ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7NPS3 | MPLKLRVAGVDEAGRGPLAGAVFAAAVILDPAKPIAGLADSKVLSEAQRDELAVLIKRDALAWCVASASVEEIDKLNILHATMLAMTRAVEGLPVRPDLAQIDGNRVPKHLPVPGEAIVKGDAKVAAISAASILAKTARDAELVALDALHPQYGFARHKGYPTAEHLAAIEAHGVLPAHRKTFGPVKAWLASHQGALF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 20736
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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B5EBC6 | MTGLFPDNPEAPIDLLALEGQALRRGYFRIAGIDEAGRGPLAGPVVAAAVMLPAGLLLPGVNDSKQLTEEKREELFDVIHREALAVGVGIGDHALVDSINILQATLSAMRDAVRALSITPGFLLIDGISNIPMNIPQRTVKKGDSLSLSIAAASIIAKVTRDRMMVEYDAQYPGYGFASHKGYGAASHLAAIAELGPCPIHRKTFSGVKEHLPSQPDSDTAGPSTGLFSF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 24267
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A6LSN4 | MIQFNEDIRSLSFAEIKEEIHKLSIVDLYRNDEHTKLINWLEEDKRKNVLSLKEKIEKDLESYLNEVKRVKTMYEFDKSFGSYRYIAGVDEVGRGPLAGPIVACSVILDLNVLEKDLILYINDSKKVKEHKREELSEIIKEKALSYQIAVSSNKEIDEKGIAFANNKVFLESCNSLSIKPDLVLSDGYLIKNIGIENKSVIKGDTKSASIAAASIVAKVYRDRLMKEYAKKYPHYDFENNVGYGTSKHIEGLKKYGKSDIHRNSFLTKLL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 30936
Sequence Length: 270
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A5I4L9 | MNLNNLENIRYNEIKEFSDKIKKEFTFSQKKQVMDIIEKLNKDSRKNVIKLGQALEKFLNKYEEELKRTNNMYNFDRRYGNNYLIAGVDEVGRGPLAGPIVAAAVVLDLNVEEMQRIFNIKDSKKLSEKKREELDIIIREKAISYNIALVDNKTIDERGISWSNNEVLKRAVEGLKVKPDLVLSDGYAVKNLNIRNEFIIKGDSKSISIASSSIIAKVYRDSMMKEYSKGLNMYGFNHNAGYGTEEHVQAIKKHGPSKIHRMSFLTNIL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 30929
Sequence Length: 269
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q18BC9 | MQDKSVREIKEIIETLEVEKYMEYIELLRVDERKSVQGLAIKLAKKLDNIRKEEERLETINIFENEGYDKGYLYIGGIDEAGRGPLAGPVVASVVVFKKDTKIEGVNDSKKLSEAKRDELFEVIKEEALDYGIGIVNNEEIDEFNILNATYMAMKKAINCLKKAPDYLLVDAATIPGIDISQNPIVKGDSKSISIAAASILAKVTRDSIMYQYDRVYPEYGFKSHKGYGTKEHYEAIEKYGITPIHRKSFLKNIL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 28910
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A1UEF9 | MPASWPPRTVIRKASGLRTLESALYRNGLGPVAGVDEVGRGACAGPLVVAACVLGPNRLESLAALDDSKKLGEKERERLFPVIRRYALAYHVVFIPSEEVDRRGVHVANIEGMRRAVAGLSVRPGYVLSDGFRVPGLPMPSLPVVGGDAAAACIAAASVLAKVSRDRLMVAMEREHPGYGFAEHKGYSTPAHTAALAELGPCAQHRYSFINVRRLVTAGTPQISGGLTDAEPGQCCELG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 25290
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q74MH3 | MRYGGVDEAGRGPIIGPMVIALVIGDSGYLKELGVKDSKLLTKEQREELFNEIVKNSLVKYEIVSPSLIDRYNLNELEAKVTANLINSIEDEISHIVIDSPERPENYKLRILKYLKKRVKIITKNKGEEDPLVAAASIVAKVIRDREIEKIKEQTGIDFGSGYPSDKRTRKALEQYYRILKPYIRKKWPFEINKKLTDFI | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 22995
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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B2A2P0 | MMYYCGIDEAGFGAGAAQVYVSACVLDPQKPINESLTDSKQLTPKKRELLAEEIKQDALTWCIATASVEEIEKLNIRKATILAMKRSLEGLTVKPDMVYIDGINSPEVPFPVETVVKGDSKIPAISAASILAKVARDNRMLEYDEQYPEYGFKDHKGYLTKNHIKAIQKYGPSPIHRKTYKPIKKIIDNQKNQQLELF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 22263
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q2GD69 | MVYRKSENGLIAGVDEVGRGCLAGPVVACAVILTENLAIPGDSKVLSRAVRLSWYEEIISNSYNAIGMSSVKEIETMNILNATLLAMERALERLPVVPTTVLIDGRDIINNAAKYKEVKSVVSGDKIYGEIKAASIVAKVTRDRLMEGLDLTYPYYRWKFNKGYGTKEHLEALAKYGVTDHHRRKFAPVKRMLLR | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 21732
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q0AEI5 | MYCSGHLIRLAGRLEIKTSGVVVREWIHPEGKAIYGVDEAGRGPLAGPVYAACVVLDSCYVINGLADSKQLSEKRRASLAEQIKQHARAWAIASASVEEIDRLNILQASMLAMRRAVIELMPVSNALILVDGTHVPQLDYEVQAVIRGDSLVAEISAASILAKTARDAEMLRLHEIYPIYGFDRHKGYPTRVHLDAIRLHGITATHRKSFAPCAEKSTV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 24020
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q82U06 | MAERRIPLKHEYAQDGKVIYGVDEAGRGPLAGPVYAACVVLDPADVIEGLADSKQLSEKKRISLADQIKQRARAWAIASASVEEIDRLNILQASLLAMQRAVVSLRPISNALVLVDGNHAPRLDCEVQTVIRGDSLVAEISAASILAKTARDIEMLRLHEAYPVYGFDRHKGYPTKAHLEAIRLHGITDIHRRSFAPCVGQSVSGARTTSFINQKEA | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 23698
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A4XKQ3 | MKEVVIYTDGACSKNPGPGGWCAILIYKGIKKVLKGFEENTTNNRMELKAIIEGLKALKEPCKVTVYTDSAYIVNAINQNWIGKWQKNNWKTSEKEEVKNIDLWQELLEFLKVHNVKFEKVKGHSTDTLNNMCDEIARSMIKEMR | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16696
Sequence Length: 145
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A8Z6F7 | MKIVTLFSDGSCLGNPGAGGWAYILRYNEAQKKASGGEAYTTNNQMELKAAIMGLKALKEPCEVRLFTDSSYVANSINEWLANWQKRNFKNVKNVELWQEYLEISKPHKVVASWVKGHAGHPENEECDQMARNEALKIKDENKI | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16277
Sequence Length: 144
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A7H185 | MKTVTLFSDGSCLNNPGAGGWAYILEFNGAVKKDSGGAAMTTNNQMELTAVIEGLKALKEPCEVRLFTDSSYVANAVNSWLDGWVKKNFIGSDKKPVKNIELWQEYLRVSRPHKVTASWIKAHNGHPQNEECDTMAREKATKFQNEADI | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16551
Sequence Length: 149
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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A4WNV1 | MSDLFAYTDGACSGNPGPGGWGVLMLAREGEAVVKERTLQGGEALTTNNRMELMAAISALEALTRPTEITIVTDSAYVKNGVTTWIHGWKRNGWKTADRKPVKNAELWERLDAAQQRHKVVWRWIKGHAGHAENERADELARAGMAPFKTR | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16728
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q3B2H0 | MQKKITIYTDGACSGNPGKGGWGAMLMYGDAVRELSGYSPATTNNRMELTAAIEALRALKEPCSVALYSDSSYVVNAFREGWLDRWTRNNWKTAAKKNVENTDLWKQILELTARHTVTFHKVKGHSDNPYNNRCDELARQAIQKKP | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16454
Sequence Length: 146
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q8EE30 | MTELKLIHIFTDGSCLGNPGPGGYGIVMNYKGHTKEMSDGFSLTTNNRMELLAPIVALEALKEPCKIILTSDSQYMRQGIMTWIHGWKKKGWMTSNRTPVKNVDLWKRLDKAAQLHQIDWRWVKGHAGHAENERCDQLARAAAEANPTQIDTGYQAES | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 17782
Sequence Length: 158
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q9X7R6 | MRERAVAACDGASKGNPGPAGWAWVVADASENPVRWEAGPLGKATNNIAELTALERLLASTDPDVPLEVRMDSQYAMKAVTTWLPGWKRNGWKTAAGKPVANRELVVRIDELLDGRSVEFRYVPAHQVDGDRLNDFADRAASQAAVVQEAAGSALGSPEPPPAPDVPAARRAPRRGSSGAARKGGGGSSARTIKAKFPGRCLCGRPYAAGEPIAKNDQGWGHPECRTVAAG | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 24297
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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P77766 | MSDTNYAVIYDLHSHTTASDGCLTPEALVHRAVEMRVGTLAITDHDTTAAIAPAREEISRSGLALNLIPGVEISTVWENHEIHIVGLNIDITHPLMCEFLAQQTERRNQRAQLIAERLEKAQIPGALEGAQRLAQGGAVTRGHFARFLVECGKASSMADVFKKYLARGKTGYVPPQWCTIEQAIDVIHHSGGKAVLAHPGRYNLSAKWLKRLVAHFAEHHGDAMEVAQCQQSPNERTQLAALARQHHLWASQGSDFHQPCPWIELGRKLWLPAGVEGVWQLWEQPQNTTEREL | Cofactor: Binds 1 Mn(2+) ion per subunit . However, the sequence similarity to CV_1693 from C.violaceum tends to indicate a trinuclear metal center.
