCREKCEIGGYHIPVGTKAFINVWAIGRDPAYWPNPESFIPERFDDNTYEFTKSEHHAFEYLPFGAGRRMCPGISFGLANVELPLALLLYHFNWQLPDGSTTLDMTEATGLAARRKYDLQLIATSYA
|
alkaloid metabolic process endoplasmic reticulum membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Catharanthus roseus Alkaloid metabolism Endoplasmic reticulum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix MEFHESSPFV MEFHESSPFVFITRGFIFIAISIAVLRRIISKKTKTLPPGPWKLPLIGNLHQFLGSVPYQILRDLAQKNGPLMHLQLGEVSAIVAASPQMAKEITKTLDLQFADRPVIQALRIVTYDYLDISFNAYGKYWRQLRKIFVQELLTSKRVRSFCSIREDEFSNLVKTINSANGKSINLSKLMTSCTNSIINKVAFGKVRYEREVFIDLINQILALAGGFKLVDLFPSYKILHVLEGTERKLWEIRGKIDKILDKVIDEHRENSSRTGKGNGCNGQEDIVDILLRIEEGGDLDLDIPFGNNNIKALLFDIIAGGTETSSTAVDWAMSEMMRNPHVMSKAQKEIREAFNGKEKIEENDIQNLKYLKLVIQETLRLHPPAPLLMRQCREKCEIGGYHIPVGTKAFINVWAIGRDPAYWPNPESFIPERFDDNTYEFTKSEHHAFEYLPFGAGRRMCPGISFGLANVELPLALLLYHFNWQLPDGSTTLDMTEATGLAARRKYDLQLIATSYA
|
heat acclimation phosphorylation regulation of cell growth
|
membrane; plasma membrane
|
ATP binding protein serine kinase activity protein serine/threonine kinase activity receptor serine/threonine kinase binding
|
Oryza sativa subsp. japonica
|
ATP-binding Cell membrane Glycoprotein Growth regulation Kinase Leucine-rich repeat Membrane Nucleotide-binding Receptor Reference proteome Repeat Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix
|
MTTTTTTRLL
|
MTTTTTTRLLLAAILLAVAAADDDGQTLLEIKKSFRNVDNVLYDWAGDGAPRRYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAIGNLKSVESIDLKSNELSGQIPDEIGDCTSLKTLDLSSNNLGGDIPFSISKLKHLENLILKNNQLVGMIPSTLSQLPNLKILDLAQNKLNGEIPRLIYWNEVLQYLGLRSNNLEGSLSPEMCQLTGLWYFDVKNNSLTGIIPDTIGNCTSFQVLDLSYNRLTGEIPFNIGFLQVATLSLQGNNFSGPIPSVIGLMQALAVLDLSFNQLSGPIPSILGNLTYTEKLYLQGNRLTGSIPPELGNMSTLHYLELNDNQLTGFIPPELGKLTGLFDLNLANNNLEGPIPDNISSCMNLISFNAYGNKLNGTVPRSLHKLESITYLNLSSNYLSGAIPIELAKMKNLDTLDLSCNMVAGPIPSAIGSLEHLLRLNFSNNNLVGYIPAEFGNLRSIMEIDLSSNHLGGLIPQEVGMLQNLILLKLESNNITGDVSSLINCFSLNVLNVSYNNLAGIVPTDNNFSRFSPDSFLGNPGLCGYWLGSSCYSTSHVQRSSVSRSAILGIAVAGLVILLMILAAACWPHWAQVPKDVSLCKPDIHALPSSNVPPKLVILHMNMAFLVYEDIMRMTENLSEKYIIGYGASSTVYKCVLKNCKPVAIKKLYAHYPQSLKEFETELETVGSIKHRNLVSLQGYSLSPAGNLLFYDYLENGSLWDVLHAGSSKKQKLDWEARLRIALGAAQGLAYLHHDCNPRIIHRDVKSKNILLDKDYEAHLADFGIAKSLCTSKTHTSTYVMGTIGYIDPEYACTSRLNEKSDVYSYGIVLLELLTGKKPVDNECNLHHLILSKAADNTVMEMVDPDIADTCKDLGEVKKVFQLALLCSKRQPSDRPTMHEVVRVLDCLVYPDPPSKPALPPALPQSSTVPSYVNEYVSLRGGSTLSCENSSSASDAELFLKFGEVISQNTE
|
heat acclimation phosphorylation regulation of cell growth membrane; plasma membrane ATP binding protein serine kinase activity protein serine/threonine kinase activity receptor serine/threonine kinase binding Oryza sativa subsp. japonica ATP-binding Cell membrane Glycoprotein Growth regulation Kinase Leucine-rich repeat Membrane Nucleotide-binding Receptor Reference proteome Repeat Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix MTTTTTTRLL MTTTTTTRLLLAAILLAVAAADDDGQTLLEIKKSFRNVDNVLYDWAGDGAPRRYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAIGNLKSVESIDLKSNELSGQIPDEIGDCTSLKTLDLSSNNLGGDIPFSISKLKHLENLILKNNQLVGMIPSTLSQLPNLKILDLAQNKLNGEIPRLIYWNEVLQYLGLRSNNLEGSLSPEMCQLTGLWYFDVKNNSLTGIIPDTIGNCTSFQVLDLSYNRLTGEIPFNIGFLQVATLSLQGNNFSGPIPSVIGLMQALAVLDLSFNQLSGPIPSILGNLTYTEKLYLQGNRLTGSIPPELGNMSTLHYLELNDNQLTGFIPPELGKLTGLFDLNLANNNLEGPIPDNISSCMNLISFNAYGNKLNGTVPRSLHKLESITYLNLSSNYLSGAIPIELAKMKNLDTLDLSCNMVAGPIPSAIGSLEHLLRLNFSNNNLVGYIPAEFGNLRSIMEIDLSSNHLGGLIPQEVGMLQNLILLKLESNNITGDVSSLINCFSLNVLNVSYNNLAGIVPTDNNFSRFSPDSFLGNPGLCGYWLGSSCYSTSHVQRSSVSRSAILGIAVAGLVILLMILAAACWPHWAQVPKDVSLCKPDIHALPSSNVPPKLVILHMNMAFLVYEDIMRMTENLSEKYIIGYGASSTVYKCVLKNCKPVAIKKLYAHYPQSLKEFETELETVGSIKHRNLVSLQGYSLSPAGNLLFYDYLENGSLWDVLHAGSSKKQKLDWEARLRIALGAAQGLAYLHHDCNPRIIHRDVKSKNILLDKDYEAHLADFGIAKSLCTSKTHTSTYVMGTIGYIDPEYACTSRLNEKSDVYSYGIVLLELLTGKKPVDNECNLHHLILSKAADNTVMEMVDPDIADTCKDLGEVKKVFQLALLCSKRQPSDRPTMHEVVRVLDCLVYPDPPSKPALPPALPQSSTVPSYVNEYVSLRGGSTLSCENSSSASDAELFLKFGEVISQNTE
|
long-chain fatty acid biosynthetic process unsaturated fatty acid biosynthetic process
|
chloroplast; chloroplast membrane
|
heme binding metal ion binding oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
|
Chlamydomonas reinhardtii
|
Chloroplast Electron transport Fatty acid biosynthesis Fatty acid metabolism Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Oxidoreductase Plastid Transit peptide Transmembrane Transmembrane helix Transport
|
MNATMQRSAV
|
MNATMQRSAVAGRTSGKVATTARASSMARPRLPIAGRVARRSAVTVRAVAEPVVVDKAVEAPAKPVPSGGDPWEDEKWTKYKWTVYRGVAYDLTPYLDRHPGGRWLLNLAIGRDATALFESYHLRPEVAASMLKRLPVLADFPVDAVPPSPRPNDSELYNAIRERVRKEVFKGTEIKGAHRSGSEGAAFAVLGYAAAMYALYTYDANPLTGALLGLGGAWIGLTIQHCGNHGAMSTNPVVNNLMGLTNDLAGGSSLMWRYHHQVSHHIHCNDDALDEDVFSAFPMLRFDDRLPKAWYHQFQHVYMWALFPFLQLVFQIGDWQALLTNRTVGATLYGASNFERQTLIAGKLAHYFLLYGLPAFLHGPTAMLGGAAGYLFTQSIVLAATFAVSHNVPETKPLDPGPTRENLDESAVTRDWGVQQVLTSANWGGVIGNFFTGGLNLQIEHHLFPAISFMHYPAISKIVADECKQRGIPYSHYDTLPEILGRFVRYMKEVGAAPQKPVKRDGEMLMLSKF
|
long-chain fatty acid biosynthetic process unsaturated fatty acid biosynthetic process chloroplast; chloroplast membrane heme binding metal ion binding oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Chlamydomonas reinhardtii Chloroplast Electron transport Fatty acid biosynthesis Fatty acid metabolism Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Oxidoreductase Plastid Transit peptide Transmembrane Transmembrane helix Transport MNATMQRSAV MNATMQRSAVAGRTSGKVATTARASSMARPRLPIAGRVARRSAVTVRAVAEPVVVDKAVEAPAKPVPSGGDPWEDEKWTKYKWTVYRGVAYDLTPYLDRHPGGRWLLNLAIGRDATALFESYHLRPEVAASMLKRLPVLADFPVDAVPPSPRPNDSELYNAIRERVRKEVFKGTEIKGAHRSGSEGAAFAVLGYAAAMYALYTYDANPLTGALLGLGGAWIGLTIQHCGNHGAMSTNPVVNNLMGLTNDLAGGSSLMWRYHHQVSHHIHCNDDALDEDVFSAFPMLRFDDRLPKAWYHQFQHVYMWALFPFLQLVFQIGDWQALLTNRTVGATLYGASNFERQTLIAGKLAHYFLLYGLPAFLHGPTAMLGGAAGYLFTQSIVLAATFAVSHNVPETKPLDPGPTRENLDESAVTRDWGVQQVLTSANWGGVIGNFFTGGLNLQIEHHLFPAISFMHYPAISKIVADECKQRGIPYSHYDTLPEILGRFVRYMKEVGAAPQKPVKRDGEMLMLSKF
|
dense core granule maturation
|
cytoplasmic vesicle membrane; cytosol; early endosome; Golgi medial cisterna; Golgi trans cisterna
|
GTPase activator activity small GTPase binding
|
Caenorhabditis elegans
|
Alternative splicing Cytoplasmic vesicle Endosome Golgi apparatus GTPase activation Membrane Reference proteome
|
MQMFRHSSAD
|
MQMFRHSSADMWRAKKPTLERRSTDGRRSSIVDWINGLSDNNNYKSDHWVEKHDEGCERMTRNGSVCAVEESEPDVPTQHREVLLTKLKIEIKNIMAEHGAKKYLNLNSPYVTSLCIAVDACIMDGLRRRLLTLFNSPSSMSLLQIIAKSNGPAQQVLDQTREIEELRTSAIPVHLIWIREALYLKSLSTIINHFIDSKSVRRYYDNSALLLDPVKGRLVATLMMAPCMVTYRRMSNRIEQEATAEELVEGATRGSTSTVPSRPPLSITRQVSSIAASVERNGSVSRDYVFSLHHSCKSTLLYGKNNVCVAMNGSDFAKGYMSLQKFYDGNLSLKWVPNQLMHASSQPSSGHSNNGEFTNIWKNTINIEMQDIIYIHLHQKDEISPTCLTFVNCEGVQSAPFQLPAGQHSIAFLSSLETGLAPLLRLDPPLWVGTTKEKILPRLRKRSTAVANPAMLDYVFRLVRTSGVEPAPEDIEDPLAPTSHSPPIHDNCVSLPNSPYIVDNVDSIVNFQIGTACQSMRNQIMARAFYGWLTYVRHLRTIRTHLLHLVDTKTLICDDDCDPVDEKFWKQARAEPTEENEKEFLKRVYWRGIEGINTKEVRRMAWPYLLGLFEWNESPESRLEQFTSQYWQDIEEWRVLEAEVRRRDEEAFRAARARKAASPVREESCDVFEDPNEPTCSQHYDRENLITLFRANLHRIDKDVERCDRNLMFFSNKDNLESLRRVMYTYVRRNLEEGYTQGMCDLLAPLLVTFEDEALTLECFSLLMLRQRGKFPQRPGMSKCLLNLRSLIQVVDPQIYALISDIDYAQALSFAFRWFLLDFKRELSYECTYKVWEVIWAAQRLRITDDFAIFFGLATITNYHDVLITNNFDYTDMIKFFNEMAERHDCSRLLSSARTHVKCLQNLVQHLK
|
dense core granule maturation cytoplasmic vesicle membrane; cytosol; early endosome; Golgi medial cisterna; Golgi trans cisterna GTPase activator activity small GTPase binding Caenorhabditis elegansAlternative splicing Cytoplasmic vesicle Endosome Golgi apparatus GTPase activation Membrane Reference proteome MQMFRHSSAD MQMFRHSSADMWRAKKPTLERRSTDGRRSSIVDWINGLSDNNNYKSDHWVEKHDEGCERMTRNGSVCAVEESEPDVPTQHREVLLTKLKIEIKNIMAEHGAKKYLNLNSPYVTSLCIAVDACIMDGLRRRLLTLFNSPSSMSLLQIIAKSNGPAQQVLDQTREIEELRTSAIPVHLIWIREALYLKSLSTIINHFIDSKSVRRYYDNSALLLDPVKGRLVATLMMAPCMVTYRRMSNRIEQEATAEELVEGATRGSTSTVPSRPPLSITRQVSSIAASVERNGSVSRDYVFSLHHSCKSTLLYGKNNVCVAMNGSDFAKGYMSLQKFYDGNLSLKWVPNQLMHASSQPSSGHSNNGEFTNIWKNTINIEMQDIIYIHLHQKDEISPTCLTFVNCEGVQSAPFQLPAGQHSIAFLSSLETGLAPLLRLDPPLWVGTTKEKILPRLRKRSTAVANPAMLDYVFRLVRTSGVEPAPEDIEDPLAPTSHSPPIHDNCVSLPNSPYIVDNVDSIVNFQIGTACQSMRNQIMARAFYGWLTYVRHLRTIRTHLLHLVDTKTLICDDDCDPVDEKFWKQARAEPTEENEKEFLKRVYWRGIEGINTKEVRRMAWPYLLGLFEWNESPESRLEQFTSQYWQDIEEWRVLEAEVRRRDEEAFRAARARKAASPVREESCDVFEDPNEPTCSQHYDRENLITLFRANLHRIDKDVERCDRNLMFFSNKDNLESLRRVMYTYVRRNLEEGYTQGMCDLLAPLLVTFEDEALTLECFSLLMLRQRGKFPQRPGMSKCLLNLRSLIQVVDPQIYALISDIDYAQALSFAFRWFLLDFKRELSYECTYKVWEVIWAAQRLRITDDFAIFFGLATITNYHDVLITNNFDYTDMIKFFNEMAERHDCSRLLSSARTHVKCLQNLVQHLK
|
cell differentiation innate immune response NAD catabolic process negative regulation of MyD88-independent toll-like receptor signaling pathway nervous system development protein localization to mitochondrion regulation of dendrite morphogenesis response to axon injury signal transduction
|
axon; cytoplasm; dendrite; microtubule; mitochondrion; synapse
|
NAD(P)+ nucleosidase activity NAD+ nucleosidase activity NAD+ nucleotidase, cyclic ADP-ribose generating signaling adaptor activity
|
Sus scrofa
|
Cell projection Cytoplasm Differentiation Hydrolase Immunity Innate immunity Mitochondrion NAD Neurogenesis Phosphoprotein Reference proteome Repeat Synapse Transit peptide
|
MVLTILFSAY
|
MVLTILFSAYKLCRFFAMSSPRPGAERLAVPGPDGGGGAGPWWTAGGRGPREVSPGVGAEVQGALERALPELQQALSALKQAGGGRAVGAGLAEVFQLVEEAWLLPAMGREVAQGLCDAIRLEGGLDLLLRLLQAPELETRVQAARLLEQILVAENRRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCAMHGGQAAQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSSRMEAQCIGAFYLCAEAVIMHIKNRNKVFSDIGAIQSLKRLVSYSTNGTTSALAKRALRLLGEEVPRPILPCVASWKEAEVQTWLQQIGFSQYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRVRILTAAREMLHSPLPCTGSKPSGDVPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSIMSARNFVLVLSAGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPVIDGFEWPEPHTLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT
|
cell differentiation innate immune response NAD catabolic process negative regulation of MyD88-independent toll-like receptor signaling pathway nervous system development protein localization to mitochondrion regulation of dendrite morphogenesis response to axon injury signal transduction axon; cytoplasm; dendrite; microtubule; mitochondrion; synapse NAD(P)+ nucleosidase activity NAD+ nucleosidase activity NAD+ nucleotidase, cyclic ADP-ribose generating signaling adaptor activity Sus scrofa Cell projection Cytoplasm Differentiation Hydrolase Immunity Innate immunity Mitochondrion NAD Neurogenesis Phosphoprotein Reference proteome Repeat Synapse Transit peptide MVLTILFSAY MVLTILFSAYKLCRFFAMSSPRPGAERLAVPGPDGGGGAGPWWTAGGRGPREVSPGVGAEVQGALERALPELQQALSALKQAGGGRAVGAGLAEVFQLVEEAWLLPAMGREVAQGLCDAIRLEGGLDLLLRLLQAPELETRVQAARLLEQILVAENRRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCAMHGGQAAQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSSRMEAQCIGAFYLCAEAVIMHIKNRNKVFSDIGAIQSLKRLVSYSTNGTTSALAKRALRLLGEEVPRPILPCVASWKEAEVQTWLQQIGFSQYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRVRILTAAREMLHSPLPCTGSKPSGDVPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSIMSARNFVLVLSAGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPVIDGFEWPEPHTLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT
|
angiogenesis defense response to fungus defense response to Gram-positive bacterium G protein-coupled receptor signaling pathway lymphocyte chemotaxis mast cell degranulation negative regulation of cell cycle G1/S phase transition negative regulation of cell division regulation of keratinocyte proliferation regulation of T cell migration T cell homeostasis
|
extracellular space
|
chemokine activity G protein-coupled receptor binding receptor ligand activity
|
Sus scrofa
|
Antibiotic Antimicrobial Chemotaxis Cytokine Direct protein sequencing Disulfide bond Reference proteome Secreted Signal
|
MRFLALTSLL
|
MRFLALTSLLCILLLCLSFFSAEGRRHPRNPAKPGKIRICCPRLPGPDLMPQKGHHMRICRPCKFKQKPQLWVVPGALPQV
|
angiogenesis defense response to fungus defense response to Gram-positive bacterium G protein-coupled receptor signaling pathway lymphocyte chemotaxis mast cell degranulation negative regulation of cell cycle G1/S phase transition negative regulation of cell division regulation of keratinocyte proliferation regulation of T cell migration T cell homeostasis extracellular space chemokine activity G protein-coupled receptor binding receptor ligand activity Sus scrofa Antibiotic Antimicrobial Chemotaxis Cytokine Direct protein sequencing Disulfide bond Reference proteome Secreted Signal MRFLALTSLL MRFLALTSLLCILLLCLSFFSAEGRRHPRNPAKPGKIRICCPRLPGPDLMPQKGHHMRICRPCKFKQKPQLWVVPGALPQV
|
activation of innate immune response cAMP-mediated signaling cellular response to exogenous dsRNA cGAS/STING signaling pathway cGMP-mediated signaling defense response to virus DNA damage response DNA repair innate immune response negative regulation of cGAS/STING signaling pathway negative regulation of double-strand break repair via homologous recombination paracrine signaling positive regulation of cellular senescence positive regulation of defense response to virus by host positive regulation of type I interferon production
|
cytosol; nuclear body; nucleus; plasma membrane; site of double-strand break
|
2',3'-cyclic GMP-AMP synthase activity ATP binding chromatin binding DNA binding double-stranded DNA binding GTP binding metal ion binding molecular condensate scaffold activity nucleosome binding phosphatidylinositol-4,5-bisphosphate binding poly-ADP-D-ribose modification-dependent protein binding protein homodimerization activity
|
Sus scrofa
|
3D-structure Acetylation ADP-ribosylation Antiviral defense ATP-binding Cell membrane Chromosome Cytoplasm DNA damage DNA repair DNA-binding GTP-binding Immunity Innate immunity Isopeptide bond Lipid-binding Lipoprotein Magnesium Membrane Metal-binding Methylation Nucleotide-binding Nucleotidyltransferase Nucleus Palmitate Phosphoprotein Reference proteome Transferase Ubl conjugation Zinc
|
MAARRGKSTR
|
MAARRGKSTRTASEVGAAGPRASARSVNGAPTVPEAARPGARRNGPSRASGCRREKSGPDPREKPQVRTRTARAEDQAEGPSAPSERVEPPSAQGASLLRAGSCRAREARSARELRPQAGATELAAPARMEAPPGAWKLQTVLEKVRLSRHEISEAAEVVNWVVEHLLRRLQGGESEFKGVALLRTGSYYERVKISAPNEFDVMFKLEVPRIQLEEYCNSGAHYFVKFKRNPGGNPLEQFLEKEILSASKMLSKFRKIIKEEIKNIEGVTVERKRRGSPAVTLLISKPKEISVDIILALESKSSWPASTQKGLPISQWLGAKVKNNLKRQPFYLVPKHAKEGSGFQEETWRLSFSHIEKDILKNHGQSKTCCEIDGVKCCRKECLKLMKYLLEQLKKKFGNRRELAKFCSYHVKTAFFHVCTQDPHDNQWHLKNLECCFDNCVAYFLQCLKTEQLANYFIPGVNLFSRDLIDKPSKEFLSKQIEYERNNGFPVFW
