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
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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
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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.
Subcellular Location: Secreted
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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.
Subcellular Location: Secreted
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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
Sequence Length: 157
Subcellular Location: Cytoplasm
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A0A1C9J6A7 | MSSCINPSTLATSVNGFKCLPLATNRAAIRIMAKNKPVQCLVSTKYDNLTVDRRSANYQPSIWDHDFLQSLNSNYTDETYKRRAEELKGKVKTAIKDVTEPLDQLELIDNLQRLGLAYHFEPEIRNILRNIHNHNKDYNWRKENLYATSLEFRLLRQHGYPVSQEVFSGFKDDKVGFICDDFKGILSLHEASYYSLEGESIMEEAWQFTSKHLKEMMITSNSKEEDVFVAEQAKRALELPLHWKAPMLEARWFIHVYEKREDKNHLLLELAKLEFNTLQAIYQEELKDISGWWKDTGLGEKLSFARNRLVASFLWSMGIAFEPQFAYCRRVLTISIALITVIDDIYDVYGTLDELEIFTDAVARWDINYALKHLPGYMKMCFLALYNFVNEFAYYVLKQQDFDMLLSIKHAWLGLIQAYLVEAKWYHSKYTPKLEEYLENGLVSITGPLIITISYLSGTNPIIKKELEFLESNPDIVHWSSKIFRLQDDLGTSSDEIQRGDVPKSIQCYMHETGASEEVAREHIKDMMRQMWKKVNAYTADKDSPLTRTTAEFLLNLVRMSHFMYLHGDGHGVQNQETIDVGFTLLFQPIPLEDKDMAFTASPGTKG | 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 diphosphate .
Catalytic Activity: (2E)-geranyl diphosphate = (4R)-limonene + diphosphate
Sequence Mass (Da): 70354
Sequence Length: 607
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Plastid
EC: 4.2.3.20
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O45962 | MAPTGQGGQWQEVLCCSICNRHFNETFLPVSLICGHVICRKCAEKPENQTKPCPHDDWKTTHSPSEYPNNVALLSVIFPRKQCMTLSGAVSEAEKRVDQLSIQIAKFFREADSERGGTVSSREISRTLQRKVLALLCYQWREVDGRLKTLKMCRGISERVMIEIILSIQSNTHVSSQLWSAVRARGCQFLGPAMQDDVLRLILMTLETGECIARKNLVMYVVQTLASDYPQVSKTCVGHVVQLLYRASCFNVLKRDGESSLMQLKEEFRTYESLRREHDSQIVQIAFESGLRIGPDQWSALLYADQSHRSHMQSIIDKLQSKNSYQQGVEELRALAGSQTSMLVPAYRYFLTQVIPCLEFFAGIEHEDTSMRMIGDALHQIRILLKLHCSQDDLRKMPKEERRGVILQAEVPGGMGGGPGGSGGAEAGRIGGLHPLYSQIDETGRSISRTNPKDNSHNSPQTPPKQPRQKRYQMGIPPNRMGYSSDAPPFIPSHQQQPPPQFFNSQHLPQRFRGGRQRGAPPPPPPQPMPMLIGYDMPGAPMMQATEVLTADGQMVNGTPQRVVIMQSPTHLPGGPVVMIPQQQMVPPPQSMTPVGGPMGPMGPMTPSIPVQVPPNTMWTATSPTGSVIYPAASPPGQPPHTIWIQSTDGNMFPMFDRGSGGMVWGPGTMLRESGADAEQLLAKRYEILKRLQPSEDDDDPEDGGIGHVSYTVASSVLDDRMDHHPLTMIPVPTIDLPAIPISFANMPTEETMTMIGEMVQNRPRAPSLTAPSSNQPMNVNASASATVQAECGTMSVMDSICQPISTSAIHNSATIPQPVIPMVQVPVQVPIVPAENFNPNVPPPPPPPQGQPMLVDSAIGLLTPIRPILVAHPQNVVSNSLDKIVDVKERISEAQGNASEAENAHLRMELRMAESQMAHLDPYTKNNCLLRALQQVDMELQQLHLNPTVEG | 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 infection .
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): 104766
Sequence Length: 952
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
EC: 2.3.2.27
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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 activation of some intracellular mitogen-activated protein kinases (By similarity).
PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine protease (subtilase).
Sequence Mass (Da): 11390
Sequence Length: 103
Subcellular Location: Secreted
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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 activation of some intracellular mitogen-activated protein kinases (By similarity).
PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine protease (subtilase).
Sequence Mass (Da): 12397
Sequence Length: 110
Subcellular Location: Secreted
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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 activation of some intracellular mitogen-activated protein kinases. Mostly active in roots. Prevents plant growth (e.g. root and leaf length). Suppresses cell elongation of the primary root by activating the cell surface receptor FER and triggering phosphorylation of AHA2 and subsequent extracellular alkalinization.
PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine protease (subtilase).
