ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9JKU1 | MMEGHILFFFLVVMVQFVTGVLANGLIVVVHAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLCLFSLVRHTLFEDNITFVFIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILGSVLYVIITTFIHSRETSAILKPIFISLFPKNATQVGTGHATLLSVLVLGLTLPLFIFTVAVLLLIYSLWNYSRQMRTMVGTREYSGHAHISAMLSILSFLILYLSHYMVAVLISTQVLYLGSRTFVFCLLVIGMYPSIHSIVLILGNPKLKRNAKMFIVHCKCCHCTRAWVTSRSPRLSDLPVPPTHP... | Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37852
Sequence Length: 335
Subcellular Locatio... |
O00300 | MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACK... | Function: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial... |
Q7M721 | MNLVEWIVTIIMMTEFLLGNCANVFITIVNFIDCVKRRKISSADRIITAIAIFRIGLLWAMLTNWHSHVFTPDTDNLQMRVFGGITWAITNHFTTWLGTILSMFYLFKIANFSNSLFLHLKRKLDNVLLVIFLGSSLFLVAYLGMVNIKKIAWMSIHEGNVTTKSKLKHVTSITNMLLFSLINIVPFGISLNCVLLLIYSLSKHLKNMKFYGKGCQDQSTMVHIKALQTVVSFLLLYATYSSCVIISGWSLQNAPVFLFCVTIGSFYPAGHSCILIWGNQKLKQVFLLLLRQMRC | Function: Putative taste receptor which may play a role in the perception of bitterness.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33594
Sequence Length: 295
Subcellular Location: Membrane
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Q61382 | MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLAIRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVCPQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLKDSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRR... | Function: Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis. Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby ... |
O00463 | MAYSEEHKGMPCGFIRQNSGNSISLDFEPSIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICPVDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQPVQCSNEKCREPVLRKDLKEHLSASCQFRKEKCLYCKKDVVVINLQNHEENLCPEYPVFCPNNCAKIILKTEVDEHLAVCPEAEQDCPFKHYGCAVTDKRRNLQQHEHSALREHMRLVLEKNVQLEEQISDLHKSLEQKESKIQQLAETIKKLEKEFKQFAQLFGKNGSFLPNIQVFASHIDKSA... | Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediatin... |
P70191 | MAHSEEQAAVPCAFIRQNSGNSISLDFEPDTEYQFVEQLEERYKCAFCHSVLHNPHQTGCGHRFCQQCIRSLRELNSVPICPVDKEVIKPQEVFKDNCCKREVLNLHVYCKNAPGCNARIILGRFQDHLQHCSFQAVPCPNESCREAMLRKDVKEHLSAYCRFREEKCLYCKRDIVVTNLQDHEENSCPAYPVSCPNRCVQTIPRARVNEHLTVCPEAEQDCPFKHYGCTVKGKRGNLLEHERAALQDHMLLVLEKNYQLEQRISDLYQSLEQKESKIQQLAETVKKFEKELKQFTQMFGRNGTFLSNVQALTSHTDKSA... | Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediatin... |
Q6IWL4 | MACNDVDKSSFDDVCCDSGHSSCAAAMEKERESFLSPTENPSTISVSSSMPPDQQGYDVEFDPPLESKYECPICLMGLRSAVQTPCGHRFCDSCIRKSIRDTGQKCPVDNEVLLEEQLFPDNFAKREILSLTVKCSNFGCSEKMELRQLEKHLSQCRFATAPCPQCQESVPISHLDEHKSQHCLQRIMTCPDCAGSFVYAVKQNHEQFCPFANTVCEYCEMELIRDQLALHCDTDCLKAPVACTFSTFGCREKMTRNELAQHMQEFTQMHMRYMAEFLRSQTLNNCTMPSAAAHLSSDDRGASARSPDSCQCKQELLNLR... | Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation.
Catalytic Activity: S-ubiqu... |
Q9Y4K3 | MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKM... | Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2 . Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation . Leads to the activ... |
Q6Q0C0 | MSSGKSARYNRFSGGPSNLPTPDVTTGTRMETTFGPAFSAVTTITKADGTSTYKQHCRTPSSSSTLAYSPRDEEDSMPPISTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNVKLTVVVNNIAVAEQIGELFIHCRHGCRVAGSGKPPIFEVDPRGCPFTIKLSARKDHEGSCDYRPVRCPNNPSCPPLLRMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLG... | Function: E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MAP3K3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators . Induces apoptosis when overexpressed . Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its i... |
A0A481WQD3 | MTSGTEQATLNTEENGSDSDHLSKEPIAMPALDWDGPTDSNNPRNFSTPKKVFITACLASLVCISTFGSSVMSPASGQLIHEFGISKELSILATALYVLGFAVGPLLFGPASEVLGRKYPLSVGVFLFAIFSIPIAVAKNVATIFVCRFLCGTFAAAPLAIAGGGLADLWEPLSRGIAVAGFASATFLGPVLGPLVGGFVTKSHLGWRWTQWLSIIFSLVFLAIYFVFCPETYSPIVLARLAKKRGQMPPGGKVDFKQLAKVYMLRPFIMLVQEPILALLTLYMGFIYGFLYLCFEAFPIAFEEHRGWDIGIGSLPFLSI... | Function: MFS-type transporter; part of the tra gene cluster that produces terrestric acid . The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52532
Sequence ... |
P02788 | MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFK... | Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.
PTM: Phosphorylation at Ser-10 activates the transcriptional activity . Phosphorylation at Ser-10 also promotes proteasomal degradation . Alternatively can undergo ... |
Q9VTZ5 | MASSLVFVALVGALCFTLANAQHHYDEHKTTRMVWCTKSQAEQYKCQNLTVAIERDRALFDEVFLNLTCFMAYSADECIHHIDREKAHITTLDAGDVFTAGRYNSLIPIMQEKLEGGFADYQSVAVIKKGSLPDLNNLRDMRNKRVCFPWVGSLAGWIVPIHTLQREGGMEVVDCNNQVKTAASYFNNSCAVYSLSDKHNPIGDNSDKLCTLCTGKIPGGRCSSADPYFGYEGAFKCLLEKGDVAFLRHSTVNEMLQTTEFKNIAPDTFELLCRDGRRASINDYRQCNWGQVPADAIVTSSARSFSDRKQYQQFLKRIAE... | Function: Iron-binding protein and component of septate junctions that form the paracellular permeability barrier in epithelial tissues . In an iron-dependent manner, required for septate junction assembly during epithelial maturation in embryos and mature septa junctions stability .
Location Topology: Lipid-anchor
Seq... |
P08582 | MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQ... | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc.
Location Topology: Lipid-anchor
Sequence Mass (Da): 80215
Sequence Length: 738
Subcellular Location: Cell membrane
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Q9R0R1 | MRLLSVTFWLLLSLRTVVCVMEVQWCTISDAEQQKCKDMSEAFQGAGIRPSLLCVQGNSADHCVQLIKEQKADAITLDGGAIYEAGKEHGLKPVVGEVYDQDIGTSYYAVAVVRRNSNVTINTLKGVKSCHTGINRTVGWNVPVGYLVESGHLSVMGCDVLKAVGDYFGGSCVPGTGETSHSESLCRLCRGDSSGHNVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGNTLPSWGKSLMSEDFQLLCRDGSRADITEWRRCHLAKVPAHAVVVRGDMDGGLIFQLLNEGQLLFSHEDSSFQMFSSKAYSQ... | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc.
