UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 5 15.6k | Functional Description stringlengths 6 12.4k |
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P11269 | MGQTVTTPLSLTLEHWGDVQRIASNQSVEVKKRRRVTFCPAEWPTFDVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVPYIVTWEAIAYEPPSWVKPFVSPKLSLSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLTEDPPPYGEQGPSSPDGDGDREEATYTSEIPAPSPMVSRLRGKRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNSAFPLERPDWDY... | Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligase... |
Q8EJJ5 | MNLKHKWDVYSRLTRLDRPIGTLLLLWPCLMALVLAAGGMPDLKVLIIFIIGVVIMRACGCIINDYADRDLDSHVERTKSRPLASGEISTKEALLLFVILGLAAFGLVLLLNGLVVKLSVVGIILTIIYPFTKRVTNMPQMFLGVVWSWSIPMAYAAQTGEVPIEAWWLFAANWFWTVAYDTMYAMVDRDDDLKIGIKSTAILFGKYDRQIIGLFQIAALFCFVAAGWSADRGLVYGLGLLTFVGFSTYQQMLIFGRERAPCFKAFLNNNWAGLVLFVSLGADYLF | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... |
Q8DDG1 | MPKYRSATTTHGRNMAGARALWRATGVKDEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEAAGGIAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASMRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDEQSEQIERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFISAGQRIVELTKRYYEQDDESALPRNIATKAAFENAMALDIAMGGSTNTVLHLLAAAQEGEVDFDMTDIDRMSRMVPHLCKVAPSTQK... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... |
Q1LPV5 | MLLAIKDFFNSLLLKELFKGMALTGRYLFARKITVQFPEEKTPMSPRFRGLHALRRYPNGEERCIACKLCEAVCPALAISIESDVRNDGTRRTTRYDIDLTKCIFCGFCEEACPVDAIVETHILEYHGEKRGDLYFTKDMLLAVGDRYEPQIAAAKAADAKYR | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... |
B7NRB1 | MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAAFSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQ... | Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essentia... |
P57688 | MKSYLKALVFAVLFLFILGFVYPTVTSLITEHALPFQSEGQPVEIDGHIYGSYLLAEAFNSSFFFHPRPSAIDYNLSESGSYDYSLGNPAMLNLTEKYLHRFLSENPGVNISEIPYAMISYSGSGLDPGIPLQGAIIQIPRISIAIHNITNLSVSDLYSYLYNLVNSTKTQNFPFFGSYYVNVVRLNVDIVEFLLKGGYISQSQI | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation... |
P51469 | MVKVGINGFGCIGRLVTRAAFDSGKVQVVAINDPFIDLDYMVYMFKYDSTHGRFKGTVKAENGKLIINDQVITVFQERDPSSIKWGDAGAVYVVESTGVFTTTEKASLHLKGGAKRVVISAPSADAPMFVVGVNHEKYENSLKVVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHAFTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKITGMAFRVPTPNVSVVDLTCRLQKPAKYDDIKAAIKTASEGPMKGILGYTQDQVVSTDFNGDTHSSIFDADAGIALNENFVKLVSWYDNECGYSN... | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) int... |
Q8LE93 | MEAQIHILEQEAYSAVLRAFQAQADEFSWDKATVMTNLRKELRISDDENRQLLNNVHNDDLIKRIRDSRPRGGNQVVRHQSLDVHPSPTFSASRKKQKTFQSYPSIGSTRSKSFNNRVVSANEPAEALIGRKVWTKWPEDNSFYEAVVTQYNANEGRHALVYDINTVNETWEWVDLNEIPTKDIRWDGEEDGVTLNVGHGGGTTRGNRRTLSHGGRGRGPRTQPRREHLATENGGGRKFFGEIELFNTDSLVKEVERVFDSNLPDPHELDKAKKLLKEHEQALIAAIARLTDASDYESDGEEPYSHELPMLLG | Probably involved in the regulation of chromatin states (Probable). Contributes to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1. Regulates negatively EDM2-dependent floral transition (PubMed:21830950). Interacts with EDM2 in nucleus. Slightly induced by heat stress. ... |
B3QCH2 | MPLRLVFMGTPEFAVPTLLALAAHGHDIAAVYTREPKPAGRGMKLQETPVALAAHRLQAPVLTPKTLRTDEALANFRAHEADAAVVVAYGMILPQAILDAPELGCYNLHGSLLPRWRGAAPLNRAIMAGDAETGVMVMKMDAGLDTGDVAMAERIAITDAMTVTDVHDQLARLGADLMVRAMAALERGGLQLTKQSEDGVTYAAKIDKAEAKIDFAKPAWAVLRHIHGLSPFPGAWCELPIEGQPVRIKVLRCAIADGRGEPGEVIDDHLTIACGDGAIRVSQLQRAGKQPMTAEEFLRGTPIAKGVRVG | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. (6S)-10-formyltetrahydrofolate + L-m... |
A7NEH3 | MTKKYLKVDVVSPLGSVFKGEADMVSLRGSAGEMGIVYGHTELLSTLPAGVVNVRKGQHTDVLYVSGGIVEVTPTRVTIMVDDMERAENLNQAEAEKARARAKEVLKNPDASKLDIEAANKRLKEADARLKALNSSNGLYYSKDD | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the AT... |
O28380 | MSSDMEGGMITMKANDTTKYLIHAEIEAEGVVERPDVVGAIFGQTEGLLGGDLDLRELQKTGRIGRIEVKIESKGGRSFGEIKVPSSLDKVETAILAAALETIERVGPCSAKIKVLKIEDVRASKRKRIVERAMNILREHFEEPEIESERIVEIVRQAIRADEIVEYGEEKLPAGPAIDESDAIIVVEGRADVLNLLKHGIKNVIAVEGTNIPKTIVELSKKKTVTAFLDGDRGGDLILKELLQVAEVDYVARAPEGKEVEDLTQKEILKSLRNKVPVEQLHVLKKEAKEGREREKLAEMPKDSISDVLRKHTESVKGRL... | RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the ex... |
Q50945 | LQAVAVFKQLPEAAALAAANKRVQNLLKKADAALGEVNESLLQQDEEKALYAAAQGLQPKIAAAVAEGNFRTALSELASVKPQVDAFFDGVMVMAEDAAVKQNRLNLLNRLAEQMNAVADIALLGE | ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) Tetramer of two alpha and two beta subunits. Belongs to the class-II aminoacyl-tRNA synthetase family. |