|
activation of innate immune response cAMP-mediated signaling cellular response to exogenous dsRNA cGAS/STING signaling pathway cGMP-mediated signaling defense response to virus DNA damage response DNA repair innate immune response negative regulation of cGAS/STING signaling pathway negative regulation of double-strand break repair via homologous recombination paracrine signaling positive regulation of cellular senescence positive regulation of defense response to virus by host positive regulation of type I interferon production cytosol; nuclear body; nucleus; plasma membrane; site of double-strand break 2',3'-cyclic GMP-AMP synthase activity ATP binding chromatin binding DNA binding double-stranded DNA binding GTP binding metal ion binding molecular condensate scaffold activity nucleosome binding phosphatidylinositol-4,5-bisphosphate binding poly-ADP-D-ribose modification-dependent protein binding protein homodimerization activity Sus scrofa 3D-structure Acetylation ADP-ribosylation Antiviral defense ATP-binding Cell membrane Chromosome Cytoplasm DNA damage DNA repair DNA-binding GTP-binding Immunity Innate immunity Isopeptide bond Lipid-binding Lipoprotein Magnesium Membrane Metal-binding Methylation Nucleotide-binding Nucleotidyltransferase Nucleus Palmitate Phosphoprotein Reference proteome Transferase Ubl conjugation Zinc MAARRGKSTR MAARRGKSTRTASEVGAAGPRASARSVNGAPTVPEAARPGARRNGPSRASGCRREKSGPDPREKPQVRTRTARAEDQAEGPSAPSERVEPPSAQGASLLRAGSCRAREARSARELRPQAGATELAAPARMEAPPGAWKLQTVLEKVRLSRHEISEAAEVVNWVVEHLLRRLQGGESEFKGVALLRTGSYYERVKISAPNEFDVMFKLEVPRIQLEEYCNSGAHYFVKFKRNPGGNPLEQFLEKEILSASKMLSKFRKIIKEEIKNIEGVTVERKRRGSPAVTLLISKPKEISVDIILALESKSSWPASTQKGLPISQWLGAKVKNNLKRQPFYLVPKHAKEGSGFQEETWRLSFSHIEKDILKNHGQSKTCCEIDGVKCCRKECLKLMKYLLEQLKKKFGNRRELAKFCSYHVKTAFFHVCTQDPHDNQWHLKNLECCFDNCVAYFLQCLKTEQLANYFIPGVNLFSRDLIDKPSKEFLSKQIEYERNNGFPVFW
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negative regulation of protein glutathionylation positive regulation of sodium ion export across plasma membrane potassium ion transport sodium ion transport
|
apical plasma membrane; caveola; intercalated disc; sarcolemma; sodium:potassium-exchanging ATPase complex; T-tubule
|
sodium channel regulator activity transmembrane transporter binding
|
Sus scrofa
|
Cell membrane Glutathionylation Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Potassium Potassium transport Reference proteome Signal Sodium Sodium transport Sodium/potassium transport Transmembrane Transmembrane helix Transport
|
MASLSHILVL
|
MASLSHILVLWVGILTVVNAEAPQEHDPFTYDYQSLRIGGLIIAGILFILGILIVLSRRCRCKFNQQQSLGKMRSPHLAAQFSSESC
|
negative regulation of protein glutathionylation positive regulation of sodium ion export across plasma membrane potassium ion transport sodium ion transport apical plasma membrane; caveola; intercalated disc; sarcolemma; sodium:potassium-exchanging ATPase complex; T-tubule sodium channel regulator activity transmembrane transporter binding Sus scrofa Cell membrane Glutathionylation Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Potassium Potassium transport Reference proteome Signal Sodium Sodium transport Sodium/potassium transport Transmembrane Transmembrane helix Transport MASLSHILVL MASLSHILVLWVGILTVVNAEAPQEHDPFTYDYQSLRIGGLIIAGILFILGILIVLSRRCRCKFNQQQSLGKMRSPHLAAQFSSESC
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cinnamic acid biosynthetic process cinnamic acid metabolic process circadian rhythm green leaf volatile biosynthetic process phenylpropanoid metabolic process phytoalexin biosynthetic process response to ethylene
|
peroxisome
|
(E)-caffeate-CoA ligase activity 4-coumarate-CoA ligase activity ATP binding CoA-ligase activity trans-cinnamate-CoA ligase activity
|
Petunia hybrida
|
Alternative splicing ATP-binding Ligase Nucleotide-binding Peroxisome Phenylpropanoid metabolism
|
MDELPKCGAN
|
MDELPKCGANYVPLTPLTFLTRAFKSYANRTSIIYAGARFTWEQTYKRCCRLASSLQSLNIVKNDVVSVLAPNVPATYEMHFAVPMAGAVLNTINTRLDPMNIAIILKHSEAKLLFVDYEYLEKARKALELLMSTNFITAQNSKKISMPQVILIDDLYSPTRIQQQDQLEYEQLVHQGNPEYAPENIVDDEWDPIVLNYTSGTTSEPKGVVYSHRGAFLSTLNTIMGWEMGTEPVYLWSLPMFHINGWTLTWGIAARGGTNVCIRNTTAQEIYSNITLHKVTHMCCAPTVFNILLEAKPHERREITTPVQVMVGGAPPPTTLIGKIEELGFHVVHCYGITEAGGTTLVCEWQSEWNKLSREDQANLKARQGISVLALEDVDVKNSKTMQSVPHNGKTMGEICLRGSSIMKGYFKNDKANSQVFKNGWFLTGDVAVIHQDGYLEIKDRCKDIIISGGENISSIEVENAILKHPSVIEAAVVAMPHPRWGETPCAFVIKTKNPEIKEADIIVHCKKELPGFMVPKHVQFLEELPKTGTGKVKKLQLREMAKSFGIFDNANQTSQILDLPARL
|
cinnamic acid biosynthetic process cinnamic acid metabolic process circadian rhythm green leaf volatile biosynthetic process phenylpropanoid metabolic process phytoalexin biosynthetic process response to ethylene peroxisome (E)-caffeate-CoA ligase activity 4-coumarate-CoA ligase activity ATP binding CoA-ligase activity trans-cinnamate-CoA ligase activity Petunia hybrida Alternative splicing ATP-binding Ligase Nucleotide-binding Peroxisome Phenylpropanoid metabolism MDELPKCGAN MDELPKCGANYVPLTPLTFLTRAFKSYANRTSIIYAGARFTWEQTYKRCCRLASSLQSLNIVKNDVVSVLAPNVPATYEMHFAVPMAGAVLNTINTRLDPMNIAIILKHSEAKLLFVDYEYLEKARKALELLMSTNFITAQNSKKISMPQVILIDDLYSPTRIQQQDQLEYEQLVHQGNPEYAPENIVDDEWDPIVLNYTSGTTSEPKGVVYSHRGAFLSTLNTIMGWEMGTEPVYLWSLPMFHINGWTLTWGIAARGGTNVCIRNTTAQEIYSNITLHKVTHMCCAPTVFNILLEAKPHERREITTPVQVMVGGAPPPTTLIGKIEELGFHVVHCYGITEAGGTTLVCEWQSEWNKLSREDQANLKARQGISVLALEDVDVKNSKTMQSVPHNGKTMGEICLRGSSIMKGYFKNDKANSQVFKNGWFLTGDVAVIHQDGYLEIKDRCKDIIISGGENISSIEVENAILKHPSVIEAAVVAMPHPRWGETPCAFVIKTKNPEIKEADIIVHCKKELPGFMVPKHVQFLEELPKTGTGKVKKLQLREMAKSFGIFDNANQTSQILDLPARL
|
cinnamic acid biosynthetic process cinnamic acid metabolic process circadian rhythm ferulate metabolic process phenylpropanoid metabolic process phytoalexin biosynthetic process
|
cytosol
|
(E)-caffeate-CoA ligase activity 4-coumarate-CoA ligase activity ATP binding benzoate-CoA ligase activity CoA-ligase activity trans-cinnamate-CoA ligase activity trans-feruloyl-CoA synthase activity
|
Petunia hybrida
|
ATP-binding Cytoplasm Ligase Nucleotide-binding Phenylpropanoid metabolism
|
MPMETETNQG
|
MPMETETNQGDLIFRSKLPDIYIPKHLPLHSYCFENISEFSSRPCLINGANNHIYTYADVELTSRKVAAGLNKLGIQQKDTIMILLPNSPEFVFAFMGASYLGAISTMANPLFTPAEVVKQAKASNAKLIITQACFVNKVKDYAFDNNLNVICIDSAPEGCIHFSELTQADEHDIPDVKIQSDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENANLYMHSEDVLMCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVQFCELIEKYKVTIGPFVPPIVLAIAKSPVVDNYDLSSVRTVMSGAAPLGKELEDAVRIKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFDIKSGACGTVVRNAEMKIVDPDTGCSLPRNQPGEICIRGDQIMKGYLNDPAATTRTIDKEGWLHTGDIGYIDNDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSDITEDEVKDFVSKQVIFYKRIKRVFFVETVPKSPSGKILRKDLRARLAAGVPN
|
cinnamic acid biosynthetic process cinnamic acid metabolic process circadian rhythm ferulate metabolic process phenylpropanoid metabolic process phytoalexin biosynthetic process cytosol (E)-caffeate-CoA ligase activity 4-coumarate-CoA ligase activity ATP binding benzoate-CoA ligase activity CoA-ligase activity trans-cinnamate-CoA ligase activity trans-feruloyl-CoA synthase activity Petunia hybrida ATP-binding Cytoplasm Ligase Nucleotide-binding Phenylpropanoid metabolism MPMETETNQG MPMETETNQGDLIFRSKLPDIYIPKHLPLHSYCFENISEFSSRPCLINGANNHIYTYADVELTSRKVAAGLNKLGIQQKDTIMILLPNSPEFVFAFMGASYLGAISTMANPLFTPAEVVKQAKASNAKLIITQACFVNKVKDYAFDNNLNVICIDSAPEGCIHFSELTQADEHDIPDVKIQSDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENANLYMHSEDVLMCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVQFCELIEKYKVTIGPFVPPIVLAIAKSPVVDNYDLSSVRTVMSGAAPLGKELEDAVRIKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFDIKSGACGTVVRNAEMKIVDPDTGCSLPRNQPGEICIRGDQIMKGYLNDPAATTRTIDKEGWLHTGDIGYIDNDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSDITEDEVKDFVSKQVIFYKRIKRVFFVETVPKSPSGKILRKDLRARLAAGVPN
|
nitrate assimilation
|
cytoplasm
|
4 iron, 4 sulfur cluster binding ferredoxin-nitrate reductase activity metal ion binding molybdopterin cofactor binding
|
Haloferax mediterranei
|
4Fe-4S Cytoplasm Iron Iron-sulfur Metal-binding Molybdenum Nitrate assimilation Oxidoreductase
|
MPRNLRFLSV
|
MPRNLRFLSVVNHVTKQVPTTCMRCAVGCGHVHLGSENAYGLETVRGDPSHPVNNGLACGRGIRESADPAGEWLTRPLVREDGELVQTSWSDAMARVGATIRTAVATDPDEVAVLGSGQQTNEAAYALGKLARAGIGTRNYDANTTLCMASAVTAYYRAFGSDAPPPTYDDIPNAETHLVWGANPAVAHPVMFRWIRQSATDGRLVVVDPVETKTAAVADDHVSVAPGGDLALARAILRHLVDTDQIDESFVRSNTEGFDDVVSALPSVTDAAARAGVSLDTVEELAALLDAPTLIYWGMGVNQSVRGTATAGALVNLCLASGNLGPGTGPFSLTGQANSMGTRVCSSKGTWSGHRPFEHPDHRRAVAEAWDVPVSRLPDDSGPGPVGILDSSPSVVWTVATNPLAGFPDATAAREVLRDSFLVVQDAFRSDTVELADVVLPAATWGESEGTAMNMERTVSRIRAATETPPGVRQDLDIIADVAARVAPGLLPRPPVSPSAIFDEFAALTEGTDADCSGISYTRLDGERAVRWPAPEPNSDAGYRYYDPSTSRWTFPTPSGKARFSTLDGEPLPEPVDGDYPLTLTTGREADGYNTGVRSRSDTPEEPVARVNPETVDTYHDAVADTDGELRTTVVSRRASVSVTLDRDDAVPPGLVWLSIHHPMTNQLTSPAVDPQSNEPNFKQCAVRFVHPDAPAKADFLAAEVSD
|
nitrate assimilation cytoplasm 4 iron, 4 sulfur cluster binding ferredoxin-nitrate reductase activity metal ion binding molybdopterin cofactor binding Haloferax mediterranei 4Fe-4S Cytoplasm Iron Iron-sulfur Metal-binding Molybdenum Nitrate assimilation Oxidoreductase MPRNLRFLSV MPRNLRFLSVVNHVTKQVPTTCMRCAVGCGHVHLGSENAYGLETVRGDPSHPVNNGLACGRGIRESADPAGEWLTRPLVREDGELVQTSWSDAMARVGATIRTAVATDPDEVAVLGSGQQTNEAAYALGKLARAGIGTRNYDANTTLCMASAVTAYYRAFGSDAPPPTYDDIPNAETHLVWGANPAVAHPVMFRWIRQSATDGRLVVVDPVETKTAAVADDHVSVAPGGDLALARAILRHLVDTDQIDESFVRSNTEGFDDVVSALPSVTDAAARAGVSLDTVEELAALLDAPTLIYWGMGVNQSVRGTATAGALVNLCLASGNLGPGTGPFSLTGQANSMGTRVCSSKGTWSGHRPFEHPDHRRAVAEAWDVPVSRLPDDSGPGPVGILDSSPSVVWTVATNPLAGFPDATAAREVLRDSFLVVQDAFRSDTVELADVVLPAATWGESEGTAMNMERTVSRIRAATETPPGVRQDLDIIADVAARVAPGLLPRPPVSPSAIFDEFAALTEGTDADCSGISYTRLDGERAVRWPAPEPNSDAGYRYYDPSTSRWTFPTPSGKARFSTLDGEPLPEPVDGDYPLTLTTGREADGYNTGVRSRSDTPEEPVARVNPETVDTYHDAVADTDGELRTTVVSRRASVSVTLDRDDAVPPGLVWLSIHHPMTNQLTSPAVDPQSNEPNFKQCAVRFVHPDAPAKADFLAAEVSD
|
anaerobic respiration nitrate assimilation
|
periplasmic space; plasma membrane
|
4 iron, 4 sulfur cluster binding metal ion binding oxidoreductase activity
|
Haloferax mediterranei
|
4Fe-4S Cell membrane Electron transport Iron Iron-sulfur Membrane Metal-binding Nitrate assimilation Oxidoreductase Plasmid Repeat Transport
|
MSTDSDAETV
|
MSTDSDAETVDLADGVDHQVAMVMDLNKCIGCQTCTVACKSLWTEGGGRDYMYWNNVETKPGKGYPRNWEESGGGWKSSEHKERKPGQIPDKEDYGDAWEFNHEEIMYNGSDRPLRPDSDPEWGPNWDEDQGTGEYPNSYYFYLPRICNHCTHPSCVEACPRKAIYKREEDGIVLIDQERCRGYRYCVEGCPYKKVYYNATQKTSEKCIFCYPRIEGEGPDGKTFAPACAEDCPPQLRLVGFLDDEQGPIHKLVEEYEVALPLHPEYQTQPNVYYIPPFAPPQHSEDGESVDVDRIPRNYLEELFGERVHDALDTIEREREKVNRGGGSELLDMLTDTNPARKFRLEVFDDD
|
anaerobic respiration nitrate assimilation periplasmic space; plasma membrane 4 iron, 4 sulfur cluster binding metal ion binding oxidoreductase activity Haloferax mediterranei 4Fe-4S Cell membrane Electron transport Iron Iron-sulfur Membrane Metal-binding Nitrate assimilation Oxidoreductase Plasmid Repeat Transport MSTDSDAETV MSTDSDAETVDLADGVDHQVAMVMDLNKCIGCQTCTVACKSLWTEGGGRDYMYWNNVETKPGKGYPRNWEESGGGWKSSEHKERKPGQIPDKEDYGDAWEFNHEEIMYNGSDRPLRPDSDPEWGPNWDEDQGTGEYPNSYYFYLPRICNHCTHPSCVEACPRKAIYKREEDGIVLIDQERCRGYRYCVEGCPYKKVYYNATQKTSEKCIFCYPRIEGEGPDGKTFAPACAEDCPPQLRLVGFLDDEQGPIHKLVEEYEVALPLHPEYQTQPNVYYIPPFAPPQHSEDGESVDVDRIPRNYLEELFGERVHDALDTIEREREKVNRGGGSELLDMLTDTNPARKFRLEVFDDD
|
nitrate assimilation
|
plasma membrane
|
4 iron, 4 sulfur cluster binding metal ion binding molybdopterin cofactor binding oxidoreductase activity
|
Haloferax mediterranei
|
4Fe-4S Cell membrane Electron transport Iron Iron-sulfur Membrane Metal-binding Molybdenum Nitrate assimilation Oxidoreductase Plasmid Signal Transport
|
MSRNDASQLD
|
MSRNDASQLDDGETTAESPPDDQANDAPEVGDPPGDPVDADSGVSRRTFLEGIGVASLLGIGTSAASDDSLFQMGGLKPVDDPIGNYPYRDWEDLYREKWDWDSVSRSTHSVNCTGSCSWNVYVKNGQVWREEQSGDYPRFDESLPDPNPRGCQKGACYTDYVNADQRIKHPLKRVGERGEGKWKRISWDEALTEIAEHVVDEVEAGRYDAISGFTPIPAMSPVSFASGSRLVNLLGGVSHSFYDWYSDLPPGQPITWGTQTDNAESADWYNADYIIAWGSNINVTRIPDAKYFLESGYNGTKRVGVFTDYSQTAIHTDEWLSPDSGTDTALALGMAQTIVDEGLYDEAHLKEQTDMPLLVRQDTGKFLRASDVPSVNTDADRPEWMLLMLDSNGRIREAPGSLGERDGQKDYSKSIELDFDPQLDGETTVQTQSGRVQVRTVWAELRDELANWDPEMVHEETTVGKETYQRIAREFAEADKAKIIQGKGVNDWYHNDLGNRALQLLVTLTGNLGEQGTGLDHYVGQEKIWTFHGWKTLSFPTGKVRGVPTTLWTYYHAGILDNTDPDTAAKIRESIDKGWMPVYPEERDNGSRPDPTTMFVWRGNYFNQAKGNVAVEEQLWPKLDLVVDINFRMDSTAMYSDIVLPTASHYEKHDLSMTDMHTYVHPFTPAVEPLGESKTDWQIFRELAQKIQEVATERGVEPISDRKFDREIDLQSVYDDYVRDWETGEEGALAEDRAACEYILEHSEESNPADSDEQITFADTVEQPQRLLEAGDHWTSDIEDGEAYAPWKDFVQDKNPWPTVTGRQQYYIDHDWFLELGEELPTHKEGPENTGGDYPMEYNTPHGRWAIHSTWRDSEKLLRLQRGEPLLYLHPEDAEERGIEDGDSVEVFNDLAEVELQAKIYPSSQRGTARMYFAWERFQFDSDSNFNSLVPMYMKPTQLVQYPEDSGEHLHFFPNYWGPTGVNSDVRVDVRKAGGGDE
|
nitrate assimilation plasma membrane 4 iron, 4 sulfur cluster binding metal ion binding molybdopterin cofactor binding oxidoreductase activity Haloferax mediterranei 4Fe-4S Cell membrane Electron transport Iron Iron-sulfur Membrane Metal-binding Molybdenum Nitrate assimilation Oxidoreductase Plasmid Signal Transport MSRNDASQLD MSRNDASQLDDGETTAESPPDDQANDAPEVGDPPGDPVDADSGVSRRTFLEGIGVASLLGIGTSAASDDSLFQMGGLKPVDDPIGNYPYRDWEDLYREKWDWDSVSRSTHSVNCTGSCSWNVYVKNGQVWREEQSGDYPRFDESLPDPNPRGCQKGACYTDYVNADQRIKHPLKRVGERGEGKWKRISWDEALTEIAEHVVDEVEAGRYDAISGFTPIPAMSPVSFASGSRLVNLLGGVSHSFYDWYSDLPPGQPITWGTQTDNAESADWYNADYIIAWGSNINVTRIPDAKYFLESGYNGTKRVGVFTDYSQTAIHTDEWLSPDSGTDTALALGMAQTIVDEGLYDEAHLKEQTDMPLLVRQDTGKFLRASDVPSVNTDADRPEWMLLMLDSNGRIREAPGSLGERDGQKDYSKSIELDFDPQLDGETTVQTQSGRVQVRTVWAELRDELANWDPEMVHEETTVGKETYQRIAREFAEADKAKIIQGKGVNDWYHNDLGNRALQLLVTLTGNLGEQGTGLDHYVGQEKIWTFHGWKTLSFPTGKVRGVPTTLWTYYHAGILDNTDPDTAAKIRESIDKGWMPVYPEERDNGSRPDPTTMFVWRGNYFNQAKGNVAVEEQLWPKLDLVVDINFRMDSTAMYSDIVLPTASHYEKHDLSMTDMHTYVHPFTPAVEPLGESKTDWQIFRELAQKIQEVATERGVEPISDRKFDREIDLQSVYDDYVRDWETGEEGALAEDRAACEYILEHSEESNPADSDEQITFADTVEQPQRLLEAGDHWTSDIEDGEAYAPWKDFVQDKNPWPTVTGRQQYYIDHDWFLELGEELPTHKEGPENTGGDYPMEYNTPHGRWAIHSTWRDSEKLLRLQRGEPLLYLHPEDAEERGIEDGDSVEVFNDLAEVELQAKIYPSSQRGTARMYFAWERFQFDSDSNFNSLVPMYMKPTQLVQYPEDSGEHLHFFPNYWGPTGVNSDVRVDVRKAGGGDE
|
proteolysis
|
extracellular region
|
serine-type endopeptidase activity toxin activity
|
Gloydius halys
|
3D-structure Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin
|
IIGGDECNIN
|
IIGGDECNINEHRFLVALYTSRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSKHIAPFSLPSSPPSVGSVCRIMGWGRISPTEGTYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCKGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP
|
proteolysis extracellular region serine-type endopeptidase activity toxin activity Gloydius halys 3D-structure Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin IIGGDECNIN IIGGDECNINEHRFLVALYTSRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSKHIAPFSLPSSPPSVGSVCRIMGWGRISPTEGTYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCKGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP
|
defense response
|
chloroplast
|
hydrolase activity lyase activity
|
Tulipa gesneriana
|
Chloroplast Direct protein sequencing Lyase Plant defense Plastid Transit peptide
|
MSVASFFSSL
|
MSVASFFSSLPARPFGYKDGRGRTGMVPTTDIGRRMVKPPVLACRPIESNTYHGSVTSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPSLAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWRGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
|
defense response chloroplast hydrolase activity lyase activity Tulipa gesneriana Chloroplast Direct protein sequencing Lyase Plant defense Plastid Transit peptide MSVASFFSSL MSVASFFSSLPARPFGYKDGRGRTGMVPTTDIGRRMVKPPVLACRPIESNTYHGSVTSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPSLAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWRGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
|
defense response
|
chloroplast
|
hydrolase activity lyase activity
|
Tulipa gesneriana
|
Chloroplast Direct protein sequencing Lyase Plant defense Plastid Transit peptide
|
MSVASFFSSL
|
MSVASFFSSLPARPFGYKDGRGRTGMVSTTDIGRRMVKPPVLACRPIESNTYHGSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPILAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWGGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
|
defense response chloroplast hydrolase activity lyase activity Tulipa gesneriana Chloroplast Direct protein sequencing Lyase Plant defense Plastid Transit peptide MSVASFFSSL MSVASFFSSLPARPFGYKDGRGRTGMVSTTDIGRRMVKPPVLACRPIESNTYHGSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPILAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWGGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
|
arachidonic acid secretion defense response to bacterium lipid catabolic process phospholipid metabolic process
|
extracellular region
|
calcium ion binding phospholipase A2 activity toxin activity
|
Bothrops brazili
|
3D-structure Antibiotic Antimicrobial Direct protein sequencing Disulfide bond Myotoxin Secreted Toxin
|
SLFQLGKMIL
|
SLFQLGKMILQETGKNPAASYGAYGCNCGVLGRGKPKDATDRCCYVHKCCKKKLTGCDPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENLNTYNKKYRYHLKPFCKKADPC
|
arachidonic acid secretion defense response to bacterium lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrops brazili 3D-structure Antibiotic Antimicrobial Direct protein sequencing Disulfide bond Myotoxin Secreted Toxin SLFQLGKMIL SLFQLGKMILQETGKNPAASYGAYGCNCGVLGRGKPKDATDRCCYVHKCCKKKLTGCDPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENLNTYNKKYRYHLKPFCKKADPC
|
chiasma assembly homologous chromosome pairing at meiosis protein ubiquitination reciprocal meiotic recombination
|
chiasma; chromosome
|
metal ion binding transferase activity
|
Oryza sativa subsp. japonica
|
Alternative splicing Chromosome Coiled coil DNA recombination Meiosis Metal-binding Nucleus Reference proteome Transferase Ubl conjugation pathway Zinc Zinc-finger
|
MKCNACWREL
|
MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT
|
chiasma assembly homologous chromosome pairing at meiosis protein ubiquitination reciprocal meiotic recombination chiasma; chromosome metal ion binding transferase activity Oryza sativa subsp. japonica Alternative splicing Chromosome Coiled coil DNA recombination Meiosis Metal-binding Nucleus Reference proteome Transferase Ubl conjugation pathway Zinc Zinc-finger MKCNACWREL MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT
|
multi-pass transmembrane protein insertion into ER membrane protein localization to nuclear inner membrane regulation of apoptotic process regulation of cytokine production regulation of mononuclear cell proliferation regulation of nitric oxide biosynthetic process regulation of phagocytosis
|
endoplasmic reticulum membrane; multi-pass translocon complex; nuclear membrane; plasma membrane
|
ribosome binding
|
Capra hircus
|
Cell membrane Endoplasmic reticulum Membrane Nucleus Reference proteome Transmembrane Transmembrane helix
|
MTLFHFGNCF
|
MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTYRPAVLLLMFLSVYKAFVMETFVHLCSLGSWTALLARALVTGLLALSTLALYVAVVNVHS
|
multi-pass transmembrane protein insertion into ER membrane protein localization to nuclear inner membrane regulation of apoptotic process regulation of cytokine production regulation of mononuclear cell proliferation regulation of nitric oxide biosynthetic process regulation of phagocytosis endoplasmic reticulum membrane; multi-pass translocon complex; nuclear membrane; plasma membrane ribosome binding Capra hircus Cell membrane Endoplasmic reticulum Membrane Nucleus Reference proteome Transmembrane Transmembrane helix MTLFHFGNCF MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTYRPAVLLLMFLSVYKAFVMETFVHLCSLGSWTALLARALVTGLLALSTLALYVAVVNVHS
|
cannabinoid biosynthetic process olivetolic acid biosynthetic process terpenoid biosynthetic process
|
cytoplasm
|
cyclase activity lyase activity metal ion binding
|
Cannabis sativa
|
3D-structure Cytoplasm Lyase Magnesium Metal-binding
|
MAVKHLIVLK
|
MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK
|
cannabinoid biosynthetic process olivetolic acid biosynthetic process terpenoid biosynthetic process cytoplasm cyclase activity lyase activity metal ion binding Cannabis sativa 3D-structure Cytoplasm Lyase Magnesium Metal-binding MAVKHLIVLK MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK
|
dephosphorylation suppression by symbiont of host inflammatory response symbiont-mediated suppression of host defense-related programmed cell death
|
extracellular region; host cell cytoplasm; host cell plasma membrane; membrane
|
myosin phosphatase activity phosphatase activity phosphatidylinositol-4,5-bisphosphate phosphatase activity phosphatidylinositol-4-phosphate phosphatase activity protein tyrosine phosphatase activity ubiquitin binding
|
Mycobacterium tuberculosis
|
3D-structure Host cell membrane Host cytoplasm Host membrane Hydrolase Membrane Protein phosphatase Reference proteome Secreted Virulence
|
MAVRELPGAW
|
MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
|
dephosphorylation suppression by symbiont of host inflammatory response symbiont-mediated suppression of host defense-related programmed cell death extracellular region; host cell cytoplasm; host cell plasma membrane; membrane myosin phosphatase activity phosphatase activity phosphatidylinositol-4,5-bisphosphate phosphatase activity phosphatidylinositol-4-phosphate phosphatase activity protein tyrosine phosphatase activity ubiquitin binding Mycobacterium tuberculosis 3D-structure Host cell membrane Host cytoplasm Host membrane Hydrolase Membrane Protein phosphatase Reference proteome Secreted Virulence MAVRELPGAW MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
|
DNA repair DNA replication nucleoside phosphate metabolic process ribose phosphate metabolic process
|
cytosol
|
8-oxo-dGDP phosphatase activity 8-oxo-GDP phosphatase activity ADP-ribose diphosphatase activity metal ion binding
|
Mycobacterium tuberculosis
|
3D-structure DNA damage DNA repair DNA replication Hydrolase Magnesium Manganese Metal-binding Reference proteome
|
MAEHDFETIS
|
MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER
|
DNA repair DNA replication nucleoside phosphate metabolic process ribose phosphate metabolic process cytosol 8-oxo-dGDP phosphatase activity 8-oxo-GDP phosphatase activity ADP-ribose diphosphatase activity metal ion binding Mycobacterium tuberculosis 3D-structure DNA damage DNA repair DNA replication Hydrolase Magnesium Manganese Metal-binding Reference proteome MAEHDFETIS MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER
|
rRNA methylation
|
extracellular region; host cell cytoplasm; host cell nucleolus
|
methyltransferase activity nucleic acid binding
|
Mycobacterium tuberculosis
|
3D-structure Host cytoplasm Host nucleus Methyltransferase Reference proteome rRNA processing S-adenosyl-L-methionine Secreted Transferase Virulence
|
MTRIIGGVAG
|
MTRIIGGVAGGRRIAVPPRGTRPTTDRVRESLFNIVTARRDLTGLAVLDLYAGSGALGLEALSRGAASVLFVESDQRSAAVIARNIEALGLSGATLRRGAVAAVVAAGTTSPVDLVLADPPYNVDSADVDAILAALGTNGWTREGTVAVVERATTCAPLTWPEGWRRWPQRVYGDTRLELAERLFANV
|
rRNA methylation extracellular region; host cell cytoplasm; host cell nucleolus methyltransferase activity nucleic acid binding Mycobacterium tuberculosis 3D-structure Host cytoplasm Host nucleus Methyltransferase Reference proteome rRNA processing S-adenosyl-L-methionine Secreted Transferase Virulence MTRIIGGVAG MTRIIGGVAGGRRIAVPPRGTRPTTDRVRESLFNIVTARRDLTGLAVLDLYAGSGALGLEALSRGAASVLFVESDQRSAAVIARNIEALGLSGATLRRGAVAAVVAAGTTSPVDLVLADPPYNVDSADVDAILAALGTNGWTREGTVAVVERATTCAPLTWPEGWRRWPQRVYGDTRLELAERLFANV
|
folic acid biosynthetic process folic acid-containing compound biosynthetic process response to antibiotic tetrahydrofolate biosynthetic process
|
cytoplasm
|
ATP binding dihydrofolate synthase activity metal ion binding tetrahydrofolylpolyglutamate synthase activity
|
Mycobacterium tuberculosis
|
3D-structure Antibiotic resistance ATP-binding Folate biosynthesis Ligase Magnesium Metal-binding Nucleotide-binding Reference proteome
|
MNSTNSGPPD
|
MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGERFGPDRVRTAENLRDAIDVATSLVDDAAADPDVAGDAFSRTGIVITGSVVTAGAARTLFGRDPQ
|
folic acid biosynthetic process folic acid-containing compound biosynthetic process response to antibiotic tetrahydrofolate biosynthetic process cytoplasm ATP binding dihydrofolate synthase activity metal ion binding tetrahydrofolylpolyglutamate synthase activity Mycobacterium tuberculosis 3D-structure Antibiotic resistance ATP-binding Folate biosynthesis Ligase Magnesium Metal-binding Nucleotide-binding Reference proteome MNSTNSGPPD MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGERFGPDRVRTAENLRDAIDVATSLVDDAAADPDVAGDAFSRTGIVITGSVVTAGAARTLFGRDPQ
|
lipid catabolic process
|
cell surface; cytoplasm; extracellular region
|
acetylesterase activity triglyceride lipase activity
|
Mycobacterium tuberculosis
|
Cell wall Cytoplasm Hydrolase Lipid degradation Lipid metabolism Reference proteome Secreted Virulence
|
MVSYVVALPE
|
MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA
|
lipid catabolic process cell surface; cytoplasm; extracellular region acetylesterase activity triglyceride lipase activity Mycobacterium tuberculosis Cell wall Cytoplasm Hydrolase Lipid degradation Lipid metabolism Reference proteome Secreted Virulence MVSYVVALPE MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA
|
cell wall macromolecule catabolic process cell wall organization peptidoglycan catabolic process
|
outer membrane-bounded periplasmic space
|
metal ion binding N-acetylmuramoyl-L-alanine amidase activity
|
Mycobacterium tuberculosis
|
3D-structure Cell wall biogenesis/degradation Disulfide bond Hydrolase Metal-binding Periplasm Reference proteome Signal Zinc
|
MIVGVLVAAA
|
MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR
|
cell wall macromolecule catabolic process cell wall organization peptidoglycan catabolic process outer membrane-bounded periplasmic space metal ion binding N-acetylmuramoyl-L-alanine amidase activity Mycobacterium tuberculosis 3D-structure Cell wall biogenesis/degradation Disulfide bond Hydrolase Metal-binding Periplasm Reference proteome Signal Zinc MIVGVLVAAA MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR
|
cell wall organization peptidoglycan-protein cross-linking regulation of cell shape
|
plasma membrane
|
acyltransferase activity metal ion binding peptidoglycan L,D-transpeptidase activity
|
Mycobacterium tuberculosis
|
3D-structure Acyltransferase Calcium Cell membrane Cell shape Cell wall biogenesis/degradation Lipoprotein Membrane Metal-binding Palmitate Peptidoglycan synthesis Reference proteome Signal Transferase
|
MPKVGIAAQA
|
MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
|
cell wall organization peptidoglycan-protein cross-linking regulation of cell shape plasma membrane acyltransferase activity metal ion binding peptidoglycan L,D-transpeptidase activity Mycobacterium tuberculosis 3D-structure Acyltransferase Calcium Cell membrane Cell shape Cell wall biogenesis/degradation Lipoprotein Membrane Metal-binding Palmitate Peptidoglycan synthesis Reference proteome Signal Transferase MPKVGIAAQA MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
|
carbohydrate metabolic process propionate metabolic process, methylcitrate cycle tricarboxylic acid cycle
|
cytoplasm
|
2-methylcitrate synthase activity citrate (Si)-synthase activity citrate synthase activity
|
Mycobacterium tuberculosis
|
3D-structure Reference proteome Transferase Tricarboxylic acid cycle
|
MTGPLAAARS
|
MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
|
carbohydrate metabolic process propionate metabolic process, methylcitrate cycle tricarboxylic acid cycle cytoplasm 2-methylcitrate synthase activity citrate (Si)-synthase activity citrate synthase activity Mycobacterium tuberculosis 3D-structure Reference proteome Transferase Tricarboxylic acid cycle MTGPLAAARS MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
|
positive regulation of cell population proliferation protein modification process
|
cytoplasm; protein-containing complex
|
ATP binding biotin binding biotin- ligase activity protein homodimerization activity
|
Mycobacterium tuberculosis
|
3D-structure ATP-binding Biotin Ligase Nucleotide-binding Reference proteome
|
MTDRDRLRPP
|
MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR
|