Location Topology: Lipid-anchor
Sequence Mass (Da): 81293
Sequence Length: 738
Subcellular Location: Cell membrane
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O97490 | MRCRSAAMWIFLALRTALGSVEVRWCTASEPEQQKCEDMSQAFREAGLQPALLCVQGTSADHCVQLIAAHEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVKRSSNVTINTLRGVKSCHTGINRTVGWNVPVGYLVDSGRLSVMGCDVLKAVSEYFGGSCVPGAGETRYSESLCRLCRGDTSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGRTLPSWGHMLMSRDFELLCRDGSRASVTEWQHCHLARVPAHAVVVRADTDAGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQ... | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 80170
Sequence Length: 736
Subcellular Location: Cell membrane
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P34981 | MENETVSELNQTQLQPRAVVALEYQVVTILLVLIICGLGIVGNIMVVLVVMRTKHMRTPTNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSLYCMLWFFLLDLNISTYKDAIVISCGYKISRNYYSPIYLMDFGVFYVVPMILATVLYGFIARILFLNPIPSDPKENSKTWKNDSTHQNTNLNVNTSNRCFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIY... | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45085
Sequence Length: 398
Subcellular Locatio... |
Q9BVG3 | MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSSFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFDELQRELKDQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTLDPGTAHQRLILSDDCTIVAYG... | Function: E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways . E3 ubiquitin ligase activity is dependent on E2 ubiquitin-con... |
Q80V85 | MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSAFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFEELQRELKEQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTMDPGTAHQRLILSDDCTIVAYG... | Function: E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). E3 ubiquitin ligase activity is dependent on E... |
Q969Q1 | MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALR... | Function: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle... |
Q38HM4 | MDYKSGLIPDGNAMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLVDSCRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEEKLGFIEALILQYREQLEKSTKLVETAIQSLDEPGGATFLSSAKQLIKSNVEASKGCQLGKTEQGFENMDYFTLDLEHIAEALR... | Function: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle... |
Q6PJ69 | MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVC... | Function: E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation . Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs . This... |
Q8BFW4 | MAAQLLEEDVVTCSICLGRYRDPVTLPCGHSFCGNCIQDSWRSCEKSCPECRQPFPEGAKLSRNVKMSTLLQALPVLPAPPAVTPRRDSATSHSARCLRHGRPLEFFCRTEGLCVCSACTVHDCSHHERALLDVERRVREDQLRARVLVTQQQVAQAETQLQELQEQRSRIESSACTLASVVSRRFSSLLQALEKQQASTLSDIEVAKKQALGQVLNEKQRLTDHLRALSQYDQSVQDLLAQADDCIFFQELQQLPEPTESLGPLTSPQWNEEQQLSNVNQLLSPLCELLLEEKSLPKVAAKAADAGPLETLGPLAPVPS... | Function: E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation . Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs. This ... |
Q6AZZ1 | MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVEKVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAWKLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQVLWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSE... | Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity.
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine +... |
Q86WT6 | MEVSTNPSSNIDPGDYVEMNDSITHLPSKVVIQDITMELHCPLCNDWFRDPLMLSCGHNFCEACIQDFWRLQAKETFCPECKMLCQYNNCTFNPVLDKLVEKIKKLPLLKGHPQCPEHGENLKLFSKPDGKLICFQCKDARLSVGQSKEFLQISDAVHFFTEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCP... | Function: E3 ubiquitin ligase that plays an important role in antiviral immunity by restricting different viral infections including dengue virus or vesicular stomatitis indiana virus . Ubiquitinates viral proteins such as dengue virus NS3 thereby limiting infection . In addition, acts as a key mediator of type I inter... |
Q6ZMU5 | MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPP... | Function: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond forma... |
K9IMD0 | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFK... | Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.
PTM: N-glycosylated . Glycosylation is important for draculin anticoagulant activity . Probably also O-glycosylated .
Sequence Mass (Da): 76856
Sequence Length: 708... |
Q4WXA1 | MEDDDRPRKYPKLNHDEVQEGSEPVMTGAVGAVHDDDAESADSDNRASPSNDRIDNDVKQACDEEGQDAHGKDGPPTLSKNQLKKLKRKEHWEAMREQRKVKRKEKLVAKRERRRAALEQAKQEGAEATEETRKAFESTQKKFQRSTLLPVTLVLDCSYDDLMLDKERVSLGAQITRSYSDNSRAPFRSHLVVSSFNKLLKERFDTVLGKTHENWKGVRFLQEDFAEAAEMAKEWMQGPKGGQLAGVFADKADAKPEDGEIVYLSSDSPNILTELKPYSTYIIGGLVDKNRHKGICYKSAVAKGIKTAKLPIGEYIQMAH... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q59Q39 | MTEQTSEATVVNNSPAPTIPKIKREKPTPEEIEERRKLKQLEVVPEGFSRKQWKRELKKQRWQDTKQEYLEVQREKKRLARQRKRERLKDLDENDELRKAQPIPSRQISTNNVSVIIDCDFDELMHEKEIVSLSNQIKACYSAMRHCTYKLPIQITSFNKRLKQRFEAQLHDYHLWQGNISFTDRSLTEYVTGAPNSESKDNDGNSNSNTTNSTDTINTENLVYLTADTDEEITKLEPNHTYIIGGIVDKNRHKQLCYNKAKELGIKVARLPIGKYIEMNGRHVLVTSHVYELLCKWFENDGDWETAFNKVLPPRKIKSK... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