A8EY39 | MTNVITRFAPSPTGFLHIGSARTALFNYLFARHHNGKFLLRIEDTDKERSTNEAVEAIFSGLKWLGLDWDGEVIFQSKRNDLYKETALKLLQAGKAYYCFTSQEEIEKQRQKALENKQYFIFNSDWRDKDPAAYPTDIKPVIRLKTPREGSITIRDTLQGDVVIENSHIDDMVLLRSDGTATYMLAVVVDDHDMGITHIIRGDDHLTNAARQIAIYQACGYAVPSMTHIPLIHGADGAKLSKRHGALGVAAYKDMGYLPESVCNYLLRLGWSHGDDEIISMDQAIKWFNLDSLGKSPAKLDFANMNSLNAHYLRLLDNDS... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu) Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family.... |
Q9K6Z0 | MSKPFMFEKPFGMRDTLPEWYKTKKNICDQMTEEINLWGYDMIETPTLEYYETVGVVSAILDQQLFKLLDQQGNTLVLRPDMTAPIARLVASSLKDRAYPLRLAYQSNVYRAQQNEGGKPAEFEQLGVELIGDGTASADGEVIALMIAALKRAGLSEFKVAIGHVGYVNALLMDVVGNEQRADRLRRFLYEKNYVGYREHVKSLNLSTIDKSRLMNLLSLRGGRAAIEEARGLIQTEKGKTALAEMTKLYEVLESYGASEYVKFDLTLVLHMSYYTGVVFEGYGNRLGVPLCSGGRYDELLSKFHRPAQATGFGVRIDLL... | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. Heteromultimer composed of HisG and HisZ subunits. This f... |
Q1XHV8 | MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVVFHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKFQEKEDS | 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. Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Belongs to the archaeal RpoM... |
A5VIS1 | MTQKLHIALLFGGNSSEHDVSKRSAHNIYDALDKEKYDVSLFMFTKDGILLGNEDSQKIFDGEPEDQVVAEAYQKMDMSSPLAPIMALNEQKEIDFFFPVIHGNLGEDGTIQGLFKLLNKPYVGSNIAASAMSFDKDLTKKIISQAGIRNTPYVVVTPENQADYSWGRIEEKLGNLTFVKPAKQGSSVGIHRVTNAEEYEKALDDAFKYDYKILVEQGIANPQEIEISILGNEHPIASKLGAVRVPKDDPFYDYENKFVDASGVVFELPVKLPQYLVDEITDMALKAYKALGMKGMARIDFLVDSNNVPYLGEPNTLPGF... | Cell wall formation. ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate Binds 2 magnesium or manganese ions per subunit. Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the D-alanine--D-alanine ligase family. |
B9DY39 | MKIDIIISADDIKKEKILHKSVIVVDMLRATSVIITAINNGCREVIPVLTIEEALEIYHKNREKYVMGGERKALKIEGFHCSNSPLEYSRQVVENKTLVITTSNGTKAIKGSIMAKNILIGALINADEVANRSINLNNDVVIVNAGTCGQFSIDDFICSGYMINCVIKKIKVDLTDIARTALYIYEQNPDIITFIKKASHYKRIKKLKLYDDLEYCCRKDIIKIVPEYIDGIIKCNKLIY | (2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate Belongs to the ComB family. |
Q9M9E3 | MEGLIQTRGILSLPAKPIGVRRLLQPSHGLKQRLFTTNLPALSLSSNGHKKFQAFQQIPLGISVSHKERSRGFICKAEAAAAGGGNVFDEGDTAAMAVSPKIFGVEVTTLKKIVPLGLMFFCILFNYTILRDTKDVLVVTAKGSSAEIIPFLKTWVNLPMAIGFMLLYTKLSNVLSKKALFYTVIVPFIVYFGAFGFVMYPLSNLIHPEALADKLLATLGPRFMGPLAIMRIWSFCLFYVMAELWGSVVVSVLFWGFANQITTVDEAKKFYPLFGLGANVALIFSGRTVKYFSNMRKNLGPGVDGWAVSLKAMMSIVVGM... | Belongs to the ADP/ATP translocase tlc (TC 2.A.12.2) family. |
A8Z426 | MVKTVYVTGYKSFELNIFKDDAPEVHYLKQFIKHKIEQLLDEGLEWVLIQGQMGIELWTAEVVIELQRTYDSLKFAVITPFQGHTEKWNEHNQSKYANIIKHADYVDSIFHTSYQGPFQFKQADQFMLEHSDQTLLIYDEEQEASPKFFKQMLVDFMDKTNYTCDIVTFDELTAFINDLQWSEDQSF | Belongs to the UPF0398 family. |
Q1JPD6 | MAAVDSDIEPLPRGGFRCCLCHITTANQPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSTQLSEYFQAFGPVASVVMDKDKGVFAIVEMGDLGAREAVLSQPQHSLGGRRLRVRPREQIEFQSPASRSPKRVAPDSHQLIKALAEAPDVEAQMVKLVGLRELSEAERQLRSLVVALMQEVFAEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLDEPQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFEAPSSSLAPRTPDSALASETLASPRSLPPASPLQEDQGDGDQ... | Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pr... |
Q9D132 | MASAATEGEKGSPVVVGLLVVGNIIILLSGLALFAETVWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFVVASFGVGAALCRRRYMILTYLLLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTYYSADTDQGQELTRLWDRIMIEQECCGTSGPMDWVNYTSAFRAATPEVVFPWPPLCCRRTGNFIPINEDGCRVGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTTL | Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane... |
Q023P9 | MIQPDSYVRSLLKRSPGESVTARGWVKTRRDSKNVHFIQLNDGSSPVDLQVVLDAGVVPEDVVAKITTGACISVEGDLVASMGKGQAVEIKARALTVHGTADPEHYPLQKKKHTLETLRELGHLRTRSNTFGAVFRVRNALACAIHKFFQDRGFMYVHTPVISASDAEGAGSMFQVTTLDLQSPKPADFTGDFFGKHTYLTVSGQLEAEIFAHAFANVYTFGPTFRAENSNTPRHLAEFYMIEPEMAFCDLKDNQDLAEAFLKSQVEYVVNACGPDLDFLAKWYDPELRKTLDGLMNASFERITYTEAIDLLQRSGRSFE... | ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. |
P34604 | MVQESIISSFRGKLENDPSKSTSLATVETLLEVLDRSRATTVAEFQNELNQVVAALEKTDYSSTSIRSAADLFTRFTSLAPAALLDQEDFSQVLDLYRQRARSFIKNVRGSRAKISKCARLFFTHHMNILTHSYSKVVLETILDAHKSGYHLHVWVTESQPDASGKLVFEELKKNGVPTTLVLDSCVGYVMERIQAVLVGAEGVMETGGIINKIGTVNVCIIAKSRHVPVYVCAETIKFVREFPLNQADIPQEFKYRTSVIERNNLELEHPDVDYTAPEFLTLIITDVGAMKPEAVGEELIKMYI | Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Belongs to the eIF-2B alpha/beta/delta subunits family. |
B7NKV9 | MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLLADSFKGGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHISCVGNDFGFNDIFSRYVEAVGREGDVLLGISTSGNSANVIKAIAAAREKGMKVITLTGKDGGKMAGTADIEIRVPHFGYADRIQEIHIKVIHILIQLIEKEMVK | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate Binds 1 zinc ion per subunit. Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosy... |
B9L889 | MAVPKRRNSKTRGAKRRTHYKIKLSSVIKCSNCGAYKRPHRVCPSCGEY | Belongs to the bacterial ribosomal protein bL32 family. |
