ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9JLK4 | MGNCAKTPWHRGSKERWQWPGSPLGGSRPSPGPRTEEQEGTQGYSVLGSLVGPACIFLRPSIAATQLDRELRPEEIEELQIAFQEFDRDRDGYIGYRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISVGELRAALKALLGERLSQREVDEILQDIDLNGDGLVDFEEFVRMMSR | Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs . Required for the normal transfer of light signals through the retina .
Location Topology: Lipid-anchor
Sequence Mass (Da): 24223
Sequen... |
Q8HZJ4 | MAEEQGRGRHGPDPAPRPQKPPVEVLASSSGAEGPPLMRKRSSKREKGLRGSRKGPSSSGEQTPMQGPEAPGSSKNPSRTREGQEGPIPSASGLAPRRQSHRHRPGPQHDAAQRMYGPLLNRIFGKDRELGPEELDELQAAFEEFDTDHDGYIGYRDLGECMRTLGYMPTEMELIEVSQHVKMRMGGRVDFEEFVEMMGPKLREETAHMLGLRELRIAFREFDRDRDGRITVAELREAAPALLGEPLVGPELEEMLQEVDLNGDGTVDFNEFVMMLSRH | Function: May play a role in normal synaptic function, probably through regulation of Ca(2+) influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1F, shifting the activation range to more hyperpolarized voltages (By similarity).
PTM: Phosphorylated. Pho... |
P45594 | MASGVTVSDVCKTTYEEIKKDKKHRYVIFYIRDEKQIDVETVADRNAEYDQFLEDIQKCGPGECRYGLFDFEYMHQCQGTSESSKKQKLFLMSWCPDTAKVKKKMLYSSSFDALKKSLVGVQKYIQATDLSEASREAVEEKLRATDRQ | Function: Exhibits F-actin depolymerizing activity and regulates actin cytoskeleton dynamics . Required for cytokinesis in both mitotic and meiotic cells and for aster migration and separation . Promotes cell motility during ovary development and oogenesis . During larval development, required for the cell rearrangemen... |
P42495 | MGSLEAERKTTGWAARDPSGVLSPYTYTLRETGPEDVFIKIIYCGICHTDIHQIKNDLGASNYPMVPGHEVVGEVVEVGSDVTKFKVGDCVGDGTIVGCCKTCRPCKADVEQYCNKKIWSYNDVYTDGKPTQGGFSGHMVVDQKFVVKIPDGMAPEQAAPLLCAGVTVYSPLTHFGLKEISGLRGGILGLGGVGHMGVKLAKAMGHHVTVISSSDKKKEEAIDHLGADAYLVSSDATQMQEAADSLDYIIDTVPVFHPLEPYLSLLKLDGKLILMGVINTPLQFISPMVMLGRKAITGSFIGSMKETEEMLDFCNEKGIT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
Q9CAI3 | MSSSESVENECMCWAARDPSGLLSPHTITRRSVTTDDVSLTITHCGVCYADVIWSRNQHGDSKYPLVPGHEIAGIVTKVGPNVQRFKVGDHVGVGTYVNSCRECEYCNEGQEVNCAKGVFTFNGIDHDGSVTKGGYSSHIVVHERYCYKIPVDYPLESAAPLLCAGITVYAPMMRHNMNQPGKSLGVIGLGGLGHMAVKFGKAFGLSVTVFSTSISKKEEALNLLGAENFVISSDHDQMKALEKSLDFLVDTASGDHAFDPYMSLLKIAGTYVLVGFPSEIKISPANLNLGMRMLAGSVTGGTKITQQMLDFCAAHKIYP... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
P08641 | MGRRWGSPALQRFPVLVLLLLLQVCGRRCDEAAPCQPGFAAETFSFSVPQDSVAAGRELGRVSFAACSGRPWAVYVPTDTRFKVNGDGVVSTKRPLTLYGRKISFTIYAQDAMGKRHSARVTVGRHRHRRHHHNHHLQDTTPAVLTFPKHDPGFLRRQKRDWVIPPISCLENHRGPYPMRLVQIKSNKDKESKVYYSITGQGADSPPVGIFIIERETGWLEVTEQLDREKIDRYTLLSHAVSASGQPVEDPMEIIITVMDQNDNKPVFIKEVFVGYIEENAKPGTSVMTVNATDADDAVNTDNGIVSYSIVSQQPPRPHP... | Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. E-cadherin is a ligand for integrin alpha-E/beta-7.
Location Topology: Single-pass type I m... |
P12830 | MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTIN... | Function: Cadherins are calcium-dependent cell adhesion proteins . They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation ... |
P09803 | MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFT... | Function: Cadherins are calcium-dependent cell adhesion proteins . They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation ... |
Q8H859 | MAAECGSGNCDAWAARDPSGILSPYKFNRRAVQSDDVSLRITHCGVCYADVAWTRNILNNSMYPLVPGHEIAGVVTEVGADVKSFKVGDHVGVGTYVNSCRDCENCNSSLENYCSQHVFTFNGVDTDGTVTKGGYSTHIVVHERYCFKIPDGYPLEKAAPLLCAGITVYSPMMRHNMNQPGKSLGVIGLGGLGHMAVKFGKAFGLKVTVISTSESKRKEAIDLLGADNFVVSSDENQMETLKSSLNFIIDTASGDHPFDPYLTLLKVGGVMALLSFPSEIKVHPANLNLGGRSLSGSVTGGTKDIQEMINFCAANKIYPD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
P85913 | MGSLESERFVVDVAASNLDK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol (By similarity).
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + ... |
Q9SJ25 | MVDQNKAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTSRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALLPLFSLLKVNGKLVALGLPEKPLDLPIFSLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective al... |
Q13111 | MLEELECGAPGARGAATAMDCKDRPAFPVKKLIQARLPFKRLNLVPKGKADDMSDDQGTSVQSKSPDLEASLDTLENNCHVGSDIDFRPKLVNGKGPLDNFLRNRIETSIGQSTVIIDLTEDSNEQPDSLVDHNKLNSEASPSREAINGQREDTGDQQGLLKAIQNDKLAFPGETLSDIPCKTEEEGVGCGGAGRRGDSQECSPRSCPELTSGPRMCPRKEQDSWSEAGGILFKGKVPMVVLQDILAVRPPQIKSLPATPQGKNMTPESEVLESFPEEDSVLSHSSLSSPSSTSSPEGPPAPPKQHSSTSPFPTSTPLRR... | Function: Core component of the CAF-1 complex, a complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicati... |
Q9QWF0 | MLEEPEAATRTAAAVDCKDRPGFPVKRLIQARLPFKRLNLVPKEKVEEDTSPKAAVESKVPDLQLSLGTFESQCHTGSHVGLSTKLVGGQGPIDSFLRATIKPVPSVVIIDLTENCSDIPDSPEGHSELSPDTAGVVTTVEGAAKQQEHSAAELCLLETPSDITCHMEEEPGSPGDPKRTGDCQAGSLQSCPELTPGSRTCPTKELSSWSKAGDLLFIEKVPVVVLEDILATKPSIASLPMMSLDRSVTSESEILESCPEDDSILSHSSTNSSSPTSSPEGPSTPPEHRGGRSSPSTPACRVAKNFVKGSTEKGRSKLHR... | Function: Core component of the CAF-1 complex, a complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicati... |
P26949 | MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHES... | Function: A probable role in capsular biogenesis. It is likely that the caf1A molecule binds F1 antigen subunits during the extracellular secretion process.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93003
Sequence Length: 833
Subcellular Location: Cell outer membrane
|
