ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q99578 | MEVENEASCSPGSASGGSREYKVVMLGAGGVGKSAMTMQFISHQFPDYHDPTIEDAYKTQVRIDNEPAYLDILDTAGQAEFTAMREQYMRGGEGFIICYSVTDRQSFQEAAKFKELIFQVRHTYEIPLVLVGNKIDLEQFRQVSTEEGLSLAQEYNCGFFETSAALRFCIDDAFHGLVREIRKKESMPSLMEKKLKRKDSLWKKLKGSLKKKRENMT | Function: Binds and exchanges GTP and GDP. Binds and modulates the activation of POU4F1 as gene expression regulator.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24668
Sequence Length: 217
Subcellular Location: Nucleus
EC: 3.6.5.2
|
P70425 | MEVENEAHCCPGSSSGGSREYKVVMLGAGGVGKSAVTMQFISHQFPDYHDPTIEDAYKTQVRIDNEPAYLDILDTAGQAEFTAMREQYMRGGEGFIICYSVTDRQSFQEAAKFKELIFQVRHTYEIPLVLVGNKIDLEQFRQVSTEEGMNLARDYNCAFFETSAALRFGIDDAFQGLVREIRRKESMLSLVERKLKRKDSLWKKIKASLKKKRENML | Function: Binds and exchanges GTP and GDP. Binds and modulates the activation of POU4F1 as gene expression regulator.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24802
Sequence Length: 217
Subcellular Location: Nucleus
EC: 3.6.5.2
|
P0CV69 | MRGAHYVAIVLLVAAGGQTAAGFDQDEPQHAPDNGYMASVDLRNEFLQSRALQASRNPKDDLMFSAGDEERTPLARSNYLKKVTIPDSIINTANAMRMEGKQVRL | Function: Secreted effector that partially suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 11534
Sequence Length: 105
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellul... |
P0CV70 | MRGAYYVAIAFLVAASSRTAAEFDQAEPQPAINNDILTSGGTVNEMLPKRVLRGSRDLKDKLAVYANDEQRTFDLFPNENNFSKALNPTITKTANVMRADRDDVMAKAAEQ | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 12254
Sequence Length: 111
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P83731 | MKVELCSFSGYKIYPGHGRRYARTDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEIQKKRTRRAVKFQRAITGASLADIMAKRNQKPEVRKAQREQAIRAAKEAKKAKQASKKTAMAAAKAPTKAAPKQKIVKPVKVSAPRVGGKR | Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
PTM: Mono-ADP-ribosylation at Glu-4 by PARP16 inhibits polysome assembly and mRNA loading, thereby inhibiting protein translation.
Sequence Mass (Da): 17779
Sequen... |
A0A1C9J6A7 | MSSCINPSTLATSVNGFKCLPLATNRAAIRIMAKNKPVQCLVSTKYDNLTVDRRSANYQPSIWDHDFLQSLNSNYTDETYKRRAEELKGKVKTAIKDVTEPLDQLELIDNLQRLGLAYHFEPEIRNILRNIHNHNKDYNWRKENLYATSLEFRLLRQHGYPVSQEVFSGFKDDKVGFICDDFKGILSLHEASYYSLEGESIMEEAWQFTSKHLKEMMITSNSKEEDVFVAEQAKRALELPLHWKAPMLEARWFIHVYEKREDKNHLLLELAKLEFNTLQAIYQEELKDISGWWKDTGLGEKLSFARNRLVASFLWSMGIA... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit . The best cofactor is Mn(2+) . No effect with monovalent cations .
Function: Catalyzes the conversion of geranyl diphosphate to (+)-(4R)-limonene . Produces exclusively the (+)-enantiomer . Can use neryl diphosphate as substrate . Has no activity with farnesyl diphos... |
O45962 | MAPTGQGGQWQEVLCCSICNRHFNETFLPVSLICGHVICRKCAEKPENQTKPCPHDDWKTTHSPSEYPNNVALLSVIFPRKQCMTLSGAVSEAEKRVDQLSIQIAKFFREADSERGGTVSSREISRTLQRKVLALLCYQWREVDGRLKTLKMCRGISERVMIEIILSIQSNTHVSSQLWSAVRARGCQFLGPAMQDDVLRLILMTLETGECIARKNLVMYVVQTLASDYPQVSKTCVGHVVQLLYRASCFNVLKRDGESSLMQLKEEFRTYESLRREHDSQIVQIAFESGLRIGPDQWSALLYADQSHRSHMQSIIDKLQ... | Function: E3 ubiquitin-protein ligase. Regulates the activity of daf-16 and is thereby involved in regulating aging and stress resistance . Regulates nsy-1 activity and thereby attenuates the activation of sek-1 and pmk-1, two components of the p38 pathway, which results in susceptibility to pathogenic bacterial infect... |
Q9T1W9 | MDLISVLALWPYLLPVVAGGAVWAMRRSFASTERVERLENRMTEMETRYASIPGTEDVHEMRLRIAELSGDIRVLSQRVQSFSHQLELLLENAVNRSNS | Function: Facilitates the release of the SAR-endolysin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 11316
Sequence Length: 99
Subcellular Location: Host cell inner membrane
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O49320 | MMNNMKLLIIAVMIISAALLPALVVGSRPVKCDNCMDGGEKEEIMKMSSGVDVSHRILQAKRFIDYEALKKNLPAKPDGKPDKPDNKYRRGCSAATGCYRFTN | Function: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant act... |
Q6NME6 | MGIKILLILGLLTLAVVAESANATWTLTKSCVNGQGCIGEDGELDYLMDSETNRRQLAARRSYISYGALRKNNVPCSRRGRSYYDCKKRKRANPYRRGCSVITHCYRQTS | Function: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant act... |
Q9SRY3 | MDKSFTLFLTLTILVVFIISSPPVQAGFANDLGGVAWATTGDNGSGCHGSIAECIGAEEEEMDSEINRRILATTKYISYQSLKRNSVPCSRRGASYYNCQNGAQANPYSRGCSKIARCRS | Function: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant act... |