P25414 | AVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEDNQWICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLRHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHSGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVI... | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity)... |
Q1JJ36 | MAKPTRKRRVKKNIESGVAHIHATFNNTIVMITDVHGNALAWSSAGALGFKGSRKSTPFAAQMAAEAAAKSAQEHGLKTVEVTVKGPGSGRESAIRALAAAGLEVTAIRDVTPVPHNGARPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3. Belongs to the universal ribosomal protein uS11 family. |
Q9H5E9 | MLSPVSRDASDALQGRKCLRPRSRRLPLPAAVRAHGPMAELTDSARGCVVFEDVFVYFSREEWELLDDAQRLLYHDVMLENFALLASLGIAFSRSRAVMKLERGEEPWVYDQVDMTSATEREAQRGLRPGCWHGVEDEEVSSEQSIFVAGVSEVRTLMAELESHPCDICGPILKDTLHLAKYHGGKARQKPYLCGACGKQFWFSTDFDQHQNQPNGGKLFPRKEGRDSVKSCRVHVPEKTLTCGKGRRDFSATSGLLQHQASLSSMKPHKSTKLVSGFLMGQRYHRCGECGKAFTRKDTLARHQRIHTGERPYECNECGK... | May be involved in transcriptional regulation. Belongs to the krueppel C2H2-type zinc-finger protein family. |
B3PHR3 | MLGLIQRVRRASVEVDQQVVGEIDQGMLLLLGIQKTDTEASADKLIDKLLAYRLFADADNRMNCNLQQVDGGILVVSQFTLAADTKKGLRPSFSSAAPPAQAQQLYDYFVTQLRSRHAKVATGIFAADMQVSLVNDGPVTFMLEMD | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... |
P06504 | MSKAGTKITFFEDKNFQGRHYDSDCDCADFHMYLSRCNSIRVEGGTWAVYERPNFAGYMYILPRGEYPEYQHWMGLNDRLSSCRAVHLSSGGQYKLQIFEKGDFNGQMHETTEDCPSIMEQFHMREVHSCKVLEGAWIFYELPNYRGRQYLLDKKEYRKPVDWGAASPAVQSFRRIVE | Crystallins are the dominant structural components of the vertebrate eye lens. Monomer. Has a two-domain beta-structure, folded into four very similar Greek key motifs. Belongs to the beta/gamma-crystallin family. |
Q1JM42 | MELQFLGTGAGQPAKQRNVSSLALKLLDEINEVWMFDCGEGTQRQILETTIKPRKIRKIFITHLHGDHIFGLPGFLSSRSFQASEEQTDLDIYGPIGIKTYVLTSLKVSGARVPYQIHFHEFDDKSLGKIMETDKFEVYAERLAHTIFCMGYRVVQKDLEGTLDAEALKAAGVPFGPLFGKIKNGQDVELEDGRLICAKDYISAPKKGKIITIIGDTRKTSASVKLAKDADVLVHESTYGKGDERIARNHGHSTNMQAAQIAHEAGAKRLLLNHVSARFLGRDCRQMEKDAATIFENVKMVQDLEEVII | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the ... |
Q04E23 | MAKKDKHDDALARNRRASFNYFIGETYEAGIQLTGTEIKSVRLGQITIGDAYITVRDQQAFLNNANISPYKQGNQFNVDPLRRRKLLLHKKEILALDRAVSKEGKTIVPLRVYIVKGFAKILIAIGTGKKNYDKRQTIKERDLKRELGKNLKNFH | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... |
B7JJ50 | MNEQQRLASQQVNSSTKKEEKDYSKYFESVYQPPSLKDAKKRGKEEVKIERDFGLPEEFRNFGTGRKFYIRTYGCQMNEHDTEVMAGIFTALGYEPTFSTEDADVVLLNTCAIRENAENKVFGELGHLKSLKRRNPDLLIGVCGCMSQEESVVNKIMQKNQHVDMVFGTHNIHRLPYILKDAMFSKETVVEVWSKEGDVIENLPKVRRGDIKAWVNIMYGCDKFCTYCIVPYTRGKERSRRPEDIIQEIRHLAANGYKEITLLGQNVNAYGKDFEDIEYGLGDLMDELRKVDIARIRFTTSHPRDFDDHLIEVLGKGGNL... | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-me... |
Q8P001 | MSERGLLIVFSGPSGVGKGTVRQEIFSTPDHKFEYSVSMTTRPQRPGEVDGVDYFFRTREEFEELIKTGQMLEYAEYVGNYYGTPLTYVNETLDKGIDVFLEIEVQGALQVKSKVPDGVFVFLTPPDLDELEDRLVGRGTDSQEVIAQRIERAKEEIALMREYDYAVVNDEVALAAERVKRIIETEHFRVERVIGRYDKMIKITKNPFKAK | Essential for recycling GMP and indirectly, cGMP. ATP + GMP = ADP + GDP Belongs to the guanylate kinase family. |
O27957 | MLYLGVIGYPIKHSVSPAMHNAALQHEGIEGIYLAFEVKPDRLRDAVFGAKALGFRGLNVTIPFKESVVEFVELEGEAAKIKTVNTIDLVEMVGYNTDVYGVKAALSGTELGGKTALVVGAGGAGKAAALALLDMGSTVIVANRTEEKGREAVEMLRRYGECIFWPLSRVEELKGKVDVVVNATPLGMRGFKAEIPVPPSMLDGVELVFDTVYNPMETPLIREAKKRGCKVVYGIEMLVHQGAKAFEIWTGIEPDVGVMREAALRALRF | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH Metabolic intermediate biosynthesis; chorismate biosynthe... |
B4S5M6 | MELKVINTAGAETGEVISLDDKVFAAKVSEHAVYLDVKSLLANKRQGTHKVKNRSEVRGGGKKPYRQKGTGHARQGSSRSGLMSGGGSIFGPQPHGYDLKVNRKIKRLARRSALSSKAGEGRIIVIEDFTFEQIKTRQFADILKNLGLDQKKTLVLLPEHNEIINRSGRNIPVLNIRVADQASTYDILDCQTVVMQKAAVKKIEETLA | One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. Forms part of the polypeptide exit tunnel. Part of... |
Q2GLH3 | MVGYIGDIHISESDAEVAECLSAEYKRQNTSLQMIASENFVSRAVLQAQGSVLTNKYAEGYPGSRYYCGCSEVDVAETLAVERLCKLFGCKYANVQPHSGSQANQQVYMALLKPGDTVLGMSLDSGGHLTHGAGPNVSGKWFNAVPYNVRRDTNLLDMGEIEEIALRVKPNLIIAGASSYPRRIDFKAFRAIADKVGAYFLADIAHYSGLIAGGQYPTPFGYAHVVTSTTHKTLRGPRGGVIMTDDEEIHKKLRSAVFPGMQGGALMHVIAAKAVAFREAMSPDFKVYVSQILDNSRALAAVLATGGLDVVTGGTDSHMV... | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent a... |
Q7U9K4 | MDTHAFKRSLHHSERYNRRGFGRAEEVAESLEQAYQSGLIGTIRDNGYKLSHGRLTVRLAEAFGFCWGVERAVAMAYETRKHYPAERLWITNEIIHNPSVNDHLREMDVQFIPVEQGVKDFSGVTSGDVVILPAFGATVQEMQLLNERGCHIVDTTCPWVSKVWTTVEKHKKHTITSIIHGKVKHEETLATSSFAGTYLVVLDMEEAQIVADYILGKGDRDAFMQRFSAACSPGFDPDRDLSRLGVANQTTMLKSETEEIGRLFERTMLSKYGPAELNDHFVAFNTICDATQERQDAMFSLVDEPLDLMVVIGGFNSSNT... | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredox... |
