ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A251S005 | MNYSYSSDEDDKPLVFKRTSAADKLKHSGQLKSASSADKLKHSGQLKSASSADKLKHSGQLKSASSADKLKHSGQIKSTSIVNREKPSTSTKPKPPAKQESDTEDSEDDKPLSARISTAPKTNSNHAKTGPVSASQRPKPQVKNDDSDDKKPLSSKFTSVGPSVKKPDDSDDDDKPLSARVKQNGSTSRDNNNNNNNNNNQLNKKPNIGLNKRPPNEERLAGQSSVKKPKLSDSEDENDHVPISQRMKKQTPSGSKPSSSVKQKVVKVNSSSFKKTFKKSNKFEKKSKYSKSSKVPPGSGEGQKWTTLVHNGVIFPPPYK... | Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile ... |
A0A251NC15 | MESSEEQKLQVRKLELSDKSKGFIELLQQLTVCDSVSDKDFEDRFRELNARAEDHRVLVIEEDRSGKIVATGSVFIERKFIRNCGKVGHIEDVVVDANARGMQLGKKIINALTDYAHSLGCYKVILDCNVENKAFYEKCGYKQKEIQMFERSWGTHMIKPFICLNKNWRSSSKSKHLAGGQVWTGKPIILENEYPRGLGSDLDLIAHPLLCFQSLQHSLLCLLVSGSTSNWFFYFIL | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
U9UPF8 | MSSETKAETSSGSNKINGKAKGNLNSYLLLYNAASWAGWTYVLTVSVLELFKNGGDVTKLYDRIGWTLTLVQTAAILEIFHVLLGLVRSPFITTVIQVSSRLTLVWLIVNKFPEVRSHWAFTSMTIAWSITECIRYAFYGLNLIGNQPGWLLWCRYTFFFILYPVGAGSESILVFESLRFAIRISQSFYWILVILLLIYVPGFYTMYNHMIGQRRKILGKGKVKKNQ | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A3T0I7W5 | TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDMAIFSLHLAGVSSILGAVNFITTVINMRSSGMSLDRMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A251SDR6 | MDKGVFLEKTKERSLKITPSWAVAVVVFVILAISIALEYILHLIGHWLQHKQKKSLHEALEKIKAELMLLGFISLLLTVGQEPIASICISSKVARTWHPCNDDSADTDFYDPCLKKGKVQMVSNYGIHQLHIFLFVLAVVHVAYCLLTLALGRLKMRRWKAWEDETRTSEYQYHHDPERFRFARETTFGRRHLRSWSTSSILMWIGCFFRQFFSSVAKVDYLTLRHGFINTHLNHLSPESQHKFDFHKYITKSLEEDFKEVVGISPIVWFFAVLLLLTNTHDWYAYLWLPFIPLVIILLVGAKLQLIITQMGRRTNDMAD... | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 553
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 63987
Location Topology: Multi-pass membrane protei... |
A0A7S3MQT2 | MAPKMTDFSKGTTTLAFEFQEGVLVAVDARATQGSFISSNQVRKVIEINDFLLGTMAGGAADCQFWEGYVAMLCRIHQLRHGEAPSVAMASMMLCSIMRQYKGYGLSMGTMFTGSDKTGASLYYIDNDATRLRGRLFAVGSGGTFAYGVLDTNYRYDMSLDEAVNLGIRAIASATFKDSASGGVVRIYHVTNNGDWNLVHDQIDVSQ | Function: Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Catalytic Activity: Cleavage of pe... |
R4J886 | EFRGLGDCLTKIYKSDGLFGLYRGFTVSVQGNFMYRASYFGFYDTVKGMLPDHLRRNILISWVVAQTVTTCSGIIAYPFDTL | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 82
Sequence Mass (Da): 9304
Location Topology: Multi-pass membrane protein
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K3ZQJ4 | MAQPLVVKKDDDLDEEEYYSPFLGIEKGAVLQEARVFHDPQLDARRCCQVITKLLYLLNQGDTFTKVEATEVFFATTKLFQSKDAGLRRMVYLMIKELSPSADEVIIVTSSLMKDMNSKTDMYRANAIRVLCRIIDSTLLTQIERYLKQAIVDKNPVVASAALVSGIYLLQTSPEVVKRWSNEVQEAVQSRAALVQFHALALLHQIRQNDRLAVSKLVTSLTRGSVRSPLAQCLLIRYTSQVIRESGTNQSGDRPFFDFLESCLRNKAEMVILEAARAITELNGVTSRELTPAITVLQLFLSSSKPVLRFAAVRTLNKVA... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
K4AL20 | MAAADCSGRRRFAVACGVLSRCVRAEAAAGKMVAAESHARAGSASTMLLMPGADVALDVVGEGAAEATPAPTRARLTIMHGGRVLVFDDVTADRAAELVRVAAGQQVILGGSRTTDDVPVARKASLRRFMEKRRDRIATRSPYAAAAAFPTAAENGKEGEADTAGCCLELGISGGSAC | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 178
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 18191
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A0A1E1FA49 | SGSTKEEIKTAVNNGVVKMNVDTDTQFAYLAGIRDFVIKKKDYLQTQVGNPEGS | Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or gl... |
A0A191T686 | MNLSVIIQLVVLALIVISGPVVIGLLALRKGNL | Function: A core subunit of photosystem II (PSII).
Subcellular Location: Membrane
Sequence Length: 33
Sequence Mass (Da): 3440
Location Topology: Single-pass membrane protein
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K3Y980 | MSLWRAAASRLLLRRSPPLSPSTAASSYALLLHARPFSPPPPPPPPPPRPAPAEAEVTPAEARRLVRLVGVEALKHRLRDGRDEVVGYSELLDACVEAGAARTHAEAEELARAMDDAGVVLLFRDKAYLHPEKVVDLVKRAVPLALGPENDPRKEEFKQLQEKKEEIDKLAHKQVRCILWSGLGFFMCQVGLFFRLTFWEFSWDVMEPIAFFTTASGLLVGYAYFLITSRDPTYQDFMERLFLSRQRKLCAAQKFDMERYMELQKHCRCPLEGHHPHGPKLHGL | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
K3ZJ60 | MHAAAAAEEERAAELAGPLRDILPPVDFCCAYGSTLLHARPDGTSMVDYILGVADPLHWHSENLKRNPAHYSRWMGCLGASAITGLADRIGVGVYFNPFVEWRDKRIKYGVVRMKDLAMDVLTWDRFYLSGRLQKPVHVLVDNWDIRKVNTINLEMATSASLLLLPEEFNEYDLYAQICSLSYMGDLRMLFAEDKNKVKKIVEGSFQSFQTMYRPLLQEYIAEGLLKTSSHGQQKIFRQDCGPSTTNELFSVLPWTIQRQMQGRYGSHGKEMPTRMVVSSKEMAANCVRRALRRRVMVSSVRQAVSGLLASGGAVAAQYL... | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 333
Sequence Mass (Da): 37461
Location Topology: Peripheral membrane protein
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A0A5D2DRU7 | MSASMLLCKYEYDELALAEVIFVITSAVKDVCGKLPTERLFLGKYGRICLTLDEIIWKIFFSSELELMELLDGHCDILALIAYQFEDINVHYCYFHDLTNLRLYITQIIWYCVFPVTHMYITCYVVSTGIIGIMRPLHLHELLMKLYQLRF | Function: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 17764
Location Topology: Peripheral membran... |
U9UUL8 | MSQKNINKPPLSHSASWSAGVASSEHTSSSIYSEHKNISNASINSEKFINDDSYSNIHPYIGLRGKLSLAWITYPIISFIFVIGRLFIAMNSIDPIIEDIRQRVNKSCDALELATSSLISLPHFMAGPFNDSITDTINSTIRGFVRTLDLGIQALNGIIVFFINLYKSTFRCLLELAVRGSISAVSEAVIFLQGFSNNALAGIKTAIDNSIAGINSSLEGVRNALSNVGGLLNLPEIPTVSIPAAEDLNKVTFPTTGIVNGLDTLNASIPSMDEIENRLTNLISIPFNELRVIINNSMSDIKFNSSILPVPPMGNNIKFC... | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Subcellular Location: Cell membrane
Sequence Length: 665
Sequence Mass (Da): 74176