Sequence Mass (Da): 12967
Sequence Length: 120
Subcellular Location: Secreted
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A3QB25 | MKCAYFDANQCLSCRHLKTPLSDQVAAKTATLAALLKDLSVEQWLPPVVGPESGFRNKAKMVVLGAAHQPILGLVSPSGEAVSLCDCSLYPQDMQQLLHRLEAFVRQAGIPPYRVDKAKGELKFILLTRSQVRGEYMLRFVMRSEQAIPRIERELPRLLAEHPEIKVVSVNLQPVHMAILEGEEEIFLTEATRLEEEFNGVPLYIRPKSFFQTHPEVAAKLYLSARKWTRELAPTSIWDLFCGVGGFGLHCASKEVALTGIEIEAEAIACAKMSAETLGLDKVRFTALDSTSFASDSRGEEKPELIIVNPPRRGIGEALCHSLSEFAPKAILYSSCNPKTLAKDLHCISGYRVTKVQLFDMFPHTDHFEVLVMLQRIGE | 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
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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): 24160
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 23750
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 23215
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 24053
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 23420
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 21702
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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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): 23411
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.1.1.166
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A8GJW6 | MSQLDLGTQQLELERYPQQEESTQLQAWEAADEYLLQQLENVNIGDRPVLIFNDNFGTLACALHSHQPYSISDSYMSQLATRHNLKLNELDPQQVTLLDTLAELPASPAVVLIRIPKALALLEQQLRALRDVVAPDTVIIAGAKARDVHTSTMQLFEKVLGPTRTSLAWKKARLIHCEVADIVPPAAPVTTNWVLDGTDWVIHNHANVFSRSNLDIGARLFLDHLPHDIEGHIIDLGCGNGVIGMAALMQNPQAQVSFVDESYMAVASSELNVEHNLPQDMDRCQFEVNNSLAGIERESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNCTLIASNKKFVILKAVKSGARY | 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: 2.1.1.174
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B1KD54 | MTTQFSVAGIELELARYPKDQESNLQAWDAADEHLIKHLIETEQTPVVTAIINDNFGALTACLRSIAPTWPLMVETDAKTSLLGNLQNLATNNLSSEGIEWLNSREALPEQIELVLMKLPKNLTYFAHQLNRLSQVLPKGTQVLISAKAKSINKSVLELIGKNLGSASASLTWKKTRVITCISDGEIRSLPKEMQWSVPRLNLEIRNLSNVFAANKLDIGAEIMLENMPKGDFKSIIDLGCGNGILGLHAKQLFPQAYIHFVDDSEMAIESAKQNWALNKLDTQGLVGEQATFGWDDCLTHMSEGVRPDLVLCNPPFHQGEAITDHIAWQMFLQSWRALKNGGILHVVGNRHLAYHIKLQRIFKNCTTVASNGKFVILQAQKISKKAEPFETHPTEAEAKVEVTESKPHPQSSLYGTKK | 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: 2.1.1.174
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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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: Cytoplasm
EC: 2.1.1.177
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A0Q621 | MQKFTFFVSCAKGIELLLKDELERLGISSQEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINWMDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVTNQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHKRSYRQFQGQAPLKESLAAAILIKAGWLEELKKHQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEFKIFNSKFHNKELWDNLLEIAKNSQKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPPYGERLYGDQLDELLDIFNGFGDRLSQDFYGWKVAVLTSFADSIKEMQLRTTKRNKFYNGAIETILYQFEINEHAKFKHETQLEKNIRIAEASVQKSDEHIDFANKLKKNLKSLKPWLKQTGLECYRLYDADIPTFAVAVDVYGEHIFLQEYRADATIDQNIAKQRFYQAIYQIHKTLDIKYENIHTRVRQRQKGKEQYQKENDKNKFHIINEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAKNKTLLNLFSYTCTASVHAALKGAKTTSVDMSNTYLEWGKNNFELNKLDIKKHSFIQADCISWLKTNKDKFDVIFLDPPTFSNSKRMDDILDIQRDHELLINLAMDSLKKDGILYFSNNYRRFKMSPQILEKFNCENIDKICLSRDFLSNKNIHNCWEIKYKK | 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: 718