Q1C744 | MKLLKDSGAALLALFFVLVYLLPVNSRLLWQPDETRYAEISREMLQRGDWVVPYFMDIRYFEKPVAGYWFNNISQWIFGDSNFAVRFGSIFSTALSAVLVYWLATLLWRNRSTSVLATLIYLSFLLVFGIGTYAVLDPMISLWLTAAMVSFYLTLKAENWQQKVGAYALLGVACGMGFMTKGFLALAVPVIAVLPIVIQQKRIKDLVVFGPIAIVCAVLLSLPWALAIAQREPDFWNYFFWVEHIQRFAEASAQHKSPIWYYLPILCIGVLPWLGLLPGALFKGWRERATKPELFFLLSWVVMPLLFFSVAKGKLPTYIL... | Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate... |
A8Z1Q8 | MEHTIAVIPGSFDPITYGHLDIIERSTDRFDEIHVCVLKNSKKEGTFSLEERMDLIEQSVKHLPNVKVHQFSGLLVDYCEQVGAKTIIRGLRAVSDFEYELRLTSMNKKLNNEIETLYMMSSTNYSFISSSIVKEVAAYRADISEFVPPYVEKALKKKFK | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Homohexamer. Belongs to the bacterial C... |
Q979T3 | MGRKEDNIEKALRIVEHTELVRNIGIVAHIDHGKTTLSDNLIAGAGMMSEELAGKQLVLDYDEQEQARGITINAAVASMVHAFQGKEYLINLIDTPGHVDFGGDVTRAMRAVDGVIVVVDSVEGVMPQTETVIRQALREYVKPVLFINKIDRLINELRLNSDEMQKRFTKIISDVNKLISKYAPKEFTKEWQVSVQDGKVAFGSAYNNWAISVPSMAETKITFKDIVEYVKNGKQKELAQKNQLHKIILNMVIRHLPDPKTAQSYRIKQIWKGDLETEVGKSMVSCDFKGPVAMMVTKIIIDPHAGEIAIGRLFSGTVKK... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... |
Q4UT63 | MHRIAVPAAKGAPTAQAPVKVAARNLDFYYDKYHALKGINIEIPEKRVTALIGPSGCGKSTLLRIFNRIYALYPKLEARGEVLLDGENILSPKYPMNRLRSKVGMVFQKPVPFPMTIFENVAYGIRHHEKLSKADMQNRVEHALRQGALWDEVKDKLGQSALGLSGGQQQRLCIARAVALRPDVLLLDEPTSALDPISTSRIEQLVEELKRDYTIVIVTHNMQQAARVSDYTAFMYLGDLIEHDRTETIFSQPSKQQTEDYITGRFG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in) The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein... |
A1INV5 | MPDFSMSNLAVAFSITLAAGLFTVLGSGLVMFSKTPNPRVLSFGLAFAGGAMVYVSLTEIFSKSSEAFAEIYDKDHAFAAATMAFLAGMGGIALIDRLVPNPHETLDAQDPSFQESKRRHIARVGMMAAFAITAHNFPEGLATFFATLENPAVGMPLALAIAIHNIPEGISIAAPVYFATRSRKKTVWACLLSGLAEPLGAALGYLVLQPFLSPAVFGSVFGVIAGVMVFLALDELLPAAKRYSDGHETVYGLTMGMAVIAVSLVLFHF | Mediates zinc uptake. May also transport other divalent cations (By similarity). Belongs to the ZIP transporter (TC 2.A.5) family. ZupT subfamily. |
Q15UW6 | MNLHEYQGKQLFAEYGLPVSEGYAAETPQAAVEAADRIGGTEWVVKCQVHAGGRGKAGGVKLVKNKDEIKAFAQKWLGQNLVTYQTDEAGQPVSKILVESCTDIAQELYLGAVVDRASRRVVFMASTEGGVEIETVAEETPEKILKAEIDPLVGAQPYQAREIAFKLGLKGVQIKQFTQIFMGLAKLFEEKDIALIEVNPLVIKDDGNLHCLDAKVAMDSNAAYRQPKLQEMHDPSQEDAREAQAAKWELNYVALDGNIGCMVNGAGLAMGTMDIVNLHGGSPANFLDVGGGATKERVAEAFKIILSDSNVAAVLVNIFG... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinat... |
Q313K7 | MTKKKSSGGALIAQNKKARHLYELLEFFEAGIALAGTEVKSLRAGQVSFTDSYVTIHNNEAWIVGMHIAPYANAGYVQHDPDRDRKLLLHAREIDTLRARVEQKGLTVVPVKLYFKNSRVKLEIAVGRGKKLHDKRQDIKQRDVERETRREIMRH | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... |
Q8NLG1 | MKLILTAAVENLGVAGDIVEVKNGYGRNLLLPRGLAIVATPGAEKQIEGIKRAQEAREIRDLDHAREVKVALEALEGVTIAVRTSESGKLFGSVKTDDIVDAVKAAGGPNLDKRAIVLPKNLVKTTGKYQVEAKLTDGIVSRVKFEVVAA | Binds to the 23S rRNA. Belongs to the bacterial ribosomal protein bL9 family. |
A7X426 | MHFETVIGLEVHVELKTDSKMFSPSPAHFGAEPNSNTNVIDLAYPGVLPVVNKRAVDWAMRAAMALNMEIATESKFDRKNYFYPDNPKAYQISQFDQPIGENGYIDIEVDGETKRIGITRLHMEEDAGKSTHKGEYSLVDLNRQGTPLIEIVSEPDIRSPKEAYAYLEKLRSIIQYTGVSDVKMEEGSLRCDANISLRPYGQEKFGTKAELKNLNSFNYVRKGLEYEEKRQEEELLNGGEIGQETRRFDESTGKTILMRVKEGSDDYRYFPEPDIVPLYIDDAWKERVRQTIPELPDERKAKYVNELGLPAYDAHVLTLT... | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... |
A1T5H1 | MTTPLTFDNIRRAPKALLHDHLDGGLRPSTVLELAEQYGYEDLPAHDADGLATFFRTAAHSGSLVRYLEPFAHTVGVMQNPDALHRVARECVEDLAADNVVYAEVRFAPELHIDGGLSLDAVVDAVLAGFADGEKAAAADGRAITVRCLVTAMRHAARSREIAELAIRFRDKGVVGFDIAGAEAGYPPSRHLDAFEYMRSNNARFTIHAGEAFGLPSIHEAIAFCGADRLGHGVRIVDDIEIDADGNAKLGRLASLLRDKRIPFEMCPSSNVQTGAVASIAEHPFDRLARLRFRVTVNTDNRLMSDTSMSMEMLRLVEAF... | Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. adenosine + H(+) + H2O = inosine + NH4(+) 2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+) Binds 1 zinc ion per subunit. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subf... |
B4SYJ9 | MKLQLVAVGTKMPDWVQTGFTEYLRRFPKDMPFELIEIPAGKRGKNADIKRILDKEGEQMLAAAGKNRIVTLDIPGKPWDTPQLANELERWKQDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITTNHPYHRE | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine Homodimer. Belongs to the RNA methyltransferase RlmH family. |
A6WS34 | MSAAIVNAVKQCGYFNQGQCLSCRHIQQPLAQQVAVKTQTLQQLLAPFIPANSAELFLPPITGDDSGFRNKAKMVVLGAAHEPVLGIVSPSGEAVDLCDCLLYPGDMQALLHRLTRFVQQAGLPPYRVDKAKGELKFILLTRSQVRGEYLLRFVLRSHNGIERIERELPALLAEYPQIKVVSVNIQPIHMAILEGDEEIFLTENTRLEERFNHVPLFIRPKSFFQTNPQVAAQLYQTARDWVAEFSPRSLWDLFCGVGGFGLHCASNDITLTGIEIEAEAIACAQMSAQMMGLENVQFMALDSTDFAKGKSAADKPDLII... | Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfami... |
Q07VD3 | MPDPMRSYLDFEKPVAELDSKIDELHALAAGGSNIGEEIAKIEEKALAALTELYAALTPWQKTQVARHPQRPHCVDYIEGLITEFTPLAGDRKFGEDEALIGGFGRFRGESVCVLGQEKGFSTETRLKHNFGMARPEGYRKAVRLMEMADRFGLPVLSLVDTAGAYPGIGAEERGQAEAIARSTEACLKLGVPNVAVVIGEGGSGGAIAIATANKVLMLEHAIYSVISPEAASSILWRDSSKAQEAATSMKITAQDLLRFGVIDQILTEPRGGAHRDSAAMIAKAGDAIAKSFADLSSLDSDAIRAQRRQKFLDIGRKLG | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-... |
