ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q0VRF1 | MAERGQSSSAEGGASSQLVVVGRILGVHGVKGWVKVYSYTDPMVNLQQYQPWHLKQGALNSGGSSAAGTWKPVKVTGFRPQGKGLIAQLEGVSDREAAAALVGQDIGVPADLLPQSGQGEYYWRDLIGLRVKHVNGMDLGSVTRMVETGANDVVVVRGDRNSLDRRERLIPWLPEDVITAISLEDGEMTVDWDPDF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21185
Sequence Length: 196
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A8EW70 | MSMNSNVYVAKLGKTVGLQGHLRLFIDSDFPEQFKKGVTFTTNRNLQLKVLEYNSSRELVKFENYEDVELAKKLTNQELYATIEQTKENCKLAKNEFFWFDLISCEVFENNLKLGTVKEIHRYPLNDYLEIITDSELVKKALPKNFLIPHIFDKFILNIDIENKRIDVINSFDILENS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20878
Sequence Length: 178
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q5WFN5 | MTNWYNVGRLVNTHGVRGEVRVLSNTDFPEERYANGSVLKVAKSPQAEGTLVTVRSHRTHKNFDLLTFEGYNSINEVECFKGSYLYVSEDQLSELDEHEYYYHEIIGCTVVDEEGTKLGKIKDIIETGANDVWVVDRQQRKDLLLPYIEEVVKEVDVENKRIRVHIMEGLDDE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19981
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A6TRS7 | MKKMLKVGQIVNTHGIKGELKVTSLSDYLERFEELEWVYIQGYDEKYYIGNIKYRPTTVILSFEGYDNINIVEQFKGKYVLIDESQRRELPEDTFYKADLIGLDGYTVEEVYLGKLVDIIQAGSNEVYVFRDKETNKDILIPAVKEFIPEISLEKKRITVDPIEGMIE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19574
Sequence Length: 168
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A8MHC3 | MAKMLRVGKITNTHGIKGDLKVLPLTDYFERFEELEWVYIEGFKDKFYIENIKYKPTLVILSFEGYGDINLVEKFKDRYLLIDESQRRILPEDTYYIADIIGLDVFTVKDEYIGKVVDIIQTGSSEVYVIRMNNLKEIMIPSVKEFMPEISLEKKRITIDPIEGMIE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19617
Sequence Length: 167
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B3ERZ2 | MNKNCVEVGKITQARGLKGCVVARIEPILESFDPINYIFIKIGHTLVPYQVEEITGQAQQVFIKFQHISDRDSVRELIGSSIWLSQEILDKLVVQEEPYIDIIGYQVTDKYQGELGIIKDIEQFPLHVCLVVDYLDKELLIPYEPALIQDLDHEQKKIIVELPMGFLEAMGCK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19787
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A7HBQ0 | MARIRLGKVVRAVGLKGHLGVAGSEGALATVRRIALRREGEPEPPLQEVLEARPQGRLWAVRIEGVSDRTSAEAWVGAEVLALREDLPEAGEARHYWADLEGLPVVTVAGAAIGTVTGLYETGGVDVLVVTTEEGGEKLVPLAPYVEVDVAGRRVVVDPPEGLLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 17456
Sequence Length: 165
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q5P9G0 | MVRGDMVLLGVVRAPHGVMGLVKVRTFTEDPSHISAYGPLTDGHNCFNVTVVSVLGADSVIAKFDGLSSRTESEKLRGKRLYVSRSSLPRLQEDEFYENELIGMDAKLEDGTAYGVISAILNFGSCDIIELSTSTGKVVMVPFSRSTFPVVDVERRVVIVVPPEVIGVGSR | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18531
Sequence Length: 171
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q2GIL4 | MNIDDTFILLGVIYAAHGVRGCVKIKTFTHDPSDIAAYGPLTDGSESLKVSVMSVIKNGCVIAKISGIDDRCSAEALKNKKLYVSSSCLPKLKNDEFYKDELIGLSVKLPDDTIFGIVTEVFNFGSGDIVEISTPQGKKEMFSFTSNIFPSIDMKTREMTIVPPEIVGVYK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18681
Sequence Length: 171
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q72DU2 | MEASRFIEIGLLTRPHGLKGEVCVDYYADSPFLLEGTVYLKAGRAAPRPVKVQSMRMHKGRPLVIFEGVNDRTAAELLRGHVMLVPEDTLPELDEDEVYLFELEGISVVIDESGEHLGVIERIDTDAYQEIWVIRTPQGKEVLFPAAAPFVLDIDLDSRTARIAPPPGLLDIYLSD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19629
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A5EXZ2 | MKAQPTLIALGRIIGVHGVRGWVKIHSECRPREAIFNYSVFQATRHHHAQTLKLLDARRSGKSLIALFADICDRDAALQLNGFTLNVTRADLPQLKNGQYYWTDVLGLTVINRSGEHLGKVCDIFETGANDVLVINKDGQEYLIPFISERYIDRIDFENKYLYVDWQMAWTDDAD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20010
Sequence Length: 175
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A1AN01 | MIDSESLIPVGKLVATHGIRGMLKLHSYSGSVESLCTCDSVILRSRDGALNRFEPKPVLPRPGKFLIGFKGVDHIDQAQTLVGSEICLRRDQLPEPEEDEYYWCDLIGLEVATVEGMALGVLEEIFKAGSSDIYVVRGAGREYLIPAIADVIHSVDLEMGRMLITPLEGLLDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18982
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A9BF00 | MNSLSNLLDNKISVAKIVNSHGVHGEVKIVPFTNVKDVITNLEEVLLYNTSTRNFFFSKVLQVKPLNKFFVLNLRGIKDMDEAKKMIGYEVFIDKKDLPSLNSEEYYWYEILDSEVYYEDGEYVGKVEEIIQTGANDVISIKNLEDDKEVLIPMTDHYIIELKKEDKSIIVKKIEWYENGTNQAD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21451
Sequence Length: 185
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A6L0W6 | MIKKDEVFKIGIFNKPHGVKGEISFTFTDDIFDRVECEYLVCLLDGIFVPFFIEEYRFRSDTTALVKLEGVDTSEKARMFTNVEVYFPKKYVGEEEDSDDIPTWNYFIGFKVEDVNHGELGEIVAVDDSTMNVLFAIEKGGEELLLPAHEEFITKLDKKKRLLTVEVPDGLI | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19761
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A4SW74 | MSTPSLDNLIELGAISEAQGLQGQVKVRPHSPDPVALLSSKVVWLSLLPRRSAGALSSTEEATLTQYKVKSAKMHSGNVVLTLDGVSDRDQALALKGARILLDRDAFPKAESDSYYWVDLIGCKAKNLQDEILGDVIDVTENGAHGVIAIGDISTKTIQYLVPFVKEVVRNVDLPNKLLTLDWQSDWV | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20464
Sequence Length: 188
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A1VM98 | MRPGLQPSLGLTSSSLPDDALEVGRILDAWGVKGWVKILPHSTDPEALFSAKTWYLQTPDVKFRPGFSLFSGTVSLKVDEAKIHSGAVVAKFSGLDDRDAAEALRGARIFLSRSSFPAASADEYYWVDLIGLNVLNREGVALGCVRDLMATGPHSVLCVEYASTQEDGTSATAERMIPFVAAYVDKVDIAGKCITVDWQPDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21871
Sequence Length: 202
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q12CW5 | MGANSSSPAGLTPSSLPDDAIEVGRILDAWGVKGWVKILPHSTDPEALFSAKSWFLQAPEAKFRPGFNAFSGTVLLSVDEAKTHSDTVVAKFSGQDDRNAAEALRGARIFLPRSSFPVASKDEYYWVDLIGLNVVNREGVPLGQVRDLMTTGPHSVLCVEYTAQQEDGTAVTAERMIPFVSAYIDTVDIAGKCITVDWQPDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21908
Sequence Length: 202
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q7MUW2 | MIDLDSLEHIGVLGKPHGVQGECNARLTADLSTLFEEEERLFLFFELDALPVPFRLIGYREKTDDITLLRFAGIESKEEMEQYTGVSLFMERRYFDTDSIEFTWEHFIGFTVFDREGCFVGTIDDVDESTLNVLLSITTPEGKELLLPVAEDLLEEIDVPNRKLTMIIPDGLLQL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20025
Sequence Length: 175
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q9X1Q4 | MIRTIQDLLNERVAIGKIVNTHGLKGEVKFFPYTNSEEIVKNLSSVVLYNSEKKAFYNLTVESVRRMNKLFLIRFKSIDTIEAAERIKGCEVFIKYEELPKLSEDEYYFYEILDCDVFYESGENVGKVVDIIETGSNDVLVVRKKKKETLIPMTKDCIVEIDKGAKKIIAKEMEWI | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20419
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q5SJH5 | MRLVEIGRFGAPYALKGGLRFRGEPVVLHLERVYVEGHGWRAIEDLYRVGEELVVHLAGVTDRTLAEALVGLRVYAEVADLPPLEEGRYYYFALIGLPVYVEGRQVGEVVDILDAGAQDVLIIRGVGERLRDRAERLVPLQAPYVRVEEGSIHVDPIPGLFD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18073
Sequence Length: 162
Domain: The isolated N-terminus (residues 1-80) forms a closed, 6-stranded beta barrel; it probably has the same form in full-length protein . The PRC barrel domain binds ribosomal protein uS19 (By similarity).