Subcellular Location: Cytoplasm
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Q7VP04 | MSNQITYFATAARGFEEMLKIELEQICGADGKVVQGGVHFTTNQKGAYQALLHSRLASRILLPLVSTKIFSDLDLYATIIAINWADIFDPRDTFYVDFNGTNREIRNTQFGAMRVKDGIVDYFERKRFARPIVDKDRPDIRIHVYLDREKLIVSLDLSGEALHMRGYREDTGKAPLRETLAAIIVLRSGWQKGTPLVDPMCGSGTLLIEAAQMQAGIVPQLQRKYWGFNAWKGHQQAIWQQVLEEAHSQKNTQIDPLFYGFDLDHRVLAKAKQNAQNAGVAHLIHWQQADIAALKNPCLDQKGTLVSNPPYGERLGTTPALIALYSVFGQRLKQQFAGWNVSIFSGEPSLLNCLRLRSTRQFKAKNGPLDCLQKNYQIAEYAIHNQHISESSVAQNTQVAPDFANRLTKNIKKIEKWAKQQQLDAYRLYDADLPEYNFAVDRYSDHIVIQEYAAPKSIEQNKARQRLLDAVTATLHVTGIETNKLVLKVRQKQKGTNQYEKLANKGEYFYVNEYGAKLWVNLTDYLDTGIFLDHRLTRKMVGQMAKGKTFLNLFAYTGSATIHAALHGAKATTSVDMSNTYLNWAEQNLELNGLKSRNHRLFQADCLQWLAECRERFELIFVDPPTFSNSKRMEDSWDVQRDHIKLMTQLKRILTSDGMIVFSNNKRGFKMDFNGLTALGLVAENISYKTLPLDFERDPHIHNCWIIRHIEN | 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: 712
Subcellular Location: Cytoplasm
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O34617 | MAELNKTKVRKELRTERPSIYSFELDEIKQWLTDNGEKPFRAAQIFEWLYEKRVSSFEDMTNLSKDLREKLNTRFVLTTLKTAVKQTSQDGTMKFLFELHDGYTIETVLMRHEYGNSVCVTTQVGCRIGCTFCASTLGGLKRNLEAGEIVAQVVKVQKALDETDERVSSVVIMGIGEPFDNFNEMLAFLKIINHDKGLNIGARHITVSTSGIIPKIYEFADQQMQINFAISLHAPNTEIRSRLMPINRAYKLPDLMEAVKYYINKTGRRISFEYGLFGGVNDQVEHAEELADLLEGVKCHVNLIPVNYVPERDYVRTPRDQIFAFEKTLKSRGVNVTIRREQGHDIDAACGQLRAKERQDETR | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41570
Sequence Length: 363
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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Q89ZK5 | MMSKYPLLGMTLIELQSLVKRLGMPGFAAKQIASWLYDKKVTSIDEMTNLSLKYRELLKQNYEVGAEAPVEEMRSVDGTVKYLYPVGENHFVESVYIPDDERATLCISSQVGCKMNCKFCMTGKQGYSANLTAHQIINQIHSLPERDKLTNVVMMGMGEPLDNLEEVLKALDILTGSYGYAWSPKRITVSTVGLRKGLRRFIEESDCHLAISLHSPVTAQRAELMPAEKAFSITEMVELLKNYDFSKQRRLSFEYIVFKGLNDSQVYAKELLKLLRGLDCRMNLIRFHSIPGVALEGADMDTMTRFRDYLTTHGLFTTIRASRGEDIFAACGMLSTAKQEENNKS | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38992
Sequence Length: 345
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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Q6MPV7 | MEANAGSTLAPVNYSDDNVAKPLENQPVNFYSLTLEDLKAYIKSKGKEQFRAQQIFKWVYEQRVTDPEQMTNLSKEFRQDLPSMLSFDLPPVLQHLKSVDGTQKFLFDMKDGMSVEAVVIPSEDRLTLCISSEVGCNMACKFCFTGKQKLKRRLRTEDIVGQFMQVHDRLAEGQRITNIVFMGMGEPLDNPEAVFKTIDVIHSPWGINLSRKKITVSTSGIVPEMWRVADAKVRLAVSLNGPNDEIRSQVMPINKRWDTKALLEACKEHYRVSKDKITFEYVLLKGITDQLEHARQLVKLVKDVPCKINIIPFNEHPGSGYERPDDDTIQAFHTELMNLGAHVLLRRSMGRDIFAACGQLTTVKERPQTMDISNSRLAGLPKYKRELLAAQEAEQNNQH | 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 occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 45369
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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Q8G481 | MTTQHPDTPETGITPGGTSGAFRDVLSKDHARRGKPPLHFVDMTPEQRVEKAAELGLPKFRVKQLANHYFGHFDVNAAEFTDFPAAKRSEAAAAFFPQLITEVTRQVADEGTTIKTLWKLFDGSLIESVLMRYPTRTTLCISSQVGCGMDCPFCATGKLGLTRNMSTGEIIEQVRVAAKMMRDGEVAGGEGRLSNIVFMGMGEPMGNYNSVLSAVRQISAMPPEGFGISARNITVSTVGVVPGIKKLTAEGIPVRLAVSLHAPSDELRDELVPMNKRFNTKQVLDAAHDYWLASKRRVSIEYALMRGINDQAEHAQLLAKRLNHYGDNWAHVNPIPLNPIEGSKWTASKPEDEQRFLEILHRAGITATLRDTRGQDIDGACGQLAAKER | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42694
Sequence Length: 389