Q81E30 | MEKVDVKESAVGREMRIRKQWNEQNIFEQSIQNREGAQSFVFYEGPPTANGLPHVGHALGRTIKDLVARYKTMAGYKVLRKAGWDTHGLPVELGVEKQLGISGKHEIEEYGIEPFIQKCKESVFTYEKQWREFTESIGYWVDMDDPYVTLKNPYIESVWHILGTIHEKGLLYKGHRVSPYCPSCQTSLSSHEVAQGYKTVKDLSATVKFKVKDSENEYFLGWTTTPWTLPANVALAVHPNMEYVKAKQESHVYIVAKERVQEVLKENYEVLSVHKGEELLNTSYTAPFPMKEVTNGYRVIAADFVTGDSGTGLVHIAPAY... | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrol... |
Q5E8Q8 | MIIKQLPLTDLHRHLDGNIRIETILDLGQKFGLDLPAYDIEALRPHVQIVEAEPSLVAFLSKLDWGVAVLGDLDACRRVAYENVQDAMNAQIDYAELRFSPYYMAMKHNLPIAGVVEAVVDGVEAGCRDFGIKANLIGIMSRTFGQDACQQELDGLLTQKHKLVAIDLAGDELGQPGDLFVNHFKQVKDADLRVTVHAGEAAGAASMWQAINELGAVRIGHGVKAIEDPKLMEYLAKNNIGIESCLTSNIQTSTVASFESHPIKTFLDYGVKVCLNTDDPAVEGIELPHEYEVAAPKVGLTPEQLKQIQINGLDLAFLSD... | Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. adenosine + H(+) + H2O = inosine + NH4(+) 2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+) Binds 1 zinc ion per subunit. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subf... |
B8K287 | MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVVLTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNMSLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDLDFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQREVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKA... | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:18674515, PubMed:18719240, PubMed:... |
Q9CUH3 | MKLIIYLTILAGTALVTHSSVQKEDHAPYLAYLKSNFNPCVGVLIKASWVLAPSHCYLPNLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLMLIKLAKPATFNHKVQVLPIATTNVRPGTVCTLSGLDWSQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSSHRNSLCVRFVKVFSRIFGEVAVATVICKNKLQGIEVGHFMGGDVGIYTNIYSYVPWIEKTTKEKMT | Plays a role in male fertility (PubMed:23553430). May have a role in sperm migration or binding to zona-intact eggs (PubMed:23553430). Involved in the activation of the proacrosin/acrosin system (By similarity). Testis-specific (PubMed:23553430). Expressed in spermatids (PubMed:23553430). Weakly expressed in mature spe... |
Q72DU5 | MPPRPQRLAPVADLPPVFAGIDEAGRGCLAGPVVAAAVILPQEYALPGLTDSKKLTAARRESLAEGIRSCAVTWGIGVVWPRDIDRINILQATFRAMARAVRVLRQPPPAILIDGDKTLPPHVLTSLSCDGHLPTQRAIIGGDGCIPAISAASILAKTFRDRLMDTLDRRYHGYGFAKHKGYGTAEHLAAIAAHGPCAQHRLTFRGVRPNPAAEEQLTLW | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytic cleavage to 5'-phosphomonoester. Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. Belongs to the RNase HII family. |
A8M2A2 | MATRDSGGQSQTGRSQQGEEIEDVTTEASPEVAERHAEITEDVDDLLDEIDSVLEENAEEFVRGYVQKGGE | Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Protein degradation; proteasomal Pup-dependent pathway. Strongly interacts with the proteasome-associated ATPase ARC through a hydrophobic i... |
Q8HZN8 | FNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILGILHSCLNPLIYAFIGQKFRH... | Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity... |
Q1JF50 | MRYNQFSYIPTSLERAAEELKELGFDLDLQKTAKANLESFLRKLFFHYPDSDYPLSHLIAKNDMDALSFFQSEQELSKEVFDLLALQVLGFIPGVDFTEADAFLDKLAFPIHFDETEIIKHIHHLLATRCKSGMTLIDDLVSQGMLTMDNDYHFFNGKSLATFDTSQLIREVVYVEAPLDTDQDGQLDLIKVNIIRPQSQKPLPTLMTPSPYHQGINEVANDKKLYRMEKELVVKKRRQITVEDRDFIPLETQPCKLPIGQNLESFSYINSYSLNDYFLARGFANIYVSGVGTAGSTGFMTSGDYAQIESFKAVIDWLNG... | Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile. H... |
Q7D7Q0 | MTYVLDTNVVSALRVPGRHPAVAAWADSVQVAEQFVVAITLAEIERGVIAKERTDPTQSEHLRRWFDDKVLRIFVFARRGTNLIMQPLAGHIGYSLYSGISWF | Toxic component of a type II toxin-antitoxin (TA) system. An RNase. The cognate antitoxin is VapB14 (By similarity). Belongs to the PINc/VapC protein family. |
A8GYX9 | MAVIKCKPTSPGRRHLVKVVNSDLHKGKPFAGLLAKKSKSGGRNNTGRITVRHIGGGHKQHYRLIDFKRNKDGIPAKVERLEYDPNRTANIALVLYADGERRYILAAKGMKAGDKIQSGIDAEIKSGNALPLRNIPVGSVVHAVEMKPAKGAQIARSAGAYVQVIARDGAYATLRLRSGEMRKVPVDCRATLGEVGNAEHMLRQLGKAGAKRWRGVRPTVRGVAMNPVDHPHGGGEGRTSGGRHPVSPWGQPTKGYKTRSNKRTDKYIVRRRNKK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. ... |
Q4V7W5 | MTSGNGSSPVPTAATGNRTQNGENKPPQAVVKPQILTHFIEGFVIQEGAQPFPSHRSRAVLEVGHSSLLTGAQEKYQQSLLAEKVPQQDNNTTTTTTDSEMEETLVPGFPESKGDGDPPKLKCELCGRVDFEYKFKRSKRFCSMACAKRYNVGCTKRVGLFHPDRSKLQKPTVAKHARRRSRKTPLQTVGADPKKQQAAPVTPMNPGPIPSPSALKLSNSQEDSSRCSDNSSYEEPLSPMSASSSLSRARQEHNVEPPNLHSRDPIAMSQDFLPSDPTKWNVEDVYDFVRSLPGCQEISEEFRAQEIDGQALLLLKEDHL... | Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histo... |
Q9HJ17 | MYKGIVTPMITPMGQNGEIDYRATEILIDNLADFGVDGLFPMGSTGLFPMFSTDEKKKFLGFVRDHSKKIEVYAGVGSSSTQESVELSKYTEDIGIKVRVLMPTYYIKPDEDWMYRHFSTVISAASNDLFIYNIPQLSGSWISESLIEKLTREFSNVKGIKDSSGDMRFFSRIIRHKNEKFDIFQGQDDLLFLSLSIGASGGVCGLSNISPYITNLYHEFSAGNLEKARKIQIDEVNPLMYAINEATFPAGYYYAFYKMNGIKGGYRAPMVEPTTDQKKKIDQELTKIPKKQ | Homotetramer. Belongs to the DapA family. |