Subcellular Location: Cytoplasm
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Q8DK05 | MVTPFPEVSEWLCIGQIVGAHGLRGEVKVKPFSDFPERFTVPGCRWLRSPRQPQPYAVTLLRGRFLPRAEQFVVTFAEISDRTAAEALKGAEILVPASDRPPLAANEYHLMDLIGLAVYHQGERVGEVVGLVNAGNDLLEVQLLDPAPKAPQSVYIPFVPAIVPVVDLAARRIEIDPPLGLLP | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20047
Sequence Length: 183
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q3SGC3 | MAPSCPTRSRVWSSRTSPPPDLAESEAWVVMGRVSAPFGVKGWVKVQPFSEDPGTLMDFESWRVGRGEQQAQYAVEAVQDHGKSLVAKLVGIDDRDAAFALRGQEVSVAKSALPPPEENEFYWSDLIGLTVMNREGVELGKVDSLMESGAHDLLVVKGRREHLIPFVAAFVGKVDLAGGTVEVDWGEDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20643
Sequence Length: 189
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q73PB6 | MDLLATGRIRGTFGIEGFVKVESFSGEYEHFLGFDRVFLSILKEKLREQKYKDGWFEIEEVNLRKADALVKFKGIDNPEAAKCLTGSELFIPRDKAAPLDEGEVYVHDLCNCNLVCEGTLVGKITSVAEGGGGYLLEIAGKTSEAAAESSFYVPFNKEFIGKIDLKAKTVELMHRWILE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19977
Sequence Length: 179
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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O83877 | MTARIVSTFGVAGLLRLKSFSGEYAHLATLKQVCLAPPRSRSSGTLACALPREAVHMVEHVLLRAQDALLKLHRVDTVECARTFVGAELRVPRAEACPLSAGEFYLADLCRCELVFEGSAVGVVLSVVEGGGSSLLEVQRTHGGVCYVPFHRTFIGDVDVGRKKIELLQRWILE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18945
Sequence Length: 174
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q10VX5 | MSEWIEIGKIVAPQGLKGDLRVYPSSDFPERFTEPGKRWLLSPGQVEPISIELLSGRYVPGKGLYVIELAGIKSRQQAEALRNSQLLIEKGDRPQLEADEFYVPDLIGLTVINQLNGKTIGKVINIIFAGNDLLEVEKISTDTPVISEVVENNLPSKSKRSRDTKNQKKNQSPPSKKILIPFVKEIVPIVNFEQSIIEITPPDGLIDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 23153
Sequence Length: 208
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B0TIH8 | MDGALFLLRGRTEAILTMKIHITSLGCAKNRVDTEVMMGLLREAGYELTQREEDAHVLLVNTCGFILPAKEESIQTILELARYKETGRCRALLVAGCLPQGYAGELAAELPEVDAFFGPGDVPRVTSIVAEVLRGKRSLEVGKPDFLYDHTMPRVLSTPFHYAYVKIADGCDNRCGYCAIPNLRGRFRSRSEESIVEETRSLVDRGIQEALLIAQDTTCYGVDRYGEFRLAQLIGKLASIDGLRWIRLMYCYPSHFTPELIEAMAAEPKVCRYVDLPLQHADDELLRSMNRHAGVDEIRRLIRTLRERLPGLAIRTSFIVGLPGETEEKFQRLLDFLAEMRFDRVGIFTYSREENTPAGKLADQVPEEVKEERYHRAMVLQQEISLSIQQEWIGKTLEVLVEEEVAPGLYRGRSEREAPEVDGHIEFKGRHRMIGEWANVRITAASHYDLMGEAIDEPGE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52105
Sequence Length: 460
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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O25434 | MQVKENKQLCLISLGCSKNLVDSEVMLGKLYNYTLTNDAKSADVILINTCGFIESAKQESIQTILNAAKDKKEGAILIASGCLSERYKDEIKELIPEVDIFTGVGDYDKIDIMIAKKQNQFSEQVFLSEHYNARIITGSSVHAYVKISEGCNQKCSFCAIPSFKGKLQSRELDSILKEVENLALKGYTDMTFIAQDSSSFLYDKGQKDGLIQLIRAIDKQQALKSARILYLYPSSTTLELIGAIESSPIFQNYFDMPIQHISDSMLKKMRRNSSQAHHLKLLDAMKQVKESFIRSTIIVGHPEENESEFEELSAFLDEFQFDRLNIFAFSAEENTHAYSLEKVPKKTINARIKALNKIALKHQNHSFKALLNKPIKALVENKEGEYFYKARDLRWAPEVDGEILINDSELTTPLKPGHYTIAPSEFKDNILLAKVLSPF | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49634
Sequence Length: 439
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A6W833 | MPPTSGTSRSVALVTLGCARNDVDSEELAGRLADAGWTLVDDADGADVAVVNTCGFVEQAKKDSIDTVLAAADLKEAGRTKAVVAVGCMAERYGKDLAESLPEADAILGFDSYGDLSSHLEAILHGEKPQSHVPRDRRTLLPLAPAERQAARPVIAEPDLPEGLAPASGPRVVRRRLGSGPWAPVKIAAGCDRRCTFCAIPAFRGSFVSRPAEEVLAETRWLAEQGVKEVFLVSENTTSYGKDLGDLRALEALLPHVAAVEGIERVRVSYLQPAEVRPGLLDALTSTPGVVPYFDLSFQHSSPAVLRRMRRFGGTEPFLALLEQVRERHPQAGIRSNVIVGFPGETEADVDELCSFLERARLDVVGVFGYSDEDGTEAETLDGKLPDEVVAARVDRVTRLVEELVTQRAEERLGEVVEVLVESVVDEDGDPHVVGRAAHQGPDVDGETELDLPAGFVVHVGDLVTARVTGVAGADLLAEPLVRATV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51946
Sequence Length: 486
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q1IPQ5 | MPETKSSVSTLEQPETKPKKVGFVSLGCPKNLVDSEVMMGLLATNGAEITARAEDADIIVVNTCSFIDTAKQESVDTILEMAGHKATGRAQKLIVAGCLVERYRNEIQKNIPEVDAVVGTGELEAILAASGIEPRKSEANSPFVILNSTSASQQLKSGIADRPEGAAREEAGRFARTDWDGAVADLPNYLYDENTPRVLATPKYMAYIKVAEGCDHPCSFCIIPQLRGKFRSRRFESVVAEAERLAKQGVKEITLIGQDTTCYGEDLGLKDGLAQLLERLAQIEELQWVRFLYAYPNKITKRLLQTIADNPKIPKYMDVPLQHSAANVLKRMKRGAHGDIFLKSIEEMRRVIPDLTLRTSFIVGFPGETEEDFNQLCEFVKAAQIDWLGVFSYSDEEGAKAFALDEKVPPREIERRRKKLMSLQKQISKKKRKALIGREFDVILEGPSEETDLLWEGRTAMHAPEIDGKVYINDFAEHENVEPGQVFRCEITEAHDYDLVARLL | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 56293
Sequence Length: 504
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q5SJ39 | MAKIGFVSLGCPKALVDSEQILSRLKALGYETSPSYEEAELVIVNTCGFINEAVEESLEVIGEALKENGKVVVTGCLGARPEKIRERHPQVLAITGPGEVERVLEAVQVVLPAPRDPFLDLIPPQVKLTPRHYAYVKLSEGCDHRCSFCIIPKLRGRLRSRDAADVLAEAARLVATGTKELLLVAQDLSAYGVDLGHRESLWGDRPVRAELKDLLAHMAELGAWIRLHYVYPYPHVKDLLPLMAEGKVLPYLDVPLQHASPRILRLMRRPGGYESHLKALKAWREVVPELALRSTFIVGFPGETEEDFQILLDFLEEAELDRVGVFAYSPVEGAEANRLPDPVPEEVKEERKARLLELQARVSLRKNQRFVGKTLEVLVDELPEPGLAVGRTYRDSPGIDGVVYVETDGTVRVGERIPVRILRADTYDLHGVQA | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48283
Sequence Length: 434