Function: Exoribonuclease that catalyzes the last steps of 5S, 16S and 23S rRNA 5'-end maturation. Removes 3 nucleotides (nt) from the 5' end of 5S, 16S and 23S rRNA precursors to generate the mature 5' ends. Precursors with longer extensions are not processed (7 nt at the 5' end of pre-23S rRNA or 66 nt at the 5'-end of 16S rRNA are not processed). 5S and 23S rRNA maturation occurs more efficiently and accurately on ribosomal particles as compared to free RNA; the enzyme overdigests free RNA but generates the correct 5'-end in ribosomes from rnm deletion strains . Efficiently catalyzes the hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and DNA, with no specificity toward the identity of the nucleotide base. Is more efficient at hydrolyzing RNA oligonucleotides than DNA oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency approximately 10-fold lower than that of the corresponding single-stranded oligonucleotides.
Catalytic Activity: a ribonucleoside 3',5'-bisphosphate + H2O = a ribonucleoside 5'-phosphate + phosphate
Sequence Mass (Da): 32580
Sequence Length: 293
EC: 3.1.13.-
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Q7M456 | KDWNYFTFAQQWPIAVCAEHKSCFIPDSVVGWGIHGLWPSSDTESKGPENCNGSWPFDINNVMPLVPELKKYWPNLYPDTKANSFWEHEWSKHGTCATSLPATSNELKYFGMGLKLHAKYNISRILVNQGILPSKTAGYMINETEAAVKRELGVDAVIECVYDKEKTKKQLLYEISICLTKEFELISCNKKEVSETTCPRKEPFFYPPVHDNN | Function: Releases mononucleotides from RNA in the order of 3'-GMP, 3'-AMP and 3'-UMP.
Sequence Mass (Da): 24360
Sequence Length: 213
Subcellular Location: Secreted
EC: 3.1.27.-
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Q9YF79 | MKGRRPSHRRQLIPPLLTGLRVKVLAHSDPSLEGLEGWVVVEEARSLRILTLEGRVSTVLKDLAVIEVEAPGGEYIRISGRVLIGNPLDRVKEYRWRVSRRCRSSSRLKT | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 12493
Sequence Length: 110
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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O28362 | MRGRLQGVELIARDWIGLMVEVVESPNHSEVGIKGEVVDETQNTLKIMTEKGLKVVAKRGRTFRVWYKGKIMRIKGDLINFRPEDRIKRGLMMLKRAKGVWI | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 11806
Sequence Length: 102
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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P22527 | MPLTPETLPRHELVGLDCEVVAASNPDVIGISGTVVMETTQMLTLEGADRVWHVPKDSATFAFDLSTETVLVDGDRLVARPARRTENTGDSLWR | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 10277
Sequence Length: 94
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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Q1QS97 | MSDQGFPRRQRLLTAGDYQHVFAHASFKVHGKGLLVLARPNALGYPRVGFVFSKKNVRRAVDRNRLKRLVRESFRLQSHRLPAVDIIVLARRGVDALDNATLHRQLHGMWRRLEKDVRKQSVASTPSP | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14686
Sequence Length: 128
EC: 3.1.26.5
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Q7NPT6 | MSAYRFRRAHRLLKTDEFSSVFSLRQQRSNAFFQVFARPNGLDHARVGLVVGKKVAKRAVRRNYIKRCVREWFRLNQQGLDGVDYVVRAKTAFTREQRAEAVTALQALFAKLARCRASSSS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13967
Sequence Length: 121
EC: 3.1.26.5
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B5EGY0 | MTSSNFPKAERLLRRPEFLQFNEGASKLHTQYFLVLLKPNEGTGTRVGFTVSKKVGNAVVRNSIKRRLREFYRQNKSLFISADINIVAKKGADVLDFHQISTELAAAFGRLRKKYA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13218
Sequence Length: 116
EC: 3.1.26.5
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A5CVC5 | MLARRNRVTSGADYRIIVRRGRRTTTGTAVVSALAGPDDAPTRFGFIISKKVGNAVTRNLVRRRLKAVSAGLLHSVPPGTSIVIRVLPGMERTAWDTLQEEMASAVTRAVRTI | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 12282
Sequence Length: 113
EC: 3.1.26.5
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Q97CV8 | MKENRIRKNAEFRRVYRKGKSFSNRLLVLYVYKNYILKDINRIGISVSKKVGKSVVRSRVKRLIGESYRLNSSNLKKGHDFVIIARTACNGKRYSDIEDSIKNLFNKAGLVIYDEKNIT | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13889
Sequence Length: 119
EC: 3.1.26.5
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C3KWJ9 | MKENKIRKNKEFRHVYRRGKSYSNKLLVLYVCKNRYNINRLGVSVSKKVGKSVVRNKVKRLIKESYRLNLDKDMKRGYDLVFIARNSSNDKDYKDIESALINLLKKAGIYN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13160
Sequence Length: 111
EC: 3.1.26.5
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Q181T2 | MDFNRTKGLKKDSDFRKVYKHGKSFANKYLVIYILKNKSDYSRVGISVSKKVGKAITRNRVRRLIKEAYRLNIDEKIKPGYDIVFIARVSSKDATFKDIDKSIKNLVKRTDISI | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13276
Sequence Length: 114
EC: 3.1.26.5
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A5N455 | MDVYRIKKNAEFRAVYKRGKSFSNNLLVLYVYMNRKNVNRLGVSVSKKVGKSVVRNRIKRLIKESFRLNSDYMKVENGYDLVFIARKASNGKSYVEINNSVKNLIKKAGLYK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13045
Sequence Length: 112
EC: 3.1.26.5
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A2BXQ2 | MALPKAMRLKGHRTFDYIHKNSEKYYGKLMTFKIARSNPKILISHKNFNSLNNFKIAIAISKKVSKKAVVRNKIRRLLQDYFLKNFRKDKNHKPYWLLVNLKSSDSCNYESKLLQEFQHLIFKSGLLND | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 15319
Sequence Length: 129
EC: 3.1.26.5
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Q7TVA1 | MVLPKGMRLKGYKSFDYIHKSAKRYKSDSMMLRVTKANERLIKSTIKNSKSNSCRCAISISNKVSKKAVIRNRLRRLLHNHLKKRLFQKDAFSNNWLLLSLSPKCLDKNTENLLEECDKLLIEAGFC | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14762
Sequence Length: 127
EC: 3.1.26.5
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Q7V612 | MVLPASMRLRGSRCFEHLQKWGYRFYGTSMVLRVIEANPQLLKAPHRHHNSTACRCAVVISSKVSKRAVIRNRLRRLLHDHLRSRLEVAPEHCNHWVLISLKPVASAIEASPLLEECDRLLNQAGLLS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14637
Sequence Length: 128
EC: 3.1.26.5
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Q46JN4 | MVLPKHMRLKGHRCFDFIYKEGSRFYSSSMVLRVTDANKKPQVKGKQSKTRHSIKCAISISNKVSKKSVTRNKLRRLFHHHLSLRLSNMACDNEIWAFISLKPSCMKNPDSTLLKECDKLLTKAGITK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14748