positive regulation of cell population proliferation protein modification process cytoplasm; protein-containing complex ATP binding biotin binding biotin- ligase activity protein homodimerization activity Mycobacterium tuberculosis 3D-structure ATP-binding Biotin Ligase Nucleotide-binding Reference proteome MTDRDRLRPP MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR
|
phosphorelay signal transduction system
|
cytoplasm; protein-DNA complex
|
DNA-binding transcription activator activity transcription cis-regulatory region binding
|
Pseudomonas putida
|
Activator Cytoplasm DNA-binding Phosphoprotein Transcription Transcription regulation Two-component regulatory system
|
MPARWGCLFP
|
MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
|
phosphorelay signal transduction system cytoplasm; protein-DNA complex DNA-binding transcription activator activity transcription cis-regulatory region binding Pseudomonas putida Activator Cytoplasm DNA-binding Phosphoprotein Transcription Transcription regulation Two-component regulatory system MPARWGCLFP MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
|
adaptive immune response cellular response to ionomycin innate immune response natural killer cell differentiation negative regulation of type II interferon production NK T cell differentiation regulation of extrathymic T cell differentiation regulation of gene expression regulation of natural killer cell differentiation regulation of natural killer cell differentiation involved in immune response regulation of NK T cell differentiation regulation of transcription by RNA polymerase II T cell receptor signaling pathway
|
nucleus
|
DNA-binding transcription factor activity metal ion binding promoter-specific chromatin binding RNA polymerase II cis-regulatory region sequence-specific DNA binding
|
Mus musculus
|
Adaptive immunity DNA-binding Immunity Innate immunity Metal-binding Nucleus Reference proteome Repeat Transcription Transcription regulation Zinc Zinc-finger
|
MKALDGLRES
|
MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHLRVHSGERPFQCALCQKRFTQLAHLQKHHLVHTGERPHQCQVCHKRFSSSSNLKTHLRLHSGAKPSQCGLCPSYLTPNVYPKLHHRLRAPQLRGLTHTHLPLASLTCLAQWHQGALDLVEKKMGWTVDKVSSESKGKQG
|
adaptive immune response cellular response to ionomycin innate immune response natural killer cell differentiation negative regulation of type II interferon production NK T cell differentiation regulation of extrathymic T cell differentiation regulation of gene expression regulation of natural killer cell differentiation regulation of natural killer cell differentiation involved in immune response regulation of NK T cell differentiation regulation of transcription by RNA polymerase II T cell receptor signaling pathway nucleus DNA-binding transcription factor activity metal ion binding promoter-specific chromatin binding RNA polymerase II cis-regulatory region sequence-specific DNA binding Mus musculus Adaptive immunity DNA-binding Immunity Innate immunity Metal-binding Nucleus Reference proteome Repeat Transcription Transcription regulation Zinc Zinc-finger MKALDGLRES MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHLRVHSGERPFQCALCQKRFTQLAHLQKHHLVHTGERPHQCQVCHKRFSSSSNLKTHLRLHSGAKPSQCGLCPSYLTPNVYPKLHHRLRAPQLRGLTHTHLPLASLTCLAQWHQGALDLVEKKMGWTVDKVSSESKGKQG
|
ATP transport protein heterooligomerization response to stimulus sensory perception of taste
|
basolateral plasma membrane; plasma membrane
|
monoatomic cation channel activity voltage-gated monoatomic ion channel activity
|
Mus musculus
|
Cell membrane Ion channel Ion transport Membrane Reference proteome Sensory transduction Taste Transmembrane Transmembrane helix Transport
|
MDRFRMLFQH
|
MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAASPRRWGPGLNHRAPIAAPGTKLCHQLNV
|
ATP transport protein heterooligomerization response to stimulus sensory perception of taste basolateral plasma membrane; plasma membrane monoatomic cation channel activity voltage-gated monoatomic ion channel activity Mus musculus Cell membrane Ion channel Ion transport Membrane Reference proteome Sensory transduction Taste Transmembrane Transmembrane helix Transport MDRFRMLFQH MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAASPRRWGPGLNHRAPIAAPGTKLCHQLNV
|
cellular aldehyde metabolic process
|
cytoplasm; plasma membrane
|
3-chloroallyl aldehyde dehydrogenase activity aldehyde dehydrogenase (NAD+) activity aldehyde dehydrogenase activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
|
Mus musculus
|
Cell membrane Lipoprotein Membrane NAD Oxidoreductase Prenylation Reference proteome
|
MSTKGKHPRA
|
MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGVGSSGMGRYHGKFSFDTFSNQRACLLSCPGMEKLNGLRYPPYSPRRQQLLRWAIGSESCTLL
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cellular aldehyde metabolic process cytoplasm; plasma membrane 3-chloroallyl aldehyde dehydrogenase activity aldehyde dehydrogenase (NAD+) activity aldehyde dehydrogenase activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity Mus musculus Cell membrane Lipoprotein Membrane NAD Oxidoreductase Prenylation Reference proteome MSTKGKHPRA MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGVGSSGMGRYHGKFSFDTFSNQRACLLSCPGMEKLNGLRYPPYSPRRQQLLRWAIGSESCTLL
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meiotic DNA double-strand break formation reciprocal meiotic recombination
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chromosome
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DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
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Mus musculus
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3D-structure Alternative splicing Chromosome Meiosis Reference proteome
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MERTALAVCE
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MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMNAQGPALLLFLFVDFQSDVPVQQAKIWGLHTLLTAHLSAILSESRSTVQQSIQSAVDQVWQLYHHDAKTQQRLQASLSVAVNSIMSVLTGSTRSSFRKTCLQALEAADTQEFGVKLHRIFYDITQHQFLKHCSCDTEQHLTPEKNISAQNTKDQHKNIAQEFPEESIGQAENKRPKRGSPNHGREESRVLGSARDRSPPKSATRDRELTEVSLTARGSQTQAAHGRAQAAEAASPAGGLEDLWLQEVSNLSEWLNPGHRS
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meiotic DNA double-strand break formation reciprocal meiotic recombination chromosome DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Mus musculus 3D-structure Alternative splicing Chromosome Meiosis Reference proteome MERTALAVCE MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMNAQGPALLLFLFVDFQSDVPVQQAKIWGLHTLLTAHLSAILSESRSTVQQSIQSAVDQVWQLYHHDAKTQQRLQASLSVAVNSIMSVLTGSTRSSFRKTCLQALEAADTQEFGVKLHRIFYDITQHQFLKHCSCDTEQHLTPEKNISAQNTKDQHKNIAQEFPEESIGQAENKRPKRGSPNHGREESRVLGSARDRSPPKSATRDRELTEVSLTARGSQTQAAHGRAQAAEAASPAGGLEDLWLQEVSNLSEWLNPGHRS
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protein processing
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cytoplasm
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cysteine-type aminopeptidase activity initiator methionyl aminopeptidase activity
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Mus musculus
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Alternative splicing Aminopeptidase Cytoplasm Hydrolase Protease Reference proteome
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MTSPCSFPLK
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MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
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protein processing cytoplasm cysteine-type aminopeptidase activity initiator methionyl aminopeptidase activity Mus musculus Alternative splicing Aminopeptidase Cytoplasm Hydrolase Protease Reference proteome MTSPCSFPLK MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
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autophagosome assembly phosphorylation piecemeal microautophagy of the nucleus protein transport regulation of autophagy reticulophagy
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Atg1/ULK1 kinase complex; autophagosome membrane; cytosol; phagophore; phagophore assembly site membrane; vacuole-isolation membrane contact site
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ATP binding protein serine kinase activity protein serine/threonine kinase activity
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Beauveria bassiana
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ATP-binding Autophagy Cytoplasm Kinase Membrane Nucleotide-binding Protein transport Reference proteome Serine/threonine-protein kinase Transferase Transport
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MTSRQEGASS
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MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENFFAHHVVTGDILGLVEDDIPKPPKRELETIRQGEALPSSPRVQMARQLSSDPRDTRSSPKSPRSSPRSSTVNSSADAAPRRQSQNAERRLSISSHNSGQGLGIQRPAPPIQSHTAPNHPRAADRSGREPQPSSLRVARQPSDVSLTEEEKAAQDVMFERDYVVVERRHVEVNALADELAANEKLGQNNSSAKSSPLQRRYTQQGSATSTTGAIPTPASRTALVAQGRAGQDRRSSYEKALSASPGSASSAISKAIQDASLRLFGYKVNTMRQKGSSPPLYQPFPAYPTPTSAGLLSDGKGSQVSDEDAKAAQAIEEFATRSDCVYGFAEVKYKQLLPMAPSMDYGLGGVSPDKGTSEEDGLTVDATVALSEEALVLYVKSLTLLARAMDIASLWWSKKTRAESSVVSQTLVQRINAVVQWVRQRFNEVLEKSEVVRLKLTEAQKLLPEDHPSNPAHQGEDSIASSAVGAKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLPGCEISYLTAIRMLEAVLDSDDEATARNISSGKEIAKDATQEGSDLDTEEAAHVRKMITMITGRLNMVRKKQQMIAEANNQAKHVSAMRRLSGDVTPRSVPSYGST
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autophagosome assembly phosphorylation piecemeal microautophagy of the nucleus protein transport regulation of autophagy reticulophagy Atg1/ULK1 kinase complex; autophagosome membrane; cytosol; phagophore; phagophore assembly site membrane; vacuole-isolation membrane contact site ATP binding protein serine kinase activity protein serine/threonine kinase activity Beauveria bassiana ATP-binding Autophagy Cytoplasm Kinase Membrane Nucleotide-binding Protein transport Reference proteome Serine/threonine-protein kinase Transferase Transport MTSRQEGASS MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENFFAHHVVTGDILGLVEDDIPKPPKRELETIRQGEALPSSPRVQMARQLSSDPRDTRSSPKSPRSSPRSSTVNSSADAAPRRQSQNAERRLSISSHNSGQGLGIQRPAPPIQSHTAPNHPRAADRSGREPQPSSLRVARQPSDVSLTEEEKAAQDVMFERDYVVVERRHVEVNALADELAANEKLGQNNSSAKSSPLQRRYTQQGSATSTTGAIPTPASRTALVAQGRAGQDRRSSYEKALSASPGSASSAISKAIQDASLRLFGYKVNTMRQKGSSPPLYQPFPAYPTPTSAGLLSDGKGSQVSDEDAKAAQAIEEFATRSDCVYGFAEVKYKQLLPMAPSMDYGLGGVSPDKGTSEEDGLTVDATVALSEEALVLYVKSLTLLARAMDIASLWWSKKTRAESSVVSQTLVQRINAVVQWVRQRFNEVLEKSEVVRLKLTEAQKLLPEDHPSNPAHQGEDSIASSAVGAKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLPGCEISYLTAIRMLEAVLDSDDEATARNISSGKEIAKDATQEGSDLDTEEAAHVRKMITMITGRLNMVRKKQQMIAEANNQAKHVSAMRRLSGDVTPRSVPSYGST
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methylation O antigen biosynthetic process phosphorylation
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plasma membrane
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ATP binding methyltransferase activity protein kinase activity
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Escherichia coli
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3D-structure ATP-binding Cell inner membrane Cell membrane Coiled coil Kinase Lipopolysaccharide biosynthesis Membrane Methyltransferase Nucleotide-binding S-adenosyl-L-methionine Transferase
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MTKDLNTLVS
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MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDMLAAGEEIDREKILGSLLRSLAALEKQGFWHDDVRPWNVMVDARQHARLIDFGSIVTTPQDCSWPTNLVQSFFVFVNELFAENKSWNGFWRSAPVHPFNLPQPWSNWLYAVWQEPVERWNFVLLLALFEKKAKLPSAEQQRGATEQWIIAQETVLLELQSRVRNESAGSEALRGQIHTLEQQMAQLQSAQDAFVEKAQQQVEVSHELTWLGENMEQLAALLQTAQAHAQADVQPELPPETAELLQRLEAANREIHHLSNENQQLRQEIEKIHRSRSWRMTKGYRYLGLQIHLLRQYGFVQRCKHFIKRVLRFVFSFMRKHPQVKHTAVNGLHKLGLYQPAYRLYRRMNPLPHSQYQADAQILSQTELQVMHPELLPPEVYEIYLKLTKNK
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methylation O antigen biosynthetic process phosphorylation plasma membrane ATP binding methyltransferase activity protein kinase activity Escherichia coli3D-structure ATP-binding Cell inner membrane Cell membrane Coiled coil Kinase Lipopolysaccharide biosynthesis Membrane Methyltransferase Nucleotide-binding S-adenosyl-L-methionine Transferase MTKDLNTLVS MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDMLAAGEEIDREKILGSLLRSLAALEKQGFWHDDVRPWNVMVDARQHARLIDFGSIVTTPQDCSWPTNLVQSFFVFVNELFAENKSWNGFWRSAPVHPFNLPQPWSNWLYAVWQEPVERWNFVLLLALFEKKAKLPSAEQQRGATEQWIIAQETVLLELQSRVRNESAGSEALRGQIHTLEQQMAQLQSAQDAFVEKAQQQVEVSHELTWLGENMEQLAALLQTAQAHAQADVQPELPPETAELLQRLEAANREIHHLSNENQQLRQEIEKIHRSRSWRMTKGYRYLGLQIHLLRQYGFVQRCKHFIKRVLRFVFSFMRKHPQVKHTAVNGLHKLGLYQPAYRLYRRMNPLPHSQYQADAQILSQTELQVMHPELLPPEVYEIYLKLTKNK
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defense response to virus
|
cytoplasm
|
hydrolase activity nucleotide binding
|
Bacillus cereus
|
3D-structure Antiviral defense Cytoplasm Hydrolase NAD Nucleotide-binding
|
MKMNPIVELF
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MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNIVSGFGLGVGSFVINGVLEELYMNQGTIDDDRLILRPFPQGKKGEEQWDKYRRDMITRTGVSIFLYGNKIDKGQVVKAKGVQSEFNISFEQNNYVVPVGATGYIAKDLWNKVNEEFETYYPGADARMKKLFGELNNEALSIEELINTIIEFVEILSN
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defense response to virus cytoplasm hydrolase activity nucleotide binding Bacillus cereus 3D-structure Antiviral defense Cytoplasm Hydrolase NAD Nucleotide-binding MKMNPIVELF MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNIVSGFGLGVGSFVINGVLEELYMNQGTIDDDRLILRPFPQGKKGEEQWDKYRRDMITRTGVSIFLYGNKIDKGQVVKAKGVQSEFNISFEQNNYVVPVGATGYIAKDLWNKVNEEFETYYPGADARMKKLFGELNNEALSIEELINTIIEFVEILSN
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de novo' IMP biosynthetic process
|
cytosol
|
IMP cyclohydrolase activity phosphoribosylaminoimidazolecarboxamide formyltransferase activity
|
Cryptococcus neoformans var. grubii serotype A
|
3D-structure Cytoplasm Hydrolase Multifunctional enzyme Purine biosynthesis Transferase
|
MSSEAPIALL
|
MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGADRMSSFGDFIALSHTVDTPTAKIISREVSDGVIAPGYEPEALEILSKKKGGKYCVLQMDPTYVPPEIETRQVYGISLQQKRNDCKIDESLFKNVVTANKDLPKSAVTDLVVATLALKYTQSNSVCYALNGTVIGLGAGQQSRIHCTRLAGDKADNWWLRHHPRVLELPFKKGTKRADKANAIDLFVTGQAFEAEGGERAQWESLFETVPEPLTKEEREKHMKELTGVACASDAFFPFPDNVHRAKRSGATYLAAPSGSIMDKECIKAADESNLVFCHTDLRLFHH
