ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B2KC48 | MDLEKTRDNLKNNVFGRFFLYVLSKGYELGTIVNKFLYENGWRKSYSVNTRVVCVGNITAGGTGKTTAVLLAARTLAEAGIRTAIISRGYKRDKKNKNPVVLFDDELENNWVTAGDEPFMMSRALADVKVPIVIHEDRHLAATEALKRFKSQVLLLDDGFQHFRLKRDANIVLIDARNPFGGGQLLPYGTLREGLSGLKRANLVLLTHSNQADQRKKEDIKDQIRLQNEDIEILEAVHQPEHYFDICNSVKVPLNHLKGEAGVFSAIGEPGGFEDTLKDLGLKLVKVWRYPDHRRYTEEDLKTFVDLAGENPLVTTFKDFVKFPENWRDILKKNVYVLSVSMKIKGKKEFDIFAEALYPKFTNLNVKKESKSRK | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 42606
Sequence Length: 374
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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A4W8T4 | MIARIWSGKSPLWLLLLPLSWLYGLVSGLIRLCYRIGIKRSWRAPVPVVVVGNLTAGGNGKTPVVIWLVEQLAHRGIQAGVVSRGYGGKAESYPLLLTSQTTTEQAGDEPVLIFQRTGAPVAVSPNRSEAVQVLLAAHPVDIVITDDGLQHYALARDKEIVVIDGVRRFGNGWWLPAGPMRERASRLRTVDAVIVNGGEALPGEIPMRLIPSQAVNLLTGERREVSQLPALVAMAGIGHPPRFFATLEQCGAHLEARIPLADHQALSIVDVDPLVTVNQNLIMTEKDAVKCRAFAKSNWWYLPVDAEFSGEKPELLLQELMSLVR | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35511
Sequence Length: 325
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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A5FNE6 | MNLLRKILFPFAILYGLITSIRNFLFDKGILKSTSFDLPVIAVGNLSVGGTGKTPQIEYLIRLLSNKYRAATLSRGYKRKSEGFVLADENSNAEILGDEPFQFYQKFPDVQVAVDANRTNGITQLLSQNVKPQVILLDDAYQHRKVKAGFYILLTSYDDLYADDFMLPTGNLRESRSGANRANIVVVTKCPKNLSEEKQAEIRLKLKLSCSQQIFFTYIDYDVEIYGKDEKISAAEIKSESKLLLAGIAKPKPFFEYLKNENDECLTFPDHHHFSDADLESIQNKANGRKIITTEKDYVRLKDSKLVSQLYYLPIKSTFINHQQNFDVSILQYIKENLEP | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38794
Sequence Length: 340
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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A6GZM3 | MNFLRKTLFPFAILYGFITSIRNFLFDCGILKSHAFPIPVIAVGNLSVGGTGKTPQIEYLIRLLSNKYQIATLSRGYKRKSEGFILANPTSNAEILGDEPFQFYKKFPNIQVAVAANRKNGIERLLSLPNKPEIILLDDAFQHRKVKAGFYILLTAYNDLFINDFMLPTGNLRESRSGAKRANMIIVTKCPKDISELAQNKIKEALINYNNKKAEVFFTFIDYDDKIYSANKALNVNEVKTASKLLLAGIAKPESFFAHLQSQNDECLVYPDHHHFLEKNITDIKEKAKNKIIITTEKDFVRLSEKLNSDNLFYLPIKSLFVNNEKKFDKKIINYVESSTTNG | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 39052
Sequence Length: 343
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q47909 | MLDKIWYRSKPNLLSRVLQPISLVFIDIANKRKIKQQLKQYKSKIPIIVVGNISVGGTGKTPVVRMLAQQYLAQGKKPAIISRGYGAKADNYPFEVTSGTLATQCGDEPAMLFDALQAQVPIVIAPERVQAVKYIEKNFPDTDIIISDDGLQHYKLARDKEIVVVDAIRMFGNKLCLPAGPLREPIERLKEVDQIIVIGNCSDKDKELLKNYKNVTYAKVVATEFVNILTAKKVAKTEFNHQNVIAIAGIGNPTKFFKTLEESAINITAKKVFKDHHKFTQSDFEGIDSDITVVMTYKDAIKCKNFAKANWWYLDIALDINV | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36145
Sequence Length: 322
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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P0CC10 | MAQAHIQGSPCPLLPPGRMSWPQGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRYIGELDQSHFTCYAPVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNVSAVDPVAAGGPGGGGPGGGGGAGGAGGYTYFTTVTVETLETQPGEEAQQPRGTEKEPPGPTTDGAWGGGRPDAAAPASASTTAPAPRSSRPTEKAFTVPITDVTENALKDLDDVMKTTKIIIGCFVAITFMAAVMLVAFYKLRKQHQLHKHHGPTRTVEIINVEDELPAASAVSVAAAAAVAGGAGVGGDSHLALPALERDHLNHHHYVAAAFKAHYGGNPGGGCGAKGPGLNSIHEPLLFKSGSKENVQETQI | Function: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner.
PTM: N-glycosylated. O-glycosylated; contains sialic acid.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76119
Sequence Length: 709
Domain: The extreme C-terminus binds to the first 2 PDZ domains of DLG4.
Subcellular Location: Membrane
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Q9HCJ2 | MLNKMTLHPQQIMIGPRFNRALFDPLLVVLLALQLLVVAGLVRAQTCPSVCSCSNQFSKVICVRKNLREVPDGISTNTRLLNLHENQIQIIKVNSFKHLRHLEILQLSRNHIRTIEIGAFNGLANLNTLELFDNRLTTIPNGAFVYLSKLKELWLRNNPIESIPSYAFNRIPSLRRLDLGELKRLSYISEGAFEGLSNLRYLNLAMCNLREIPNLTPLIKLDELDLSGNHLSAIRPGSFQGLMHLQKLWMIQSQIQVIERNAFDNLQSLVEINLAHNNLTLLPHDLFTPLHHLERIHLHHNPWNCNCDILWLSWWIKDMAPSNTACCARCNTPPNLKGRYIGELDQNYFTCYAPVIVEPPADLNVTEGMAAELKCRASTSLTSVSWITPNGTVMTHGAYKVRIAVLSDGTLNFTNVTVQDTGMYTCMVSNSVGNTTASATLNVTAATTTPFSYFSTVTVETMEPSQDEARTTDNNVGPTPVVDWETTNVTTSLTPQSTRSTEKTFTIPVTDINSGIPGIDEVMKTTKIIIGCFVAITLMAAVMLVIFYKMRKQHHRQNHHAPTRTVEIINVDDEITGDTPMESHLPMPAIEHEHLNHYNSYKSPFNHTTTVNTINSIHSSVHEPLLIRMNSKDNVQETQI | Function: May promote neurite outgrowth of developing thalamic neurons.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71950
Sequence Length: 640
Domain: The LRR region is both necessary and sufficient for the interaction with NTNG1.
Subcellular Location: Postsynaptic cell membrane
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Q8IWT6 | MIPVTELRYFADTQPAYRILKPWWDVFTDYISIVMLMIAVFGGTLQVTQDKMICLPCKWVTKDSCNDSFRGWAAPGPEPTYPNSTILPTPDTGPTGIKYDLDRHQYNYVDAVCYENRLHWFAKYFPYLVLLHTLIFLACSNFWFKFPRTSSKLEHFVSILLKCFDSPWTTRALSETVVEESDPKPAFSKMNGSMDKKSSTVSEDVEATVPMLQRTKSRIEQGIVDRSETGVLDKKEGEQAKALFEKVKKFRTHVEEGDIVYRLYMRQTIIKVIKFILIICYTVYYVHNIKFDVDCTVDIESLTGYRTYRCAHPLATLFKILASFYISLVIFYGLICMYTLWWMLRRSLKKYSFESIREESSYSDIPDVKNDFAFMLHLIDQYDPLYSKRFAVFLSEVSENKLRQLNLNNEWTLDKLRQRLTKNAQDKLELHLFMLSGIPDTVFDLVELEVLKLELIPDVTIPPSIAQLTGLKELWLYHTAAKIEAPALAFLRENLRALHIKFTDIKEIPLWIYSLKTLEELHLTGNLSAENNRYIVIDGLRELKRLKVLRLKSNLSKLPQVVTDVGVHLQKLSINNEGTKLIVLNSLKKMANLTELELIRCDLERIPHSIFSLHNLQEIDLKDNNLKTIEEIISFQHLHRLTCLKLWYNHIAYIPIQIGNLTNLERLYLNRNKIEKIPTQLFYCRKLRYLDLSHNNLTFLPADIGLLQNLQNLAITANRIETLPPELFQCRKLRALHLGNNVLQSLPSRVGELTNLTQIELRGNRLECLPVELGECPLLKRSGLVVEEDLFNTLPPEVKERLWRADKEQA | Function: Essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine . Mediates efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress . LRRC8A and LRRC8D are required for the uptake of the drug cisplatin . In complex with LRRC8C or LRRC8E, acts as a transporter of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol: mediates both import and export of 2'-3'-cGAMP, thereby promoting transfer of 2'-3'-cGAMP to bystander cells . In contrast, complexes containing LRRC8D inhibit transport of 2'-3'-cGAMP . Required for in vivo channel activity, together with at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition . Can form functional channels by itself (in vitro) . Involved in B-cell development: required for the pro-B cell to pre-B cell transition . Also required for T-cell development (By similarity). Required for myoblast differentiation: VRAC activity promotes membrane hyperpolarization and regulates insulin-stimulated glucose metabolism and oxygen consumption (By similarity). Also acts as a regulator of glucose-sensing in pancreatic beta cells: VRAC currents, generated in response to hypotonicity- or glucose-induced beta cell swelling, depolarize cells, thereby causing electrical excitation, leading to increase glucose sensitivity and insulin secretion . Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: chloride(in) = chloride(out)
Sequence Mass (Da): 94199
Sequence Length: 810
Domain: The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.
Subcellular Location: Cell membrane
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Q6P9F7 | MITLTELKCLADAQSSYHILKPWWDVFWYYITLIMLLVAVLAGALQLTQSRVLCCLPCKVEFDNHCAVPWDILKASMNTSSNPGTPLPLPLRIQNDLHRQQYSYIDAVCYEKQLHWFAKFFPYLVLLHTLIFAACSNFWLHYPSTSSRLEHFVAILHKCFDSPWTTRALSETVAEQSVRPLKLSKSKILLSSSGCSADIDSGKQSLPYPQPGLESAGIESPTSSVLDKKEGEQAKAIFEKVKRFRMHVEQKDIIYRVYLKQIIVKVILFVLIITYVPYFLTHITLEIDCSVDVQAFTGYKRYQCVYSLAEIFKVLASFYVILVILYGLTSSYSLWWMLRSSLKQYSFEALREKSNYSDIPDVKNDFAFILHLADQYDPLYSKRFSIFLSEVSENKLKQINLNNEWTVEKLKSKLVKNAQDKIELHLFMLNGLPDNVFELTEMEVLSLELIPEVKLPSAVSQLVNLKELRVYHSSLVVDHPALAFLEENLKILRLKFTEMGKIPRWVFHLKNLKELYLSGCVLPEQLSTMQLEGFQDLKNLRTLYLKSSLSRIPQVVTDLLPSLQKLSLDNEGSKLVVLNNLKKMVNLKSLELISCDLERIPHSIFSLNNLHELDLRENNLKTVEEIISFQHLQNLSCLKLWHNNIAYIPAQIGALSNLEQLSLDHNNIENLPLQLFLCTKLHYLDLSYNHLTFIPEEIQYLSNLQYFAVTNNNIEMLPDGLFQCKKLQCLLLGKNSLMNLSPHVGELSNLTHLELIGNYLETLPPELEGCQSLKRNCLIVEENLLNTLPLPVTERLQTCLDKC | Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92390
Sequence Length: 803
Domain: The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.