Sequence Length: 128
EC: 3.1.26.5
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Q15MS5 | MGENSFSRELRLLTPTHFEFVFKNATPAVSPNLTLLARHNDSPNPRLGITVAKKRVKKAHDRNRIKRIVRESFRNHQQSLPNIDIVVVGKSGLDKLSNQELFLVLSKLWKKLAKRCEKSQ | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13798
Sequence Length: 120
EC: 3.1.26.5
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O86449 | MLPNQNRLRRREDFAKVYAKGDRYRGTYLSLKILFDSNTTYTRIGIVVSKKVSKLAVTRNRFKRQLRAIFRQLLSQLKDGLQIVVTVTTVASKPNYQELGDDLKNILAKAKVLHGN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13353
Sequence Length: 116
EC: 3.1.26.5
|
Q5LY00 | MKKSYRVKKEKDFKALFDAGHSVANRKFVVYCLDRNLPHFRVGLSVSKHLGNAVTRNRVKRRLRHALMDMSSQLEHQDFVVIARKGVEDLSYQDIYSNLVHVLKIAKLYKD | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 12987
Sequence Length: 111
EC: 3.1.26.5
|
A4VS84 | MSRGFGREKRLLTPRQFKAVFDSPSGKVPGRNVLLLARENDLQHPRLGLVIGKKSVKLSVERNRIKRQIRETFRHHQLELAGWDIVIIARKGLADLDNPELAKQFAKLWKRLSRNPAKTAAEPGAANNTHA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14833
Sequence Length: 131
EC: 3.1.26.5
|
Q67J29 | MKKAYRLKSRLAFQSVYAQGRSVANRAAVVHVLKQQAGTPTRVGFAAGRKLGKAVVRNRAKRRLREAVRLLWPRVRQGYYIVVIARQAALDMPFPELRQKVEELFERAGLLQREG | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13144
Sequence Length: 115
EC: 3.1.26.5
|
Q2LSG2 | MKKLTLKKSERIRKRRSYLQIYQHGKRSFTKHFTIVVSENDLDFPRLGMTVTKKIGNAVKRNRIKRLIREFFRLNKDRFKASQDIVIIAKGNTSSMKYADVCRELGVLLTKEPQNITQE | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14058
Sequence Length: 119
EC: 3.1.26.5
|
Q31MS4 | MALPRCHRLRQRDRFPALYRGGRKLSTPSLLLRWLPQAEIESVNESRFAIVISLKVHKRAVRRNRLRRRLQAALLRLRDRLRPGFDGLLTVKPGLDLDTSTSQFLQELEDLLTRAEIIHGRQ | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14286
Sequence Length: 122
EC: 3.1.26.5
|
A0LLH1 | MRGSSRFRPHEKLRASDDYQRVKRSGRRVRTAHFGVNFAANDLPHHRLGLVVQKRYWNAVGRNRIKRRIREWFRLNKTRIPAPYRDIVVVARPGAEKLSSLDVTKELLAIFLHKDGRIR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14080
Sequence Length: 119
EC: 3.1.26.5
|
Q2JQX0 | MLPAPYRLRDRRAFQALYQAGQRRSGAGLILLFQPMPAGCEGIPSQVGLVIGKKVSKSAVKRNRLRRRLREILRPLCPNLKPGYRLLLISKPNLLTYKWPELQAEVHRLLQKADLLVSPSPDPEPS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14259
Sequence Length: 126
EC: 3.1.26.5
|
B1XJD2 | MGLPKEHRLKHWRDFKTIYSQGKRFRGDALAIILLPQPAAPTKIGISISRKVSKKAVVRNLIKRRIRHACRTLLPQIQPGWHIVIAVRYNARECEYEHFLQELKRLLIQAEVFHGH | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13607
Sequence Length: 116
EC: 3.1.26.5
|
Q6A759 | MSETSRIDGRRLDQLRDVRIERGWLSQAEGSVLVSFGRTTVLCNASVTEGVPRWRKGSGLGWVTAEYEMLPRATNERSGRESRKGKVGGRTHEISRLVGRSLRAVVDDKALGENTIILDCDVLQADGGTRTASITGAYVALIDAVNWLRGRGGLVSEPIIGSVQAISVGVVDGIPMLDLAYKEDSRADTDMNVVMSGNGDFVEIQGTAEGTPFNRNLLNELLDLAAGGCATLKQAQSEALGVTL | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 26103
Sequence Length: 244
EC: 2.7.7.56
|
Q3Z6Z8 | MQRGDGRNFNQLRPITITPGFQSFAEGSVLIEQGKTRVICSVSMEDKVPQFLRNSGTGWVTAEYSMLPRSTVTRTQRDSSAGKISGRSQEIQRLIGRSLRSCVDLAALGERSFIIDCDVIQADAGTRTASITGAYIALYLAFKKMVDMGILSKMPFTSQVAAVSVSIFKGNIVLDPCYDEDFQAEVDFNLVMNDRAEFVEIQGTAEGKTFSRDTLDQVLKLGEAGIWQLFDIQNSITRP | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 26385
Sequence Length: 239
EC: 2.7.7.56
|
Q40381 | MLNSPLTSVLFVLLFVLSPIYGAFEYMQLVLQWPTAFCHTTPCKRIPNNFTIHGLWPDNVSTTLNYCAAKENFKNIEDDTKKDDLYKRWPDLTTAETYCKQHQNFWRHEYNKHGKCCSESYNREQYFDLAMALKDKFDLLSSLRNHGIIPGRGMKYTVQKINSTIKKITQGYPNLSCTKGIMELVEIGICFDSMVKNVINCPHPKTCKPTGSNEIKFP | Function: Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species of the Solanaceae, self-incompatibility is controlled by the single, multiallelic locus S. This stylar glycoprotein is associated with expression of self-incompatibility in potato.
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 25178
Sequence Length: 218
Subcellular Location: Secreted
EC: 4.6.1.19
|
P05798 | DVSGTVCLSALPPEATDTLNLIASDGPFPYSQDGVVFQNRESVLPTQSYGYYHEYTVITPGARTRGTRRIITGEATQEDYYTGDHYATFSLIDQTC | Catalytic Activity: [RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].
Sequence Mass (Da): 10576
Sequence Length: 96
Subcellular Location: Secreted
EC: 4.6.1.24
|
Q5SLP1 | MRIVPFGAAREVTGSAHLLLAGGRRVLLDCGMFQGKEEARNHAPFGFDPKEVDAVLLTHAHLDHVGRLPKLFREGYRGPVYATRATVLLMEIVLEDALKVMDEPFFGPEDVEEALGHLRPLEYGEWLRLGALSLAFGQAGHLPGSAFVVAQGEGRTLVYSGDLGNREKDVLPDPSLPPLADLVLAEGTYGDRPHRPYRETVREFLEILEKTLSQGGKVLIPTFAVERAQEILYVLYTHGHRLPRAPIYLDSPMAGRVLSLYPRLVRYFSEEVQAHFLQGKNPFRPAGLEVVEHTEASKALNRAPGPMVVLAGSGMLAGGRILHHLKHGLSDPRNALVFVGYQPQGGLGAEIIARPPAVRILGEEVPLRASVHTLGGFSGHAGQDELLDWLQGEPRVVLVHGEEEKLLALGKLLALRGQEVSLARFGEGVPV | Cofactor: Binds 2 Zn(2+) ions.
Function: Has endoribonuclease activity towards 23S and 16S rRNA (in vitro).
Sequence Mass (Da): 47055
Sequence Length: 431
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
A5HAK0 | MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV | Function: Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity.
PTM: Cleavage between Arg-55 and Arg-56 is catalyzed by a membrane-localized Gram-negative bacterium protease (OmpT in E.coli). The excised fragment is then transported to the bacterium cytosol for cleavage of the disulfide bridge linking Cys-48 and Cys-109, thus separating the N-terminal and LF-ZF3. LF-ZF3 but not the N-terminal peptide possesses bactericidal activity.
Sequence Mass (Da): 17011
Sequence Length: 149
Subcellular Location: Secreted
EC: 3.1.27.-
|
O61887 | MKLLLLLCISCIPLAYSHDGEPFDYLMFTTIYPTAVCRADDDSVPESCEIPSGTPQWSIHGLWPNFENGSYPQNCRGTPRHFDENLIKSIEDRLVVVWPNLYPKKTIQSFWKHEYDKHGTCAQSEKLFESELAYFTEVMKVFDSIDVAGGLKSVGPSEKPITSSDLKNALSGVTSGKTFQFHCLRDKKTKQFLLGDIRLCLNKDLTIRDCPTDGKHPNRVSRFERSIGRNRRGPPLPSFQPCPAEFIYLPEMSSISKSSDSTSPSIFGRIWSAIKNIGN | Function: Probable endoribonuclease involved in the autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes.