Q9S9P2 | MSQAPNPEEEDDTIEIREVWNHNLEQEMALIEQSIDDFPYVAMDTEFPGIVCKTVTANPNPNPYSIHYEYNYDTLKANVNMLKLIQLGLTLSDEKGNLPTCGTNKQCIWQFNFREFNVISDMFALDSIELLRKSAIDLEKNNECGVDAKRFAELLMGSGVVLNDKIHWVTFHCGYDFGYLLKLLSGKELPEEISDFFDQMEKFFPVVYDIKYLMGFCTNLYGGLEKIAELLGVKRVGISHQAGSDSLLTLRTFIKMKEFFFTGSLLKYSGFLFGLDNPRLLTGSKN | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32635
Sequence Length: 286
Subcellular Location: Nucl... |
Q13112 | MKVITCEIAWHNKEPVYSLDFQHGTAGRIHRLASAGVDTNVRIWKVEKGPDGKAIVEFLSNLARHTKAVNVVRFSPTGEILASGGDDAVILLWKVNDNKEPEQIAFQDEDEAQLNKENWTVVKTLRGHLEDVYDICWATDGNLMASASVDNTAIIWDVSKGQKISIFNEHKSYVQGVTWDPLGQYVATLSCDRVLRVYSIQKKRVAFNVSKMLSGIGAEGEARSYRMFHDDSMKSFFRRLSFTPDGSLLLTPAGCVESGENVMNTTYVFSRKNLKRPIAHLPCPGKATLAVRCCPVYFELRPVVETGVELMSLPYRLVFA... | Function: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to th... |
Q9SFX6 | MKQISSGEVWRWNKEVEMNSIRDCLKHCSSIAIDTEFPGCLKETPMDASEEIRYRDMKFNVDNTHLIQLGFTLFDRRGFAKTWEINLSDFDEHKCFKNDKSIAFLKSNGLNLDKIREEGIGIDEFFRDFSQILTEKDGKITWVNFQGSYDNAYLVKGLTGGKPLPETKEEFHETVQQLLGKFVFDVKKIAESCSGLSSQFGLQRIADVLQMKRVGKAHHAGSDSELTARVFTKLTFDLLNSRKQSVRRVDHQQFQLEQQQHQQFMMTRCYIPIPMPIPRPRPVMFAAHHQNPYFGGGYFRMPVQGMNYVL | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 35923
Sequence Length: 310
Subcellular Location: Nucl... |
Q9SAI2 | MSLFLKDDSIQIREVWNDNLQEEMDLIRDVVDDFPYVAMDTEFPGIVVRPVGTFKSNADYHYETLKTNVNILKMIQLGLTFSNEQGNLPTCGTDKYCIWQFNFREFDLDSDIFALDSIELLKQSGIDLAKNTLDGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPDSQTDFFKLINVYFPTVYDIKHLMKFCNSLHGGLNKLAELLEVERVGICHQAGSDSLLTSCTFRKLKENFFVGPLHKYSGVLYGLGVENGQVAI | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31201
Sequence Length: 274
Subcellular Location: Nucl... |
Q9SKZ2 | MSLFLKDDSIQIREVWNDNLESEMALIREVVDDFPFVAMDTEFPGIVCRPVGTFKTNTEYHYETLKTNVNILKMIQLGLTFSDEKGNLPTCGTDNKYCIWQFNFREFDLESDIYATDSIELLRQSGIDFVKNNEFGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPETQTGFFEMISVYFPRVYDIKHLMKFCNSLHGGLNKLAELLDVERVGICHQAGSDSLLTSCTFRKLQENFFIGSMEKYSGVLYGLGVENGQIVH | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31543
Sequence Length: 275
Subcellular Location: Nucl... |
Q9LXM4 | MSLIEDCLRSYRFIAIDTEFPSTLRETTQHATDEERYMDMSFSVDRAKLIQLGLTLFDINGRIGGTWEINFSDFGVDDARNEKSIEFLRRNGLDLRKIREEGIRIEGFFSEMFWMLKKTRRNITWVTFHGSYDIAYLLKGFTGEALPVTSERFSKAVARVLGSVYDLKVMAGRCEGLSSRLGLETLAHEFGLNRVGTAHHAGSNNELTAMVFAKVLSPFPLFLRFGSLELRTIESEAIV | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 27213
Sequence Length: 239
Subcellular Location: Nucl... |
Q9LXM2 | MAIIKPNRDLKPDGVTVVTREVWAENLESEFELISEIIDDYPFISMDTEFPGVIFKSDLRFTNPDDLYTLLKANVDALSLIQVGLTLSDVNGNLPDLGDDLHRGFIWEFNFRDFDVARDAHAPDSIELLRRQGIDFERNCRDGVESERFAELMMSSGLVCNEEVSWVTFHSAYDFGYLMKILTRRELPGALGEFKRVMRVLFGERVYDVKHMMKFCERRLFGGLDRVARTLEVNRAVGKCHQAGSDSLLTWHAFQRMRDLYFVQDGPEKHAGVLYGLEVF | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32233
Sequence Length: 280
Subcellular Location: Nucl... |
Q9LEU4 | MAETLKEDSIMIREVWDYNLVEEFALIREIVDKFSYIAMDTEFPGVVLKPVATFKYNNDLNYRTLKENVDLLKLIQVGLTFSDENGNLPTCGTDKFCIWQFNFREFNIGEDIYASESIELLRQCGIDFKKNIEKGIDVVRFGELMMSSGIVLNDAISWVTFHGGYDFGYLVKLLTCKELPLKQADFFKLLYVYFPTVYDIKHLMTFCNGLFGGLNRLAELMGVERVGICHQAGSDSLLTLGSFRKLKERYFPGSTEKYTGVLYGLGVEDGTTTTVAN | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31533
Sequence Length: 277
Subcellular Location: Nucl... |
Q9FMS6 | MIKSEADLSDVIVIRDVWAYNLESEFDLIRGIVEDYPFISMDTEFPGVIYKADLDVLRRGNPNYLYNLLKSNVDALSLIQVGLTLSDADGNLPDLGGQKNRRYIWEFNFRDFDVERDPHAPDSIELLRRHGIDFERNRREGVESERFAELMMSSGLICNESVSWVTFHSAYDFGYLVKILTRRQLPVALREFLGLLRAFFGDRVYDVKHIMRFCEQRLYGGLDRVARSLEVNRAVGKCHQAGSDSLLTWQAFQRMRDLYFVEDGAEKHAGVLYGLEVF | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32169
Sequence Length: 278
Subcellular Location: Nucl... |
P54212 | MGSRRITLLGALFAVLAVAIEGRTLLTHNLKAEAAETVDAVSSVVAGSAGRQLLVSEPHDYNYEKVGFDWTGGVCVNTGTSKQSPINIETDSLAEESERLGTADDTSRLALKGLLSSSYQLTSEVAINLEQDMQFSFNAPDEDLPQLTIGGVVHTFKPVQIHFHHFASEHAIDGQLYPLEAHMVMASQNDGSDQLAVIGIMYKYGEEDPFLKRLQETAQSNGEAGDKNVELNSFSINVARDLLPESDLTYYGYDGSLTTPGCDERVKWHVFKEARTVSVAQLKVFSEVTLAAHPEATVTNNRVIQPLNGRKVYEYKGEPN... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 64258
Sequence Length: 589
EC: 4.2.1.1
|
O52535 | MKTSLGKAALLALSMMPVTVFASHWSYEGEGSPEHWGALNEEYKTCQNGMNQSPINIDATFKTHLSPLDTHYIDGPITLINNGHTIQAALKTTTADTITIDGTPFILQQFHFHAPSENTVHGKHYAMEMHLVHKNAKGAVAVVAVMFEQGAENTELNKLWATMPEQAEQTAKIVTQMDLNALLPIDKTYWRFSGSLTTPPCSEGVTRIVLKHPLTLSSAQLAKFSHAMHHDNNRPVQPLNGRVVIE | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 27145
Sequence Length: 246
Subcellular Location: Periplasm
EC: 4.2.1.1
|
P84537 | DELNKKVDSDETISDDGVVAHGASMDEKHDYMDNGVRHVHNGRTRRKGSEHEVDGRFTPMEARLVFHLTTPPCTESVLWVVQKDDDEHHTRREEGPHWHDTHSFKHAEDLDVHLTPEDDLEDDKRHDDTYTYEGSLTTEEVQVEGYKDEPEELEMVDNWRPAQKNKVTVYKASEH | Function: Reversible hydration of carbon dioxide. Also acts as a structural protein, having a role in calcium carbonate crystal formation in the bio-calcification process.
PTM: Glycosylated.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 20383
Sequence Length: 175
EC: 4.2.1.1
|
Q57752 | MISKNVRIAKGAVIVGDVTIGDYSSVWYNAVIRGDVDKIIIGNYSNIQDCCVVHCSKGYPTIIGDYVSIGHGAVIHGCRIEDNVLVGMNATILNGAKIGENCIIGANALVTQNKEIPPNSLVLGVPGRVVRELTEEEIKSIKENALRYVKLSETLESYK | Function: Probably reversibly hydrates carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 17174
Sequence Length: 159
EC: 4.2.1.1
|
P40881 | MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS | Cofactor: Binds 1 Zn(2+) per subunit, at the subunit interface.