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de novo' IMP biosynthetic process cytosol IMP cyclohydrolase activity phosphoribosylaminoimidazolecarboxamide formyltransferase activity Cryptococcus neoformans var. grubii serotype A 3D-structure Cytoplasm Hydrolase Multifunctional enzyme Purine biosynthesis Transferase MSSEAPIALL MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGADRMSSFGDFIALSHTVDTPTAKIISREVSDGVIAPGYEPEALEILSKKKGGKYCVLQMDPTYVPPEIETRQVYGISLQQKRNDCKIDESLFKNVVTANKDLPKSAVTDLVVATLALKYTQSNSVCYALNGTVIGLGAGQQSRIHCTRLAGDKADNWWLRHHPRVLELPFKKGTKRADKANAIDLFVTGQAFEAEGGERAQWESLFETVPEPLTKEEREKHMKELTGVACASDAFFPFPDNVHRAKRSGATYLAAPSGSIMDKECIKAADESNLVFCHTDLRLFHH
|
removal of superoxide radicals symbiont defense to host-produced reactive oxygen species
|
cytoplasm; mitochondrion; plasma membrane raft
|
copper ion binding superoxide dismutase activity
|
Cryptococcus neoformans var. grubii serotype A
|
Antioxidant Cell membrane Copper Cytoplasm Disulfide bond Membrane Metal-binding Mitochondrion Oxidoreductase Zinc
|
MVKAVVVLKG
|
MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST
|
removal of superoxide radicals symbiont defense to host-produced reactive oxygen species cytoplasm; mitochondrion; plasma membrane raft copper ion binding superoxide dismutase activity Cryptococcus neoformans var. grubii serotype A Antioxidant Cell membrane Copper Cytoplasm Disulfide bond Membrane Metal-binding Mitochondrion Oxidoreductase Zinc MVKAVVVLKG MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST
|
cell wall chitin catabolic process cell wall organization fungal-type cell wall biogenesis polysaccharide catabolic process
|
extracellular region; fungal-type cell wall; plasma membrane; side of membrane
|
chitin binding chitin deacetylase activity metal ion binding
|
Cryptococcus neoformans var. grubii serotype A
|
Carbohydrate metabolism Cell membrane Cell wall Cell wall biogenesis/degradation Chitin degradation Chitin-binding Cobalt Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Metal-binding Polysaccharide degradation Secreted Signal
|
MIPSTAAALL
|
MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLNHELTNYTMSVFMTMFPKIKSAFNYIVPICTAYNITQPYAESNITCPNFETYISGVTNISSSTTQKDGSSSTNTASGSGAAGSASATSSSDDSSSSGGSSGSSGSNNASSGALGMFDSLSGVGLILGGVVAGVMLL
|
cell wall chitin catabolic process cell wall organization fungal-type cell wall biogenesis polysaccharide catabolic process extracellular region; fungal-type cell wall; plasma membrane; side of membrane chitin binding chitin deacetylase activity metal ion binding Cryptococcus neoformans var. grubii serotype A Carbohydrate metabolism Cell membrane Cell wall Cell wall biogenesis/degradation Chitin degradation Chitin-binding Cobalt Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Metal-binding Polysaccharide degradation Secreted Signal MIPSTAAALL MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLNHELTNYTMSVFMTMFPKIKSAFNYIVPICTAYNITQPYAESNITCPNFETYISGVTNISSSTTQKDGSSSTNTASGSGAAGSASATSSSDDSSSSGGSSGSSGSNNASSGALGMFDSLSGVGLILGGVVAGVMLL
|
cell wall chitin catabolic process cell wall organization evasion of host immune response fungal-type cell wall biogenesis polysaccharide catabolic process
|
extracellular region; fungal-type cell wall; plasma membrane; side of membrane
|
chitin binding chitin deacetylase activity metal ion binding
|
Cryptococcus neoformans var. grubii serotype A
|
Carbohydrate metabolism Cell membrane Cell wall Cell wall biogenesis/degradation Chitin degradation Chitin-binding Cobalt Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Metal-binding Polysaccharide degradation Secreted Signal Virulence
|
MFTFAAFSAL
|
MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAPKLDTGFITLEHDIYQQSVDLAVGYILPQVLANGTYQLKSIINCLGKDTSEAYIETSSNQTTTQITAATGSQSTFFQPIVGTATGAEVSAPSEATGSTAAGSAASTTSGSGASASTGAASNTSSSGSGRSATMGGALIALAAVAVGMVYVA
|
cell wall chitin catabolic process cell wall organization evasion of host immune response fungal-type cell wall biogenesis polysaccharide catabolic process extracellular region; fungal-type cell wall; plasma membrane; side of membrane chitin binding chitin deacetylase activity metal ion binding Cryptococcus neoformans var. grubii serotype A Carbohydrate metabolism Cell membrane Cell wall Cell wall biogenesis/degradation Chitin degradation Chitin-binding Cobalt Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Metal-binding Polysaccharide degradation Secreted Signal Virulence MFTFAAFSAL MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAPKLDTGFITLEHDIYQQSVDLAVGYILPQVLANGTYQLKSIINCLGKDTSEAYIETSSNQTTTQITAATGSQSTFFQPIVGTATGAEVSAPSEATGSTAAGSAASTTSGSGASASTGAASNTSSSGSGRSATMGGALIALAAVAVGMVYVA
|
iron-sulfur cluster assembly iron-sulfur cluster export from the mitochondrion
|
mitochondrial inner membrane; mitochondrial membrane
|
ABC-type transporter activity ATP binding ATP hydrolysis activity
|
Cryptococcus neoformans var. grubii serotype A
|
ATP-binding Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Transit peptide Translocase Transmembrane Transmembrane helix Transport
|
MGFGSCSRHA
|
MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLNSAIKDTPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSNSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHRLWQAQLTESTQPTDEEIERQREELEVVDEKKKQ
|
iron-sulfur cluster assembly iron-sulfur cluster export from the mitochondrion mitochondrial inner membrane; mitochondrial membrane ABC-type transporter activity ATP binding ATP hydrolysis activity Cryptococcus neoformans var. grubii serotype A ATP-binding Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Transit peptide Translocase Transmembrane Transmembrane helix Transport MGFGSCSRHA MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLNSAIKDTPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSNSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHRLWQAQLTESTQPTDEEIERQREELEVVDEKKKQ
|
removal of superoxide radicals symbiont defense to host-produced reactive oxygen species
|
cytosol; mitochondrion
|
metal ion binding superoxide dismutase activity
|
Cryptococcus neoformans var. grubii serotype A
|
Alternative splicing Antioxidant Cytoplasm Manganese Metal-binding Mitochondrion Oxidoreductase Transit peptide
|
MITAITRTAL
|
MITAITRTALPRATLRTSLATMSTIRAKHTLPPLPYAYDALEPSISAEIMNLHHTKHHQTYVNGLNAAEESLQKASADGDFKTAISLQPALKFNGGGHINHSLFWKNLAPTGSAQVKVPTSGVFYDQVQADFGGFENLKKEMNAKTAAIQGSGWGWLGYNKATKKLEIVTTPNQDPLLSHVPIIGIDIWEHAFYLQYKNVKPDYLNAIWNVINYEEAESRLKAAQ
|
removal of superoxide radicals symbiont defense to host-produced reactive oxygen species cytosol; mitochondrion metal ion binding superoxide dismutase activity Cryptococcus neoformans var. grubii serotype A Alternative splicing Antioxidant Cytoplasm Manganese Metal-binding Mitochondrion Oxidoreductase Transit peptide MITAITRTAL MITAITRTALPRATLRTSLATMSTIRAKHTLPPLPYAYDALEPSISAEIMNLHHTKHHQTYVNGLNAAEESLQKASADGDFKTAISLQPALKFNGGGHINHSLFWKNLAPTGSAQVKVPTSGVFYDQVQADFGGFENLKKEMNAKTAAIQGSGWGWLGYNKATKKLEIVTTPNQDPLLSHVPIIGIDIWEHAFYLQYKNVKPDYLNAIWNVINYEEAESRLKAAQ
|
de novo' IMP biosynthetic process purine nucleobase biosynthetic process
|
cytosol
|
ATP binding metal ion binding phosphoribosylamine-glycine ligase activity phosphoribosylformylglycinamidine cyclo-ligase activity
|
Cryptococcus neoformans var. grubii serotype A
|
3D-structure ATP-binding Cytoplasm Ligase Magnesium Manganese Metal-binding Multifunctional enzyme Nucleotide-binding Purine biosynthesis
|
MPEITAFPQP
|
MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL
|
de novo' IMP biosynthetic process purine nucleobase biosynthetic process cytosol ATP binding metal ion binding phosphoribosylamine-glycine ligase activity phosphoribosylformylglycinamidine cyclo-ligase activity Cryptococcus neoformans var. grubii serotype A 3D-structure ATP-binding Cytoplasm Ligase Magnesium Manganese Metal-binding Multifunctional enzyme Nucleotide-binding Purine biosynthesis MPEITAFPQP MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL
|
response to oxidative stress
|
cytoplasm
|
NADH-dependent peroxiredoxin activity
|
Amphibacillus xylanus
|
3D-structure Antioxidant Cytoplasm Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome
|
MSLIGTEVQP
|
MSLIGTEVQPFRAQAFQSGKDFFEVTEADLKGKWSIVVFYPADFSFVCPTELEDVQKEYAELKKLGVEVYSVSTDTHFVHKAWHENSPAVGSIEYIMIGDPSQTISRQFDVLNEETGLADRGTFIIDPDGVIQAIEINADGIGRDASTLINKVKAAQYVRENPGEVCPAKWEEGGETLKPSLDIVGKI
|
response to oxidative stress cytoplasm NADH-dependent peroxiredoxin activity Amphibacillus xylanus 3D-structure Antioxidant Cytoplasm Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome MSLIGTEVQP MSLIGTEVQPFRAQAFQSGKDFFEVTEADLKGKWSIVVFYPADFSFVCPTELEDVQKEYAELKKLGVEVYSVSTDTHFVHKAWHENSPAVGSIEYIMIGDPSQTISRQFDVLNEETGLADRGTFIIDPDGVIQAIEINADGIGRDASTLINKVKAAQYVRENPGEVCPAKWEEGGETLKPSLDIVGKI
|
defense response to virus
|
cytoplasm; nucleus
|
RNA binding translation initiation factor activity
|
Arachis hypogaea
|
Cytoplasm Disulfide bond Host-virus interaction Initiation factor Nucleus Plant defense Protein biosynthesis Reference proteome RNA-binding Translation regulation
|
MVVEDTQKSS
|
MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI
|
defense response to virus cytoplasm; nucleus RNA binding translation initiation factor activity Arachis hypogaea Cytoplasm Disulfide bond Host-virus interaction Initiation factor Nucleus Plant defense Protein biosynthesis Reference proteome RNA-binding Translation regulation MVVEDTQKSS MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI
|
biological process involved in interaction with host
|
extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane
|
metal ion binding
|
Marssonina brunnea f. sp. multigermtubi
|
Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence
|
MKYSMITLGA
|
MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL
|
biological process involved in interaction with host extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane metal ion binding Marssonina brunnea f. sp. multigermtubi Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence MKYSMITLGA MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL
|
biological process involved in interaction with host
|
extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane
|
metal ion binding
|
Marssonina brunnea f. sp. multigermtubi
|
Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence
|
MRVLKFLSLM
|
MRVLKFLSLMAMLGCTIGQSGSATPGSLHLLGGPTTTDWYPECALRCWENTKYVTKCSEDQQCLCSDVNYQNSVFQCIYSQCDTVHFGSALHHAIAQCLGTDNEVFFAIPPIPDRDALRRREDEYAAGAKLFGSGSAAGYPTESAAFPVQSANYPTDSVGGPYSPSPTASVPFPYFSLTSVTSPAAKSATTTEATRNTVPASTTAPSPSPQLYTGNASTSRATVSLTVVLTVAAVYLVL
|
biological process involved in interaction with host extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane metal ion binding Marssonina brunnea f. sp. multigermtubi Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence MRVLKFLSLM MRVLKFLSLMAMLGCTIGQSGSATPGSLHLLGGPTTTDWYPECALRCWENTKYVTKCSEDQQCLCSDVNYQNSVFQCIYSQCDTVHFGSALHHAIAQCLGTDNEVFFAIPPIPDRDALRRREDEYAAGAKLFGSGSAAGYPTESAAFPVQSANYPTDSVGGPYSPSPTASVPFPYFSLTSVTSPAAKSATTTEATRNTVPASTTAPSPSPQLYTGNASTSRATVSLTVVLTVAAVYLVL
|
biological process involved in interaction with host
|
extracellular space; host cell cytoplasm; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane
|
metal ion binding
|
Marssonina brunnea f. sp. multigermtubi
|
Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host cytoplasm Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence
|
MKFSAPVLAI
|
MKFSAPVLAIFLASASAQSTAELAAQIPSCAQTCLATAITGAGCTAGDYACQCGTSQNTITASATPCVISACTSEEALNTQRTTSQICALVAAGSASSPSASSSASASASSSASSTSGAASASASASSSASSASAAASALTLAHPIPNPSHPPSPTIQTNLRKKVRNSNRLTPASLSSVSSALVSSASSVRASASSAVSAATTAANPAATTAAGVKEEASFFIPAAVALFAVFAV
|
biological process involved in interaction with host extracellular space; host cell cytoplasm; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane metal ion binding Marssonina brunnea f. sp. multigermtubi Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host cytoplasm Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence MKFSAPVLAI MKFSAPVLAIFLASASAQSTAELAAQIPSCAQTCLATAITGAGCTAGDYACQCGTSQNTITASATPCVISACTSEEALNTQRTTSQICALVAAGSASSPSASSSASASASSSASSTSGAASASASASSSASSASAAASALTLAHPIPNPSHPPSPTIQTNLRKKVRNSNRLTPASLSSVSSALVSSASSVRASASSAVSAATTAANPAATTAAGVKEEASFFIPAAVALFAVFAV
|
biological process involved in interaction with host
|
extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane
|
metal ion binding
|
Marssonina brunnea f. sp. multigermtubi
|
Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence
|
MQFSIVVMAA
|
MQFSIVVMAALASLASAQSMDGIPTCALQCLAQAVVTGGCEASDQACQCGPAREAITAAATPCLLSACTDAADLATAASVGNGMCDKYKMGGDDAAPSPSVNTPAAAAPYPTAPAPNGTVPIGTAAAPSPTANTNETTTVATGSAPQNVAGGLAGIFGLVVAAAFAL
|
biological process involved in interaction with host extracellular space; host cell nucleus; host cell plasma membrane; plasma membrane; side of membrane metal ion binding Marssonina brunnea f. sp. multigermtubi Cell membrane Disulfide bond Glycoprotein GPI-anchor Heme Host cell membrane Host membrane Host nucleus Iron Lipoprotein Membrane Metal-binding Reference proteome Secreted Signal Virulence MQFSIVVMAA MQFSIVVMAALASLASAQSMDGIPTCALQCLAQAVVTGGCEASDQACQCGPAREAITAAATPCLLSACTDAADLATAASVGNGMCDKYKMGGDDAAPSPSVNTPAAAAPYPTAPAPNGTVPIGTAAAPSPTANTNETTTVATGSAPQNVAGGLAGIFGLVVAAAFAL
|
abscisic acid homeostasis abscisic acid-activated signaling pathway leaf senescence regulation of DNA-templated transcription regulation of reproductive fruiting body development response to abscisic acid response to absence of light
|
nucleus
|
sequence-specific DNA binding
|
Solanum lycopersicum
|
Abscisic acid signaling pathway Activator DNA-binding Nucleus Reference proteome Transcription Transcription regulation
|
MVGKNNSNHL
|
MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ
|