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 31477
Sequence Length: 279
Subcellular Location: Lysosome
EC: 4.6.1.19
|
P00669 | MALKSLVVLPLLVLVLLLVRVQPSLGKESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV | Function: This enzyme hydrolyzes both single- and double-stranded RNA.
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 16377
Sequence Length: 150
Subcellular Location: Secreted
EC: 4.6.1.18
|
Q29539 | SGSSPSSNSNYCNLMMFCRKMTQGKCKLVNTFVHESLADVKAVCSQKKVACKNGQTNCYQSNSAMRITDCRQTGSSKYPNCTCKTTRAEKHIIVACEGKXFMP | Function: This enzyme hydrolyzes both single- and double-stranded RNA.
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 11358
Sequence Length: 103
Subcellular Location: Secreted
EC: 4.6.1.18
|
Q9RRM6 | MPTLYVILSLLLGLIGGVLVQRAIGSRQQAVTDDRLQREAQAEAQQIRAEAQRHARELHEAAEQDRQDAISKTQDAARRVQDAAERDTLAAAHEARLDEQREQVRALRAQLEAEREQAKADAAQQREALSTDRQETRREREDLGREIERLGRRTEQLDARSDKLDALEERLEGGWREVQRQEQEVAERLRQADLKLYEVAGLTPEVAREQILGRLNAELEEEKAIRVKAMTEKAGAEARRSARSIIAQAIQRSASETSAQLSVSVVPIPSDAMKGRLIGREGRNIRAFESLTGVDLIIDDTPEAVILSSFNPLRREVARHVLDALVADGRIHPTRIEEMVHKAQDDMKTFIHQQGEEAAIEAGVVGLKPGLVQLLGRMYFRTSYSQNVLKHSVQVAHLTGIMADELGLDAALARRAGLMHDVGKSIDREIEGTHVEIGINLARRFGEPAEVIDAIAHHHDPENGETLYSVLVAAADAISAARPGARREALESYVRRLEQLEQIAVAFPGVQQAYAIQAGREVRVIVQPEKVTDAQATLLARDIAGRVEQDMEYPGQVQVTVVRESRAVGVAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63513
Sequence Length: 572
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q6AJ81 | MFFIEHPFVYLGLDLIVGCLIGFFLRKQLVERQQQNIQAQSKQIIENAIIDAEQLKKEALLQSKEEVYQIKQSLEAEVKLERDDLKDEHRQLKKQRDNIKRENERFEKRQSRHVVAEKALERRLREVDVKHEEADNEILKQRDELARIAGITQDEAKKLLMESIESEAQMDAAKRLSKIENEMKLEADRKARSILALAICRYAGDYVADKTVSMVPLPSDEMKGRIIGREGRNIRAIEAATGIDIIIDDTPEAVILSGFNPVRREVARLALIQLISDGRIHPGRIEEVVEKVSKELDEVMCEAGEQATFDVGAHGVHVELIKLLGRLRYRTSYGQNVLQHSLEVAFLCGIMAAELGIDVKMAKRAGLLHDIGKAVDHEVEGSHAVIGRDLAKKYGEPDEIVYAIGAHHADQPPKSVLDILVQAADALSGARPGARKEMLQSYVKRLEDLEAIANKFPGVDKSYAIQAGRDLRIIADAQKISDAEATLLSRNIAASIEEKLTYPGQIRVTVIRETRSVEYAK | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58590
Sequence Length: 521
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q728D2 | MGLMIFAYIAIGAVLGAGTGYLLHRYVSAKRIGDANELAKRIVEEARKEAQAQKKEILLQGQDEIFNQKRELENEFKERERELKARDRKLEEQGERLEEKLEKATQKEHEVLAIEKELTRKERRLATLEEELEGKIAEQDHRLEEVSGLTAEEARARIMEEVEARTRHESAKMIRVIEMEARETADRKAKEILASAIQRYAGDYVGEQTVTAVTLPSEDMKGRIIGREGRNIRALEAATGVDLIIDDTPETVILSAYSPLRRQVAKMALERLIQDGRIHPARIEDIVRKCEQELEVQVREVGEQATFDAGVHGIHPDIIKLLGQLRYRTSFSQNVLQHSLEVSALCGMMAAELGMDIKKAKRAGLLHDIGKAVDHEVEGPHALIGADIAKKYGEGKDIIHAIAAHHEDQPPKTALAVLVQAADSISGARPGARKELLENYVKRLEDLENIATGFEGVSKVYAIQAGREIRVMVNSENVDDDQTYMLCKDIAAKIEKNLTYPGQIRVTVIRERRAVGYAK | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58247
Sequence Length: 519
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
B1GZX3 | MGNITVIVITAFVASIVGYILRLIYAKLNIRSVEQTSKRVIEEMKLIAETKAKEIILDARLIVDRERKEFEHKIKERRQFIQNMENKLNQREESLDRKMDAVDKKEKNLSEREKDFSSKEHLLSVKFSEVDKVKEEQKKFLERISGMTREEAKKILISGMEEDAKQCAAVLLQKLEQEMRENADKKSKEILSIAIQRVAADHTADITTSTIQISNDEIKGRIIGREGRNIKAFEHATGVDLIVDDTPESITISAFDGIRRQIAKIALERLIADGRIHPARIEEVVKKVKKDMEQHLKETGEQAVIEAGVPCSNLEIIKLLGKLKYRTSYGQSQLQHTLEVTWLAGAIAGELGLDVMFCKKAALLHDIGKAVDHEVEGTHHQISANIAKKYGESHKMINAILSHHEGFEVPSSPEAFVIATADAISAARPGARKESVERYLKRLEKLEKVVKEFRGVSIAYAMQAGREVRILVEPEKINDNQTQILAHDIAKKIEQELEYPGQIKITVVRETRVQEIAK | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58669
Sequence Length: 518
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
A7HMK7 | MEWLIYIVILFVGIAAGAFFGISVGRKRAEEALEKKLKAAKEDAESIIKSAEKEASEIKKKAIIEAREEAHQIREEIEKERKKREEEIKQLEERLLKREEMLSKREELIDKRENYVENLKIELESKAKEIEEKAKEIERRFIELAGITHEQAREIVLQEAREKYEHEIAKFFVQIKTRYEDEADKYAKKIIADAIQRYAPEYIGEVTISTVALPNDDMKGRLIGREGRNIRTFEKITGVDLIIDDTPEMVTLSSFNPLRREVARRTIEKLVQDGRIHPARIEEMYEKAKAEVEREIKEAGQDAVITVGVGGLHPEIIKLLGRLKFRTSYGQNVLAHSVEVAQIAGLLAAELGLNVDKAKRGGLLHDIGKAIDHEVEGSHTDIGAEMLKRYGESDEIINMVMAHHGQEEPITPEAAIVAAADAISAARPGARREDVENYIKRLMKLEEIAKSYKYVENAYAIQAGREIRVIVQPDKTDDATIEKLAHDIATRIENELQYPGVLKVVVIREKRSVSYAK | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58829
Sequence Length: 517
Subcellular Location: Cell membrane
EC: 3.1.-.-
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Q0RDW7 | MDGVLVILLSLVLLVLVALILAVAWLARTARGDRHYGAATRATRSSSGMAASVDALALDDDDGPAVRVLPPVRPAAEGERPAGDAPGAAYGESAAAPDAGLGSPAPRAPHHDAAAAPEPGAAIGGAPTPAAGSPADASDTGRIAETVDTGTVLAVAAVADTPSRVAATEDTSLEAPLRESALRESAPGESASVRRAAEREAAQIVARAEREAAERLARVEREAAEIRRRGEDEVASLRNQARAEAAADASRAEAAVRDAARVELEAARAEIATARTSFEEELRVRRAELRGREEALAAREQRVEERTAGLDEHASRLAGREQDLLDREDELAHRTAEAADDEAARQAALERIAELTAVQARAELVSTIEHEARREAALLVREIEARAEEEGEERARRIVTTAIQRVASDQTTESVVTVLHLPGDEMKGRIIGREGRNIRTFESVTGVNVLIDDTPEAVLLSCFDPVRREIGRITLAALVSDGRIHPHRIEEEYARAQVEVEERCVRAGEDALLETGISEMHPELVTLLGRLRYRTSYGQNVLAHLIESAHLAGIMAAELRMALPLAKRAALLHDLGKALTHEVEGSHALIGADVARRYGESEEVVHAIEAHHNEVAPRSLCAVLTQAADQISGGRPGARRDSLESYVKRLERIEQIAGDRPGVDRVFAMQAGREVRVMVVPEEVDDVAAHLLARDVARQIEDELTYPGQIRVTVVRETRAVGTAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77751
Sequence Length: 725
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q2J766 | MEGVLVVLLSLVLVVLSVLILAVARLVRATRVDKVPDPAPVVPRTPAARGVGDVTGPADFDEEPTVRVLPAPWEGSGAPATTDADSPADRDGTAARTGDSAVTAGRSDGGLRAAHGGSAEEAAQIVARAEREAAERLARAERDAAEIRRRGEEDVALLRERMLAEAAVETSRVQAAARESVRAEQEAARTEIAATRAAFDGEQQAWRTELQSREVAIAAREQRVEDRMASLDDHGRRLADRDRDLLDRENDLTRRTAEVADLERARHAALEQVAGLTAGQARGELIAVIEQEARREAALTVREIEARAEEEGEERARRIVTTAIQRVASDQTTESVVTVLHLPGDEMKGRIIGREGRNIRAFESVTGVNVLIDDTPEAVLLSCFDPVRREVGRITLAALVSDGRIHPHRIEEEYARAQLEVAERCVRAGEDALLETGISEMHPELVNLLGQLRYRTSYGQNVLAHLIESAHLAGIMAAELRMPLPLAKRAALLHDLGKALTHEIEGSHALIGADVARRYGEDEQVVHAIEAHHNEVAPRSICAVLTQAADQISGGRPGARRDSLESYVKRLERIEQIAGDRPGVDKVFAMQAGREVRVMVVPEEIDDLAAHLLARDVARQIEEELTYPGQIRVTVVRETRAVGTAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70338