Function: Reversible hydration of carbon dioxide. Important for growth on acetate . As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on... |
Q2RGM7 | MQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVNDFTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVRKDVQEPAKPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQIDDPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALGVALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTNSASDLVIGHSVMKDAIDADAVRAALKDAGLKFDCCPPAEELAKIVNVLAKAEAASSGTVRGRRNTMLDDSD... | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide a... |
Q50940 | MPRFPRTLPRLTAVLLLACTAFSAAAHGNHTHWGYTGHDSPESWGNLSEEFRLCSTGKNQSPVNITETVSGKLPAIKVNYKPSMVDVENNGHTIQVNYPEGGNTLTVNGRTYTLKQFHFHVPSENQIKGRTFPMEAHFVHLDENKQPLVLAVLYEAGKTNGRLSSIWNVMPMTAGKVKLNQPFDASTLLPKRLKYYRFAGSLTTPPCTEGVSWLVLKTYDHIDQAQAEKFTRAVGSENNRPVQPLNARVVIE | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 28085
Sequence Length: 252
Subcellular Location: Periplasm
EC: 4.2.1.1
|
P94170 | MSSTLYRRQLLKLLGMSVLGTSFSSCVTSPARAKTVNWGYIGKVGPEHWGELSPDFALCQIGRKQTPIDLQIADVKDVHSSSQDLLVTNYQPTALHLINNGKTVQVNYQPGSYLKYAHQKFELLQFHFHHFSEHRVDGKLYDMELHLVHRSKSGDLAVMGIFLQAGAFNPTLQIIWDATPQNQGTDKRIEDINIDASQFLPAQHRFFTYSGSLTTPPCSENVLWCVMATPIEASPAQIAKFSQMFPQNARPVQPLNDRLVIEAI | Function: Reversible hydration of carbon dioxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29639
Sequence Length: 264
EC: 4.2.1.1
|
Q6DAJ6 | MKGKFSIALMLSACFSASASDSVHWGYEGSGDPAHWGKLSPDFSLCETGKNQSPVNIQQALNAQHDPLQLAFQSGTQQIINNGHTVQVNVSSGNTLLLDNETFALQQFHFHAPSENEIDGKQFPLEGHFVYKNADGALTVIALMFQEGAANPQLATAWQQIPAHVDQAEDVRTPIAIQALLPTSLNYYRFSGSLTTPPCSEGIRWLVLDHPVTASAEQINQFSSVMHHANNRPIQPLNGRIIIH | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 26664
Sequence Length: 244
Subcellular Location: Periplasm
EC: 4.2.1.1
|
H8ZKW0 | MSSTALYTVPTAGPDDVAALKALDGHSASDILAVIGKTEGNGCVNDFSRTLSAAVWHPLLEDSAITVFSGGAEGVISPHVNIFVRDERQYSGHPRGLVTAVGRTRVIGPEEIGRPAQVDAVHETVVALLTELGVGPDDVHLVLIKCPLLSSDAIAGVHRRGLRPVTTDTYESMSRSRAASALGIAMALKECDRDRALLALEGRDDVWSARASASSGAELDDCHILVVAESDAAANPLRAAHTAMRDALDIQALTEVFDRIAAEGGTVRQIFAKAEADPSGAIRGYRHTMLTDSDVNATRHARAAVGGLIAALHGNGAVYV... | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide a... |
U3N9N6 | MAPIEILKFPISSPGDISPLKKLQDAGYDPSNILAVVGKTEGNGCVNDFSRTLASAVWEPRIPSDAVTIFSGGTEGVLSPHVTFFLRSPGDKETGLSAAVGHTRRFEPHEIGTDEQAQQVATTTSSLIEQMGVTPDQVHMVLIKCPLLTSEKLETIRALGRVPVTTDTYESMARSRYASAVGIAAAVGEIQHTRIPEAVSKAGTWSAKASCSSGAELEDCHILVLASTSAQGSRLHAVSRPMADAMDAASILALMELAKKDGGKIVQVFAKAEADPSGHVREWRHTMNTDSDIHSTRHARAAVGGLIAGLVSDAEIYVSG... | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide a... |
Q8XA35 | MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVVSQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEESYSYIRSGVLKHYPSVLHSEDAIEGPLAFAEKRDPVWKGR | Function: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.
Catalytic Activity: (R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O
Sequence Mass (Da): 28137
Sequence Length: 261
Pathway: Amine and polyamine metabolism; carnitine metabolism.
EC: 4.2.1.149
|
A0A1V6PAA5 | MATEKTPDWKIVDLQWAPDLGPVPVQDAMRPTRESQGEQEMIARMWVMCAIQMQDKLCAAKCTKQHFERYRSWLTAEYERFKQPGYPQVPDSRELVDMSNDARLAAMNKLREGVKNTYMWPVIEGPWRVYDNVVDIVEGRVKLVKVLLQDGLLEKFYDWANGLSEVRPLFNRMGRSNSSLRILEIGAGTGGTTARALEGLKSDDGELLYSSYEFTDISPLFFDAARRRFEGYSNIEYRALDISRNAVEQGFEAGAYDLVIASNVLHATPCLVDTLKNVRLLLKPNGFLFNQELSPPGKYVDFMVGLLPGWWLGDADGRAE... | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a b... |
A0A1V6PAN1 | MALDRYAALHVSTPQGRGDGRPTADQVLRDQDPLGSHWSDKVILITGGTAGLGAESARVLHKTGAKIFIMGRDIAKGEKVAADISASNPDYPPIEVIQMDQSRLESVREGAVEFLKRSGGKLNVLMANAGIVASPVKETQDGFEAVFAINYLSTFLLVQLLAPALVASTTPEYNSRLVVVSSAGHRASNIDPDKYNLVGEGYDPSKAYARSKTASILMANEFERRYGDRGVHALSLNPGIIMDTEISRGLPGTSASRREQYYKMEPLLAQYEKDVMQGAATQVWATVAKELEGKGGLYLDDVQVAREATHEGQFCRPGWK... | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicy... |
P0CU81 | MSDFDALLANYTSKETPKVHGVICKCVDRHGICPTPHLAKRDLRLTLLGNEIYSKVAGYDSVLPGASPLREDVVLKVASATKLITSIALLQCIDKGLIDLDEPVTKVLPEFDQKQILTDVSGSDLVLEPSKTPITARHLLTHTSGLGYPFTHRLLRLRAEVRNRAGVSPSLRVTERYEMPLVFEPGTGWLYGCSLDWAGVIVSRLHGGISLEQYFVENIWQRLGLSEPFPCFNIARHPEYNARVMGGAIQTPEGRLQPKDHWAFDNPEDQDGGSGLSCTTKDYVAVLADLVSDSPKLLKPATIAEMFTPQLEAKSPGVQM... | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bic... |
A0A1V6PAP3 | MSSPIQTAIVQTSETSAARLPLRVDRSAPIPQVKSEHHVLVRVLAVALNPNDHKMVTHFNMPDSIAGCDFCGIVTESSSNGTSLSSSAGARLPVGTRVCGALFPYSPEDPDNGSFAQYCVVDARLLVRVPDSWSDLEAASLGVGWSTISLAFSDPNALGLEGLPTQPSHRAKEPVLVYGGGTASGTLACQLLNLMGYTPIAIASNQSSELAMKYGASATACYTSKDCVDTVKSLAGKPIRRILDCITDAESAAICYSAMARSSGTYACLEECPDACRTRRIIKVKEVMGFQVLGVDIKLGDSTYTRLGDQKLMAIGIQWA... | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond:... |
Q9STD3 | MKWGVVAVLATLVVAASAKDYFKETFDGSWADRWTKSSWKVSDGSAGEFKLTAGKWYGDAEADKGIQTGPDSKFFAISAPLATVFDNTGKDTVVQFSVKHEQDLDCGGGYIKVVPATSEKQMGEFGGDTPYSIMFGPDICGYSTRKVHVILTYKGKNYLIKKDIKAETDQLTHVYTLVIKPDNTYQVLIDLKEVASGSLYEDWDMLPPKTIKDPKASKPEDWDEREEIADPEDKKPEGWDDIPATIADKDAKKPEDWDDEEDGTWEPPMIPNPEYKGEWKAKMIKNPAYKGIWVAPDIDNPDYVHDDKLYNFKDLKFVGF... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 47328
Seq... |
Q23858 | MRLLLCLIFLVFVFNFALSTVHFKDTFDNDWESRWVVSDWHKEDGKSGKLVHTAGKWFGDENQKGIQTSEDARFYAVSAKFPSFSNKGKDLVLQYTVKNEQKVDCGGSYIKLLPSKLDQSAFDGESEYSIMFGPDVCGASKRVHVILNYKGKNHLIKKEINKVETDQLTHQYTLVISPDNTYKVLVDNKEIQAGNLADDWELLPSKQIKDPKQSKPVDWVDVKEIDDPEDVKPAGHDDIPASIVDPEAVKPEDWNEEDDGEWEAPTIANPEYKGEWKAKKIPNPEYKGEWVHPLIDNPEYAEDNELYLFNDLGAIGFELW... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 48365