Q13520 | MDAVEPGGRGWASMLACRLWKAISRALFAEFLATGLYVFFGVGSVMRWPTALPSVLQIAITFNLVTAMAVQVTWKASGAHANPAVTLAFLVGSHISLPRAVAYVAAQLVGATVGAALLYGVMPGDIRETLGINVVRNSVSTGQAVAVELLLTLQLVLCVFASTDSRQTSGSPATMIGISVALGHLIGIHFTGCSMNPARSFGPAIIIGKFTVHWVFWVGPLMGALLASLIYNFVLFPDTKTLAQRLAILTGTVEVGTGAGAGAEPLKKESQPGSGAVEMESV | Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism. Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Belo... |
Q62821 | MSSEQVRAGSPGSRVPGARRTGAVWTAPSENLDSSTIPALCVSLLFPSQPLDVVVTMGHNTLGMRQLWKLALQRPQLLSGSTGVKPQWQQTAPSFHLNVKQENPIEPYNVKNEQSYAEYMEHFGKKGKLLDQIDDTRSAPSTSRSKVKSPHKERENFRSTLVNVIMQQDSSLEPDVTDESGIPKATTSAIEKDILRYYYYIHHGIDTDNVAPMEDSWLEHVLQLVPQHLKVLTNSITVLSDEMREDYLLSVKKSIVDFVLKDPREKEDDTKITELPPHRAEMEVLPKPWRRSFLSACSYIRDHLNAMNPTMLAVLDLWHS... | Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). The dynein complex consists of at least two heavy chains and a number of intermediate and light chains... |
A4TMZ6 | MSVVPVVDVLQGRAAVGSEVTVRGWVRTRRDSKAGISFVAVYDGSCFDPLQAVVNNTLPNYQDEVLHLTTGCSVEVTGTVVASPGEGQSFEIQATAINVVGWVDDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQAIHRFFDENGYFWVSTPLITASDTEGAGEMFRVSTLDLENLPRTDTGAVDFSEDFFGKEAFLTVSGQLNGETYACALSKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFASLDDVAGLAEKMLKYVFQAVLNERADDMKFFAERVDKDAVDRLQRFVTSDFAQVDYTDAIEIL... | ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. |
Q2GDJ8 | MTVIKELNFGPQHPAAHGVLRLIMQLDGETVERLDPHIGFLHRGTEKLIEHKTYLQALPYFDRLDYVSPMAQEHAYSLCVEKLLGITVPPRAQYLRVIFVEITRILNHLLNVTTHALDVGAMNPLFWMFEEREKMLSFYEKASGARFHAAYIRPGGLAADIPDGLDEEIMSFLESFTHKLDDVADVLTDNPIFKQRLVDIGKVSKREAVALGFSGPVLRASGVPWDLRKSQPYEVYESLDFAIPVGSCGDSYDRYLVRMAEMYESVKIIKQCIDKLPEGPVVVDDRKVAPPSRAEMKTSMEALIHHFKLYSEGYHVPEGE... | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... |
P49504 | MPVKEKVGIVVSNKMQKTIVVKVESRYSHPIYSKTMTKTRKYLAHDEMGECNIGDQVLVQECRPLSKRKRWTLSKVLSKSSLVS | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. Part of the 30S ribosomal subunit. Belongs to the universal ribosomal protein uS17 family. |
B8BJ22 | MAAAPVLLLAAAAAVVVVAMVLRWLLLLGGPAAGRLGKRALMPPGSTGLPLIGETLRLISAYKTPNPEPFIDERVARHGGVFTTHVFGERTVFSADPAFNRLLLAAEGRAVHSSYPSSIATLLGARSLLLTRGAAHKRLHSLTLTRLGRPASPPLLAHIDRLVLATMRQWEPAATVRLMDEAKKITFNLTVKQLVSIEPGPWTESLRREYVKLIDGFFSIPFPLANLLPFTTYGQALKARKKVADALREVIKKRMEEKAENGGSIGDDEGKKEKKDMVEELLEAEGGSFSEEEMVDFCLSLLVAGYETTSVLMTLAVKFL... | Catalyzes the C23-alpha-hydroxylation step in brassinosteroid biosynthesis (By similarity). Converts 6-deoxocathasterone (6-deoxoCT) to 6-deoxoteasterone (6-deoxoTE) in the late C6-oxidation pathway and cathasterone (CT) to teasterone (TE) in the early C6-oxidation pathway of brassinolide (BL) biosynthesis (By similari... |
Q98N66 | MAQTQTFNGRRRVRKFFGKIPEVAEMPNLIEVQKASYDQFLMVDEPKGGRPDEGLQAVFKSVFPISDFSGSSMLEFVKYEFEGPKFDVDECRQRDLTYAAPLKVTLRLIVFDIDEDTGAKSIKDIKEQDVYMGDMPLMTLNGTFIVNGTERVIVSQMHRSPGVFFDHDKGKSHSSGKLLFAARVIPYRGSWLDIEFDSKDVVHARIDRRRKIPVTSLLMALGMDGEEILSTFYNKITYVRAGDHWRIPFNVERFRGLKAVGDLVDADTGEIVVEAGKKITARQARQLGEKGLKAIKATDEDLLGNYLAEDIVNYATGEIF... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with ... |
B8ZKQ6 | MAYRKLGRTSSQRKAMLRDLTTDLLINESIVTTEARAKEIRKTVEKMITLGKRGDLHARRQAAAFVRNEIASENYDEATDKYTSTTALQKLFSEIAPRYAERNGGYTRILKTEPRRGDAAPMAIIELV | Part of the 50S ribosomal subunit. Contacts protein L32. Belongs to the bacterial ribosomal protein bL17 family. |
Q5FLX8 | MLQPIGDRVIVKVKEEEEKTVGGIVLASNAKQKPTEGEVVAVGEGAYTSNGDKLPMVVKKGDVVLYDKYSGTNVEYEGEKYLVLHEKDILAIEK | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... |
Q30KM0 | MALIKKTFFFLFAMFFILVQLSSGCQAGLDFSQPFPSGEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFLCCRQRI | Has antimicrobial activity. Belongs to the beta-defensin family. |
Q55GG1 | MNPIQPIPKSKIEIRIKCKDLTSKDLLSQSDPQAIVYLKQQQRNDWIQQGKTEKLKNQKSPEFKQSITVDYHFEEVQLLKIVVIDIDKDIKLLKDFDDHDLIGEVNVSLGSILSSPGGRMKMSLTKNGILSGSITISTEEIRETGANIYFALEGNHLDKKDLLSSDPYFKIYKSGGTLVYQSDVIKNTLNPTFPPVYLKLEELNGGDMFRELTFEFMDWDKIGDHDLIGRFTTNTDTILRGGALEFEIINPKKVGKSGYKNSGIIKFYIARIQGDPTFLDYLHGGLEINLMVAIDCTASNMPPDVSTSLHYNTPTQPSQY... | Expressed at relatively high levels in vegetative cells. The expression goes down until the 8th hour of development and then goes up at 14 to 16 hours. Belongs to the copine family. |
Q0WWH1 | MESIMEEADSYIEYVSVAERRAIAAQKILQRKGKASELEEEADKEKLAEAKPSLLVQATQLKRDVPEVSATEQIILQEKEMMEHLSDKKTLMSVRELAKGITYTEPLLTGWKPPLHIRKMSSKQRDLIRKQWHIIVNGDDIPPPIKNFKDMKFPRPVLDTLKEKGIVQPTPIQVQGLPVILAGRDMIGIAFTGSGKTLVFVLPMIMIALQEEMMMPIAAGEGPIGLIVCPSRELARQTYEVVEQFVAPLVEAGYPPLRSLLCIGGIDMRSQLEVVKRGVHIVVATPGRLKDMLAKKKMSLDACRYLTLDEADRLVDLGFE... | ATP + H2O = ADP + H(+) + phosphate The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Belongs to the DEAD box helicase family. DDX41 subfamily. |