Sequence Length: 646
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q89NF8 | MFALTFLGTSASVPSAERNHPALLVEAAGKRILIDCGEGTQRQLLRSGAGFRRLDRILLTHAHLDHVLGIPGLFSTLGLRQSSDVMTIHGGPGTLDIVIRMLAGLWGAGRAPIPVEFAALSEGQVIDAGGFTIDCFPVRHRDTDSFGFVFQSPARRHLLPDRLASLGVPDGPLRGELAQGRPVVIEDGRTIDPEDVLGPATGGRKLVVIGDTETTEGLSQYVADADMLVIEATFLDRDASIARDYGHLTAAEAAAFAAANNVGQLVLTHMSGRYEDEEILAEAARIFPNSRIAADFDHIVV | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 32133
Sequence Length: 301
EC: 3.1.26.11
|
A4YN80 | MFELIFLGTSASVPSHDRNHPGLLVQAGGQRILVDCGEGIQRQLLASGAGFRRLDRILLTHGHLDHVLGIPGLFSTLRLRRSADVMSVHGSPGTIDVVIRMLAGLWGDGRAPIPLELVPLTPGQVLDAGAFTINCFAVRHRDTDSFGFEFVSPARRHLLPERLAALAVPDGPIRKTLADGYPVTLDDGRIVTPEDVLGTPGGGKKLVIVGDTETTDGLQAHVRGADLLVIEATFLQRDSATARDYGHLTAAEAAALAASGNVGQLVLNHISGRYPDEEILAEARSIFPATRIASDFDRLTV | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 32117
Sequence Length: 301
EC: 3.1.26.11
|
Q97IQ6 | MLDICLLGCGGSLPTSDRNLTSLLISYNGRKILIDCGEGTQVSMKEIAWGFKDIDVICFTHYHADHVMGLTGLLLTIANSGRIDPLTIIGPEGLREVVKGLTVVAPFFPYEIELIELDSKCSDNFLDKVFKIEDVEIFALPVDHSIECLSYSVRVNRKRKFDVNKAKANEVPLKIWNELQRGKEITYENKLYVPDMVLGESRKGIKITYCTDTRPVDSLHKFAYKSDLFVCEGMYGEEEKKEKAVDKKHMIFSEAAGIAKAAEVKELWLTHFSPALSEPEKYLENAKEIFENTHIGSDRKIKIINFENN | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 34960
Sequence Length: 309
EC: 3.1.26.11
|
P60199 | MELQFLGTGAGQPAKQRNVSSLALKLLDEINEVWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHIFGLPGFLSSRSFQASEEQTDLDIYGPIGIKTYVLTSLKVSGARVPYQIHFHEFDDKSLGKIMETDKFEVYAERLAHTIFCMGYRVVQKDLEGTLDAEALKAAGVPFGPLFGKIKNGQDVELEDGRLICAKDYISAPKKGKIITIIGDTRKTSASVKLAKDADVLVHESTYGKGDERIARNHGHSTNMQAAQIAHEAGAKRLLLNHVSARFLGRDCRQMEKDAATIFENVKMVQDLEEVII | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 34430
Sequence Length: 309
EC: 3.1.26.11
|
P39137 | MNTNQDNGNQLQRTMKSRHLFMISLGGVIGTGFFLGTGFTINQAGPLGAVLSYLVGGFIMFLTMLCLGELAVAFPVSGSFQTYATKFISPAFGFAFGWLYWLGWAVTCAIEFLSAGQLMQRWFPHIDVWIWCLVFAALMFILNAITTKAFAESEFWFSGIKILIILLFIILGGAAMFGLIDLKGGEQAPFLTHFYEDGLFPNGIKAMLITMITVNFAFQGTELIGVAAGESEDPEKTIPRSIKQTVWRTLVFFVLSIIVIAGMIPWKQAGVVESPFVAVFEQIGIPYAADIMNFVILIALLSVANSGLYASTRILYAMANEGQAFKALGKTNQRGVPMYSLIVTMAVACLSLLTKFAQAETVYMVLLSLAGMSAQVGWITISLSQIMFRRKYIREGGKIEDLKFKTPLYPVLPLIGLTLNTVVLISLAFDPEQRIALYCGVPFMIICYIIYHVVIKKRQQANRQLEL | Function: Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51634
Sequence Length: 467
Subcellular Location: Cell membrane
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Q8LES0 | MATANGAKSPSSMGPKVLFYSILLTLQYGAQPLISKRCIRKDVIVTSSVLTCEIVKVICALILMARNGSLKGLAKEWTLMGSLTASGLPAAIYALQNSLLQISYRSLDSLTFSILNQTKIFFTAFFTFIILRQKQSILQIGALCLLIMAAVLLSVGEGSNKDSSGINADQKLFYGIIPVLAASVLSGLASSLCQWASQVKKHSSYLMTVEMSIVGSLCLLVSTLKSPDGEAIKKYGFFHGWTALTLVPVISNALGGILVGLVTSHAGGVRKGFVIVSALLVTALLQFAFEGKPPSSYCLVALPLVMSSISMYQKYPYIDKKKKKV | Function: Mediates the transport of UDP-linked acetylated hexosamines across the endoplasmic reticulum (ER) membrane . Facilitates UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc) transport . Regulates the cytokinin signal in meristematic cells through modulating activity of cytokinin oxidases/dehydrogenases . Part of the ER quality control system, which determines the fate of aberrant proteins in the secretory pathway .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34836
Sequence Length: 325
Subcellular Location: Endoplasmic reticulum membrane
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Q8MIT6 | NSKSQMDKDYYQLQAVLEAERRDRGHDSEKIGDLQARITSLQEEVKHLKHNLERVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEERDAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLIENKDRMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQSEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTLSRLEETNSMLTKDIELLRKENEELTDKMRKAEEEYKLKKEEEINILKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKKKKK | Function: Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity . Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A . Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (By similarity). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis . Plays a role in terminal erythroid differentiation (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52386
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9FGT1 | MEEKSSGGGVRLHVGGLGESVGRDDLLKIFSPMGTVDAVEFVRTKGRSFAYIDFSPSSTNSLTKLFSTYNGCVWKGGRLRLEKAKEHYLARLKREWEAASSTSDNTIKAPSDSPPATHLNIFFPRLRKVKPMPLSGTGKHKYSFQRVPVSSSLPRSFCDCEEHSNSSLTPREIHLHDLEAVNVGRQEAEVNVMNSVMNKLFEKNNVDPEEDNEIEADQDNLIINVASSGNDMDSALDMLSRKRKSILNKKTPSEEGYSEGRKGNLTHPSKNRQTISLEETGRQESSQAIRGKKKPSEVVPDKSSDEPSRTKDLEQSIDNISWSQKSSWKSLMANGNSNDFSVSSFLPGVGSSKAVQPAPRNTDLAGLPSRENLKKKTKRKRVTSTIMAEDLPVSDDIKRDDSDTMADDIERDDSDAVEYYTACESMADDTASDSVAERDDSDAVEDDTAIDSMADDPASDSVAESDDGDAVENDTAIDSMADDTVSNSMAESDDGDNVEDDTAIDSMCDDTANDDVGSDDSGSLADTVSDTSVEAVPLEFVANTEGDSVDGKSNVEKHENVAEDLNAEKESLVVKENVVDEEEAGKGPLKASNKSTGGSSWLQKASWTQLVSDKNTSSFSITQLFPDLTSDKGEAAGVINNVGNQFSNSNQTASAMKQTDYASSSGGFVAAGVPVDSTPVRSLDENRQRLNGKNVSEGAKLGAKKKIIKRKVGSGDTCTFMRSSTSLKEWAKAKKALSEPRRKKNSEE | Function: RNA-binding protein required for DNA demethylation and to eluviate siRNA-mediated transcriptional gene silencing (TGS), probably by guiding ROS1 . Can bind specifically single stranded G-rich RNAs of 21-, 24- or 26-nt corresponding to promoter sequence of target genes; this interaction directs demethylation of target sequences .