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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B5YKD1 | MKNFTVITLGCPKNTVDSRHLIDALTKEGFYYVEEFKKADFVFINTCCFINDAKEESIDEILTAAKFKIDRKLIVFGCLSKRYGKELEKEIPEIDAVFGVDEKDKIIDYIKQFSKNSNFISQNFQYTVEPPSYRYIKIAEGCSRRCSFCIIPDVRGPFRSLNPEEILKEVENFVHSGIKEFILVAQDITQYGKDLKGYTLKRLLKDLCSIKGDFWIRLLYLYPSDIDENLIETIADEEKIVKYLDIPMQHSEERILRLMGRRGTKKEYLKKIKQIRQAIPEVTLRSTFIVGFPTETEEEFQRLVDFIEEVQFDRLGVFKYSKEEGTKAYSLKGQIPENVKNRRYNEIMARQAVISLEKNRALIGKKYEALIDYIDADIAIARLYCHAPEIDGVVILENTADLKAGEKVTILITEGYEYDVKGVIV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49257
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q73JG6 | MDLHGCAKNQVDAELIIGIMENLSWKNTSDPDEADLIIVNSCGFINSAKEESINAVLQAKAAHPKAKVLLAGCLAERYADILKNDLPEADGIFGNGNLSLLPQLIDSMFPKKTSDEKFIEKTLVPPQIGICGGERPKILNFPRSTYIKITEGCDNFCSFCAIPIIRGRLRSRPIKDICDEIKTFLKKSFYEFNLIGQDLAAYQTGKDDLSEDELHRENCSGLALLLKSISKIKGNFKIRLLYIHPDHFPLDILPIMTADKRFLPYFDIPFQSGAQKIIRAMNRNGAAEVYLDIIKNIREAFEKTNSPYGEPQIRTTFLVGFPGETDEDFNETIKFLKELRPLWSGGFTYSREEDTPSYSFKGKVPKKTAEARLAEIQNAQTSITEKKLDSFIGKEIEVLVEELIQAEDKTFLALGRAWFQAPEVDGAVVLNFNLNKKDIDGNPIAPGSIVKARIAARNGFDLEAVAV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52131
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A1WMV5 | MTTMTAERAPRIGMVSLGCPKALTDSELILTQLSAEGYETSKTFQGADLVIVNTCGFIDDAVKESLDTIGEALAENGKVIVTGCLGARTGADGGNMVRQLHPSVLAVTGPQATQQVLDAVHRNLPKPHDPFIDLVPGGMGIAGLKLTPRHYAYLKISEGCNHRCTFCIIPTLRGALVSRPIGAVLNEARALFAGGVKELLVISQDSSAYGVDMQYRTGFWDGQPLKTRLLELVQALGALAEPYGAWVRLHYVYPYPSVDALIPLMAQGRVLPYLDVPLQHSHPEVLRRMKRPASGERNLERIQRWREVCPEIVIRSSFIVGFPGETQAEFEHLLDFLRAARIDRVGCFAYSDVSGAVANDLPGMLPMPLRQERRARFMAVAEALSSAKLQRRVGATMQVLIDAAPGLGRKGGVGRSYADAPEIDGAVHLLPPEKISKTLKVGEFTQARIVGVRGHDLLAQPI | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50124
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q9ZEN7 | MSKKLHLISLGCTKNLVDSEVMLGRLKSYEITPLIEKADVIIVNTCGFIEAAKQESLSVLFEALERRKKGAILVASGCLSERYHEELLREIPEIDIITGVGDYDKIDQMVRERQGFHSGEVFLASEEQERVITGSSVHAYVKLSEGCNQTCSFCAIPQFKGKLHSRTLESTLKEVKNLIAKGFTDFSFIAQDTSSYLRDRGEKEGLIQLIGALDSLEGIKSARILYLYPSTASAKLIQAIQKSQVVQNYFDMPLQHIAESMLKRMKRGANQKKHKELLERMRQVPHSFVRTTLILGHPGESEEEFEELCRFLEEFRFDRVNLFAYSDEEGTSAHKMEGKLDKRVINARLKRLDKIIQKQHRALLKEMVGQEIPVILEGGSSEHEFFYSARDARWAPEIDGEILINETLLPQPAPGHYWAKITQVAGKQLLATLTRRWEK | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49941
Sequence Length: 439
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q8IUF8 | MPKKAKPTGSGKEEGPAPCKQMKLEAAGGPSALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSLFKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHYDDVEVFILQLEGEKHWRLYHPTVPLAREYSVEAEERIGRPVHEFMLKPGDLLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTAKEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDMKKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPDQDQSDEAQEKMVYIYHSLKNSRETHMMGNEEETEFHGLRFPLSHLDALKQIWNSPAISVKDLKLTTDEEKESLVLSLWTECLIQVV | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Catalytic Activity: 2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L-histidyl-[protein] + CO2 + succinate
Sequence Mass (Da): 52800
Sequence Length: 465
Subcellular Location: Nucleus
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P24476 | MKIYLVAAIAWILFQSSSWTTDAATAYTLNLANPSASQYSSFLDQIRNNVRDTSLIYGGTDVAVIGAPSTTDKFLRLNFQGPRGTVSLGLRRENLYVVAYLAMDNANVNRAYYFKNQITSAELTALFPEVVVANQKQLEYGEDYQAIEKNAKITTGDQSRKELGLGINLLITMIDGVNKKVRVVKDEARFLLIAIQMTAEAARFRYIQNLVTKNFPNKFDSENKVIQFQVSWSKISTAIFGDCKNGVFNKDYDFGFGKVRQAKDLQMGLLKYLGRPKSSSIEANSTDDTADVL | Function: Single-chain ribosome-inactivating protein.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 32717
Sequence Length: 293
EC: 3.2.2.22
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Q68A49 | MRIGKSSGWLNESVSLEYEHVSPPTRPRDTRRRPRAASDGGLAHLHRRLAVGYAEDTPRTGARSPAPRRPLPVAPASAPPAPSLVPEPPMPVSLPVVSSPRFSAGSSAAITDPFSSLPPTPVLYAMARELKALSDATWQPAVPLPAEPPTDARRGNTVFDEASASSPVIASACPQAFASPPRAPRSARARRARTGGDAWPAPTFLSRPSSSRIGRDVFGKLVALGYSREQIRKLKQESLSEIAKYHTTLTGQGFTHADICRISRRRQSLRVVARNYPELAAALPELTRAHIVDIARQRSGDLALQALLPVATALTAAPLRLSASQIATVAQYGERPAIQALYRLRRKLTRAPLHLTPQQVVAIASHDGGKPALEAVWAKLPVLRGVPYALSTAQVVAIACISGQQALEAIEAHMPTLRQAPHSLSPERVAAIACIGGRSAVEAVRQGLPVKAIRRIRREKAPVAGPPPASLGPTPQELVAVLHFFRAHQQPRQAFVDALAAFQTTRPALLRLLSSVGVTEIEALGGTIPDATERWQRLLGRLGFRPATGAAAPSPDSLQGFAQSLERTLGSPGMAGQSACSPHRKRPAETAIAPRSIRRRPNNAGQPSEPWPDQLAWLQRRKRTARSHIRADSAASVPANLHLGTRAQFTPDRLRAEPGPIMQAHTSPASVSFGSHVAFEPGLPDPGTPTSADLASFEAEPFGVGPLDFHLDWLLQILEA | Function: Does not activate plant gene transcription, because it has too few core repeats.
Sequence Mass (Da): 77065
Sequence Length: 720
Domain: There are at least 4 possible nuclear localization signals, both N- and C-terminal regions contribute to nuclear localization.
Subcellular Location: Secreted
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P33185 | MIKLLVLWLLILTIFLKSPTVEGDVSFRLSGATTTSYGVFIKNLREALPYERKVYNIPLLRSSISGSGRYTLLHLTNYADETISVAVDVTNVYIMGYLAGDVSYFFNEASATEAAKFVFKDAKKKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLYYYTASSAASALLVLIQSTAESARYKFIEQQIGKRVDKTFLPSLATISLENNWSALSKQIQIASTNNGQFESPVVLIDGNNQRVSITNASARVVTSNIALLLNRNNIAAIGEDISMTLIGFEHGLYGI | Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells.