Seq... |
P83003 | MFTLFLLIALSSAKVYFHETFENRDKWIDSTSSGKALGPFKIVSGKWYGDANNKGLQTSEDNKFYIAAAKLDEEFSNKDKNLIVQYNLKFEQGIDCGGGYIKLLPKKSIESEEKFTPESEYNIMFGPDVCGGSKRTHVIMNYKGKNNLIRKEIKCESDDISHLYTLIIRPNNTYVVKIDGVEKQEGKFDEDWDMLAPKEIDDPNVSKPADWVDEKEIDDPNDKKPEGWDDIPKTIVDPNAKKPEEWNDEDDGEWEAPTIENPEYKGEWKPKRIPNPAYKGEWVHPQIANPDYVYDPELYKYDSFAYIGIDVWQVKAGTIY... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Plays a role ... |
Q9ZNY3 | MRKELWLGLLLSSQAVLSTIYYKETFEPDWETRWTHSTAKSDYGKFKLTSGKFYGDKAKDAGIQTSQDAKFYAISSPIASSFSNEGKDLVLQFSVKHEQDIDCGGGYLKLLPSVDAAKFTGDTPYHIMFGPDICGATKKIHFILTYKGKNLLWKKEPRCETDTLSHTYTAVIKADRTYEVLVDQVKKESGTLEEDWEILKPKTIPDPEDKKPADWVDEPDMVDPEDKKPEDWDKEPAQIPDPDATQPDDWDEEEDGKWEAPMISNPKYKGEWKAKKIPNPAYKGVWKPRDIPNPEYEADDKVHIFDEIAAVGFDLWQVKS... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 45911
Seq... |
P27797 | MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQ... | Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER . Interacts with the DNA-bindin... |
Q9SP22 | MAIRKGSSYAVAALLALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDAEDKGIQTSEDYRFYAISAEYPEFSNKDKTLVLQFSVKHEQKLDCGGGYVKLLGGDVDQKTLGGDTSYSIISRPDISRYSTKKVHTILTKDGKNHLIKKDVPCQTDQLTHVYTFIIRPDATYSILIDNEEKHTGSIYEHWDILPPKKIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDSLKY... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 47940
Seq... |
Q9SLY8 | MAIRARSSSYAAAAVALALALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDPEDKGIQTSEDYRFYAISAEYPEFSNKDKTLVLQFSVKHEQKLDCGGGYVKLLGGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHTIFTKNDKNHLIKKDVPCETDQLSHVYTLIIHPDATYTILIDNVEKQSGSIYEHWDILPPKQIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFD... | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
PTM: Phosphorylated.
Sequence... |
Q9D805 | MPYLHRSLRPQPQPVPGDARTIHSSGQSFEQLRQGCLQSGTLFEDADFPASNVSLFYSERPQVPFVWKRPGEIVEKPEFILGGATRTDICQGELGDCWLLAAIASLTLNQKALTRVVPQDQGFGSGYAGIFHFQFWQHSEWLDVVIDDRLPTFKDRLVFLHSADHNEFWSALLEKAYAKLNGSYEALKGGSAIEAMEDFTGGVAENFQIREAPEDFFEILEKALKRGSLLGCSIDTLNASESEARTSLGLIKGHAYTVTGLDQVNFHGQRIKLIRVRNPWGQVEWNGPWSDSSPEWRSVDLEEQKRLGHTALDDGEFWMA... | Function: Calcium-regulated non-lysosomal thiol-protease.
Sequence Mass (Da): 78977
Sequence Length: 690
Subcellular Location: Cytoplasm
EC: 3.4.22.-
|
D0PX84 | MIMRMTLTLFVLVVMTAASASGDALTEAKRIPYCGQTGAECYSWCIKQDLSKDWCCDFVKDIRMNPPADKCP | Function: Neurotoxin that induces excitatory symptoms in mice following intracranial administration. No symptoms are observed after intraperitoneal and intravenous (tail vein) injections.
Sequence Mass (Da): 8040
Sequence Length: 72
Domain: The cysteine framework is XXIII (C-C-C-CC-C).
Subcellular Location: Secreted
|
Q11002 | MDDLRGFLRQAGQEFLNAAGEAAMGAAKDVVGSVINEIFIKKEADTKRVLPSIKNMRVLGEKSSSLGPYSEVQDYETILNSCLASGSLFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKI... | Function: Calcium-regulated non-lysosomal thiol-protease. Involved in the organization of the actin-related cytoskeleton during embryogenesis.
PTM: Undergoes calcium-dependent autolytic cleavage between Lys-54 and Asn-55, which is necessary for activation of the protein.
Sequence Mass (Da): 93963
Sequence Length: 828
S... |
P63098 | MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV | Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19300
Sequence Length: 170
Subcellular Location: Cytoplasm
|
A1RZN3 | METPRLMCTQHPDSTVKVPVQEEVEEAVRSFLVYGCDEVMSDYEGKLTPYAQPKEIVVKAGELGVPVGEGFYVTVRAPNPRLEDFDRVDLALEAAVLANYYSYKRLGVQAVRWVVLPMTDSAETVRLVQRLLARKTRVLCEEVGQPCEQAQLVPLLEDVDSLLRVREILRDLHSALAELGSDPGVLRVFLGKSDSALKAGHIASALSLLYALGESAKAGEELGLEVKPILGGGSPPFRGGVNNPRLVGVEVQRYRGYSTVTVQSAVRYDASFSEYQEVRSKLLGGAGGEPGDAGGRVAELARLAASMYRSLASKYLDFVN... | Function: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 51243
Sequence Length: 464
... |
Q6F6Q6 | MIQQIDAPLREDVRLLGNLLGETLKQHAGQDLFNQIEQIRALAKGARDGQAETEKKLEQLFLDLKDEEILPLTRAFSYFLNFANIAEQYHVVRSRRRSEFDEQGPPPNPLIHLFEKFKQNQISSKQLFQQVSNLSIELVLTAHPTEVSRRTLIQKYDDINEGLSKLDQQKLTPRERQQVLDDLKQLICSAWQTDEIRQNKPTPLDEAKWGFTTIEQTLWNAVPKFVRELDTLVHQHCDAHLPLDISPIRFASWMGGDRDGNPNVTHNVTQEVLWLSRWQAADLYLRDIEDLRWELSIQACSEELSQTLGRRHPEPYREYL... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 102249
Sequence Length: 894
EC: 4.1.1.31
|
A1K454 | MTPDKDAPLREDIRLLGRLLGDTVRDQQGAASFDLIERIRQTSVRFRRDEDLAARRELEDTLDALSREQTIQVVRAFSYFSHLANIAEDQHHIRRSRAHLLAGSAPREGSLAHAVGHALDEQRLDPTDLAAFFDTALISPVLTAHPTEVQRKSILNCQTVIARLLDERDRMQLTPDEAEANLDALRRAVLTLWQTRMLRPAKLSVIDEVNNGLSYFETTFLRELPRLYAALEDRLAGAQPALANHELPAFLQVGSWIGGDRDGNPYVTADVLEEALAMQARVALDYYLDELHTLGSQLSLSQGLVGASDALLALADRSPD... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 101775
Sequence Length: 917
EC: 4.1.1.31
|
Q7W0D0 | MAAYNAPVSNCQFRLTHILPIPQRHGAPTDPFQMNAIRQQSDSAEPLRHDIRLLGRCLGEVIQACEGKRVYDTIETLRRTAVRFRRAGDPADDKLLQARVKQLRGNDPNSVARAFSYFLHLSNIAEDRDQNRRQRERALAGAGPERGSLRQAIESLKAQGVNNARIRRLLSEACVMPVLTAHPTEVQRKSTLDVHREISSLLVQRERELTADELSELDLALIGQVATLWQTRMLRYTRLTVADEIENALSYYRSTFLNVIPRVYGDLARLLNREPVKPFTPPPPPLEPFLRMGSWIGGDRDGNPNVDAATLERALLRQAT... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 107774
Sequence Length: 980
EC: 4.1.1.31
|
Q14444 | MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVET... | Function: mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types . Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartmen... |
Q60865 | MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPTVEDQVAEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWTVETVE... | Function: mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types . Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartmen... |