Location Topology: Multi-pass membrane protein
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A0A251TJP5 | MEVNNIMQFLEDRTILVTGGTGFLAKVMVEKILRVQPNVRKLYLLIRACDLEEAIKRFQMEVCLTLANVVFVRVSLLSTPIHAMLSNVLYMGLAKVQLAIHFNGHFF | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 107
Sequence Mass (Da): 12195
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A0A0K3CG06 | MTSVLSERQKDELHKSILDYLRTNGFTETLNAFKAEAKQEDFQPDGKAKWSGLLEKKWTSVIRLQKKIMDLETRNSQLQEELSTAPSKRPSASSPDWTPRTPARHSLSGHRSPVTRVTFHPLFSVVVSASEDSTLKVWDWETGDFERTVKGHTKAVQDVDFDSKGNLLVSCSSDLTIKLWDTNNDWKNIRTLHGHDHSISTARFLPNDDFIVSASRDRTIRIWEVASGFCTRTISGHNDWVRSVLPSSDGQQLISCSVDQTARIWDLGKGDTKAELRGHEHVIEAAVFAPVAAYPAIRELAGMTVPSGRSAEAKAVGLFA... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome ... |
A0A4Q9LMA0 | MGQAVFVMGPAGSGKTTFCKKLYEHGIAIHRSFHLINLDPAQIQENTVYSIDLRDFVTVEDIMENYDFGPNGGLIVALEELYDNIDELDLESLSSDFLIVDCPGQIELFTHSDTFKNIVEHFKKYFTCCIVYLIEAQFVSDPTKFISGCFVALLSMCRFSLPHLNIISKLDQLEISREILEEFCQLSESIKDHIQKKKGEYNQLCLKMYDFIVENNLVSFLELNYDDENTFDTILYSIDEAVQYFDDAEPKDHSYN | Function: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
EC: 3.6.5.-
Subcellular Location: Cytoplasm
Sequence Length: 256
Sequence Mass (Da): 29478
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A0A0R3SE48 | MTFRKIGVCPEIIELLHDKGILIPSEVQAACIPEILNGRDVVACAQTGSGKTAAFVIPILQALMSEPRPFYALIITPTRELAHQIGEQTAGLNLVQGSSICTVQVITGGRSIVKQGIDLALGPHVIVATPGRLADLLRTQKASAESDSTPEWSLSRLKVLVLDEADRLLEDNFGQDLTEIMSSLPRQRQTLLFSATFSDTVKRAMEAAKMSAVAENRKPPVMWQSKGITQSTEEKAAKSATVDTLSQYYLITKPELKDSFLVYIVDHFLTENPHSLIIVFSNKCKWCHLLGMIMQSVGIQSVVLHSSMSQNDRISSLNAF... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 439
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 48371
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A0A8S3C1Y3 | IKSLIKDIDQWNKIIEQLGTPPREFLCRLQPTVRNYVENRPKYAGYSLDRLFPDQLFPPDSEQSKLTGLSLCIYFVK | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.24
Subcellular Location: Cytoplasm
... |
A0A251VP85 | MASSILISFALLASTLFFMSGPSSAQLTPNFYSKSCPKVFDVVGSVVRAAVAKEKRMGASLLRLHFHDCFVNGCDGSILLDDTSSFTGEKTARPNVNSVRGFNVIDDVKKKVEGVCPGVVSCADILAISALESMLALGGPEWTVKLGRRDSKTASFSAANSGVIPPPTSTLSNLINRFQAVGLSTRDMVALSGAHTIGQARCTTFRARIYNDTNIDAAFARSRRSNCPRPSGSGDNNLAPLDVKTPNSFDNAYYGNLISQKGLLRSDQQLHNGGSTDSLVEQYNKNPRSFYADFAAAMVRMGDIRPLTGRNGEIRKNCRV... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A1C9P7I0 | TLYFIFGAWSGMVGTSLSILIRAELGXPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLTSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1W5LC88 | YQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQMNYSPSMIWALGFVFLFTIGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGLIQWYPLFTGLTLNNKFLKIQFLVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYSTWNIISSIGSLISLLAIIFFLFIIWESMISSRKSINAINMSTSIEWLQNMPPAEHSYSELPMLTNF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A2S1CR63 | TLYLLAGAWAGFIGTALSMIIRLELGSAGSLIGDDQIYNTIVTAHAFVMIFFMVMPILIGCFGNWLVPLMLGAPDMAFPRLNNMSFWFLLPALVLLLMSSMVESGAGTGWTVYPPLSGNLAHSGSSVDFAIFSLHLAGISSLLGAVNFISTLGNLRIFYMGLDNVPLFGWAVFITAVLLLLSLPVLAGAITMLLTDRNLNSSFYDVGGGGDPVLYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
K4A6T9 | MRRSPGPGAPCRRRAIQGFVALFLAYALVVLLLESPLVSTSLPGAAGASAAASRKLHLDGAWEGGRAAPARPSKHPHRETLSADGGRRRSGIVSGLELRHLNSTRSGSLRKVAAEAAELGARVFSDLQTLATTLPSLEDSSDEEEKSKCPHSIVLSGDEFRERGRAVELPCGLTLGSHITVAATPHEAHPERDPKITLLKDGEEPIMVSQFMMELQGLKTVDGEDPPRILHFNPRLRGDWSGKPVIEQNTCYRMQWGTPLRCEGWRSRADEETVDGLVKCEKWIRDDERRLEESKTSWWLNRLIGRTKTVSVDWPYPFVE... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 652
Sequence Mass (Da): 73320
Location Topology: Single-pass type II membrane protein
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A0A0K2TK56 | MTTRLLVCLTVLSTISGWRSKNINGEYWKSFDIFKTCKHGRKQSPVNIIKNDASIMQCAPMNFSYYDHPNDFDILNNGHTVILTLKNGTSRIPHITGEQLPKGVFRFSQLHFHWGKNNTIGSEHQINGCQYPLEGHFVHFNTNYGSTLDEALKVNGVKDNLFVIAVLFHLSSQKSNSGLQPIIKSLKSIKKCQRKSTISKLNLRKLLPRKLTEFYSYEGSLTIPPCQEIVLWTVFKKRCPVSAGQMRTFRKVFNDGDTHMNIFRLPQPLNGRTVLYNRS | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 279
Sequence Mass (Da): 31935
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A0A397ERE9 | MDGVTASKDDDDDTTNYVELKTFRMLNTSKDRFTFERYKLLAFWIQSYLVGVPTIRVGFRNESFILTKEQAFETDHLPRYGDKHWCMTMSLSSTTPPFVKTPLSNY | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 106
Sequence Mass (Da): 12405
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Q6GN39 | MARFRPINVTVAGFFLLQTIFLILIYSRHTVLPDTETKTEKVHLLILSSWRSGSSFIGQIFSQHPDVFYLMEPAWHVWMSMFQNNAKVLHMAVRDLIRSVFLCDMSVFDAYIPNKKNVSELFQWAVSRALCSYPACSHFDREAITNETVCKIICKHNPFSKIEESCNTYSHIVLKEVRFFDLKVLYPLLTDPSLNLKIIHLVRDPRAVAKSREQAMKYLTRDNGIVLNTNGTKIDDIRYDVMREICQSHAQMYETAMDKAPSFLKGRYMLVRYEDVVRDPLREINQMYEFANLKLTAKLKNWFYNITHGVGPGTKKEEFQ... | EC: 2.8.2.-
Subcellular Location: Membrane
Sequence Length: 392
Sequence Mass (Da): 45969
Location Topology: Single-pass type II membrane protein