PTM: Appears to undergo proteolytic cleavage in the C-terminal to produce a shorter protein.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 31789
Sequence Length: 290
EC: 3.2.2.22
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Q5F0I3 | MRVARFCTVVAILLYFGFHIAECDINFSLAGADGQTYNTFIAKLRQELSIGTQKVANITVLKHHVSSNTQRFLSINLFNYNGDKITLGIDVFDVYVVGFLTGTNSYIFKEAPDLAYNKSLLFPGSVRENLSYTGGYDDLERRGAGREDIPLGLLPLDTAITNLFRRDSTSFRRSFIVIIQMVSEAARFKIIEAKIAKNLYGENTFKPDQAIISLENNWGALSKQIQKAQDRGGVFPNLVTLTTSSGKPLIIRNDSDPLVQNGIALLKYMSERSVEYSITDDTVNESNGAFLEIMEIHDLM | Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 33505
Sequence Length: 300
EC: 3.2.2.22
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P56568 | PRGSPRTEYEACRVRCQVAEHGVERQRRCQQVCEKRLREREGRREVD | Function: Inhibits protein synthesis in animal cells.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 5698
Sequence Length: 47
EC: 3.2.2.22
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Q40372 | MASSSPCQIFLVFVMVTLVTSLIPSNALLTPHFYDNVCPQALPTIKSVVLHAILREKRIGASLLRLHFHDCFVNGCDGSVLLDDTPNFTGEKTALPNINSIRGFSVVDEIKAAVDKVCKGPVVSCADILATAARDSVAILGGPQFFYNVLLGRRDARTASKAAANANLPSPTFNFSQLISNFKSQGLNVKDLVALSGGHTIGFARCTTFRNRIYNETNIDPIFAASLRKTCPRNGGDNNLTPLDFTPTRVENTYYRDLLYKRGVLHSDQQLFKGQGSESDKLVQLYSKNTFAFASDFKTSLIKMGNIKPLTGRQGEIRLNCRRVR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 35682
Sequence Length: 325
Subcellular Location: Secreted
EC: 1.11.1.7
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P50620 | MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAGRKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQMGQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMNEMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYESPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKKLKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 80689
Sequence Length: 700
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P32282 | MQLINVIKSSGVSQSFDPQKIIKVLSWAAEGTSVDPYELYENIKSYLRDGMTTDDIQTIVIKAAANSISVEEPDYQYVAARCLMFALRKHVYGQYEPRSFIDHISYCVNAGKYDPELLSKYSAEEITFLESKIKHERDMEFTYSGAMQLKEKYLVKDKTTGQIYETPQFAFMTIGMALHQDEPVDRLKHVIRFYEAVSTRQISLPTPIMAGCRTPTRQFSSCVVIEAGDSLKSINKASASIVEYISKRAGIGINVGMIRAEGSKIGMGEVRHTGVIPFWKHFQTAVKSCSQGGIRGGAATAYYPIWHLEVENLLVLKNNKGVEENRIRHMDYGVQLNDLMMERFGKNDYITLFSPHEMGGELYYSYFKDQDRFRELYEAAEKDPNIRKKRIKARELFELLMTERSGTARIYVQFIDNTNNYTPFIREKAPIRQSNLCCEIAIPTNDVNSPDAEIGLCTLSAFVLDNFDWQDQDKINELAEVQVRALDNLLDYQGYPVPEAEKAKKRRNLGVGVTNYAAWLASNFASYEDANDLTHELFERLQYGLIKASIKLAKEKGPSEYYSDTRWSRGELPIDWYNKKIDQIAAPKYVCDWSALREDLKLFGIRNSTLSALMPCESSSQVSNSTNGYEPPRGPVSVKESKEGSFNQVVPNIEHNIDLYDYTWKLAKKGNKPYLTQVAIMLKWVCQSASANTYYDPQIFPKGKVPMSIMIDDMLYGWYYGIKNFYYHNTRDGSGTDDYEIETPKADDCAACKL | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 85973
Sequence Length: 754
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P0C702 | MATTSHVEHELLSKLIDELKVKANSDPEADVLAGRLLHRLKAESVTHTVAEYLEVFSDKFYDEEFFQMHRDELETRVSAFAQSPAYERIVSSGYLSALRYYDTYLYVGRSGKQESVQHFYMRLAGFCASTTCLYAGLRAALQRARPEIESDMEVFDYYFEHLTSQTVCCSTPFMRFAGVENSTLASCILTTPDLSSEWDVTQALYRHLGRYLFQRAGVGVGVTGAGQDGKHISLLMRMINSHVEYHNYGCKRPVSVAAYMEPWHSQIFKFLETKLPENHERCPGIFTGLFVPELFFKLFRDTPWSDWYLFDPKDAGDLERLYGEEFEREYYRLVTAGKFCGRVSIKSLMFSIVNCAVKAGSPFILLKEACNAHFWRDLQGEAMNAANLCAEVLQPSRKSVATCNLANICLPRCLVNAPLAVRAQRADTQGDELLLALPRLSVTLPGEGAVGDGFSLARLRDATQCATFVVACSILQGSPTYDSRDMASMGLGVQGLADVFADLGWQYTDPPSRSLNKEIFEHMYFTALCTSSLIGLHTRKIFPGFKQSKYAGGWFHWHDWAGTDLSIPREIWSRLSERIVRDGLFNSQFIALMPTSGCAQVTGCSDAFYPFYANASTKVTNKEEALRPNRSFWRHVRLDDREALNLVGGRVSCLPEALRQRYLRFQTAFDYNQEDLIQMSRDRAPFVDQSQSHSLFLREEDAARASTLANLLVRSYELGLKTIMYYCRIEKAADLGVMECKASAALSVPREEQNERSPAEQMPPRPMEPAQVAGPVDIMSKGPGEGPGGWCVPGGLEVCYKYRQLFSEDDLLETDGFTERACESCQ | Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 93031
Sequence Length: 826
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P36603 | MGLEHLEEFSYPKEHGEEVEYDSEQGVRKIYVKSIKETFNFDNVSEEEKQEGGDYYLGKKEDELDEVVLRPNPHRFVLFPIKYHEIWQFYKKAEASFWTAEEIDLSKDLVDWDNKLNADERYFISTVLAYFAASDGIVNENLLERFSSEVQIPEARCVYGFQIMIENIHSETYSLLLDTYIREPKEKQRHFDAILTMGSIKAKAKWALRWINDEDSTYAIRLVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELICRDEGLHTDFACLMFSHLKHRPGRKVVEAIIVEAVDIEKEYFTDALPVSLLGMNKDLMCQYIEFVADRLLVALGNDKYYNVTNPFDFMENISLAGKTNFFEKKVSDYQIAGVMSGTKRAEKDDHTFTIDEDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 45405
Sequence Length: 391
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Nucleus
EC: 1.17.4.1
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P07201 | MLSINTTRKENELSGNLGKMKITEENKPKKVLGEITNFQRSTQKTPLKQEIKPVVKKSQQVEPLLADNPRRFVVLPIQYHDIWKMYKKAEASFWTAEEVDLSKDMAHWESLKKEEKHFISHVLAFFAASDGIVNENLVERFSKEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPQERDFLFNAIETMPCVKEKADWAMRWINDDSSSYAERVVAFAAVEGIFFSGSFASIFWLKKRGIMPGLTFSNELISRDEGLHCDFACLMFSHLVNKPSQERIHQIIDEAVKIEQVFLTEALPCRLIGMNCDLMRQYIEFVADRLLLELKCDKLYNKENPFDFMEHISLEGKTNFFEKRVGEYQKMGVMSGGNTGDSHAFTLDADF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 44447
Sequence Length: 384
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P50645 | MEYFYTSQCPDMDHLRSLSVANRWLETDLPLGDDAKDVAALSEPELEFYRFLFAFLSAADDLVNVNLGSLSELFTQKDILHYYIEQECIEVVHSRVYSAIQLMLFRGDAAARERYVRAALRDEAIRRKVEWLDSRVAECASVAEKYLLMILIEGIFFASSFASISYLRTHNLFVVTCQSNDFISRDEAIHTSASCCIYNNYLGDAPRPDEARIHQLFAEAVEIECEFLRARAPRDSLLLDLPAIISYVRYSADRLLQAIGASPLFGAPAPAADFPMALMVAEKHTNFFERRSTNYTGTVVNDL | Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 34375
Sequence Length: 303
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Host membrane
EC: 1.17.4.1
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P49730 | MPLIPEEPLLASSPDRFCMFPIQYPQIWEMYKKALASFWTAEEVDLSSDTRHWETLTPGERHFITHVLAFFAASDGIVLENLAGRFMKEVQVAEARAFYGFQIAIENIHSEMYSLLLESYIKDSDEKSRLFRAVETNPCVEKKAKWALRWIDGSETFAERLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLRTKLTEERVKGIVADAVEIEREFVCDALPCALVGMNGDLMSKYIEFVADRLLDALGYDKLYNAQNPFDWMELISLQGKTNFFEKRVGEYQKASVMSSLNGNGATHEFKLDEDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 37608
Sequence Length: 329
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Cytoplasm
EC: 1.17.4.1
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O83092 | MMESSTILQRRALFNEAGDIELHKRRMVGGNTTNLNDFNNMKYPWVSKWYRQAMNNFWIPEEINMSSDVQDYRNLSAIEKTAYDKILSFLIFLDSIQTANLPNIGQYITANEINLCLTIQAFQEAVHSQSYSYMLDTICSPEERNDILYQWKDDEHLLARNKFIGNLYNEFQDDKSVLALLKVAIANYVLEGIYFYSGFMFFYNLGRNNKMPGSVQEIRYINRDENTHLWLFRSIIQELQKEEPQVFTARNVRLFRDMIREGCEQEIKWGDYVIGDQIPGLNRHMVADYIRYLGNLRCENLGFEPLYEGHRVEPESMSWVSQYSNANLIKTDFFEAKSTAYAKSSAMVDDL | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 41199
Sequence Length: 351
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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O15910 | MPPKSHKCSRKEGEVEEPLLTENPDRYVIFPIKYPDIWQKYKEAESSIWTVEEIDLGNDMTDWEKLDDGERHFIKHVLAFFAASDGIVLENLAERFMCEVQVPEVRCFYGFQIAMENIHSETYSVLIDTYVVDPDEKQRLLHAIRTIPCIEKKAKWAIEWIGSQTSFPTRLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYEKYIVNKLPRDRVLEIICNAVSIEREFICDALPVRLIGMNSQLMTQYIEFVADRLLVSLGYDRHYNSKNPFDFMDMISLQGKTNFFEKKVGEYQKAGVMSSERSSKVFSLDADF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 39009
Sequence Length: 337
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P11158 | MEPILAPNPNRFVIFPIQYYDIWNMYKKAEASFWTVEEVDISKDINDWNKLTPDEKYFIKHVLAFFAASDGIVNENLAERFCTEVQITEARCFYGFQMAIENIHSEMYSLLIDTYVKDSNEKNYLFNAIETMPCVKKKADWAQKWIHDSAGYGERLIAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLLHPPSEETVRSIITDAVSIEQEFLTAALPVKLIGMNCEMMKTYIEFVADRLISELGFKKIYNVTNPFDFMENISLEGKTNFFEKRVGEYQKMGVMSQEDNHFSLDVDF | Cofactor: Binds 2 iron ions per subunit.
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 36973
Sequence Length: 319
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P09938 | MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALLGMNADLMNQYVEFVADRLLVAFGNKKYYKVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKSTKQEAGAFTFNEDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 46147
Sequence Length: 399
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Nucleus
EC: 1.17.4.1
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Q9DHU2 | MNTSCEPILKPTLNKYVVFPIVYEDIWKMYKKAVASFWTVEEVDLSKDFSDWLKLSDNEKNFIKHILAFFAASDGIVNENLAERFYSEVQISEARCFYGFQIAMENIHSEMYSLLIDTYILDSKEKNYLFNAIENMNCVKQKANWAKKWIESKNRTYGERLVAFAAVEGIFFSGSFAAIFWIKKRGLMPGLTFSNELISRDEGLHCDFACIMFKHLLNPPLNSVVRDIIIEAVNIEKNFLTEAIPVKLIGMNCDLMKQYIEFVADRLLLELGCDKYYCSKNPFDFMENISLEGKTNFFEKRVSEYQKMSVMSNKKDNVFSLDIDF | Cofactor: Binds 2 iron ions per subunit.
