ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q49V09 | MLNNEYKNSALKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIIQPTSNPVNLHLMELLIMIDACRRASAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGADRMIALDLHAPQIQGFFDMPIDHLMGVPILAQYFKNETDIDPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGEIEGRTAIIIDDIIDTAGTITLAAQALKDKGAKDVYACCTHPVLSGPAKERIENSAIKELVVTNSIQLDEKRKPENTKELSVAGLLAQAIIRVYERESVSVLF... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
Q9K3U0 | MTGIKTTGEKKMMFFSGRAHPELAEEVAQQLGVGVVPTKAFDFANGEIYVRYQESARGADCFLIQSHTAPINKWVMEQLIMIDALKRASARSITVIVPFYGYARQDKKHRGREPISARLIADLMKTAGADRILAVDLHTDQIQGFFDGPVDHLFALPLLADYVGAKVDRSKLTVVSPDAGRVRVADRWCDRLGAPLAIVHKRRDKDVANQVTVHEVVGDVKGRICVLVDDMIDTGGTICAAADALFAHGAEDVIVTATHGVLSGPAADRLKNSKVSEFVFTNTLPSASELELDKITVLSIAPTIARAVREVFEDGSVTSL... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
Q55848 | MSAVSRIATLTRQSMLSALSDNNRLRLFSGSSNPSLSQEVARYLGMDIGPMLRKRFADGELYIQIQESIRGGDVYLIQPCCHPVNDNLMELLIMIDACRRASARQITAVLPYYGYARADRKTAGRESISAKLVANLITGAGAQRVLAMDLHSAQIQGYFDIPCDHMYGSPVIIDYLKSKQLTDLVVVSPDVGGVARARAFAKKLNDAPLAIIDKRRQSHNVAEVLNLIGDVDGKTAVLVDDMIDTAGTLSEGSRLLRAQGARQVYACATHAVFSEPAINRLSGGLFEEVIVTNTIPVPDDHHFPQLTILSVANLIGEAIW... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
B7IFM5 | MQIAKNEMKIFSGNANRELAIKVSEYIGTRLADCEVGRFADGEINVKIGETVRGHDTFIIQPTCPPVNENLMELLIMIDALKRASANSIAVVIPYYGYARQDRKAKGRDPITAKLVANLLTVAGATRVMTVDLHSEQIQGFFDIPLDNLWSFPIFAKKLKEDKIVDDDYVIVSPDVGGVKRARQFAERLGGPLAILDKRRPKDNVAEILNIIGEVEGKTAIIVDDIADTARSLVNAAKAIKEKGAKRVIACITHPVLSDGAIERIQNSEIEKIYISDSISHSNLPDKFSVVSLAPLLGEAIVRVRKNLSISILFRQ | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
O52958 | MFLLGSGGKHFEDELRNAGAKILEVEIKRFPDGEKYVRVMGNGDEATVVSSTFYPQDEKIVELLLLGDALREKGFEKLKLVVPYFAYSRQDRVTKDGEPISVRAVMRALGIYYEELYIFDTHNPETLRFFPGKAVNVSPARVIGEYFREKLGDGLVLAPDKGALERARAVAEVLGLEYSHFEKRRISPTEVEMHPVDVDVKGKNVLIVDDIISTGGTMVRAAELLRKLGAKKIYVSATHGVFAEGAIERVSRAVDELAVTNTIPTPVSRISIVPELLKLE | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use CTP and GTP as substrates in addition to ATP.
Cataly... |
Q40545 | MSQALNFFVSSSSRSPATFTISRPSVFPSTGSLRLLVKKSLRTLVVEASSAAASDLDEPQSSPVLVSENGSGGVLSSATQEYGRNAAPGTDSSSIEVDTVTEAELKENGFRSTRRTKLICTIGPATCGFEQLERLAEGGMNVARINMCHGTREWHRMVIERLRRLNEEKGFAVAIMMDTEGSEIHMGDLGGASSAKAEDGEIWNFTVRSFDPPLPERTVTVNYDGFAEDVKVGDELLVDGGMVRFEVIEKIGPDVKCLCTDPGLLLPRANLTFWRDGKLVRERNAMLPTISSKDWLDIDFGIAEGVDFIAVSFVKSAEVI... | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 65228
Sequence Length: 593
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Plastid
EC: 2.7.1.40
|
B8BM17 | MHSTNLLLEEPIRMASILEPSKPSFFPAMTKIVGTLGPKSRSVDTISSCLKAGMSVARFDFSWGDAEYHQETLENLKVAIKSTKKLCAVMLDTVGPELQVVNKSEASISLEENGTVILTPDQGQEASSQVLPINFAGLAKAVKPGDTIFVGQYLFTGSETTSVWLEVSQIKGDDVVCVIKNTATLAGSLFTLHCSQIHIDLPTLSDEDKEVIRKWGAPNKIDFLSLSYTRHVEDVRQAREFLSKLGDLSQTQIFAKIENVEGLNNFDEILQEADGIILSRGNLGIDLPPEKVFLFQKSALHKCNMAGKPAVVTRVVDSMT... | Function: Key regulatory enzyme of the glycolytic pathway that catalyzes the final step of glycolysis, converting ADP and phosphoenolpyruvate (PEP) to ATP and pyruvate by essentially irreversible transphosphorylation.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 57442
Sequen... |
P22200 | MANIDIAGIMKDLPNDGRIPKTKIVCTLGPSSRTVPMLEKLLRAGMNVARFNFSHGTHEYHQETLDNLKIAMQNTQILCAVMLDTKGPEIRTGFLTDGKPIQLKEGQEITVSTDYTIKGNEEMISMSYKKLVMDLKPGNTILCADGTITLTVLSCDPPSGTVRCRCENTATLGERKNVNLPGVVVDLPTLTEKDKEDILEWGVPNNIDMIALSFVRKGSDLVNVRKVLGPHAKRIQLMSKVENQEGVINFDEILRETDSFMVARGDLGMEIPVEKIFLAQKMMIYKCNLAGKAVVTATQMLESMIKSPAPTRAEATDVAN... | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 55170
Sequence Length: 510
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.40
|
Q42806 | MANIDIEGILKQQQPYDGRVPKTKIVCTLGPASRSVEMTEKLLRAGMNVARFNFSHGTHDYHQETLNNLKTAMHNTGILCAVMLDTKGPEIRTGFLKDGKPIQLKEGQEVTITTDYDIKGDPEMISMSYKKLPVHLKPGNTILCSDGTITLTVLSCDPDAGTVRCRCENTATLGERKNVNLPGVVVDLPTLTEKDKEDILGWGVPNKIDMIALSFVRKGSDLVNVRKVLGPHAKNIQLMSKVENQEGVLNFDEILRETDAFMVARGDLGMEIPVEKIFLAQKMMIYKCNLVGKPVVTATQMLESMIKSPRPTRAEATDVA... | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 55302
Sequence Length: 511
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.40
|
P55964 | NAQSHDNVVSIMLDTKGPEVRSGDVPQPMLKEGQEFNPTIRRGVSTQDTVSVNYDDFVNDVVVGDILLVDGGMMSLAVKSKTSDLVKCVVVDGGELKSRRHLNVRGKSARLPSITDKDWGDIKFGVDNQVDFYAVSFVKDAKVVHELKEYLKRCNADIHVIVKIESADSIPNLHSIISASDGAMVARGDLGAELPIEEVPLLQEDIIRRCHSMQKPVIVATNMLESMINHPTPTRAEVSDIAIAVREGADAVMLSGETAHGKYPLKAVRVMHTVALRTESSSPVNTTPPAQGAYKGHMGEMFAFHATIMANTLNTPIIVF... | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 46007
Sequence Length: 418
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Plastid
EC: 2.7.1.40
|
P77983 | MKKTKIVCTIGPKTESEEMLSKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKKAAILLDTKGPEIRTIKLEGGNDVSLKAGQTFTFTTDKSVVGNNEIVAVTYEGFTSDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVVEIREHLKAHGGENIQIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKY... | Function: Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 50657
Se... |
Q55863 | MPALINPVKFMRPLSHRTKIVATIGPASSSVEVIRQMVDAGMNVARLNFSHGSYEDHATMVRLLRSVEQEMDTPITLLQDLQGPKIRIGQLPGGEKQLREGEKVSLVPVEIGDRHPGAVGIDYPHLATEAKVGERILLDDGLLEMKVVSIQDPEVICEVVTGGILKSRKGVNLPGLVLTLPSMTTKDKQDLEFGLSQGIDWVSLSFVRKGEDIHTLKQFLAERGHPDLPVIAKIEKPQAIDNLEEIVAVSNGIMVARGDLGVEVNPEKVPRLQKEIIRRCNVRAIPVITATQMLDSMIQNSRPTRAEASDVANAILDGTD... | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 53105
Sequence Length: 483
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
|