Q5RJ80 | MRKTETMVQLSPSRTLETLTPSELTVEKDDGQGSPKPESPRMLSALQLALSSTTVYCGYEKYIEDGLICLKHKIRNIEKKKLKLERYSDKLKKGEKLNEDQLEAVGKYDEVVHNLKFAKELQKTIGSLTQDLLKAQRKAVRQEKQMKTDEEKSRLSLMLQVQYVLHSLQREDVRKNFCNTRQYSCYMSTQDMEGLMDLASLVGCKRDYSISLEDQMRRAAIVYWELLEGNEKPVAGSTYKHMKEKLLRLVDSGFFDNIPLPKSDSQEKTETIKPDSQSRPSGLTTLVKLSSNEVPSKEFLNRRYMPETDERRRGETASPR... | Function: Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway. Facilitates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling. May regulate the transport and translation o... |
P12871 | MVSKAARRRRAAPRQQQRQQSNRASNQPRRRRARRTRRQQRMAATNNMLKMSAPGLDFLKCAFASPDFSTDPGKGIPDKFQGLVLPKKHCLTQSITFTPGKQTMLLVAPIPGIACLKAEANVGASFSGVPLASVEFPGFDQLFGTSATDTAANVTAFRYASMAAGVYPTSNLMQFAGSIQVYKIPLKQVLNSYSQTVATVPPTNLAQNTIAIDGLEALDALPNNNYSGSFIEGCYSQSVCNEPEFEFHPIMEGYASVPPANVTNAQASMFTNLTFSGARYTGLGDMDAIAILVTTPTGAVNTAVLKVWACVEYRPNPNST... | Function: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, 240 calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via... |
Q83884 | MMMASKDATSSVDGASGAGQLVPEVNASDPLAMDPVAGSSTAVATAGQVNPIDPWIINNFVQAPQGEFTISPNNTPGDVLFDLSLGPHLNPFLLHLSQMYNGWVGNMRVRIMLAGNAFTAGKIIVSCIPPGFGSHNLTIAQATLFPHVIADVRTLDPIEVPLEDVRNVLFHNNDRNQQTMRLVCMLYTPLRTGGGTGDSFVVAGRVMTCPSPDFNFLFLVPPTVEQKTRPFTLPNLPLSSLSNSRAPLPISSMGISPDNVQSVQFQNGRCTLDGRLVGTTPVSLSHVAKIRGTSNGTVINLTELDGTPFHPFEGPAPIGF... | Function: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2... |
Q9JH65 | MAEKPQQKAVASAAKQLAKEVVKLDKITKSNGKQHPQKNVPARKWRPRQAKPNNRRVTHKIKRELHKQGLEGPASRFRVTVSATIGKVGPNKEQGPELQIATFLHPSLVKEPNDGSNFGPLQAAAAQWGLWRISDLEVRFTPLVGSSAVTGSVTRASLNLTQSPGATSWGGLGARKHLDVPTGVSKVWKLRRGDLTGPRQTWWVTDTNEEGGQSCGPMLEVHGLGKTTSTYKDSDWTGDLFIVELHGTWEFSNYNAKPALGMLERVTDQTNVELGVDTEGQITMTIPENSPMARHMGERFERASASNASSVGETIWQIVD... | Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in thre... |
P19896 | MAKINELLRESTTTNSNSIGRPNLVALTRATTKLIYSDIVATQRTNQPVAAFYGIKYLNPDNEFTFKTGATYAGEAGYVDREQITELTEESKLTLNKGDLFKYNNIVYKVLEDTPFATIEESDLELALQIAIVLLKVRLFSDAASTSKFESSDSEIADARFQINKWQTAVKSRKLKTGITVELAQDLEANGFDAPNFLEDLLATEMADEINKDILQSLITVSKRYKVTGITDSGFIDLSYASAPEAGRSLYRMVCEMVSHIQKESTYTATFCVASARAAAILAASGWLKHKPEDDKYLSQNAYGFLANGLPLYCDTNSPL... | Function: Capsid protein that self-associates to form pentons, building the capsid in association with hexamers of the major capsid protein and one dodecamer of the portal protein. The capsid vertex protein self-associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of the major ... |
P77885 | MKRYLVLEDGTIYPGTGFGATTATVGELVFNTGMSGYQESITDQSYNGEILMFTYPLIGNYGINRDDHESIKPTCKGVVVHEVARRASNWRNAQSLDDYLKQNAIPGIMDIDTRAVTKHIRTKGAMKATIVDNVLPDTVDRLKVTELNRAVVAQSSTNNAYPNPATGPNVVVVDFGLKHSILRELAKRQCNLTVLPYNTTASEIMALNPDGVMLTNGPGDPKDVPGALEMIREVEKHVPLFGICLGHQLFALANGADTFKMKFGHRGFNHPVREIATGRIDFTSQNHGYAVDRDSLAQTDLLITHEEINDGTVEGLRHRD... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39983
Sequence Length: 364
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
EC: 6.3.5.5
|
Q1MPN3 | MKALLALEDGFILEGQSINGHCESSGEVIFNTGMTGYQEILTDPSYYGQMVCMTWPLIGNYGINKEDMESEKIHVSALIVKECCRNPSNWRSETSLPKFLQEYNIAGIEGIDTRALTRHIRINGAMRGIISTSITDPNDLILRVKKVPSMEGQNYVTKVAPNSPWVLYGQCVVPADIKEDGSFLWKQNKIPLIVYDYGIKWNIIRLLEGAGFDPLMVPPLFSLEQVKASGAKAIFLSNGPGDPGTLIDEIQIIRELMEYYPIAGICLGHQLLGHAVGGTTRKLTFGHHGSNHPIKNLATGHIEISSQNHGFCVNFESNND... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 41736
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q8F6R2 | MKAFLVLDNGTIFEGESFGYETESVGEIVFNTSMAGYQEILTDPSYCNQIITLTYPMIGNYGIHPDNMESSKIQASGLIVKEYVDLPSNFKSEKTLSQFLKEYKIPAIQGIDTRKLTRFIRTNGSPNGGIFVASEYSPSFLEKVKSFPGIINADLAKVVTTSSKYIFGTHTGKKFKLAVYDYGVKTNILRLLDANGFAVTVYPAKTPSEEIMKEGTDAFFLSNGPGDPAPLDYAIASTQKIMEKRYPLFGICLGHQIIGLSLGKKTEKMKFGHRGGNQPVKNLETGQVEITSQNHGFAVIDDQKQDEPISFLNLNDHTVE... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40130
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q8Y664 | MTKRILMLEDGNYFIGDAIGSEKETIGEVVFNTGMTGYQETITDPSYYGQIITFTYPLVGNYGVNRDDFESINPAVKGVVVREAAEFASNWRNQITLNEFLKEKGIPGIAGIDTRKLTKLIRKEGTLKGILAAETADKEELLHHLRSVRLPVDQVHEVSSAKAFASPGDGKRVVLVDYGVKSSILRELNKRNCYVTVVPYNTSAEEILAMHPDGVMLSNGPGDPKDVPEALEMIRGIQGKLPLFGICLGHQLFALANGADTFKLKFGHRGANHPVKELATGRVDFTAQNHGYAVEKDSLIGTDLKVTHIELNDETVEGLA... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40055
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q0AMR3 | MTSTPTPTPTGALALADGSVFLGHGTGATGIALGEVCFNTAMTGHQEILADPSYAGQVVCFTFPHVGNVGANGEDEEAASPQARKAAVGMIARAKITPPASWRADTTFEEWLCTRGIVALTGIDTRALTRKIREGGMQMCAIAHDAAGNIDIEALKAAAAGAPTMEGRELAADVARTEGGDWTEGNWTLGEGYAVGPEDGPRVVVLDYGVKANILRLLTGAGARVAVLPGKASIDDIKALNPDGVVVSNGPGDPAETGKYALPTIKAVLDANIPTLGICLGHQMLALAIGAKTAKMPQGHHGANHPVKNHETGQVEIVSM... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40256
Sequence Length: 390
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
C6C0A9 | MKAILALEDGTYFEGTSFTGPGESGGEAIFNTGMTGYQEVLTDPSYTGQMVCMTYPLIGNYGITKEDIESAKVHVAAFIVKECCKHPSNWRSVMSLPEYLKEAGVMGIEGIDTRALTRHLRINGAMRGIISTEELDPEKLVAKAKQLPTMEGQNLADTVTSETCYAWQDGKPVPVDVSSGYKWSDKGPRLVLVDYGVKWNILRLLDEQGFEVLSVPSHYSEEQVRALEPDAIFLSNGPGDPAVLDQAVKNAKSYCEDLPVAGICLGHQILGQALGGKAFKLKFGHHGCNHPVMDMESKKIEISSQNHGFCVDISDCSDLK... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40988
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q8TNY3 | MKAVLGLEDGTVIRGTGFGAEGTACGELVFTTQFTGYEEALTDPSYKGQILMFTYPLIGNYGVSGERFQSDNIHAEGLVVREACKKPYHYKSTRSIHQFLEDEGKPGIEGVDTRMLTIGARERGTMRAALITGSDDGEEAVKVARNFPQITDEELIARVTCKEPHFIPGAECAWKGSGKPKHAVVVDLGIKRNIINNLHKRGIDLTLVPATTKPKEIAGFEPDLLFISNGPGDPEKATDAINAVKAFAGTIPVAGICFGHQIISLAMGARTYKLKFGHRGGNQPVKDLIENKIFISSQNHGYAVDADSLEGTGLYVKYLN... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39829