Q9SVW1 | MAVPLLTKKVVKKRSAKFIRPQSDRRITVKESWRRPKGIDSRVRRKFKGVTLMPNVGYGSDKKTRHYLPNGFKKFVVHNTSELELLMMHNRTYCAEIAHNVSTKKRKAIVERASQLDVVVTNRLARLRSQEDE | Belongs to the eukaryotic ribosomal protein eL32 family. |
B5XRE3 | MASYDLVERLNDTFRQIELELQTLQQALSSCRLLAARVFELPAVSKDAEHDPLANIPVVQHSGKAALALALRHYSHLFIQQQSENRSSKAAVRLPGAICLQVTAAEQQDLQARIQHINALKATFEKIVTVDSGLPPTARFEWVHRHLPGLITLSAYRTLTPLIDPSTIRFGWANKHVIKNLTRDQVLMMLEKSLQSPRAVPPWTREQWQSKLEREYQDIAALPQRARLKIKRPVKVQPIARVWYASEQKQVQYACPSPLIALISGSQGVSVPDIGELLNYDADNVQYRYKPEAQSLRLLIPRLHLWLASE | Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence. Belongs to the Tus family. |
P81509 | DCPSDWSSYEGHCYRVFQQEMTWDDAEKFCTQQHTGGHLVSFRSSEEVDFLVSILKFDLFWMGWRDIWNERRLQWSDGTKVNYKAWSAEPECIVCRATDNQWLSTSCSKTHNVVCKF | Binds to the subunit GPIbalpha (GP1BA) of the platelet GPIb/V/IX receptor system. It inhibits ristocetin- and vWF-induced platelet aggregation in platelet-rich plasma by inhibiting the binding of vWF to GPIbalpha. Heterodimer of subunits alpha and beta; disulfide-linked. Expressed by the venom gland. Belongs to the sna... |
A6V7Y9 | MNADHAPFRHYLDLADARLGSQVVAVSDEWFAPASRMLQAGEPVWKEGVFDDSGKWMDGWETRRKRFEGHDQAVIRLGVSGVLKGVDIDTRFFTGNHPPAASLDGCFCAEGDPDDGTSWSEVLPSVELQGDRHHYHAIDDERPWTHLRLNIYPDGGIARLRVYGVPYRDWRSQTPGTALDLAAAINGGRALACSDQHFGPMVNLLKPGRALNMGDGWETGRRRTPGHDWAIIALGHPGSIEAAVVDTLHFKGNYPESCSIQAAFVEDGNEARIEAQSLFWRELLPAQKLEMHHEHRFERQLNALGPVSHVRLNIFPDGGV... | allantoate + H2O = (S)-ureidoglycolate + urea Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. Belongs to the allantoicase family. |
B1LM86 | MKKPVVIGLAVVVLAAVVAGGYWWYQSRQDNGLTLYGNVDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLMLAGYRDEEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQYRSGNREQDIAQAKASLEQAQAQLAQAELNLQDSTLIAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPV... | Belongs to the UPF0194 family. |
Q7XY82 | MAFISGPALPTARVNRTVAATPVRMASGEDTPVVSRRALLSSTLAAAAAALLSAAAPAKADREYGNVGFLGGGDKIDVNNANVRVYGRLPGMYPTLAGLIVANGPYKSVGDLYNIPGLDDKQTGLLKKYEDSFVALEPRPEYEIDKFNNGLYR | Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. The oxygen-evolving complex in red algae is composed of PsbO (OEC33), PsbQ', cytochrome c-550 and PsbU. Associated with photosystem II at the lumenal ... |
Q6B8U0 | MLDIISLGWGSLLAIFSFSIALVVWGRNGF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rie... |
P37282 | MSKDIKFSSDARTAMMRGIDILADTVKTTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVREGLKNVTAGANPVGIRRGIELAAETAVASIKEMAIPVHDKSAIAQVATVSSRSEKVGEYISDAMERVGSDGVITIEESKGMQTELDVVEGMQFDRGYLSQYMVSNTEKMVAELDNPYILITDKKISNIQEILPLLEQILKTNRPLLIVADDVDGEALPTLVLNKIKGVFNVVAVKAPGFGDRRKAQLEDLAILTGGTVITEELGLDLKDATLEALGQAAK... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. ATP + H2O + a folded polypeptide =... |
Q14C12 | MAPRPLGPLVLALGGAAAVLGSVLFILWKAYFGRGRERRWDRGEAWWGADTARLPQWDEWEPEDEEDEPALEELEQREVLVLGLDGSGKSTFLRMLAGKPPVEGHVPTWGFNSVRLPTKNFEVDLLEIGGSQNLRFYWKEFVNEVDVLVFMVDSTDRLRLPWARQELQKLLDRDPDLPVVIVANKQDLSGAMNMVELQQELGLLASYNQREVFLLAASIAPAGSGFGEPGTVHIWKLLLQLLS | Belongs to the small GTPase superfamily. Arf family. |
V5IPD9 | MSLPRRPGPSPPHEEPRRYRQSGSRRSRPPPADVETGYAPMAGERPSQQQRVPSISSFPETLPSPNPNVERDPLAPTPEPAHPSGIPQRKRSLIRPERNRIGKDHPNYHYRKHAANMNTLPSSTGHDPIYEDLEGATDDVSGTGSRNDDDVSEESPPRRKHSTKMQVIETEKSGDERRRRRKSDTTKHGKIVKASKGKREKSGGLPTPSFWNIYCGFVTFWCPGFVLKCFGMPEMAQQRAWREKMGLISIILLIMGFVGFITFGFTQVVCGKPPLRLRINEVGSGYMIFHGSAYDLTKSHHPPAEGIPRRPDGLGANVIY... | Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP Belongs to the... |
C4K2H7 | MSSYKYYDLIRKPIITEKTTTLSEQNKYAFYVDKFAEKLTIKKAIEEIFKVKVKKVNILNVKGKKKRFKGIIGTQINRKKAIVTLEKDHNIDFAGGIK | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the... |
Q2G8E3 | MRAMQTHTEIAPMPIPGHVDPVPVPREVTPREDGRIDLIGLPRKQIAELFAQAGLDAKAAKLRAKQVFHWLYHRGVTDFDAMTDIAKTMRPWLAERFVIGRPEIVEAQVSTDGTRKWLLRTADKHDFEMVFIPDADRGTLCVSSQVGCTLNCRFCHTGTMRLVRNLTPGEIVGQVMLARDALGEWPKGANDSRVATMAGLDFDDEDEGSYTSDGRLLTNIVMMGMGEPLYNFDNVRDALKLVMDGDGLALSKRRITLSTSGVVPMMERCGEEIGVNLAVSLHAVTKDVRDEIVPINRKYGIEELLQACADYPGASNARRI... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. adenosine(2503) in 23S rRNA + 2 reduced [2Fe-... |
Q5N893 | MVPREQAEEAIVADSNGKEEEVGVMGVSAGEHGADDHHGGGGKFSMKNLLWHGGSVWDAWFSCASNQVAQVLLTLPYSFSQLGMLSGVLLQLFYGFMGSWTAYLISVLYVEYRSRKEKEGVSFKNHVIQWFEVLDGLLGPYWKAAGLAFNCTFLLFGSVIQLIACASNIYYINDRLDKRTWTYIFGACCATTVFIPSFHNYRIWSFLGLGMTTYTAWYLAIAALLNGQAEGITHTGPTKLVLYFTGATNILYTFGGHAVTVEIMHAMWKPAKFKYIYLLATLYVFTLTLPSASAMYWAFGDELLTHSNAFSLLPKTGWRD... | Carrier protein involved in proton-driven auxin influx. May mediate the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips (By similarity). Belongs to the amino acid/polyamine transporter 2 family. Amino acid/auxin permease (AAAP) (TC 2.A.18.1) subfamily. |