P54644 | MSTAPIKHEGFLTKEGGGFKSWKKRWFILKGGDLSYYKTKGELVPLGVIHLNTSGHIKNSDRKKRVNGFEVQTPSRTYFLCSETEEERAKWIEILINERELLLNGGKQPKKSEKVGVADFELLNLVGKGSFGKVIQVRKKDTGEVYAMKVLSKKHIVEHNEVEHTLSERNILQKINHPFLVNLNYSFQTEDKLYFILDYVNGGELFYHLQKDKKFTEDRVRYYGAEIVLALEHLHLSGVIYRDLKPENLLLTNEGHICMTDFGLCKEGLLTPTDKTGTFCGTPEYLAPEVLQGNGYGKQVDWWSFGSLLYEMLTGLPPFY... | Function: Predominantly involved during the aggregation to control cell polarity and chemotaxis. Phosphorylates talB, gefN, gefS, PI4P 5-kinase and gacQ.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51062
Sequence Length: 444
EC: 2.7.11.1
|
Q07292 | MSRINFKKSSASTTPTSPHCPSPRLISLPRCASSSIDRKDQASPMASPSTPLYPKHSDSLHSLSGHHSAGGAGTSDKEPPKFKYKMIMVHLPFDQHSRVEVRPGETARDAISKLLKKRNITPQLCHVNASSDPKQESIELSLTMEEIASRLPGNELWVHSEYLNTVSSIKHAIVRRTFIPPKSCDVCNNPIWMMGFRCEFCQFKFHQRCSSFAPLYCDLLQSVPKNEDLVKELFGIASQVEGPDRSVAEIVLANLAPTSGQSPAATPDSSHPDLTSIKRTGGVKRHPMAVSPQNETSQLSPSGPYPRDRSSSAPNINAIN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Protein kinase that participates in the induction of vulva and has roles in fertility and viability. Acts downstream of the Ras protein let-60 . Required for progression of developing oocytes through the pachytene stage . Plays a role in responses to M.nematophilum-m... |
P11346 | MSSESSTEGDSDLYDPLAEELHNVQLVKHVTRENIDALNAKFANLQEPPAMYLIEYQELTSKLHELEAKEQELMERLNSQDQQEDSSLVERFKEQPHYQNQTQILQQQRQLARVHHGNDLTDSLGSQPGSQCGTLTRQPKILLRAHLPNQQRTSVEVISGVRLCDALMKALKLRQLTPDMCEVSTTHSGRHIIPWHTDIGTLHVEEIFVRLLDKFPIRTHIKHQIIRKTFFSLVFCEGCRRLLFTGFYCSQCNFRFHQRCANRVPMLCQPFPMDSYYQLLLAENPDNGVGFPGRGTAVRFNMSSRSRSRRCSSSGSSSSS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Serine/threonine kinase required in the early embryo for the formation of terminal structure . Also required during the proliferation of imaginal cells . May act downstream of Ras85D in the tor signal transduction pathway . During larval development, mediates Ptth/to... |
P27812 | MDSTTLVYADLNLARIQEPKHDSPPSLSPDTCRCPRWHRLALKFGCAGLILLVLVVIGLCVLVLSVQKSSVQKICADVQENRTHTTDCSVNLECPQDWLSHRDKCFRVFQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLKITGDTENGSCASISGDKVTSESCSTDNRWICQKELNHETPSNDS | Function: Receptor for CLEC2D/OCIL. Ligand-binding contributes to inhibition of cytotoxic natural killer (NK) cells. May mediate MHC class I-independent 'missing-self' recognition of allografts, tumor cells and virus-infected cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 25158
Seque... |
Q8UFA0 | MAEKTGLFISFEGGEGAGKSTQIRTLAEALRGRGFEVVVTREPGGSPGAEAVRHVILSGAAESFGVRMEAILFAAARNDHVEEVIRPALARGEIVLCDRFLDSSRVYQGTTGNLEPDFIETLQRIAIDGVVPELTLIFDIAAEKGLARARKRADEGATPDRFEKEEIETHEKRREAYLDIALAEPRRCRIVNADQPEDKVTEDVMSFVEPLLERAGNAADAAHE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24501
Sequence Length: 224
EC: 2.7.4.9
|
B2UN87 | MSFTGERKGRLIVFEGIDGTGKSTHIGHLRKYLEEKELEVVQSFEPTRGRWGRMLRDSAVTGRLSVEEEVALFLKDRREHVKMLIAPALARGAWVLLDRYYLSMMAYQGARGIDPEVIRAANEEFAPVPDAVVWLDIPVSVALERIGNRGERDAFETEAGLAACRSVFASVHAPWMLRIDADAGKEEVAARVRKALSMRFPDVIGA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23010
Sequence Length: 206
EC: 2.7.4.9
|
Q22018 | MATDQKRGLLIVFEGLDRSGKSTQAKRLVESINKKSTESGDASSSPSAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSADRFSKNQMIRDNIAKGIDVICDRYCYSGVAYSLAKGLPEQWVRSSDVGLPKPDAVLFFDVSPEVAAQRGGFGEERLETATIQQKVAAVMPTLRDDAYWKTVNADGDLDSVEKNVFRIYENLDREKPFESLEKI | Function: Catalyzes the conversion of dTMP to dTDP.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24342
Sequence Length: 218
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.9
|
Q8RDE6 | MRGKFISFEGIDGCGKTTQVKLLEEHLKKEGYDLLVLREPGGTRVGEKVREILLDRENLIFPVTEMLLYASSRAQLVEEKILPALSKGQMVIVDRFIDSSYVYQGYARGLGLEKVKIVNEIATKGLFPDITVYIDITPEEAIKRRQGKKADRLEGEDYEFHKKVREGYLRLVKDFPERFILIDGMQEVLAVHKMVVKAVEEYLKGAKV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23779
Sequence Length: 208
EC: 2.7.4.9
|
A4XHH4 | MKGKFIVFEGNDGSGKSTQILKVEKYLKEKGYKVVTTREPGGTEVGFRIRKLLLDPAYKMDGLTEALLLAADRNEHVKNVLIPALEDGYVVVCDRYILSSIVYQGIVRGVGVENIIKLNSIFEEKIKPDLYIILTLSPEIALQRLKMAGKNDKLDTENFDFHRKVYNGFKEVSKMFKKCVNIEAEGTVEDVFEKVRKVIDDLLKKR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23433
Sequence Length: 206
EC: 2.7.4.9
|
A7ZDK0 | MYVLFEGIDGVGKSTQIEILASKFSDAIVTKEPGGTQLGVNLREILLRSSIKIGKRAEILLFLADRAEHFEKLVAPNLGKLILSDRGFISGIAYALANDENLDENVLLELNKFALNDKFADKIIFFEASRELISSRLKARGTSDKIEARGLEYLLKVQSLMKQILIKNGFETLFIDASKSIELISKEIENFINFK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 21827
Sequence Length: 195
EC: 2.7.4.9
|
A7I1U4 | MLIFFEGIDGVGKSTQIELLKSVYNKNYLITKEPGGTLLGEKLREILLESDFKISKTAELFLFLADRAEHFEKVLKFSDKKDIICDRSFVSGIAYALANEQNLDINDLINLNKIALGGKIPNAKFIFLKISKDNLRFRLENRGNFDKIEERGLEYLMKVQKNMSEIFKILKIDALEIDANGDINEIHKKIKEFVK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22406
Sequence Length: 195
EC: 2.7.4.9
|
Q9PPF3 | MYVVFEGIDCVGKSTQISLLKEIYKDAIFTLEPGGTELGKHLREILLNKTHPINKRAELLLFLADRAQHFEEILKTNQNKLIISDRSFISGMAYAKDFENDLLFALNSFALENFFPQKIIFLKGDANLIQERLSQKELDSIEKRGIEYFLSVQDKLEKVLHFLKEKISVEILTLDAKESKEKLHQQIKEFLQ | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22275
Sequence Length: 192
EC: 2.7.4.9
|
B9KG87 | MYIAFEGVDCVGKSTQIELLKKCFKDAIFTKEPGGSELGVHLRKILLESKMQFSKKAELLLFLADRANLIDIHLVQNKNKLIISDRSFVSNMAYAKFDFDQNILFDLNSFATGGFFPQKIVFLHGSKELIEQRLSKKNLDSIEKRGVEYFLNIQNALEETLEILKTKIDIKILKLDASLSIENLHEKIKEFIND | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22260
Sequence Length: 194
EC: 2.7.4.9
|
Q3AG12 | MRGKFITIEGVEGSGKTTQIQYIARYLTEKNIPHIITREPGGTALGKKIRELLLNPSYPVVPEAEILLYLADRAQHVGEKIIPHLDKGVWVISDRYFDSTLAYQGYGRGFDLTLLKSFIAFATKGLIPDLTVLIDLPPEVGLSRVKGRGEYDRLERETLEFHQRVREGFLQLARDQRFRVVDGRKKPEEIFWEIKGFLEGLNG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23156