P0CS10 | MKFHLGLTEALQEREPNINASSKDLSPLHFELYRRSEPIMDIDEESYLNAGPSAPSKIPQGGEGDRLQGMSKKAMKRAAKQARLEEIKPLKRAAERERRRQRTAQLAEGYAAGTLSEADKELVERRRRVEKERKEAQRRIESGDQANDWLGGVVIDLGFDDLMTDQEIASMAQQLGYLYSSNRTAEKPVRTVIHTTFSPAASPRLWQRMENFNWHKWSRCHWWEQGLETLKSQLDPSTSILSVQSVVSKETQDKAGIDTKSLLSRLTGPQVPVDLQAGKHKLVYLSADAEDELLSLSEDEIYIIGGIVDRNRHKNLCQGK... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q6BWG3 | MENQDTEQSQKRSGSEVEKDDFKRQKVVVPEGMTKREYKRQLKQQRWEETKDEYKQKKREKKKAARERRKERIKEAEANGETNEELYNYHQMKRAKVAPQEQIDTDVKIIMDCEFDSLMNDKEIVSLSNQITRSYSAKKHSTYDVQLDITSFNKNLKKRFEKAIPQYDKWTNVTFVENDKLEDILPMDDKQALSKYVYLTADTDEVIDTLEPHHTYIIGGIVDKNRYKNLCLNKAQSLGLKIGRLPIDKFIKMNGRQVLATSHVFELCCKWFENDKDWGKAFNEVLPPRKVKGKLTHGSDPEKSIEPSEVSEQPVSSEQS... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q5B8X0 | MEEEERPRKIQKLGSSEAHESEPLITGAIKGSQDDTSPAEQTNSQKAIPGATTDNSKESEEPASSTATDGPETTEQKISKRQLRRQAKLEQWEAKREERKIIRKQKTAARKERRRELWEEAKREGKDPNEELNKLFPMTTRTRHRKSTRLPLTLIIDCGFDDLMQDKERVSLGQQLTRSYSENNKSAFNGHLIISSFNKKLKERFETVLHKTHEGWKGVRFTGEDWLQAAKEASEVMQGPNGGKLVGPFEDKTDAKPEDGEIVYLTSDSSETLTELKPYSTYIIGGLVDKNRHKGICHKRATELGIRTAKLPIGQYIQMN... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q4I8X0 | MDLDPAHKPSQAEETKEQGNEQGQVEQNQAQQDPTTGPQAETEKAIIPSQGSTIPQKRSAEDEPAQPMSKNALKRLRKQQQWEAGKEDRKLKRKDSRIARKVRKREERDALIAQGINPYANKQKPPSVNVPISLIFDCEFEQYMREKEIISLGSQITRSYSENKNAKYRTNIYVSNWNGKLAERFHQILDDKHQNWKGIDFVEGDFIECAEKAREKMKHENMIEPLQRSLTEKSPWARDEKDPLPLPDPEPEPRPEYSDIVYLSSDSPYTLERLEPNTSYVIGGLVDKNREKGLCYKRARERGIRTARLPIGQYMVMQSR... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q6CUM6 | MSDTSENSNAEIPADTSDVKDKPKPIVRAPQFPPPPEGISKSQWKKICRKKRFEETRAEYAQIRKEKRNRAKLARREKLKEYTDRGEEIPEELKRPPKVNLNQSDSGISIILDCSFDDLMNDREIVSLSTQVTRAYSSNKRENNYAKIKVTSFDKRLKQRFDNDLSNSNYTKWKNFEFTADPTLPTENAVYLTADTEEKLDTLEPGTTYIVGGIVDKNRHKNLCYNKAKELNIPTKRLPIGEFINLAGRKVLTTSHMVQLMLRYFDNKDWKEAFESVLPPRKLEVDSTKEDSETASAE | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
O14214 | MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q4J894 | MTLAKVFSQKLRELGISSIYIGHERPSLQSLAIKMLLKNYGLVEERREGMLITQDHGIKLISGKGTETSRYTFRKGGKKVSIHLPEYPKMVIDLGLFEFLNEEEKEKTLLQVDLCLSVIRKFLWDGNLTVVGKADYVLGRANIVQSLSLSDEDNPVILDPYGDVVATDQILRDHNVFVIGGIVDKGRRLDRATERLALSRGYSFPRVKIQLRGSIIGVPDEINKILEIILRVKELDQSLEEAIISLQSKSDKISRLLHDVQLYGMEVLEEEARWLRADDKVIEIVRSRLGKN | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.
Catalytic Activity: adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33153
Sequence Length: 292
Subcellular Locat... |
Q5JD38 | MKTLADVFREALKEKGISSIGTLSKRFRKSKNKLQDIAIEIVHGKGAVFRVPEKTAVAWDLNGNRVDGSYYAYAPLCMREKFEPVLTPEELREKLPDWPYFIIDLYHWDKHTQKEKGKICLQVNQSYGLLRDYFTGSELAVTWANEEFREMFHGPLDRITTYGGPTSEFLKENGINEVVLLDPWAEEVLSEKDFDVKAFIIGGIVDTGGNKKKTTPKIGEELESAGIKVRRRKIVLRGDVVGVPDRINRILGIILKMMVEGKSMDEAVYEMQEPLHARWRLRKELPKRATRYMVEGKVYRVVEKELFDEYSKWLKIRWED... | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of either N(1)-methyladenine or N(1)-methylguanine at position 9 (m1A9 or m1G9) in tRNA.
Catalytic Activity: adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42996
S... |
Q6C1W9 | MVDVTEPVAPVEAVKETAGASSATPEVDRTSEPHPKNPQNVPAPYNTKTAVIPEGMSKNEWKKAQKKAIWESKKDEIAAVKKEKKKAARKRKQLAISRGEIPAPIPQDERPPQTQLPISIVLDCGFDEMMTQKEKVSLSAQVGRCYSANRKADARFDLTVNSFNKGLKDRFNNEMNKVHELWTNIKFVEDDYTVPEDETAKSKLVYLSSDSDNVINELEDGKTYIIGGIVDKGRYKNLCQDKASKQGLQTGRLPIADFIKLSGRKVLTTNHVFEILLKWTELKDWKAAFEAVLPMRKLDPANYGRAHRRARKKARLAEGA... | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (D... |
Q12400 | MSNDEINQNEEKVKRTPPLPPVPEGMSKKQWKKMCKRQRWEENKAKYNAERRVKKKRLRHERSAKIQEYIDRGEEVPQELIREPRINVNQTDSGIEIILDCSFDELMNDKEIVSLSNQVTRAYSANRRANHFAEIKVAPFDKRLKQRFETTLKNTNYENWNHFKFLPDDKIMFGDEHISKDKIVYLTADTEEKLEKLEPGMRYIVGGIVDKNRYKELCLKKAQKMGIPTRRLPIDEYINLEGRRVLTTTHVVQLMLKYFDDHNWKNAFESVLPPRKLDAEAKSASSSPAPKDT | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (... |
Q58780 | MVVEVLRLGHRGDRDKRISTHVALTARALGADKIIFTTEDEHVENSVKKVVESWGGNFEFVVEKHWRKYIREFKKRGIVVHLTMYGANINEIMPEIREISRDKDILVIVGAEKVPKEVYELADYNVSVGNQPHSEVAALAIFLDRLFEGKTLYRDFEDAKIKIVPSKDGKVVIREKQNK | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20573
Sequence Length: 179
Subcellular Location: ... |
O27185 | MDVKVLRLGHRPSRDARITTHVCLTARAFGASEVILSGEEDPKLMEGVEDVVRRWGGPFSVVYRRNWQGVIDSWKKDGGEVIHLTMYGLPARDVVPGIMDNGKDKLIVVGGARVPGKVYSLADYNVGVTNQPHSEVSSLAVFMHMLLDGAEFDLKFEDARIEVIPQARGKMLREIDDGD | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 19831
Sequence Length: 179
Subcellular Location: ... |
A9A624 | MVIEVVRIGQRLVRDDRVTTHVALVSRAFGAERIFMTEINPEIKDTLGKINDTWGGNFEIEFIDSWKPIVKKKKEEGFKIVHLSMYGEKINDAQEEIRKEENLLIVVGAEKVPREIYELADFNVGVGSQPHSEISALAILLDRIQGGQQFEKEFPNAKRKIIPTKTGKNVQVKETRD | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20187
Sequence Length: 177
Subcellular Location: ... |
Q5P8D0 | MPLPAIDPAEYASQLADKVTQFKHAFTPFAVPEPTVFPSAPLHYRLRAEFRMWHDGERIDYAMFDPAEPKQPIAIEQFDIAAEPICAAMPRLRERLRASETLKRRLFQVEFLATLSGELMISLIYHRPLDESWEAAARELAAELNVQLIGRSRKQKIVLDRDWVLERFALDGRPLQYKQIEGSFTQPNGGVNRQMLGWACEQVRGVGGDLLELYCGNGNFTVALAPLFDRVLATEVSKTSVEAAHYNLAANDIGNVAMVRMSSDEISAALARTREFRRMKDVDLDRYRFSTLFVDPPRSGLDAPTVELARGFDRILYISC... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