abscisic acid homeostasis abscisic acid-activated signaling pathway leaf senescence regulation of DNA-templated transcription regulation of reproductive fruiting body development response to abscisic acid response to absence of light nucleus sequence-specific DNA binding Solanum lycopersicum Abscisic acid signaling pathway Activator DNA-binding Nucleus Reference proteome Transcription Transcription regulation MVGKNNSNHL MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ
|
abscisic acid catabolic process abscisic acid metabolic process fruit ripening response to abscisic acid response to water deprivation sterol metabolic process
|
membrane
|
(+)-abscisic acid 8'-hydroxylase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
|
Solanum lycopersicum
|
Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix
|
MEFVSMLCLF
|
MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKVLNWQDTRQMPMTTRVIQETLRVASILSFTFREAVEDVEFEGYLIPKGWKVLPLFRNIHHSPDNFPEPEKFDPSRFEVSPKPNTFMPFGNGVHSCPGNDLAKLEILILVHHLTTKYRWSMVGPQNGIQYGPFALPQNGLPIKLSLKTSST
|
abscisic acid catabolic process abscisic acid metabolic process fruit ripening response to abscisic acid response to water deprivation sterol metabolic process membrane (+)-abscisic acid 8'-hydroxylase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Solanum lycopersicum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Transmembrane Transmembrane helix MEFVSMLCLF MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKVLNWQDTRQMPMTTRVIQETLRVASILSFTFREAVEDVEFEGYLIPKGWKVLPLFRNIHHSPDNFPEPEKFDPSRFEVSPKPNTFMPFGNGVHSCPGNDLAKLEILILVHHLTTKYRWSMVGPQNGIQYGPFALPQNGLPIKLSLKTSST
|
abscisic acid-activated signaling pathway fruit ripening negative regulation of response to water deprivation regulation of abscisic acid-activated signaling pathway response to abscisic acid seed germination
|
cytoplasm; nucleus
|
abscisic acid glucosyltransferase activity indole-3-acetate beta-glucosyltransferase activity quercetin 3-O-glucosyltransferase activity quercetin 7-O-glucosyltransferase activity
|
Solanum lycopersicum
|
Abscisic acid signaling pathway Cytoplasm Developmental protein Glycosyltransferase Nucleus Reference proteome Transferase
|
MVQPHVLLVT
|
MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQEEEKEEEKLSCMMELEKQGKIVPWCSQLEVLTHPSLGCFVSHCGWNSTLESLSSGVPVVAFPHWTDQGTNAKLIEDVWKTGVRMRVNEDGVVESDEIKRCIEIVMDGGEKGEEMRKNAQKWKELARAAVKEGGSSEVNLKAFVLQVSKSC
|
abscisic acid-activated signaling pathway fruit ripening negative regulation of response to water deprivation regulation of abscisic acid-activated signaling pathway response to abscisic acid seed germination cytoplasm; nucleus abscisic acid glucosyltransferase activity indole-3-acetate beta-glucosyltransferase activity quercetin 3-O-glucosyltransferase activity quercetin 7-O-glucosyltransferase activity Solanum lycopersicum Abscisic acid signaling pathway Cytoplasm Developmental protein Glycosyltransferase Nucleus Reference proteome Transferase MVQPHVLLVT MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQEEEKEEEKLSCMMELEKQGKIVPWCSQLEVLTHPSLGCFVSHCGWNSTLESLSSGVPVVAFPHWTDQGTNAKLIEDVWKTGVRMRVNEDGVVESDEIKRCIEIVMDGGEKGEEMRKNAQKWKELARAAVKEGGSSEVNLKAFVLQVSKSC
|
proteolysis
|
extracellular region
|
serine-type endopeptidase activity toxin activity
|
Bothrops barnetti
|
Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Signal Toxin Zymogen
|
APKELQVSYA
|
APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP
|
proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrops barnetti Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Signal Toxin Zymogen APKELQVSYA APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP
|
proteolysis
|
extracellular region
|
metal ion binding metallopeptidase activity
|
Paenibacillus alvei
|
3D-structure Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc
|
MKWDKRVVAL
|
MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN
|
proteolysis extracellular region metal ion binding metallopeptidase activity Paenibacillus alvei 3D-structure Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc MKWDKRVVAL MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN
|
aldosterone metabolic process artery smooth muscle contraction cellular response to acidic pH cellular response to aldosterone epithelial fluid transport erythrocyte homeostasis gene expression intracellular sodium ion homeostasis leukocyte activation involved in inflammatory response mucus secretion multicellular organism growth multicellular organismal-level water homeostasis neutrophil activation involved in immune response neutrophil-mediated killing of bacterium potassium ion homeostasis renal system process response to food response to xenobiotic stimulus sodium ion import across plasma membrane sodium ion transmembrane transport
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apical plasma membrane; cytoplasmic vesicle membrane; external side of plasma membrane; extracellular exosome; sodium channel complex
|
ligand-gated sodium channel activity WW domain binding
|
Pelodiscus sinensis
|
Cell membrane Cytoplasmic vesicle Ion channel Ion transport Membrane Reference proteome Sodium Sodium channel Sodium transport Transmembrane Transmembrane helix Transport
|
MNLKKYFIRV
|
MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQQDYIPYLTSTAGARLMLHEQRSFPFLKDLGIYAMSGTETSIGVLVDELERMGFPYSDCTMNGSDVPVKNLYNEYNTTYSIQACLRSCFQAQMFETCGCGHYLFPLPEGVSYCNSEDDPDWAYCYSSLRSSIGHRQFCIDSCKETCNDIQYKMTISMADWPSEASEEFQYMQHPLTYERDQSRNATLDRNGIIKLNIYFQEYNYRTISESAATTIVWLLSSLGGQFGFWMGGSVLCLIEFGEIIIDFLWITVIKISNWGKGLKQKRARAQYPDAPPTVSELVEAHINL
|
aldosterone metabolic process artery smooth muscle contraction cellular response to acidic pH cellular response to aldosterone epithelial fluid transport erythrocyte homeostasis gene expression intracellular sodium ion homeostasis leukocyte activation involved in inflammatory response mucus secretion multicellular organism growth multicellular organismal-level water homeostasis neutrophil activation involved in immune response neutrophil-mediated killing of bacterium potassium ion homeostasis renal system process response to food response to xenobiotic stimulus sodium ion import across plasma membrane sodium ion transmembrane transport apical plasma membrane; cytoplasmic vesicle membrane; external side of plasma membrane; extracellular exosome; sodium channel complex ligand-gated sodium channel activity WW domain binding Pelodiscus sinensis Cell membrane Cytoplasmic vesicle Ion channel Ion transport Membrane Reference proteome Sodium Sodium channel Sodium transport Transmembrane Transmembrane helix Transport MNLKKYFIRV MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQQDYIPYLTSTAGARLMLHEQRSFPFLKDLGIYAMSGTETSIGVLVDELERMGFPYSDCTMNGSDVPVKNLYNEYNTTYSIQACLRSCFQAQMFETCGCGHYLFPLPEGVSYCNSEDDPDWAYCYSSLRSSIGHRQFCIDSCKETCNDIQYKMTISMADWPSEASEEFQYMQHPLTYERDQSRNATLDRNGIIKLNIYFQEYNYRTISESAATTIVWLLSSLGGQFGFWMGGSVLCLIEFGEIIIDFLWITVIKISNWGKGLKQKRARAQYPDAPPTVSELVEAHINL
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defense response
|
cytoplasm; nucleus
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histone H2A acetyltransferase activity histone H3 acetyltransferase activity N-acetyltransferase activity
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Glycine max
|
Acyltransferase Cytoplasm Nucleus Plant defense Reference proteome Transferase
|
MSMLSLLRSQ
|
MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH
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defense response cytoplasm; nucleus histone H2A acetyltransferase activity histone H3 acetyltransferase activity N-acetyltransferase activity Glycine max Acyltransferase Cytoplasm Nucleus Plant defense Reference proteome Transferase MSMLSLLRSQ MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH
|
defense response to virus innate immune response positive regulation of autophagy positive regulation of canonical NF-kappaB signal transduction protein polyubiquitination regulation of protein localization regulation of viral entry into host cell
|
cytoplasm; cytosol; mitochondrion; nucleoplasm
|
identical protein binding protein homodimerization activity protein kinase binding ubiquitin protein ligase activity zinc ion binding
|
Mus musculus
|
Antiviral defense Coiled coil Cytoplasm Metal-binding Mitochondrion Reference proteome Transferase Zinc Zinc-finger
|
MASTGPTNIQ
|
MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILGSKCFSSGKHYWEVDVSEKNAWTLGVYTRKRTLRFDVRQRKGQPNGYHRYKPQNGYWVIGLQHGSKYSIFEDSSNCDPTVLNPFVATPLHRVGIFLDCEEGTVSFLNVTNHGSLIYKFSQCCFSQPAYPYFNPWDCPAPMTLCPLNS
|
defense response to virus innate immune response positive regulation of autophagy positive regulation of canonical NF-kappaB signal transduction protein polyubiquitination regulation of protein localization regulation of viral entry into host cell cytoplasm; cytosol; mitochondrion; nucleoplasm identical protein binding protein homodimerization activity protein kinase binding ubiquitin protein ligase activity zinc ion binding Mus musculus Antiviral defense Coiled coil Cytoplasm Metal-binding Mitochondrion Reference proteome Transferase Zinc Zinc-finger MASTGPTNIQ MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILGSKCFSSGKHYWEVDVSEKNAWTLGVYTRKRTLRFDVRQRKGQPNGYHRYKPQNGYWVIGLQHGSKYSIFEDSSNCDPTVLNPFVATPLHRVGIFLDCEEGTVSFLNVTNHGSLIYKFSQCCFSQPAYPYFNPWDCPAPMTLCPLNS
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isoleucine biosynthetic process leucine biosynthetic process valine biosynthetic process
|
chloroplast
|
L-isoleucine transaminase activity L-leucine transaminase activity L-leucine:2-oxoglutarate aminotransferase activity L-valine transaminase activity
|
Humulus lupulus
|
Amino-acid biosynthesis Aminotransferase Branched-chain amino acid biosynthesis Chloroplast Plastid Pyridoxal phosphate Transferase Transit peptide
|
MDCAAALLPG
|
MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRKSIIDVARTLGFQVEERLVHVDELLDADEVFCTGTAVVVSPVGSITYHGERVPYNEGGVGAVSQQLYSALTRLQMGFIKDNMNWTVELS
|
isoleucine biosynthetic process leucine biosynthetic process valine biosynthetic process chloroplast L-isoleucine transaminase activity L-leucine transaminase activity L-leucine:2-oxoglutarate aminotransferase activity L-valine transaminase activity Humulus lupulus Amino-acid biosynthesis Aminotransferase Branched-chain amino acid biosynthesis Chloroplast Plastid Pyridoxal phosphate Transferase Transit peptide MDCAAALLPG MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRKSIIDVARTLGFQVEERLVHVDELLDADEVFCTGTAVVVSPVGSITYHGERVPYNEGGVGAVSQQLYSALTRLQMGFIKDNMNWTVELS
|
isoleucine biosynthetic process leucine biosynthetic process valine biosynthetic process
|
mitochondrion
|
L-isoleucine transaminase activity L-leucine transaminase activity L-leucine:2-oxoglutarate aminotransferase activity L-valine transaminase activity
|
Humulus lupulus
|
Amino-acid biosynthesis Aminotransferase Branched-chain amino acid biosynthesis Mitochondrion Pyridoxal phosphate Transferase Transit peptide
|
MIHRGLWLHN
|
MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID
|
isoleucine biosynthetic process leucine biosynthetic process valine biosynthetic process mitochondrion L-isoleucine transaminase activity L-leucine transaminase activity L-leucine:2-oxoglutarate aminotransferase activity L-valine transaminase activity Humulus lupulus Amino-acid biosynthesis Aminotransferase Branched-chain amino acid biosynthesis Mitochondrion Pyridoxal phosphate Transferase Transit peptide MIHRGLWLHN MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID
|
positive regulation of DNA-templated transcription regulation of lignin biosynthetic process response to auxin
|
nucleus
|
DNA-binding transcription factor activity sequence-specific DNA binding transcription cis-regulatory region binding
|
Zea mays
|
Activator DNA-binding Nucleus Reference proteome Repeat Transcription Transcription regulation
|
MGRPPCCDKA
|
MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY
|
positive regulation of DNA-templated transcription regulation of lignin biosynthetic process response to auxin nucleus DNA-binding transcription factor activity sequence-specific DNA binding transcription cis-regulatory region binding Zea mays Activator DNA-binding Nucleus Reference proteome Repeat Transcription Transcription regulation MGRPPCCDKA MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY
|
plastid membrane organization polyprenol biosynthetic process response to cold
|
chloroplast; chloroplast stroma
|
2-cis,6-cis-farnesyl pyrophosphate synthase activity dehydrodolichyl diphosphate synthase activity dimethylallylcistransferase activity magnesium ion binding polyprenyltransferase activity prenyltransferase activity
|
Solanum lycopersicum
|
Chloroplast Magnesium Metal-binding Plastid Reference proteome Transferase Transit peptide
|
MNSLFVGRPI
|
MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY
|
plastid membrane organization polyprenol biosynthetic process response to cold chloroplast; chloroplast stroma 2-cis,6-cis-farnesyl pyrophosphate synthase activity dehydrodolichyl diphosphate synthase activity dimethylallylcistransferase activity magnesium ion binding polyprenyltransferase activity prenyltransferase activity Solanum lycopersicum Chloroplast Magnesium Metal-binding Plastid Reference proteome Transferase Transit peptide MNSLFVGRPI MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY
|
monoterpenoid biosynthetic process
|
cytosol
|
identical protein binding oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor protein homodimerization activity
|
Catharanthus roseus
|
3D-structure Cytoplasm NAD NADP Oxidoreductase
|
MSWWWKRSIG
|
MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVWDEIVKKNNLVPTKLKEIAAFWFADIAFCSENLISSMNKSKELGFLGFRNSMKSFVSCIDKMRDYRFIP
|
monoterpenoid biosynthetic process cytosol identical protein binding oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor protein homodimerization activity Catharanthus roseus 3D-structure Cytoplasm NAD NADP Oxidoreductase MSWWWKRSIG MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVWDEIVKKNNLVPTKLKEIAAFWFADIAFCSENLISSMNKSKELGFLGFRNSMKSFVSCIDKMRDYRFIP
|
carbohydrate derivative metabolic process chloroplast organization FAD metabolic process response to high light intensity riboflavin biosynthetic process