A3QB25 | MKCAYFDANQCLSCRHLKTPLSDQVAAKTATLAALLKDLSVEQWLPPVVGPESGFRNKAKMVVLGAAHQPILGLVSPSGEAVSLCDCSLYPQDMQQLLHRLEAFVRQAGIPPYRVDKAKGELKFILLTRSQVRGEYMLRFVMRSEQAIPRIERELPRLLAEHPEIKVVSVNLQPVHMAILEGEEEIFLTEATRLEEEFNGVPLYIRPKSFFQTHPEVAAKLYLSARKWTRELAPTSIWDLFCGVGGFGLHCASKEVALTGIEIEAEAIACAKMSAETLGLDKVRFTALDSTSFASDSRGEEKPELIIVNPPRRGIGEALC... | Function: Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42218
Sequence Length: 379
EC: 2.1.1.189
|
A1W8H0 | MKAQTKSKKVNKAWLHDHVNDTYVKLAQKEGYRARAAYKLKEIDEQLGLIKPGHVVVDLGSSPGAWSQYVRRRLSPDGAAVGQLNGVIIALDILPMEPIEGVTFLQGDFREEEVLAGLQEAVQARPVDVVVSDMAPNLSGVESVDAVRIAHLIELAVDFAVHHLKPEGALVVKLFHGSGYSQLVQLFKDTFRVVKPMKPKASRDKSSETFLVGMGLKRQG | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
A5UKI5 | MGSRWQMEKKHDPYYKKAKKEDYRSRASYKIKQLDKKFKLIKEGDTVVDLGAAPGGWSQVALEKVGEEGLVIGVDLNRIKPFPEENFHGIRGDFTTTEVQEKVMNLIGGKAKVVISDASPSLCGIKNIDQLRSIDLTNTVIGIADNILEPKGNLVMKVFQGPEYKDMLTRLKKKYRQVKTTKPPSSRKKSSEMYVVGLDFKPKKNKKSKD | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
Q1D841 | MLGSPPDMGKPYRPKDHYFQKAKQEGLRARSAFKVDELIKRFPMVKKGHVVLDLGAAPGGFLQILADAVGPKGRVIGVDIVAIRPFSQPFVQTAVLDVLADDFDAKLTELHAGPFDAVISDMAPKTSGIKATDEARSLRLAGKALELAAARGRPGSSFVAKVFMGRDFEDFRNQIRALFEEVKVVRPEATRGASMEVYLVGLRRRAPEAPEAN | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
Q2GDL7 | MKNKLHRVGRCTASSSRWLYRHVNDPFVKKAKAEQYRSRAAYKLLEIDEKFNLIRKGFVVLELGSAPGGWSQVIADILNGTGRLIAVDLADMDPISGVEVVKLDIELQRKELYEYISGVELDVIVSDLAPSASGSRVTDSISSIRLAELVLHYAKNSLKKFGTVVTKILRGSEDEYRFVNSLRKQFKKIEYFKPDASRKASREIYLILLGKLS | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
Q8D2X0 | MKNMCSNWWLSEHYSDKFVKESKKCKYRSRAWFKIDEIQKKNNIIKPGMVVLDIGSSPGGWSKYSSQKVGMSGKVIACDIDLMNPIPNVSFILGNIFEKITIKKIKKVKKKVHIILCDISPNITGLSIIDHSRWISLNNNILNICKYLLLKNGKLIIKSFNSVEIKNFCKKIENSFKKIKIFKPISSRSRSKEIYIVAVNYKL | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
Q73IS9 | MNDQYVQKTSKDGYRSRSAYKLVEMDNKFKLFQEGQKIIDLGASPGGWSQVASQKGANVVALDIKPMNAINGVEFIQCDIINEFEILREKFKDQKFDVILSDMAPESCGLKSLDHIRIMLLCEAALNFAKHFLSHGGTFVVKIFQGESDKDFCNELKKMFKTVKYFKPKSSRSESTEMYLVSLGFIGSKPSI | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
Q4UTQ4 | MPSRSKSSQRWLKEHFADPFVKKAQAEGMRSRAAYKLEELLQRDRLLKPGMVVVDLGAAPGGWSQQVRKSMGASGRVVALDILEMPPLAGVEFLHGDFREQAVLSEFEAMLGDVPVDLVLSDMAPNKSGMDAVDQPRMMHLAELAMEFADTHLKVGGAFLIKLFQGVGSDDYIRELRRRYEKVTIRKPAASRKRSAEVYVLGQGKRAQIK | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da)... |
A8GJW6 | MSQLDLGTQQLELERYPQQEESTQLQAWEAADEYLLQQLENVNIGDRPVLIFNDNFGTLACALHSHQPYSISDSYMSQLATRHNLKLNELDPQQVTLLDTLAELPASPAVVLIRIPKALALLEQQLRALRDVVAPDTVIIAGAKARDVHTSTMQLFEKVLGPTRTSLAWKKARLIHCEVADIVPPAAPVTTNWVLDGTDWVIHNHANVFSRSNLDIGARLFLDHLPHDIEGHIIDLGCGNGVIGMAALMQNPQAQVSFVDESYMAVASSELNVEHNLPQDMDRCQFEVNNSLAGIERESVQAVLCNPPFHQQHAITDHTA... | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42282
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 2... |
B1KD54 | MTTQFSVAGIELELARYPKDQESNLQAWDAADEHLIKHLIETEQTPVVTAIINDNFGALTACLRSIAPTWPLMVETDAKTSLLGNLQNLATNNLSSEGIEWLNSREALPEQIELVLMKLPKNLTYFAHQLNRLSQVLPKGTQVLISAKAKSINKSVLELIGKNLGSASASLTWKKTRVITCISDGEIRSLPKEMQWSVPRLNLEIRNLSNVFAANKLDIGAEIMLENMPKGDFKSIIDLGCGNGILGLHAKQLFPQAYIHFVDDSEMAIESAKQNWALNKLDTQGLVGEQATFGWDDCLTHMSEGVRPDLVLCNPPFHQG... | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46575
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2... |
Q899K8 | MNITIISVGKLKEKYLKLAVEEYSKRLSRYCKLNIIEVTDEKTPDNASEKEELQIKEKEGDLILKNIKDNMFVIALDLNGNELTSIDFSNFINDLGIKGESNLTFVIGGSLGLSSKVLSRSNYKLCFSKMTFPHQLFRVMLLEQIYRGYRIMNGEPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18278
Sequence Length: 159
Subcellular Location:... |
B5Y9X7 | MKVHIVAVGKLKNGYVAEGVKDYYERIKHYIPITMVETKQENPFNMTTKEGFHIVLDAQGKLMTSEEFASFIEDLLTTQSNDVYFYIGGPEGFSEAFKNNAQMRISLSLMTFPHELARLFFLEQLYRALTIIKGEKYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16081
Sequence Length: 139
Subcellular Location:... |
B6J870 | MKINVVAVGKRLPAWIKAGFQSYADRLPRDFDLNLIEIAAFKRSKGADLKKIMLQESQQLIDAVPKESEIIVLDRLGEEVDTPTLAQKLSQWRHENRSISLLIGGPEGLSATCIDKARWVWSLSALTLPHALARVIVAEQIYRAWSIITNHPYHR | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17536
Sequence Length: 155
Subcellular Location:... |
Q0KD64 | MQLVIVAVGHKMPGWIETGFSEYAKRMPPELRIELREVKPETRSSSNNAATVMQREAARIEAVLGSLSKQCRIVALDERGRDFTTVQLAAQLTDWQREGGDVAFLIGGADGLDPALKARASTLIRLSSLTLPHGMVRVLLAEQLYRAWSVTQNHPYHRA | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17663
Sequence Length: 159