Sequence Mass (Da): 81080
Sequence Length: 748
Domain: The RRM domain is required for single stranded RNA binding.
Subcellular Location: Nucleus
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K4RFM2 | MRPEPTEHPERTAAQRLYQYNVDLKVAFVLYAVAKLHLPDLLADGPRTTADLAAATGSDPSRLRRLLRAAAGADALREVPEDSFELAPMGDLLRSGHPRSMRGMTTFFAEPDVLAAYGDLVESVRTGVPAFQLRHREPLYDFLARPQHKEVRDEFDAAMVEFGQYFADDFLTSFDFGRFTRFADIGGGRGQFLAGVLTAVPSSTGVLVDGPAVAASAHKFLASQNLTERVEVRIGDFFDVLPTGCDAYVLRGVLEDWADADAVRLLVRIRQAMGDAPEARLLILDSVIGETGELGKVLDLDMLVLVEGEHRTRAQWDDLLARAGFDIVGIHPAGDVWAVIECRGTAG | Function: Catalyzes the S-adenosyl methionine-dependent conversion of 8-amino-8-demethyl-D-riboflavin (AF) into 8-methylamino-8-demethyl-D-riboflavin (MAF) and roseoflavin (RoF), the last two steps in the biosynthesis of the antibiotic roseoflavin.
Catalytic Activity: 8-amino-8-demethylriboflavin + 2 S-adenosyl-L-methionine = 2 H(+) + roseoflavin + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 37936
Sequence Length: 347
Pathway: Antibiotic biosynthesis.
EC: 2.1.1.343
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K4REZ6 | MALKALILNTTLRRSPSRSQTQGLIDKAVPLYEKEGIETEVVRVIDHDIEQEYWDDYDDWNAGEKARREDEWPWLLEKIREADILVIATPITLNMCTSAAHVILEKLNLMDELNGDTKQFPLYNKVAGLLMCGNEDGAHHVAGTVLNNLGRLGYSVPPNAAAYWLGPAGTGPGYIEGKGDRHFHTNKLIRFMVANTSHLARMLQETPYTTDLEACAQAAREESDDVFAIRVNVNTPAIRYKRFQKLGEVKVEESQLG | Function: Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin) . Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined oxidation, decarboxylation and transamination reaction . The catalysis is initiated by an oxidation step in which the C-8 methyl group on the dimethylbenzene ring of FMN is converted to a formyl group to yield the 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) intermediate . In the presence of thiamine, the formyl group is oxidized into a carboxyl group to yield the 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate . Finally, in the presence of L-glutamate as an amino donor, decarboxylation and aminotransfer occur, resulting in production of 8-demethyl-8-aminoriboflavin-5'-phosphate . Addition of NAD (but not NADP) to the reaction increases the yield 1.7-fold . The reaction also proceeds without the addition of any electron acceptor, and it is possible that molecular oxygen serves this role .
Catalytic Activity: 3 A + FMN + H2O + L-glutamate + O2 = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5'-phosphate + 3 AH2 + CO2 + H(+)
Sequence Mass (Da): 28865
Sequence Length: 257
Pathway: Antibiotic biosynthesis.
EC: 2.6.1.114
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O44252 | MQLFDDFCKSFNKELQRANFGFAYNRVHLFYRSQWQKDEINTIYLLYRWIWALFFLGVYIMCVIVQFCDGKFFIYMTNWGFGLCTITMLISAVQVTCWHFDVRSTRSLVQESGHKAETSRGLKIYWWLYNMTLSLALIISTVYWVFLHGKMNKPMRFPAISIITHGMNSVMMLIDFLVIAFPLRILHMVYGMSLAIFFFLFTLIYHLCGGTDEFGNHYVYPILDWNNPNRCMVTFVGIFLLIMCYWVLLFGLYKLKRMFNRAFSVVWSPHAVGLI | Function: May have a central role in the fusion process during myogenesis, within the somatic mesoderm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32635
Sequence Length: 275
Subcellular Location: Membrane
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Q755J8 | MVYVSWSAAALLCASFFSTVVLAQSAKDLYGTWSAKSNQVFTGPGFYNPADELLIEPSLPGISYSFTEDGFFEMATYRVSGNPRNLACPSAVMTFQHGKYEILANGTLILRPFEVDGRQLVSEPCVDKGVSTYLRYSQVETFQRFAVELDEYHGKHALHLFQFDGSPVQPLYLAYRPPLMLPTITLNPTDHAGATATAGPGHRKRSLGELVRAGLQDKHKTTAVRNPSLFNAAFYWWCSAGVIAAGTVLFFMV | Function: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27881
Sequence Length: 253
Subcellular Location: Endoplasmic reticulum membrane
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A2QMB8 | MATYFFLGLLLTAVGTSSSSSASDLEGTWTTKSRQVVTGPGFYDPIGDKFLEPNLTGISYSFSADGHYEEAYYRAIANPQDPSCPKGVMQWQHGTYTVNSDGSVDLTPIAVDGRQLLSDPCQSSTGTYTRYNQTEHFESFAVSVDSYHGVQRLDVKNFDGSPMHPMYLIYKPPQMLPTQTLNPSSSSKSKRQVEGGTGGRFSIKDLVSREKVGDPNNWLWLGIFMTTLGGITFFRS | Function: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25992
Sequence Length: 236
Subcellular Location: Endoplasmic reticulum membrane
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Q5ABP8 | MIFSRYFIPIILTLLTSSPLFVDADPNMEELEGTWSSKSNTVFTGPGFYDPVEELLIEPDLPGICYSFTKDGHYEEALYRVKPNPKNHSCAVASVTYQHGKYELLSNGSLVLTPIAVDGRQLLSDPCNSEDPSKSTYTRYVQSTWFKTYQVYVDSYHGRWTLQIYQFDGSKMQPLYLAYKPPVMLPTIALNPTDEASETASTLGSVSHKIKRSRMRIKRSLENQYRTNAKREIYTEKFDKIWWSSVFCLALASSYFFLKR | Function: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29880
Sequence Length: 260
Subcellular Location: Endoplasmic reticulum membrane
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Q1DNE5 | MVLIVALLVFFCFLTAVPAALDPKLTGTWATKSRKVVTGPAFYDPAEDRFQEPENTGISYSFTEDGYFEEAYFRAIPNPTKPSCASAMMQFQHGKYSVESNGSLVLTPFAVDGRQLISSPCKSEGSMYFRFNQTEVFKRYEVLTDPFHNVKRLNLYQFDGTPMNPMFLVFDPPQMLPTETLNPTAQASATGRSKAKRGLPYGSGMASSRNKRPSTQVGGLTDPDKWWWAGVMMTLVGGVAFLYSESPWKDW | Function: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 28059
Sequence Length: 251
Subcellular Location: Endoplasmic reticulum membrane
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O15446 | MEEPQAGDAARFSCPPNFTAKPPASESPRFSLEALTGPDTELWLIQAPADFAPECFNGRHVPLSGSQIVKGKLAGKRHRYRVLSSCPQAGEATLLAPSTEAGGGLTCASAPQGTLRILEGPQQSLSGSPLQPIPASPPPQIPPGLRPRFCAFGGNPPVTGPRSALAPNLLTSGKKKKEMQVTEAPVTQEAVNGHGALEVDMALGSPEMDVRKKKKKKNQQLKEPEAAGPVGTEPTVETLEPLGVLFPSTTKKRKKPKGKETFEPEDKTVKQEQINTEPLEDTVLSPTKKRKRQKGTEGMEPEEGVTVESQPQVKVEPLEEAIPLPPTKKRKKEKGQMAMMEPGTEAMEPVEPEMKPLESPGGTMAPQQPEGAKPQAQAALAAPKKKTKKEKQQDATVEPETEVVGPELPDDLEPQAAPTSTKKKKKKKERGHTVTEPIQPLEPELPGEGQPEARATPGSTKKRKKQSQESRMPETVPQEEMPGPPLNSESGEEAPTGRDKKRKQQQQQPV | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.