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q58425 | MEAVLILEDGTILKGKGFGAEKEVFGELVFTTVMTGYVEVLTDPSYKGQIVMMTYPLEGNYGVKKDWFESDGIKAEGFVVREVTSKALDDFLKEYDIPGIQDIDTRFLTRKIRDKGVVKSCLKVAEEISDDEISELLERVKRYSDISDIDLVPLVSTKEPKIHKTANPKARCVLIDCGVKLNIIRSLVQRNCEVIQVPYNTKYDEILEYKPDFVLISNGPGDPARLKEVIKNIKNLIGVVPITGICLGNQLLSLAFGGETYKMKFGHRGGNQPVKDLKTQKVYITSQNHGFAVRKESLPDDVEVSFINLNDMTVEGIRHK... | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39920
Sequence Length: 354
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
|
Q9Y2G2 | MEKKECPEKSSSSEEELPRRDSGSSRNIDASKLIRLQGSRKLLVDNSIRELQYTKTGIFFQAEACVTNDTVYRELPCVSETLCDISHFFQEDDETEAEPLLFRAVPECQLSGGDIPSVSEEQESSEGQDSGDICSEENQIVSSYASKVCFEIEEDYKNRQFLGPEGNVDVELIDKSTNRYSVWFPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLALDLQHHEQWLVGGPLFDVTAEPEEAVAEIHLPHFISLQAGEVDVSWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIASGTRLSIPITSNTL... | Function: Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages . Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated sign... |
Q5RAV7 | MGIPTSSVSEEQESSEGQDSGDICSEENQIVSSYASKVCFEIEQDYKNRQFLGPEGNVDVELIDKSTNTYSVRFPTAGWYLWPATGLGFLVRDVVTLTIGFGSWNQHLALDLQHHEQWLVGGPLFDITAEPEEAVAEIHLPHFISLQAGEVDVSWFLIAHFKNEGMVLEHPARVEPFYAVLEKPSFSLMGILLRIASGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALLTKMIDDEEDRFCGVRLQTSPPVEPLNFGARYIVSNSAHLEIIPTELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKRHETLVWKT... | Function: Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signa... |
Q9H257 | MSDYENDDECWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYKKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKALLQARVQELEASVQEGKLDRSSPYIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCME... | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors . CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota . Transduces signals in myeloid cells downstrea... |
A2AIV8 | MSDYENDDECWSTLESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYELAMCLAHLSEEKGAALMRNRDLQLEVDRLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKDLLQARVQELQVSVQEGKLDRNSPYIQVLEEDWRQALQEHQKQVSTIFSLRKDLRQAETLRARCTE... | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors . CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota . Transduces signals in myeloid cells downstrea... |
Q9EPY0 | MSDYENDDECWSALESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYDLAMRLAHLSEEKGAALMRNRDLQLEVDQLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWDLQQERDLLQARVQELEVSVQEGKLHRNSPYIQVLEEDWRQALQEHQEQASTIFSLRKDLRQAEALRTRCME... | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors (By similarity). CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota (By similarity). Transduces sign... |
Q9XFX3 | MGTSIKANVLALFLFYLLSPTVFSVSDDGLIRIGLKKRKVDRIDQLRGRRALMEGNARKDFGFRGTVRDSGSAVVALTNDRDTSYFGEIGIGTPPQKFTVIFDTGSSVLWVPSSKCINSKACRAHSMYESSDSSTYKENGTFGAIIYGTGSITGFFSQDSVTIGDLVVKEQDFIEATDEADNVFLHRLFDGILGLSFQTISVPVWYNMLNQGLVKERRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANGVMNQQCKTVV... | Function: Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin.
PTM: N-glycosylated. Glycans found at Asn-139 include approximately 6% oligomannose, 82% oligosaccharides of the plant modified type with proximal fucose but without xylose ... |
Q9XFX4 | MGTPIKASLLALFLFFLLSPTAFSVSNGGLLRVGLKKRKVDRLDQLRAHGVHMLGNARKDFGFRRTLSDSGSGIVALTNDRDTAYYGEIGIGTPPQNFAVIFDTGSSDLWVPSTKCDTSLACVIHPRYDSGDSSTYKGNGTTASIQYGTGAIVGFYSQDSVEVGDLVVEHQDFIETTEEDDTVFLKSEFDGILGLGFQEISAGKAVPVWYNMVNQGLVEEAVFSFWLNRNVDEEEGGELVFGGVDPNHFRGNHTYVPVTRKGYWQFEMGDVLIGDKSSGFCAGGCAAIADSGTSFFAGPTAIITQINQAIGAKGVLNQQC... | Function: Aspartic protease. Cleaves alpha-lactalbumin but not beta-lactoglobulin.
Sequence Mass (Da): 54951
Sequence Length: 506
Subcellular Location: Microsome membrane
EC: 3.4.23.-
|
P85136 | DSGSAIVALTNDRDTSYFGEIGIGTPPQKYTVIYDTGSSVLWVPSSKEQDFIEATDETDNVFLHRRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANSEELNVKFGLTPEQYILKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA | Function: Aspartic protease with a high preference for bonds between hydrophobic residues.
PTM: N-glycosylated.
Sequence Mass (Da): 24507
Sequence Length: 224
Subcellular Location: Microsome membrane
EC: 3.4.23.-
|
P85137 | ADSGSAVVALTNDRDTSYYGEIGIGTPPQKFTVIFDTGSSVLWVPSSKAHSMYESSGSSTYKSQDSVTIGDLVVKEQDFIEATEEADNVFLNRLFDGILGLSFQTISVPVWYNMLNQGLVKRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANGSEELNVKFGLTPEQYILKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA | Function: Aspartic protease with a high preference for bonds between hydrophobic residues.
PTM: N-glycosylated.
Sequence Mass (Da): 30561
Sequence Length: 281
Subcellular Location: Microsome membrane
EC: 3.4.23.-
|
A4XES9 | MVTKGVVVVSSFRRSRQDANRPHAFLTGIHAPVKEERTIEDLAVTGTIPAELSGRYVRIGPNPFRADPRGHHWFVGDGMVHGVCMKGGKALWYRNRYVRSRNLQDAGGPAAAPGPRRSTFDTVNTNVIQHAGRTFALVEAGSFPVELTHDLESFAYSDLGGTLKGPFSAHPHLDPLTGELHAVTYDGQTLDTVWHVVVDREGRVRREEPVPVAHGPSIHDCAITAKYVLILDLPVTFSMAALVGGARFPYRWNPAHRARVGLLPREGTAADVIWCDVDAAYVFHVANAFDNPDGTVTVDLAAYETMFAHGPDGPNGKSLG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the conversion of 8'-apo-beta-carotenal to 13-apo-beta-carotenone and C12-dialdehyde. Has also weak activity with 4'-apo-beta-carotenal and gamma-carotene.