Subcellular Location:... |
Q11RC7 | MKLQLWTIGKTNDAYLKEGCAQYTKRLPHYLPFEYLEIPEPKNTKLSSDVLKKEEEKLIFDRLQDSDQLILLDEKGNEFTSTEFGQYIQKKMNSVAGNLIFLIGGPYGFSDAVYKRANGKIALSKMTFSHQMVRLFALEQLYRACTIIKGEKYHH | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17963
Sequence Length: 155
Subcellular Location:... |
Q9RWP7 | MRLHLITVGEPKLAYARSGWDEYEKRLRRYHKVQVSRVSGKTQQAESEAILKAAGKSPLILLDPRGKQFSSEKLSEYLDAEALGGHGELAFAIGGPDGHTDALRGQAKLLWSLGELTLPHDLAMLVLVEALYRAATISAGEPYHRG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16018
Sequence Length: 146
Subcellular Location:... |
Q2YC51 | MKFLVYAVGHKMPEWIAAGFQEYAKRMPREANIELLEIKPERRDSGKKVEQLLAAEGARIRALLPSNCRLVVMDERGSQWTTAGLAHAIGSWMKDGGDTAFLIGGADGLDPALRNAADEVLALSALTLPHGLVRILLAEQLYRAISLIKGHPYHRA | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17154
Sequence Length: 156
Subcellular Location:... |
Q04HG9 | MLNIRILVVGKIKEKYFRNALDQYLKRLSRFTKIEIIEVKDEATPEKASKSENLEILQTEGGRLLDKINNRDFVIALAIEGKLITSPDLADMIREIPLDGYSTIDFVIGGSLGLSNEIKNRANAKISFGRITLPHQLARVLLTEQIYRSFMINEGSPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18190
Sequence Length: 160
Subcellular Location:... |
A6LDQ1 | MKIGLIVIGKTDAGYFVEAINEYKNRLTHYIPFEMEVIPDIKNVKNLSEAQQKEKEGELILKALQPGDYLVLLDEKGKEFTSMQFSTYLEKKMHTVPKRLVFVVGGPYGFSEAVYKAASEKISLSKMTFSHQMIRLIFIEQIYRAMTILNNEPYHHE | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18152
Sequence Length: 157
Subcellular Location:... |
Q6MAG7 | MLKLRILSVGKTKEKWLEDAFNEYQKRLKANLQIECLWAKDSYQLLEWTQKESLIICLDPTGRLLTSEAFATFFSKCWEQGGSRLTIVIGGAEGLPLELKQHSILISLSLLTFTHQITRLILIEQIYRATEILKNSQYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16227
Sequence Length: 140
Subcellular Location:... |
A4VYG8 | MKIKLITVGKLKEKYLKEGIAEYSKRLGRFTKLDMIELPDEKTPDKASQAENEQILKKEADRIMSKIGERDFVIALAIEGKQFPSEEFSQRISDIAVNGYSDITFIIGGSLGLDSCIKKRANLLMSFGQLTLPHQLMKLVLIEQIYRAFMIQQGSPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18097
Sequence Length: 159
Subcellular Location:... |
A0Q621 | MQKFTFFVSCAKGIELLLKDELERLGISSQEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINWMDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVTNQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHKRSYRQFQGQAPLKESLAAAILIKAGWLEELKKHQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEFKIFNSKFHNKELWDNLLEIAKNSQKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPPYGERLYGDQ... | Function: Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
Catalytic Activity: guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 83680
Sequence Length... |
Q7VP04 | MSNQITYFATAARGFEEMLKIELEQICGADGKVVQGGVHFTTNQKGAYQALLHSRLASRILLPLVSTKIFSDLDLYATIIAINWADIFDPRDTFYVDFNGTNREIRNTQFGAMRVKDGIVDYFERKRFARPIVDKDRPDIRIHVYLDREKLIVSLDLSGEALHMRGYREDTGKAPLRETLAAIIVLRSGWQKGTPLVDPMCGSGTLLIEAAQMQAGIVPQLQRKYWGFNAWKGHQQAIWQQVLEEAHSQKNTQIDPLFYGFDLDHRVLAKAKQNAQNAGVAHLIHWQQADIAALKNPCLDQKGTLVSNPPYGERLGTTPA... | Function: Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
Catalytic Activity: guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 81310
Sequence Length... |
O34617 | MAELNKTKVRKELRTERPSIYSFELDEIKQWLTDNGEKPFRAAQIFEWLYEKRVSSFEDMTNLSKDLREKLNTRFVLTTLKTAVKQTSQDGTMKFLFELHDGYTIETVLMRHEYGNSVCVTTQVGCRIGCTFCASTLGGLKRNLEAGEIVAQVVKVQKALDETDERVSSVVIMGIGEPFDNFNEMLAFLKIINHDKGLNIGARHITVSTSGIIPKIYEFADQQMQINFAISLHAPNTEIRSRLMPINRAYKLPDLMEAVKYYINKTGRRISFEYGLFGGVNDQVEHAEELADLLEGVKCHVNLIPVNYVPERDYVRTPRD... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q89ZK5 | MMSKYPLLGMTLIELQSLVKRLGMPGFAAKQIASWLYDKKVTSIDEMTNLSLKYRELLKQNYEVGAEAPVEEMRSVDGTVKYLYPVGENHFVESVYIPDDERATLCISSQVGCKMNCKFCMTGKQGYSANLTAHQIINQIHSLPERDKLTNVVMMGMGEPLDNLEEVLKALDILTGSYGYAWSPKRITVSTVGLRKGLRRFIEESDCHLAISLHSPVTAQRAELMPAEKAFSITEMVELLKNYDFSKQRRLSFEYIVFKGLNDSQVYAKELLKLLRGLDCRMNLIRFHSIPGVALEGADMDTMTRFRDYLTTHGLFTTIR... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q6MPV7 | MEANAGSTLAPVNYSDDNVAKPLENQPVNFYSLTLEDLKAYIKSKGKEQFRAQQIFKWVYEQRVTDPEQMTNLSKEFRQDLPSMLSFDLPPVLQHLKSVDGTQKFLFDMKDGMSVEAVVIPSEDRLTLCISSEVGCNMACKFCFTGKQKLKRRLRTEDIVGQFMQVHDRLAEGQRITNIVFMGMGEPLDNPEAVFKTIDVIHSPWGINLSRKKITVSTSGIVPEMWRVADAKVRLAVSLNGPNDEIRSQVMPINKRWDTKALLEACKEHYRVSKDKITFEYVLLKGITDQLEHARQLVKLVKDVPCKINIIPFNEHPGSG... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