Subcellular Location: Cell membrane
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Q8TDW0 | MIPVTEFRQFSEQQPAFRVLKPWWDVFTDYLSVAMLMIGVFGCTLQVMQDKIICLPKRVQPAQNHSSLSNVSQAVASTTPLPPPKPSPANPITVEMKGLKTDLDLQQYSFINQMCYERALHWYAKYFPYLVLIHTLVFMLCSNFWFKFPGSSSKIEHFISILGKCFDSPWTTRALSEVSGEDSEEKDNRKNNMNRSNTIQSGPEDSLVNSQSLKSIPEKFVVDKSTAGALDKKEGEQAKALFEKVKKFRLHVEEGDILYAMYVRQTVLKVIKFLIIIAYNSALVSKVQFTVDCNVDIQDMTGYKNFSCNHTMAHLFSKLSFCYLCFVSIYGLTCLYTLYWLFYRSLREYSFEYVRQETGIDDIPDVKNDFAFMLHMIDQYDPLYSKRFAVFLSEVSENKLKQLNLNNEWTPDKLRQKLQTNAHNRLELPLIMLSGLPDTVFEITELQSLKLEIIKNVMIPATIAQLDNLQELSLHQCSVKIHSAALSFLKENLKVLSVKFDDMRELPPWMYGLRNLEELYLVGSLSHDISRNVTLESLRDLKSLKILSIKSNVSKIPQAVVDVSSHLQKMCIHNDGTKLVMLNNLKKMTNLTELELVHCDLERIPHAVFSLLSLQELDLKENNLKSIEEIVSFQHLRKLTVLKLWHNSITYIPEHIKKLTSLERLSFSHNKIEVLPSHLFLCNKIRYLDLSYNDIRFIPPEIGVLQSLQYFSITCNKVESLPDELYFCKKLKTLKIGKNSLSVLSPKIGNLLFLSYLDVKGNHFEILPPELGDCRALKRAGLVVEDALFETLPSDVREQMKTE | Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine . Plays a redundant role in the efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress . The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol . Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92450
Sequence Length: 803
Domain: The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.
Subcellular Location: Cell membrane
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Q7L1W4 | MFTLAEVASLNDIQPTYRILKPWWDVFMDYLAVVMLMVAIFAGTMQLTKDQVVCLPVLPSPVNSKAHTPPGNAEVTTNIPKMEAATNQDQDGRTTNDISFGTSAVTPDIPLRATYPRTDFALPNQEAKKEKKDPTGRKTNLDFQQYVFINQMCYHLALPWYSKYFPYLALIHTIILMVSSNFWFKYPKTCSKVEHFVSILGKCFESPWTTKALSETACEDSEENKQRITGAQTLPKHVSTSSDEGSPSASTPMINKTGFKFSAEKPVIEVPSMTILDKKDGEQAKALFEKVRKFRAHVEDSDLIYKLYVVQTVIKTAKFIFILCYTANFVNAISFEHVCKPKVEHLIGYEVFECTHNMAYMLKKLLISYISIICVYGFICLYTLFWLFRIPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQHISRNAQDKQELHLFMLSGVPDAVFDLTDLDVLKLELIPEAKIPAKISQMTNLQELHLCHCPAKVEQTAFSFLRDHLRCLHVKFTDVAEIPAWVYLLKNLRELYLIGNLNSENNKMIGLESLRELRHLKILHVKSNLTKVPSNITDVAPHLTKLVIHNDGTKLLVLNSLKKMMNVAELELQNCELERIPHAIFSLSNLQELDLKSNNIRTIEEIISFQHLKRLTCLKLWHNKIVTIPPSITHVKNLESLYFSNNKLESLPVAVFSLQKLRCLDVSYNNISMIPIEIGLLQNLQHLHITGNKVDILPKQLFKCIKLRTLNLGQNCITSLPEKVGQLSQLTQLELKGNCLDRLPAQLGQCRMLKKSGLVVEDHLFDTLPLEVKEALNQDINIPFANGI | Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine . Plays a redundant role in the efflux of amino acids, such as aspartate, in response to osmotic stress . LRRC8A and LRRC8D are required for the uptake of the drug cisplatin . Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition . Also acts as a regulator of glucose-sensing in pancreatic beta cells: VRAC currents, generated in response to hypotonicity- or glucose-induced beta cell swelling, depolarize cells, thereby causing electrical excitation, leading to increase glucose sensitivity and insulin secretion (By similarity). VRAC channels containing LRRC8D inhibit transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol . Mediates the import of the antibiotic blasticidin-S into the cell .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 98201
Sequence Length: 858
Domain: The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.
Subcellular Location: Cell membrane
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Q6NSJ5 | MIPVAEFKQFTEQQPAFKVLKPWWDVLAEYLTVAMLMIGVFGCTLQVTQDKIICLPNHELQENLSEAPCQQLLPRGIPEQIGALQEVKGLKNNLDLQQYSFINQLCYETALHWYAKYFPYLVVIHTLIFMVCTSFWFKFPGTSSKIEHFISILGKCFDSPWTTRALSEVSGENQKGPAATERAAATIVAMAGTGPGKAGEGEKEKVLAEPEKVVTEPPVVTLLDKKEGEQAKALFEKVKKFRMHVEEGDILYTMYIRQTVLKVCKFLAILVYNLVYVEKISFLVACRVETSEVTGYASFCCNHTKAHLFSKLAFCYISFVCIYGLTCIYTLYWLFHRPLKEYSFRSVREETGMGDIPDVKNDFAFMLHLIDQYDSLYSKRFAVFLSEVSESRLKQLNLNHEWTPEKLRQKLQRNAAGRLELALCMLPGLPDTVFELSEVESLRLEAICDITFPPGLSQLVHLQELSLLHSPARLPFSLQVFLRDHLKVMRVKCEELREVPLWVFGLRGLEELHLEGLFPQELARAATLESLRELKQLKVLSLRSNAGKVPASVTDVAGHLQRLSLHNDGARLVALNSLKKLAALRELELVACGLERIPHAVFSLGALQELDLKDNHLRSIEEILSFQHCRKLVTLRLWHNQIAYVPEHVRKLRSLEQLYLSYNKLETLPSQLGLCSGLRLLDVSHNGLHSLPPEVGLLQNLQHLALSYNALEALPEELFFCRKLRTLLLGDNQLSQLSPHVGALRALSRLELKGNRLEALPEELGNCGGLKKAGLLVEDTLYQGLPAEVRDKMEEE | Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine . Mediates efflux of amino acids, such as aspartate, in response to osmotic stress . The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol . Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition . Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90247
Sequence Length: 796
Domain: The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins.
Subcellular Location: Cell membrane
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Q7Z2Q7 | MCGLQFSLPCLRLFLVVTCYLLLLLHKEILGCSSVCQLCTGRQINCRNLGLSSIPKNFPESTVFLYLTGNNISYINESELTGLHSLVALYLDNSNILYVYPKAFVQLRHLYFLFLNNNFIKRLDPGIFKGLLNLRNLYLQYNQVSFVPRGVFNDLVSVQYLNLQRNRLTVLGSGTFVGMVALRILDLSNNNILRISESGFQHLENLACLYLGSNNLTKVPSNAFEVLKSLRRLSLSHNPIEAIQPFAFKGLANLEYLLLKNSRIRNVTRDGFSGINNLKHLILSHNDLENLNSDTFSLLKNLIYLKLDRNRIISIDNDTFENMGASLKILNLSFNNLTALHPRVLKPLSSLIHLQANSNPWECNCKLLGLRDWLASSAITLNIYCQNPPSMRGRALRYINITNCVTSSINVSRAWAVVKSPHIHHKTTALMMAWHKVTTNGSPLENTETENITFWERIPTSPAGRFFQENAFGNPLETTAVLPVQIQLTTSVTLNLEKNSALPNDAASMSGKTSLICTQEVEKLNEAFDILLAFFILACVLIIFLIYKVVQFKQKLKASENSRENRLEYYSFYQSARYNVTASICNTSPNSLESPGLEQIRLHKQIVPENEAQVILFEHSAL | Function: Renders cells highly sensitive to the activation by cytokines and lipopolysaccharide (LPS).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70301
Sequence Length: 622
Subcellular Location: Membrane
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Q9HBW1 | MKLLWQVTVHHHTWNAILLPFVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQASFQCSAPFIMDAPRDLNISEGRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSHVLLSDTGVYTCMVTNVAGNSNASAYLNVSTAELNTSNYSFFTTVTVETTEISPEDTTRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVAVPATDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAATSAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI | Function: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72717
Sequence Length: 653
Domain: The last 4 C-terminal residues bind to the first 2 PDZ domains of DLG4.
Subcellular Location: Membrane
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Q99PH1 | MKLLWQVTVHHTWNAVLLPVVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQAAFQCSAPFIMDAPRDLNISEDRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNVSSAELNTPNFSFFTTVTVETTEISPEDITRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVPVPSTDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAAAPAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI | Function: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72619
Sequence Length: 652
Domain: The last 4 C-terminal residues bind to the first 2 PDZ domains of DLG4.
Subcellular Location: Membrane
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Q2T0H4 | MAKTLSKSSGGALAPWLGISLIVILFDQLTKIAVLKTFAYGAMHQLTPFFNLTLIYNRGAAFGFLATAGGWQRWAFTALGIGATLVICYLLKRHGHQRLFSLSLALILGGALGNVIDRLIYGHVIDFLDFHVGAWHWPAFNLADSAITVGAVLLIYDELRRVRGAR | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18156
Sequence Length: 166
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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B9MS17 | MVYWIIIMSTFVLDQLTKARAEKFFVDSPVNLLGGILSLTYVQNRGGAFSILEGKRRFFIIVSIILILFLCYMIFKSTSNLYKFSFSLIVGGAIGNLFDRIVKGYVVDFIDIKVIPVFNLADFFITGGVLLLTFLILKEGGEELFLKKKP | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16966
Sequence Length: 150
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q8R9R0 | MAIVIVAFVVFLDQFTKYLAAKYLMPIGSYPVIKHFFHLTYVENRGAAFGMLQNKTLFFIVITVVVGIVLIYSMIKLPENSLYNYTLAMILGGAIGNLIDRVRLGYVVDFIDFKFFPAVFNVADSFIVVGAIILGYLMIFKGGIR | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16280
Sequence Length: 145
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q0PBE9 | MAKTFKFIFYFWGAFVLVFALDQWVKSLTLAGFRWQSEYLDLTYALNTGVAFSMLSFLEHNLKYLHLALIGVLFIYLFWQRTLLKTHSIAFGMMLGAGVSNLLDRFIHGGVVDMFFWHKWFNFAIFNVADVMINISVALILIQEIFKKRKKDDRMD | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18327
Sequence Length: 156
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q9AAA6 | MPSLSITRQGWIAYAIAAVTVVLDQISKLWILGLLGREPGASLPLLGPIHLTMVHNYGMSFGLLRDSDWGRWLLIGFSILVVIGLAVWVHKATRPLLAVGIGLIIGGAIGNNLIDRVIYGYVVDFIDVSRLYFPWVFNIADSGISVGVALLLLDSFLSEENKLSHQTE | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18354
Sequence Length: 168
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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B3PE13 | MTKKVYHQYWFWYLAAFVVFLLDQGSKHWIEAAFDYNETKVFTSFFNFTLRYNPGAAFSFLADAGGWQRWFFTIVAVAASVLLIVWICRVASSKPREAFALSFILGGAVGNLYDRIIHGHVVDFIVVHYQDYYWPAFNLADAAISLGAMVLIADLFINPDKTSGEKPTNA | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19312
Sequence Length: 170
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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B2RI39 | MASFLSRLPQGKVVAALIVLLLVVDQVIKIWVKTTMVLGQSHVVAPWFQIHFVENPGMAFGIELGSKLFLSLFRIVAMGFCIYLLAKLVRKREHTLAFLSCLSLIIAGGIGNIIDSIFYGVIFSGSHGQIAQLFPSGGGYETWFHGRVVDMFYFPLIEGVFPSWLPFWGGEEFVFFHPVFNFADSCISIGLILLLVCYPRTVSLLLDGKKTLPEGTTEDSEPTKRE | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25138
Sequence Length: 226
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q9HVM5 | MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRSKKSGEAAHG | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18997
Sequence Length: 169
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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A1SZP2 | MAEIIEKSGLRWLWLAAIMLALDQVTKYWTIQSLDLYESYEIFSFFSFTYARNYGAAFSFLGDAGGWQRYLFTAIAIVVSSYLVYLLKKNASTDRWINCAYALILSGALGNVVDRMMFGYVIDFLDFDLGFYRWPTFNIADSAIFTGAVIMIFESFFAKQAKPIKQPKGNKNV | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19791
Sequence Length: 173
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q98GR1 | MRSWSPYALLVVAAIALDQWIKHLVETGLPFQEKLDLVPFLALFRTYNTGIAFSMFSSFGDTGLVVIAVLVVAFVLYLATRTPSGHVIARTGFALIIGGALGNLIDRAVYGHVIDYILFHTPVWSFAIFNLADAFISVGAALVVFDELIGWRREPSNAKPSKAKPSKD | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18385
Sequence Length: 168
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q92SJ3 | MRQEQTLFSRPLPIALFILIALAADQFIKYLVEAYLPFQQGVPVMPMLALYRTYNYGVAFSMLSGMEGWFIVGIRLAVVTFVLWLWRRTPKDRFFAHLGYAMIIAGALGNLVDRLLFGYVIDYILFYTATWSFAVFNLADSFITVGAGAIILDELLQAKKERSLKL | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18920
Sequence Length: 166
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q7UF32 | MNSAKVNPSGHAPTPAPTASQGAAFPANRYALFFGLAIAGGALDLWSKEAIFRWRGLPGTQDVYWIIEGYFGIETAVNIGAVFGLGAGQGLVFAAISVFAAAAIIAWLFFFKAARSCWLTFALGCITGGIIGNLYDRLGFWWKPGLPDQWQSGVRDWILWQASDQWKWPNFNIADSLLVTGAIMLLVQSFFFPPPPHGEADGNELPGRRAPDEPTEGTKPAAS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24063
Sequence Length: 223
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q0SHT6 | MDDERVSQDPTAENETDAEDRNDDDPSGSAPPQPVTHQRRLLLFVIAGVVLATDLLTKILAVANIEPGRPVWLIGDIVSLRLVRNPGAAFSMATGMTWLLTLVAVGVVIGVVRIGRTLRSPWWALGLGLVLGGALGNLVDRFFRAPGVMQGHVVDFVSVGWWPVFNVADSGIVCGAILLVVLTLIGLEPDGTRKGVEK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21151
Sequence Length: 198
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q2NKS0 | MKDEVALLASVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERIYRAQVNCSEYFPLFLAMLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQQRLAPLYASARALWLLVALAALGLLAHFLPAELRAALLGQLRKLLLRS | Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyzes the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions.
PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity.
Location Topology: Multi-pass membrane protein
Catalytic Activity: leukotriene C4 = glutathione + leukotriene A4
Sequence Mass (Da): 16701
Sequence Length: 150
Pathway: Lipid metabolism; leukotriene C4 biosynthesis.
Subcellular Location: Nucleus outer membrane
EC: 4.4.1.20
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Q16873 | MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA | Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity . Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions .
PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity.
Location Topology: Multi-pass membrane protein
Catalytic Activity: leukotriene C4 = glutathione + leukotriene A4
Sequence Mass (Da): 16567
Sequence Length: 150
Pathway: Lipid metabolism; leukotriene C4 biosynthesis.
Subcellular Location: Nucleus outer membrane
EC: 4.4.1.20
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Q925U2 | MKEETALLATVTLLGVLLQAYFSLQVISARRTFHVSPPLTSGPPEFERVFRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLFYLFARLRYFQGYARSAQHRLDPLYASARALWLLVAMAALGLLVHFLPGTLRAALFRWLQVLLPMA | Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity . Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (By similarity).
PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity.
Location Topology: Multi-pass membrane protein
Catalytic Activity: leukotriene C4 = glutathione + leukotriene A4
Sequence Mass (Da): 16850
Sequence Length: 150
Pathway: Lipid metabolism; leukotriene C4 biosynthesis.
Subcellular Location: Nucleus outer membrane
EC: 4.4.1.20
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Q8VY88 | MASSSISFSCAPSLATSLFSTTSSSPRLLSSRFLGTRNLKLRIRPARLGPSNGSRTTCWFKFGKNGVDAENAGIYGSQSRDDFDRDDVEQYFNYMGMLAVEGTYSKMEALLNLNIHPVDILLMLAATEGDRPKIEELLKAGADYSVKDADGRTAIDRANSEEIRDLILGYSTQKA | Function: Involved in the import of light-harvesting complex proteins (LHCP) and subsequent routing of these proteins to the chloroplast signal recognition particle (SRP) pathway.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19190
Sequence Length: 175
Subcellular Location: Plastid
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Q9C9B1 | MASSTLLITLLISLSAFFLRMVLAQVPATCASRLLSLAPCGPFVQGFAQLPAQPCCDSLNQIYSQEATCLCLFLNNTSTLSPAFPINQTLALQLPPLCNIPANSSTCSSSFPGEAPSDSSSVAPPPSSSTGSQISQGAKNNSRVAATPVAQMAPRPTSFMGLGYGLKSSGSKSEIQLTIFALAAILPAALLLI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19881
Sequence Length: 193
Subcellular Location: Cell membrane
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Q9ZQI8 | MAYATILMIFSVVALMSGERAHAAVDCSSLILNMADCLSFVTSGSTVVKPEGTCCSGLKTVVRTGPECLCEAFKNSGSLGLTLDLSKAASLPSVCKVAAPPSARCGLSVSGDPPATAPGLSPTAGAGAPALSSGANAATPVSSPRSSDASLLSVSFAFVIFMALISSFY | Function: Probable lipid transfer protein (By similarity). Proteoglycan-like factor that exhibits xylogen activity consisting in mediating local and inductive cell-cell interactions required for xylem differentiation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 16816
Sequence Length: 169
Subcellular Location: Cell membrane
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Q9ZVC7 | MLTTNTLAVLLLLFLSLCSGQSPPAPEPIAADGPSSPVNCLVSMLNVSDCFSYVQVGSNEIKPEAACCPELAGMVQSSPECVCNLYGGGASPRFGVKLDKQRAEQLSTICGVKAPSPSLCSVLGFPTISPAGSEDSSSGSEGSDKDKKNGAMTTKYCGVALNSLALLLLFTFLSLS | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18089
Sequence Length: 176
Subcellular Location: Cell membrane
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O64865 | MESRKINLMATAIALIVVAMVVAAADDKTKDKEECTEQLVGMATCLPYVQGQAKSPTPDCCSGLKQVLNSNKKCLCVIIQDRNDPDLGLQINVSLALALPSVCHAAADVTKCPALLHLDPNSPDAQVFYQLAKGLNKTGPASAPTGSSPGPISISPTSGSDDGNNSGRTTSVPGRNHAQSFYKQWLGLEVVFHFFVIFYIFILV | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21706
Sequence Length: 204
Subcellular Location: Cell membrane
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Q7EB72 | MGYRRSYAITFVALVAALWSVTKAQPSSSCVSTLTTLSPCLSYITGNSTTPSQPCCSRLDSVIKSSPQCICSAVNSPIPNIGLNINRTQALQLPNACNIQTPPLTQCNAATGPTAQPPAPSPTEKTPDVTLTPTSLPGARSGVGGGSKTVPSVGTGSSSRNVDPLPLHFLMFAVLVVCTSSFL | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18853
Sequence Length: 183
Subcellular Location: Cell membrane
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Q94AX3 | MEGLTLIVVMMSSFMLGGQGQQISTPCTSSMISTFTPCLNFITGSSGGSVTPTAGCCDSLKTLTNTGMGCACLILTANVPLPTGFINRTLALALPRACKMGGVPIQCQAAGTPLPAPGQVPFLIAPPPQVSAFSPGASKAAGTTPTQAPAPDTPADGPTGPTTKSGIRPVDQPMQPTGLAQSSTSPFLPLLFISLILLNL | Function: Essential protein involved in female gametophyte development . Probable lipid transfer protein (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20145
Sequence Length: 200
Subcellular Location: Cell membrane
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B3EWF5 | MKVLVIIALCFFILQTALSEDKYESFESYVEDLKSGNMKGEARECIPLYNDCKEFKYNNNCCKDPEKKYQYKCSCIMCEGGEEQCTCQRKETVENMMKCVRFVKKVVEKVG | Function: Insect toxin.
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 12948
Sequence Length: 111
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P13894 | MASLRRLTELLCLPVTATAADIKTAYRRTALKYHPDKGGDEEKMKELNTLMEEFRETEGLRADETLEDSDPEPEESGYATFENVSVPDIDGAFFKLMKLKKCMQTYFSVNERRKQQSCPDCHLLITSITKMPQLKAHLYEHFGIKGHIVAHWTGIALLVLQLEKPTRISTVHNFCKKYCTISICSVRGIKKNCVHALIKTLLDVPGLDLEECSIDMNVVDEKQFMHAMLYDYAVQIDCTDALLLLAIYKRLAQPTDKCPECQKDKDTVKRKRSTHIDDHPRHQHNASLFLHIKDQKRLCQCAVDAVLAEKRFRSATMTRDERLKERFRTVLRNIQELLDGETEAIDDFVTAILLFNMLFPDVDVIVDILQTMVKNPPKRRYYIFKGPVNTGKTTVAAAILALCTGASLNVNGTPDRLQFELGCAIDQFMVLFEDVKGTPEPDTNLPSGFGMVNLDNLRDHLEGSVPVNLERKHQNKVSQIFPPGIITMNNYVLPHTIQARARTLVNFKHIKVYAKALRNNISVLEQRLITKPETLLAYLLIRPESEKEISADLRAEFLTVIENLKFEVDERFFQYNNRLHEGLCVHE | Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription (By similarity).
PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A (By similarity).
Sequence Mass (Da): 67133
Sequence Length: 587
Domain: The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation.
Subcellular Location: Host nucleus
EC: 3.6.4.-
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P0DOJ4 | MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQGSPPRTAERGTEESGHSPLHDDYWSFSYGSKYFTREWNDFFRKWDPSYQSPPKTAESSEQPDLFCYEEPLLSPNPSSPTDTPAHTAGRRRNPCVAEPDDSISPDPPRTPVSRKRPRPAGATGGGGGGVHANGGSVFGHPTGGTSTPAHPPPYHSQGGSESMGGSDSSGFAEGSFRSDPRCESENESYSQSCSQSSFNATPPKKAREDPAPSDFPSSLTGYLSHAIYSNKTFPAFLVYSTKEKCKQLYDTIGKFRPEFKCLVHYEEGGMLFFLTMTKHRVSAVKNYCSKLCSVSFLMCKAVTKPMECYQVVTAAPFQLITENKPGLHQFEFTDEPEEQKAVDWIMVADFALENNLDDPLLIMGYYLDFAKEVPSCIKCSKEETRLQIHWKNHRKHAENADLFLNCKAQKTICQQAADGVLASRRLKLVECTRSQLLKERLQQSLLRLKELGSSDALLYLAGVAWYQCLLEDFPQTLFKMLKLLTENVPKRRNILFRGPVNSGKTGLAAALISLLGGKSLNINCPADKLAFELGVAQDQFVVCFEDVKGQIALNKQLQPGMGVANLDNLRDYLDGSVKVNLEKKHSNKRSQLFPPCVCTMNEYLLPQTVWARFHMVLDFTCKPHLAQSLEKCEFLQRERIIQSGDTLALLLIWNFTSDVFDPDIQGLVKEVRDQFASECSYSLFCDILCNVQEGDDPLKDICEYS | Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription.
PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A (By similarity).
Sequence Mass (Da): 87662
Sequence Length: 782
Domain: The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation.
Subcellular Location: Host nucleus
EC: 3.6.4.-
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P24851 | MELTSEEYEELRGLLGTPDIGNADTLKKAFLKACKVHHPDKGGNEEAMKRLLYLYNKAKIAASATTSQVPEYGTSQWEQWWEEFNQGFDEQDLHCDEELEPSDNEEENPAGSQAPGSQATPPKKPRTSPDFPEVLKEYVSNALFTNRTYNCFIIFTTAEKGKELYPCIQAAYKCTFIALYMYNGDSVLYIITVGKHRVNAMENLCSKKCTVSFLQAKGVLKPQEAYNVCCTFELISQNIQGGLPSSFFNPVQEEEKSVNWKLISEFACSIKCTDPLLLMALYLEFTTAPEACKVCDNPRRLEHRRHHTKDHTLNALLFQDSKTQKTICNQACDTVLAKRRLDMKTLTRNELLVQRWQGLFQEMEDLFGARGEEHLAHRMAAVMWLNALHPNMPDVIFNYIKMVVENKPKQRYLLLKGPVNCGKTTVAAGLIGLCGGAYLNINCPPERLAFELGMAIDQFTVVFEDVKGKKSSKSSLQTGIGFENLDNLRDHLDGAVPVNLERKHQNKVTQIFPPGIVTCNEYDIPLTVKIRMYQKVELLHNYNLYKSLKNTEEVGKKRYLQSGITWLLLLIYFRSVDDFTEKLQECVVKWKERIETEVGDMWLLTMKENIEQGKNILEK | Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription.
PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A.
Sequence Mass (Da): 70674
Sequence Length: 619
Domain: The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation.
Subcellular Location: Host nucleus
EC: 3.6.4.-
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P03075 | MDRILTKEEKQALISLLDLEPQYWGDYGRMQKCYKKKCLQLHPDKGGNEELMQQLNTLWTKLKDGLYRVRLLLGPSQDPNASTSTSRPGEFYNPDTGGYWSYSYGSAGYSDQQKKYWEEFFSKWDVNEDLTCQEELSSSEDEFTPWHPNPPPSPVSISSDSSSSSCDEEYPRNSSRKRKRVHANGSPNTPIQPNKRAHTPGGGRTTIRGDTDIPRTPARESQSTFGSYFNSTEELEEEISQTQQSHHNTTPKKPPPTVSPDDFPTILRGFLSHAIFSNKTQNAFIIYSTKEKCEVLYEQIDKYNPDYKGIFIMKQTEAFVMFMTPGKHRVAAVKSYCCKFCTVSFLLCKAVTKPLELYNCVAKCDDFQILKENKPGLYHFEFCDEKKEVKQIDWNFLTSFAVENELDDPLVIMGHYLEFSQCESSCKKCAEALPRMKVHWANHSQHLENAELFLHCKQQKSICQQAADNVLARRRLKVLESTRQELLAERLNKLLDQLKDLSPVDKHLYLAGVAWYQCMFPDFEMMLLDILKLFTENVPKKRNVLFRGPVNSGKTSLAAAIMNLVGGVALNVNCPADKLNFELGVAIDKFAVVFEDVKGQTGDKRHLQSGLGINNLDNLRDYLDGSVKVNLEKKHVNKRSQIFPPCIVTANEYFFPQTLYARFHKVYNFEVKDFLAKSLEENSYMGRHRVCQSPLTMLIALLWNVPTENFDKSLKEKVETEKKVLSDMCNFTTFAEMCLNIQRGADPLEAL | Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription (By similarity).
PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A (By similarity).
Sequence Mass (Da): 85988
Sequence Length: 751
Domain: The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation.
Subcellular Location: Host nucleus
EC: 3.6.4.-
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P19840 | MKFGLFFLNFINSTTVQEQSIVRMQEITEYVDKLNFEQILVYENHFSDNGVVGAPLTVSGFLLGLTEKIKIGSLNHIITTHHPVAIAEEACLLDQLSEGRFILGFSDCEKKDEMHFFNRPVEYQQQLFEECYEIINDALTTGYCNPDNDFYSFPKISVNPHAYTPGGPRKYVTATSHHIVEWAAKKGIPLIFKWDDSNDVRYEYAERYKAVADKYDVDLSEIDHQLMILVNYNEDSNKAKQETRAFISDYVLEMHPNENFENKLEEIIAENAVGNYTECITAAKLAIEKCGAKSVLLSFEPMNDLMSQKNVINIVDDNIKKYHMEYT | Function: Light-emitting reaction in luminous bacteria. The specific role of the beta subunit is unknown, but it is absolutely required for bioluminescence activity.
Catalytic Activity: a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu
Sequence Mass (Da): 37595
Sequence Length: 327
EC: 1.14.14.3
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P29239 | MNFGLFFLNFQPEGMTSEMVLDNMVDTVALVDKDDYHFKRVLVSEHHFSKNGIIGEPLTAISFLLGLTKRIEIGSLNQVITTHHPVRIGEQTGLLDQMSYGRFVLGLSDCVNDFEMDFFKRKRSSQQQQFEACYEILNEALTTNYCQADDDFFNFPRISVNPHCISEVKQYILASSMGVVEWAARKGLPLTYRWSDSLAEKEKYYQRYLAVAKENNIDVSNIDHQFPLLVNINENRRIARDEVREYIQSYVSEAYPTDPNIELRVEELIEQHAVGKVDEYYDSTMHAVKVTGSKNLLLSFESMKNKDDVTKLINMFNQKIKDNLIK | Function: Light-emitting reaction in luminous bacteria. The specific role of the beta subunit is unknown, but it is absolutely required for bioluminescence activity.
Catalytic Activity: a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu
Sequence Mass (Da): 37701
Sequence Length: 326
EC: 1.14.14.3
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P18300 | MKFGLFFQNFLSENQSSE | Function: Light-emitting reaction in luminous bacteria. The specific role of the beta subunit is unknown, but it is absolutely required for bioluminescence activity.
Catalytic Activity: a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu
Sequence Mass (Da): 2153
Sequence Length: 18
EC: 1.14.14.3
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P19841 | MCNAEFKGDCMIKKIPMIIGGAERDTSEHEYRELTLNSYKVSIPIINQDDVEAIKSQSVENNLNINQIVNFLYTVGQKWKSENYSRRLTYIRDLVRFLGYSPEMAKLEANWISMILSSKSALYDIVETELGSRHIVDEWLPQGDCYVKAMPKGKSVHLLAGNVPLSGVTSIIRAILTKNECIIKTSSADPFTAIALASSFIDTDEHHPISRSMSVMYWSHNEDIAIPQQIMNCADVVVSWGGYDAIKWATEHTPVNVDILKFGPKKSIAIVDNPVDITASAIGVAHDICFYDQQACFSTQDIYYIGDNIDAFFDELVEQLNLYMDILPKGDQTFDEKASFSLIEKECQFAKYKVEKGDNQSWLLVKSPLGSFGNQPLARSAYIHHVSDISEITPYIENRITQTVTVTPWESSFKYRDVLASHGAERIVESGMNNIFRVGGAHDGMRPLQRLVKYISHERPYTYSTKDVAVKIEQTRYLEEDKFLVFVP | Function: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
Catalytic Activity: a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain fatty acyl-CoA + H(+) + NADPH
Sequence Mass (Da): 55238
Sequence Length: 488
Pathway: Lipid metabolism; fatty acid reduction for biolumincescence.
EC: 1.2.1.50
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A0A218QX08 | MKISLVTWLITALCLMEIEEIDGDTPGNYPVDFQGIYYECIVYNRCERDCKIHGASYGYCYAGVCFCEYLPDENKNFWDVMKKQCDYMNN | Function: The edited BmKBTx-like may modulate voltage-gated sodium channels (Nav).
Sequence Mass (Da): 10569
Sequence Length: 90
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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A0A7S8MVN3 | MKIGVLFTIISMLCLLEVRKICSKKEGGYPRYFSFGYKCQNWGTNEYCRTVCQLHKGEYGYCYAGDCYCEGLTEENRLFWNVYRKYCKNPLFD | Function: The edited BmKBTx-like may modulate voltage-gated sodium channels (Nav).
Sequence Mass (Da): 11052
Sequence Length: 93
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q2NCA3 | MPLKGEISAQAGREFDTSRLDLRAIIDPRDLRVDPTRLFLETTQQTRLAICISDPHQPDCPVVYVNQAFLDLTGYAREEIVGRNCRFLQGADTDPEQVRKLREGIAAERYTVVDLLNYRKDGIPFWNAVHVGPIYGEDGTLQYFYGSQWDITDIVAERRKAETQRRIAAELRHRTGNIFAVLNAIIGLTSRRERDVSEFADKLSERVSALASAHRMTIMDEPDQEAVAIDDLVTGVMKPYRNRFAERVTTSGPKIELGPRSVTALGLALHELATNAVKYGALSVDAGRVEISWSREDGDVTLVWQEQGGPTVSQEQSEPVKGNGTMLIDGMIASLTGSIERDFAAAGLQAKITLPVHQPE | Function: Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light.
PTM: FMN binds covalently to cysteine after exposure to blue light and this bond is spontaneously broken in the dark.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 39975
Sequence Length: 360
EC: 2.7.13.3
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Q2NB77 | MAVGLAEHDKEAWGRLPFSLTIADISQDDEPLIYVNRAFEQMTGYSRSSVVGRNCRFLQGEKTDPGAVERLAKAIRNCEEVEETIYNYRADGEGFWNHLLMGPLEDQDEKCRYFVGIQVDMGQSESPDRATELDRQLAEVQHRVKNHLAMIVSMIRIQSSQAGGVGSQFDSLSRRVEALQLLYQEMDIAGAAKATDKIIPLGAYLGRIASAINHIDGRGAIKVNVQADTVDVPVETAGRIGLLVSEVLTNALQHAFSDRASGVVQLRSSVMSGEQLRVTVEDDGRGIPEDCDWPNEGNLGSRIVRQLVQGLGAELNVTRGGTGTIVNIDIPLSQQKTLIADERTKD | Function: Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light.
PTM: FMN binds covalently to cysteine after exposure to blue light and this bond is spontaneously broken in the dark.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 37948
Sequence Length: 346
EC: 2.7.13.3
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Q2NB98 | MLDMGQDRPIDGSGAPGADDTRVEVQPPAQWVLDLIEASPIASVVSDPRLADNPLIAINQAFTDLTGYSEEECVGRNCRFLAGSGTEPWLTDKIRQGVREHKPVLVEILNYKKDGTPFRNAVLVAPIYDDDDELLYFLGSQVEVDDDQPNMGMARRERAAEMLKTLSPRQLEVTTLVASGLRNKEVAARLGLSEKTVKMHRGLVMEKLNLKTSADLVRIAVEAGI | Function: Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark.
PTM: FMN binds covalently to cysteine after exposure to blue light, this bond is spontaneously broken in the dark; Cys-78 is 3.9 Angstroms from C4a of FMN in the dark, suggesting this is the adduct that is made.
Sequence Mass (Da): 24741
Sequence Length: 225
Domain: Light induces structural changes; in the dark protein is compact and resistant to exogenous protease, in the light protein is less compact while protease treatment generates an N-terminal fragment corresponding to approximately residues 14-156 (the LOV domain).
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P06962 | MKKIIICVILLAIMLLAACQVNNVRDTGGGSVSPSSIVTGVSMGSDGVGNP | Function: Lysis proteins are required for both colicin release and partial cell lysis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 5088
Sequence Length: 51
Subcellular Location: Cell outer membrane
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P83673 | MNGLILFCAVVFATAVCTYGSDAPCLRAGGRCQHDSITCSGRYRTGLCSGGVRRRCCVPSSSNSGSFSTGMVSQQCLRCICNVESGCRPIGCHWDVNSDSCGYFQIKRAYWIDCGSPGGDWQTCANNLACSSRCVQAYMARYHRRSGCSNSCESFARIHNGGPRGCRNSNTEGYWRRVQAQGCN | Function: Has antibacterial activity against the Gram-positive bacteria L.garvieae, M.luteus and Enterococcus sp., and the Gram-negative bacteria E.coli and V.vulnificus. Weak antibacterial activity against the Gram-negative bacterium A.hydrophila. No antibacterial activity detected against the Gram-positive bacterium S.iniae or against the Gram-negative bacterium E.ictaluri. Shows some chitinase activity but no isopeptidase activity.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 19986
Sequence Length: 184
Subcellular Location: Secreted
EC: 3.2.1.17
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Q870G1 | MGSNKIWLRAETKPAEARSALTPTTCKALIDAGYEVTVERSTQRIFDDDEFAKVGAPLVEEGSWVKDAPKDAYILGLKELPEDDFPLEHVHISFAHCYKEQAGWEKVLSRWPRGGGVLLDLEFLTDDAGRRVAAFGFSAGYAGAALAVKNWAWQLTHPEGEPLAGEKPYANQDLLIQSVKESLQAGQKQSGKSPKILVIGALGRCGKGAVQLAKDVGIPESDIIQWDMEETKKGGPFKEIVEDADIFVNCIYLSSKIPHFVNVESLSTPSRRLSVICDVSADTTNPNNPIPVYNITTTFDKPTVPVTLPNGTQGTPLSVISIDHLPSLLPRESSEMFSEALMPSLLQLKDRENARVWKQAEDLFNQKVATLPQTA | Function: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis.