Q0ACP5 | MERRADAATGKRPIRSFVRREGRLTAGQQRALELLWPAFGLERPPAGQPLDLDRAFGRRAPRILEIGFGNGESLAEQAATHPERDYLGIEVHRPGVGHLLMEVEKRHLGNVRVMMADAAEVLAHHIPDGSLHGVQLFFPDPWPKKRHHKRRLVQPQWVRAVAAKLAPGGFLHLATDWADYAEHMLDVLEAEPDLENTCGPRQFSPRGERPETKFERRGLRKGHQVFDLYYRKREHPG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27016
Sequence Length: 237
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A6TMJ6 | MRVRHIPGAKEQLKEYEFYIQDPSQYQNQWHLYFQNQHPIHLEVGLGKGQFLTTLAKVHKNINYLGLEKSQEVLLQALKKLDRQVSRQELSNMGLFHYNALDLNEVFGEGNIEKIYLNFSDPWPKERHKKRRLTHQGFLKIYRGLLSEQGEIQIKTDNKALFEFSLQQLKEENFHFVQVIYNLHNDGIKDPFMTEYEEKFVKAGKTIYKCIATV | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25387
Sequence Length: 214
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q2IG43 | MIFSIEDDAPIVRDLLPDWRARFGEAGGRLELEIGCGHGGFALGFARAFPERALVGIEQRRKFAAELAAKGARHGLSNLLVLNGDARLLAPRLFAAGSLAAIHVHFPDPWWKRRHHRRRLVDDRMSALLLGLLAPGGVLDFRTDVERYAREAVVRLEEVGFRNAAGPGRFAEAAPDEIPSTRERRYLASGEPVWRLRLVKA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22375
Sequence Length: 201
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q7Q2P7 | MEEAIDDHVKLPQKRFYRQRAHSNPIADHSFDYPLLPELSNWNELYPNIGNRQVVFADIGCGYGGFLVTLGETFPDKLAIGMEIRVKVSDYVMDRIKALRQRHKGKYENIACIRTNAMKYLPNYFRKHQLEKLFFLYPDPHFKKAKHKWRIINPTLLSEYAYVLRPGGKIYTVTDVRELHEWMCKHIEEHPCFKRLPDTEAQEDILAPKLLDSSEEGQKVTRMSGEKFMAIFTRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27662
Sequence Length: 235
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
O66479 | MLCYVNYKRVKRPVEIPNLEVEIGFGRGDFIVKLAKENPDKNFFGIEISQISIEKLMKRVGKKGLKNVYCTNVDAYWGFYFLFRDNYVENIYMNYPDPWFKKRHHKRRLTKPERLYMFAKKLKLGGEIRIRTDNYEFLEFTKESAKVLDCFEVEEGTLNVKEPLTKYEQKWLSMGKTLYKLILRKVKEPKFVEHPEVEEVRELFPVKVKVESVDPKKIESREIKLDEEVYFKTFKVWQRDKDFLVECLLSEKGYLQKFFIQIKRKEDGYVIDVSPYSEVLRTRNLQRSIQTVAQLLS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35639
Sequence Length: 297
Domain: The C-terminal region is probably involved in ... |
Q8GXB7 | MDNETKATTFSKSTGLPRKRFYRARAHSNPLSDSHFPIPISPAHVDYSLHFPKFVEADNKFIKKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVTEYVKERILALRRTSSEGQYENISVVRTNSMKYIPNYFEKGQLSKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDPVVELLCSATEEGQKVARNGGQTFRAVFRRIAYVS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28818
Sequence Length: 251
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q8G9C6 | MTFPSHNPPETGHPSAAPDEALPAAEAPVPGDPEARFSSRSIRSFVLRQGRMSVAQQRHLDETLPKVGIPYRVAPLDLDAAFGRAAPKIVEIGFGMGETTAKIAAALPDKDFLTIEVHGPGVGSLCKLIAEGVLDNVRIVQHDAVEVLRDMIPERALAGVHVFFPDPWHKKRHHKRRIIQPDFVALIASRLAPGAYLHCATDWEEYAQWMLEVLAAEPALENTADGYAPRPAYRPLTKFENRGLKLGHGVWDLVFRRRG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28575
Sequence Length: 259
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A0K1I7 | MSESPETPEPSPAQSPEAAPEQPQAARPVTPGSQASFGTYGGRPVSFVRRGTRLQGRRQQAWEEHSDRWAVDVPRHIANTSVHPDYVFDAEAEFGRSAPLIVEIGSGLGDAVCHAAEENPDWDFLAVEVYTPGLANTVIKINSRKLSNVRVVEANAPEVLATMLPAGSVSEVWVFFPDPWHKSRHHKRRLIQPEFAALVAAALKPGGLFRVATDWSNYAVHVRDVMAGSADFVNLHDGERRGPESPLTQVWQSGVESLVGGAPVKEGRAPVSTEHTGPNEGVDETGGWAPRFEGRIRTSFENKAHEAGRLIFDLCYRRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34907
Sequence Length: 319
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q4WQB9 | MTPPPPKRQKRDEYRKATAEATSQSGASDVAEIKLPKKKYYRQRAHANPFSDHHLKYPLSPAHMDWSSHYPAFVNPDPSHINLAGARRLLKDVEVVDIGCGFGGLLIGLAPLLPESLIVGMEIRVSVLEYVTTRIQALRAQQQKLRAATATATAASETPSQQQAQIDGKQANANAAADAASPAPSTDTEHMPTTLVPGSYENISAIRSNTMKFFPNFFARHQLSKIFICFPDPHFKARKHKARIISETLNAEYAYALRPGGLLYTITDVEEYHHWILRHFGVELGAEEESEEKSTSPNANANAGVRELFERVSEEELEKD... | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39946
Sequence Length: 358
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A8IG13 | MTALSETEHKGAFYGRRVGKTLRQGQQQALARTLPRYLIDLPTVAEPAALFPCPVDEIRLEIGFGGGEHLLSEAKRFPRAGYIGIEPFLNGMAKAVLELDLAPQENVRLFNLDAALLLARLPEGSVSQVELLYPDPWPKRRHWKRRFVRPDNLDLLARALKPGGVFRFASDVPDYVDWTLREVRAHPAFRWTQTRADDWRTPYEGWPGTRYEAKAIAAGRVPTYLSFARV | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26108
Sequence Length: 230
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B0TXQ5 | MSDNSKENLRQIKSYVQRAGRVTKKQQQALDDYASKYMIEYDQNKSLDFSEIFKNSNDVVLEIGFGMGGSLVQMALENPTKNYLGIEVHKAGVGNILYEIEHQNISNLLVMSHDAVEILENMISDNSLSGMQIYFPDPWHKKKHNKRRLVNQSNVDLFAKKLKVGGVFHYASDWLPYAEEVLELLENDNKYKNLYDGFAPRPEWRPLTKFEKRGQNLDHPISDILFEKI | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26515
Sequence Length: 229
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q8Y1I7 | MQPNEQPGTGPADTTLEQQDTAAAEVGHPRRIRSFVRRAGRTSTGQQRAIDELGPRFLLPYAAAPLDWEAAFGRTGARRIFEIGFGMGETSAHIAQLRPDDDFLGVEVHEPGVGALLKLIGERGIGNVRIVSHDAVEVLAQMIPEGTLDGIHVFFPDPWHKKRHNKRRLIQGPFVARLAAHLRPGGYLHCATDWEEYAHQMLEVLSAEPLLENTADGFAPRPDYRPVTKFEKRGLRLGHGVWDVVFRKRAA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27913
Sequence Length: 251