Q2U9B0 | MPVAEASPVASSEPGFVKMEDRKRAATSDHNDSAPPLKKQATSVNGGSKPHPDADMPWKDDLEVSLGLAGVVGFMSFQGGLRYPSSAEPTTSLTIKDAIWRQMQEYKREKVSLEAKLKDMSKAATRHNEHLRVIDTWYNQVCGSTLIDEVKLLLGAAEDIKGDRPTFQSSLSFDDVDNFEKHLKSRSNDIRDIISRLVKNTPKSPPEICELQSQLAKKLAEEKATIAELDKALSEKQQLEESLEEASLRYMVAEKKLDRARSLTVAKLEKQYILGPQRPGGDSASGQREEQSVSNGATPSAERGPELDEAHNKLVAISEK... | E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine ... |
Q8K997 | MLKDYLEITKPRIIIGNIILIIGSFLFSSFPFFNVFLFFFTILGTSLVIASSCIFNNLIDIDIDTKMNRTKNRVLVKNLISPTSASIFASFIGIVGFFILGLFVNILSMFLSFIGFVIYVFFYTFFLKRKSMYSTFIGSFSGSIPSVIGHTAISNSIDLFCFLLFIIFIFWQMSHFYAIAILYINDYRKANLPFFPVVKGILKTKKHIFYYITCFIIASSMLTFLGYLSYIFLLFFSFFSFYWLYISYLSIREKDDRKFSSKLFYYSIAVVILFNFLISIDFIF | Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1... |
B8GVE7 | MRVGLYPGTFDPVTNGHLDIIGRAVKLVDKLVIGVAINIGKGPLFSLEERVEILERETAHLKKIAEIEVRPFDSLLMHFARDVNAQMIVRGLRAVADFEYEFQMTAMNQQLDREIETVFLMADPRHQAIASRLVKEIATLGGDIGKFVPPGVAQQLLAKVGKG | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Homohexamer. Belongs to the bacterial C... |
Q58E95 | MDETDSQITCADSSVDKLSHLKRNEVKSCPLPELHGADEMLPELNKSCLTNPDILRYSRQLVLPDLGVQGQLKLSKASVLVIGCGGLGCPVAQYLAASGIGRLGLLDYDVVEMSNLHRQVLHGENRLGMSKSVSVAKTLRKLNSAVVYLPYHISLNPENALQIIQQYDIIADCSDNVPTRYLVNDTCVLAGKPLVSASALRWEGQLTVYNYHQGPCYRCLFPKPPPSETVTNCADGGVLGIVPGIIGSLQALEVLKIASGMAPSYSGVLLMFDALEGRFRNIKIRGKKNDCAACSNPSETAILQDYEAFCGSSASDKCRM... | Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs... |
Q8CQ78 | MSEKVKFEKRESLKEKPDTANLGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKHNGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIRPFVFATEGVLGVRSSHQYKLLIILSPSGAYYGGDTLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAYDKGELTEVFGSGTAAVISPVGTLRYEDREIV... | Acts on leucine, isoleucine and valine. 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2... |
Q4WHT9 | MPVTQFSHPDPYSYQTGFDSYHETEAVKGALPVGQNSPQKAPYGLYAEKLSGTAFTAPRHENKQTWVYRILPAAAHENFKAEDADSYHTSMTTETHKLHHIPNQLRWDPFDLDETVDWVHGLHLVAGAGDPTLKHGLGIILYAAGKDMGKEAFYSADGDFLIVPQHGVLDIQTELGRLMVRPNEICVIPRGVRYRVTLPAGPVRGYICELYQGHYQLPELGPIGSNCLANARDFQAPVASFEDEEEPTEWRLYSKFNNTLFSARQDHTPFDIVAWHGNYYPYKYDLGRFNTIGSISFDHPDPSIFTVLTGPSDHAGTAIA... | Homogentisate 1,2-dioxygenase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:19715768, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate... |
P48585 | MAIANKNIIFVAGLGGIGLDTSREIVKSGPKNLVILDRIDNPTAIAELKAINPKVTVTFYPYDVTVPVAETTKLLKTIFAQLKTVDLLINGAGILDDHQIERTIAVNFTGTVNTTTAIMEFWDKRKGGPGGVIANICSVTGFNAIYQVPVYSASKAAALSFTNSLARLAPITGVTAYSINPGITRTPLVHRFNSWLDVEPRVGELLLEHPTQTTLECAQNFVKAIEANKNGAIWQLDLGQLIAVEWTKHWDSHI | a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH Homodimer. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
C1CHW2 | MTKRVLISVSDKAGIVEFAQELKKLGWEIISTGGTKVALDNAGVDTIAIDDVTGFPEMMDGRVKTLHPNIHGGLLARRDLDSHLEAAKDNKIELIDLVVVNLYPFKETILKPDVTYADAVENIDIGGPSMLRSAAKNHASVTVVVDPADYAVVLDELAANGETSYETRQRLAAKVFRHTAAYDALIAKYFTAQVGESKPEKLTLTYDLKQPMRYGENPQQDADFYQKALPTDYSIASAKQLNGKELSFNNIRDADAAIRIIRDFKDSPTVVALKHMNPCGIGQADDIETAWEYAYESDPVSIFGGIVVLNREVDAATAEK... | (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Purine metabolism; IMP biosynthesis via de novo pathway; 5-form... |
D6VVV3 | MNLRFELQKLLNVCFLFASAYMFWQGLAIATNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE | Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:2644273, PubMed:7615509, PubMed:10206957, PubMed:11058593). Specifically cleaves N-terminal signal pept... |
P08479 | DPPPAIGREVDCSSYKGKGSQIACPRHLQPICGTDHNTYSNECMFCALTLNKEFEVRKLQDTACDIECTEYSDMCTMDYRPLCGSDGKNYSNKCIFCNAVVRSRGTIFLAKHGEC | This inhibitor is composed of two homologous actively inhibiting halves: one which inhibits trypsin, the other which inhibits elastase. |
P31921 | MLIKVNFMEHYLLNKQFELASAIKSRNKILIHKLVSDVLVSYNSLCYAVYKTLKNSDDKSSSNIQKKKKKKKNFQNLVDSLKCFVLNYDFYKIRCLNLYYLRNFIDCKDQFLHFHFLDIALQNLYSFIFFPFLESNLDKFTYGPRVFRSSIDAVKVLFLLGKQKKYSNYNKYLFCFAFNYTIVKCFDAVFNSWVLSNVSFIDKSILSFWVKNGFDNFYSGDQFFFQKKNFEINRGTSLIFLVIFNFVFMGMQFFLESSILSKFGFFSKFVLITDLNSVVILSSDLKTAKIVKSSLLIFFHSRGICQNFRDNSIVDFFCKN... | To group II intron maturases. |
B8IZT9 | MALEKTRGRRISVGETAVVVGAGRSGLAAARLLCREGAQVRLLDSNADAFSGREALAGELRQLGISIELGPHKPDQFENAAFVVPSPGMPVARLAGLVDEERAEILAEMELAWRYLENEPVLAVTGTSGKTTTASLAAAMLHEQGYAVFLGGNIGTPLSEYVLSGHKADVLVLEISSFQLQTCSTFCPRAGILLNITPNHLDYHKDMAEYTEAKFRLFRCQDEGDLAVLGESLRSLAARYGLKARQVYVSDAGRFSGSSLMGAHNRVNEEAAWQACRLFGVSEENAARALARFAPLPHRLERVRELEGVLFVNDSKCTTV... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate Cell wall biogenesis; peptidoglycan biosynthesis. Belongs t... |
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