Catalytic Activity: H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
Sequence Mass (Da): 41098
Sequence Length: 375
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
EC: 1.5.1.7
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Q27650 | MFALFLCIALASAKLGIDVSQPTSTSSFTCLRNKGFTTMVIVRAWKSTGSFDTNAPQTLKNANAAGFSIENSDVYYYPCISCGNMAGQVRTFWQKVGQYSLKVKRVWFDIEGTWTSSVSTNQNYLMQMMNEARAIGIVHGIYGSKYYWGNLFGSSYKYAYASSTPLWYPHYDNSPSFSDFSSFGGWTSPSMKQYRGDVSVCSAGVDYNYKP | Function: Has antibacterial activity against Gram-positive bacteria. No activity against S.aureus . Does not appear to have chitinase activity .
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 23562
Sequence Length: 211
Subcellular Location: Cytoplasmic granule
EC: 3.2.1.17
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P85152 | IAIQGGXGYLXQPGDGYKYA | Function: Has bacteriolytic activity.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 2094
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.2.1.17
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Q7YT16 | MKFFIVLVAALALAAPAMGKTFTRCSLAREMYALGVPKSELPQWTCIAEHESSYRTNVVGPTNSNGSNDYGIFQINNYYWCQPSNGRFSYNECHLSCDALLTDNISNSVTCARKIKSQQGWTAWSTWKYCSGSLPSINDCF | Function: May not function as a self-defense protein, but as a digestive enzyme, probably in the gut of the insect body. Inactive towards Micrococcus luteus. Active toward glycol chitin.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 15733
Sequence Length: 141
EC: 3.2.1.17
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Q7SFX6 | MAPTVLHLRSETKHLEHRSALTPTTTAELIKAGYIVNVERSPERIFDDEEFEKAGATLVPEHSWVDAPKEHIIVGLKELEEKDFPLKHVHVQFAHCYKQQAGWENVLARFPRGGGTLLDLEFLVDEHGRRVAAFGFHAGFAGAALALEVWAWQLNHSEPFPGVESYPNEDALIADVKKAVKEGVEAAGRLPRVIVIGARGRCGSGAVSALKKAGIPDENILDWDMAETAKGGPFKEITDSDIFVNCIYLTSKIPNFVNMESLQVPDRQLRVVCDVSADTTSPFTPVPIYTVATTFDKPTVPVDGLTSGPPLSVISIDHLPSLLPREASEAFSHDLLPSLLTLNDWQNSPVWARAKQLFDEKVATLPESALQK | Function: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis.
Catalytic Activity: H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
Sequence Mass (Da): 40877
Sequence Length: 372
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
EC: 1.5.1.7
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Q09694 | MVAPHLWLRAETKPLEERSALTPRTAKILADAGFQITIERSSQRAFKDKEFERLGFPMVPEGSWRHAPKDAYIIGLKELPENDNSPLKHTHIQFAHCYKNQEGWREVLSRFPAGNGLLYDLEFLQDDNGRRVAAFGYHAGFAGSAISCLVWAHQLLHPNKQFPAIRPFPNEKSLVRHVARQVRLALKKNNNQYPRILVIGALGRCGTGACDLASKIGIPFDNILRWDINETKKGGPFTEITESDIFVNCIYLSMPIPKFCTVESLNVPNRKLRVVCDVSCDTTNPNNPIPIYNVNTTFDHPTVEVKGVTTPPPLEVISIDHLPTLLPRESSEAFSEALIPSLLALKDVDNAPVWVRAKKLYETMVQKL | Function: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis.
Catalytic Activity: H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
Sequence Mass (Da): 41393
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
EC: 1.5.1.7
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P38998 | MAAVTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYRQAGAIIVPAGSWKTAPRDRIIIGLKEMPETDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDEDLPAVSPYPNEKALVKDVTKDYKEALATGARKPTVLIIGALGRCGSGAIDLLHKVGIPDANILKWDIKETSRGGPFDEIPQADIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPTVLVPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLPQRKTAPVWVRAKKLFDRHCARVKRSSRL | Function: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysine biosynthesis.
Catalytic Activity: H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
Sequence Mass (Da): 41465
Sequence Length: 373
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
Subcellular Location: Peroxisome
EC: 1.5.1.7
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I6XEI5 | MSVSRRDVLKFAAATPGVLGLGVVASSLRAAPASAGSLGTLLDYAAGVIPASQIRAAGAVGAIRYVSDRRPGGAWMLGKPIQLSEARDLSGNGLKIVSCYQYGKGSTADWLGGASAGVQHARRGSELHAAAGGPTSAPIYASIDDNPSYEQYKNQIVPYLRSWESVIGHQRTGVYANSKTIDWAVNDGLGSYFWQHNWGSPKGYTHPAAHLHQVEIDKRKVGGVGVDVNQILKPQFGQWA | Function: May function as a peptidoglycan hydrolase with glycosidase activity . In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4) .
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 25370
Sequence Length: 240
Pathway: Cell wall degradation; peptidoglycan degradation.
Subcellular Location: Secreted
EC: 3.2.1.17
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Q1XG90 | MNFLILFCVVASASVVYSSISDQCLRCICEVESGCRAIGCHWDVYSNSCGYFQIKQGYWTDCGSPGHSMESCADNYNCASGCVRSYMDHYIKYNGCADTCESYARMHNGGPNGCKSSHHHATDNYWRLVQAKGCS | Function: The main role of this lysozyme is in digestion. Has antibacterial activity against the Gram-positive bacterium P.cerevisiae and the Gram-negative bacteria E.coli and V.vulnificus. Shows some chitinase activity but no isopeptidase activity.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 14950
Sequence Length: 135
Subcellular Location: Secreted
EC: 3.2.1.17
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P35865 | MNTQSDSAGSQGAAATSRTVSIRTLIALIIGSTVGAGIFSIPQNIGSVAGPGAMLIGWLIAGVGMLSVAFVFHVLARRKPHLDSGVYAYARVGLGDYVGFSSAWGYWLGSVIAQVGYATLFFSTLGHYVPLFSQDHPFVSALAVSALTWLVFGVVSRGISQAAFLTTVTTVAKILPLLCFIILVAFLGFSWEKFTVDLWARDGGVGSIFDQVRGIMVYTVWVFIGIEGASVYSRQARSRSDVSRATVIGFVAVLLLLVSISSLSFGVLTQQELAALPDNSMASVLEAVVGPWGAALISLGLCLSVLGAYVSWQMLCAEPLALMAMDGLIPSKIGAINSRGAAWMAQLISTIVIQIFIIIFFLNETTYVSMVQLATNLYLVPYLFSAFYLVMLATRGKGITHPHAGTRFDDSGPEISRRENRKHLIVGLVATVYSVWLFYAAEPQFVLFGAMAMLPGLIPYVWTRIYRGEQVFNRFEIGVVVVLVVAASAGVIGLVNGSLSL | Function: Permease that is involved in the transport across the membrane of lysine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53630
Sequence Length: 501
Subcellular Location: Cell membrane
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Q8ZV07 | MGRIAKYYREYGIRIVKGFMQYVWDDKGQRYIDCNTNHGVVFLGHANPKIVEAVKKQVEEIWAVPLNFATPARERFIEEFSKLLPPKFGVVFLQNTGTEAVEVAIKIAKKVTRKPTIVAFTNSFHGRTMGSLSITWNEKYKKAFEPLYPHVRFGKFNVPHEVDKLIGEDTCCVVVEPIQGEGGVNPATPEFLKALREEAQRKGALLIFDEVQTGFGRTGAVWAFQKYGVEPDIFTAGKPVAGGLPIGLAVAREDFGDVFEPGEHGSTFAGNAVVMAAAAAASRLLREEDVPGRAERIGAELAKALGDTGSRLAVRVKGMGLMLGLELRVKADQFIQPLLERGVMALTAGVNTLRFLPPYMISKEDVEVVHAAVTEVLKKAEQQ | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: 2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Sequence Mass (Da): 42146
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.6.1.118
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Q7SI94 | MIKLLKFYQDRGIKIIKGEGQYVWDEKNNKYLDMHAGHGVAFLGHRNKVIIDHLKKQMEEISTLSLAFDTPIREEMIKELDELKPEDLDNLFLLNSGSEAVELALKIARKITKRRKIVAFKNSFHGRSMGALSVTWNKKYREPFEPLIGPVEFLEYNNVDSLKSITEDTAAVIVEPVQGEGGVIPAKKEFVKSLREVTEKVNALLIIDEVQTGFGRTGKIWAYQHFDIKPDILTAGKAIGGGFPVSAVFLPNWISEKIEEGDHGSTYGGNPLAAAAVTAACKVAKSEKIAEQAQKKGELFMRILKEKLEDFKIVREIRGLGLMIGIDLKVNPSIAIKVLQDEKVLSLKAGLTTIRFLPPYLITQSDMEWASDATRKGISETESKRVAS | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: 2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Sequence Mass (Da): 43323
Sequence Length: 388
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.6.1.118
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Q4JAP8 | MKLIQLYGDRGLTIVKGEAQYVWDIEGRRYLDFHTGIGVAFLGHRNPIILEYLKNQLENISILSTSFSTPIKDEMLQALDKVKPDKMDNAMLLNSGTEAVEAALKTARKITGRKKIIAFKNAFHGRTAGSLSVTWNKKYREPFEPLVGPVEFLTFNNIEDLSKIDNETAAVIVEPIQGESGVIPANIEFMKALKEKTENTGSLLIFDEIQTGFGRTGKLWAYKHYNIVPDILTAGKAIGGGFPVSVVFLPDHIANKLEEGDHGSTYGGNPMAMAAVTAACKVIEKENVVEQANQKGQQFSNILVKNLADLKVVREVRGKGLMIGIDIRFQPGQVLKYLQEKGILAVKAGSTVIRFLPSYLITYENMEEASNVLREGLLKIENKAVSS | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: 2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Sequence Mass (Da): 42743
Sequence Length: 387
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.6.1.118
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Q5JFW3 | MPLYRKRLRLVRGEGVYVWDEKGRRYLDLIAGIGVNVLGHAHPEWVLDMSRQLEKIVVAGPMFEHDEREEMLEELSHWVDYEYVYMGNSGTEAVEAAIKFARLATGRSEIVAMTNAFHGRTLGSLSATWKKKYREGFGPLVPGFKHIPFNNVEAAKEAITKETAAVIFEPIQGEGGIVPADEEFVKTLRDLTEDVGALLIADEVQSGLRTGKFLAIEHYGVRPDIVTMGKGIGNGFPVSLTLTDLEIPRGKHGSTFGGNPLACRAVATTLRILRRDRLVEKAGEKFMEFSGERVVKTRGRGLMIGIVLRRPAGNYVKALQERGILVNTAGNRVIRLLPPLIIEGDTLEEARKEIEGVLNDIL | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: 2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Sequence Mass (Da): 40170
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.6.1.118
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Q93R93 | METRTLEDWRALLEAEKTLDSGVYNKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVANLGHGNPEVVEAVKRQAETLMAMPQTLPTPMRGEFYRTLTAILPPELNRVFPVNSGTEANEAALKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYREPFLPLVEPVEFIPYNDVEALKRAVDEETAAVILEPVQGEGGVRPATPEFLRAAREITQEKGALLILDEIQTGMGRTGKRFAFEHFGIVPDILTLAKALGGGVPLGVAVMREEVARSMPKGGHGTTFGGNPLAMAAGVAAIRYLERTRLWERAAELGPWFMEKLRAIPSPKIREVRGMGLMVGLELKEKAAPYIARLEKEHRVLALQAGPTVIRFLPPLVIEKEDLERVVEAVRAVLA | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the transfer of the amino group of L-glutamate to [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine (Probable). In vitro, can use N(2)-acetyl-L-ornithine and N(2)-acetyl-L-lysine .
Catalytic Activity: 2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Sequence Mass (Da): 43451
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.6.1.118
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Q9YBY3 | MVSSDAYVEGLAAKLALDLLRVYTPTGSEERLYPVLERWASELGLGFSLDSAGNAVLSAGPDGLPVVGLVGHLDTVPGRLEARLEGYTLWGRGAVDAKGPLAAMILGLHLASSEGLSCSSAVLGLVGEEGDSPGAWSLVSRGDTPLHIIVGEPTGGDGVAIGYRGSLTIEIECTGHEGHSSNPERGAADMLVKALASILERDSRATVTRLKAGTAANITPGRALATVNMRFNEPGLEALQLASELCSSLHQHRCHCSSISLLHPVKTSLSNATARALVASLRTAGVKPRIVVKRGTSDMNVLSIATESIAAYGPGDPRLSHTKHENIRVGDIVKAAMIYSRTLTILCNSL | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine.