Sequence Length: 203
EC: 2.7.4.9
|
Q9RQJ9 | MTQGFFISFEGGEGAGKSTQIRRLADRLKAAGHDVIVTREPGGSPGAEAIRELLVNGAADRWSPVTESLLMYAARRDHIERVIRPGLARGAVVLCDRFADSTRAYQGAGGDAPASLIAALEEHVLGGTVPVLTLILDLPAEVGLQRAEARGGAARFESKGLAFHERLRAGYLEIARREPDRCVVIDADAELDAVTAAISDVVVQRLGL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22107
Sequence Length: 208
EC: 2.7.4.9
|
Q28SW8 | MPPLFISLEGIDGSGKSTQTARLVDWLRVRGRDPLQTREPGGSEGAEEIRRLLVEGDPDRWSAETEILLFTAARRDHLERTIRPALASGRDVVTDRFADSTRVYQGATRGALRGLVDRIHAEAIEAEPDLTLILDMDPELALSRGLARDSGEDRFEDFGLPFQQKLRAGFQALAREYPDRCHIVDASADPDAIAHTIQTIVGQRLAEA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23025
Sequence Length: 208
EC: 2.7.4.9
|
C5CHP2 | MFISFEGIDGSGKSTQVALFREYLERNSMEYVFIREPGGTQAGEDIREILLHNEYKLFPETELLLFMASRAQIVREVIIPALKKKKLVLADRFLDSSVAYQGYGRGLSIQMVTTLNEFSTGGVTPHLTLFIDVPVDVAVKRMRREMKHDKIEMESLDFFKRVRQGYLELAKRDPKRILVIDGTMSVEKIHEQVVKEFLLCLKKLGHGL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23883
Sequence Length: 208
EC: 2.7.4.9
|
Q5FM02 | MKGYFVSFEGPDGAGKSTVLKEVLAEIAPQLKTQYLVTREPGGSKIAEKIRDIILDPANDKMDPKTEALLYAAARSQHVEEIIKPAINEGKVVFSDRFVDSSLAYQGQGRDLGIAKVKQINDFATDKLDPDLTFFLDIAPEIGLSRIKKLRPAQEDRLEQEDIAFHQKVYEGFLKVIKMYPDRFVVINATQPIDQVVKQVVTELKQRLPKTILENN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24300
Sequence Length: 216
EC: 2.7.4.9
|
Q88YP6 | MLTGKLVTFEGPDGAGKTSALNAIVAKLQPQLGDRLVVTREPGGNQISEAIRKIILDRHNTAMDDRTEALLYAAARRQHIVQTIQPALQNDQLVLCDRYIDSSVAYQGAGRGIGEQAVYDMNQFATAGLTADLTLYFDVDAAVGLNRIQQHRQNEINRLDVEALSFHHRVQAAYLRLLADHPDRIKRVDASQPLDQVVTQALEIMASQLPTYVASKGGEDQ | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24314
Sequence Length: 221
EC: 2.7.4.9
|
Q1MQB3 | MFITIEGIEGSGKTTLINRLSEYFSSRGEDVIVTREPGGCELGGLLRSLVLSSELGLTAESELFLFLADRAQHVSECIQPAIMNGKTVFCDRYADSTIVYQGYGRGMNIGKLWEFNEVAIKGIWPQKTLLLDIDVEKALERACIRNEALGLNIVEGRFESEPMDFHNRIRDGFLHWAGRNPDRITILNADTTPEDLFQQSVSVLREIV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23328
Sequence Length: 208
EC: 2.7.4.9
|
Q5ZVP1 | MSSLTGKLIVIEGLEGAGKSTAVNLVVELLSQKKISTITTREPGGTKIGEILRSIIKNPEYNNVLDDRSELLLLYAARIQLIEQVIKPALNVGQWVIADRFELSTLAYQGGGRKMDMRVINELSNFCLKGFKPDLTLYLDINPELGMIRAKSRGKFDRIEQESIEFFHRIHDTYHILVKQNPEIIMIDANRSLEEVQSSIQSVIEEFIEHNL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24010
Sequence Length: 212
EC: 2.7.4.9
|
C4XNX1 | MFVTFEGVEGSGKSTQMTRLCAALEAAGRTVCRTRQPGGCFLGQTLRAILLSQKTAGLDDRAELFLYLADRAQHVAEVIRPALAAGQVVVCDRYTDSTVAYQGYGRGLDTTLLQNLNAVAAAGVVPDLTVLLDLDPAIGLTRATSRNAAAGTAEAEGRFEAERLEFHQRVRAGYRALAAAEPARFAVIDAAPSPDAVAEAVWGVVGKLL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22062
Sequence Length: 209
EC: 2.7.4.9
|
A7WYM2 | MSAFITFEGPEGSGKTTVINEVYHRLVKDYDVIMTREPGGVPTGEEIRKIVLEGNDMDIRTEAMLFAASRREHLVLKVIPALKEGKVVLCDRYIDSSLAYQGYARGIGVEEVRALNEFAINGLYPDLTIYLNVSAEVGRERIIKNSRDQNRLDQEDLKFHEKVIEGYQEIIHNESQRFKSVNADQPLENVVEDTYQTIIKYLEKI | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23425
Sequence Length: 205
EC: 2.7.4.9
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Q9SEX2 | MVGSSNSLAGLQDHLKLAREYALEGSYDTSVIFFDGAIAQINKHLNTLDDPLARTKWMNVKKAIMEETEVVKQLDAERRAFKEAPTGRRAASPPINTKSSFVFQPLDEYPTSSGGGPMDDPDVWRPPTRDVTSRRPARAGQTGTRKSPQDGAWARGPTTRTGPASRGGRGGATSKSTAGARSSTAGKKGAASKSNKAESMNGDAEDGKSKRGLYEGPDEDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMV... | Function: Severs microtubules in vitro in an ATP-dependent manner. Required for oligomerization of functional KTN80-KTN1 complexes that catalyze microtubule severing . This activity may promote rapid reorganization of cellular microtubule arrays. May be required for reorientation of cortical microtubule arrays during c... |
P34808 | MNGDVQSVIRGYLERAQVAKTMSDAGRWNEAGDLLRQLMTDVKSCKISASNRDEHDARNTFLRALEANLKLVQQNVRDEDDLHEAMTRQSGSPEPPADPDVWSKPSPPLPSSSKFGATKKGVGAAGPRPREISKSTSSMSTNPADVKPANPTQGILPQNSAGDSFDASAYDAYIVQAVRGTMATNTENTMSLDDIIGMHDVKQVLHEAVTLPLLVPEFFQGLRSPWKAMVLAGPPGTGKTLIARAIASESSSTFFTVSSTDLSSKWRGDSEKIVRLLFELARFYAPSIIFIDEIDTLGGQRGNSGEHEASRRVKSEFLVQ... | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner . Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of m... |
Q5RII9 | MSLGEINENVKLAREYALLGNYSSAVVCYQGVLEQIKKYLYSVRDSSLQQKWQQVWQEINEETKQVREIMTTLESFQMESTPSKPSSFAQDNDIMPVHVEHRSSPCVVRKSSVPYKDSKGHGNRLSVGPRGQARPSPRVANGDKGKPQKSKEKKENPSKPKEDKNKAEAVETEVKRFDRGGEDKDLIDALERDIISQNPNVTWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECRTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEA... | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phos... |
Q9WV86 | MSLQMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPSPQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTS... | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depol... |
B5X3X5 | MSLHEINENVKLAREYALLGNYSSAIVCYRGVLEQIKKYLFTVRDSSFQQKWQQVWQEINEENNQVQEIMRTLESFQLETTPSKPPSNQDGINDIWPVQVERRSSPLPVRRPPVPYKDSKPHNNRLSVAGVRAQHRQSPRGANGDRAKPLKGKEKKEAKPKDDKNKAEVSEKEVKRFDGQGYDKDLIEALERDIISQNPNVKWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECRTTFFNVSSSTLTSKYRGESEKLVRILFEMARFYAPTTIFIDEIDSMCSRRGTSEEHEA... | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phos... |
Q9PUL2 | MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTFLQQKWQQVWQEINMECKHVKDIMSTLEGFKLDSSPVKTTQHEFPSHDGEVWSLPVPVERRPSPGPRKRQSVQCNDNKSHNNRFSAAAKGPNLPSARNANNVKMKPVRAREKKDALIKNKSSADVSETEVKRFDGSGYDKDLIEALERDIISQNPNIRWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNISSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEH... | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. In mitotic spindles this could allow depolymerization of the micro... |