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A0A1T0A052 | MNKPVINVCDEFDGREQVRTLVLALGSNHHHERSFELALAKLGELGELDCSDVAASKDFTGKTERVYHNACVLLDAAAPNTVRAWIAATKEIERQCGRGDGQDVAMDIDVLAVQGSDGAWCVHQKRLPFKAHERTGLMQVAAWLI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A0K3CHL3 | MSDDWSASAVQALQIRFARSKAQAADLSEDERSLVDPFSPIFVYPIYGEEETIFGYKGLTIDYRFASGSLNQYLNVSWEDKFPETTTVKADDPEKTLYEFIPPSYTKSLERFQETVEKDALEFKPLGKRVGAYRMKGEDELTGGGKGKGKAKSQGGPILPERSWEAIDDFENDGEDGVRYEAYWTNWDTPGFKEYHRKMQIFVLLFIEGASYIDEEDGRWEFVTLFERRKKGDSTSYHFVGFVSFYSFFCWPDTKRLRLAQFVLLPPWQGQGHGSALYSLCYRNILSRDEISELTVEDPSEAFEDMRDKCDLYTLISTNA... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subc... |
A0A1I8GHC0 | MQRKRKLWEINMSSRRQVHFLDAKENGCTNNAQQKQQSLQQRKEKQSPSKASWDQLEILGGVKIFPQGLCSMSFLRYLYMSHNRISVIPPEIAQLKNLVHLDLSYNMVKILPPEIGEITELKELHLQCNQIRCLPMQLGRLFQLTVLNLNHNPLNPDMLQLYNSETTQSMLSWLLDSEGFAMTPPPSRKWCYLGGRSNTDSISRNGHASAPNNSQSTTSGSNGTTSGANGSSIHGTAFTVMCYNVLCEAYATKKQYPYCPSWALQWEYRRRGIMDELRAYQADILCLQEVETEQFGVFFRPELAKAGYEGIFSPKSRART... | Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Cytoplasm
Sequence Length: 603
Sequence Mass (Da): 68804
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A0A819Q138 | MDNITLQKQVENLRQQLKVDRAPLSRTLMERIIPNACLVEKQARILSLKIQPLSDSCRPRSKTQADIMDKSSLQKQIDSLRYQLRVEKVPLSKTLQELKRYIQENEQADPLIHPPDKKSNPWAEKGKCTVI | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
A0A2E4X165 | MRVRLFCKKSSAQAEALAQDLIDHRSEDLDIARLQDDEILQKDDLALVLGGDGTLIQWARRWGSSGASVLGVNLGRLGYLTPFAPGTAKAALDAALAGELERESRMRLRVVSDSLPDLGPALNEVVISGKDAGRIGEFSLRREGKALARLRGDALLVATPTGSTAYALSAGGPVLAPDLEAMVVVPVAPHSFSFRPLVLRPDERIEVEIHGEGWVSVDGQARFALEHGQIVEMTRAPSPITLLRQRTDDPLDHLRKKLGWGLSPQT | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A109L1B7 | MDVLNSISLERLESTQADYEISRLRECCVNDGFFYLADHGIRPSLIADALETARQFFALPLSTKNQFCQDRQVVIPKTCRGYVDTFGETLHPPTGPDRKQHFDMGREAPACDLPFTGPNLLPSEGQAPGFAKSMLALQQEVLDRVVPALLRGLALSLGLDRDFFQAFFSNPVLIQRALYYPPSGSGAGKHTDNGMFTLLFQDPRDACALSAFSQGRWIDVPCRANEVVVNLGDMLMKWSNGLFTSTPHQVIHRASSARVSLPFFVYPDIAAVFTPLGSDQTVACRQVMLDNFNSIWVSGQGAGRAREFA | Pathway: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate.
EC: 1.13.12.19
Catalytic Activity: 2-oxoglutarate + 2 H(+) + O2 = 3 CO2 + ethene + H2O
Sequence Length: 309
Sequence Mass (Da): 34144
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A0A251SR57 | MAMTNTKAAALAVGFIFLNLTCVLGGLQYGFYDGKCETSDVEAIVRNTVFSEFLVDQTIAPALIRMHFHDCFVNGCDASILLDGHNAEKTAPPNLSVRGFDVIDAAKAAVEGVCPGVVSCADIIAIATRDVVALSGGGRYTVQTGRRDGLVSLAENTIVLPAPNASVSSAIHTFASKGLTATDMVYLSGNCFTEFLSHVL | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 200
Sequence Mass (Da): 20994
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G9D7H7 | MNNLSFWLLPPSLFFLLMSSMSDTGVGSGWTIYPPLSSISGHGGVCMDFAIFSLHLAGASSIMGAINFISTIINMRLGAMKMDKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGFGMVSHIVSSSVGKREPFGALGMIYAMAGIGLMGFLVWAHHMFSVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLFGSYFKFDAPLMWSMGFIFLFTIGGITGVILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMSGITYWFPLFFGMMMNPNRLILQFLV... | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A146PQQ5 | MPQVDKTAKRLWARHSSETIFSPIWEQPFNIEPFAFEGKRIPFKMTDVDRARRKRWLKELRLNPDDVKNVPELKKLLYNPIRRFIRAPLDWVFTKYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGLGIFGPYNGVARKLVPKLGYIYLTFLSLTYAMIYHSNDWEMRHTNQIRMKHLRVSDDPEYQKERKPQDFSDRKFQKRKVFTGPQFAY | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
F3L1P2 | MKKAPLVMMMAGGTGGHIFPALAVAKALEVKGYRVSWLGTQAGLEARIVPAAGIPLHNLSVRGLRGKSLTRIVSGVARLIWSIEQATFLMLRHRPSLVIGMGGYVAAPGGVAAMLMGRPLFIHEQNAVAGSTNRWLRRIASRIFAAFDGAFNASVNAEVVGNPVRAEIVAVGEQRQAFDGQRDLRVLVLGGSQGALAINRVIPDAVAQFETNEASDGLSVWHQVGQAHMADVGAMYAARGITHVRISPFIDDMAAAFAWADVVVARAGALTCSELLAAACPAALIPLPIAIDDHQRKNAQHLVNAGAAIVIEQDTLNAAD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A126G1W9 | ALSLLIRAELGQPGALLGDDQVYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLLWFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1F2PLG6 | MIKTENLTYQYPDGTTALKGVSIDGSRGNCIALIGENGAGKSTLMSALIGLLKPTGGTVFFKDQPLSYQKKKLYEFRKSIGLVIQESDKQVFYSGIYDDVAFALRNMGMAAEQIDQRVQAAMEATGITQLADRPVHYLSYGQKKRVAMAGVLAVEPEIILMDEPTLGLDPKSKAGVKAIIEGALAKGIKIILSSHDMDFIYEFCDYTYVLHHGGVLVEGETTDVFKNTEALETASLEQATMTRLEQCLGIKGFRSIAALEEAIRNQKKEVQTDETGSSGH | Function: Part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 280
Sequence Mass (Da): 30543
Location Topology: Peripheral membrane protein
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A0A1S3GVX4 | MLNYDYVWDMIFHPNGAIEVKVHTTGYISSVFLFGDALKYGNRVGEHTLGTVHTHSVHFKVDLDVAGLENWVWAEDMAFVPTAVPWNPEYQIQRLQVTRKLLETEEQAAFPMG | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 113
Sequence Mass (Da): 12938
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A0A3B6EDY5 | MEAKSSSIKKETEAMEEAERVVKKQNVTMAMEVFDCPVCSTPLRPPVFQCALGHFVCSPCRDKLPDSKCQACSGVVLKSSCYGIERIVESILVPCPYAEHGCTDMITYYLKGEHKQACPHEPCYCPEPGCGFAGTTAALLDHFTSQHKWPTTVFKYYVPFDLIAKPGMHVLRAQDGNLFLLNVSSPESVLHGISLVRIQPKVSELSRFGCSVGFSCWKGHYQLSSLDAITSTSLSDGLPKSSFFSFVPKSSAVLTVTIDMELMCDINDDELEEETSDDDDSYGEEDGGEE | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 290
Sequence Mass (Da): 31916
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A0A7M7R8B7 | MSTQFPHYIAVIVLLLLKSIMDSDGKELISVIQWGCIGNQSIEKYTLKNKVGQEVDIITYGATITSIRIPDKYGNIADIVLGFDSIEEYMMPYNPYFGATIGRVANRIKKGEFTLKGKKYHLTKNEGQNHLHGGTKGWNSKIWHADVQYNQLVLSLLSEDGDEGYPGDTIASVIFQLTKDGELCIEMKVFVTKATPINLTNHSYFNLAGHTGNASELYKHQFTINADHWTVTDAESIPTGEIRSVDNSVMDLRNSTILGDVIDKVPGGGYDYNFCLTMNDTENEKNLVATVLHPTSGRYLKVFSNQPGIQFYTANFLPES... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 378