|
chloroplast
|
5-amino-6-(5-phosphoribosylamino)uracil reductase activity diaminohydroxyphosphoribosylaminopyrimidine deaminase activity dihydropyrimidine dehydrogenase (NADP+) activity hydrolase activity, hydrolyzing N-glycosyl compounds NADP binding
|
Zea mays
|
Chloroplast Glycosidase Hydrolase Multifunctional enzyme NADP Oxidoreductase Plastid Reference proteome Transit peptide
|
MPLPQPLLGG
|
MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQRKLAMKGVEVVEFDMLNPRAVMSYCYDRGYLAVLWECGGTLAASAISASVIHKVYAFWAPKIIGGLNAPTPVGELGMSQMTQAINLIDVSYEQIDRDMLMSGFIEPIPDLSPVIPSVEEIPSIDPEVSPYETNIISFYKTWDIFGAFSNFSPHSIQMPDENGDYFTWPTVEHYYQAHKFVGVDNPQARDIVQEIKLAKSPEEAARIGRTRQKGFPELVRTDWESTKIDVMYRAIKCKFSTYPHLTNMLLSTAGSVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEILGTVPASAEVGEAD
|
carbohydrate derivative metabolic process chloroplast organization FAD metabolic process response to high light intensity riboflavin biosynthetic process chloroplast 5-amino-6-(5-phosphoribosylamino)uracil reductase activity diaminohydroxyphosphoribosylaminopyrimidine deaminase activity dihydropyrimidine dehydrogenase (NADP+) activity hydrolase activity, hydrolyzing N-glycosyl compounds NADP binding Zea mays Chloroplast Glycosidase Hydrolase Multifunctional enzyme NADP Oxidoreductase Plastid Reference proteome Transit peptide MPLPQPLLGG MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQRKLAMKGVEVVEFDMLNPRAVMSYCYDRGYLAVLWECGGTLAASAISASVIHKVYAFWAPKIIGGLNAPTPVGELGMSQMTQAINLIDVSYEQIDRDMLMSGFIEPIPDLSPVIPSVEEIPSIDPEVSPYETNIISFYKTWDIFGAFSNFSPHSIQMPDENGDYFTWPTVEHYYQAHKFVGVDNPQARDIVQEIKLAKSPEEAARIGRTRQKGFPELVRTDWESTKIDVMYRAIKCKFSTYPHLTNMLLSTAGSVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEILGTVPASAEVGEAD
|
plastid membrane organization polyprenol biosynthetic process response to cold
|
chloroplast; chloroplast stroma
|
dehydrodolichyl diphosphate synthase activity dimethylallylcistransferase activity magnesium ion binding polyprenyltransferase activity prenyltransferase activity
|
Solanum lycopersicum
|
Chloroplast Magnesium Metal-binding Plastid Reference proteome Transferase Transit peptide
|
MNSSIVSQHF
|
MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY
|
plastid membrane organization polyprenol biosynthetic process response to cold chloroplast; chloroplast stroma dehydrodolichyl diphosphate synthase activity dimethylallylcistransferase activity magnesium ion binding polyprenyltransferase activity prenyltransferase activity Solanum lycopersicum Chloroplast Magnesium Metal-binding Plastid Reference proteome Transferase Transit peptide MNSSIVSQHF MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY
|
aggrephagy protein processing protein transport
|
cytoplasm
|
cysteine-type endopeptidase activity protein-phosphatidylethanolamide deconjugating activity
|
Caenorhabditis elegans
|
Alternative splicing Autophagy Cytoplasm Hydrolase Protease Protein transport Reference proteome Thiol protease Transport
|
MLSILPLAYS
|
MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPKTESTAKMYAEKDSTATTDDVGFSHLEELVPLPSQTADVYTKMDDSTYHCQMMLWIEYENVDPSLALAMFCETRDEFENLCETLQKTTLPASQPPMFEFLQRRPKYLPKFEPYTGVSMKIEMKEFDDIGAANVKIDDDFEVLDVHTEEEDADEDNDDDVANA
|
aggrephagy protein processing protein transport cytoplasm cysteine-type endopeptidase activity protein-phosphatidylethanolamide deconjugating activity Caenorhabditis elegansAlternative splicing Autophagy Cytoplasm Hydrolase Protease Protein transport Reference proteome Thiol protease Transport MLSILPLAYS MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPKTESTAKMYAEKDSTATTDDVGFSHLEELVPLPSQTADVYTKMDDSTYHCQMMLWIEYENVDPSLALAMFCETRDEFENLCETLQKTTLPASQPPMFEFLQRRPKYLPKFEPYTGVSMKIEMKEFDDIGAANVKIDDDFEVLDVHTEEEDADEDNDDDVANA
|
calcium ion-regulated exocytosis of neurotransmitter cellular response to calcium ion regulation of calcium ion-dependent exocytosis regulation of dopamine secretion synaptic vesicle endocytosis
|
axon; dense core granule; exocytic vesicle; plasma membrane; synaptic vesicle membrane
|
calcium ion binding calcium-dependent phospholipid binding clathrin binding phosphatidylserine binding syntaxin binding
|
Caenorhabditis elegans
|
Calcium Cytoplasmic vesicle Exocytosis Metal-binding Reference proteome Repeat
|
MWATGAIVCS
|
MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEVTLGSKHLNLPQITHACSEQWAEMMTSRRPVVQWHTLQERMEKEKKKDDD
|
calcium ion-regulated exocytosis of neurotransmitter cellular response to calcium ion regulation of calcium ion-dependent exocytosis regulation of dopamine secretion synaptic vesicle endocytosis axon; dense core granule; exocytic vesicle; plasma membrane; synaptic vesicle membrane calcium ion binding calcium-dependent phospholipid binding clathrin binding phosphatidylserine binding syntaxin binding Caenorhabditis elegansCalcium Cytoplasmic vesicle Exocytosis Metal-binding Reference proteome Repeat MWATGAIVCS MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEVTLGSKHLNLPQITHACSEQWAEMMTSRRPVVQWHTLQERMEKEKKKDDD
|
defense response to bacterium immune system process iron ion transport negative regulation of blood coagulation ossification proteolysis
|
extracellular space
|
metal ion binding serine-type peptidase activity toxin activity
|
Desmodus rotundus
|
Antibiotic Antimicrobial Blood coagulation cascade inhibiting toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Immunity Ion transport Iron Iron transport Metal-binding Osteogenesis Protease Repeat Secreted Serine protease Signal Toxin Transport
|
MKLLFLALLS
|
MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN
|
defense response to bacterium immune system process iron ion transport negative regulation of blood coagulation ossification proteolysis extracellular space metal ion binding serine-type peptidase activity toxin activity Desmodus rotundus Antibiotic Antimicrobial Blood coagulation cascade inhibiting toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Immunity Ion transport Iron Iron transport Metal-binding Osteogenesis Protease Repeat Secreted Serine protease Signal Toxin Transport MKLLFLALLS MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN
|
cellular response to virus defense response to virus innate immune response positive regulation of immune response type III interferon-mediated signaling pathway tyrosine phosphorylation of STAT protein
|
cytoplasm; extracellular space
|
cytokine activity signaling receptor binding
|
Homo sapiens
|
Alternative splicing Antiviral defense Cytokine Cytoplasm Reference proteome Secreted Signal
|
MRPSVWAAVA
|
MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL
|
cellular response to virus defense response to virus innate immune response positive regulation of immune response type III interferon-mediated signaling pathway tyrosine phosphorylation of STAT protein cytoplasm; extracellular space cytokine activity signaling receptor binding Homo sapiens Alternative splicing Antiviral defense Cytokine Cytoplasm Reference proteome Secreted Signal MRPSVWAAVA MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL
|
negative regulation of interferon-beta production viral RNA genome packaging
|
host cell endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi apparatus; ribonucleoprotein complex; viral capsid; viral nucleocapsid
|
RNA binding
|
Middle East respiratory syndrome-related coronavirus
|
3D-structure ADP-ribosylation Host Golgi apparatus Phosphoprotein Reference proteome Ribonucleoprotein RNA-binding Transcription Transcription regulation Viral nucleoprotein Virion
|
MASPAAPRAV
|
MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNNDDHGNPVYFLRYSGAIKLDPKNPNYNKWLELLEQNIDAYKTFPKKEKKQKAPKEESTDQMSEPPKEHRVQGTQRTRTRPSVQPGPMIDVNTD
|
negative regulation of interferon-beta production viral RNA genome packaging host cell endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi apparatus; ribonucleoprotein complex; viral capsid; viral nucleocapsid RNA binding Middle East respiratory syndrome-related coronavirus 3D-structure ADP-ribosylation Host Golgi apparatus Phosphoprotein Reference proteome Ribonucleoprotein RNA-binding Transcription Transcription regulation Viral nucleoprotein Virion MASPAAPRAV MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNNDDHGNPVYFLRYSGAIKLDPKNPNYNKWLELLEQNIDAYKTFPKKEKKQKAPKEESTDQMSEPPKEHRVQGTQRTRTRPSVQPGPMIDVNTD
|
potassium ion transmembrane transport protein homotetramerization
|
membrane
|
identical protein binding potassium channel activity proton channel activity
|
Chamaesiphon minutus
|
3D-structure Ion channel Ion transport Membrane Potassium Potassium channel Potassium transport Reference proteome Transmembrane Transmembrane helix Transport
|
MVEAPEQSET
|
MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA
|
potassium ion transmembrane transport protein homotetramerization membrane identical protein binding potassium channel activity proton channel activity Chamaesiphon minutus 3D-structure Ion channel Ion transport Membrane Potassium Potassium channel Potassium transport Reference proteome Transmembrane Transmembrane helix Transport MVEAPEQSET MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA
|
defense response to bacterium killing of cells of another organism lipid catabolic process
|
extracellular region
|
lyase activity metal ion binding phosphoric diester hydrolase activity toxin activity
|
Loxosceles gaucho
|
Antibiotic Antimicrobial Cytolysis Dermonecrotic toxin Direct protein sequencing Disulfide bond Hemolysis Lipid degradation Lipid metabolism Lyase Magnesium Metal-binding Secreted Toxin
|
ADNRRPIWVM
|
ADNRRPIWVMGHMVNSLAQIDEFVGLGSNSIETDVSFDKQANPEYTYHGIPCDCGRACLHSTKFNDFLKGLRKVTTPGDSKYLEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLNHYKLITGFKETLKNEGHEELLEKVGTDFSGNDDISDVQKTYNKAGVTGHVWQSDGITNCLLRGLTRVKAAVANRDSGSGIINKVYYWTVDKRQSTRDTLDANVDGIMTNYPDITVEILNEAAYKKKFRIATYEDNPWETFKG
|
defense response to bacterium killing of cells of another organism lipid catabolic process extracellular region lyase activity metal ion binding phosphoric diester hydrolase activity toxin activity Loxosceles gaucho Antibiotic Antimicrobial Cytolysis Dermonecrotic toxin Direct protein sequencing Disulfide bond Hemolysis Lipid degradation Lipid metabolism Lyase Magnesium Metal-binding Secreted Toxin ADNRRPIWVM ADNRRPIWVMGHMVNSLAQIDEFVGLGSNSIETDVSFDKQANPEYTYHGIPCDCGRACLHSTKFNDFLKGLRKVTTPGDSKYLEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLNHYKLITGFKETLKNEGHEELLEKVGTDFSGNDDISDVQKTYNKAGVTGHVWQSDGITNCLLRGLTRVKAAVANRDSGSGIINKVYYWTVDKRQSTRDTLDANVDGIMTNYPDITVEILNEAAYKKKFRIATYEDNPWETFKG
|
ammonium ion metabolic process nitrate assimilation
|
periplasmic space
|
calcium ion binding heme binding nitrite reductase (cytochrome, ammonia-forming) activity
|
Thioalkalivibrio nitratireducens
|
3D-structure Calcium Direct protein sequencing Electron transport Heme Iron Metal-binding Oxidoreductase Periplasm Signal Thioether bond Transport
|
MNDLNRLGRV
|
MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADSNVMCAQCHVEYNCNPGYQLSDGSRVGMDDRRANHFFWANVFDYKEAAQEIDFFDFRHATTGAALPKLQHPEAETFWGSVHERNGVACADCHMPKVQLENGKVYTSHSQRTPRDMMGQACLNCHAEWTEDQALYAIDYIKNYTHGKIVKSEYWLAKMIDLFPVAKRAGVSEDVLNQARELHYDAHLYWEWWTAENSVGFHNPDQARESLMTSISKSKEAVSLLNDAIDAQVASR
|
ammonium ion metabolic process nitrate assimilation periplasmic space calcium ion binding heme binding nitrite reductase (cytochrome, ammonia-forming) activity Thioalkalivibrio nitratireducens 3D-structure Calcium Direct protein sequencing Electron transport Heme Iron Metal-binding Oxidoreductase Periplasm Signal Thioether bond Transport MNDLNRLGRV MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADSNVMCAQCHVEYNCNPGYQLSDGSRVGMDDRRANHFFWANVFDYKEAAQEIDFFDFRHATTGAALPKLQHPEAETFWGSVHERNGVACADCHMPKVQLENGKVYTSHSQRTPRDMMGQACLNCHAEWTEDQALYAIDYIKNYTHGKIVKSEYWLAKMIDLFPVAKRAGVSEDVLNQARELHYDAHLYWEWWTAENSVGFHNPDQARESLMTSISKSKEAVSLLNDAIDAQVASR
|
defense response to bacterium innate immune response regulation of defense response to virus
|
extracellular region
|
DNA binding
|
Sphaenorhynchus lacteus
|
Amidation Amphibian defense peptide Antibiotic Antimicrobial Antiviral protein Cleavage on pair of basic residues Direct protein sequencing DNA-binding Immunity Innate immunity Pharmaceutical Secreted Signal
|
MAFLKKSLFL
|
MAFLKKSLFLVLFLGLVSLSMGEREKREEEEEEEEENKEEEANEEGKGESEEKRGLVGTLLGHIGKAILGG
|
defense response to bacterium innate immune response regulation of defense response to virus extracellular region DNA binding Sphaenorhynchus lacteus Amidation Amphibian defense peptide Antibiotic Antimicrobial Antiviral protein Cleavage on pair of basic residues Direct protein sequencing DNA-binding Immunity Innate immunity Pharmaceutical Secreted Signal MAFLKKSLFL MAFLKKSLFLVLFLGLVSLSMGEREKREEEEEEEEENKEEEANEEGKGESEEKRGLVGTLLGHIGKAILGG
|
defense response vasodilation
|
extracellular region
|
toxin activity
|
Agalychnis dacnicolor
|
Amphibian defense peptide Direct protein sequencing G-protein coupled receptor impairing toxin Hydroxylation Secreted Signal Toxin Vasoactive Vasodilator
|
MSFLKKSLFL
|
MSFLKKSLFLVLFLGFVSFSICEEEKREDEEEENEREENKESEEKRNQEERPPGFTPFRVD
|
defense response vasodilation extracellular region toxin activity Agalychnis dacnicolor Amphibian defense peptide Direct protein sequencing G-protein coupled receptor impairing toxin Hydroxylation Secreted Signal Toxin Vasoactive Vasodilator MSFLKKSLFL MSFLKKSLFLVLFLGFVSFSICEEEKREDEEEENEREENKESEEKRNQEERPPGFTPFRVD
|
defense response vasodilation
|
extracellular region
|
toxin activity
|
Agalychnis callidryas
|
Amphibian defense peptide Direct protein sequencing G-protein coupled receptor impairing toxin Hydroxylation Secreted Signal Toxin Vasoactive Vasodilator
|
MSFLKKSLFL
|
MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMDKESEEKRESPERPPGFTPFRVD
|
defense response vasodilation extracellular region toxin activity Agalychnis callidryas Amphibian defense peptide Direct protein sequencing G-protein coupled receptor impairing toxin Hydroxylation Secreted Signal Toxin Vasoactive Vasodilator MSFLKKSLFL MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMDKESEEKRESPERPPGFTPFRVD