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B2U7E2 | MQPIEQPGTGPDDITPESQDTNTAESAESGAETGHPRRIRSFVRRAGRTSTGQQRAINELGPRFQLPYTTEPLDWDAAFGRAGAKRIFEIGFGMGETTAHIAQLRPDDDFLGVEVHEPGVGALLKLIGEREIGNIRIVSHDAVEVLAQMIPEGTLDGIHVFFPDPWHKKRHNKRRLIQSPFVARLAAHLKPGGYLHCATDWEEYAHQMLEVLSSEPTLENTADGFAPRPDYRPVTKFEKRGLRLGHGVWDVVFRKRG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28698
Sequence Length: 257
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q98BJ3 | MSPQDRPSRTTEAFFGRRRGKPVRPQQAAALESGLDAYRLDLTADAPSDLRTLFETEVSAVRLEIGFGGGEHLLHRAIEAPTTGFIGVEPFVNGMAKMMMAVRARPLANLRVHDDDATRLLDWLPPASLGGIDLLYPDPWPKKKHWKRRFVSPVNLERFARVLKPGAKFRFASDIDTYVNWTLLHCRAHGAFAWQAAEAADWHRPYEGWPGTRYEAKAIREGRRPAYLTFVRK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26434
Sequence Length: 233
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q92SI3 | MTETRGARATEAFFGRRKGKPLRERQAAHLEHLLPLLKLDLEEPAPADLTALFPEPVERIRLEIGFGGGEHLIHRAAEDPATGFIGVEPFVNSMAKLLGQIEAKAIRNIRLYDDDATQVLDWLPAASVDQIDLLYPDPWPKRKHWKRRFVSQINLDRFARILKPGGLFCFASDIDSYINWTLIHCREHAAFEWTAERAADWLTPFAGWPSTRYEAKARREGRSSAYLAFRRA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26532
Sequence Length: 232
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q7UN36 | MLVVAAMRVWNPEEGWANRVGRKREGKIVEILRRVTMTAHGLSHFPRQLLRMPRAALRKPNPALDLDSWLKTPEDLPATINSQTLFGNDQPLEIEVGSGKGLFIQTESDRRPEHNYFGIEIARKYAAHAAARLAKRERANAKMLAGDATPLFAVTDEGKRIEDGSLDGVHVYFPDPWWKKRHRKRRVLSHDNILNFSRCLRVGGRLHFWTDVLDYFELTVELIAEIAPELGVPLPETQRESTHDLDFHTHFERRSRKMGIPVYRVCYRKRS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31306
Sequence Length: 271
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q0S679 | MPETPLMRDNGPVNHADQDAPAVPEEGQTKDSKGSRLHPRVTSFRSRRGALTVAQQESWDRQWPRIGADVSDHRLDAPSWFGRDAPLILEIGSGTGTATAAMAKAEPHVNLMAVEVYRPGLAQLLQQIERDEIPNIRVLRGDAMDVLENMIEPESLTGVRVFFPDPWPKARHHKRRLLQSPTFALIASRLKAGGVLHVATDHAEYAEAIAEAGNAEPLLTSLDWESPMTHERPVTKFEDKAHQVGSAITELIWGKIRS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28586
Sequence Length: 258
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q2RMS4 | MPEKPTEDARFYGRRKGKPLRATRQRLLDTMLPALTLPLAGLGEGERLDPRGLFPRPVDQLWLEIGFGGGEHLVAQAAAHPEVGLIGSEVFAYGVGKALSQIDETGVDNIRLWPEDVRQVLPALPDGCLQRLFVLFPDPWPKRRHARRRMIQPARLDDFARLLADGGELRVASDDMGYVRWTLMHVTAHPAFRWTAQGPTDWRERPADWVETRYEAKALQAGRKPAYLIFRRRPRAADPGTLAEAPAGEGADNNP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28578
Sequence Length: 255
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q161H1 | MSKQTRPHRNFYGRLKGKSLKAAQKRYLDEDLAALSPGAVGWEENPDRRPLDLPGLFEGKPVWLEIGFGGGEHLVHQAAQNPDIGIIGAEPYINGVAMLLGKIRRAGVENLAVHAGDARDLMDVLPAASIDRAFLLYPDPWPKARHHRRRFVTAEHLDPLARALKPGSVFRVATDIEDYVRQTLQEVPKHGFKWLANAPQDWRRPWPDWISTRYEQKALREGRTPHYLTFVRE | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26531
Sequence Length: 233
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q1AUF5 | MTRRKLGRMKVRPPDPETAQRYLLRFTGRQLYHEAERLPGLSSPELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRAVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTGFDPPVKSRFQKMWERRGRTIYRFELVRP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26541
Sequence Length: 223
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B8I005 | MRLRRKPWARPELAACDFYVDDPPSYKGRWREFFDNSNPIHLELGCGKGGFISELAADNQNINYIAVDIKSEVLALAKRKIEKEYKERGIQEIKNIRLMSHNIELIDNMLDTVDFIEKIYINFCNPWPKTPYKKKRLTHGKQLIKYKQFLASGAEIWFKTDDDGLFEDSVKYFEENGFIIKYKTWNLHESGFGENVPTEHEIMFSEEGIPIKFLIAEYKQKIHQAVCIGINIKEEN | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27703
Sequence Length: 236
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
O31741 | MKIDFLTLFPEMFEGVLGSSILQKAQEKDAVQFQVVNFREYSDNKHNTVDDYPYGGGAGMVLKPQPVFDAVEDLTSKAAAAPRIILVCPQGERFTQKKAEQLAKEEHLLFICGHYEGYDERIREHLVTDEISIGDFVLTGGELPAMMIADSVVRLLPGVLGKEASHIEDSFSTGLLEHPHYTRPADYKGLKVPETLLSGNHAKIEEWRNKESIRRTYLRRPDLLKDHPLTEQQRKWISEWEKE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27709
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q8A9C2 | MRIDIITVLPEMIEGFFNCSIMKRAQNKGLAEIHIHNLRDYTEDKYRRVDDYPFGGFAGMVMKIEPIERCINALKAERDYDEVIFTTPDGEQFNQPMANSLSLAQNLIILCGHFKGIDYRIREHLITKEISIGDYVLTGGELAAAVMADAIVRIIPGVISDEQSALSDSFQDNLLAAPVYTRPADYKGWKVPDILLSGHEAKIKEWELQQSLERTKKLRPDLLED | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25558
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q6G1R9 | MKFQARVLTLYPEMFPGFLGCSLAGQALKQGIWSLETVQIRDFALDKHHSVDDTPAGGGAGMVMRADVLAAALDSCPNDSPRLLMSPRGRLLNQAYARSLARSSGVTLVCGRFEGVDERIIEARELEEVSIGDYILSGGETAALVLLDAIVRLLPGVMGNEISAKCESFENGLLEHPQYTRPAVFEGRGIPPVLTSGHHKAIANWRQQQAESLTRQRRPDLYALYNKNRQKT | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25463
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q5ZYH6 | MALHLGVITLLPEIIQGIHYGVTGRAIEQGLVKIDCWNPRDWSSRPYKQVDDKPYGGGPGMVMMYEPLHAAIKHARSEMKENCKTIYLSPQGKVVRQNDLKQIAAQKQSLLFVAGRYEGIDERIISHHVDEEWSLGDFVLSGGELAAMVFIDAIIRLIPGSLGHLGSAEQDSFMNGLLDCPHYTRPATINGLDVPDVLLGGNHKEIERWRRKQSLGKTWLKRPDLLEKVQLSETDKQLLAEFKCEHGDSC | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28022
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q72S28 | MKFNFITLFPDKIQSYFSEGLQQKAIESGVFSVNIIQLRNFSGNKHNRVDDTIYGGGPGMLLRVEPIHKAILSLGEEKGIVILTSPSGIPFNQSIAMDLKKGGKPLTFISGYYEGVDHRVTEHLVDMEMSLGNYVLSAGDLASICIADAVSRLLPGFLGADESLLDESHNHPDILEYPQFTKPSEYNGWKVPDVLLSGNHASILAWREQNRKKIERGNYESTFKRSADSGC | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25594