Sequence Mass (Da): 42255
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A0A3B6JBS9 | MSAAQIRAEINGLIASKFAEGTVDQYFLQLYVMRRYKKIRKGMVVEVMERFLQDADKILTEIAVLLNEPQLDYDKVEGIADQLEGCSSSSVGAKRVNLSCVEYFHPEAKTEEGNQPVVDFDKVDALVQQLKGCSSSVGANKLSVSCMHFRRFNHSKSKEGYLIALAPIMNEFCDVRNMFLTILQMEEQVDALGPKY | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 196
Domain: Histidine-containing phosphotransfer domain (HP... |
A0A662IWY4 | MVSELLKDVPGERLFLLGNEAIARGALEGGVQVAAAYPGTPSSEILMTLASIAKDAGIYVEWSTNEKVALEVALAASICGLRAMCSMKHVGLNVAHDPFVTAGYIGAKGGFVVVSADDPWAWSSQNEQDNRWVAKQAYIPVLEPSDVQEAKDMMAAAFNLSEQFNHVFMLRSVTRIGHARGDVTLGPLFKEKRKGVFKKDPSWLTYVPATARKNRPLMIQRLEKIKKAVNGWPFNKLDLVDGAKLGIIASGLSYAYAIEAVKWLGLEGKVSMLKIGTTHPIPEELTKKLLSSVEEVLVIEELEPFVELHVKALACEEDIK... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.8
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredo... |
A0A657APS2 | MPKVFLNLGSNVERDQNFRSGLSSLKRTFGDLSLSSIYESEPVGFDGACFYNMAVSIETELSLPKVIKALKTIEDSHGRLRGDKHFAPRTLDIDVVSYGQLTGFHDGVELPRPELYYNGFVLWPMAELAPDDIDSKTGLSYQVLWQLKQVEIEAKQKVWRIDPSSVAAILKP | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A536YAH7 | MPDLTAKKKRPLWYNLSPLNLPVPGLVSIFHRISGVLLFLGLVAFLYLLDLSLASESGYAQAGEYLRTPIAKLLVIASIWALLHHMCAGIRHLFLDIDVGTSLHAARRSALAVFIVSLALTASIAVRMW | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 129
Sequence Mass (Da): 14163
Location Topology: Multi-pass membrane protein
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A0A158PJK0 | MNVSSKAVVGPGSCGAVKSKALPPRFQTQNDLDFLKSEVAKNVLSSSEHSISRLRRIQKYMIPLVLNEISFLAIGPSGSGKTCGYLLPLINKLIELKEMVVSLEFVRFFVIEDFERCVEKSFYKEDLTILKKHLSESEAIPVCIFLSNAVHEKGIFDINFMKELAKTKLTKLMVSSLSDNESISCILFELPVDSSSNFKRRLLDLSAKLNYSGRIHIMVDVDLDREKAKTILTANSSFNEESHLRNEALQFLEELDQRVPEFLVDMLSCVGEPSTEVELPHSSDVSNGQQVGAKPSVEFGERHFIGRTNTPLVLILGNTQ... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 743
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 83870
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A0A497GJG0 | MRGEPLTSEDVRRLDENAQLLGLTALQLMENAGRSVADIISSHINIKGKNVVVICGLGNNGGDGFVVARHLANKGAHVDVILVGSAEMIRTDEARHNWAILEGMELSIRLHEARSTDEVKEYKDKIMNADVVVDAIFGIGFKGTVREPYRTAIELMNKSKGFKVAVDIPSGIDADTGEIGGIAFKADLTVTFHAPKVGLDKAKEYVGKVVVADIGIPKEAEYIVGLYDVRKCFKTRDPLSKKGDNGRVLIIGGSRLYSGAPALSGMAALRAGIDIAVITTPKSAAWIIKTFSPALIVWPLKSDEYLGLDDIEYIMSVKER... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
I1H7Q3 | MQAIRAVLLGIAVVLGLGGVPGGEAQLDEKFYDGSCPGVHRIVRRVLKEAHQADVRIYASLTRLHFHDCFVQGCDGSILLDNSTSIVSEKFAKPNNNSVRGYTVVDAVKAALEEACPGVVSCADILAVAAKISVELSGGPRWRVPLGRRDGTTANLTAANHVLPSPRDNITMLQRKFRAVGLDDTDLVALSGAHTFGRAQCQFVTDRLYNFSKTGKPDPTMDAGYRVQLARSCPRRHGNRTALRDLDPATPDAFDKSYFTNLQASRGFLQSDQELLLAPGAPTAAIVARFAGSEKAFFRSFASSMVNMGNIRPLTGGQGE... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A074ZZ64 | MSWNNIPADPKQPLLFPDVDYPRQPNFIEKDVNPSVRVKLDAESTTPYRRTRDVDLTDWDDDAAAHLRSTADTPGDLIDCLSPCRGILGLRKPSKRKFLSLRQLSRFRRPFGVIWLVRDVCGIVCLVFTWVLILYAEFVISSVILMRAPSSSFCWITGSMYHLFVSLACISHIFAFSTDPGTVPIGNATREAGIFLCEVYGDPRPPIIRCPKCLCIKPPRAHHCRICFRCVRKMDHHCPWINNCVGEANQKYFVLFTLYICLQSTMAIYMCVHFVVQCIESDWEACQLNTSHHGWSHLLAFEFSPFVTCVFILGLIVEAF... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 447
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 50432
Location Topology: Multi-pass membrane protein
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A0A3B6FJR6 | MAEVVQVHKDWVGSFPSGKKITVVFVIGGPGSGKGTQCAKIVSQFGFTHLSAGDLLREEVKSDTEQGATIKNLMHEGKLVPSEIIVRLLLKAMLASGNDKFLIDGFPRNEENREAYEKIIKIEPEFALLIDCSREEMERRILHRNQGRDDDNMETIRRRFEVFQQSTLPVIQHYEKMGKLRRVDGDRQPDMVFEDVKAIFAQLNTQANQGSNVSRAQTNPFKSWFLDIFCSCFDVADRRN | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
EC: 2.7.4.14
Catalytic Activity: AMP + ATP = 2 AD... |
A0A2U3PYW3 | MRIDVSLLPALAASFMLAFARVGAMVMLLPGLGETNIPTRIKLSIALLLTLIILPLHRNAYHVDMGSLAPLLVLMLHEIAIGIVLGATARVTLSALQVAGSVIAQQMGLGFVTSVDPTQGQQGVLVGNFLTMLGVTLLFATDSHHLVIAALNDSYTIFSPGETVSSGDVASLATRAFAAAFRLGLQLSGPFLVFGLVFNIGLGVLARLMPQMQVYFVGVPLSIFAGFLVLAVVLTAMMGTFLDYFIGVMHQMMPLK | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 256
Sequence Mass (Da): 27084
Location Topology: Multi-pass membrane protein
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A0A3B6PQR9 | MANTGLSRRNSCPKVHSALCSELTMMLDKISSILPSIEAARPGCRAGIQELCNLYHIVEKGRLITQHCIECSKLYLAITGEAILSRCERVRDSLKRSLFLIQNMVPTVLANQIADVHNDLRDVKFSVDPLEQEAGKSILEMLRQSDATEELLLQTFMQAASKLNLTSPKAILIERRAIKKLLDKITGTDQKKEQVLKFLLHLVTKYGKNVKPDTGERNENLQSESKSLSPSLSLASDASTPEKCDKPTYFQGYEYQSSMSGETTPPTEFCCPISTKLMHDPVIITSGQTYEREYIEKWFSEGYNTCPKTQKKLENFAMIP... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 769
Sequence Mass (Da): 86157
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A0A3B6LPX2 | MIRWGDVYKVVAAMAPIYFALGLGYGSVRWWKLFTPDQCDAVNRLVAYFAVPFFALDFAARMDPYALNYRVLAADALSKLAVALALAAWAAASTHCCRGGGKRGGELASSWCITGFSLATLTNTLVVGVPLLDAMYGGWARDLVVQISVVQIIVYFPLLLLAFEARRAWGGGPGKPGAEAALASDGDVEDGGAEDSRQRQPVWPLVRAVWLKVARNPNVYAGMLGVAWSCITNRWHIETPSIIEGSVLIMSRTGLGLCMFSMGQFMALQERVVACGAQLTAVGMALRFLVGPAATAAGAVALGLHGDVLRVTIIQAALPQ... | Function: May act as a component of the auxin efflux carrier.