PTM: Isoform 2 undergoes tyrosine phosphorylation upon T-cell receptor (TCR) stimulation. This phosphorylation has not been confirmed by other groups.
Sequence Mass (Da): 54986
Sequence Length: 510
Subcellular Location: Nucleus
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O43036 | MPDLSLYKQTVDLYLSIAPGHSRDPLNAIQEHMDSMILSKLPRINGIVLAYDNIRFLEKSAKVMYDSPFSFIWVRVDVLVFSPKKGDCLEGKINLVSPSHIGLLILGIFNASIPRKSIPKDWIFIEPDTTEEQGRWKTNDGNILEPGKDLEFVVDGIQREAGLTMVQGTLANS | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. May be involved in recruitment of Pol I to rDNA promoters.
PTM: Contains an average of four phosphates per molecule.
Sequence Mass (Da): 19385
Sequence Length: 173
Subcellular Location: Nucleus
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P46669 | MSQVKRANENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHNDVEEDADVINTDENNGNNNNEDNKDSNGGSNSLGKFSFGNRSLGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLISDADEEGNGYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDLPEVKEDNGSEIVYEENTSESNDGESSDSD | Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Through its association with RRN3 is involved in recruitment of Pol I to rDNA promoters. In vitro, the A13-A43 subcomplex binds single-stranded RNA.
PTM: Contains an average of four phosphates per molecule.
Sequence Mass (Da): 36224
Sequence Length: 326
Subcellular Location: Nucleus
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H8EZH5 | MLRLVVGALLLVLAFAGGYAVAACKTVTLTVDGTAMRVTTMKSRVIDIVEENGFSVDDRDDLYPAAGVQVHDADTIVLRRSRPLQISLDGHDAKQVWTTASTVDEALAQLAMTDTAPAAASRASRVPLSGMALPVVSAKTVQLNDGGLVRTVHLPAPNVAGLLSAAGVPLLQSDHVVPAATAPIVEGMQIQVTRNRIKKVTERLPLPPNARRVEDPEMNMSREVVEDPGVPGTQDVTFAVAEVNGVETGRLPVANVVVTPAHEAVVRVGTKPGTEVPPVIDGSIWDAIAGCEAGGNWAINTGNGYYGGVQFDQGTWEANGGLRYAPRADLATREEQIAVAEVTRLRQGWGAWPVCAARAGAR | Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity (By similarity). Plays a role in reactivating bacteria from chronic tuberculosis (TB) in mice.
Location Topology: Lipid-anchor
Sequence Mass (Da): 38078
Sequence Length: 362
Subcellular Location: Cell membrane
EC: 3.-.-.-
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P0C0F7 | MKSPLPWLKRRLSGRADSEHAQNLIRIIITTLFISYLGWRYQHTHGDTLMATWLILVGELLVSLGLMVAILLRPQVSHTRRLIGMLLDYTCTGAIMAIQGEPASPLYAVCMWVTIGNGLRYGSNYLRAATAMGSLCFLGAILISPYWKANPYLSWGLLLGLIAVPLYFDSLLRAMTRAVREARHANQAKSRFLANMSHEFRTPLNGLSGMTEVLATTRLDAEQKECLNTIQASARSLLSLVEEVLDISAIEAGKIRIDRRDFSLREMIGSVNLILQPQARGRRLEYGTQVADDVPDLLKGDTAHLRQVLLNLVGNAVKFTEHGHVLLRVTRVSGSAEDAVRLRFDVEDTGIGVPMDMRPRLFEAFEQADVGLSRRYEGTGLGTTIAKGLVEAMGGSIGFKENQPSGSVFWFELPMAIGEPLKSSTVRVPTGALVDAPEELESSNIIAFSNPFLRHRARVRSMRMLVADDHEANRMVLQRLLEKAGHKVLCVNGAEQVLDAMAEEDYDAVIVDLHMPGMNGLDMLKQLRVMQASGMRYTPVVVLSADVTPEAIRACEQAGARAFLAKPVLAAKLLDTLADLAVSTRQLATPATTVQVATSFEGVLDSSVLDELAALGMGEEFERQFVRQCLDDAQNCVGDIERDGTCSDWEQLRESAHALRGVASNLGLAQVASSGGELMRMADWQLQAEWRLRLSTLREQLKAGKDALDARVQGVKDGECSPRSNE | Function: Hybrid sensor kinase that regulates diverse biological functions through two distinct molecular mechanisms . At low cell density, the extracellular concentration of the diffusible signaling factor (DSF) is below a threshold, and unphosphorylated RpfC is involved in the negative regulation of DSF synthesis, via direct interaction with the DSF synthase RpfF. Interaction prevents synthesis of DSF, which remains at a basal level. This activity does not involve the phosphorelay mechanism and is not dependent on RpfG . Is also member of the two-component regulatory system RpfG/RpfC, which is involved in the perception and response to DSF, which is essential for cell-cell signaling . At high cell density, the level of extracellular DSF increases and binding of DSF to the sensor region of RpfC causes autophosphorylation of RpfC, which results in the release of RpfF and the activation of RpfG via a four-step phosphorelay . Activation of RpfG leads to the positive regulation of biofilm dispersal and the production of virulence factors .
PTM: Autophosphorylated . Activation may require a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain (Probable).
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 79806
Sequence Length: 726
Domain: The N-terminal input region plays an essential role in DSF perception. DSF binds with high affinity to a 22-amino acid sensor region at the N-terminus . The response regulatory domain, but not the HPt domain, is required for repression of DSF biosynthesis .
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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Q4UU85 | MQDVLGNPAGVSSAETWGSWSEKADLGLNIVIVDDQMSARTMLRHVIEDIAPELKVYDFGDPLDALSWCEAGRVDLLLLDYRMPGMDGLEFARRLRRLPSHRDIPIILITIVGDEPIRQAALEAGVIDFLVKPIRPRELRARCSNLLQLRQQSESVKQRALSLEQRLLASMNEVEERERETLSRLARAIEYRDGGTSAFLERMSHVAGLVAEQLGLSEEEVRIIEMAAPLHDMGKIAIPDSVLLKPGKLTEDEMNVMKRHPRIGYELLSGSQNRFIQVGALIALRHHERYDGSGYPDGLVGEAIPLEARIVAVADVFDALLSARPYKEAWTMDAALAYLYAQRGRLFDPRCVDALLRGRAQLEQICGQFSTASARPGV | Function: Member of the two-component regulatory system RpfG/RpfC, which is involved in the perception and response to the diffusible signaling factor (DSF), which is essential for cell-cell signaling . Detection of DSF leads to the positive regulation of biofilm dispersal and the production of virulence factors . Activated RpfG degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in DSF pathway. May also directly control genes involved in biofilm dispersal .
PTM: Phosphorylated and activated by RpfC.
Catalytic Activity: 3',3'-c-di-GMP + 2 H2O = 2 GMP + 2 H(+)
Sequence Mass (Da): 42173
Sequence Length: 378
Domain: Contains a C-terminal HD-GYP (modified HD) domain, which is involved in degradation of cyclic di-GMP. The GYP motif is required for interaction with GGDEF domain-containing proteins.
Subcellular Location: Cytoplasm
EC: 3.1.4.-
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O86308 | MDTMTLFTTSATRSRRATASIVAGMTLAGAAAVGFSAPAQAATVDTWDRLAECESNGTWDINTGNGFYGGVQFTLSSWQAVGGEGYPHQASKAEQIKRAEILQDLQGWGAWPLCSQKLGLTQADADAGDVDATEAAPVAVERTATVQRQSAADEAAAEQAAAAEQAVVAEAETIVVKSGDSLWTLANEYEVEGGWTALYEANKGAVSDAAVIYVGQELVLPQA | Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity. In pM quantities promotes the resuscitation and growth of dormant, nongrowing cells from M.luteus in addition to Mycobacterium tuberculosis, M.avium, M.bovis, M.kansaii and M.smegmatis. Hydrolyzes endogeneous cell walls, peptidoglycan preparations from Mycobacterium tuberculosis and M.smegmatis as well as an artificial lysozyme substrate 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (MUF tri-NAG). Overexpression in E.coli (when the enzyme is targeted to the periplasm) causes cell lysis.
PTM: May be subject to further C-terminal cleavage as the protein identified in gels is smaller than is expected.
Sequence Mass (Da): 23192
Sequence Length: 223
Domain: The LysM domain is not required for resuscitation activity in vitro; in its absence the protein is active in the fM range.