Q8G481 | MTTQHPDTPETGITPGGTSGAFRDVLSKDHARRGKPPLHFVDMTPEQRVEKAAELGLPKFRVKQLANHYFGHFDVNAAEFTDFPAAKRSEAAAAFFPQLITEVTRQVADEGTTIKTLWKLFDGSLIESVLMRYPTRTTLCISSQVGCGMDCPFCATGKLGLTRNMSTGEIIEQVRVAAKMMRDGEVAGGEGRLSNIVFMGMGEPMGNYNSVLSAVRQISAMPPEGFGISARNITVSTVGVVPGIKKLTAEGIPVRLAVSLHAPSDELRDELVPMNKRFNTKQVLDAAHDYWLASKRRVSIEYALMRGINDQAEHAQLLAK... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q1IRD1 | MERLGQPAYRSRQLWQGLYRDRIASLDQFTTLPIPLREELKSSGWAIAFPFVQKRFTSTDGTVRYLLQFSDGQSVETVWMPEGDGGEQGDGSEDGPSYDRATICVSSQVGCAVDCQFCMTALLGLLRNLSAGEIVGQILAVLKDENVDVEKSRINLVFMGQGEPFLNFDNFVKAVTLLAEAVGIPESRMTVSTSGIVPRIVDFGQLAIRPKLAISLNASNDESRRELMPITKKWTLEKLMSAAREFPLRNRERMTFEYVLLGGVNDSEQNAREVVQLLRGLRAKVNLIAWNPGPEIPFSTPDPQHVEAFQQILIDAGIPT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
C4Z523 | MTDIKSLNYDELVTYMAGLGEKKFRAGQLYQWMHEKLADSFDECTNLSNALRQKLKETSEYVCLEPVRVQHSKLDGTEKYLFRLSDGNYVESVLMKYHHGNSVCISSQVGCRMGCRFCASTLNGKVRDLRPSEMLDQIYRIQKITGERVSNVVVMGSGEPMDNYDNLIKFIELLNDERGLNISQRNITVSSCGIVPKLKELADLKLQITLAISLHAPNDELRKTMMPIANKYSIEEIMDVCRYYIECTGRRISFEYSLVKGVNDSMECAKQLIELVKGMNCHINLIPVNPIKERDYKQTGKEEVYAFKNKLEKNGINVTI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
O86754 | MPKPGELTFVAPRGVKKPPRHLADLTPAERKEAVAAIGEKPFRAKQLSQHYFARYAHAPEQWTDIPAGSREGLREALLPELMTVVRHLSTDQGTTRKTLWKLFDGTLVESVLMRYPDRVTMCISSQAGCGMNCPFCATGQAGLDRNLSTAEIVHQIVDGMRALRDGEVPGGPARLSNIVFMGMGEPLANYNRVVGAIRRLTDPEPDGLGLSQRGITVSTVGLVPAIHRFTGEGFKCRLAISLHAPDDELRDTLVPVNTRWKVREVLDAGFEYAAKSGRRLSIEYALIRDINDQAWRGDRLGRLLRGRPVHVNLIPLNPTP... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q9MA83 | MIPSQSNSFSGSVITLYFFLLGSLVLRTLASSRLHYCRHDQRDALLEFKHEFPVSESKPSPSLSSWNKTSDCCFWEGVTCDDESGEVVSLDLSYVLLNNSLKPTSGLFKLQQLQNLTLSDCHLYGEVTSSLGNLSRLTHLDLSSNQLTGEVLASVSKLNQLRDLLLSENSFSGNIPTSFTNLTKLSSLDISSNQFTLENFSFILPNLTSLSSLNVASNHFKSTLPSDMSGLHNLKYFDVRENSFVGTFPTSLFTIPSLQIVYLEGNQFMGPIKFGNISSSSRLWDLNLADNKFDGPIPEYISEIHSLIVLDLSHNNLVGP... | Function: Receptor for microbe-associated molecular patterns (MAMPs) that induces a BAK1-dependent basal immune response to necrotrophic fungi (e.g. S.sclerotiorum) in the presence of MAMPs (e.g. flg22 and SCLEROTINIA CULTURE FILTRATE ELICITOR1 (SCFE1) from the necrotrophic fungal pathogen S. sclerotiorum). Functionali... |
Q9SHI4 | MTNEGRFKAKGFVRTSSTTRPIQALSFHMIGILLQCVLFISVLSIAVSEALCNSQDRESLLWFSGNVSSSVSPLNWNPSIDCCSWEGITCDDSPDSHITAISLPFRALYGKLPLSVLRLHHLSQLNLSHNRLSGHLPSGFLSALDQLKVLDLSYNSLDGELPVEQTFRNGSNRCFPIRIVDLSSNFLQGEILPSSIFMQGTFDLISFNVSKNSFTGSIPSFMCKSSPQLSKLDFSYNDFTGNIPQGLGRCLKLSVLQAGFNNISGEIPSDIYNLSELEQLFLPVNHLSGKINDDITHLTKLKSLELYSNHLGGEIPMDIG... | Function: Involved in the perception of CLV3 and CLV3-like peptides, that act as extracellular signals regulating meristems maintenance (By similarity). Contributes, with WAKL22/RFO1, to resistance to F.oxysporum (f.) matthioli in cv. Columbia relative to cv. Ty-0 .
Location Topology: Single-pass type I membrane protei... |
Q9LJS0 | MSKSLLRLTFLLLLLLSCVSPSSFFTFNNPAEGPGACGPHQIQAFTQFKNEFDTRACNHSDPWNGVWCDNSTGAVTMLQLRACLSGTLKPNSSLFQFHHLRSLLLPHNNFTSSSISSKFGMLNNLEVLSLSSSGFLAQVPFSFSNLSMLSALDLSKNELTGSLSFVRNLRKLRVLDVSYNHFSGILNPNSSLFELHHLIYLNLRYNNFTSSSLPYEFGNLNKLEVLDVSSNSFFGQVPPTISNLTQLTELYLPLNDFTGSLPLVQNLTKLSILHLFGNHFSGTIPSSLFTMPFLSSIYLNKNNLSGSIEVPNSSSSSRLE... | Function: Recognizes fungal (e.g. B.cinerea and A.niger) endopolygalacturonases (PGs, e.g. BcPG3, BcPG2, BcPG4, BcPG6 and AnPGB) and acts as a microbe-associated molecular pattern (MAMP) receptor to mediate defense response against fungi (e.g. B.cinerea) and oomycetes (e.g. H.arabidopsidis). Functionality seems to depe... |
A3LZU7 | MTGLLNGKVVAITGGVTGIGRAIAIEMARNGAKVVVNHLPSEEQAQLAKELKEEISDGENNVLTIPGDISLPETGRRIVELAVEKFGEINVFVSNAGVCGFREFLEITPETLFQTVNINLNGAFFAIQAAAQQMVKQGKGGSIIGISSISALVGGAHQTHYTPTKAGILSLMQSTACALGKYGIRCNAILPGTISTALNEEDLKDPEKRKYMEGRIPLGRVGDPKDIAGPAIFLASDMSNYVNGAQLLVDGGLFVNLQ | Function: NAD-dependent dehydrogenase that has high activity with L-rhamnose and L-lyxose, and shows only low activity with L-mannose. Has no activity with NADP. Catalyzes the first step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.
Catalytic Activity: L-rhamnofu... |
P0C7J0 | MATWLVTGRAGFIGGNFVLEAVSRGIRVVNLDALTYAGNLNTLASLEGNADHIFVKGDIGDGALVTRLLQEHQPDAVLNFAAESHVDRSIEGPGAFIQTNVVGTLALLEAVRDYWKALPDTRRDAFRFLHVSTDEVYGTLGETGKFTETTPYAPNSPYSASKAASDHLVRAFHHTYGLPVLTTNCSNNYGPYHFPEKLIPLVIAKALAGEPLPVYGDGKQVRDWLFVSDHCEAIRTVLAKGRVGETYNVGGNSERQNIEVVQAICALLDQHRPREDGKPRESQIAYVTDRPGHDRRYAIDASKLKDELGWEPAYTFEQGI... | Cofactor: Binds 1 NAD(+) per subunit.