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q8CX44 | MWLGVITLFPEMFRAVTDFGVTGRAVKNGLLELHTWNPRDFTHDRHSTVDDRPYGGGPGMLMMVQPLRDAIHAARAAAGEDAKVIYLSPQGRKLDQQGVTELAKSSRLILVCGRYEGIDERIIQTEVDEEWSVGDYVLSGGELPAMTMIDAVSRLVPGVLGKQASAEQDSFSDGLLDCPHYTRPESLDGLDVPAVLLSGNHEQIRLWRLQQSLGRTLLRRPELLQNLALTDEQSTLLAQFVEAMDKNA | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27451
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q7NFC3 | MIEPVRVIGGGIAGAEAAWQCARAGVPVVLSEMRPVRPSPAHHTDHLGELVCSNSFGAMATDRAPGLLKEELRRLGSLVIAVADAHAVPAGGALAVDRAVYTRELTERVANHPLIELRREEVTEIPAAGLVVFATGPLTSEPLAHGLQALTGLGYLSFFDAASPIVAGESLDTEKVFLASRYDRGEAAYYNCPMSEPEYRAFWEALASAEQAELKEFEHEERKFFEACLPVEELARRGYETLRYGPLKPVGLTDPRTGRWPFACVQLRQEDRAGRLWNLVGFQTNLKWGEQKRVFQMIPGLEQAEFVRLGVMHRNTFLCS... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49166
Sequence Len... |
B4U7L4 | MKVNVIGAGLAGSEAAYFLANKGIKVRMFEMRPITSHFTSRQDEKTGTHDVRNATQTRPITTTEAHKTDKFGELVCSNTLGSFEITTGAGLLKKEMELLNSLVIKAAKHSYVKAGSALAVDRNEFSDFITKTILSHPNIEVVREEVESLNENELNIVATGPLTSEKFSKYLKNLITDDYLYFYDAIAPIVEASSVDFSKGFWGSRYDKGDDYFNCTMTKEEYDIFYNELLKAEKVPTKDFERVVHFEGCLPIEEIASRGYETLVFGPMSPKGLKHHISKDVYAIVQLRKETKEGEALSLVGFQTKLTYKEQVRVFRLIPC... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 51415
Sequence Len... |
Q1IHM1 | MNLKIRIIGAGLAGCEAAWQCARRGLDVELYEMRPVKSTPAHQTSDFAELVCSNSLKSAGENSAPWLLKEEMRRGGSLLLEIAQKTSVPAGHALAVDRGAFAAEVTRVIEAEPRIRVVRGEVTKIDENDALTVIATGPLTSDALSQEIARLSGNTHLYFYDSISPIVEADSIDMSRVYMAARYDKGTADYINCPMNKEEYDRFLDALIEAHSVDAKEWENLNYFEGCLPIEEIARRGRDTLRFGPMKPVGLTDPKTGRYPYAVVQLRQENLRADSYNLVGFQNHLKYGDQARVMRLIPGLENAKFLRYGQIHRNTYINSP... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49565
Sequence Len... |
Q88W23 | MASIPTVNVIGAGLAGSEAAWHIANMGVNVRLYEMRPNKMTPAHHTAQFAELVCTNSLRANQLANAAGLLKAEMRQMDSIVMQAAEHHAVPAGGALAVDRDTFSAEITAAITALPNVEIINEEITSLPDGITVVATGPLTAASLAKSIQAFNDEDDLHFFDAAAPILTKDSIDMDKVYLKSRYDRGEAAYLNCPMTEAEFDVFYDALIHAEMAEAHDFENSDVFEGCMPIEVMAQRGRQTMLFGPLKPVGLEDPKTGKQPFAVVQLRQDDAAGDLYNIVGFQTHLKWGEQKRVFSLIPGLENVEFVRYGVMHRNTFMKSP... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 48261
Sequence Len... |
Q58871 | MIIMISVILVNPKYSGNVGSIARVMMNFGFEELRIVGDKSIINNEAYMMAVHAREILDNAKFYNTFDEAIGDLDFVIATSGARGGDRNLKRVPITPKELADKILEVKGNIGIVFGREDDGLRNEEIDKCDLLVSIPTSEKYPIMNLSHAVAVILYEIYTKKVRNKFLDINMREASKEDKELLIRKFNEFIDKNEKIPEHKKELCKIIFKRLVNRAFISGKEAWTLMSAFK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26280
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q6D257 | MLDNIRIVLVETSHTGNMGSVARAMKTMGLSKLYLVNPLVKPDSQAIALAAGASDVIGNATLVDSLDQALEGCNLVVGTSARSRTLPWPMLEPRECGVRSAQEAEHAPVALVFGRERVGLTNDELQKCHYHVAIPANPEYSSLNLAMAVQIIAYEVRIAHLDRLQAGQPEHEESPYPLVDDLERFYQHLEQTLLQTGFIRPAHQGQVMNKLRRLFTRARPEAQELNILRGILSSVQKTHDE | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26690
Sequence Length: 241
Subcellular ... |
A0A0H2ZF87 | MLDRIRVVLVNTSHPGNIGGAARAMKNMGLSQLVLVQPESFPHGDAVARASGATDILDAARVVDTLEEALSGCSVVLGTSARDRRIPWPLLDPRECATTCLEHLEANGEVALVFGREYAGLTNEELQRCQFHVHIPSDPEFGSLNLAAAVQVLTYEVRMAWLAAQGKPTKMEKFESTSMLNTELVTADELELYYAHLERTLIDIGFLDPEKPRHLMSRLRRLYGRSAISKLEMNILRGILTETQKVARGLSYKRSDD | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32), 2'O-methylated uridine (Um32) or 2'O-methylated adenosine (Am32) at position 32 in tRNA. Confers resistance to oxidative stress.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L... |
Q2NS29 | MLHNIRIVLVETSHTGNIGSTARAMKTMGLSNLYLVNPLHKPDAQAIALSAGASDIIGNASVVDNLDQALAGCSLVVGTSARSRTLPWPMLEPRECGVKSIQEAAQAPVALLFGRERVGLTNDELQKCHFHVQIPANHEYSSLNLAMAVQILAYEVRVAWLDSQRQDATVQEASVYPVAEDLERFYQHLEQVLSGTGFIRRAHPGLVMNKLRRLFNRARPESQELNILRGMLTSIEHTQKPETPAPDTGHGRPQA | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28024
Sequence Length: 255
Subcellular ... |
Q4JB16 | MTIRLVIVEPEGAYNLGFIARLVKNFLIDEFYVVNPKCDINEAIKFSAKGSEVIEKMMKITNNFDDAIRDVDLKIATSSIADIKGDLLRKSIRPIDLERLIKDKKVAFIFGRESVGLTREEIAKSDFLLFIPANPEYPVLNLSHAVGIVLYELWRNRDNKVPTVSSEPIKLIDDYSKKITDILVNKEATKSMYLVLKRVLIKGIEDNEEAMTIVRILRKIYVRLAKKENESDKLL | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA. Is specific for cytidine.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26902
Sequence Length: 235
Subcellular Locatio... |
Q1C5G8 | MLHNIRIVLVETSHTGNMGSTARAMKTMGLTNLYLVNPLVKPDSQAIALSAGASDVIGKATIVDTLDEALAGCSLVVGTSARSRTLPWPMLEPRECGVRSAREAEHAPVALVFGRERVGLTNDELQKCHYHVAIPANPEYSSLNLAMAVQILAYEVRVAYLDRQQANAPVEEEEEAPYPLVDDLERFYQHLEQVLSHSGFIRQAHPGQIMSKLRRLFTRARPEAQELNILRGMLTSIEKQDKYPQRGTGDTAGKSKD | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28385
Sequence Length: 257
Subcellular ... |
Q72IH5 | MWLEATTHPGLEDLLLEELSALYPGEGAEVDARKGRVRIPRAWVGEEALGLRLAHHLVLFRARLLLSREDPLGALERAALALPWPELEGAGSFRVEARREGEHPFTSPEVERRVGEALHRAYGVPVDLKRPAVRVRVDVRGEEAFLGVQLTERPLSRRFPKAALRGSLTPVLAQALLRLADARPGMRVLDPFTGSGTIALEAASTLGPTSPVYAGDLDEKRLGLAREAALASGLSWIRFLRADARHLPRFFPEVDRILANPPHGLRLGRKEGLFHLYWDFLRGALALLPPGGRVALLTLRPALLKRALPPGFALRHARVV... | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe).