|
mitochondrial fission mitochondrial large ribosomal subunit assembly mitochondrial respiratory chain complex I assembly positive regulation of mitochondrial translation
|
mitochondrial matrix; mitochondrion
|
mitochondrial large ribosomal subunit binding
|
Homo sapiens
|
3D-structure Alternative initiation Alternative splicing Direct protein sequencing Mitochondrion Reference proteome Ribosome biogenesis Translation regulation
|
MAPWSREAVL
|
MAPWSREAVLSLYRALLRQGRQLRYTDRDFYFASIRREFRKNQKLEDAEARERQLEKGLVFLNGKLGRII
|
mitochondrial fission mitochondrial large ribosomal subunit assembly mitochondrial respiratory chain complex I assembly positive regulation of mitochondrial translation mitochondrial matrix; mitochondrion mitochondrial large ribosomal subunit binding Homo sapiens 3D-structure Alternative initiation Alternative splicing Direct protein sequencing Mitochondrion Reference proteome Ribosome biogenesis Translation regulation MAPWSREAVL MAPWSREAVLSLYRALLRQGRQLRYTDRDFYFASIRREFRKNQKLEDAEARERQLEKGLVFLNGKLGRII
|
regulation of DNA-templated transcription
|
cytoplasm
|
anti-sigma factor antagonist activity metal ion binding
|
Mycobacterium tuberculosis
|
Cytoplasm Metal-binding Phosphoprotein Reference proteome Transcription Transcription regulation Zinc
|
MADPGSVGHV
|
MADPGSVGHVFRRAFSWLPAQFASQSDAPVGAPRQFRSTEHLSIEAIAAFVDGELRMNAHLRAAHHLSLCAQCAAEVDDQSRARAALRDSHPIRIPSTLLGLLSEIPRCPPEGPSKGSSGGSSQGPPDGAAAGFGDRFADGDGGNRGRQSRVRR
|
regulation of DNA-templated transcription cytoplasm anti-sigma factor antagonist activity metal ion binding Mycobacterium tuberculosis Cytoplasm Metal-binding Phosphoprotein Reference proteome Transcription Transcription regulation Zinc MADPGSVGHV MADPGSVGHVFRRAFSWLPAQFASQSDAPVGAPRQFRSTEHLSIEAIAAFVDGELRMNAHLRAAHHLSLCAQCAAEVDDQSRARAALRDSHPIRIPSTLLGLLSEIPRCPPEGPSKGSSGGSSQGPPDGAAAGFGDRFADGDGGNRGRQSRVRR
|
cell wall organization peptidoglycan biosynthetic process regulation of cell shape
|
plasma membrane
|
penicillin binding
|
Mycobacterium tuberculosis
|
3D-structure Cell membrane Cell shape Cell wall biogenesis/degradation Membrane Peptidoglycan synthesis Reference proteome Transmembrane Transmembrane helix
|
MSRAAPRRAS
|
MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQFYVQQQVQQAKNLSGAHNVSAVVLDAKTGEVLAMANDNTFDPSQDIGRQGDKQLGNPAVSSPFEPGSVNKIVAASAVIEHGLSSPDEVLQVPGSIQMGGVTVHDAWEHGVMPYTTTGVFGKSSNVGTLMLSQRVGPERYYDMLRKFGLGQRTGVGLPGESAGLVPPIDQWSGSTFANLPIGQGLSMTLLQMTGMYQAIANDGVRVPPRIIKATVAPDGSRTEEPRPDDIRVVSAQTAQTVRQMLRAVVQRDPMGYQQGTGPTAGVPGYQMAGKTGTAQQINPGCGCYFDDVYWITFAGIATADNPRYVIGIMLDNPARNSDGAPGHSAAPLFHNIAGWLMQRENVPLSPDPGPPLVLQAT
|
cell wall organization peptidoglycan biosynthetic process regulation of cell shape plasma membrane penicillin binding Mycobacterium tuberculosis 3D-structure Cell membrane Cell shape Cell wall biogenesis/degradation Membrane Peptidoglycan synthesis Reference proteome Transmembrane Transmembrane helix MSRAAPRRAS MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQFYVQQQVQQAKNLSGAHNVSAVVLDAKTGEVLAMANDNTFDPSQDIGRQGDKQLGNPAVSSPFEPGSVNKIVAASAVIEHGLSSPDEVLQVPGSIQMGGVTVHDAWEHGVMPYTTTGVFGKSSNVGTLMLSQRVGPERYYDMLRKFGLGQRTGVGLPGESAGLVPPIDQWSGSTFANLPIGQGLSMTLLQMTGMYQAIANDGVRVPPRIIKATVAPDGSRTEEPRPDDIRVVSAQTAQTVRQMLRAVVQRDPMGYQQGTGPTAGVPGYQMAGKTGTAQQINPGCGCYFDDVYWITFAGIATADNPRYVIGIMLDNPARNSDGAPGHSAAPLFHNIAGWLMQRENVPLSPDPGPPLVLQAT
|
intracellular zinc ion homeostasis zinc ion transmembrane transport
|
apical plasma membrane; plasma membrane; recycling endosome membrane
|
identical protein binding metal ion binding zinc ion sensor activity zinc ion transmembrane transporter activity
|
Pteropus alecto
|
3D-structure Cell membrane Disulfide bond Endosome Ion transport Membrane Metal-binding Reference proteome Signal Transmembrane Transmembrane helix Transport Ubl conjugation Zinc Zinc transport
|
MAILAWLEPR
|
MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQAEKYLYGSLATLLICLCSTFGLLLLTCAACSTAAHYVIQTFLGMAVGALTGDALLHLTPKVLGLHQHGGDSEHRADSHGPQTTWRLVVALSGLYVFFLFEKLCDLLLPQDPEDRKGTPRSHSGHSHGMSLQLAPRELRPPKQPHEGSRADLVAEESPELLSPEPRRKSPELRLLPYMITLGDGLHNFADGLAVGAAFASSWKTGLATSLAVFCHEVPHELGDFAALLHAGLPVSRALLLNLASGLTAFAGLYVALALGVGEESESWTLAVAIGLFLYVALCDMLPAMLNVRDPRPWLLFLLHNVGLLGGWAVLLLLSLYEDSIAL
|
intracellular zinc ion homeostasis zinc ion transmembrane transport apical plasma membrane; plasma membrane; recycling endosome membrane identical protein binding metal ion binding zinc ion sensor activity zinc ion transmembrane transporter activity Pteropus alecto 3D-structure Cell membrane Disulfide bond Endosome Ion transport Membrane Metal-binding Reference proteome Signal Transmembrane Transmembrane helix Transport Ubl conjugation Zinc Zinc transport MAILAWLEPR MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQAEKYLYGSLATLLICLCSTFGLLLLTCAACSTAAHYVIQTFLGMAVGALTGDALLHLTPKVLGLHQHGGDSEHRADSHGPQTTWRLVVALSGLYVFFLFEKLCDLLLPQDPEDRKGTPRSHSGHSHGMSLQLAPRELRPPKQPHEGSRADLVAEESPELLSPEPRRKSPELRLLPYMITLGDGLHNFADGLAVGAAFASSWKTGLATSLAVFCHEVPHELGDFAALLHAGLPVSRALLLNLASGLTAFAGLYVALALGVGEESESWTLAVAIGLFLYVALCDMLPAMLNVRDPRPWLLFLLHNVGLLGGWAVLLLLSLYEDSIAL
|
circadian rhythm green leaf volatile biosynthetic process positive regulation of DNA-templated transcription regulation of phenylpropanoid metabolic process shikimate metabolic process
|
nucleus
|
DNA-binding transcription factor activity transcription cis-regulatory region binding
|
Petunia hybrida
|
DNA-binding Nucleus Repeat Transcription Transcription regulation
|
MDKRTCNSQD
|
MDKRTCNSQDVEVRKGPWTMEEDLILINYIANHGEGVWNSLARSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQADQNMKKPSKCEQNDQKAISTSQASTGPTDTIDSYSPSSYTENTNNNMENITFQGNFPTETNENIWSMEDLWSLQLLNDATN
|
circadian rhythm green leaf volatile biosynthetic process positive regulation of DNA-templated transcription regulation of phenylpropanoid metabolic process shikimate metabolic process nucleus DNA-binding transcription factor activity transcription cis-regulatory region binding Petunia hybrida DNA-binding Nucleus Repeat Transcription Transcription regulation MDKRTCNSQD MDKRTCNSQDVEVRKGPWTMEEDLILINYIANHGEGVWNSLARSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQADQNMKKPSKCEQNDQKAISTSQASTGPTDTIDSYSPSSYTENTNNNMENITFQGNFPTETNENIWSMEDLWSLQLLNDATN
|
isoquinoline alkaloid biosynthetic process
|
membrane
|
heme binding iron ion binding methyltetrahydroprotoberberine 14-monooxygenase activity
|
Papaver somniferum
|
Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix
|
MRTESIKTNR
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MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKSTCLDMILGGSDTTTVTLTWAMSLLLNHPQVLQKAKEELETQVGKNRQVDDSDIPNLPFIQAIIKETMRLYPAGPLIERRTMEDCEVAGYQVPAGTRLLVNVWKMQRDGNVYKGDPLEFRPDRFLTSNADVDLKGQHYELIPFGAGRRICPGVSFAVQLMHLVLARLLHEFEITTVEPETKVDMAESGGLLCYKIMPLEVLIKPRLEI
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isoquinoline alkaloid biosynthetic process membrane heme binding iron ion binding methyltetrahydroprotoberberine 14-monooxygenase activity Papaver somniferum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix MRTESIKTNR MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKSTCLDMILGGSDTTTVTLTWAMSLLLNHPQVLQKAKEELETQVGKNRQVDDSDIPNLPFIQAIIKETMRLYPAGPLIERRTMEDCEVAGYQVPAGTRLLVNVWKMQRDGNVYKGDPLEFRPDRFLTSNADVDLKGQHYELIPFGAGRRICPGVSFAVQLMHLVLARLLHEFEITTVEPETKVDMAESGGLLCYKIMPLEVLIKPRLEI
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muscle cell development protein glycosylation protein O-linked mannosylation
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Golgi apparatus; Golgi membrane
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glucuronosyltransferase activity metal ion binding
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Danio rerio
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Glycoprotein Glycosyltransferase Golgi apparatus Manganese Membrane Metal-binding Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix
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MHFSKKCSVF
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MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVNLASKSSGPLEVSYTINWVDPWEPFYIGARSVPLYDESFRQYGFNRISQACELHIAGYRFSVVSNAFLLHKGFKVQGEFHSRKDEENRKNRILFRSFKESLKAKYPTSPRRC
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muscle cell development protein glycosylation protein O-linked mannosylation Golgi apparatus; Golgi membrane glucuronosyltransferase activity metal ion binding Danio rerio Glycoprotein Glycosyltransferase Golgi apparatus Manganese Membrane Metal-binding Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix MHFSKKCSVF MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVNLASKSSGPLEVSYTINWVDPWEPFYIGARSVPLYDESFRQYGFNRISQACELHIAGYRFSVVSNAFLLHKGFKVQGEFHSRKDEENRKNRILFRSFKESLKAKYPTSPRRC
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amylopectin catabolic process carbohydrate catabolic process glycogen catabolic process glycogen metabolic process starch catabolic process
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cytoplasm
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alpha-1,4-glucosidase activity alpha-amylase activity
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Haloarcula japonica
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Carbohydrate metabolism Cytoplasm Direct protein sequencing Glycosidase Hydrolase Polysaccharide degradation
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MHHPGPPRFV
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MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ
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amylopectin catabolic process carbohydrate catabolic process glycogen catabolic process glycogen metabolic process starch catabolic process cytoplasm alpha-1,4-glucosidase activity alpha-amylase activity Haloarcula japonica Carbohydrate metabolism Cytoplasm Direct protein sequencing Glycosidase Hydrolase Polysaccharide degradation MHHPGPPRFV MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ
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axon development axon guidance larval locomotory behavior neuron differentiation neuron fate specification positive regulation of transcription by RNA polymerase II regulation of gene expression regulation of transcription by RNA polymerase II synapse organization
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nucleus
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DNA-binding transcription factor activity, RNA polymerase II-specific RNA polymerase II transcription regulatory region sequence-specific DNA binding
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Caenorhabditis elegans
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Alternative splicing DNA-binding Homeobox Nucleus Reference proteome Transcription Transcription regulation
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MSDNLLNGAN
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MSDNLLNGANGASTVSQFQEKVKDLGVSLHDFTAYYPSSLDTVSASLRPISDPSSDGAFKKIKTEGLGGSVFGSSIAGVTNTPARLCSLERPESERLNSRRRHRTTFTQEQLQELDAAFQKSHYPDIYVREELARITKLNEARIQVWFQNRRAKHRKHEKQLNKAINPPHSFLSNPANTLMRQGMYPAALNRDGFWYQSYQRPMPYPTASPSYSNSFTNPIANFGHSITSFQADDEFYQKSLALRMTTTPSAATAATSLANINYQQTQPSEASTNPPSI
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axon development axon guidance larval locomotory behavior neuron differentiation neuron fate specification positive regulation of transcription by RNA polymerase II regulation of gene expression regulation of transcription by RNA polymerase II synapse organization nucleus DNA-binding transcription factor activity, RNA polymerase II-specific RNA polymerase II transcription regulatory region sequence-specific DNA binding Caenorhabditis elegansAlternative splicing DNA-binding Homeobox Nucleus Reference proteome Transcription Transcription regulation MSDNLLNGAN MSDNLLNGANGASTVSQFQEKVKDLGVSLHDFTAYYPSSLDTVSASLRPISDPSSDGAFKKIKTEGLGGSVFGSSIAGVTNTPARLCSLERPESERLNSRRRHRTTFTQEQLQELDAAFQKSHYPDIYVREELARITKLNEARIQVWFQNRRAKHRKHEKQLNKAINPPHSFLSNPANTLMRQGMYPAALNRDGFWYQSYQRPMPYPTASPSYSNSFTNPIANFGHSITSFQADDEFYQKSLALRMTTTPSAATAATSLANINYQQTQPSEASTNPPSI
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ameloblast differentiation amelogenesis negative regulation of transcription by RNA polymerase II positive regulation of transcription by RNA polymerase II regulation of transcription by RNA polymerase II
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chromatin; RNA polymerase II transcription regulator complex
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DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity, RNA polymerase II-specific DNA-binding transcription factor binding DNA-binding transcription repressor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding
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Mus musculus
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DNA-binding Nucleus Reference proteome Transcription Transcription regulation
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MNSNFCRALV
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MNSNFCRALVDRGPPGGMQLGVVAPAGQTPLAATEPLSNVPFLLYPGHSEPPYYDAYTGVFPYVPFPGAFGVYDYPFEPAFIQKRNERERQRVKCVNEGYARLRGHLPGALTEKRLSKVETLRAAIRYIKYLQELLSATPDGAPPPATSPPPAHTGHSNVPQPSSLVAESSGSPFSSSPFLESEEPSL
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ameloblast differentiation amelogenesis negative regulation of transcription by RNA polymerase II positive regulation of transcription by RNA polymerase II regulation of transcription by RNA polymerase II chromatin; RNA polymerase II transcription regulator complex DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity, RNA polymerase II-specific DNA-binding transcription factor binding DNA-binding transcription repressor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding Mus musculus DNA-binding Nucleus Reference proteome Transcription Transcription regulation MNSNFCRALV MNSNFCRALVDRGPPGGMQLGVVAPAGQTPLAATEPLSNVPFLLYPGHSEPPYYDAYTGVFPYVPFPGAFGVYDYPFEPAFIQKRNERERQRVKCVNEGYARLRGHLPGALTEKRLSKVETLRAAIRYIKYLQELLSATPDGAPPPATSPPPAHTGHSNVPQPSSLVAESSGSPFSSSPFLESEEPSL
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