Q88NK7 | MVQASSHAESGHEGKQGASRSVGLLVAAVGVVYGDIGTSPLYTLKEVFTGGYGVSVNHDGVLGILSLILWSLLWVVSFKYVMFILRADNQGEGGTMALTALARRATAAYPRLRTLMVICGLIGASLFYGDSMITPAVSVLSAVEGVGLAFDGIDHWVVPISLVVLVALFLVQRHGTEKIGKLFGPIMVTWFLALGALGVHGISQSPEVLKAFNPAWAVNFFVVHPGIGVAILGAVVLALTGAEALYADMGHFGRKPIARAWFILVLPALVLNYFGQGALLLQNPEAARNPFYLLAPGWALLPLVGLATMATVIASQAVIS... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68569
Sequence Length: 636
Subcellular Location: Cell inner membrane
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Q9YDF8 | MSVERWVFPGCSVMARFRRGLSDLGGRVRNIGDVMEHPLVELGVSYAALLSVIVVVVEYTMQLSGEYLVRLYLVDLILVIILWADYAYRAYKSGDPAGYVKKTLYEIPALVPAGLLALIEGHLAGLGLFRLVRLLRFLRILLIISRGSKFLSAIADAADKIRFYHLFGAVMLTVLYGAFAIYIVEYPDPNSSIKSVFDALWWAVVTATTVGYGDVVPATPIGKVIGIAVMLTGISALTLLIGTVSNMFQKILVGEPEPSCSPAKLAEMVSSMSEEEFEEFVRTLKNLRRLENSMK | Function: Mediates a strong voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemic... |
A1CHT0 | MSTTTTSSKPEFPADAATKEYAASLDASDPLAGFREKFIIPSKANIASKKLAKPGLSSEPCIYFCGNSLGIQPKATAKYLEAQLDTWSSIGVSGHFTNVEDSPLREWQNLAEQAAESMSRVVGAAPEEVAAMGTLTMNLHLLLASFYRPTATKHKILMDWKAFPSDHYAIESHIAWHDLDPKESMVLIGPDEGTFEIPTEKILSYIDQHADDAALILLPGIQYYTGQLFDIQKITEYAQSRGLVVGWDLAHAYGNVHLKLHDWNVDFAAWCTYKYGNAGPGAMAGLFVHERHGRVDYREGEDSPKFRHRLTGWYGGDKSV... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 51324
Sequence Length: 464
Pathway: Amino-acid degra... |
A2QJI5 | MSKSNGVSLAFPAEAATKEYAASLDSSDRLAAFREKFIVPSKANIASKKLAKPGLSPESCIYFCGNSLGIQPKATAKYLEAQLDTWSSIGVGGHFTDLEGSPLKQWQLLSEQAADSMSKIVGAKPEEVAAMGTLTTNLHLLLASFYKPTQTKHKILMDWKAFPSDHYAIESHIAWHDLDPKESMVLIGPDEGEYEISTQKIFSYIDKHADEAAMILLPGIQYYTGQLFDIQKITKYAHSRNMVVGWDLAHAFANVELKLHDWNVDFAAWCTYKYGNAGPGAMGGLFVHEQHGEVDYSAGEDAPKFRHRLTGWYGGDRSVR... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 51300
Sequence Length: 463
Pathway: Amino-acid degra... |
Q2H7G2 | MDTEYQSFVETLRAGQKPEFPAHAKTIEYARELDAHDKLSQLRSDFNIPTKGSLRKKALDGGVAGETKEPRVPNGVSSATKPNGTVNSDLKDDEASIYFVGNSLGAQPKCIRQYIDAHLETWASIGVNGHFTSFDNSPLASWQDMAAACAAQSVDLVGAKSANEIIYMNTLTVNLHLMMASFYRPTAKRHKIIAEWKPFPSDSYALASQLHWHGLAPATSLIEIHPPNPTGSSPPTLTLTTSHILATIDAHADSTALLLLPGIQYYTGQLFDMARITRHARARGIVVGWDLAHAVGNVELELHAWGVDFAVWCTYKYLNA... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 57881
Sequence Length: 539
Pathway: Amino-acid degra... |
Q5BC73 | MSNHVNGVNGVNGVNGVKPVFPENAASKEYAKALDAADPLASFRDKFIIPSKANIQSKRLAKPNISADPCIYFCGNSLGLQPKATAKYMEAHLDTWASIGVNGHFTKIEDSPLDPWWVMAEQAAGSMSKLVGAAPEEVIAMGTLTSNLHLLLASFYKPTATKHKILLDWKAFPSDHYAIESHIAWHDGLDPKKSMVLIGPDEGEYEIPTQKILSIIDEHADEAALILLPGIQYYTGQYFDINTITEYAHSKGLMVGWDLAHAFANVELKLHEWDVDFAVWCTYKYANAGPGSMGGLFVHEKHGKVDYSQGEDSPQFRHRL... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 52467
Sequence Length: 474
Pathway: Amino-acid degra... |
A1CWY1 | MSTNGTLSKPEFPANAASKEYAASLDAADPLAGFREKFIIPSKANIASTKLAKPGLSSEPCIYFCGNSLGIQPKATQKYLEAQLDTWSSIGVCGHFTKIEDSPLKEWQNLAEQAAESMSKIVGAAPDEVAAMGTLTMNLHLLLASFYKPTATKRKILMDWKAFPSDHYAIESHVAWHHLDPQETMVLIGPDEGTYEIPTEKILSYIDTHADEAALILLPGIQYYTGQLFDIPKITEYAHSRGLIVGWDLAHAYANVQLKLHDWDVDFAAWCTYKYGNAGPGAMAGLFVHEKHGQVDYSEGEDAPKFRHRLTGWYGGDKSV... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 51232
Sequence Length: 464
Pathway: Amino-acid degra... |
Q7RXY2 | MSTAAVQDARKQAEALDNEDSIAFVRDEFNIPTKAQIASSRLADSHPAALPASEDDAKCIYLCGNSLGVQPKRTVTRLNQYLTTWATQGVQGHFKPLEESPLPTWLDADAKAAELIAPVVGANVSEVAVMQTLTANIHLLMSAFYRPDINGRHKIILENKAFPSDHFAVETQIRHHSLSTEKSMVLIESSSKDNIISTEEVLSVISAHADTTALLLLPGIQYYTGQLLDIPAITAFAHKHGIFVIWDLAHAVGNVPLYLHDWGVDAAAWCSYKYLNGGPGCIGGLFVHTNNSVVTKEITDEKPEEGYNNRLAGWWGNDKK... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 51627
Sequence Length: 472
Pathway: Amino-acid degra... |
Q9FY79 | MEFKLNIPNTIIKTLQTIVFFLFVLLAFQIAEAEIHHHTFKIKSKAYTRLCNTNKILTVNGEFPGPTLKAYRGDKLIVNVINNANYNITLHWHGARQIRNPWSDGPEYVTQCPIRPGESYVYRIDLKVEEGTIWWHAHSQWARATVHGAFIVYPKRGSSYPFPKPHREIPLILGEWWKKENIMHIPGKANKTGGEPAISDSYTINGQPGYLYPCSKPETFKITVVRGRRYLLRIINAVMDEELFFAIANHTLTVVAKDGFYLKHFKSDYLMITPGQSMDVLLHANQRPNHYFVAARAYSSAFGAGFDKTTTTAILQYKGD... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 64878
Sequence Length: 569
Subcellular Location: Secreted
EC: 1.10.3.2
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Q84J37 | MSHSFFNLFLISLFLYNNCIAHHYTFTVREVPYTKLCSTKAILTVNSQFPGPIIKVHKGDTIYVNVQNRASENITMHWHGVEQPRNPWSDGPEYITQCPIRPGSDFLYKVIFSIEDTTVWWHAHSSWTRATVHGLIFVYPRPPQILPFPKADHEVPIILGEWWKRDVREVVEEFVRTGGAPNVSDALTINGHPGFLYPCSKSDTFHLTVEKGKTYRIRMVNAAMNLPLFFAIANHSLTVVSADGHYIKPIKATYITISPGETLDMLLHADQDPERTYYMAARAYQSGNIDFNNSTTIGILSYTSSCKAKTSSFSGYYPTL... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products (By similarity). Involved in lignin synthesis in seed coats, in seed coat permeability, in seed germination, and in root elongation. Required for the seed coat (testa) brown pigmentation by mediating the... |
Q339K6 | MKRCQSSRPTAAVAAVVAAVSMIIVLVSGTAIPSAAAAAAVEHTFVVSQVNMTHLCKEMAFTVVNGQLPGPTIEVTEGDSVTVHVVNKSPYNLTIHWHGVYQLLNCWNDGVPMITQRPIQPNHNFTYRFNVAGQEGTLWWHAHDAFLRGTVHGALIIRPRHGAASYPFPRPHREVPIIIGEWWEKDLPQVDRNMTNGYFDDYSSGSTINGKLGDLFNCSGVLEDGYVLDVEPGKTYLLRIINAALFSEYFLKIAGHRFTVVASDANYLTPYSTDVVVIAPGETLDAIVVADAPPSGRYYIAAQPIQAPPPDTQTPEYATR... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 65670
Sequence Length: 599
Subcellular Location: Secreted
EC: 1.10.3.2