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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Q1IRD1 | MERLGQPAYRSRQLWQGLYRDRIASLDQFTTLPIPLREELKSSGWAIAFPFVQKRFTSTDGTVRYLLQFSDGQSVETVWMPEGDGGEQGDGSEDGPSYDRATICVSSQVGCAVDCQFCMTALLGLLRNLSAGEIVGQILAVLKDENVDVEKSRINLVFMGQGEPFLNFDNFVKAVTLLAEAVGIPESRMTVSTSGIVPRIVDFGQLAIRPKLAISLNASNDESRRELMPITKKWTLEKLMSAAREFPLRNRERMTFEYVLLGGVNDSEQNAREVVQLLRGLRAKVNLIAWNPGPEIPFSTPDPQHVEAFQQILIDAGIPTFIRKPRGRDIFAACGQLKRTELVTLS | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38541
Sequence Length: 346
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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C4Z523 | MTDIKSLNYDELVTYMAGLGEKKFRAGQLYQWMHEKLADSFDECTNLSNALRQKLKETSEYVCLEPVRVQHSKLDGTEKYLFRLSDGNYVESVLMKYHHGNSVCISSQVGCRMGCRFCASTLNGKVRDLRPSEMLDQIYRIQKITGERVSNVVVMGSGEPMDNYDNLIKFIELLNDERGLNISQRNITVSSCGIVPKLKELADLKLQITLAISLHAPNDELRKTMMPIANKYSIEEIMDVCRYYIECTGRRISFEYSLVKGVNDSMECAKQLIELVKGMNCHINLIPVNPIKERDYKQTGKEEVYAFKNKLEKNGINVTIRREMGRDIDGACGQLRNKYMEDIDESDGGY | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40047
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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O86754 | MPKPGELTFVAPRGVKKPPRHLADLTPAERKEAVAAIGEKPFRAKQLSQHYFARYAHAPEQWTDIPAGSREGLREALLPELMTVVRHLSTDQGTTRKTLWKLFDGTLVESVLMRYPDRVTMCISSQAGCGMNCPFCATGQAGLDRNLSTAEIVHQIVDGMRALRDGEVPGGPARLSNIVFMGMGEPLANYNRVVGAIRRLTDPEPDGLGLSQRGITVSTVGLVPAIHRFTGEGFKCRLAISLHAPDDELRDTLVPVNTRWKVREVLDAGFEYAAKSGRRLSIEYALIRDINDQAWRGDRLGRLLRGRPVHVNLIPLNPTPGSKWTASRPEDEKAFVEAIAAHGVPVTIRDTRGQEIDGACGQLAASER | 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] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40402
Sequence Length: 368
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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Q9MA83 | MIPSQSNSFSGSVITLYFFLLGSLVLRTLASSRLHYCRHDQRDALLEFKHEFPVSESKPSPSLSSWNKTSDCCFWEGVTCDDESGEVVSLDLSYVLLNNSLKPTSGLFKLQQLQNLTLSDCHLYGEVTSSLGNLSRLTHLDLSSNQLTGEVLASVSKLNQLRDLLLSENSFSGNIPTSFTNLTKLSSLDISSNQFTLENFSFILPNLTSLSSLNVASNHFKSTLPSDMSGLHNLKYFDVRENSFVGTFPTSLFTIPSLQIVYLEGNQFMGPIKFGNISSSSRLWDLNLADNKFDGPIPEYISEIHSLIVLDLSHNNLVGPIPTSISKLVNLQHLSLSNNTLEGEVPGCLWGLMTVTLSHNSFNSFGKSSSGALDGESMQELDLGSNSLGGPFPHWICKQRFLKYLDLSNNLFNGSIPPCLKNSTYWLKGLVLRNNSFSGFLPDVFVNASMLLSLDVSYNRLEGKLPKSLINCTGMELLNVGSNIIKDTFPSWLVSLPSLRVLILRSNAFYGSLYYDHISFGFQHLRLIDISQNGFSGTLSPLYFSNWREMVTSVLEENGSNIGTEDWYMGEKGPEFSHSNSMTMIYKGVETDFLRIPYFFRAIDFSGNRFFGNIPESVGLLKELRLLNLSGNSFTSNIPQSLANLTNLETLDLSRNQLSGHIPRDLGSLSFLSTMNFSHNLLEGPVPLGTQFQSQHCSTFMDNLRLYGLEKICGKAHAPSSTPLESEEFSEPEEQVINWIAAAIAYGPGVFCGLVIGHIFFTAHKHEWFMEKFHRNKRRVVTTSAR | 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). Functionality seems to depend on the presence of the receptor kinase SOBIR1 as an adapter protein . Required for full non-host resistance to bacterial pathogens (e.g. P.syringae pv phaseolicola) .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87527
Sequence Length: 786
Subcellular Location: Cell membrane