Subcellular Location: Membrane
Sequence Length: 364
Sequence Mass (Da): 38967
Location Topology: Multi-pass membrane protein
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A0A139JR63 | MFYNNLLKESFFLSNFQLKQLEKYYFFLKSYSNKINLTSLLSEKEVYLKHFYDSFLVSKIINLIKFEHLCDLGTGAGFPGIPLKILYPHLKVFLLESISKKIIFLKKLVSILNLSNIFIFHHRIEEHKNKYNFIITRSLGKMDVIFKLSSLVIKKKGYLIAMKGPNYIEELKNIKKKFSFHLKKKKKSELPFNLGKRVNLLFQKK | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 24311
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W8C3N7 | MREVVRLGFDLNGAWRISKANEEFKLCPTYPKKILVPGCITDDTLQIVANYRASRRLPSVVWRHKRNGAIIARCSQPEVGWLGWRSESDEQFLKALADACAFDRGEQMRRLMQTARSAVPAMFLPPDTQPTNADVESHEEVSLDEVRKVLIVDARSYTSAIGNRARGGGCECIEYYPFAEIQFMCLGNIHVIRKSFHALRTLCAAPPTDANWLGLLEKTNWLQHLSGLFAATTTVLQAIEKKGCPVVVHCSDGWDRTPQIVATAQLCLDPYYRTVEGFRILVEREWLSFGHKFAKRCGHGPESDDLNERSPIFIQWLDLV... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
EC: 3.1.3.64
Subcellular Location: Cytoplasm
Sequence Length: 810
Sequence Mass (Da): 89757
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A0A147E9G4 | MGFSRGVRMGVDVGNARVGLALSDPDGILATPLKTLKRNLNTDSDRRVLRRLLEIHEVAEVYVGLPRTLSGGSSASTQMAEDYASGLVAELAAEGREIPVWLVDERLSTVSAQRSLHEAGVSSRRFKTMVDQVAAVAILQQSLDALKADRAVAGYRVEAPTVPREDARSQHLDPTSEPRPEQNGDPA | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 20169
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A0A7S3N2X0 | MTRDDLKKWSHRLHMNQPPNLFGKDKVPYRTIGYSFFLFLVGTIFLCLGFMDYVETGSMTTATSEESGRPYEKLLLGALMFIPGSYHVFVGLLAYLKVDGFKYKDVASFESDQWWNDHCD | Function: Involved in trafficking and recycling of synaptic vesicles.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 120
Sequence Mass (Da): 13894
Location Topology: Multi-pass membrane protein
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A0A183LVI7 | MVFRLDPCEQLLNPLFYHLPFLYSFWAILNTICFNIVASLLLFSHICAAVTDPGLIPLHRYTVSQLASVQKPDGWTTCNKCGIHRPPRAHHCRICRRCVRRMDHHCPWLVIYVCI | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 115
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 13404
Location Topology: Multi-pass membrane protein
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A0A672FDE9 | MSQPAEAGCCPDGYRALSTAELRELLRDDGKMERIIRLDEKFQELQLDRESLLTSNRSLAEESLARKPRLRTGTLQLAHSYRELARLAAACGDKQSRLEGGVQRRGLQTAQNLLQEEVTRAEEQSEELLERFMEGTVDLDRFLDSFQSSRKTYHVRRAQAEKLQEFIQSRRQGGGGGRPGPPQGQRAAAGPPQAQRLHGTGPAPGLPGPLRPDARHPAAPLPRRPPGPRPRPRPGPPAGTCPAAAARPARRPAGHRTAVGRLAGRRAAGSSPAAVQAPAARAPLPIDHRGGGGAQAPGPDPGPDPGPDPGPDPHQTHAGR... | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Subcellular Location: Endosome membrane
Sequence Length: 331
Sequence Mass (Da): 35421
Loca... |
A0A0Q3PR06 | MANASRRPATATMALLLLLVLLELAAMTGLSQGQLQVGFYSESCPDAEDIVSSAVQDAAASDPTLLPALVRLQFHDCFVRGCDGSVLIAGAEVKNSKHQGLRGLDVVDAAKALLEEQCPGVVSCADVLALAARDAIGMTNGPSFDVPTGRRDGLASNVRDADVLPDASDNIQTLRSKFATAGLDDRDLVLLTAAHTIGTTACFFVKDRLYGASGSDPGIPAGYLAELKARCAPGDFNTRVPLDRGSEARFDGSILRNIQAGLVPIASDAALVADNATAALVGAYIGSPRFRRDFVGAMVKMGTIGVITGGNGEIRDVCSA... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A7C7HEX0 | MINKKLDYRANSSVIRKLVLRCLVQLERRNSQIAPVIDMVIRQNQLNNVDRGLLTEIVYGAIRWRGHLDWIIRQFVKPDFQLDLQMRNILRIGVYQLLYLDKIPAHAAINETVKLANQKGQKSKNFVNAILRSIQRSTNSLTPPRFKLDPISHISTKLSYPGWLVKKWIRQSNPEWTLKFCHASNQVAPVSIRTNTLRTDRKKLAKSLQEDGNQVVESQISPDGLLLTKTNPIRSLSDFQAGLFQIQDEAAQLVSHLLDPQEKSQIVDLCASPGGKTTHLAQLVGNVTNIVAIDLSTKKIKRIQENCKRLGITNVRTQVA... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 457
Sequence Mass (Da): 51468... |
B2C5W3 | MAYSSINNLGWTIMIMALSPNLAVMNISIYIIMTTPIFLMMTSTSTKTLQNLATTWTTSTATTLSIALLMLSTSGLPPFTGFMPKMLALNELITQKLTALATLTIMTSLISLLFYLRIAYLTMMLTPPMTTPSSTKWRTQNQKSQLMTMMTPTALFITHLIPAIPF | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
V4L1I2 | MSFVDRTHIHVTAGDGGNGCVSFRREKYVARGGPDGGDGGRGGDVILRASAGVRTLAEYGRKHHFKAAPGGHGSGADKHGKSGADCILEVPVGTTVYAKNDEARVLADLVSDGQYYVAAKGGRGGSGNRQYAGGARRAPKFAGKGKAGEQRWLTIELKLIADIGLIGMPNGGKSSLLAALTAATPKVADYSFTTLAPQLGVLQHGFMEPLILADIPGLIKGAHAGKGLGHHFLRHVERTSILVHVVDCALGDFERNYHAINEELSIYDRSLIGRVKIVVLNKIDLLDDRQRAEVYEKAGHFAAGVVGVSARTGEGIDTLR... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A7M7IK12 | MIQFKVSAPGKVILFGEHAVVYGKTAVAASIDLRTVLNFTELPEAEQVVKICFSKVNLFITIPLQQIQNFFFINKNVEFIENYEIFYNKIKEFVCIVSYANFQQKLSLEAFFYTLIYIAQKEEMEIKPFQIQLNTELAINSGLGSSASFAVCLAACFVHWSHLQKNIYKVFDFSTLDVISKYALNCERIMHGNPSGIDNCICTYGSIIEFKKGNYIQPINTNNIQAMKILLVDTRVNRSTKALLEKVLELKHTYPVIIDLIMDSIDNISKEAVKIIQKLKTFSNTNEFFLEGYKQLMILINMNQGLLATCQISHPSLDRI... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