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 37836
Sequence Length: 325
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P39452 | MATTTAECLTQETMDYHALNAMLNLYDSAGRIQFDKDRQAVDAFIATHVRPNSVTFSSQQQRLNWLVNEGYYDESVLNRYSRDFVITLFTHAHTSGFRFQTFLGAWKFYTSYTLKTFDGKRYLEDFADRVTMVALTLAQGDETLALQLTDEMLSGRFQPATPTFLNCGKQQRGELVSCFLLRIEDNMESIGRAVNSALQLSKRGGGVAFLLSNLREAGAPIKRIENQSSGVIPVMKMLEDAFSYANQLGARQGAGAVYLHAHHPDILRFLDTKRENADEKIRIKTLSLGVVIPDITFHLAKENAQMALFSPYDVERVYGKPFADVAISQHYDELVADERIRKKYLNARDFFQRLAEIQFESGYPYIMYEDTVNRANPIAGRINMSNLCSEILQVNSASEYDENLDYTRTGHDISCNLGSLNIAHTMDSPDFARTVETAVRGLTAVSDMSHIRSVPSIEAGNAASHAIGLGQMNLHGYLAREGIAYGSPEALDFTNLYFYAITWHALRTSMLLARERGETFAGFKQSRYASGEYFSQYLQGNWQPKTAKVGELFTRSGITLPTREMWAQLRDDVMRYGIYNQNLQAVPPTGSISYINHATSSIHPIVAKVEIRKEGKTGRVYYPAPFMTNENLALYQDAYEIGAEKIIDTYAEATRHVDQGLSLTLFFPDTATTRDINKAQIYAWRKGIKTLYYIRLRQMALEGTEIEGCVSCAL | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 80479
Sequence Length: 714
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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Q9Z733 | MKTLKGHLSAKNLRIAIVGSCFNQAMADALVSGTQETFLKFGGSEDGLMTIRVPGAFEIPCTIKKLLSSERKFDAIVACGVLIQGETDHYNQIVNQVAAGIGALSLEFCLPITLSIVAAPSAEIAWQRSGIKGRHLGVSGMTTAIEMATLFTQI | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16340
Sequence Length: 154
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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A5UMS3 | MAKYNIGAVVAEFNYDITQMMLGLAKEEAKSRDCEITQVVTVPGVFDMALAIKKLLEKDEIDAVITLGAVIEGATDHDQIVAQHASRKIADLSLEYEKPVALGISGPGMTRLDAHKRVDYGKRAVEAAIKMCDRLNEI | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 15089
Sequence Length: 138
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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B0JLM0 | MTVFEGNFTEDISSLRFAIVIGRFNDLVTDKLLSGCQDCLKRHGVDVNPDGTQVDYIWVPGSFEVPMVARQVALSHRYDAVICLGAIIRGQTPHFDYVAAEAAKGIAAAAFQTGVPVVFGILTTDTLQQALERAGIKSNLGWNYGLSALEMASLMRQLRPRNEDKPLELLENNPQQALMEG | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 19839
Sequence Length: 181
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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P66035 | MKGGAGVPDLPSLDASGVRLAIVASSWHGKICDALLDGARKVAAGCGLDDPTVVRVLGAIEIPVVAQELARNHDAVVALGVVIRGQTPHFDYVCDAVTQGLTRVSLDSSTPIANGVLTTNTEEQALDRAGLPTSAEDKGAQATVAALATALTLRELRAHS | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16371
Sequence Length: 160
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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A4TC12 | MSGAGVPDMPALHAEDVTLAIVASTWHETICDALLDGARKVAEQAGVTDPTVVRVLGAIEIPVVAQALARTHDAVIALGVVIRGETPHFDYVCDAVTQGLTRVSLDASTPVANGVLTVNTENQALDRAGLPNSAEDKGAQAAAAALSTALTLRQLASPS | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16227
Sequence Length: 159
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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P73527 | MTVYEGSFTPPARPFRFALVIARFNDLVTEKLLSGCQDCLKRHGIDVDPAGTQVDYIWVPGSFEVPLVTRKLAVSGQYDAIICLGAVIRGQTPHFDFVAGEAAKGIAAIASQTGVPVIFGILTTDTMQQALERAGIKSNHGWGYAMNALEMASLMRAMAPLTEG | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 17617
Sequence Length: 164
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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C5BS85 | MTIKIIEGDFKSATGKYALLVSRWNSFVVEHLKEGALDTLRRHGVSDDDIEIVYAPGAFEFPLAAQKLAASGDYDAIVALGAVIRGGTPHFDYVAGECTKGLAQVSLATGIPVAFGVLTVDSIEQAIERSGTKAGNKGSEAAETALEMVSLLGKL | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16270
Sequence Length: 155
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q5JD31 | MEVRVIEGEFKGEGVKIGVVVARFNDLLTNELLSGALDCFERHSVEEVDVVKVPGSFEIPLVAKKLAESGKYDAVLALGAVVRGETKHFDLVANEVAKGVAKVSLDSGVPVIFGVITVEDELQGFNRAGVKSNKGFEYAMAALEMANLMKKLREKE | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16867
Sequence Length: 156
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q9X2E5 | MKVVQGDYRGEGLKIAVVVPRFNDLVTSKLLEGALDGLKRHGVSDENITVVRIPGSMEAIYTLKRLLDLGVHDAIIVLGAVIRGETYHFNVVANEIGKAVAQFNMTSDIPIVFGVLTTDTLEQALNRAGAKSGNKGFEAAMVAIEMANLRKRLRRDVFESDSNGR | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 17967
Sequence Length: 165
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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P61728 | MKPKTLSPILTAKGVRLAIAVGRFNERVTKLLLEGALEAYARLGGDPAEVLVAWVPGSFELPLVAKRLAQRPDVDAVVALGAVIRGETPHFEYVAGQAASGLMQAMLQTEKPIVFGVLTTNTPEEAQERAGGKAGNKGAEAVFTAIEMVRLLEAISR | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16647
Sequence Length: 157
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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B5YHQ1 | MKIIEGKLEAQGLKFGIIVSRFNEFITSRLLEGAIDALIRHGAIEKDIEIVRVPGSFEIPLIAKKLAQSGRFHAIICLGTLIRGATPHFDYIAAEVSKGIALVSLETSIPVSFGIITADTIEQAIERAGSKSGNKGWDAALVAIEMAKVMGQLK | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16542
Sequence Length: 154
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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P17353 | MLSPKRTRFRKQHRGRMKGISYRGNRICFGRYALQALEPAWITSRQIEAGRRAMTRNARRGGKIWVRIFPDKPVTVRPAETRMGSGKGSPEYWVAVVKPGRILYEISGVAENIARRAVAIAASKMPIRTQFIISG | Function: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus.
PTM: Partially alpha-N-monomethylated at Met-1 (10%), whereas 90% of it is blocked to Edman degradation, probably by trimethylation.