Catalytic Activity: all-trans-8'-apo-beta-carotenal + O2 = 13-apo-beta-carotenone + 2,6-dimethyldeca-2... |
P75409 | MPNPVRFVYRVDLRSPEEIFEHGFSTLGDVRNFFEHILSTNFGRSYFISTSETPTAAIRFFGSWLREYVPEHPRRAYLYEIRADQHFYNARATGENLLDLMRQRQVVFDSGDREMAQMGIRALRTSFAYQREWFTDGPIAAANVRSAWLVDAVPVEPGHAHHPAGRVVETTRINEPEMHNPHYQELQTQANDQPWLPTPGIATPVHLSIPQAASVADVSEGTSASLSFACPDWSPPSSNGENPLDKCIAEKIDNYNLQSLPQYASSVKELEDTPVYLRGIKTQKTFMLQADPQNNNVFLVEVNPKQKSSFPQTIFFWDVY... | Function: The main virulence factor for this bacteria, a mono-ADP-ribosylating toxin (mART), that transfers the ADP-ribosyl group from NAD(+) to multiple target proteins in vitro . Also elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal ... |
H6LGM7 | MRILVCAKQVPDTNEVKIDPKTGTMIREGVPSILNPDDANALEAALVIKDENPGTEVIVMTMGPPQASEMLRECLAMGADEAYLLSDRAFGGADTWATSATLAAGIKKVKKVDLVLAGRQAIDGDTAQVGSQIAQRLKMPVVTYVEDIKIEDKKAIVHRQMEDGYEVIEVQLPCLLTCVKELNDPRYMSVGGIMDAYEQPITIWNHEDIGLSPEACGLNASPTQVFRSFSPPAKGGGEMITGTTVNEVAGSLVSKLKEKHII | Cofactor: Binds 1 FAD per subunit.
Function: Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bif... |
F6IBC7 | MAANNLSYTIAPLEHTPLDEIAAKVDLVRKTFRSGRTKDMEFRMKQIRKLYWAIVDNTELMQDALIKDLRKCKYEAVLAEIDWCKQECIDMVNNMEKWLRDEPVPNVPLQFRAMKHRTRFEPLGVVLNIGSFNFPFQLNLPVVIGAIACGNCVVLKASESSPNCAMVLKKIFDESLDPECFTYVNGALPETQLLLEQKFDKICFTGGKAVGKIIAQKAAETLTPVLLELGGLNPAFVTKHANLKLAARRLLWQKSLNAGQVCMSHNYILVERSVLSQFLGELNNQMRTFFPQGAKNSPDLCRIVNAGHFNRLKKMLDGTN... | Function: Beta-apo-4'-carotenal oxygenase involved in the last step of synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation . Converts the aldehyde beta-apo-4'-carotenal into neurosporaxanthin . Is also able to use shorter apocarotenals... |
Q1K615 | MAASKVEIAPFEVTPLDAIPAVCSTARATFASHKTKNLQWRLVQLRKLYWALDDFKASLMAALQQDLRKGGYESDFTEVDWVKNDCLHMINNLETFAKTEKLKDLPVTYSMMNFRVKKEPLGTVLIIGPYNFPIQLVLAPLVGAIGAGCTAVIKPSELTPACAMAMKEMIESRLDRDAFAVVNGGVPETNALMEEKWDKIMFTGSAQVGSIIARKAAETLTPVCLELGGRNPAFVTKKANLALAARRLMWGKVLNAGQVCMSHNYVLVDKDVADTFIEFLKIAYKDMFPNGAKASPDLSRIVNARHFNRIKKMLDETKGK... | Function: Beta-apo-4'-carotenal oxygenase involved in the last step of synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigment and leading to orange pigmentation . Converts the aldehyde beta-apo-4'-carotenal into neurosporaxanthin . Neurosporaxanthin is synthesized from gera... |
O15234 | MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFK... | Function: Required for pre-mRNA splicing as component of the spliceosome . Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factor... |
Q96PB1 | MAALAYNLGKREINHYFSVRSAKVLALVAVLLLAACHLASRRYRGNDSCEYLLSSGRFLGEKVWQPHSCMMHKYKISEAKNCLVDKHIAFIGDSRIRQLFYSFVKIINPQFKEEGNKHENIPFEDKTASVKVDFLWHPEVNGSMKQCIKVWTEDSIAKPHVIVAGAATWSIKIHNGSSEALSQYKMNITSIAPLLEKLAKTSDVYWVLQDPVYEDLLSENRKMITNEKIDAYNEAAVSILNSSTRNSKSNVKMFSVSKLIAQETIMESLDGLHLPESSRETTAMILMNVYCNKILKPVDGSCCQPRPPVTLIQKLAACFF... | Function: O-acetyltransferase that catalyzes 9-O-acetylation of sialic acids . Sialic acids are sugars at the reducing end of glycoproteins and glycolipids, and are involved in various processes such as cell-cell interactions, host-pathogen recognition .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane prote... |
Q0S4D9 | MTAPTDPQLHLDQVMSRLTGPGGRFELVEEPVLGTRMPVMKNRGRSVGELLTTSLRWGDRDYLVTADRRMSYTEHAAAVAALATALREDYGVRKGDRVAILAANTPEWVVAFWATQVLGAISVGLNGWWVPREVEYGLTHSRPTVVVADAKRAETLAAVGTDLPVLTMEEDLPALFARYAGSPMPHTDVDEDDPAAILYTSGTSGRPKGALHSQRNILAVVDYHRFSDAVVGEFSGRPVDPAVPSPLRYLLTSPLFHIASLHNLVIPRLATGGAVVMHQGGFDVDAVLRLVERERVTNWGAVPTMASRLVEHDDLDKYDL... | Function: Involved in cholate catabolism . Catalyzes the transformation of cholate to cholyl-CoA, thus initiating degradation of the C5 cholate side chain . Can also catalyze the ATP-dependent formation of CoA thioesters of deoxycholate and chenodeoxycholate .
Catalytic Activity: ATP + cholate + CoA = AMP + choloyl-CoA... |
Q0S4D7 | MELERTTIARMLFDRLGDDRLGVRTREQDWTWDEVVRESAARGAVASSLRRDGPFHVGVLLENTPEFLFWLGGAALAGAAVVGVNPTRRGAELEAEIRYVDCQLIVTDTAGKAQLAGLDLGLSEDRFLLVDDPAYTELVAAHAVESPAEDPGIDASTLFLLLFTSGTTGTSKAVRCSQGRLARLAYANTAKYGHVREDVDYCCMPLFHGNALMALWAPALANGATVCLPRKFSASGFLPDVRFFGATFFTYVGKALAYLMATPEQPDDRDNTLVRGFGTEASPEDKTEFVRRFGAELYEGYGSSEGAGSVTLDPDAPEGA... | Function: Involved in cholate catabolism . Catalyzes the ATP-dependent formation of CoA thioesters of steroids with isopropanoyl side chains, likely occurring as degradation intermediates . Can use 4-BNC, HSBNC and HIDP as substrate .