EC: 2.7.1.36
Subcellular Location: Cytoplasm
Sequence Length: 382
Sequence Mass (Da): 4282... |
A0A5Y4YMA5 | MKILGVIPARYASTRFPGKPLADILGKPIIWWVYQQAKKSEKLTDLVVATDDERISKACDKFDIPNITTKIHESGISRIHEVSQKIAADLYVQINGDEPLIEPKIIDRIVPKTINKDFVANLICKIKSPNELLDPSNIKIIFDSNKKAIYMSRTPIPTPYKSLNFDYYKHIGVLAYAKSMLDFFVLSKPSKYEKIEGLETLRFIEYGKNFYCIEVENIKSLSVDTPKDLEEVESILKLRTKN | Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activi... |
I1HWH6 | MSAPDGSGPEPVVMLHGDLDLTIHEARGLPNMDVLSTLLRRLCLFRPPRRSSRPLPPRSVSASDEEDNPSTSSSHHHRHHHLHRRRPRRPKQPHGPRHLLPTSDPYAVLLIPPATVLARTHVVRNADRPVWSARIRVPLAHAASRIVFNVRDADPFGSDLIAAASLPASDLLSGTPIVSRWLDLLRPDGRGGKPKPDSAIRISASFTPAYSSLSRGGGIIPAYFPERRGCEVKLYQDAHGGAAKGGCWEDVCMAVLGAQSLVYVAGWAVGARVRLARKGEMSPEMEEKAAEVMALSSAAGGGGGDEAASPELGEMTLGDL... | Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond.
EC: 3.1.4.4
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Sequence Length: 931
Sequence Mass (Da): 101541
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A0A9J7LL07 | MELMGEFDYEILSLPDDQATDCLYMNGTILHCTKEEFPDSYKVFETVTDYHRVAVSNRELRKVGGALSRLALLIPLTKTK | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 8... |
A0A7M7FYE4 | MAMQVPTNVDPEQIKSVRDFVASYNKLIETCFLDCINEFTTRDVKAKEETCALNCMEKYLKMNQRISQRFEEFQMLANENILAAQKKLDSKES | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A199P8N7 | MQHGQYLLLLGACLLLTLPLEFVFRARVYRRPLLTLRVIGVVLVLFGAWDVIAYHRGHWTYDAQYFLGISIPGGLPLEEILFFVAIPLCALLTYGAVGTCLGWLRRLRRGTGALARGPRDPRAPGAGEGPHA | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 132
Sequence Mass (Da): 14566
Location Topology: Multi-pass membrane protein
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A0A2A6CX70 | MPETATDGAPSVGGGGSSSRGGKGGGRSRGGGGNRGGGRTGNADSNGGNSRRGEGRGGGGGAGENNGRRSPQQHNHQQGGRNEQRKTKVGDHKVDMRKYERMITATQSNFSDIKATDPITEDCLICCKPNDIFGVGACRHPLCIECAIRIRVIANSEGCPVCRQPMEKMAFVFASANPTTASLSMPHIHPDEKRYKVCFQNKEASARYEQYLSHVCKLCVVDGERKEFASFVSLRQHMAATHQLSFCHHCVANLQLFSRERTTYSRAQLQEHIRGGDRDDRSQKGHPKCLFCEDRFFDEDDRYRHLRREHFFCQLCETTG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 956
Sequence Mass (Da): 102622
|
A0A2C9L2D7 | MTLTNRSRQDSTKLGVHVLVVLLGITSWSIMNGLWVELPILVVHLPEGWTLPSYLTIICQFGNIGPIVFSLLVYLTPRKKIETPTSFVIVVALTLCAALYGFLWKKTSPIGSNEHSVALMSLTLCQSIFAATTSTAYLAFMSHLKAQYIGSIFIGMSLSGLIPALAAVVQIPGEVECLRGAINSTNESVAYQLKNFTQSNLFDLNAFEPVIEAASNQTIHMTRLLQNSSDFENTLQLYKEEPSFSVKYFFLMLASLGGLSFLSLVLLIYHPYCKTEHADIKKEDNCRLVPIKRSNSSANDSNNSQGVNLEPTEQAQLDNK... | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membran... |
A0A8E0WQ72 | MTESVKPPFGLSLSKPSAERSEAPSTSSGEPFDKLRANGGVKVRSDFPGLLNGEGGDWHYLDSAATAQKPNAVIDAIARAYGPDYATVHRGVYERSANMTLAYEAARRKVAQFIGAASDSEIVYVRGATEGINLVAQCWAGTQLKTGDRILLSMLEHHSNIVPWQIAAEKVGAAIDVVPLTPDGRIDLDAMQAMITPAHRMVALAHVSNVLGSVLDVRRAADIAHSVGAKILIDGCQAVPRLAVDVQALDCDFYVFSAHKLYGPTGIGALWGRKELLDAMPPYQGGGSMIDKVTFEKTTYAPPPTRFEAGTPHITGVVGL... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 439
Sequence Mass (Da): 46601
|
A0A7M7LK33 | MSIRKAFSLVFIRKSTEILLGLKKRGFGKDKWNGFGGKIEPGESILHGAMRELKEECGLSAQELRKIGILEFEFEENEVLLEVHVFETYKYYGEIIESEEMRPKWYNLKDIPFKEMWPDDEYWFPYMLRGQFFKGYFLYRGQDLILKYNIETMEELPSLDHIS | Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)
EC: 3.6.1.56
Subcellular Location: Nucleus
Sequence Length: 163
Sequence Mass (Da): 19471
|
A0A2A6BVP6 | MDYITLNPQESGDHIMKTAKHVKVDLEKCKEAALLVMDAVVEGKIGEIDYSANPLHPSGLSDEEKMLWVFLLDVLNFSFWPDEGEEYNVTFEGQTYTGYLAMCAAFRKAHKELNAPIATVQWMLTVDVGVLDFILKDDKGFSIPMITQRKQAVKEAGEWLFWSHDASFLNVVRKSNCNAQVFLRYILACESFRDYGFYNNRKVSFFKRAQILINDTVGALIGSEENKHLVDFKDLDTLSMFADYRVPQALNYLECLEYSPELLDELQSNKLLTYGAEKEVEIRGASIYAVQQMYKEIQRVRAAGPYSECDVDTVSGEYRL... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-pho... |
A0A536XYD5 | MSEFFAMGGYGFYVWGAYGVSFALLALEVFLLMKRKREAKA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 41
Sequence Mass (Da): 4657
Location Topology: Single-pass membrane protein
|
A0A0W0TSZ4 | MKPMRVFFALAMPKSTQRLLAEILASAQRYIPAAEAHWVPKENLHITLQFIPEVHINDLPQLIENVRSSLTNLSSFYLELKGMEFFPTPTHPRIISLAVGPSDCLTQLSAAIGQGIKASNYPVETRAFRGHLTLGRLRRVHQSFSLEQIKIPLIPRIWIDVIHLFESRSGKEHSNYIPLAHLELNKN | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 187
Sequence Mass (Da): 21264
|