Catalytic Activity: [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-lysine
Sequence Mass (Da): 36495
Sequence Length: 350
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 5/5.
Subcellular Location: Cytoplasm
EC: 3.5.1.130
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Q9RUH3 | MTPTPDAQAARELIRQAVSIPSLSGEEQAIAAFLRDWMARRGFDAQVDEAGNAVGVRGSGPLTVALLGHMDTVPGDIPVRVDEAGVLHGRGSVDAKGSLCTFIAAVSALPPEALSAARFVCIGATEEEAPSSKGARYAMRQHRPDFVLIGEPSGWAGLTLGYKGRLVAKVRVEKDNFHTAGDGTSAADDLTLGWQRVREWAAGFAPADSGGGGIFDRVQVTLQDLGSSGDGLTQRAWATIGLRLPPALAPYQAEEAIEQAFAGLGADLTFTGHESAVRHPKDNALTRALRVAIREQGGTPTFKVKTGTSDMNVVAELWPVPTLAYGPGDSALDHTPEERLDLAEYDRAVAVLTSALTRLVGG | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine.
Catalytic Activity: [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-lysine
Sequence Mass (Da): 38041
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 5/5.
Subcellular Location: Cytoplasm
EC: 3.5.1.130
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Q8ZUG2 | MDVGELLEDVLRIYSPSHGEADLAKYLLEYLKRFVPDVWIDEAGNVIAVKGSGGPVVWLHAHMDTVPGPLPVKREGGVVWGRGAVDDKGPLVAYLKAFLDSNPRGTLVLALVTAEEDDSAGTEALLRGGPPRPDYVFVGEPTNLHIAYAYRGGAKVYIELESRGGHASSPIYDNIVEELFAVYQEVKRALGHAERYDAFTVTPTIIQCGEAPNKVPTKCVMVLDVRIPPGKSCRDLAQALPPKARAGPCTEPVEVSPTNPAARALTRALLKLGVEPKLSRKWGTADFNLLVSLTKNIAAFGPGDPALAHSEDERIDIAQVELAAKALKLAVEELGIIPRRL | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine.
Catalytic Activity: [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-lysine
Sequence Mass (Da): 36759
Sequence Length: 341
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 5/5.
Subcellular Location: Cytoplasm
EC: 3.5.1.130
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Q980W5 | MLQEKELVKQKAKELLLDLLSIYTPSKSEANATKFFEKISKDLNLKLEILPDSNSFILGEGDILLASHVDTVYGYIEPKIENELIYGRGAVDAKGPLISMIIATWLLNEKGIKVRVSGLADEESTSIGAKELIAKNYNFKYIIVGEPSNATDIVVEYRGSIQLDIMCEGTPEHSSSAKNNLIVDISKKIIEVYKQPENYDKPSIVPTIIRAGESYNVTPAKLYLHLDIRYAINNKREDLIKEITDKFPECNLKIVDETPPVKVSINNPVVKSLARALLKQNIKPRLVKKAGTSDMNILQRITTNIATYGPGNSMLEHTTQEKISLDEIYIGVKTYMLAIEELWQKI | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine.
Catalytic Activity: [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-lysine
Sequence Mass (Da): 38810
Sequence Length: 346
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 5/5.
Subcellular Location: Cytoplasm
EC: 3.5.1.130
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O33599 | MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR | Cofactor: Binds 1 zinc ion per subunit.
Function: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan.
Catalytic Activity: Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.
Sequence Mass (Da): 34317
Sequence Length: 316
Subcellular Location: Secreted
EC: 3.4.24.75
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Q9ZNI1 | MFVYYCKECFIMNKQQSKVRYSIRKVSIGILSISIGMFLALGMSNKAYADEIDKSKDFTRGYEQNVFAKSELNANKNTTKDKIKNEGAVKTSDTSLKLDNKSAISNGNEINQDIKISNTPKNSSQGNNLVINNNELTKEIKIANLEAQNSNQKKTNKVTNNYFGYYSFREAPKTQIYTVKKGDTLSAIALKYKTTVSNIQNTNNIANPNLIFIGQKLKVPMTPLVEPKPKTVSSNNKSNSNSSTLNYLKTLENRGWDFDGSYGWQCFDLVNVYWNHLYGHGLKGYGAKDIPYANNFNSEAKIYHNTPTFKAEPGDLVVFSGRFGGGYGHTAIVLNGDYDGKLMKFQSLDQNWNNGGWRKAEVAHKVVHNYENDMIFIRPFKKA | Function: Probably involved in peptidoglycan hydrolysis.
Sequence Mass (Da): 43183
Sequence Length: 383
Subcellular Location: Secreted
EC: 3.-.-.-
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P50468 | MARKDTNKQYSLRKLKTGTASVAVAVAVLGAGFANQTTVKANSKNPVPVKKEAKLSEAELHDKIKNLEEEKAELFEKLDKVEEEHKKVEEEHKKDHEKLEKKSEDVERHYLRQLDQEYKEQQERQKNLEELERQSQREVEKRYQEQLQKQQQLEKEKQISEASRKSLRRDLEASRAAKKDLEAEHQKLKEEKQISEASRKSLRRDLEASRAAKKDLEAEHQKLKEEKQISEASRQGLSRDLEASRAAKKDLEAEHQKLKEEKQISEASRQGLSRDLEASREAKKKVEADLAEANSKLQALEKLNKELEEGKKLSEKEKAELQAKLEAEAKALKEQLAKQAEELAKLKGNQTPNAKVAPQANRSRSAMTQQKRTLPSTGETANPFFTAAAATVMVSAGMLALKRKEEN | Function: This protein is one of the different antigenic serotypes of protein M. Protein M is closely associated with virulence of the bacterium and can render the organism resistant to phagocytosis.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 46466
Sequence Length: 407
Subcellular Location: Secreted
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P83330 | NHQLTQENERLTQK | Function: This protein is one of the different antigenic serotypes of protein M. Protein M is closely associated with virulence of the bacterium and can render the organism resistant to phagocytosis.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 1739
Sequence Length: 14
Subcellular Location: Secreted
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P0DOZ8 | CCQWPCSHGCIPCCY | Function: Does not show any effect on voltage-gated sodium and potassium channels (10 uM of toxin tested), and on nicotinic acetylcholine receptors (5 uM of toxin tested) . Does not show antibacterial activity on both Gram-negative and Gram-positive bacteria . Intraperitoneal injection into fish provokes paralysis (By similarity).
Sequence Mass (Da): 1703
Sequence Length: 15
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-2 branch, since 2 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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Q9V3Q6 | MATASLDALQAAYVDFSEITLREKVGHGSYGVVCKAVWRDKLVAVKEFFASAEQKDIEKEVKQLSRVKHPNIIALHGISSYQQATYLIMEFAEGGSLHNFLHGKVKPAYSLAHAMSWARQCAEGLAYLHAMTPKPLIHRDVKPLNLLLTNKGRNLKICDFGTVADKSTMMTNNRGSAAWMAPEVFEGSKYTEKCDIFSWAIVLWEVLSRKQPFKGIDNAYTIQWKIYKGERPPLLTTCPKRIEDLMTACWKTVPEDRPSMQYIVGVMHEIVKDYTGADKALEYTFVNQQIVTKESDGTVAAQPDSLSSQEGELSPSSTQLTPTTAANANVNAIAISKTTTSSMTENTSSTSSDITPTNSGQLDNNPLFYMVTNRWDAIPEEESNESRNDSFNLTSSAEATQRLETIRNGMILMACKPMEQLTLDVEANGFDLSPSESSSSSTNAKSDGRERLTVTDTKPVMMTTDLSNNNGGIHAHSNGLLSHANGWQARDEELQEQEHEQEIVNSLDVDVDPDEDENDGTEQSLAEILDPELQPEPPIPNDAESQLIYRDHRHMAKEYLSVDTNLYYAQDFKDKLIVQMDRTEREQKQELLRKMKDKEGLQSLYNNLQQQYASRQLAAGHHPQPHPHPHPNQLQHPHSHPPMHFLQDEGCGLLPGSVCGGSESVEEGWVVIPPHHNA | Function: Component of a protein kinase signal transduction cascade. Mediator of TGF-beta signal transduction. Responsible for activation of the JNK MAPK pathway (basket, bsk and hemipterous, hep) in response to LPS. Component of the NF-kappa-B pathway; relish-mediated JNK inhibition involves proteasomal degradation of Tak1; certain targets of Relish that are induced during immune responses may facilitate destruction of Tak1 and switch off the JNK cascade. Participates in diverse roles such as control of cell shape and regulation of apoptosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 75675
Sequence Length: 678
EC: 2.7.11.25
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O43318 | MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS | Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway . Plays an important role in the cascades of cellular responses evoked by changes in the environment . Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) . Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7 . These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1) . Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex . Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation . In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B . Promotes TRIM5 capsid-specific restriction activity . Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).
PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67196
Sequence Length: 606
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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P41279 | MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG | Function: Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the pro-inflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant.