Catalytic Activity: 3-oxochol-4-en-22-oate + ATP + CoA = 3-oxochol-4-en-22-oyl-CoA + ... |
O33950 | MNKQAIDALLQKINDSAINEGNPRTKQIVNRIVRDLFYTIEDLDVQPDEFWTALNYLGDAGRSGELGLLAAGLGFEHFLDLRMDEAEAKAGVEGGTPRTIEGPLYVAGAPVSDGHARLDDGTDPGQTLVMRGRVFGEDGKPLANALVEVWHANHLGNYSYFDKSQPAFNLRRSIRTDAEGKYSFRSVVPVGYSVPPQGQTQLLLDQLGRHGHRPAHIHFFVSAPGFRKLTTQINIDGDPYLWDDFAFATRDGLVPAVRQAEVRKANRTAWTVSSR | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at lower rates than catechol, but has no activity with 4-nitrocatechol or protocatechuic acid.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 30399
Sequence Length: 275
Pathway: ... |
P25819 | MDPYKYRPASSYNSPFFTTNSGAPVWNNNSSMTVGPRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLNMFTFLFDDIGIPQDYRHMDGSGVNTYMLINKAGKAHYVKFHWKPTCGVKSLLEEDAIRVGGTNHSHATQDLYDSIAAGNYPEWKLFIQIIDPADEDKFDFDPLDVTKTWPEDILPLQPVGRMVLNKNIDNFFAENE... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56931
Sequence Length: 492
Subcellular Location: Cytoplasm
EC: 1.11.1.6
|
P30567 | MDPYKFRPSSSFDSPFWTTNSGAPVWNNNSSLTVGARGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISQLTCADFLRAPGVQTPLIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGVPQDYRHMDGSGVHTYTLINKAGKSHYVKFHWKPTCGVKSLLEDEAIRVGGANHSHATQDLYDSIAAGNYPEWKLFIQIMDPLHEDRFDFDPLDVTKTWPEDIFPLQPMGRMVLNKNIDNFFAENE... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56935
Sequence Length: 492
Subcellular Location: Peroxisome
EC: 1.11.1.6
|
Q0D9C4 | MDPYKHRPSSGSNSTFWTTNSGAPVWNNNSALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKPHLVKFHWKPTCGVKCLLDDEAVTVGGTCHSHATKDLTDSIAAGNYPEWKLYIQTIDPDHEDRFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNIDNFFAENE... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). May prevent the excessive accumulation of H(2)O(2) during water stress in response to the accumulation of abscisic acid (ABA) . Involved in the modulation of ROS levels... |
P15202 | MSKLGQEKNEVNYSDVREDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTPENQVAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPL... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 58555
Sequence Length: 515
Subcellular Location: Peroxisome
EC: 1.11.1.6
|
P92131 | MALSLLLAVVCAKPLVSRAELRRIQALNPPWKAGMPKRFENVTEDEFRSMLIRPDRLRARSGSLPPISITEVQELVDPIPPQFDFRDEYPQCVKPALDQGSCGSCWAFSAIGVFGDRRCAMGIDKEAVSYSQQHLISCSLENFGCDGGDFQPTWSFLTFTGATTAECVKYVDYGHTVASPCPAVCDDGSPIQLYKAHGYGQVSKSVPAIMGMLVAGGPLQTMIVVYADLSYYESGVYKHTYGTINLGFHALEIVGYGTTDDGTDYWIIKNSWGPDWGENGYFRIVRGVNECRIEDEIYAVYLD | Function: Thiol protease which is required for parasite excystation and invasion of the proximal small intestine of the human host.
Sequence Mass (Da): 33508
Sequence Length: 303
Subcellular Location: Vacuole
EC: 3.4.22.-
|
O33949 | MIATPVKIESVETILVDVPTIRPHRLSVATMNCQTLVLVRIRCADGVVGVGEGTTIGGLAYGEESPESIKVNIDTYFAPLLKGLDATRPGAAMATLRGLFQGNRFARSAVETALFDAQAQRLGVPLSELFGGRIRDSVDVAWTLASGDTTRDIDEAERVFEAKRHRVFKLKIGSRALADDVAHVVAIQKALQGRGEVRVDVNQAWTESEAIWAGKRFADASVALIEQPIAAENRAGLKRLTDLAQVPIMADEALHGPADAFALASARAADVFAVKIAQSGGLSGAANVAAIALAANIDLYGGTMLEGAVGTIASAQLFST... | Function: Catalyzes a syn cycloisomerization.
Catalytic Activity: (S)-muconolactone = cis,cis-muconate + H(+)
Sequence Mass (Da): 41138
Sequence Length: 385
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3.
EC: 5.5.1.1
|
Q93VC9 | MADNCIRLLHSASVFFCLGLLISSFNLLQGIAAENLSKQKLTSWILQNEIVKEVNENPNAGWKASFNDRFANATVAEFKRLLGVKPTPKTEFLGVPIVSHDISLKLPKEFDARTAWSQCTSIGRILDQGHCGSCWAFGAVESLSDRFCIKYNMNVSLSVNDLLACCGFLCGQGCNGGYPIAAWRYFKHHGVVTEECDPYFDNTGCSHPGCEPAYPTPKCARKCVSGNQLWRESKHYGVSAYKVRSHPDDIMAEVYKNGPVEVAFTVYEDFAHYKSGVYKHITGTNIGGHAVKLIGWGTSDDGEDYWLLANQWNRSWGDDG... | Function: Thiol protease that plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required ... |
P92132 | MKLFLLAAAAFSAPALTVSELNHIKSLNPRWKAGIPKRFEGLTKDEISSLLMPVSFLKNAKGAAPRGTFTDKDDVPESFDFREEYPHCIPEVVDQGGCGSCWAFSSVATFGDRRCVAGLDKKPVKYSPQYVVSCDHGDMACNGGWLPNVWKFLTKTGTTTDECVPYKSGSTTLRGTCPTKCADGSSKVHLATATSYKDYGLDIPAMMKALSTSGPLQVAFLVHSDFMYYESGVYQHTYGYMEGGHAVEMVGYGTDDDGVDYWIIKNSWGPDWGEDGYFRMIRGINDCSIEEQAYAGFFDE | Function: Thiol protease which is required for parasite excystation and invasion of the proximal small intestine of the human host.
Sequence Mass (Da): 33002
Sequence Length: 300
Subcellular Location: Vacuole
EC: 3.4.22.-
|
Q94K85 | MAVYNTKLCLASVFLLLGLLLAFDLKGIEAESLTKQKLDSKILQDEIVKKVNENPNAGWKAAINDRFSNATVAEFKRLLGVKPTPKKHFLGVPIVSHDPSLKLPKAFDARTAWPQCTSIGNILDQGHCGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKCSRKCVSDNKLWSESKHYSVSTYTVKSNPQDIMAEVYKNGPVEVSFTVYEDFAHYKSGVYKHITGSNIGGHAVKLIGWGTSSEGEDYWLMANQWNRGWGDDGYFM... | Function: Thiol protease that possesses high activity toward the cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin (RR-AMC) and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can cleave the papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3 substrate Asp-Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no ... |
Q43931 | MYKSVETILVDIPTIRPHKLSVTTMQTQTLVLIKIITEDGIVGWGEATTIGGLNYGEESPESVKANIDTYFKPLLLSIKAPLNVAQTLKLIRKSINGNRFAKCAIQTALLEIQAKRLNVPVSELLGGRIRDRLPVLWTLASGDTDKDIAEAKKMIELKRHNTFKLKIGSNPLQHDVDHVIAIKKALGPEISVRVDVNRAWSELECVKGIQQLQDGGIDLIEQPCAIENTDALARLTARFDVAIMADEVLTGPDSAYRIAKKSGADVFAVKVEQSGGLIEACEVAKIARLAGISLYGGTMLEGPVGSIASAHAFSTFETLE... | Function: Catalyzes a syn cycloisomerization.
Catalytic Activity: (S)-muconolactone = cis,cis-muconate + H(+)
Sequence Mass (Da): 40415
Sequence Length: 370
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3.
EC: 5.5.1.1
|
Q92405 | MRLTFIPSLIGVANAVCPYMTGELNRRDEISDGDAAAATEEFLSQYYLNDNDAFMTSDVGGPIEDQNSLSAGERGPTLLEDFIFRQKIQRFDHERVPERAVHARGAGAHGVFTSYGDFSNITAASFLAKEGKQTPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSTMHTLLWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGASKLVKFHWKSLQGKASMVWEEAQQTSGKNPDFMRQDLHDAIEAGRYPEWELGVQIMDEEDQ... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
PTM: N-glycosylated.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 79910
Sequence Length: 728
Subcellular Location: Secreted
EC: 1.11.1.6
|
Q877A8 | MRALSLASLIGIASAACPYMTGELERRDTGTDDATAATEEFLSQYYMADNDTFLTSDVGGPIEDQNSLQVGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGVGAHGVFTSYGDYSNITAASFLGAEGKETPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSSLHTLLWAMSGHGIPRSLRHVDGFGIHTFRFVTDNGDSKLVKFHWKSLQGKASMVWEEAQQVSGKNPDFMRQDLFEAIEAGRYPEWELGVQIMDEEDQL... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide through its degradation into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 79868
Sequence Length: 725
Subcellular Location: Secreted
EC: 1.11.1.6
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.