Sequence Mass (Da): 15298
Sequence Length: 135
Subcellular Location: Plastid
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Q52938 | MKWLKGIGLALIPFNLHDYPIALTLGCYLLSCAVIFYTDRFALPARERRKNAPKYGRNRDRIDRLARLPVIALVFAGFFAISWRPLYAAAGTMSFFIIFTGISRAKFKFIREPLVFSDIALVADVFKYKTIFYASSLNIVFWIVAFLYVFGVSALYMYFEPTILPERSRLFWVLVMVGIAAGPWGLLFYGPVNRPTAALVQRLVKAINVKMNTVRFGTFASVVFHFIIWLGVKRDKIVAELSEILRAAVHDLIGHEEAPLIIVWQSESFIDMRHFGVDSIKLPTVDRLRKQAVQWGRLSNVFEGGYTLRTEFAVLSGLVPDDIHVDASYPYLRAAHYADIVWPGKLKRAGWRTHFIHPYDRTFFLRHKAMPLLGFEKLTMLDAFDHKPERDGLYVSDATLAARVLAEVEKLPEEESGFFFVASMANHGPWEPGRVGTLTNPVDIYLAILEQSDAALKQLIDGLNKLDRPVWFVFYGDHAPLLKSFADPFPDPRTDYFIVPLAKARAAAHSPKRAKDEDPWNLLGSMLKHANLHKDALQ | Function: Involved in antigen K (capsular polysaccharide) biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61187
Sequence Length: 538
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
Subcellular Location: Cell membrane
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Q9ZT07 | MKVVFVIFFFFLFQFCISVDTIMRRQSLRDGEVILSAGKRFAFGFFSLGDSELRYVGIWYAQISQQTIVWVANRDHPINDTSGMVKFSNRGNLSVYASDNETELIWSTNVSDSMLEPTLVATLSDLGNLVLFDPVTGRSFWESFDHPTDTFLPFMRLGFTRKDGLDRSLTSWKSHGDPGSGDLILRMERRGFPQLILYKGVTPWWRMGSWTGHRWSGVPEMPIGYIFNNSFVNNEDEVSFTYGVTDASVITRTMVNETGTMHRFTWIARDKRWNDFWSVPKEQCDNYAHCGPNGYCDSPSSKTFECTCLPGFEPKFPRHWFLRDSSGGCTKKKRASICSEKDGFVKLKRMKIPDTSDASVDMNITLKECKQRCLKNCSCVAYASAYHESKRGAIGCLKWHGGMLDARTYLNSGQDFYIRVDKEELARWNRNGLSGKRRVLLILISLIAAVMLLTVILFCVVRERRKSNRHRSSSANFAPVPFDFDESFRFEQDKARNRELPLFDLNTIVAATNNFSSQNKLGAGGFGPVYKGVLQNRMEIAVKRLSRNSGQGMEEFKNEVKLISKLQHRNLVRILGCCVELEEKMLVYEYLPNKSLDYFIFHEEQRAELDWPKRMEIVRGIARGILYLHQDSRLRIIHRDLKASNILLDSEMIPKISDFGMARIFGGNQMEGCTSRVVGTFGYMAPEYAMEGQFSIKSDVYSFGVLMLEIITGKKNSAFHEESSNLVGHIWDLWENGEATEIIDNLMDQETYDEREVMKCIQIGLLCVQENASDRVDMSSVVIMLGHNATNLPNPKHPAFTSARRRGGENGACLKGQTGISVNDVTFSDIQGR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 94891
Sequence Length: 833
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P0CV38 | MRYLLLTFFTFHCQMVADALPRAKRLRLLREAKARKESGEGKIEEAGMIVTTGAPTPENETMEHNEVPQSTTDTDQKSEEIVEKIAQVQEEGANTEDESDEELLNLAPKRANWDMERDIAPMLRKLERRTQHAIVEILRTCDLKQ | Function: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16666
Sequence Length: 145
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
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Q93VT9 | MGRRPARCYRQIKGKPYPKSRYCRGVPDPKIRIYDVGMKRKGVDEFPFCVHLVSWEKENVSSEALEAARIACNKYMVKSAGKDAFHLRIRVHPFHVLRINKMLSCAGADRLQTGMRGAFGKALGTCARVAIGQVLLSVRCKDAHGHHAQEALRRAKFKFPGRQKIIVSRKWGFTKFNRADFTKLRQEKRVVPDGVNAKFLSCHGPLANRQPGSAFLPAHY | Function: Ribosomal protein involved in translational regulation . Contribute to general translation under UV-B stress . Involved in the NIK1-mediated defense response to geminivirus infection . Acts coordinately with LIMYB as a transcriptional repressor .
PTM: Phosphorylated by NIK1 and NIK2 in vitro.
Sequence Mass (Da): 24917
Sequence Length: 220
Subcellular Location: Cytoplasm
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P0CV41 | MRSAYPVLTALLVVASSQIAAGSGHQLQAYDHDRITDDNAVMKSLSTRFLRGSRDVHNNVANEERSVYSVLARMIKKGIKKMPRTAEVLKMKPHIKKASKKSPHEARLVKELFHAAEAKETMQGAREYKKLRRATRAAVEALEKHWNPSKTAVSGDAFHDIHSNQMLSVKKWKFNLTGLKPMVVNDEHHGMIDSVHKAFLTVCDKNVKPTRAETSYLWGLMNWKLAKYPRRSHKESLIEHAQRRVLLDMRKMKATKKVWPEWENLPDSLKFGVLDYLLNLHYQRLVRMYNIFARNRPDRNPAPLNPELNPVGNTGTSAAMAVAENPKGQSPYPSTPLTAASTSKGGRSNLKKRSKRTSDGNTDTASFPSKKLKVRSSKSVMPLLTEPTTSGDHSAPAKKSKSSSSGPSRAFAPDKSGDQTFITENSRLSFDGPSSAVDPFKQSKVHESKSLAPSSSVLTPEDVDTELSLGGIYDRSTYKAPSKP | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 53837
Sequence Length: 484
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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P0CV42 | MRGPCSVITALLVVASSQIAAESDYRLQAYHHDVTAVGNAVVKPLPKRYLRGSQHVLDSNEERSVYSVLASMINEGVSKMPQAAEAVEKMPQAAEAVEKMPQAAEAVEKMPQAAEAVEKMPQAAEAVEKMPSAAMAGKKVSRVTKTGKKMPHAAEIEAVEETLHATNARKEPLRADFVEEMPHAAKAKEEMRRAKQHDLLRATEEADEALEKSWHSSEDTAAIGGASRGISSNVILSLKKWKNNFQGMRAMAVSGEHEDIIKPIHEAFVRLCGENMEPTTKEMTLIRNMLDWDVAASPESSHRQNLVSQAQRHVLIGLRIMQRDPEVWNEWNELSESLRFGVLDYLLNLHYQRWVRMYNIFKRHRPDKKDVPMNDKLSLGGNTDKNSALALQTHSKKQNLYPDEPSNVAWTSKKRDGSVLIERSKRTFNGNTDTASVPYKQLKMQSLKPVMPFLTRSTTSGHHSVSIKNPGLSFDGPIFAFVPPNVHKSQSLTPPLVHKDVDTELSLGGIYDRSTHKAPTVP | Function: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 58121
Sequence Length: 522
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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P0CV43 | MRGAYYVLTALFVVTSSDIAAESDHPLHNFNHHVITAGNAVVKALPNRSLRGSRDGRNDLANEERSISSFLANMIDEGVAKLPLVAEIIKTKPLAAKAVKQKPRAMKKKFRAAKAVEEKSRPAKAAKKTPRAAKAAKKTPPQAKVVDEILYGVEATKEMGKSEEYGVLKAATEGADQALKKHWDPSRETAVIVAPSRDISGNVILSLRKWKVGFNGMRPMVVLDKHKDNIDRVHGAFGTLCDKNMQITPVETSYLWSMLDWNIEKNFKKKHKQTLVRLAQRYVLIGLRQVKKDRKVWNQWKKLPDPLKFGVLNYLLNLHYQRWVRMYNIFRRYRPDQNGVPSTLGGNANINRALALQKHSKVRSVFPYEPFDVAWASKGRRSVLSKRSRRTFDGNTDTASLPSKQLKTRSSESSMPPLIESTTSGDDSVPTKEIKSSFDDPKSAFAPFKPGDDFVHTENSRLSFGGLSSAFVPYRRPNVHNSQSLTSPITVSSMPSLMKSTTSGDGLRPY | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 57055
Sequence Length: 510
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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P0CV71 | MVFLLTALHLSTFLLREMYQIADIFEDHFAIVLFLWSLFLIPSVAVPFMSTRIARDGLLAFNVEHMKVAQVIVQVSRLLRARQTLRTLRFVAEMKIHLRENVRRNNEQVMLNVEEKPQVPLPQAPRRRSSIIPIDATATFKAARRRSSTHLDPLVTAGVLRSIQQTPLPLPVASKATFEPPLSPLAAYLTPRKQRGDAYRREMERREIHTIFCLFDVDGSVCYSQ | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25848
Sequence Length: 225
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
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P0CV72 | MKNVPYLSAVGAIMYLMVVTRPDLAAAVGVLSQFASDPCPTHWQALKRVLRYLQSTQTYGLEFTRAGTAKLVGYSDADWAGDVESRRSTSGYLFKLNGGCVSWRSKKQRTVALSSTEDEYMALSEATQEAVWLTVRTRRTKG | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 15750
Sequence Length: 142
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
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P26784 | MSVEPVVVIDGKGHLVGRLASVVAKQLLNGQKIVVVRAEELNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRIFYKALRGMVSHKTARGKAALERLKVFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEAKRKVSSAEYYAKKRAFTKKVASANATAAESDVAKQLAALGY | Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
PTM: N-terminally acetylated by acetyltransferase NatA.
Sequence Mass (Da): 22201
Sequence Length: 199
Subcellular Location: Cytoplasm
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P26785 | MSQPVVVIDAKDHLLGRLASTIAKQVLNGQKIVVVRAEALNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRILYKAIRGMVSHKTARGKAALERLKIFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEDKRKVRSAEYYAKKRAFTKKVSSASAAASESDVAKQLASFGY | Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
PTM: N-terminally acetylated by acetyltransferase NatA.
Sequence Mass (Da): 22249
Sequence Length: 198
Subcellular Location: Cytoplasm
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P18445 | MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGMHHHRINFDKYHPGYFGKVGMRHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKNGVAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKGVGGACVLVA | Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
PTM: Hydroxylated on His-39 by MINA.