PTM: Autophosphorylated . Isoform 1 undergoes phosphorylation mainly on Ser residues, and isoform 2 on both Ser and Thr residues . Phosphorylated on Thr-290; the phosphorylation is necessary but not sufficient for full kinase activity in vitro and for the dissociation of isoform 1 from NFKB1, leading to its degradation . Phosphorylated on Ser-400 by IKBKB; the phosphorylation is required for LPS-stimulated activation of the MAPK/ERK pathway in macrophages .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52925
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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Q07174 | MEYMSTGSDEKEEIDLLIKHLNVSEVIDIMENLYASEEPGVYEPSLMTMYPDSNQNEERSESLLRSGQEVPWLSSVRYGTVEDLLAFANHVSNMTKHFYGRRPQECGILLNMVISPQNGRYQIDSDVLLVPWKLTYRNIGSGFVPRGAFGKVYLAQDMKTKKRMACKLIPIDQFKPSDVEIQACFRHENIAELYGAVLWGDTVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHILKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVKMTEDVYLPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIAGDCSPGMRELIEAALERNPNHRPKAADLLKHEALNPPREDQPRCQSLDSALFERKRLLSRKELQLPENIADSSCTGSTEESEVLRRQRSLYIDLGALAGYFNIVRGPPTLEYG | Function: Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the pro-inflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52942
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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Q9I190 | MENATQPVPLIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDERPAHPSAGVERHLQADDLSQRLAEGSSEPSGAWRAELLEAVRAAWRVMWINRFRTALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMGAFGSNIIYLSGYSPNPRAPMGIVSSDDVAAIATLPQVKKVMPVNGGELVVRYGNIDYHAYVGGNNTDFPEILNWPVAEGSYFTERDEDAATTVAVIGYKVRKKLFGSANPIGRYILIENVPFQVIGVLAEKGSSSGDKDADNRIAIPYSAASIRLFGTRNPEYVIIAAADAQRVHQAERAIDQLMLRLHRGQRDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVLLLGQVAVAFSLSAIVGAFSCALVTGLVFGFMPARKAAQLDPVAALASQ | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70861
Sequence Length: 663
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q7ULB5 | MIQLYGLRKDYRVGDHDLPVLKGITLNIEAGEYVALMGSSGSGKTTLMNLLGSLDHPTDGDYHLAGIDVSSLTPLELAAFRSQHIGFVFQNFNLLPRATALDNVMLPTIYASDGRSRRECIEDATKLLESVGLGGRLDHMPNQLSGGERQRIAIARALMNRPKLLLADEPTGNLDTVTEQEILALFRQLNQEHGITLVVVTHDAEVAHEADRVVRMKDGLVAEDVRQRASTVDRSRLANSRAEPLREPASAWSLPATWNAIVVAVLALRRNALRTVLTMLGVIIGVASVISTMELSAGASTAIEETVASMGASMLTISPGKASSTSGRQRPIQIIPDDVVAVAEQCSAVKVAAPLVYSQVQLVRQNRRWSPNLALGTTSQYLAARNWDQLELGTPFTQEQVLDAAKVCILGKTVAHELFDSEYPIGEEIRVNGVPLRVVGVLTEKGGDVIGNDQDDIIIGPWTTFKLRVNSSTGATAQFSTFADQMPPMQLASTRRSTQREEIHQIYVEAESPDHVELARQQITQVLSRRHNVEPAGAYRINDITEVSKVVGQVVGGVSALGLVIAGVSLMVGGVGIMNIMLVSVTERTREIGLRMAVGANRSAILRQFLIEATVLCVVGGFIGIFAGHMWSVLVGRVIGWPTAMSIWAPIVAVTVAATVGIVFGYYPARTASRLNPIDALRYE | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73964
Sequence Length: 684
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q2RPB4 | MADTPPPLIELIDLERVFDSSEVPVRALDRVSLTIHEGEFVAIIGQSGSGKSTLMSILGCLDRPTGGLYRLGGIDVASLDPVALAGLRRDTFGFVFQRYNLLAGASAAENVEMPAVYAGQPRHQRLERAHALLDRLGMGARSGHFPNQLSGGQQQRVSIARALMNDPRVILADEPTGALDSASGRDVLALLEALHTEGRTVILITHDRDVAARAERVIALQDGRVVEDSGRPAPVGSDRPLGRPPGGAAYLGMAASFGEALKMAGRSLRANIFRTALTLLGVVIGVAAVVTMMAIGEGSKQDVLTRIQSMGTNLLLVRPGAPGIRPSGTDVSLTPTDAEAVAQLAGMAAVAPERMASGITVRREGIDYRTTINGTWPAYAAAKDWPMAWGSFFDATDLQASAPVAVLGQTVAKNLFPGEEDPVGSYFLVRNVPFLVIGVLEAKGATPFGQDQDDIVLIPLTTAFARVSGGRYLSSLTARVEDATTIDESQAAIESLLQARHGKVDFQVRNTQSLLEMVEKTQNSLTLLLGAVALISLLVGGIGVMNIMLVSVTERTREIGIRLATGARASDILLQFNTEAVAVCGVGGLAGVGLGLGAALAVAEFGLPVRFTPGPPIVAFCCAFLTGLLFGYLPARKAARLDPVVALSAE | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68262
Sequence Length: 650
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q8EIL8 | MTKPLLEVSACYRSFQAGEQQLTVLKDINLSIARGEMVAIVGASGSGKSTLMNILGCLDKPSKGAYFIDGQDTSQMDVDELAKLRREHFGFIFQRYHLLGDLNAVGNVEVPAVYAGKDRLERRDRAESLLSRLGLGERLDHKPNQLSGGQQQRVSVARALMNGGDVILADEPTGALDSHSGEEMMRLLQELHREGHTIIIVTHDMHVAQHADRIIEIKDGVIISDEPNLASQTAVKAQVDMSLAKPSGATRVAAWDRYAEALKMALLAMSTHRLRTFLTMLGIIIGIASVVSVVALGEGSQREILKSISSMGTNTIDIRPGLGFGDRRSARVRTLTASDANALKNLPYVDSVTPSISSSVTVRLGNKAVTASVNGVGPEFFRVRGYELAQGQFWDDDSVDALAQDAVIDDNTRKQLFPDSTGAMGSVIGQVIFLGDLPVRIIGVTKPKESAFGNSDALNVWVPYTTVSGRMVGKKYLDGITVRLDESVPSNAAEQGIITLLKMRHGTQDFFTINTDTIRQNIEKTTATMTLLISAIAVISLVVGGIGVMNIMLVSVTERTREIGVRMAVGARQSDILRQFLIEAVLVCLCGGALGVALAYLIGVVFAQAGGSFQMIYSTTSIVAAFACSTLIGVLFGFLPARNAARLDPVEALARE | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70560
Sequence Length: 656
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
A1RG29 | MSAALLEISGCYRTFQAGEQQLTVLKDVNLTIERGEMVAIVGASGSGKSTLMNILGCLDKPSKGAYFINGQDTSTMDADELAQLRREHFGFIFQRYHLLSDLTAIGNVEVPAVYAGKERSARKDRAEHLLTRLGLGDRLDHKPNQLSGGQQQRVSVARALMNGGDVILADEPTGALDSHSGEEMMQLLQELHSDGHTIIIVTHDMNVAQYADRIIEIKDGIIISDERKTKAPKHVDTAVTKINNRIRVASWDRYVEAFKMALLAMSTHRLRTFLTMLGIIIGIASVVSVVALGEGSQREILNSISSMGTNTIDIRPGFGFGDRRSGKVKTLIVKDADALKHLPYVDSVTPTVDSSMTLRYGNKAVTTVVNGVGPEFFRVRGYELAMGQFWDEDSVSSLAQDAVIDDKVRKELFPRSSPIGEVIFIGNLPVRIIGVTEPKDSVFGKSDSLNVWLPYTTLSGRIVGKNYLNGITVRLNESVPSNAAEQGIITLLKMRHGIEDFFTINTDAIRQNIEKTTATMTLLISAIAVISLIVGGIGVMNIMLVSVTERTREIGVRMAVGARQSDILRQFLIEAVLVCLCGGTLGIALAYLIGVVFAQTGGSFQMIYSTTSIVAAFACSTLIGVLFGFLPARNAARLDPVDALARE | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70308
Sequence Length: 647
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
O06927 | MEIMMGQGRLAIEKIVDPESFKENTIGESSFEDNEVGPGAVVGTAQIGDQDCTIIASDAMAMNERFPVVYAGIIGLEEGYKMAMAVYKTIEADKEKKGTEKRPILLIVDTPGNGPGKQEEIFGMNKSTGAYQLALAEARKAGHPIVAMVIGRAISGAFLCHGLQADRILSLSSKFETMIHVMPLTSVSVITKLDIERLEELSKTNPVFAAGPDFFYQLGGVEELVEEVDGMRSCILKHIAEIREMKAAGEEARLGPWGRGALGEQRGGRMIRGKVMAMMDKQFFAFAEQNLY | Function: Gamma subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). The two subunits MADC and MADD are required for the transfer of the malonate carboxy group from the acyl-carrier protein (ACP) to the prosthetic group of the biotin carrier MADF. Required for the regeneration of ACP.
Catalytic Activity: malonyl-[ACP] + N(6)-biotinyl-L-lysyl-[protein] = acetyl-[ACP] + N(6)-carboxybiotinyl-L-lysyl-[protein]
Sequence Mass (Da): 31829
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.1.3.10
|
O06930 | MEIKSKMPGSIIEVKVSVGDNLEAGSLILIMEALKMKQEIRSQEGGVVKELKVNTGDRVSPGQVLAIIE | Function: Biotin-carrier subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). The carboxyl group of the carboxylated biotin carrier is released by the membrane-bound carboxybiotin decarboxylase MADB.
Sequence Mass (Da): 7436
Sequence Length: 69
Subcellular Location: Cytoplasm
EC: 4.1.1.-
|
O06928 | MAEQLKELAEMVESFGTAPTMGEMPCRTLATKGINGPTAAHVIEEIHTPFNLAYVTFTTGSTAFQNVVGVTHSEIDGRVRASLAAFDMANVERHGKFLVTYAPLVNVFSAEALKIHGLDWFFLQRSSRDAFLLSLCQEKPNVLIGESTFIRSALEDASVLGLSHSIPQGVIAFTAGTPLDLDLLQVAEKHNWKIHDLYGCQEFGWLTLDGVPLRADITLIPSPKGSDFREFVVGGLPMADSFPYAESGHVCNPEGKIITYRRARTNPEYEVIVRETKLSSKETTERVARTILRIKGRVVKVDPALKVSSTKTVLDLVPSVSAEGKSTSESYRIEGDDKTFLFETLIEAQLALQQTAKTDQVWKKTR | Function: Acyl-carrier protein (ACP) acetate ligase of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). Involved in the conversion of the thiol group of the ACP-bound 2'-(5-phosphoribosyl)-3'-dephospho-CoA prosthetic group into its acetyl thioester using the energy from the hydrolysis of ATP.
Catalytic Activity: acetate + ATP + holo-[ACP] = acetyl-[ACP] + AMP + diphosphate
Sequence Mass (Da): 40347
Sequence Length: 366
Subcellular Location: Cytoplasm
EC: 6.2.1.35
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Q27908 | MYLHLTALCVVIPLCYGASMFKHDHYMDNGVRYPNGDGICKQLNETKCDAGFSYDRSICEGPHYWHTISKCFIACGIGQRQSPINIVSYDAKFRQRLPKLKFKPHMEKLKTEVTNHQNRAPEFEPEDGENLYVKLNNLVDGHYKFHNLHVHNGRTRRKGSEHSVNGRFTPMEAHLVFHHDDQTHFEPTRTKLGGAFPGHNDFVVVGVFLEVGDDGFGDEPDDEECKHILKGHHPDNNENGNGDNGNNGYNGDNGNNGDNGNNSYNGDNGNNGVNGNNGYNGDNGNNGDNGNNGYNGDNGNNGDNGNNGENGNNGENGNNGENGHKHGCRVKKAKHLSRILECAYRNDKVREFKKVGEEEGLDVHLTPEMALPPLKYRHYYTYEGSLTTPPCTESVLWVVQKCHVQVSRRVLHALRNVEGYKDGTTLRKYGTRRPTQKNKVTVYKSFK | Function: Acts as a negative regulator for calcification in the shells of mollusks. May function both as a calcium concentrator and as a carbonic anhydrase required for production of carbonate ions, which are assembled to CaCO(3) at mineralization sites. Is important for shell formation in both the calcitic prismatic layer and the aragonitic nacreous layer.
PTM: N-glycosylated.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 50114
Sequence Length: 447
Subcellular Location: Secreted
EC: 4.2.1.1
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P55296 | MKSLNVILTLLSLIISVLSKKVYYEAEDGKLNGITVFKELSGFSGKGYVGRFENPGNSVTVTVDAPATGMYDLSIIYCANMGQKINSLTVNDQSVGDITFTENTKFETKDVGAVYLNKGKNTIGLVSSWGWMWVDAFVINDAPNAAKDVSSKLNPTLVNPKAIPAAKKLYDFLKTNYGKRILSGQVGAAGQAGDEGQEIQRIQKATGKLPAVWNMDFIFESNDCTWRPQNPDITEMAINWWKKYEGKGIMAAQWHWNIAGKTGDFAFYSKDTTFNLENAVTEGTWEYEKIIKDIDRVSGHIKKLQAVNMPLIWRPLHENNGDWFWWGNNPKACAKLWKILYERMVNYHGLNNLIWLWNGNNDANTPVDYIDIIGVDIYANDHGPQTTAYNTHFDFYGGKKMVVLSENGRIPDIQQCVDQDVWWGYFQTWNSEFILQDSYHTDAQLKEYFNHKTVMNMDELPSFNVDSYNGDSGSSHNGNSESNSNTGNSDECWSINLGYPCCIGDYVVTTDENGDWGVENNEWCGIVHKSCWSEPLGYPCCVGNTVISADESGDWGVENNEWCGIVHKSCWAEFLGYPCCVGNTVISTDEFGDWGVENDDWCGILN | Function: Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. Shows very high activity against mannohexaose but not against mannopentaose and smaller mannooligosaccharides. The major products released from mannooligosaccharide hydrolysis are mannose and mannobiose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 68055
Sequence Length: 606
Domain: Consists of a catalytic N-terminal domain linked to a reiterated non-catalytic C-terminal domain.
EC: 3.2.1.78
|
B2B3C0 | MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA | Function: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose . Also has transglycosylation activity .