Function: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.
Catalytic Activity: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
Sequence Mass (Da): 38672
Se... |
Q9LQ04 | MVADANGSSSSSFNFLIYGKTGWIGGLLGKLCEAQGITYTYGSGRLQDRQSIVADIESVKPSHVFNAAGVTGRPNVDWCESHKVETIRTNVAGTLTLADICREKGLVLINYATGCIFEYDSGHPLGSGIGFKEEDTPNFTGSFYSKTKAMVEELLKNYENVCTLRVRMPISSDLTNPRNFITKIARYEKVVDIPNSMTILDELLPISIEMAKRNLTGIYNFTNPGVVSHNEILEMYRDYIDPSFTWKNFTLEEQAKVIVAPRSNNELDATKLKTEFPELMSIKESLIKFVFEPNKKTEVKA | Function: Bifunctional enzyme involved in dTDP-beta-L-rhamnose biosynthesis. Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-4-keto-alpha-D-glucose to form dTDP-4-keto-beta-L-rhamnose and its reduction to yield dTDP-beta-L-rhamnose. Can form UDP-beta-L-rhamnose from UDP-6-deoxy-4-keto-alpha-D-gl... |
P37745 | MNVIRTEIEDVLILEPRVFGDDRGFFYESFNQSAFEHILGYPVSFVQDNHSRSSKNVLRGLHFQRGEYAQDKLVRCTHGAVFDVAVDIRPNSVSFGKWVGVLLSADNKQQLWIPKGFAHGFLVLSDIAEFQYKTTNYYHPESDCGICWNDERIAIDWPQTSGLILSPKDERLFTLDELIRLKLIA | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 21270
Sequence Length: 185
Pathway: Carbohydrate biosynthesis; dTDP... |
O27818 | MAEFRFIKTSLDGAIIIEPEVYTDERGYFMETFNEAIFQENGLEVRFVQDNESMSVRGVLRGLHFQREKPQGKLVRVIRGEIFDVAVDLRKNSDTYGEWTGVRLSDENRREFFIPEGFAHGFLALSDECIVNYKCTELYHPEYDSGIPWDDPDIGIDWPLEMVDDLIISEKDRNWKPLRENPVYL | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 21678
Sequence Length: 185
Pathway: Carbohydrate biosynthesis; dTDP... |
A0QSK5 | MTARELSIAGAWEITPVLRTDSRGLFFEWFTDAGFTEFAGHQFDMRQANCSVSARGVLRGVHFAQVPPSQAKYVTCVRGAVFDVVVDIRVGSPTFGQWDAVLLDDKDRRSIYISEGLGHAFLALDDDSTVMYLCSAPYAPQREHTVRPTDFGIEWPEVPELILSDRDAQAPSLAEAQAAGVLPTWADCQAFVETLRRNLVS | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region ... |
P9WH10 | MKARELDVPGAWEITPTIHVDSRGLFFEWLTDHGFRAFAGHSLDVRQVNCSVSSAGVLRGLHFAQLPPSQAKYVTCVSGSVFDVVVDIREGSPTFGRWDSVLLDDQDRRTIYVSEGLAHGFLALQDNSTVMYLCSAEYNPQREHTICATDPTLAVDWPLVDGAAPSLSDRDAAAPSFEDVRASGLLPRWEQTQRFIGEMRGT | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region ... |
P37763 | MDIIDTALPDVKLLKPQVFTDGRGFFMETFRDGWFKENIADRTFVQENHSNSSKGVLRGLHYQTENTQGKLVRVVVGEVFDVAVDMREGSPTFGKWAGATLSAQNRYQLWIPEGFAHGFCVLGDAAEVVYKCTDYYNPETEQVLIWNDPAIGIGWPLQTAPLLSPKDLAGKTWAQAEKSALRFPDKKCRPNVSDGIFSDRLPTRLQYALCKEKHPGNEERQAQPRSGGIPVLQIQRERRIRAAVGHREGNNKRHNYTNQAFTDNQACREKRTDTVGVFQTAFAVFRLLANDVFQHRRQHRACHDGHIDGRRQINAHTDRK... | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 37209
Sequence Length: 328
Pathway: Carbohydrate biosynthesis; dTDP... |
Q9HU21 | MKATRLAIPDVILFEPRVFGDDRGFFFESYNQRAFEEACGHPVSFVQDNHSRSARGVLRGLHYQIRQAQGKLVRATLGEVFDVAVDLRRGSPTFGQWVGERLSAENKRQMWIPAGFAHGFVVLSEYAEFLYKTTDFWAPEHERCIVWNDPELKIDWPLQDAPLLSEKDRQGKAFADADCFP | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 20766
Sequence Length: 181
Pathway: Carbohydrate biosynthesis; dTDP... |
P26394 | MMIVIKTAIPDVLILEPKVFGDERGFFFESYNQQTFEELIGRKVTFVQDNHSKSKKNVLRGLHFQRGENAQGKLVRCAVGEVFDVAVDIRKESPTFGQWVGVNLSAENKRQLWIPEGFAHGFVTLSEYAEFLYKATNYYSPSSEGSILWNDEAIGIEWPFSQLPELSAKDAAAPLLDQALLTE | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 20663
Sequence Length: 183
Pathway: Carbohydrate biosynthesis; dTDP... |
P37780 | MNVIKTEIPDVLIFEPKVFGDERGFFMESFNQKVFEEAVGRKVEFVQDNHSKSTKGVLRGLHYQLEPYAQGKLVRCVVGEVFDVAVDIRKSSPTFGKWVGVNLSAENKRQLWIPEGFAHGFCVLSDEAEFVYKTNNFYSKMQERGILWSDKSINIEWPVQNPLLSDKDINGQKFVDADYFI | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 20823
Sequence Length: 181
Pathway: Carbohydrate biosynthesis; dTDP... |
P55468 | MGGTELDEMYFQSLSIAEVKLIRPRKFGDCRGYFSEVFREKWFRKNVADVGLVQDNESLSAQIGTVRGLHFQLEPFAQGKLVRCTRGALFDVAVDVRVGSPTYGKWVSAELSQENGAQLWVPAGFAHGFMTLKADTVISYKVTAPYSAEHDRGLKWDDPAIGINWPKMTTYVLSEKDSSQPSLCELPVSFQYVKV | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 21852
Sequence Length: 195
Pathway: Carbohydrate biosynthesis; dTDP... |
P29783 | MRPLSVQGAWLSETRAFADDRGEFQELYSARSLRGALGYDPGVAQVNRSVSRRGVLRGVHFAQLPPSQAKYVTCLSGAVLDVVVDIRTGSPTYRAWEAVRLDDPHRSLYVEAGLGHSFMALTDDAVVVYLTSQGYAAGREHGVHPLDPDLGIAWPDGIEPVLSEKDRQAPGIAEMERRGLLPDYEECLAFRRSLCERGTG | Function: Involved in the biosynthesis of the dihydrostreptose moiety of streptomycin . Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose (By similarity).