Sequence Mass (Da): 16618
Sequence Length: 148
Subcellular Location: Cytoplasm
|
Q9NSD7 | MQMADAATIATMNKAAGGDKLAELFSLVPDLLEAANTSGNASLQLPDLWWELGLELPDGAPPGHPPGSGGAESADTEARVRILISVVYWVVCALGLAGNLLVLYLMKSMQGWRKSSINLFVTNLALTDFQFVLTLPFWAVENALDFKWPFGKAMCKIVSMVTSMNMYASVFFLTAMSVTRYHSVASALKSHRTRGHGRGDCCGRSLGDSCCFSAKALCVWIWALAALASLPSAIFSTTVKVMGEELCLVRFPDKLLGRDRQFWLGLYHSQKVLLGFVLPLGIIILCYLLLVRFIADRRAAGTKGGAAVAGGRPTGASARRLSKVTKSVTIVVLSFFLCWLPNQALTTWSILIKFNAVPFSQEYFLCQVYAFPVSVCLAHSNSCLNPVLYCLVRREFRKALKSLLWRIASPSITSMRPFTATTKPEHEDQGLQAPAPPHAAAEPDLLYYPPGVVVYSGGRYDLLPSSSAY | Function: Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51124
Sequence Length: 469
Subcellular Location: Cell membrane
|
Q8BGE9 | MQVASATPAATVRKAAAGDELSEFFALTPDLLEVANASGNASLQLQDLWWELGLELPDGAAPGHPPGGGGAESTDTEARVRILISAVYWVVCALGLAGNLLVLYLMKSKQGWRKSSINLFVTNLALTDFQFVLTLPFWAVENALDFKWPFGKAMCKIVSMVTSMNMYASVFFLTAMSVARYHSVASALKSHRTRGRGRGDCCGQSLRESCCFSAKVLCGLIWASAALASLPNAIFSTTIRVLGEELCLMHFPDKLLGWDRQFWLGLYHLQKVLLGFLLPLSIISLCYLLLVRFISDRRVVGTTDAVGAAAAPGGGLSTASARRRSKVTKSVTIVVLSFFLCWLPNQALTTWSILIKFNAVPFSQEYFQCQVYAFPVSVCLAHSNSCLNPILYCLVRREFRKALKNLLWRIASPSLTNMRPFTATTKPEPEDHGLQALAPLNAAAEPDLIYYPPGVVVYSGGRYDLLPSSSAY | Function: Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51573
Sequence Length: 472
Subcellular Location: Cell membrane
|
Q8TDU9 | MPTLNTSASPPTFFWANASGGSVLSADDAPMPVKFLALRLMVALAYGLVGAIGLLGNLAVLWVLSNCARRAPGPPSDTFVFNLALADLGLALTLPFWAAESALDFHWPFGGALCKMVLTATVLNVYASIFLITALSVARYWVVAMAAGPGTHLSLFWARIATLAVWAAAALVTVPTAVFGVEGEVCGVRLCLLRFPSRYWLGAYQLQRVVLAFMVPLGVITTSYLLLLAFLQRRQRRRQDSRVVARSVRILVASFFLCWFPNHVVTLWGVLVKFDLVPWNSTFYTIQTYVFPVTTCLAHSNSCLNPVLYCLLRREPRQALAGTFRDLRLRLWPQGGGWVQQVALKQVGRRWVASNPRESRPSTLLTNLDRGTPG | Function: High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41141
Sequence Length: 374
Subcellular Location: Cell membrane
|
P62426 | MAVYVKFEISQELEEKTAEVVANAEKIKKGANEVTKAVEKGIAKLVVIAQDVQPEEIVAHIPVICDEKGIAYSYSSTKEALGKAAGLEVPTSAIAVVAEGSADELKDLVEKLNGLKA | Function: Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends, this subunit dramatically stimulates RNase P activity.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 12381
Sequence Length: 117
Subcellular Location: Cytoplasm
|
P62917 | MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN | Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
PTM: Hydroxylated on His-216 by RIOX1. The modification is impaired by hypoxia.
Sequence Mass (Da): 28025
Sequence Length: 257
Subcellular Location: Cytoplasm
|
P86927 | MQLQRLGAPLLKRLVGGCIRQSTAPIMPCVVVSGSGGFLTPVRTYMPLPNDQSDFSPYIEIDLPSESRIQSLHKSGLAAQEWVACEKVHGTNFGIYLINQGDHEVVRFAKRSGIMDPNENFFGYHILIDEFTAQIRILNDLLKQKYGLSRVGRLVLNGELFGAKYKHPLVPKSEKWCTLPNGKKFPIAGVQIQREPFPQYSPELHFFAFDIKYSVSGAEEDFVLLGYDEFVEFSSKVPNLLYARALVRGTLDECLAFDVENFMTPLPALLGLGNYPLEGNLAEGVVIRHVRRGDPAVEKHNVSTIIKLRCSSFMELKHPGKQKELKETFIDTVRSGALRRVRGNVTVISDSMLPQVEAAANDLLLNNVSDGRLSNVLSKIGREPLLSGEVSQVDVALMLAKDALKDFLKEVDSLVLNTTLAFRKLLITNVYFESKRLVEQKWKELMQEEAAAQSEAIPPLSPAAPTKGE | Function: Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Catalytic Activity: ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 52226
Sequence Length: 469
Subcellular Location: Mitochondrion
EC: 6.5.1.3
|
P86924 | MLRRLGVRHFRRTPLLFVGGDGSIFERYTEIDNSNERRINALKGCGMFEDEWIATEKVHGANFGIYSIEGEKMIRYAKRSGIMPPNEHFFGYHILIPELQRYVTSIREMLCEKQKKKLHVVLINGELFGGKYDHPSVPKTRKTVMVAGKPRTISAVQTDSFPQYSPDLHFYAFDIKYKETEGGDYTTLVYDEAIELFQRVPGLLYARAVIRGPMSKVAAFDVERFVTTIPPLVGMGNYPLTGNWAEGLVVKHSRLGMAGFDPKGPTVLKFKCTAFQEISTDRAQGPRVDEMRNVRRDSINRAGVQLPDLESIVQDPIQLEASKLLLNHVCENRLKNVLSKIGTEPFEKEEMTPDQLATLLAKDALKDFLKDTEPSIVNIPVLIRKDLTRYVIFESRRLVCSQWKDILKRQSPDFSE | Function: RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Catalytic Activity: ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 47477
Sequence Length: 416
Subcellular Location: Mitochondrion
EC: 6.5.1.3
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A6VUQ2 | MRRRTSPRRTTTSKPQPIGPIQTFEVDGLTHEAKGVARLQGKVTFIEGALPGETVEAQVNKAGRRFDEAVLVNIIEPSVYRVEPSCQHFNLCGGCSFQHLANEQQLSAKADWLQGQLRNLITTQELETLSDTPTGYRRRARLAIDIKKGRMVLGFRGKASKEIISIDQCVVLTPNLQSTFLLLKLKLLENDLAGVLGHVELLEDTKGVSALFRLTSPISDELKNAWEDWAEKGRVALYWQAPKVGKAEVALEKMRYYDLGDLRLKYHPQDFIQVNAAMNQKMVVQAMDWLNPSKQDVILDLFCGVGNFSLPLAVHAQAVIGVEVQETMVEAARENARVNGFDNLSFVAADLTKPVNNELFKQTITKVLLDPPRAGAFEFLDSIIKIGPTQILYVSCNASTLARDAEYLVAKGYRVLRVSLMDMFPQTSHVETMMLLQKKK | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49183
Sequence Length: 440
EC: 2.1.1.190
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A1U2U9 | MSKRRRKVLPKEPVRCEIETLSHDGRGIARADGKTQFVDGALPGETVMAKMVRTRSRFDELRTTEVLEAAPDRQQPPCEFADLCGGCSLQHMSADAQIRFKENTLREHFAHFGGIEPEQWVAPMRSPDSLGYRRKARLGVRYVKARESVLVGFREKRNSFLTDIDRCVVLDPRIGERIEPLRELLHGMAAFDRIAQVEVACGDDTAAMVFRNMDDLVPDDREKLIAFGQAHDLHIYLQPKGPDTVHRIWPESGGRDDERLTYRMDEFDLTMAFHPMDFTQVNAGINRNMVHRAVEWLDVQPGERVLDLFCGLGNFTLPLARKGGQVVGVEGDDAMVVRGRENARLNDLSNVEFHGADLHGDFTGQSWAKEGFDKILIDPPRSGAEEICKYLTAFGANRIVYVSCNPATLARDAGVMVRNGYRLVQAGVMDMFPHTTHVESIALFERSAD | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50537
Sequence Length: 449
EC: 2.1.1.190
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E4ZBM0 | METEVNVAEISALDYEGRGVTKVGGKTVFIKGALPSERVGFRIVRQKKQFDEAEAVAIFKVSDERTVPQCRYFERCGGCSLQHISPAAQVAFKQRMMEEQLERIGKVKPKQILLPIYGHVWHYRDRARFSVSLDKLCRLKLGFQAKKTNDVVDISSCMLLPKPVSDKLSAIRGLLQDLAEEGSVARFAEFYRGSEITVLNIAFKSKLRQNEENRIRQWFDSELSDGWQVWLQIEGGVSQPFYPKTDKTLKYTLPEFGIEMPFRPGDFTQINTDTNRLMVSRVVKMLDIRRGERIADLFCGLGNFSLPMAKSGADVVGIEGAENLVRRARQNARLNGCDRQTDFIAANLFDCTEKTVASWERFDKMLIDPPRSGAYEVVKSLHTPYLPQKIVYVSCNPSTLARDAGVLVEKGYMLSQAGIMNMFAQTSHTESVAVFDLLPQTGKNFLKIKGKD | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51034