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Q9SHI4 | MTNEGRFKAKGFVRTSSTTRPIQALSFHMIGILLQCVLFISVLSIAVSEALCNSQDRESLLWFSGNVSSSVSPLNWNPSIDCCSWEGITCDDSPDSHITAISLPFRALYGKLPLSVLRLHHLSQLNLSHNRLSGHLPSGFLSALDQLKVLDLSYNSLDGELPVEQTFRNGSNRCFPIRIVDLSSNFLQGEILPSSIFMQGTFDLISFNVSKNSFTGSIPSFMCKSSPQLSKLDFSYNDFTGNIPQGLGRCLKLSVLQAGFNNISGEIPSDIYNLSELEQLFLPVNHLSGKINDDITHLTKLKSLELYSNHLGGEIPMDIGQLSRLQSLQLHINNITGTVPPSLANCTNLVKLNLRLNRLEGTLSELDFSRFQSLSILDLGNNSFSGDFPWRVHSCKSLSAMRFASNKLTGQISPHVLELESLSILSLSDNKLMNITGALGILQGCRNLSTLLIGKNFYNETFPSDKDLISSDGFPNLQIFASGGSGLRGEIPAWLIKLKSLAVIDLSHNQLVGSIPGWLGTFPHLFYIDLSENLLSGELPKDLFQLKALMSQKAYDATERNYLKLPVFVSPNNVTTHQQYNQLFSLPPGIYIRRNNLKGSIPIEVGQLKVLHVLELSHNYLSGIIPHELSKLTSLERLDLSNNHLSGRIPWSLTSLHYMSYFNVVNNSLDGPIPTGSQFDTFPQANFKGNPLLCGGILLTSCKASTKLPATTTNKADTEDEEELKFIFILGVATGFFVSYCFYWCFFARLDAFISK | 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 protein
Sequence Mass (Da): 83640
Sequence Length: 756
Subcellular Location: Cell membrane
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Q9LJS0 | MSKSLLRLTFLLLLLLSCVSPSSFFTFNNPAEGPGACGPHQIQAFTQFKNEFDTRACNHSDPWNGVWCDNSTGAVTMLQLRACLSGTLKPNSSLFQFHHLRSLLLPHNNFTSSSISSKFGMLNNLEVLSLSSSGFLAQVPFSFSNLSMLSALDLSKNELTGSLSFVRNLRKLRVLDVSYNHFSGILNPNSSLFELHHLIYLNLRYNNFTSSSLPYEFGNLNKLEVLDVSSNSFFGQVPPTISNLTQLTELYLPLNDFTGSLPLVQNLTKLSILHLFGNHFSGTIPSSLFTMPFLSSIYLNKNNLSGSIEVPNSSSSSRLEHLYLGKNHLGKILEPIAKLVNLKELDLSFLNTSHPIDLSLFSSLKSLLLLDLSGDWISKASLTLDSYIPSTLEVLRLEHCDISEFPNVFKTLHNLEYIALSNNRISGKFPEWLWSLPRLSSVFITDNLLTGFEGSSEVLVNSSVQILSLDTNSLEGALPHLPLSINYFSAIDNRFGGDIPLSICNRSSLDVLDLSYNNFSGQIPPCLSNLLYLKLRKNNLEGSIPDKYYVDTPLRSFDVGYNRLTGKLPRSLINCSALQFLSVDHNGIKDTFPFYLKALPKLQVLLLSSNEFYGPLSPPNQGPLGFPELRILEIAGNKLTGSLPPDFFVNWKASSHTMNEDLGLYMVYSKVIFGNYHLTYYETIDLRYKGLSMEQENVLTSSATIDLSGNRLEGEIPESLGLLKALIALNLSNNAFTGHIPLSLANLKKIESLDLSSNQLSGTIPNGLGTLSFLAYMNVSHNQLNGEIPQGTQITGQPKSSFEGNAGLCGFPLQESCFGTNAPPAQKPKEEEEAEEDEQELNWKAVAIGYGVGVLLGLAIAQLIASYKPEWLVCLVKSRNPLRSFFGFEY | 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 depend on the presence of the receptor kinase SOBIR1 as an adapter protein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98439
Sequence Length: 890
Subcellular Location: Cell membrane
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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-rhamnofuranose + NAD(+) = H(+) + L-rhamnono-1,4-lactone + NADH
Sequence Mass (Da): 27207
Sequence Length: 258
EC: 1.1.1.173
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P0C7J0 | MATWLVTGRAGFIGGNFVLEAVSRGIRVVNLDALTYAGNLNTLASLEGNADHIFVKGDIGDGALVTRLLQEHQPDAVLNFAAESHVDRSIEGPGAFIQTNVVGTLALLEAVRDYWKALPDTRRDAFRFLHVSTDEVYGTLGETGKFTETTPYAPNSPYSASKAASDHLVRAFHHTYGLPVLTTNCSNNYGPYHFPEKLIPLVIAKALAGEPLPVYGDGKQVRDWLFVSDHCEAIRTVLAKGRVGETYNVGGNSERQNIEVVQAICALLDQHRPREDGKPRESQIAYVTDRPGHDRRYAIDASKLKDELGWEPAYTFEQGIAQTVDWYLTNQTWVQGVLDGSYRLERIGATV | 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
Sequence Length: 351
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 4.2.1.46
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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-glucose, but cannot convert GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 33597
Sequence Length: 301
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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 of arabinogalactan to peptidoglycan via a phosphodiester linkage.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 22241
Sequence Length: 201
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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 of arabinogalactan to peptidoglycan via a phosphodiester linkage.