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rh... |
O66251 | MARLLITGAGGQLGRSLAKLLVDNGRYEVLALDFSELDITNKDMVFSIIDSFKPNVIINAAAYTSVDQAELEVSSAYSVNVRGVQYLAEAAIRHNSAILHVSTDYVFDGYKSGKYKETDIIHPLCVYGKSKAEGERLLLTLSPKSIILRTSWTFGEYGNNFVKTMLRLAKNRDILGVVADQIGGPTYSGDIASVLIQIAEKIIVGETVKYGIYHFTGEPCVSWYDFAIAIFDEAVAQKVLENVPLVNAITTADYPTLAKRPANSCLDLTKIQQAFGIQPSDWQRALKNIRAYAE | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-bet... |
Q2SYI1 | MKILVTGANGQVGWELARSLAVLGQVVPLARDEADLGRPETLARIVEDAKPDVVVNAAAYTAVDAAESDGAAAKVVNGEAVGVLAAATKRVGGLFVHYSTDYVFDGTKSSPYIETDPTCPVNAYGASKLLGELAVAETGGDWLTFRTTWVFAARGKNFLRTMLRLAKEREEMKIVADQFGAPTWARSIADGTAHALATAMRERAAGAFTSGVYHMTSAGQTSWHGFADAIVASWRAVPGAAPLAVSRIVPIPTSAYPVPARRPANSVLSNEALKERFGIELPDWRYAVGLCVRDLLSQ | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-bet... |
P37760 | MNILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLINATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNNFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPLALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS) (Probable). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity). RmlD uses NADH and NADPH nearly equally well... |
A0QTF8 | MDLINGMGTSPGYWRTPREPGNDHRRARLDVMAQRIVITGAGGMVGRVLADQAAAKGHTVLALTSSQCDITDEDAVRRFVANGDVVINCAAYTQVDKAEDEPERAHAVNAVGPGNLAKACAAVDAGLIHISTDYVFGAVDRDTPYEVDDETGPVNIYGRTKLAGEQAVLAAKPDAYVVRTAWVYRGGDGSDFVATMRRLAAGDGAIDVVADQVGSPTYTGDLVGALLQIVDGGVEPGILHAANAGVASRFDQARATFEAVGADPERVRPCGSDRHPRPAPRPSYTVLSSQRSAQAGLTPLRDWREALQDAVAAVVGATTD... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage . Catalyzes the reductio... |
P9WH08 | MAGRSERLVITGAGGQLGSHLTAQAAREGRDMLALTSSQWDITDPAAAERIIRHGDVVINCAAYTDVDGAESNEAVAYAVNATGPQHLARACARVGARLIHVSTDYVFDGDFGGAEPRPYEPTDETAPQGVYARSKLAGEQAVLAAFPEAAVVRTAWVYTGGTGKDFVAVMRRLAAGHGRVDVVDDQTGSPTYVADLAEALLALADAGVRGRVLHAANEGVVSRFGQARAVFEECGADPQRVRPVSSAQFPRPAPRSSYSALSSRQWALAGLTPLRHWRSALATALAAPANSTSIDRRLPSTRD | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage (By similarity). Catalyz... |
Q9VE61 | MSDYFEELGHEPTGPLGANDLARNLKRLQVLAIMNGIDMEIEVPEASKRAILELPVHEIVKSDEGGDLECSVCKEPAEEGQKYRILPCKHEFHEECILLWLKKTNSCPLCRYELETDDPVYEELRRFRQDEANRRERENTLLDSMFG | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-... |
Q9P0P0 | MASYFDEHDCEPSDPEQETRTNMLLELARSLFNRMDFEDLGLVVDWDHHLPPPAAKTVVENLPRTVIRGSQAELKCPVCLLEFEEEETAIEMPCHHLFHSSCILPWLSKTNSCPLCRYELPTDDDTYEEHRRDKARKQQQQHRLENLHGAMYT | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Catalyzes monoubiquitination of 26S proteasome subunit PSMC2/RPT1 .
PTM: Autoubiquitinated as part of the enzymatic reaction... |
Q9CY62 | MASYFDEHDCEPLNPEREARNNMLLELARRVRGAWSWAPGGRSLFNRMDFEDLGLVDWEHHLPPPAAKAVVESLPRTVISSAKADLKCPVCLLEFEAEETVIEMPCHHLFHSNCILPWLSKTNSCPLCRHELPTDDDSYEEHKKDKARRQQQQHRLENLHGAMYT | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Catalyzes monoubiquitination of 26S proteasome subunit PSMC2/RPT1.
PTM: Auto-ubiquitinated as part of the enzymatic reaction.... |
Q5M974 | MASYFDEHNCEPTVPEEQYRQNALLELARSLLSGMDIDLGALDFTEWDQRLPPPAAKKVVESLPKVTVTPEQADAALKCPVCLLEFEEGETVRQLPCEHLFHSSCILPWLGKTNSCPLCRHELPTDSPEYEEYKQEKERRQQKEHRLECLHDAMYT | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Catalyzes monoubiquitination of 26S proteasome subunit PSMC2/RPT1.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugatin... |
Q8N6D2 | MASQPPEDTAESQASDELECKICYNRYNLKQRKPKVLECCHRVCAKCLYKIIDFGDSPQGVIVCPFCRFETCLPDDEVSSLPDDNNILVNLTCGGKGKKCLPENPTELLLTPKRLASLVSPSHTSSNCLVITIMEVQRESSPSLSSTPVVEFYRPASFDSVTTVSHNWTVWNCTSLLFQTSIRVLVWLLGLLYFSSLPLGIYLLVSKKVTLGVVFVSLVPSSLVILMVYGFCQCVCHEFLDCMAPPS | Function: E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway . Also plays a role in the inhibition of TLR-triggered innate immune response by mediating 'Lys'-48-linked ubiquitination and subsequent degradation of NF-kappa-B componen... |
Q3SWY0 | MAEQQGREPECPVCWNPFNNTFHTPKVLDCCHSFCVECLAHISLVTPTRRRLLCPLCRHPTVLASGQPVTDLPTDTAVLTLLRLEPHHVILEGHQLCLKDQPKSRYFLRQPRVYTLDLGPEPASQAGQPQDVGPSTRPVPIRSRYSLRECFRNPHFRIFAYMMAVILCGTVLFIFSIFCTRRFFWGVG | Function: Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1. May collaborate with FATE1 to restrain BIK protein levels ... |
Q96D59 | MAEQQGRELEAECPVCWNPFNNTFHTPKMLDCCHSFCVECLAHLSLVTPARRRLLCPLCRQPTVLASGQPVTDLPTDTAMLALLRLEPHHVILEGHQLCLKDQPKSRYFLRQPQVYTLDLGPQPGGQTGPPPDTASATVSTPILIPSHHSLRECFRNPQFRIFAYLMAVILSVTLLLIFSIFWTKQFLWGVG | Function: Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins . Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 . May collaborate with FATE1 to restrain BIK protein level... |
Q8QZS5 | MSEPQGQELRAECPVCWNPFNNTFHTPKVLDCCHSFCVECLAHLSLVTPARRRLLCPLCRQPTVLASGQPVTDLPTDTAMLTLLRLEPHHVILEGHQLCLKDQPKSRYFLRQPRVYTLDLGAEPGSQTGLPQDTAPDTRPVPIPSHYSLRECVRNPHFRIFAYLMAVILSVTLLLIFSIFWTKQFFWGMG | Function: Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins . Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BI... |
Q5ZIR9 | MASKGPTTSASTKSSSTGGTSGSSSSNGAGDNTNQDNTFECNICLDTAKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAVPGTPQYVDEQFLSRLFLFVALVIMFWLLIA | Function: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination. Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and ... |
Q6PC78 | MASAAASESSSSSSSSSAGAANGQSAGESGGGGAQDSTFECNICLDTSKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAAPGTPQHTDEQFLSRLFLFVALLIMFWLLIA | Function: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination. Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and ... |
Q96GF1 | MASKGPSASASPENSSAGGPSGSSNGAGESGGQDSTFECNICLDTAKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAVPGTPQYVDEQFLSRLFLFVALVIMFWLLIA | Function: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1 . Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitin... |
Q91YT2 | MASKGPSASASTENSNAGGPSGSSNGTGESGGQDSTFECNICLDTAKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAVPGTPQYVDEQFLSRLFLFVALVIMFWLLIA | Function: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1 (By similarity). Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER... |
Q9WUS2 | MGLEKSLLLLPLLVLVLGCVQPSLGKESSAMKFERQHMDSEGTGSSPTYCNQMMKRREMTKGSCKPVNTFVHEPLADVQAVCSQEKVTCKNGKSNCYKSSSALHITDCHLKGNSKYPNCDYKTSNYQKHIIVACEGNPYVPVHFDASV | Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 1634... |
P07998 | MALEKSLVRLLLLVLILLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSSSTYCNQMMRRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQGNCYKSNSSMHITDCRLTNGSRYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST | Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
PTM: N-linked glycans are of complex type.