A0A3B6KCR3 | MPAHFRCPISLELMKDPVKAPTGINNGRERWLVRGRDTCPITGGPVWLADLVPNNATRHMIQDWCVANRAEQVPVAEADAAEVLAAFVRGNAAACGQGAARAIGKESDRNRRCLVAAGAARQLASAFRSLTGEPVESTSAAALSALGTILAALTMFFPLDDEARRCIASQASHKSQDPCLGALAQPPRPRSSRPTTPSPAATACFADVVVELVVDTDKGTSEKALAVLDGVLCADTGLRSACAYALVMPVLVKKMFRVSNMAKEFARLRALAPLLCRGHRRWRALLRGTACGLLPEAAPSVLRRHDRGSGQRAAQAAQWF... | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
S... |
A0A7S3MX72 | MCVERYDHHCPWINNCVGVNNHQYFIIFLSSLWVSNVLVFISSIVGLFYLYELPKLKKNELFYDFLPEAFALEKWVYEMASLFVIVLTGFFILPIGFLFYIQVRNFITNKTTNERFSRKKPARRHREPNELRMDSTGSSLVSTTSSMIVEDIINDVGDPEDYYAGGCVGCHNCTKMFCSKPFPSQLEMYNKFISQREALHKQ | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 202
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23590
Location Topology: Multi-pass membrane protein
|
A0A183LSJ3 | MKSQRDLVDFGTAAAEEKARRHDVMAHVYTFALACPKAAPIIHLGKSTCATSCFVGDNADLIMLKDGLNILLPKIARCIDRLAKKAMLHKSLICLARTHLQPAQPTTMGRRICMWIQDLLLDLENLERLKNHTIRFRGAKGAVGTQASFMDLFQGDHQKVIKLDEILTKKSGFQRSWCVTGQTYPRKVDSEVSNVLSNIGATVHKICTDIRLLSSFHEVEEPFETKQIGSSAMPYKRNPIRSERACSLARYLMHISTSMVSTASVQWLERSLDDSAIRRIVLPEAFLAADACLILLQNIAEGLIVYPMVMEANLNSELPF... | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Function: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxami... |
A0A1W4WHG4 | MAELRKRHETEDKRIESAESDHIDSEDDKHLDPKISTNLSDTIPSGTNKAPLILELLMKGLPDRWKNWFVRGIFTILMIFFFGIVIYGGPLALMITTLIVQVKCFAEIINIGHAVYRIHGLPWFRSLSWYFLVTSNYFFYGESLMDYFALAINRTDFLRFLTTYHRFISFSLYCGGFVWFVLSLVKKYYIKQFSLFAWTHVALLIVVLQSYLIIKNIFEGLIWFIVPVSMIICNDIMAYVFGFFFGKTPLIKLSPKKTWEGFIGGGVSTVVFGFLISHILCKYPYFVCPIQWSDNEGRMTMECTPGPLFTLTEYEVPTFL... | Pathway: Lipid metabolism.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 449
Sequence Mass (Da): 51871
Location Topology: Multi-pass membrane protein
|
W5JR37 | MSATSEYDVLVFGSCIVDFISYVPRLPKVGETLHGTRFATGNGGKGANQCVAAARLGSRTAIIGKLGDDAWGRAYRDALAAEGINVSEVAIMPGESTGIAQINVADGGDNQIVIVTGANKRLEPADAESRHALLQRARILICQLETPLEGTIAALRAFNGISILNAAPAEEHLPDPLLSLPTIFCVNETEAALLTAVPEIVDIPQAKTALLRLRELGCRTVIITLGEKGAVFAENGSTTVYHVQPTKVDKVVDTTGAGDAFIGALAHFMGQHPDAALGNCIAAANHVAALSVQKPGTQTSFPRARDLQLPLDDLKALQDR... | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A3B6QLH3 | MSRPLYRGFSGGGGGKDRCADEGRHYDPKEPSENGIGAGGCGTPARGRKRHLAAAAARIGVLVLAAAALVGSVAWAGSLYAGRGAAAAMAAASAHRGYRRLQEQLVTDLLDIGALAGGGLRSREAEACAAEYENHVPCYYNGSDAVDVSDLGGGVVISYERQCSREGRATCLVAPPRAYRTPVRWPSSKEFIWKDNVRISGHEFSSGSLFKRMMVEEDQISFPSDAHMSDGVEDYAHQIAEMIGLRNEFNFNEAGVRTVLDIECGFGTMGAHLFERDLLTMCIANYEASGSQVQITLERGIPALIGSFASKQLPYPYLSF... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 663
Sequence Mass (Da): 74131
Location Topology: Single-pass type II membrane protein
|
A0A2D4T5U4 | MNLENLNVVRWHQGQGFLVRAGHAPEPLASDEFSLPDNTCLALPSDVVRNMTVPVAPEEVKHLRRALPFMLEESLIEDVTELHFAFSPMRDDLQAVGVVKRSTIAQWMEELPDKVKELPWVTEVLCLPWRAGQCTLIFEDEWVLVRWGEAEGARVEMALLPALLDSLEAEQITLVAYGKDQQSAMVVIPERFHDELQWRQGGLSDALLLAEPLPAGPDLRQGDFAPRLPLMRWWGVWQRVAVALGVALILKTGLSIADYEMLKAEDLQLRQTIQESYRRINPRGAVVNVEKQLNRQLAELGAGARHRAFTPILVSLLSAA... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 385
Sequence Mass (Da): 43069
Location Topology: Single-pass membrane protei... |
W5JRH7 | MCILDTVEDKLSSLTTTTVMVVTPRDLEDVASYPRLFAELLGDGWTVDELEKLAGRNLLRVFEEVEKVRENQRLSGVRPYEDIPPALRPDEHHNCSTNS | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 99
Sequence Mass (Da): 11243
Location Topology: Lipid-anchor
|
A0A2A6BWE7 | MPLPFRRLILLIVALALFSLITDWLILRRIEGEEGNENGNNERKEKNEKRSLSSCELPDELAVSAMKRMKNEECKDRLREVACAIEEKRLHETFPHSTCPLYDSGRKDQYIGCYADSKGNRLLSNHSFTWKNDNSREKCGLMCSRAGYVYYGLEFGVECFCGNWIEGGRKIDEEKCRTHSCSSGMEKCGGFESIAVYATGMTKPLIWPQPKYIEVDHNKEYDIRILFVLQLNGRNVRQVRQMLRSVYSRKHHYYIHVDSRQKYMLNGINLVRLYLSPQMGLIILRLRERGDRKGRKFVSERAQKHIVSLLFFPIFELLPF... | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Golgi apparatus membrane
Sequence Length: 1004
Sequence Mass (Da): 115421
Location Topology: Single-pass type ... |
A0A3B6IYZ4 | MGLRGRGPPLLLLLLLGLVVATALAADSASASEGDADPLYRACFEECQRTGTLKEDSVKHCIVPTDDQPADKAWYAHEPLYLQWKEWNCNSECRYHCMMEREQEREELGLGPVKYHGKWPLKRASVFQEPLSAALSALTLLVQFNGWLSFFLLLSYKLPLRPETHATYYEYTGLWHINALLAMNSWFWCAIYHSCDTAWTEKLYLSSAAAFLGYSLILVILRTSNLRDEASRVMVAAPILAFVTTHILYLNFYELDKGLNMKVCTVISVAQLLLWTVWAAITRHPSRLKVVFVAIGGVLSIYLEAHDVPPRWGYVDGHAI... | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 352
Sequence Mass (Da): 39943
Location Topology: Multi-pass membrane protein
|