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Mass (Da): 22314
Sequence Length: 202
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 5.1.3.13
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P37763 | MDIIDTALPDVKLLKPQVFTDGRGFFMETFRDGWFKENIADRTFVQENHSNSSKGVLRGLHYQTENTQGKLVRVVVGEVFDVAVDMREGSPTFGKWAGATLSAQNRYQLWIPEGFAHGFCVLGDAAEVVYKCTDYYNPETEQVLIWNDPAIGIGWPLQTAPLLSPKDLAGKTWAQAEKSALRFPDKKCRPNVSDGIFSDRLPTRLQYALCKEKHPGNEERQAQPRSGGIPVLQIQRERRIRAAVGHREGNNKRHNYTNQAFTDNQACREKRTDTVGVFQTAFAVFRLLANDVFQHRRQHRACHDGHIDGRRQINAHTDRKDGQGKFTA | 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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
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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-L-rhamnose biosynthesis.
EC: 5.1.3.13
|
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-rhamnose
Sequence Mass (Da): 21956
Sequence Length: 200
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 5.1.3.13
|
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-beta-L-rhamnose + H(+) + NADPH
Sequence Mass (Da): 32356
Sequence Length: 294
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
|
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-beta-L-rhamnose + H(+) + NADPH
Sequence Mass (Da): 31631
Sequence Length: 298
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
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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 (By similarity).
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Mass (Da): 32694
Sequence Length: 299
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
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A0QTF8 | MDLINGMGTSPGYWRTPREPGNDHRRARLDVMAQRIVITGAGGMVGRVLADQAAAKGHTVLALTSSQCDITDEDAVRRFVANGDVVINCAAYTQVDKAEDEPERAHAVNAVGPGNLAKACAAVDAGLIHISTDYVFGAVDRDTPYEVDDETGPVNIYGRTKLAGEQAVLAAKPDAYVVRTAWVYRGGDGSDFVATMRRLAAGDGAIDVVADQVGSPTYTGDLVGALLQIVDGGVEPGILHAANAGVASRFDQARATFEAVGADPERVRPCGSDRHPRPAPRPSYTVLSSQRSAQAGLTPLRDWREALQDAVAAVVGATTDGPLPSTP | 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 reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity).
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Mass (Da): 34254
Sequence Length: 327
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
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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). 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-beta-L-rhamnose + H(+) + NADPH
Sequence Mass (Da): 32045
Sequence Length: 304
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
EC: 1.1.1.133
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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-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 17037
Sequence Length: 147
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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.
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): 17909
Sequence Length: 153
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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.
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): 19101
Sequence Length: 165
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 18001
Sequence Length: 156
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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 component RELA .
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27402
Sequence Length: 247
Domain: The RING-type zinc finger domain is required for E3 ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
EC: 2.3.2.27
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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 thus regulating apoptotic signaling.
PTM: Autoubiquitinated (in vitro).
Location Topology: Single-pass type IV membrane protein
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): 21492
Sequence Length: 188
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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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 levels thus regulating apoptotic signaling .
PTM: Autoubiquitinated (in vitro).
Location Topology: Single-pass type IV membrane protein
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): 21617
Sequence Length: 192
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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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 BIK protein levels thus regulating apoptotic signaling (By similarity).
PTM: Autoubiquitinated (in vitro).
Location Topology: Single-pass type IV membrane protein
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): 21625
Sequence Length: 190
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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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 subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-AMP synthase activity. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (By similarity).
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20828
Sequence Length: 194
Domain: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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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 subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-AMP synthase activity. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (By similarity).
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20520
Sequence Length: 194
Domain: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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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 ubiquitination and subsequent proteasome-mediated degradation . Protects cells from ER stress-induced apoptosis . Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway . Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS at 'Lys-173' and 'Lys-384', thereby promoting CGAS cyclic GMP-AMP synthase activity . Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 .
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20459
Sequence Length: 192
Domain: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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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) for ubiquitination and subsequent proteasome-mediated degradation (By similarity). Protects cells from ER stress-induced apoptosis (By similarity). Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway (By similarity). Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-AMP synthase activity . Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (By similarity).
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20520
Sequence Length: 192
Domain: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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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): 16348
Sequence Length: 148
Subcellular Location: Secreted
EC: 4.6.1.18
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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].