Catalytic Activity: guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36980
Se... |
P28634 | MSSFQFEQIGVIRSPYKEKFAVPRQPGLVKSANGELHLIAPYNQADAVRGLEAFSHLWILFVFHQTMEGGWRPTVRPPRLGGNARMGVFATRSTFRPNPIGMSLVELKEVVCHKDSVILKLGSLDLVDGTPVVDIKPYLPFAESLPDASASYAQSAPAAEMAVSFTAEVEKQLLTLEKRYPQLTLFIREVLAQDPRPAYRKGEETGKTYAVWLHDFNVRWRVTDAGFEVFALEPR | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU) that read codons starting with adenosine . The methyl group of m(6)t(6)A37 ... |
P37752 | SFSHIWVQFVFHGVAGAGWQPLVRPPRLGGNRKMGVFATRSPFRPNPLGLSLLKLERIETEGGVRLWCGGADLLDGTPVLDIKPYLPFVEAQPDAAPGFAAVPPVPLEVAWADEISAASLPPPNRLLIEQSIAQDPRPAYQDTPQRVYKMAVDDWEVAFRIEKGMALIEAVMAVEG | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency... |
P44740 | MNDLTLSPIAIIHTPYKEKFSVPRQPNLVEDGVGIVELLPPYNSPEAVRGLEQFSHLWLIFQFDQIQQGKWQPTVRPPRLGGNQRVGVFASRATHRPNPLGLSKVELRQVECINGNIFLHLGAVDLVDGTPIFDIKPYIAYADSEPNAQSSFAQEKLPVKLTVEFTEQAKSAVKKREEKRPHLSRFIRQVLEQDPRPAYQQGKPSDRIYGMSLYEFNVKWRIKAGTVNCVEVIEIEKDK | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency... |
Q9BU70 | MRGLEESGPRPTATPCGCVKPALETGNLLTEPVGYLESCFSAKNGTPRQPSICSYSRACLRIRKRIFNNPEHSLMGLEQFSHVWILFVFHKNGHLSCKAKVQPPRLNGAKTGVFSTRSPHRPNAIGLTLAKLEKVEGGAIYLSGIDMIHGTPVLDIKPYIAEYDSPQNVMEPLADFNLQNNQHTPNTVSQSDSKTDSCDQRQLSGCDEPQPHHSTKRKPKCPEDRTSEENYLTHSDTARIQQAFPMHREIAVDFGLESRRDQSSSVAEEQIGPYCPEKSFSEKGTDKKLERVEGAAVLQGSRAETQPMAPHCPAGRADGA... | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU) . The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA de... |
O32036 | MTDRYEQINDYIEALLKPRPDNVKRLEAYAEEHHVPIMEKAGMEVLLQILSVKQPKKILEIGTAIGYSAIRMALELPSAEIYTIERNEKRHEEAVNNIKEFQLDDRIHVFYGDALELADAVHVTAPYDVIFIDAAKGQYQNFFHLYEPMLSPDGVIITDNVLFKGLVAEDYSKIEPKRRRRLVAKIDEYNHWLMNHPDYQTAIIPVGDGLAISKKKR | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25063
Sequence Length: 217
EC: 2.1.1.-
|
B6YR34 | MNKITTLFQNRQRNIVSIYFTAGFPQLNDTIEIIKELQINGIDMIEVGVPFSDPIADGKVIQASSYKAIQNGMNLKILFKQLEAIKSKIQIPLIIMSYLNPIIQYGFENFCEDCHKIDISGIIIPDLPFEEYINEYKFITDAYDLKMIMLISPKTSEERIRLIDSNVEGFIYMVSSAATTGIQESFDEQKQEYFRRINSMKLRNPRLIGFGISNKETLTVALENASGVIIGSKFVSLLAEENNPKKAVQKLLAELK | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29090
Sequence Length: 256
Pathway: ... |
A1K4B0 | MSKIQTTFQRLQAQGRKALIPFITAGDPDPTLTVPLMHALVAGGADIIELGVPFSDPMADGPTIQRASERALAQGMTLRKVLQAVREFRSGDADTPVVLMGYANPIEAMGQQAFVAAAREAGVDGALVVDYPPEECVEFAAASKAAGLDPIFLLAPTSSEQRFADVARAGSGYIYYVSLKGVTGAGTLDLDEVARRIPQIRAAVGMPVGVGFGIRDAESARRIGAVADAVVIGSRIIEEIERSPREQACSNVTHFVKGIREALDTLPGVKQ | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28616
Sequence Length: 271
Pathway: ... |
Q81GG4 | MGVEKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREVNIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICELIYATKQKEEA | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28332
Sequence Length: 258
Pathway: ... |
Q2S1Z2 | MSRLDETFDALGPDEKAMGLFLTDGFPNPDATVPLLHAIDRGGADFIELGMPFSDPLAEGRPIQRASARALSHGVTLPDTLRTVEAFREDSDTPLLLMGYVNPVFKYGVDAFCRDAAEAGVDGLILPDLPPQESDALCDAAAAHGLELVFLIAPNTSDERIRVVDERATGFVYAVSVTGLTGSDLAETPSVDEYLMHARDFVAQNPLLVGFGIKTHDDAMELSRHTDGFIVGSALINRVEALWEDPERSTTDRLDTVEGFARHLKSGTPVPTPQPNPA | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29956
Sequence Length: 278
Pathway: ... |
Q8ECU9 | MNSISNQTIPHQASRYQAAFSRLKAEGRGAFVPFVTLGDPSPELSLKIIDTLVQNGADALELGFPFSDPLADGPVIQGANLRALAAGTTPTACFELLAKIRAKYPELPIGLLLYANLVFANGIDAFYAKAQQAGVDSVLIADVPVEEAAPFIQAAKAHGIAPIFIAPPNADSDTLAKVSQSGEGYTYLLSRAGVTGADTKAGTPVEEILAKLQEFNAPPPLLGFGIAEPAQVSAAIKAGAAGAISGSAVVKIIETHQQDEVKLLAALGEFTRTMKAAT | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28808
Sequence Length: 278
Pathway: ... |
Q59169 | MTLLNSYFGSFGGMYVPQILMPALYQLESEFVLSLKNLQFKKKLANLLKNYAGRPTPLTLCRNLTKGTNTRIYLKREDLLHGGAHKTNQVLGQALLAKQMKKKEIIAETGAGQHGVAAALSCALLNLKCRIYMGIKDIERQKQNVFRMKLMGAQVIPVKSGNGTLKDACNEALRDWSENYINAHYMLGTAAGPHPYPTIVKQFQSVIGKETKQQIFEKEHCLPNSVIACVGGGSNAIGIFSSFIEDTSVNLIGVEPGGIGIHTEKHGASLICGETGIFFGMKSKVMQTHEGQIKESWSISAGLDFPAVGPEHAWLDSIKR... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43033