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Q1PDH6 | MEIPRRFCICVLTFFVFVLLSPTTVHSIIRHYKFNVMTNTTKLCSSKPIVTVNGQFPGPTIVAREGDTILIKVVNHVKYNVSIHWHGIRQLRTGWADGPAYITQCPIQPGQNYLHNFTLTGQRGTLWWHAHILWLRATVHGAIVILPKLGVPYPFPKPYKEKTIVLSEWWKSDVEELINEASRIGTAPSASDAHTINGHSGSISNCPSQSSYGLPVRAGKTYMLRIINAALNEELFFKIAGHVLTVVEVDAVYTKPYKTDTVFIAPGQTTNVLLTANANAGSNYMVAATTFTDAHIPYDNVTATATLHYIGHTSTVSTSK... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 62373
Sequence Length: 566
Subcellular Location: Secreted
EC: 1.10.3.2
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Q7XE50 | MDRKGIVLGSKLAVFSMILLWHRHGVDQPRNPWSDGPEFITQCPIRPCGNFTYQVILFEEEGTLWWHAHSDFDRATVHGAIVIHPKHGTTFPFNKPDKEIPIILSEWWNDDVENVLDEAKRTGGDQGNTYLLRVINTGLTNDMFFAVAGHCLTVVSIDARYTKPLTVDYIMIAPGQTMDVLLEANRTLGSNSRYYMAARAFITLPVDTIPFNNSTATAIVEYTDSPTARPPGPPEFPLLLPAIKDEDAAMAFVDERMLIDIDVNFLPCDTTNATNKLCKGPQGNQFAASLNNVSFESPAIDVLDAYYYGSGRGVYEEDFP... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 52187
Sequence Length: 467
Subcellular Location: Secreted
EC: 1.10.3.2
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Q2RBK2 | MPSRGCSCWLLSLALLCSLAAAKEQYHEFVIRETTVKRLCKSHNIMTVNGQFPGPTLEINEGDSLIINLINRGRYNMTLHWHGVRQMRTGWSDGPEYVTQCPVRPGQSYRYRFTVAAQEGTLWWHAHSSWLRATVYGALLIRPRDGTSYPFDVQPTRELAPILLGEWWDMNPVDVVRAATRTGAAPNISDALTVNAQPGDLYSCSSHDTAVFPVTSGETNLLRFINAALNTELFVSLAGHNMTVVAADASYTKPYTTSLLLLAPGQTTDVLVTFDQPPGRYYLAARAYASAQGVPFDNTTTTAIFDYGAANNASSAAIAM... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 61544
Sequence Length: 567
Subcellular Location: Secreted
EC: 1.10.3.2
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Q9LMS3 | MENLGFLIISTFLLLFTTLLPYSSASTTRRFHFNVEWKKVTRLCHTKQLLTVNGQYPGPTVAVHEGDIVEIKVTNRIAHNTTIHWHGLRQYRTGWADGPAYITQCPIRSKQSYTYRFKVEDQRGTLLWHAHHSWQRASVYGAFIIYPRQPYPFSGSHIQSEIPIILGEWWNDDVDNVEKAMMKTGAGAKVSDAYTLNGLPGPLYPCSTKDTFTATVDAGKTYILRIINAALNNELFVAVANHTLTVVEVDAVYTKPVHTKAIMIAPGQTTTLLLRADQLSGGEFLIAATPYVTSVFPFNNSTTVGFIRYTGKTKPENSVN... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 65229
Sequence Length: 581
Subcellular Location: Secreted
EC: 1.10.3.2
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D4APX3 | MKRLGLAALYIGSALAWPEPHGPPSRNVPRDDFPMFNPLPSTDLNTRLIRCEYPSMKGWTYSNKKNGDWLKYVGSKPGEITEYNIDTDNDKYVPQGITRKYHLEVTDESVNMDGTMFDQAKVFNKQYPGPWIQITVTNKLKHNGTAIHWHGIRMMENMFNDGVPGVTQCPIPPGSSMTYRFKASQYGSSWYHSHYSLQYADGLFGPMTIHGPTSAGYDKAVDPLLMTDHLHSSAFEEYHKELEGKPPAMDSIILNGKGDYDQTGDLKKKYRTVLKPGKKYLLRLINTSVATTFVFSIDGHKFQVVGSDFVPIEPYVTDHI... | Cofactor: Binds 4 Cu cations per monomer.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 71552
Sequence Length: 633
Subcellular Location: Secreted
EC: 1.10.3.2
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Q12570 | MKNSFFSSLAKFASLSLAFALPTAEVIPSALEERQSCANTATTRSCWGQYSASTNSYTTVPKTGYWLVVQNTTLSADGVSRPTLNFNGTIPGPQITADWGDDVIVHVTNKLTSNGTSIHWHGIRQLNNAQYDGVPGITQCPIAPGGTLTYKFHADNYGSSWYHSHFILQYGDGLFGPLVINGPATANYDVDLGMLFLNDWNHVPVQSLWDKAKTGAPPTLLTGLMNGTNTYNGAGKKFQTTFTPGLKYRIRVVNTAVDGHFQFSIDGHSFQVIAMDFVPIVPYNATSILVSIAQRYDIIVTANAAVGNYWIRAGWQTACS... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 60337
Sequence Length: 561
Subcellular Location: Secreted
EC: 1.10.3.2
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Q55P57 | MRGLAKLFFLSCSFVSLVSSEKTDESPTAVSDNYMPKATATIDPSVFALSNDFEITDVPTTREYTFDIAKAFASPDGYEREVYVVNNMFPGPVIEANTGDTIIVHVNNHLDEGQSLHWHGLRQLGTAFMDGVPGITQCPIPPGGSFTYNFTVSHQSGTYWWHSHYSNSMADGIWGPLIVHSPNEPLQRGRDYDEDRIVFITDWMHDNSEIIIAALATPEGYKGNIAPPQGDAILINGRGQTNCTATGSSSCFYPPPPEIQVPVNCRVRLRFISATAHPMYRISIDNHPMEVVEADGTAVYGPTVHEISVAPGERYSAIIN... | Cofactor: Binds 4 Cu cations per monomer.
Function: Laccase that catalyzes the oxidation of certain aromatic compounds, including L-dopa, to quinones, which then polymerize to melanin . Able to oxidize a wide variety of aromatic diphenol and diamino groups in the ortho, meta, and para positions but not monophenolic gro... |
Q03966 | MPSFFRALFSGLIASQLSWAAPSLLHPLEPRQQPNCNTASNRACWISGSYDITTDYEVKTPLTGVVRQYDLTLTQAENWLGPDGVVKEDVMLVNGNILGPVIHAQWGDTISVTVTNNLKYNGTTIHWHGIRQLNTNLQDGVNGITECPIPPNGGSKTYTFIAHQYGTSWYHSHFSAQYGNGIVGAIQIDGPASLPYDIDLGPLVLSDYYYKTADELVVYTQSNAPPASDNVLFNGTNINPANTTQGQYKTITLTPGKRHRLRIINTSVENNFQVSIVGHSMTVIESDFVPVDSFTTDSLFVGIGQRYDVTIDASQATDNY... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 64696
Sequence Length: 591
Subcellular Location: Secreted
EC: 1.10.3.2
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P26421 | MMLTVTMNPSIDIAYQLDDLKVDTVNRVIETHKTPGGKGLNVTRVLSQLGDDVLASGLLGGKLGEFLEAELDKSAIKHSFYKISAETRNCIAILHGGYQTEILEQGPYVSAKESKGFLEFFEKLLPKLEVVAISGSLPKGVPVDYYSQMIAICKQHQVPIVLDCSGQALLEVLNGAAKPTVIKPNTEELSQIMEREITNDVAVLKHALASPIFSGIDWIIVSLGSQGAFAKHGQTFYKVTIPKIAVVNPVGSGDSTVAGITSALAAGASDEKLLKKANTLGMLNAQEKLTGHVNLENYDNLYQQIEVAEV | Catalytic Activity: ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33363
Sequence Length: 310
Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
EC: 2.7... |
Q48624 | MKDITKQKFSRNKLVEMISFALGNLGHAAFYGALSTYFIVYVTSGMFDGLPQSVANKLIGLITALVVIIRLAEVIIDPILGNIVDNTKTRWGKFKPWQVIGAVVSSVLLVVIFTGIFGLAHINWIAFAIVFTVLFILLDIFYSFADVAYWGMVPAISEDSKERGIFTSLGSFTGSIGWNGLTMIVVPVTTYFTFIATGKHEQGPSGWFGFSIVVSIVAVLSALAVAFGTKEKDNLIRNAATKKTSIKDVFSGIIHNDQILWISLAYLMYSLAYVVTNGVLFYFFKFVLGKPNEFWIAGAIATVIGFSTAPLYPVLNKFIT... | Function: Responsible for transport of beta-galactosides into the cell, with the concomitant uptake of protons (symport system), and also for transport of homologous and heterologous exchange of beta-galactosides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70153
Sequence Length: 639
Domain: The ... |
B3EWI3 | DVIGPQAQVTLANQD | Cofactor: Binds 4 Cu cations per monomer (By similarity). Copper is inhibitory at concentrations of 1.25-5.0 mM .