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA... |
P04060 | KESSAMKFERQHMDSSGSPSSNSNYCNEMMRRRNMTQDRCKPVNTFVHEPLADVRAVCFQKNVACKNGQTNCYQSNSLMHITDCRVTGSSKYPDCSYGMSQLERSIVVACEGSPYVPVHFDASVGPST | Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 1427... |
A1SWZ6 | MFQNNPLLSQLKKQIQEDIPKRQGKVKATDRGYGFLETDKGKRFFIPPSEMKKVLHGDQINAFIRGKGDKSTAEPNQLKKTGSAVFIARLVIKQKNISIIPKNPLLKGFFKIKGSQSLQSRGYQDGDWVKVELVSHALEGNGFLTQIIEKIADASDPFAYRLLTVATHNLANKAPEFDHPWKIIDPQLSRSDLTKTPFFTIDGVNTQDMDDALYIEADENGWKLTVAISDPSAYVPENSDMDAEAKRRAFTLYLPNFNVPMLPRDLSDSLCSLKEGEKRATLCCTIHINKKGEIEGEPAFYGAWIKSHYRLNYTDVSNYL... | Function: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 74164
Sequence Length: 656
Subcellular Location: Cytoplasm
EC: 3.1.... |
Q8FP16 | MSRKKTRVTGVDALAEAFDAVNHADLLERLGVDIDRDLLVLALTHRSFANENGMLPNNERLEFLGDAVLGLAVANRLYELYPSSPESDISKMRASIVSRYGLADIAREINLGEFILLGKGELLTEGRSKDSILADTTEALLGAIFRQHGYEVARDVVLTLFHHKINHASAKGIHQDWKTTLQEELAQRKKPMVEYQTTSVGPDHDLLFTAVVYLGDVEMGRGEGPNKKLAEQEAARQAFLKLREKRA | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q4JUY7 | MARKRRLTGEAALNAAYGKSDHAPLLEAWGVDLPDDLLRLALTHRSFANENGHLPNNERLEFLGDAVLGLAVAEQLYRQFPERAESDISKMRSGVVNMYALADVARRLGMGDYILLGRGEMLTGGKDKHSILADSVESMLGAIYLHHGFEVARATVLRLFAEKITEAPTTGLTMDWKTVLLEKLSDMKLPLPTYEVRGEGPEHDKTFYATVTIEDLVTHGEGHTKKVAEHAAAKQAVQKLNERA | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A9KFA0 | MNHLNKLMERLGHQFNNLELLKIALTHRSSGADNNERLEFLGDSVLGFIIASELYQRRPQAREGDLSRMRASMVNGDELAQMSTKLGINEYLQLGVGEQKSGGKRRRSILADALEAIVGAIYIDAGLETCRRCVLNWYGERVDDLSKLSPKKDAKSLLQEWLQARRLPLPTYEVKITGEAHAQTFTVNCYVKGLPHKTEGVNTTRRRAEQIAAKRFLELLDDGKGDGITERDQ | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q3Z7Q8 | MLDLTELEKSLGVKFENLSLLEQALIHTSWVNENPNHLSGSNERMEFLGDAVLGVIFADRLYHDFPDIQEGDLTRFRSLLVRRESLVRVALGINLGKYLYLGRGEDASKGRFKPANLAGAFEAVLAAIYLDKGIDATREVIFRLFKTEMERVQTLSSNIDYKSRLQELVQAQFQLTPRYRIIDFSGPEHNHLFIAEVYTEDKVLAEGSGRSKKEAETSAAKEALQQFENSFTAEDNI | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q6ANV0 | MGIDVKELIRRNRQKHAEFEKKINYKFIDLRLLQKALIHSSYAFEQAQAGKNNERLEFVGDAVLDLVVGNALYRRFPEMREGELTRLRAALVNEGHLATMARKINLGYFLCLGKGEDNSKGREKSSILSCAYEAVIGAIFQDGGYDAVAALVERFFLPVIDRRKEDLLLADAKSRLQEILQEKHNEGPSYRLDNEEGPSHKKRFTISVLFRDEVLGTGEAGSKKEAEQRGAALAIKKIESM | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A4J683 | MSKQDEQANRLKTRLGFKWHNPTLLIQALTHSSCVHENRGHGLCHNQRLEFLGDAVLELIISEHLYKMFPDRTEGELTKMRASSVCEPSLAKVARGLDLGRCLRMGRGEERSGGRERPSILADAFEALLGAIYLDQGLEISRHFVLNCLSSIIDDVVAGRLDRDYKTELQEILQQSSPDPLTYTIMDESGPDHDKTFTAGVIYKGKVIGKGSGHSKKEAEQQAAKDAFQHLEGMGKSGHKSAGPIR | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q72C44 | MWARTAAWVFGLPETLREICYRRDNVKPVDELQKTIGHRFGDMELLLTAMTHSSWANEQAVPVEHNERLEFLGDAVLELCVSEELFRRFPSAREGDLTRMRSRLVSKPSLEGVARELRLDMSLRLGKGEESQGGRERGSLLSDALEAMLGAVFLDAGYIAAKGVVMRILGPHFPEALVPVRTKDYKSQLQELTQKLFRDRPVYTLLGSSGPEHDKQFDVRVVLPDGTVFEATGPSMKRAEQMAAARAVATLDK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q8EH81 | MEPIKNLPRLCRTLGYEFKNLDLLTQALTHRSAANKHNERLEFLGDSILSIVISDALYHQFPKATEGDLSRMRATLVRGDTLTLIAQAFKLGDYLFLGPGELKSGGFRRESILADAVEAIIGAIYLDSDLEVCRQLLLNWYAERLAEIQPGINQKDAKTLLQEYLQGLKKPLPDYQVINIEGDAHDQTFTVECRIDDLSQSVIGVASSRRKAEQIAAAQVLELLKK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q969K3 | MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEE... | Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptor... |
Q99KR6 | MKAGATSMWASCCGLLNEVMGTGAVRGQQAGFPGSTGPFRFTPSSDFPTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLLLRNIPTDTCREKEDLVDLVLCHRGLGSGDDLDSSSLNSSRSQTSSFFTQSLFSNYTPPSATVSSFQGELMDRDGAFRSEVLAQVQSEIASANTDDDDDDDDDDDDDEDDDDEQEEEEQNPGLSKKKARASLSDLSSLEEVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERMQL... | Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptor... |
Q6AYH3 | MKAGATSMWASCCGLLNEVMGTGAVRGQQAGFPGSTGPFRFTPSSDFPTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLLLRNVPTDTCREKEDLVDLVLCHRGLGSGDGLDSRSLSSSRSQTSSFFTQSYFSNYTPPSATVSSFQGELMDREGTFRSEVLTQVQSELASANTDDEDGEEDDDDDDDDDDEDDDEQEENLEEQNPGLSKKKARASLSDLSSLEEVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYG... | Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptor... |
O94941 | MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLP... | Function: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugat... |