Subcellular Location: Secreted
EC: 3.-.-.-
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I1BYM7 | MVRFISFTSPIAALLLLSFGVKHASTASTNTCIVANSDSDDAITIAEAFEKCKTGGTVVFPKDSSYQLNSIVTTSDLKNVNINFAGTIHLPAREESYRNGDYYIQIKGTHIKMYGGGTINGHGQAWYDALDHTAPSVLRIAANDSIIGGFTIINSPRAHLNVTNSTNLVLHDFTLHTVSNNSYLPKNTDALDLYHSSGITFRDSMLTIGDDCVAIKEDVEKVIVSNVTCRGGHGYSIGSLGIGGRKDYVKHVNFRNSTCIDCENGVRVKTWAGGKGIVEDINYNDIILQNVDNPILVTTHYCDPNVIEYCNGNDDNSLNISSIHFKDITGTASALGNPIVNVNCSIESPCSDITFSGIDITKASNTTDNVCVYLEGSDEVSECSS | Function: Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
PTM: N-glycosylated.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate
Sequence Mass (Da): 41501
Sequence Length: 385
Subcellular Location: Secreted
EC: 3.2.1.67
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Q0K980 | MTQDELKALVAQAAADYVKQEVPEGAVLGVGTGSTANLFIDAVAAFKERFAGAVSSSEASTRRLQQHGFKVLDLNEVDEIPVYVDGADEIDASGAMIKGGGGALTREKIVASVAKRFVCIADGSKLVQTMGTFPLPVEVIPMARAAVARKLQALGGQPRLRMTKEGGIYKTDNGNVILDVAGLKIDDPRGLEQAVNQVPGVVTVGLFALRGADVLLLGTGDGVQRTDY | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 23853
Sequence Length: 228
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
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B8FL28 | MTSQDALKKQAAEKAVEYLESGMVVGLGSGSTATFAIHAIARLMKEGKLKDIVGIPSSTPTEEVARSLGIPLVGFEEHAVIDVTIDGADEVDPDLNLIKGGGGALLREKVVAQATKKNIIIVDESKISDKLGTIFALPVEVVPFATASETRFLESLGAKVTVRENQLGKAFKTDNHNRILDADFGPMDDAVKIGMALSQRAGVVEHGLFLGTTALVIVAGADGIREMKAA | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 24179
Sequence Length: 230
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
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Q551C2 | MSLDNCKKVAAYKAVDDFVKDGCKIGIGSGSTIKYAVDRIKELGLKNVICVPTSFQSTQLIVEAGLELSDLSRTPELDITIDGADEVDKDFNLIKGGGGCQLQEKIVAYSSKKLVIVADHTKESTELGENWKKGIPIEVVPMAYVPVMKKLESSSFSLTPKLRMAVNKAGPVVTDNGNFIIDAQFSKPLSNIPQLAIDIKMIPGVVETGLFVNMTKIAYFGQTDGTCKVKSI | Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 25064
Sequence Length: 232
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
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A5EVM0 | MNQQLLKEKVAAAVLEHVPENITLGVGSGSTVLCFIEALKQAKRQFRDIVAASETSSKALEAAGFRVRDLNACDPPDIYVDGADEINDDKIMIKGGGAALTREKIIASAAKEFICIIDESKKVAQLGRFPVAVEVIPMARSYVAREIVKLGAEPRWRQGVVTDNGHWILDVHYLDLTAAERMEARINTIAGVVECGIFAQRRADKVLMSQSDGEIVLW | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 23848
Sequence Length: 218
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
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Q6MC00 | MTQTNDSPSIKAKKAAALKAVEFVQDQMIIGLGTGSTIAYFIEALGKRCQAGLKITAIASSERSMRQARLVGIPIVDSDTILELDLTIDGADEIDPLKQMIKGGGGALLREKLIASASKEMIVVIDETKLVNKLGKFPVATEISIFTFRHIVKKLKDHGYCGSLRVNQDQSLYRTDNGNYIFDICFPEPIDNPIFEHNRLKSFAGVLETGLFFNLAGRVIIGYQNGMTKIVA | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 25396
Sequence Length: 232
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q6L1K2 | MFENEKRMAAMEALKFVRNDMRIGIGTGSTAYYFIEGLSELVKNGLRITGIPTSKKSEELCRSFNIPVDYNIKDIDIDFDGADEFDPYGNLIKGGGGALVREKIVAYNSREFYVLVDHSKYSERLHKFPLPVEVLPFMSEKTLENIERLGCRASFRDDKKFISDNGNYIIDCVFSYTDPELESQIKMIPGVVEVGIFRHLSTKIFQGTIDGCRIIDVK | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 24777
Sequence Length: 218
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q8I3W2 | MDSLKKIVAYKAVDEYVQSNMTIGLGTGSTVFYVLERIDNLLKSGKLKDVVCIPTSIDTELKARKLGIPLTTLEKHSNIDITIDGTDEIDLNLNLIKGRGGALVREKLVASSSSLFIIIGDESKLCTNGLGMTGAVPIEILTFGYEKIIENLLKIYTLKGCTYKIRKRNGEIFITDNKNYIVDFFFTEPIQDLLETCTRIKMTTGVVDHGIFVNMTNVALISKHDGTVLTLNKKYE | Function: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 26205
Sequence Length: 236
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q4P6V4 | MASSNATNSTSAASAANTNSSAFKSAELAALSGVEAAKRAAAYAAVDNHVKPQHEIIGIGSGSTVPYVVERIAQQGPAVNAKRWFVPTGFQSRELIINAGLRLGDVDSFPSIDVTIDGADEVDNALNCIKGGGACHLREKVLAEAANEFVVVADYRKNGSQLGTKWLQGVPIEVAPFAYAKVLQNLKKMGSDKAVLRMGKAKAGPVVTDNGNFCIDAPFPEAQMKDPSDLLKRIKLLTGVLEVGLFCNICKSAYFGNDDGTITIKTAAGDVQEGVHFDVSKAPATA | Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 29968
Sequence Length: 286
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.6
|
A5CXI2 | MTQDEMKFTVAQTALKYVIKNTIIGVGTGSTANFFIDALSTIKNNIKGAVASSKATAQRLENHGIRVFDLNKVTAISTYIDGADESDNNLNLIKGGGGALTREKIVAAVAHQFICIADESKLVSIMGSFPLPIEVIPMAANYVKNQISQKIGGIPEVRKDFITDNGNFILDIKDLKITNPKAMETKLNSIIGVVTNGLFANRGANVLLLGTPNGVKIITN | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 23520
Sequence Length: 220
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q7MHL9 | MTQDEMKKAAGWAALKYVEKGSIVGVGTGSTVNHFIDALGTMSEEIKGAVSSSVASTEKLEALGIKIFDCNEVASLDIYVDGADEINADREMIKGGGAALTREKIVAAIADKFICIVDGTKAVDVLGTFPLPVEVIPMARSYVARQLVKLGGDPCYREGVITDNGNVILDVYGMKITNPKQLEDQINAIPGVVTVGLFAHRGADVVITGTPEGAKIEE | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 22985
Sequence Length: 218
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q74MN9 | MITIPTEVKILEETDNLIKVQFKGETHTLFNALKEIAYTINGVKKAAYFIEHPLKDNNYFIIETDGSIKARDALIQALKKLKEELLNFKDWYYSNL | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 11180
Sequence Length: 96
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q3INY0 | MDLRVIENLETELAIEIEGEDHTFMNVLKGALLELDGVTAATYDVNPEQSGGQTEPIVTIKTDGSIDPLDALEQGASRVRDKTDAFEEAFEAAA | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 10151
Sequence Length: 94
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q8ZW46 | MSPVLRLEILKLDDKYLELKAKGETYTLFSPLVEYLSNDPDVEYVQFDVDHPLQENAYFKLKVKRGNPLEAIQRAVNAILSDLEELERGFFS | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 10678
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q980K0 | MEIRILKSESNYLELEIEGEDHTLGNLIAGTLRRISGVSFASYYQPHPLSDKIIVKILTDGSITPKDALLKAIENIRGMTSHYIDEIKGLTK | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 10285
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
P46217 | MEIKVIKEEQNYLELQIDGEEHTIGNLLKGMLLKVPGVKFAAYSLPHPLITSITIKILTDGSISAREALIKAIELAENYANLFIDEVKKI | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 10050
Sequence Length: 90
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q9HIC5 | MQRERTAESSLRVISKEKNSITVEMINYDNTLLRTLVEEILKDDQVDEARYYIKHPVIDNPQIYVRVKSGKPQSAIKRAVRKLSKLYEDLGTQFQKEFQRYESDHMIKAVE | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 13133
Sequence Length: 111
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
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