Function: Lignin degradation and detoxification of lignin-derived products (By similarity). Active against a variety of substrates including the benzenediols hydroquinone and catechol, the benzenetriol pyro... |
A4IU28 | MTKKIHINAFEMNCVGHIAHGLWRHPENQRHRYTDLNYWTELAQLLEKGKFDALFLADVVGIYDVYRQSRDTAVREAVQIPVNDPLMLISAMAYVTKHLAFAVTFSTTYEHPYGHARRMSTLDHLTKGRIAWNVVTSHLPSADKNFGIKKILEHDERYDLADEYLEVCYKLWEGSWEDNAVIRDIENNIYTDPSKVHEINHSGKYFEVPGPHLCEPSPQRTPVIYQAGMSERGREFAAKHAECVFLGGKDVETLKFFVDDIRKRAKKYGRNPDHIKMFAGICVIVGKTHDEAMEKLNSFQKYWSLEGHLAHYGGGTGYDL... | Function: Involved in the degradation of long-chain alkanes . Converts alkanes ranging from C(15) to C(36) into their corresponding primary alcohols .
Catalytic Activity: a long-chain alkane + FMNH2 + O2 = a long chain fatty alcohol + FMN + H(+) + H2O
Sequence Mass (Da): 50466
Sequence Length: 440
Subcellular Location:... |
Q58806 | MFIDGKWINREDMDVINPYSLEVIKKIPALSREEAKEAIDTAEKYKEVMKNLPITKRYNILMNIAKQIKEKKEELAKILAIDAGKPIKQARVEVERSIGTFKLAAFYVKEHRDEVIPSDDRLIFTRREPVGIVGAITPFNFPLNLSAHKIAPAIATGNVIVHHPSSKAPLVCIELAKIIENALKKYNVPLGVYNLLTGAGEVVGDEIVVNEKVNMISFTGSSKVGELITKKAGFKKIALELGGVNPNIVLKDADLNKAVNALIKGSFIYAGQVCISVGMILVDESIADKFIEMFVNKAKVLNVGNPLDEKTDVGPLISVE... | Function: Involved in F420 biosynthesis through the oxidation of lactaldehyde to lactate. The substrate preference order is propionaldehyde > DL-lactaldehyde, DL-glyceraldehyde > crotonaldehyde > glycolaldehyde > acetaldehyde, acrolein > formaldehyde. No activity was observed towards methylglyoxal or glyceraldehyde-3-p... |
D5SJ87 | MPVDVGTLPPPAPREAVSAAAHLLASVDGDPWGRTSPTVYETARVHAWAPHLPGRDRRVTWLLDQQRAGGLWGDGPPAYQVLPTLAAVTALLAELDRHPEAGHSSLGGRLAAAVAAGLDTLHGLSHHDPLPDTAAVELLVPGLITEVNDRLDAIDPEAAHPALAPVPHGRRLTAVHGIPALPRHRLAERLARFARLPVKLHHCFEALAPVCPPGLVPARPDHLLGSSSAATAAWLATATAAPGAPGLDRLLRSTAARYGGLFPETARITVFERLWVLTTLHRAGLLATFEPLARRWVSALAAPGGVPGVPGFEPDADDTA... | Function: Involved in the biosynthesis of the labdane-type bicyclic diterpene labda-7,13(16),14-triene. Catalyzes the conversion of geranylgeranyl diphosphate (GGDP) into labda-7,13(E)-dienyl diphosphate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (13E)-labda-7,13-dien-15-yl diphosphate
Sequence Mass ... |
Q8X5W7 | MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEVNPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDI... | Function: Involved in the transport of maltose and maltodextrins.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49968
Sequence Length: 446
Subcellular Location: Cell outer membrane
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Q65DC4 | MSKKEMILSWKNPMYRTESSYHPAGNILKELQEEEQHSIAGGTITLSTCAILSKPLGNNGYLCTVTKECMPSCN | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA1 exhibits acti... |
P86476 | MKTMKNSAAREAFKGANHPAGMVSEEELKALVGGNDVNPETTPATTSSWTCITAGVTVSASLCPTTKCTSRC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA2 exhibits acti... |
Q2QBT0 | MNNEDFNLDLIKISKENNSGASPRITSKSLCTPGCKTGILMTCPLKTATCGCHFG | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM: Maturation of lantibiotics involves the e... |
P86013 | MKVDQMFDLDLRKSYEASELSPQASIIKTTIKVSKAVCKTLTCICTGSCSNCK | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacks antibacterial activity against Gram-nega... |
O88038 | MNLFDLQSMETPKEEAMGDVETGSRASLLLCGDSSLSITTCN | Function: Stably accumulated precursor of SapB .
PTM: Maturation involves the enzymatic conversion of Ser into dehydrated AA and the formation of thioether bonds with cysteine, probably by RamC . This is followed by membrane translocation and cleavage of the modified precursor (Probable). The RamS precursor protein (de... |
P0CH60 | MKVLAALALSALAMAKPTPPMPGMSLVQTGPQETRWVTAKEKHDMVMNHIGFFDITNRPESASIASKPKSYAFPGNVSHQAEVKPLLEKISADHIKSNLEMFSSYPNRYYDAQSGVESAQWVMEQAQAVVGNIQGAKVEMVKHDWMQPSIRAIIPGKSEKIVAVGAHQDSINGKNPQGEAPGADDNGSGSMTILEALTALVSDQKIAGGEAANTLEFHWYAGEEEGLLGSQDIFQQYSQEGKEVVAMLNQDMTGYGETMGVITDNSDPNLTKFTKMILDTYTSAKYSDSECGYACSDHASANKAGFPSAFVYEAVVGQDN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Probable extracellular aminopeptidase which contributes to pathogenicity.