PTM: Not glycosylated.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 41183
Sequence Length: 373
Subcellular Location: Secreted
EC: 3.2.1.78
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P49425 | MTLLLVWLIFTGVAGEIRLEAEDGELLGVAVDSTLTGYSGRGYVTGFDAPEDSVRFSFEAPRGVYRVVFGVSFSSRFASYALRVDDWHQTGSLIKRGGGFFEASIGEIWLDEGAHTMAFQLMNGALDYVRLEPVSYGPPARPPAQLSDSQATASAQALFAFLLSEYGRHILAGQQQNPYRRDFDAINYVRNVTGKEPALVSFDLIDYSPTREAHGVVHYQTPEDWIAWAGRDGIVSLMWHWNAPTDLIEDPSQDCYWWYGFYTRCTTFDVAAALADTSSERYRLLLRDIDVIAAQLQKFQQADIPVLWRPLHEAAGGWFWWGAKGPEPFKQLWRLLYERLVHHHGLHNLIWVYTHEPGAAEWYPGDAYVDIVGRDVYADDPDALMRSDWNELQTLFGGRKLVALTETGTLPDVEVITDYGIWWSWFSIWTDPFLRDVDPDRLTRVYHSERVLTRDELPDWRSYVLHATTVQPAGDLALAVYPNPGAGRLHVEVGLPVAAPVVVEVFNLLGQRVFQYQAGMQPAGLWRRAFELALAPGVYLVQVRAGNLVARRRWVSVR | Function: Acts as endo-acting enzyme with a requirement for at least five sugar moieties for effective catalytic activity. Hydrolyzes carob-galactomannan (locust bean gum) effectively and to a smaller extent guar gum, but not yeast mannan.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 63120
Sequence Length: 558
EC: 3.2.1.78
|
P25081 | MQKLINSVQNYAWGSKTALTELYGIANPQQQPMAELWMGAHPKSSSRITTANGETVSLRDAIEKNKTAMLGEAVANRFGELPFLFKVLCAAQPLSIQVHPNKRNSEIGFAKENAAGIPMDAAERNYKDPNHKPELVFALTPFLAMNAFREFSDIVSLLQPVAGAHSAIAHFLQVPNAERLSQLFASLLNMQGEEKSRALAVLKAALNSQQGEPWQTIRVISEYYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEPKPAGELLTAPVKSGAELDFPIPVDDFAFSLHDLALQETSIGQHSAAILFCVEGEAVLRKDEQRLVLKPGESAFIGADESPVNASGTGRLARVYNKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 42591
Sequence Length: 391
Subcellular Location: Cytoplasm
EC: 5.3.1.8
|
Q59935 | MAEPLFLQSQMHKKIWGGNRLRKEFGYDIPSETTGEYWAISAHPNGVSVVKNGVYKGVPLDELYAEHRELFGNSKSSVFPLLTKILDANDWLSVQVHPDNAYALEHEGELGKTECWYVISADEGAEIIYGHEAKSKEELRQMIAAGDWDHLLTKIPVKAGDFFYVPSGTMHAIGKGIMILETQQSSDTTYRVYDFDRKDDQGRKRALHIEQSIDVLTIGKPANATPAWLSLQGLETTVLVSSPFFTVYKWQISGSVKMQQTAPYLLVSVLAGQGRITVGLEQYALRKGDHLILPNTIKSWQFDGDLEIIASHSNEC | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 35374
Sequence Length: 316
EC: 5.3.1.8
|
O74168 | MRALPTTATTLLGVLFFPSASRSQYVRDLGTEQWTLSSATLNRTVPAQFPSQVHMDLLREGIIDEPYNDLNDFNLRWIADANWTYTSGKIEGLGEDYESTWLVFDGLDTFASISFCGQFVGATDNQFRQYMFDVSSILKACPEEPTLGIQFGSAPNIVDAIAQDPSSPTWPEGVQITYEYPNRWFMRKEQSDFGWDWGPAFAPAGPWKPGYVVQLKQAAPVYVRNTDLDIYRLGQINYLPPDQTQPWVVNASLDYLGSLPENPSMAIEVKDLQSGEILASRPLTNITVTEGSVTGVTVLEGVDPKLWWPQGLGDQNLYNVTISVTDGGNQSVAEVTKRTGFRTIFLNQRNITDAQLAQGIAPGANWHFEVNGHEFYAKGSNLIPPDCFWTRVTEDTMTRLFDAVVAGNQNMLRVWSSGAYLHDYIYDLADEKGILLCSEFQFSDALYPTDDAFLENVAAEVVYNVRRVNHHPSLALWAGGNEIESLMLLLVEAADPESYPFYVGEYEKMYISLFLPLVYENTRSISYSPSSTTEGYLDIDLSAPVPMAERYSNTTEGEYYGDTDHYNYDASIAFDYGTYPVGRFANEFGFHSMPSLQTWQQALTDPADLTFNSSVVMLRNHHYPAGGLMTDNYHNTVARHGRNDPGRAGLLPDAQHSVRPRGQLQRLVPRDPALPGGPLQVTNPVLPAGQRAARTPARVPVLAARGHLAGALVGGDRVRRPLEGPHYVARDIYKPVIVSPFWNYTTGALDIYVTSDLWTAAAGSVTLTWRDLSGKPIASNGGLPTKPLPFHVGALNSTRLYRMNMKQQPLPRHEDAILALELTATGSLPNTDEEVTFTHEQWFTPAFPKDLDLVNLRVRVEYDAPLGKFAVEATAGVALYTWLEHPEGVVGYFEENSFVVVPGQKKVVGFVVQADETDGEWVHDVTVRSLWDLNEGE | Function: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan. Releases the terminal mannose residue from mannotriose and is somewaht less active on other mannooligosaccharides.
PTM: N-glycosylated.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Mass (Da): 104216
Sequence Length: 937
Pathway: Glycan metabolism; N-glycan degradation.
Subcellular Location: Secreted
EC: 3.2.1.25
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A2QWU9 | MRHSIGLAAALLAPTLPVALGQYIRDLSTEKWTLSSRALNRTVPAQFPSQVHLDLLRAGVIGEYHGLNDFNLRWIAAANWTYTSQPIKGLLDNYDSTWLVFDGLDTFATISFCGQQIASTDNQFRQYAFDVSTALGSCKGDPVLSINFGSAPNIVDAIAQDSNSQKWPDDVQLTYEYPNRWFMRKEQSDFGWDWGPAFAPAGPWKPAYIVQLDKKESVYVLNTDLDIYRKGQINYLPPDQSQPWVVNASIDILGPLPTKPTMSIEVRDTHSGTILTSRTLNNVSVAGNAITGVTVLDGLTPKLWWPQGLGDQNLYNVSITVQSRGNQTVASVNKRTGFRTIFLNQRNITEAQRAQGIAPGANWHFEVNGHEFYAKGSNLIPPDSFWTRVTEEKMSRLFDAVVVGNQNMLRVWSSGAYLHDYIYDLADEKGILLWSEFEFSDALYPSDDAFLENVAAEIVYNVRRVNHHPSLALWAGGNEIESLMLPRVKDAAPSSYSYYVGEYEKMYISLFLPLVYENTRSISYSPSSTTEGYLYIDLSAPVPMAERYDNTTSGSYYGDTDHYDYDTSVAFDYGSYPVGRFANEFGFHSMPSLQTWQQAVDTEDLYFNSSVVMLRNHHDPAGGLMTDNYANSATGMGEMTMGVVSYYPIPSKSDHISNFSAWCHATQLFQADMYKSQIQFYRRGSGMPERQLGSLYWQLEDIWQAPSWAGIEYGGRWKVLHHVMRDIYQPVIVSPFWNYTTGSLDVYVTSDLWSPAAGTVDLTWLDLSGRPIAGNAGTPKSVPFTVGGLNSTRIYGTNVSSLGLPDTKDAVLILSLSAHGRLPNSDRTTNLTHENYATLSWPKDLKIVDPGLKIGHSSKKTTVTVEATSGVSLYTWLDYPEGVVGYFEENAFVLAPGEKKEISFTVLEDTTDGAWVRNITVQSLWDQKVRG | Function: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Mass (Da): 104026
Sequence Length: 931
Pathway: Glycan metabolism; N-glycan degradation.
Subcellular Location: Secreted
EC: 3.2.1.25
|
Q9UUZ3 | MRHSIGLAAALLAPTLPVALGQHIRDLSSEKWTLSSRALNRTVPAQFPSQVHLDLLRAGVIGEYHGLNDFNLRWIAAANWTYTSQPIKGLLDNYGSTWLVFDGLDTFATISILWTANRIHGQSVSPVSGSMYLPALEACQRRILIRKVSFRGGVTAEVNTCYLHIEWPDDVQLTYEYPNRWFMRKEQSDFGWDWGPAFAPAGPWKPAYIVQLDKKESVYVLNTDLDIYRKNQINYLPPDQSQPWVVNASIDILGPLPAKPTMSIEVRDTHSGTILTSRTLNNVSVAGNAITGVTVLDGLNPKLWWPQSSVIRTSTMFLSLSKVEGTRPWPVWTNGRASAPFFLNQRNITEVQRAQGIAPGANWHFEVNGHEFYAKGSNLIPPDSFWTRVTEERISRLFDAVVVGNQNMLRVWSSGAYLHDYIYDLADEKGILLWSEFEFSDALYPSDDAFLENVAAEIVYNVRRVNHHPSLALWAGGNEIESLMLPRVKDAAPSSYSYYVGEYEKMYISLFLPLVYENTRSISYSPSSTTEGYLYIDLSAPVPMAERYDNTTSGSYYGDTDHYDYDTSVAFDYGSYPVGRFANEFGFHSMPSLQTWQQAVDTEDLYFNSSVVMLRNHHDPAGGLMTDNYANSATGMGEMTMGVISYYPIPSKSDHISNFSAWCHATQLFQADMYKSQIQFYRRGSGMPERQLGSLYWQLEDIWQAPSWAGIEYGGRWKVLHHVMRDIYQPVIVSPFWNYTTGSLDVYVTSDLWSPAAGTVDLTWLDLSGRPIAGNAGTPKSVPFTVGGLNSTRIYGTNVSSLGLPDTKDAVLILSLSAHGRLPNSDRTTNLTHENYATLSWPKDLKIVDPGLKLGYSSKKTTVTVEATSGVSLYTWLDYPEGVVGYFEENAFVLAPGEKKEIGFTVLDDTTNGAWVRNITVQSLWDQKVRG | Function: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan. Releases the terminal mannose residue from mannobiose and mannotriose, as well as from galactosyl-mannobiose (GM2), galactosyl-mannotriose (GM3) and di-galactosyl-mannopentaose (G2M5).
PTM: N-glycosylated.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Mass (Da): 104390
Sequence Length: 931
Pathway: Glycan metabolism; N-glycan degradation.
Subcellular Location: Secreted
EC: 3.2.1.25
|
Q2UN00 | MRFTATAAALVASSIPATLGQHVRDLSNEKWTLSSDALNHTVPGNLPSHAHLDLLKAGVIDDPYHGLNDFNLRWIPESNWTYTTDKIKDLMPIEFCGKYVASTNNQYRQYSFDVSQILEGCNEDPILKIDFGSAPNIVNAIAEDRNSPVWPDGIQQTYEYPNRWFMRKEQSDFGWDWGPAFAPAGPWKPAYIVQLPKAQNIHVLNTDLDIYRKGQINHLPPDQSQPWVVNASIDFVGSLPPNPSMSIEFKDTKSGEILTSKRIGNVTVSGNSVTGVTVLGGVTPKLWWPLGLGDQNLYNITVTVTGHQNQTLAHVTKRTGFRTIFLNQRNITDAQLAQGIAPGANWHFEVNGHEFYAKGSNIIPPDAFWPRVTEARMARLFDAVVAGNQNMLRVWSSGIYLHDFIYDLADERGILLWSEFEFSDALYPVDDAFLDNIAAEVVYNVRRVNHHPSLALWAGGNEIESLMLPTVERKAPEEYAKYVGEYEKLYISLILPLVYQNTRSITYSPSSTTEGYLDVDLSAPVPMVERYHNTTPGSYYGDTDFYNYDSSVSFNSHVYPVGRFANEFGYHSMPSLQTWQQAVDPEDLHFNSTTVMLRNHHYPAGGTFTDNFHNTSLGMGEMTIAVQRYYPIPNKLDSVANFSAWCHATQLFQADMYKSEIQFYRRGSGMPERQLGSLYWQLEDIWQAPSWAGIEYGGRWKVLHYVSRDIYQPIIVSPFWNYTTGDLDLYVTSDLWESAKGKVNLTWLDLSGTPLPHNAGTPGSVPFNVGALNTTKIYSTNIKNLTLPNPKDAILVLSLSGEGHLPNSDKKTTFTHQNHFTPVFPKDLALVDPGLELSYNTKSKTFTVEAKSGVSLYTWLDYPADVVGYFDENAFVLLPGQKKEIGFTVQEDNTDGKWVQGVTVQSLWNQTLEK | Function: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Mass (Da): 102870
Sequence Length: 914
Pathway: Glycan metabolism; N-glycan degradation.
Subcellular Location: Secreted
EC: 3.2.1.25
|
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