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q8ZV44 | MVDRWYNIAADLPSVLAPPRDPDEGESRIGLLSKILPSALIDQEFTAERWVSIPEEVREAYRRVGRPTPLFRAEGLEKALGTGVRIYYKYEGVLPVGSHKLNTALAQAYYAKADGAVEVATETGAGQWGMAVSLAAALFGLRAVVFMTRSSYNSKRQRLTFMRAYGAVVYPSPSDVTEAGRRHYRPDHPGSLGIAISEAVEYVLSGERRKYLPGSVMEFVLLHQTVIGLEAVRQLPEEPDVAVACVGGGSNFAGFTYPMIGMKLRGEGFGRTRFVAVESEAAPKLTRGEYKYDFPDAVGVLPMLKMYTLGHDYVPPAIHA... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 44572
Sequence Length: 410
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q2KE82 | MNETPKPNSFRSGPDEDGRFGIYGGRFVAETLMPLILDLQDEWNKAKSDPAFQAELKHLGAHYIGRPSPLYFAERLTAELGGAKIYFKREELNHTGSHKINNCIGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCVVYMGATDVERQAPNVFRMKLLGAEVKPVTAGSGTLKDAMNEALRDWVTNVEDTYYLIGTAAGPHPYPEMVRDFQSVIGAEAKEQMLAAEGRLPDLVVAAVGGGSNAIGIFHPFLDDSSVKIVGVEAGGKGLQGDEHCASITAGSPGVLHGNRTYLLQDGDGQIKEGHSISAGLDYPG... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. Essential for production of nod factors and establishment of symbiosis.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da)... |
Q7UKG9 | MSTAPSQQHASAQVPDPRGRFGDFGGRFVPETLTRALDELSEEYEKAKRDPEFQRELDGLLKTFVGRPSPLYHAKRLSSAVGGAQIWLKREDLNHTGAHKINNTIGQALLTLRMGKTRVIAETGAGQHGVASATACAHFGLPCTVYMGAEDIRRQKPNVFSMKLLGANISAVESGSRTLRDAVNEAMRDWMSSVEDTHYIIGSVIGPHPFPMMVRDFQSVIGRETREQCRDTFGRLPDCVVACVGGGSNAAGMFYPFVEDEGVRMVGVEAGGRSATPGDHASPLSYGNPGVLHGSYSYVMQDEDGQTCDVHSMSAGLDYP... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 44283
Sequence Length: 407
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q9Y210 | MSQSPAFGPRRGSSPRGAAGAAARRNESQDYLLMDSELGEDGCPQAPLPCYGYYPCFRGSDNRLAHRRQTVLREKGRRLANRGPAYMFSDRSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCVDYMGQNALQLAVANEHLEITELLLKKENLSRVGDALLLAISKGYVRIVEAILSHPAFAEGKRLATSPSQSELQQDDFYAYDEDGTRFSHDVTPIILAAHCQEYEIVHTLLRKGARIERPHDYFCKCNDCNQKQKHDSFSHSRSRINAYKGLASPAYLSLSSEDPVMTALELSNELAVLANIEKEFKNDYKK... | Function: Thought to form a receptor-activated non-selective calcium permeant cation channel . Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of... |
Q9WVC5 | MLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNLQVWSDHHRPSLSRIKLAIKYEVK... | Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium st... |
O28668 | MMDFGFVDSLKGASKRGKNAVIAEVKVRSPIHGDLLRGRRIEDILRAYEKAGAAAISYITAEQFSGNFETLKKIVGLTDLPVLRKDFIRGRKEVERTAEVEAAALLLIARHLKERTAEMVDFCFEHGIEPLVEVHHAEDLVYAENARAVLINNRDIDRMERDGGSIDVTAKIAEKIRAFKVSGSGIGSVEDLLFVLQYVDAALIGTAFMMAENTEEFVQTVCGGEKMIEDVLRGLDFDKAYELAKTLPELDEIKIAAVLAALEAKGYGAEVIAGFAKGVAEKSKIEIGKVMDTCGTGGDKTSSINVSTAVAIALSTVHPV... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Bifunctional enzyme that catalyzes the second and fourth steps of tryptophan biosynthetic pathway. The second step is catalyzed by the anthranilate phosphoribosyltransferase, coded by the TrpD domain and the fourth step is catalyzed by indole-3-glycerol phosphate ... |
A3DDS7 | MILDEIVAQKKIQLKKDMSRITIEGWKQKIKRPGIHKPLDFYGALKNNGDISIIAEVKKASPSKGIIKEDFDPLKIAKEYVESDIQAISVLTERNFFKGDEDYLVKIRQFCPLPILRKDFIIDLWQIYESRYIGADAILLIVSLLSDEELKKFQIVANILGMQCLVEVHDERELERALESGARIIGINNRDLRTFEVDLKNTEKLMNRIPNDRVVVSESGIKDTEDLKYLKELGVDAVLIGETFMRARSISEKIREFKAV | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 29895
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P00911 | MIQIQNTILGKIVDRKHEELADRLKQRNLKDVEQWVKEAPPVRGFAQSLRSKRPGVIAEIKKASPSKGVIRADFNPAEIAQQYEQAGAACLSVLTDVDFFQGADENIAIARQHCSLPALRKDFLIDPYNVVEARALQADCILLIVACLSDQQLEEMSKTAFEYDLDVLVEVHDEQELERALKLSEQCLLGVNNRNLKTFDVDLNTSLRLKKLLDPSRLLVTESGIATPQDVQLMQEHDIHSFLVGESFMKQPRPDQAFTELFGVPKLV | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 30189
Sequence Length: 268
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q8CPB2 | MTILNEIIEYKKTLLERKYYDKKLEILQDNGNVKRRKLIDSLNYDRTLSVIAEIKSKSPSVPQLPQRDLVQQVKDYQKYGANAISILTDEKYFGGSFERLNQLSKITSLPVLCKDFIIDKIQIDVAKRAGASIILLIVNILSDDQLKELYSYAINHNLEVLVEVHTIRELERAHQINPKIIGVNNRDLKRFETDVLHTNKLLKFKKSNCCYISESGIHTKEDVEKIVDSNIDGLLVGEALMKTNDLSQFLPSLKLKKNLYDS | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 30123
Sequence Length: 262
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
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