Sequence Mass (Da): 38516
Sequence Length: 357
Subcellular Location: Secreted
EC: 3.4.11.-
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Q2U1F3 | MRFLPCIATLAATASALAIGDHVRSDDQYVLELAPGQTKVVTEAEKWALRAEGKRFFDITERASSLELASNKKQKLAVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAHQDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 41105
Sequence Length: 377
Subcellular Location: Secreted
EC: 3.4.11.-
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P0ACV4 | MKYLLIFLLVLAIFVISVTLGAQNDQQVTFNYLLAQGEYRISTLLAVLFAAGFAIGWLICGLFWLRVRVSLARAERKIKRLENQLSPATDVAVVPHSSAAKE | Function: Involved in the assembly of lipopolysaccharide (LPS).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11351
Sequence Length: 102
Subcellular Location: Cell inner membrane
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P44129 | MIKYILGIVIFIAIVLVAITIGANNDQIITFNYIVAESQFQLSSLVAILFGLGLILGWLITAFFYIKLKLKNMALARQVKRQTLQINELTTTRDKVV | Function: Involved in the assembly of lipopolysaccharide (LPS).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10915
Sequence Length: 97
Subcellular Location: Cell inner membrane
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P0AB60 | MLELLFLLLPVAAAYGWYMGRRSAQQNKQDEANRLSRDYVAGVNFLLSNQQDKAVDLFLDMLKEDTGTVEAHLTLGNLFRSRGEVDRAIRIHQTLMESASLTYEQRLLAIQQLGRDYMAAGLYDRAEDMFNQLTDETDFRIGALQQLLQIYQATSEWQKAIDVAERLVKLGKDKQRVEIAHFYCELALQHMASDDLDRAMTLLKKGAAADKNSARVSIMMGRVFMAKGEYAKAVESLQRVISQDRELVSETLEMLQTCYQQLGKTAEWAEFLQRAVEENTGADAELMLADIIEARDGSEAAQVYITRQLQRHPTMRVFHK... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Location Topology: Single-pass membr... |
P44130 | MIELLFLLLPIAAAYGWYMGRRSAKKDQDDISNKLSRDYVTGVNFLLSNQTDKAVDLFLDMLQKQEIENEIESHSQFEAELTLGNLFRSRGEVDRALRIHQALDLSPNYTFEQKLLAKQQLARDFMVVGFFDRAENLYILLVDEPEFAENALQQLLVIYQKTKEWKKAVNIAEKLAKIKPQENNIELAQCYCEYSQSLEPESAVEKRSVLQKALSVSPTCVRASLLLANLAMLDGQYQQAVKILENVLEQNPDYTGEILLPLKHCYEELNQLDNFELFLIRAGQIINNDEVELALAKLIEEKDGKSAAQAKLYQQLTKKP... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Location Topology: Single-pass membr... |
Q13571 | MDPRLSTVRQTCCCFNVRIATTALAIYHVIMSVLLFIEHSVEVAHGKASCKLSQMGYLRIADLISSFLLITMLFIISLSLLIGVVKNREKYLLPFLSLQIMDYLLCLLTLLGSYIELPAYLKLASRSRASSSKFPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEDMPHNQFIKMMIIFSIAFITVLIFKVYMFKCVWRCYRLIKCMNSVEEKRNSKMLQKVVLPSYEEALSLPSKTPEGGPAPPPYSEV | Function: May have a special functional role during embryogenesis and in adult hematopoietic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29937
Sequence Length: 262
Subcellular Location: Lysosome membrane
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Q61168 | MASRAAPVRQTCCCFNIRVATIALAIYHIVMSVLLFIEHVVEVARGKVSCRFFKMPYLRMADLLSSFLLIGVLFIISISLLFGVVKNREKYLIPFLSLQIMDFLLCLLTLLGSYIELPAYLKLARPRPGPSKVPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEGVPHSQFINMMLIFSVAFITVLILKVYMFKCVYTCYKFLKHMNSAMEDSSSKMFLKVALPSYEEALSLPPKTPEGDPAPPPYSEV | Function: May have a special functional role during embryogenesis and in adult hematopoietic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29602
Sequence Length: 261
Subcellular Location: Lysosome membrane
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Q01747 | MNSFLFSLACSLLVAIPAISAQDEDAGGAGDETSEGEDTTGSDETPSTGGGGDGGNEETITAGNEDCWSKRPGWKLPDNLLTKTEFTSVDECRKMCEESAVEPSCYILQINTETNECYRNNEGDVTWSSLQYDQPNVVQWHLHACSK | Function: Inhibits collagen-stimulated platelet aggregation (IC(50)=60 nM), dense granule release and serotonin release . Does not inhibit platelet aggregation induced by ADP, arachidonic acid, and thrombin .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 15908
Sequence Length: 147
Subcellular Location: Secreted
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F4JTN2 | MDILKSYHLLAAAYSAPAWASFMAGAFLVLTLSLSLFLVFDHLSTYKNPEEQKFLIGVILMVPCYSIESFASLVKPSISVDCGILRDCYESFAMYCFGRYLVACIGGEERTIEFMERQGRKSFKTPLLDHKDEKGIIKHPFPMNLFLKPWRLSPWFYQVVKFGIVQYMIIKSLTALTALILEAFGVYCEGEFKWGCGYPYLAVVLNFSQSWALYCLVQFYGATKDELAHIQPLAKFLTFKSIVFLTWWQGVAIALLSSLGLFKSSIAQSLQLKTSVQDFIICIEMGIASVVHLYVFPAKPYGLMGDRFTGSVSVLGDYAS... | Function: Required for programmed cell death (PCD) associated with hypersensitive response (HR). Involved both in the induction of EDS1/PAD4 mediated HR and in accelerated cell death in the acd11 mutant. Not required for HR induction elicited through pathways exclusively dependent on CC-NB-LRR resistance proteins.
Loca... |
P49291 | MIRRGLLSVTAALVLLSVSCSAQETMGCADRTAINDFNATLYMGKWYEYAKMGSMPYEEGGVCVTAEYSMSSNNITVVNSMKDNTTHEVNTTTGWAEFASELHTDGKLSVHFPNSPSVGNYWILSTDYDNYSIVWSCVKRPDSAASTEISWILLRSRNSSNMTLERVEDELKNLQLDLNKYTKTEQSAKYCAGAEHVVGAMLSVAIASLFALLH | Function: Putative role in axonal outgrowth and guidance, required for the navigation of identified commissural neurons. Could be a receptor the midline morphogen.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23641
Sequence Length: 214
Subcellular Location: Cell membrane
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Q5XV40 | MKFWGWMHHKFRENSKEPLKDASTGNSYSILSAHPSLDSQEVYPTACAGSRYNTGFRKQVNLFQESSFAGPKQYTEEDFKDERNSDFFDGFLAIGTLGGETLLDEQPATPTFGMSFEDPAIDDADVTENDLKLISNELDKFLEAEAKEGHHQPSGRNSDTNTIASTIEAIEGVDDEEDNQPMKFPLQEYFFGSLIELPESKIAGKKDRASLGELFQITEVQDKQSENIYGKKKKQPNSAHKSAKHLVKKVLKKIHPSSRGSVSGKPEVDSTKKKFQKMVQVFHRKVHPEESIMETKIYSSVANPKSSKANSIDLTFEKVN... | Function: Involved in the regulation of shoot gravitropism . Involved in the regulation of inflorescence branch angle . Functions redundantly with LAZY2, LAZY3 and LAZY4 to control plant architecture by coupling gravity sensing to the formation of auxin gradients . Involved redundantly with LAZY2 and LAZY4 in the regul... |
B4FG96 | MKLLGWMHRKLRQNSNDVFKEFNNAAGGTCNCITGLAASDPATFLATANEYFTADNDFTNNHPSSPAADLFTFGGSGLLTIGTLGIAAVAVSADADEVDYDVDADADSDFDDNDDTAGDDEDQVDSAVTPTFTYAAPPPIEDATVVEKAAVAVVEAIAEKDDDTTTEDDLMVVSAELEKVLGGRNSGTAGDLVASARVSFAMGVDCPLQGFLFGSPVSDAESRLEQPRDSNGGRRTSLGELFMRTRFAEEKVALVAVEEGEDGGDIGAGGERDDRKAGKGGGGHKTTKKRSAKDEKVPRGDGAQASATVTKSKFHKILQI... | Function: Involved in the regulation of shoot gravitropism, and tassel and ear development through the regulation of polar auxin transport (PAT) and auxin signaling. Acts as negative regulator of basipetal PAT, but positive regulator of lateral auxin transport . Involved in the regulation of shoot gravitropism and leaf... |
P10881 | MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDAALDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFAVFDSIESAKKFVETPGQKYKDTDLLILFKEDYFTKKNEERKQNKMEAKLRAKQEQEEKQKLAENAEMKSLEEKIGCLLKFSGDLDDQTCREDLHTLFSNHGEIKWIHFVRGAKEGIILFKEKAKEALDKAKEANNGNLQLRNKEVTWEVLEGDVEKEALKKIIE... | Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.
PTM: Phosphorylated in the C-terminal part of the protein.
Sequence Mass (Da): 46534
Sequence Length: 404
Subcellular Location: Nucleus
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P05455 | MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIE... | Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation . In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation .
P... |
P32067 | MAENGDNEKMTALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLETMIKFNRLNRLTTDFNVIVQALSKSKAKLMEVSADKTKIRRSPSRPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLDDKGQILNIQMRRTLHKTFKGSIFAVFDSIQSAKKFVEIPGQKYKDTNLLILFKEDYFAKKNEERKQSKVEAKLKAKQEHEGRHKPGSTETRALEGKMGCLLKFSGDLDDQTCREDLHFLFSNHGEIKWVDFARGAKEGIILFKEKAKEALEKARNANNGNLLLRNKKVTWKVLEGHAEKEALKKITDD... | Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.
PTM: Phosphorylated.
Sequence Mass (Da): 47756
Sequence Length: 415
Subcellular Location: Nucleus
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A0A125SXN2 | MWRLRTGSSTVDKADSWLSSLNNHLGRQIWCYDPEAGTPQEREAVEAECARFTANRHQQRQSADTLLRLQFQKEHSANRLPSRITVNEDHEVTEDDVTTTLCRALQFYSQLQTDDGHWSGDHSGPMFFLPGMVIALYVTGALDSVLSEHHQREICRYIYNHQRQDGSWGLHPEGTGTLFGTVLSYVTLRLMGESKSNSNNREALRKAQTWIIDHGGATDVPSWGKFWLAVLGVYEWSGVNPLPPESWLLPKSLIAHPGRLPVLYRFIFLPMSYIYARRLSHHLTKIIEDLRKELYTIPYEDIDWNHARKLGAKEEIVPRS... | Function: Oxidosqualene cyclase involved in the biosynthesis of alpha-onocerin, a triterpenoid characterized by a symmetrical structure due to cyclizations at both termini of dioxidosqualene that inhibits acetylcholinesterase. Catalyzes the second half of the cyclization, exclusively from pre-alpha-onocerin.