A0A536WTZ6 | MFDIGFSELLVIGIVALIVIGPQKLPGVARTVGHLLGRLQRYVADVKADINREIELEELRKMRDSMQKATSEMQSAVDAELTKTADELNKAAAGTPGTEPPQESAKAAEQKRA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A6I0EQD0 | MSLTLEDVRRVAHLARLNLAEDEAAAYVDQLASILDYFERLGAAPTADVPPTVHALALQDVLRDDVPAAGCGPDLALRNAPSADQGYFKVPKVLADGEA | Function: 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 ... |
A0A356SGH4 | MSEDEATAVPPELEDAPSGAAGDIDLDMLMDVPVTMTVEVGRKSLTIKELLSLTPGSVVSFDRSVTEPMDIMINGTLVARGEVVSADGKFGLRLVDVVSPKARLEQLS | Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
... |
A0A811LIM5 | MSRGGFRGARAPPRPGGAFNDDDSSPFGNQEEESRGSSRGPESNGYNDTRGGNNSYNDSRGGNNSYNDTRGGNNGYNDSRGGNQNFGRESRDSNRSGFGDNSDGNRDGFGPSKGNFGGRGAPNAGFGSGGSENFGGHGGFGGSRGGQENSFGNRGNQDNSFGNRGQGNGFPGPGQGFNFKDNSNKGFGNQEEDTRGGGRGPGSNNTFGASRNEGFGNNRGGFGRNESDSGFNRGRGGRGGFSSRGNFGGDSEGGRSGGFGGQSGFGRGGSDSEGFGSRGDGFGGGRGGFGGGSGSGFGGPSEGGFSGRGGGRGGFSGREG... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 931
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 98428
|
A0A3B6EJD2 | MDSVERSRRRAQRWSKRKAAVVHLAVCFVVGAFAPLVATRGPLIDGIRASFLPFGGVQRAPAAPDIGLLLIVTVTRPDDDVVSQEASLTRLGHTLRLVPPPLLWIVVGAENRSASTVQVLRGTGVMFRHLTYANNTTGNVNDEADLKKNVALSHIERHRLAGVVHFAAASAIYDLEFFEELRQTRGVAAWPTATVSSAEQRVTVQGPTCNSSQITGWYSKDSGTNETHRESVAAAQDTGAIHNISSSPPAIETSGLGFRSSILWESEWFVNSNSSQDFIQLVREMAVGDGDERKGIPSNCSESRIMLWHLDMPKHTPEVE... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
EC: 2.4.-.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 340
Sequence Mass (Da): 37355
Location Topology: Single-pass type II membrane protein
|
I1IGY4 | MLLSPRRLHLRIPHCCSPAPAPSALLGGSGVVRRLGSGARRRGAVAMATDGRVERIASTIRVIPDFPKPGILFQDITTLLLDPQAFHDTTDLFVERYKDKGITVVAGVEARGFIFGPPIALAIGAKFVPIRKPKKLPGEVISEEYSLEYGTDKIEMHVGAVLPSDRALIVDDLIATGGTLCAAAKLIERVGAEVVECACVIELPELKGRDKLGDRPVFVLVKAD | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24038
|
A0A6P5G2L0 | MTLVLTLLACVIHALNLANKSDASNKTCFGGIDGSIRFDIYQTTCPQAEDIIFAGVEEAVANDPRMAASLLRLHFHDCFVDGCDASVLLDDTPNFVGEKTAGPNLNSLRGFEVIDSIKAELELACPETVSCADVLAIVARDSVVLSGGPTWQVEVGRKDSRSANRQAANTNIPAPTSDVATLIGKFQNLGLSSKDMVALSGAHTIGKARCSSFSSRLNGLVGSSDASMGDRDFLQSLQQLCASSNNTLADLDLSTPATFDNQYYVNLISADGLLQSDQALTSAGSGDVAALVEAYAIDPELFFEDFKASMVRMGRLAMSG... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A7Y5VWC3 | MAKRHHEQLAIIHYPDPRLRRAADPVRHFDGELATVAERMLQLMRDAKGVGLAAPQVGLGLRLFVMNATGEPGGDEVFVNPEIVDPQGQREAEEGCLSIPDVHVQVRRAQRCRIVAHDLQGRRIEKSGADLVARIWQHETDHLNGVLIIDRMGPGDRIATRNTLRELEARFVRKSTGR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A811LQY2 | METEADLGDNELSASISCRRRSASVSDDYSVQKTNDDATESKFSAVKVGYWADSFIHHFIVNPEHIHRRAPEILRGYWARHAAFELSLKRISELAGENLQIISLGAGFDTLYFRLKERGVAFKKLVEVDFSSVTARKIRTISKNEHLAAMFDSTSTESQHSDLHSRDYDLLGADIRQPSEFWAKIETAGLDPSLPVVVIAECVLVYLDVKVTENLVRKFAEKFNELVFVSYEQVNMTDKFSDVMQANLQERGIHLAGLPSCNSLDSQKSRFLNNGYPVVNAWTMQDLYAQHFNKDEIARIEKLELLDERELLAQLLEHYC... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl es... |
A0A3B5ZYN2 | MDCVLLSSHLSSHATVNARLQQCSVSLNSIGFAVIRKGCLRLRCYAIGDAGRRNDPLDENKNGPISQELNGSSASFTTVGAEITQETGDFFSSDAEGDPDKPTEGFSSIEDAINSLREGKFVIAVDDEKGDNEGDLIMAADQASPESIAFMIRNGSGIISVGMKEEDLERLMLPMMSPVTEIGDISATASTVTVDARVGISTGVSAADRAKTILALASPDSKPSDLRRPGHIFPLKYRNGGVLKRAGHTEASVDLVALAGLRPVSVLSSIIDPKDGSMASTPALKQMALEHDIPIVSITDLIRLVCLKVQEEKGETGGTD... | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
E... |
I1HJ23 | MAQPQRVYEAWKGNNRFFLGGRFIFGPDAKSLLVSVALIVVPVFVFCVFVARYLLHRFSVYNAGYAIPAVAIAFMIYVLLLLLITSAQDPGIVPRASHPPEEEFSYGNPLAGETPGRLQFPRVKEVMVNGMPVKVKYCDTCMIYRPPRCSHCSICNNCVERFDHHCPWVGQCIGQRNYRYFFLFVSSSTLLCIYVFAMSALHIKFLMDGDYPTVWKAFKHSPACLVLMIYCFIALWFVGGLTGFHSYLISTNQTTYENFRYRSDNRPNVYNQGCLNNFLEVLCSKGKPSKHRFRAYVQEEVRAPVVNFGRQMEEEPTGGS... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 426
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 48293
Location Topology: Multi-pass membrane protein
|
A0A811LD94 | MGRRTAAVSQKGSAPPLSEYYLPAEPVYNEIETVPHQTHQFPVVQKTTESQNFHGVVPKQLHGHHFVLTTQRPVVQPVVGQRAANFELRRAEKLLNKNPERAAKKPFNPIVLTRRGCTDVPFCMLFILYLFGWTFVAFIAYKYGKPERILHPTDSWGNSCGSNRPSVYETIDKPYLFFFDLTKCVSYATLLSGCPTFQMCVKKCPTKYWSYLSLNRASLWSQQSVKDNAFCDYTVDIDTIQNFSQLRDLVKAGKCAAYTVPSSVVLGRCVPEVIVEASNVFNENGTLNNLLANFGNEDNLVAPDSKISETQEVVKAIAQG... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 655
Sequence Mass (Da): 73882
Location Topology: Multi-pass membrane protein
|
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