Q9H0F5 | MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQEDAHFKAFFQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPSQHHFSGERCNTPARNRRSPPVRRQRGRRDRLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLP... | Function: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
Q8BI21 | MRESEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPNQHHFSGERCNTPARNRRSPPVRRQRGRRERLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGLPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLQVGSFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRS... | Function: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
Q7ZW16 | MGYDVTRFQGEVDEDLLCPICSGVLEEPVRAPHCEHAFCNACITQWFAQQQICPVDRTVVTLAHLRPVPRIMRNMLSKLQISCDNAGFGCTATLRLDQLQSHLKDCEHNPKRPVTCEEGCGLEMPKDEMPNHNCIKHLRSVVQQQQTKIADLEKTAAEHKHQLAEQKRDIQLLKAYMRAIRSANPNLQNLEESIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLIDSGCPLSIVNDLIENAHERNWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGEDMILEPGLVMIFAHGVEEIL | Function: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): ... |
Q9H4P4 | MGYDVTRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQIACDNAVFGCSAVVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDELPNHNCIKHLRSVVQQQQTRIAELEKTSAEHKHQLAEQKRDIQLLKAYMRAIRSVNPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQEPGLVMIFAHGVEEI | Function: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of pro-inflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By si... |
Q5FWL3 | MGYDVSRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQITCDNAVFGCTTIVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDEVPNHNCIKHLRSVVQQQQIRIGELEKTAAESKHQLSEQKRDIQLLKAYMRAIRSANPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNEIIENAHERNWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGEDMVLEPGLVMIFAHGVEEI | Function: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): ... |
Q8EE78 | MAFKIASSPHVTRNLQTSTVMQRVILCLLPGLVVQCAFFGWGTLIQVLLAIIVALSCEAAVMKLRKRSIKASLGDNSAMLTAILIGVAIPPLAPWWMIVMGTAFAIVIVKHLYGGLGHNLFNPAMAAYVLLLVSFPLQMTTWIAPSTVALNTPSIVDSLQLIFNVGAHVGMEQFRLGIDGISMATPLDTLKTDLSLGLTTTESMAKSIFDGSTGVGWFWVNLAYLAGGIVLLKLKAIRWHISTGVLAGLFVASSVGFLLSPDTHASPLFHLFSGATMLAAFFIATDPVTAATSPRGRIIFGALIGVLVYIIRTQGGYPDA... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37258
Sequence Length: 349
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q9EVN4 | MIRSSVDRIMLHVCLALLPTTAWGLYLFGWPAIYLWLLTCASAVACEAACLYLLGRPLRRLLDGSALLSGWLLALTLPPWAPWWIAVGGSMFAIGIGKQLYGGVGQNVFNPAMLARVALLIAFPLQMTTWALPLPLGTEGAPGWLEGLRITFAGGALADGLSGATALGHLQTELTLGHSAAQILDGHFALLPAFLGYSGGSLGETSELLILLGGLWLLALRIIHWEIPLGMLLTVGALAALANQIDPQVHGGGLFHLTSGGLLLGALFIATDPVTSPISRSGRLIFAIGCGALVFVIRSWGNFPEAVAFAVLLMNALVPL... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37564
Sequence Length: 354
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
A5F2R1 | MAFFIASSPHLRSKRSTADVMRWVLVCALPGLIAQTYFFGYGTLIQLLLAISVAVALEAGIMLLRKRSPISALRDYSAVVTAWLLAVAIPPLSPWWVVVIGLIFAIVIAKHLYGGLGQNPFNPAMIAYVVLLISFPVQMTSWMAPIKLTAEPSSLVDSFSLIFGGFDSDGLSLQQIRTGIDGITMATPLDAIKTSLKAGHTMSETLTQPQFSGFAGIGWEWVNIAYLLGGLILLKLRIIRWHIPVAMLAGLVFTALLAQLFAPGTTASPMIHLLSGATMLGAFFIATDPVSASTTDKGRLIYGFFIGAMVFLIRSWGGFP... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37604
Sequence Length: 348
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q87MX1 | MSFFIASSPHAHSRRSTPDLMKWVALCAIPGLAAQTYYFGWGTLIQLIFAIAVAVSLEALVMICRKRSPMRALRDNSAIVTAWLLAVAIPPWSPWWIIVIGLIFAIVIAKHLYGGIGQNLFNPAMVAYVVLLISFPVQMTSWSAPTLLIPDHVNFADTLSLIFTGFDYDGLSLQQVRAGVDGVTMATPLDAFKTGIHTGATPSEVLSQPIFGGLAGIGWQWVNIAYLIGGLVMIKKRIIQWYIPAGFLASLTLFSLIFSVITPGETASPIFHLLSGATMLGAFFIATDPVSASTTVKGRLIFGALIGALVFIIRSWGGFP... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37654
Sequence Length: 348
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q6NZ21 | MKLRAQFDRGTYSESKGSFKLRDSLDPMQPEPSSREGNGLSLTLQPELLARMPGAGSSSGTETGEDVRVPMGSSSGSTNGRGATSRRMRTASHSHSHTHGHGHSHEHESDSGESDLESGESSSSISELRYLLRWLKKSLPFIVILCAKLVIQHALGLAVAVGLFTTFMYVNKSIQTQVFLHDRRTNLHCAWLLLFLTSSSLLVFYTFHTQSLYRCLFFANATIDYHNFWEVLWSVGVTNFILKFIFMGFKCLILLVPCPLMTYRRRGQWYMLIEEVGQLYQVIAPVPLWFRYLVSYDEMDTSVGLTLGILLALLYLIMKL... | Function: E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis.
... |
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