Catalytic ... |
A0A179HJB8 | MISHRNAIANIMQIVTYESTYQSDEPELCLGVLPQSHIYSLVVVSQASIWRGDGVVVLQGFELEQTLLAIQTNGIKRLWLVPPMLVAITKAPRIVESYDLSSVSVAAVGASGISKDVMATFGELLPACKIIQGYGMTETTGVVCFGNVEDSMDGSCGHLYPGYEARLIDGEGKDVESHNTPGELVLRSPSVVIGYYNDESATSEAMMDGGWLRTGDLVEIRQSEKGHEHVFVVDRVKELIKVRGLQVAPAELESHLILHPAVAEVAVIPVPDDRAGELPKAYIVRASGAELDEQVLRKELSQYVEGQFARHKHLDGGIEF... | Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contains nine amino ... |
A0A179H324 | MAPTDRNPVQVQYYAKGKKTTESSGPAPAPLILIHDGGGTTFAYFTIGRLERDVWAIHSPTFTSAQPWEGGMDGMAKHYIELIEKVAGIKGKILLGGWSLGGYVALTMAHMIASSPASFEISIDGILMMDSPWLVAGRDLPIGTPQPALIGIPDLVRKSLDNCERMLYHWELPQWGRSSGKAFKFSAGNEKFETQPGTVLYRSLKGDWRAVERTVSHELTEQQALQTPPSGPPPAVMLRSVIPAPTKGSSGKPCRVDQFRDELLLGWDGKYNTDMIHAVLEARSHHYDMFNQLYVDEVTETIKEAIQIIETVLPNE | Function: Probable thioesterase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contains nine ... |
A0A179H2P2 | MGDNVQSDTTAAQAGITDAPTAPTSAPVSLKERLEKLIESSQQLIKRMDENNIPDPTFAPECQEDYSKLPPETITERFALLDLLNDVTFLVHGASQSITDVAQNAMADSATLNILNYFNFWDVIPLDGDASFAEIAKAVRLPQEAVEAILPYAFSNRIFEPVTIGDPNSRIRHTSRSAAMIKDPTLRIIVNLTIDGLAGPLSILNRALEKNFLGKEKLTNEISETPFGMLYNKGGPLGEYKDYYDWLDRDGEGERKGWRQRDMVESLRLAKEKMGAESALLEALDWAGAGKATVVDLGGSGGHDDVPLAEKFPDLKIIVQ... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contains nine am... |
A0A179H0I7 | MPSIHASTSELFTHLTVSNICVAAGCAFALSLLYLYVRALYLVFFHPLSRIPGPKYAACSRLPYVRNQLRGDLVKWLHSLHQQYGDVVRIAPDEVSFISNVWQDVYAAHNGEKATKGTYLKDRRWFAAPYNNTWSILQADAEAHPRMRKMIAPAFSDKVLREQEAMIQEYVELFVLRLHEQTENDSKGDVDMVKWFNFFTFDIIADMTFGESFNCLRDSDYHPWVRMLFKSVRAISLNSAIRRYPFFQAIVKRLAPKNLLEQRRQFNQFVFDRVGERLASESSHPDLMSHIKKFKDEPKGMNRDEIDSNANILLVAGSET... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contai... |
A0A179H0I3 | MDRPQWPGGLIAQVHGFVFSWWGVILLLAIINLKSFPGIWTIRALYHMKSSFNGQLRQTVASPTAENAQRRVPKTPKTGATDTIDHHPLFQPEIISSHVSPAEIDFNMHKSNSTYFTDLDISRIKLVGRIMAPAWPLDRMHVEYKGRDGEMKRERVKGRPALALGATCTSFKREMKVLARYDVESRILGWDSRWLYIGSWFVSRKGGKGKEQLFASSLSKYIVKKGRITVRPEQFLTESGWIPPRPESTGNSKSLDSLQANGHGATENGKHDAKDTWTWEEIESHRLKGMTTVGGWADADLRLEQAYSS | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contains nine amino aci... |
A0A179HJU2 | MPTSLEQAAALIGGVGTHLLYFKHGERHAYPWRYVALLLAGSLSLWAFKWSREGTTTSILAVTSSTSVLLFLYLGGLAGSVLLYRLFFNPLNRFPGPFAARLSKLYFVYLSSDLRGHRKLHELHQKYGRYVRVGPNDLSVVDPDGMKIVLGANSKCTKSAWYGQDMPYISTNTTRDRAAHDRRRRILAPAFSDKALRGYASRLQKFHDLLTSQIDASAGKPMNVTKWFGYWGMDMMCDIVFNGSFNMLASGETHWALQVVGDGLHLQGFALPPWLYRVFATMPKSSSGSRGLAAFAATQLENRMQQQGKTAHADMMQPLI... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic . Leucinostatin A contai... |
Q815X8 | MKRHTRKIAIIGTGLVGSSCAYSIVNQGICEELLLIDINHERAVGEAMDLSHCINFTNTRTKVYAGSYEDCKDMDIVIITAGPAPKPGQSRLDTLGASAKIMESVVGGVMASGFDGIFLLASNPVDIITYQVWKLSGLPRNRVIGTGTSLDSSRLRTILSEMLHVDPRSIHGYSLGEHGDSQMVAWSHVTVGGKPILQILEEQKERFGEIDLDEIVEKTAKAGWEIYKRKGTTYYGIGNSLAYIASSIFNDDHRVIAVSAILDGEYGEYDICTGVPAIITRDGIREVVELNLTEDEESRFAKSNDILRDYMKTIGY | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 34698
Sequence Length: 316
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q9CGG8 | MKINNKKVVIVGAGAVGSTYAHNLVVDDLADEIAIINTNKSKASANSLDLLHALPYLNAAPKNIYAADYSDVSDADIVVLSANAPSATFGKNPDRLQLLENKVEMIRDITRKTMDAGFDGIFLVASNPVDVLAQVVAEVSGLPKHRVIGTGTLLETSRMRQIVAEKLQINPKSIHGYVLAEHGKSSFAAWSNVTVGAIPLTTWLKKYPNPEFPTFDEIDQEIREVGLDIFMQKGNTSYGIAASLARLTRAIFRNESVILPVSAYLTGEYGQFDLYTGSPAIIDRTGVRAVLELELTQEEQEKFKASTVLLKENFDSIKEK... | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 35271
Sequence Length: 323
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q9BYZ2 | MSWTVPVVRASQRVSSVGANFLCLGMALCPRQATRIPLNGTWLFTPVSKMATVKSELIERFTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPFTKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHCKLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILGEHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWAIGLSVADLTESILKNLRRIH... | Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 41943
Sequence Length: 381
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
EC: 1.1.1.27
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Q27888 | MASTIKEVFAEIAAPVENSHGKVTVVGVGQVGMACAYSILQQNLANELCLVDVVADKLKGEMMDLQHGLAFTRHCTVKADTDYSITAGSKLCVVTAGARQREGETRLSLVQRNVEIFKGIIPQLVKYSPDTCILVVSNPVDVLTYVTWKLSGLPRERVFGSGTNLDSARFRFLLSEKLNIAPSSCHGWIIGEHGDSSVAVWSGVNVAGVTLHEIKPDIGEKTDNEHWEAEIHKKVVDSAYEIIKLKGYTSWAIGLSVAKIAQGIFSNSRNVFALSTNVKGFHGINDDVYLSLPVVLGSAGLTHVVKQQLTEAEVQKLHNS... | Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 36065
Sequence Length: 333
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q892U0 | MNKKGIKISIIGSGFVGSTTAYALMMEGLASEIVIVDINKEKAKGEAMDLSHGVSFVKPVDIIAGDYEDTKDSDIVIITAGAGPKPGETRLDLINKNYEIFKGIVPEVVKYSPKSILLVVSNPVDILTYVTYKLSGFPQERVIGSGTVLDTSRFRYLLGEHFKIDVRNVHTYILGEHGDSEIAAWSLTNIAGISVEDYCKDICKGCEGNFKNRIPEEVKNAAYEVLERKGYTSYAIALAVRRIVEAIIRDEDSILTVSTLLRGEYGINDIYMGIPSVIGETGIKRVLEVKLSKDEEKQLKESAEVLKENLNKIPIK | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 34824
Sequence Length: 316
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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