Sequence Length: 452
EC: 2.1.1.190
|
Q3JCY2 | MAHHPKRKPLSQEPQKASIEALTHEGRGIAHVAGKTVFIDGALPGETVWFHYLRRRGKFDEGRVLEVLQPAPSRVEPRCRHFGVCGGCSLQHLSTAAQLQLKQVTVREQFRHFGGVEPEQWLPPLVGGGYWGYRYKARLGVKFVKKKDRVLVGFREKGSSLIAALEGCEVLHPSVGYLLPALGELIASLSCYDRIPQIEVAAGDQSTGLVFRHLVPLTTADTEQLVAFGQAHKLQIYLQGGGAETVRLLWPAGARLSYSQFGKLEMIFLPTDFTQVNREVNTKMVRRVLELLEIKSGERVLDLFCGIGNFTLPLAIAGAEVVGIEGNAGLVARAVANATHNRLENAYFEMADLNGAEWTHYVWAREGFSKALLDPPRSGALLAVQQMSKLRVQRIVYVSCNPATLARDAGELVNRQGYRLRYAGVIDMFPHTTHVETLALFEQTRKH | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49575
Sequence Length: 447
EC: 2.1.1.190
|
Q13Z67 | MSRTAPHRRAPKRYKTPPPAPAHVVTGNEPVIEIISLDMEARGVGRTETEDGTPGKVIFVEGVLPGERVSYSTHRSKPKFEQAEVVQVLRESVMRTKPKCTYFDICGGCSMQHLDIRAQVAVKQRVLEDNLQHLAKLRPETVFRPIHGPSWGYRYRARLAVRFLPEKGGMRIGFHEKKSSYIADMKTCEVLPPHVSAMLMPLRFMVRKLSIYDRMPQLELAVGSSVTALVVRNLEPITAADEQVLRDFADEHKVQFWLQPGGPDTVTPFYPLDVQLDYTLPEYGIRMPFKPTDFTQVNHAINRVLVSRALRLLAPARTDRVLDLFCGIGNFTLPLARISKEVMGIEGSEVLTSRALANAGLNGVAGHTSFECRNLFEVTADDLRALGHFDKFLIDPPREGALAVAKALAEIARSGNGPLPKRIVYVSCAPATLARDAGLLVHEAGYRLVGAGVVNMFPHTSHVESIALFERD | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52414
Sequence Length: 472
EC: 2.1.1.190
|
P55136 | QLNMALMLFLAPSSDELDHVLGEQPYYDIDDVRLTFSPKDFIQVNRDVNVKMVEQAINWLDIQPQDRVLDLFCGLGNFSLPLARRAKAVVGVEGVDEMVARATANAAANGLDNATFYQANLDEDVTKLVWAQEQFDKILLDPARAGAAGVMQHIVNLAPSKVVYVSCNPATLARDSQMLLQQGYKLARLGMMDMFPHTGHLESMTLFVKTNHHKKNSNVM | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24490
Sequence Length: 220
EC: 2.1.1.190
|
B1XU70 | MHRGDKPVNIEVAEPITVEVLDLDAQGIARLAPSEEEAAQDQSGKVIFIKGALPTELVTYTVTSDKSRFSKAKVREILKPAVFRAEPKCAAFGICGGCTMQHLDIRAQVAMKQRVLEDDLQHIAKVKSEEILCPMGGPTWEYRHRARLSAVNRSIKKGTVLIGFHEGKSGYVADMLACEILPKHVSDLLPEMRKLVMGLSIVDRMPQIEIAIGEPEDAQSDDPQKSKPVTALVFRNLKPLTTEDEQLLRAFADQHEVWIWLQPKGIETIAPFYPLTGKLCYRLPEFEIEMPFKPCDFTQVNHMMNRALVSRAIRLLEVQPTDRVLDLFCGIGNFTLPLARKAKQVLGIEGLESLTARAKSNAQHNGLSDKASFMQSDLFEVTSETVASWGGAERWLMDPPRKGAMDICKALAELHLQQSDLLPERIVYVSCNPKTLARDVEILCHQAGYRLSSAGIINMFPHTSHVESMVVFDRA | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52975
Sequence Length: 475
EC: 2.1.1.190
|
A9N8M5 | MTHSKRWLEEHAKDPYVKRAKKEGYPSRAAYKLLEIHQKYKLFKPSMNVIDLGAAPGGWSQVAKDLVGPKGVVIAIDLLPMQSMLDVIFIQGDFNEPEIFNQLEAIVAKKTLTGQVDLVISDMAPNISGIKNVDQSRSLHLVELAWDCAQKLLARGGTFLVKVFQGPGVDRFLINLRPYFNQVKFLKPSASRSRSSEIYILAGEFLGYNQRV | 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): 23804
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q129M4 | MKVNPKNSPKDNLKDSPKVSARGKKVNKAWLHDHINDPYVKLAQKEGYRARAAYKLKEIDETLGLIKPGDCVVDLGSTPGAWSQYVRRKLSPTGAAAGELNGRIIGLDMLPMEPIEGVAFIQGDFREPEVLQKLEQALATDKGQVKVDLVISDMAPNLSGIESADAARIVHLVELAVEFAQNRMKPDGTLVVKLFHGSGYDELVKLFRATFKVVKPMKPKASRSNSSETFLVGKGLKKRAETVPELA | 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): 27071
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q4KIG3 | MARSKTSHNWLKEHFNDPFVKMAQKDGYRSRASYKLLEIQEKDRLIRPGMSVIDLGAAPGGWSQVTSRLIGGQGRLIASDILEMDSIPDVTFIQGDFTEDAVLAQILEAVGNSEVDLVISDMAPNMSGLAAVDMPRAMFLCELALDLAGRVLRPGGDFLIKIFQGEGFDEYHKSVRQMFEKVQMRKPSSSRDRSREQYLLGRGFRGRSE | 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): 23402
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q1QEW1 | MTSKPMNRRPTANNHRNRSPETAKKLGQLHPRNPHQGRYDFEVLTRALPELAKHTITNPKGESTINFSDSAAVRVLNQALLANYYGVKFWDIPEGYLCPPIPGRADYIHYIADLLAQTTHVNKDNTPPTGKEIHALDIGTGASAIYPIVGSQSYGWRFTASDIDPISVNTAALICETNPKLKSAVKVKLQTEPKFIFKNIIGRQDYFDVVVCNPPFHASLEEAMEANSRKQHNLQRHRGKNENEQISRSSTKPGNAAQNLNFGGQHKELWSEGGEIAFLTKMAKESQDFAEHVGWFTTLVSKSENVKPLQLLLKQLGVAQMRIIEMSQGQKSTRILAWRFNTDEE | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38728
Sequence Length: 345
Subcellular Location: Cytoplasm
EC: 2.1.1.181
|
Q21P11 | MHKSANSKTRKQSKGLHPRNIHRNGYDFDALKACHPPLVQYIKCNPVGAATIDFANSAAVKALNTALLQHHYKIESWSIPDGALCPPIPGRIDYIHYIAELLGCPLPSGKINTANTCTNNAVKMLDVGTGANGIYTLLACAVYGWRCVGSDINSESLANVKAVLANNPTLNANISLRLQPNKDAFFSQIIQTDDYFDVSVCNPPFHASQEEASKGTNRKLHNLARSRNKAHTAKQPSLNFGGQHAELWCNGGERLFLKKMIKESQAFAQQVGWFTSLVSKSENVQPALKLIRKLGATEVREIEMMQGNKKTRVIAWRFKP | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35321
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 2.1.1.181
|
A9MIS5 | MSAQKPGLHPRNRHQHRYDLAALCQTTPELTSFLTRTPAGEQSVDFANPQAVKALNKALLAHFYAVTHWDIPQGFLCPPVPGRADYIHHLADLLGETTGSIPVQANILDVGVGANCIYPLIGAYEYGWRFTGSEISEAAMSSAQAIIQANTGLSRAIRLRRQKDSTAIFTGIIHKNEYYDATLCNPPFHDSAAAARAGSERKRRNLGQKRDDVLNFGGQQQELCCEGGEVTFIKKMIAESQTFRRQVLWFTTLVSRGENLPPLYRALTEVGAVKVVKKEMAQGQKQSRFIAWTFMDDDQRRRFITRKR | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34491
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 2.1.1.181
|
A1SBR7 | MAPFFSAMTSKKQSQGLPKGPHPDNAHRDGYDFSALVASHPPLKPFVRANAYGNLSIDFALPEAVKALNCALLKHHYGISRWDIPKGFLCPPIPGRVDYLHHLEDLLRQTPGTDGLPLLDIGTGANGIYALLAASRFGRAVVATDIAKASLTNVATILKANPGLEKRISLRFQSNPRHILTGVTQTNEQFAACVCNPPFHASAAEAALGTNRKLEGLAKSRGQRHISGPGKPQTLNFGGQDAELWCDGGERSFLLRLIDESARLPDLCVWFTTLVSKSDNLRPCKRRLEQRGASEIKVIEMQQGQKITRILAWRFESVT | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34906
Sequence Length: 319
Subcellular Location: Cytoplasm
EC: 2.1.1.181
|
A3DAC9 | MSKPAVKSVPSATAKTATRAVNIRQKVKAPKQAKPEAKGRAKPSKDKPRAEIKKALHPRNAHLNGYDFPALYAAFTQLKTFVRPTPYGTLSIDFADPLAVKTLNAALLKHHYGIGAWDIPQGALCPPIPGRVDYVHYVADLLAEGDKSCAMDKARVLDIGTGANGIYPILGCQVYGWQYVASDINAHSLTNVQSIIEQNPVLQGRISLRLQPDDKAVFKGVIQAEERFELTLCNPPFHASMAEASEGTKRKVNNLQLNRGSSVKAAPKLNFGGQAAELWCQGGERQFLATMIRESQMFADQCLWFTSLVSKQENLKPCYQALAQLNVDTVKTIEMQQGNKITRVLAWSFQSAAKRKIWRAEHLAN | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40219
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 2.1.1.181
|
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