Sequence Mass (Da): 17644
Sequence Length: 156
Subcellular Location: Secreted
EC: 4.6.1.18
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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): 14273
Sequence Length: 128
Subcellular Location: Secreted
EC: 4.6.1.18
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A1SWZ6 | MFQNNPLLSQLKKQIQEDIPKRQGKVKATDRGYGFLETDKGKRFFIPPSEMKKVLHGDQINAFIRGKGDKSTAEPNQLKKTGSAVFIARLVIKQKNISIIPKNPLLKGFFKIKGSQSLQSRGYQDGDWVKVELVSHALEGNGFLTQIIEKIADASDPFAYRLLTVATHNLANKAPEFDHPWKIIDPQLSRSDLTKTPFFTIDGVNTQDMDDALYIEADENGWKLTVAISDPSAYVPENSDMDAEAKRRAFTLYLPNFNVPMLPRDLSDSLCSLKEGEKRATLCCTIHINKKGEIEGEPAFYGAWIKSHYRLNYTDVSNYLENEELSNDCWKPSTQLAEQLRTLDSLSLKRLQWRTDNNAVFKNQPDYTLKLNNKGEISEILCEPRRSANRLVEESMIAANICAGDFLAKHKQQGVFNTHSGFSSERLGKVVSLLSEFGIESDIQTLATVTGYTKIRQQTNLLHNSYLDHRLRKLLSYADIKNTPEAHFTLGVDHYATWTSPIRKYGDLLNHRLIKSVLLKEDNIQIDNEIGQVLNAARKLQRLAERDVNNILYSQYLKNQVESKWRYKAEIFDIIKAGIRVKIQENGATFFIPCSLLCKDSSDATKIDCNQALGKVIIAQQTELQLGDVIDVMLNNVKVESGQLIGKLAESLTISE | 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: 3.1.13.1
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 27477
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26944
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26252
Sequence Length: 233
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26848
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 27228
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 27279
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 28341
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 25297
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q969K3 | MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS | 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 receptors in the extrinsic pathway of apoptosis . May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation . Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN . Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells . Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation .
PTM: Autoubiquitinated (in vitro).
Location Topology: Peripheral membrane protein
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): 41641
Sequence Length: 372
Domain: The RING-type zinc finger is required for the ubiquitination of target proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell membrane
EC: 2.3.2.27
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Q99KR6 | MKAGATSMWASCCGLLNEVMGTGAVRGQQAGFPGSTGPFRFTPSSDFPTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLLLRNIPTDTCREKEDLVDLVLCHRGLGSGDDLDSSSLNSSRSQTSSFFTQSLFSNYTPPSATVSSFQGELMDRDGAFRSEVLAQVQSEIASANTDDDDDDDDDDDDDEDDDDEQEEEEQNPGLSKKKARASLSDLSSLEEVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERMQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS | 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 receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells . Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.
PTM: Autoubiquitinated (in vitro).
Location Topology: Peripheral membrane protein
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): 42030
Sequence Length: 376
Domain: The RING-type zinc finger is required for the ubiquitination of target proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell membrane
EC: 2.3.2.27
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Q6AYH3 | MKAGATSMWASCCGLLNEVMGTGAVRGQQAGFPGSTGPFRFTPSSDFPTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLLLRNVPTDTCREKEDLVDLVLCHRGLGSGDGLDSRSLSSSRSQTSSFFTQSYFSNYTPPSATVSSFQGELMDREGTFRSEVLTQVQSELASANTDDEDGEEDDDDDDDDDDEDDDEQEENLEEQNPGLSKKKARASLSDLSSLEEVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERMQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS | 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 receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells. Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.
PTM: Proteolytically cleaved by caspases upon induction of apoptosis by TNF.
Location Topology: Peripheral membrane protein
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): 42681
Sequence Length: 381
Domain: The RING-type zinc finger is required for the ubiquitination of target proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell membrane
EC: 2.3.2.27
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O94941 | MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLPHPSLKARIDHFLLQHSIPGCHLLGRAQTALAVIPSSIVLPSQKRKIEQAEHVPDSNFGVNASCFSATSPLVLPTTSEHTAKKMKATNEPSLTHMDCSTGPLSHEQKLSQSLEIALASTLGSMPSFTARLTRGQLQHLGTRGSNTSWRPGTGSEQPGSILGPECASCKRVFSPYFKKEPVYQLPCGHLLCRPCLGEKQRSLPMTCTACQRPVASQDVLRVHF | 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-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 58966
Sequence Length: 541
Domain: The U-box domain mediates interaction with E2 ubiquitin ligases and is required for the ubiquitin-protein ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q9H0F5 | MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQEDAHFKAFFQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPSQHHFSGERCNTPARNRRSPPVRRQRGRRDRLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLPVGGFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPIPPPPYHPSLLPYVLSMLPVPPAVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKANRTCPICRADASEVHRDSE | 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-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 57595
Sequence Length: 515
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q8BI21 | MRESEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPNQHHFSGERCNTPARNRRSPPVRRQRGRRERLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGLPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLQVGSFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPMPPPPYHPSLLPYVLSMLPVPPAVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPSNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKGNRTCPICRADASEVHRDSE | 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-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 52168
Sequence Length: 464
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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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): 36128
Sequence Length: 318
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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 similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control .
PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal degradation. Deubiquitinated by USP8 to get stabilized which induces apoptosis.
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): 35905
Sequence Length: 317
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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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): 35911
Sequence Length: 317
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q8EE78 | MAFKIASSPHVTRNLQTSTVMQRVILCLLPGLVVQCAFFGWGTLIQVLLAIIVALSCEAAVMKLRKRSIKASLGDNSAMLTAILIGVAIPPLAPWWMIVMGTAFAIVIVKHLYGGLGHNLFNPAMAAYVLLLVSFPLQMTTWIAPSTVALNTPSIVDSLQLIFNVGAHVGMEQFRLGIDGISMATPLDTLKTDLSLGLTTTESMAKSIFDGSTGVGWFWVNLAYLAGGIVLLKLKAIRWHISTGVLAGLFVASSVGFLLSPDTHASPLFHLFSGATMLAAFFIATDPVTAATSPRGRIIFGALIGVLVYIIRTQGGYPDAFAFAVLLANLCAPFIDYYVRPRTYGHSAG | 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.-.-.-
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Q9EVN4 | MIRSSVDRIMLHVCLALLPTTAWGLYLFGWPAIYLWLLTCASAVACEAACLYLLGRPLRRLLDGSALLSGWLLALTLPPWAPWWIAVGGSMFAIGIGKQLYGGVGQNVFNPAMLARVALLIAFPLQMTTWALPLPLGTEGAPGWLEGLRITFAGGALADGLSGATALGHLQTELTLGHSAAQILDGHFALLPAFLGYSGGSLGETSELLILLGGLWLLALRIIHWEIPLGMLLTVGALAALANQIDPQVHGGGLFHLTSGGLLLGALFIATDPVTSPISRSGRLIFAIGCGALVFVIRSWGNFPEAVAFAVLLMNALVPLIDRVCRPRAYGRNARGKPLVAAKWTRQVKEVDKV | 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.-.-.-
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A5F2R1 | MAFFIASSPHLRSKRSTADVMRWVLVCALPGLIAQTYFFGYGTLIQLLLAISVAVALEAGIMLLRKRSPISALRDYSAVVTAWLLAVAIPPLSPWWVVVIGLIFAIVIAKHLYGGLGQNPFNPAMIAYVVLLISFPVQMTSWMAPIKLTAEPSSLVDSFSLIFGGFDSDGLSLQQIRTGIDGITMATPLDAIKTSLKAGHTMSETLTQPQFSGFAGIGWEWVNIAYLLGGLILLKLRIIRWHIPVAMLAGLVFTALLAQLFAPGTTASPMIHLLSGATMLGAFFIATDPVSASTTDKGRLIYGFFIGAMVFLIRSWGGFPDGVAFAVLLANMCVPLIDYYTKPRTYGH | 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.-.-.-
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Q87MX1 | MSFFIASSPHAHSRRSTPDLMKWVALCAIPGLAAQTYYFGWGTLIQLIFAIAVAVSLEALVMICRKRSPMRALRDNSAIVTAWLLAVAIPPWSPWWIIVIGLIFAIVIAKHLYGGIGQNLFNPAMVAYVVLLISFPVQMTSWSAPTLLIPDHVNFADTLSLIFTGFDYDGLSLQQVRAGVDGVTMATPLDAFKTGIHTGATPSEVLSQPIFGGLAGIGWQWVNIAYLIGGLVMIKKRIIQWYIPAGFLASLTLFSLIFSVITPGETASPIFHLLSGATMLGAFFIATDPVSASTTVKGRLIFGALIGALVFIIRSWGGFPDGVAFAVLLANMCVPLIDYYTKPRTYGH | 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.-.-.-
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Q6NZ21 | MKLRAQFDRGTYSESKGSFKLRDSLDPMQPEPSSREGNGLSLTLQPELLARMPGAGSSSGTETGEDVRVPMGSSSGSTNGRGATSRRMRTASHSHSHTHGHGHSHEHESDSGESDLESGESSSSISELRYLLRWLKKSLPFIVILCAKLVIQHALGLAVAVGLFTTFMYVNKSIQTQVFLHDRRTNLHCAWLLLFLTSSSLLVFYTFHTQSLYRCLFFANATIDYHNFWEVLWSVGVTNFILKFIFMGFKCLILLVPCPLMTYRRRGQWYMLIEEVGQLYQVIAPVPLWFRYLVSYDEMDTSVGLTLGILLALLYLIMKLLALYGLSGSLQKTLRTFFSPEVNGAPASPAQIREAGDICPICQADFKQPRVLVCQHIFCEECIAQWLNQERTCPLCRTVITDKVHKWKDGATSAHLQIY | 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.
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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47191
Sequence Length: 419
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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