accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q9PCE6 | FABV_XYLFA | Enoyl-[acyl-carrier-protein] reductase [NADH] | Xylella | MIIHPKTRGFICTTTHPVGCEYNVLEQIQSTRARGVRSNGPKKVLVIGASSGYGLATRISAAFGFGADTLGVFFEKPGTEKKPGTAGWYNAAAFDKSAKNAGLYSRSINGDAFSDEMRAKVIEIIKSEMGGHVDLVVYSLASPLRKMPSTGEIKRSVLKPIGVAHISNAIDTNKDQIIQATVEPATEQEIADTVAVMGGQDWELWINALTQADVLAPQTRTVAFSYIGTEITWPIYWHGALGKAKADLDATSRRLDARLQALGGGANVAVLKSVVTQASAAIPALPLYIAIVFKVMKEKGLHEGTIEQADRLLRERLYRE... | Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). | Q9PCE6 |
Q8TAU0 | NKX23_HUMAN | Homeobox protein NK-2 homolog C | Homo | MMLPSPVTSTPFSVKDILNLEQQHQHFHGAHLQADLEHHFHSAPCMLAAAEGTQFSDGGEEDEEDEGEKLSYLNSLAAADGHGDSGLCPQGYVHTVLRDSCSEPKEHEEEPEVVRDRSQKSCQLKKSLETAGDCKAAEESERPKPRSRRKPRVLFSQAQVFELERRFKQQRYLSAPEREHLASSLKLTSTQVKIWFQNRRYKCKRQRQDKSLELGAHAPPPPPRRVAVPVLVRDGKPCVTPSAQAYGAPYSVGASAYSYNSFPAYGYGNSAAAAAAAAAAAAAAAAYSSSYGCAYPAGGGGGGGGTSAATTAMQPACSAA... | Transcription factor. | Q8TAU0 |
Q9PPF1 | UBIX_CAMJE | Flavin prenyltransferase UbiX | Campylobacter | MKVLLGISGSSSVNLGLKLLKNLENQCELYCILTQGAKLNFKTENQANLEEICQENFKYTHFLDDKNLSLSVASGSFGIEKTIIAPCSISSLAKIHAGFADTLLMRAAAVALKERKKLILGVREMPFSTLNLEHMLKLSQMGVIIAPPIIASYSKANNLEQMENFIAGKWLDLLEIKHNLYEKWQNF | Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN. | Q9PPF1 |
B7N2F3 | PEPQ_ECO81 | Proline dipeptidase | Escherichia | MESLASLYKNHIATLQERTRDALARFKLDALLIHSGELFNVFLDDHPYPFKVNPQFKAWVPVTQVPNCWLLVDGVNKPKLWFYLPVDYWHNVEPLPNSFWTEDVEVIALPKADGIGSLLPAARGNIGYIGPVPERALQLGIEASNINPKGVIDYLHYYRSFKTEYELACMREAQKMAVNGHRAAEEAFRSGMSEFDINIAYLTATGHRDTDVPYSNIVALNEHAAVLHYTKLDHQAPEEMRSFLLDAGAEYNGYAADLTRTWSAKSDNDYAQLVKDVNDEQLALIATMKAGVSYVDYHIQFHQRIAKLLRKHQIITDMSE... | Splits dipeptides with a prolyl residue in the C-terminal position. | B7N2F3 |
Q3YS64 | MDH_EHRCJ | Malate dehydrogenase | Ehrlichia | MIKRKKIALIGAGNIGGMIAYLIRLKNLGDVVLLDVNDGIAKGKALDMAESSPVGKYNGEILGTNNYADIEGADAIVVTAGITRKPGMSREDLINTNVNIIKEVADNIGKYAPNAFVVVVTNPLDVMVFAMHKYSKLSSNMVVGMAGILDSARFSYFIAKELNVSVDNVNSLVLGGHGDLMLPLVKYSSVAGISIADLIKIDLITQDKVDAIIERTRKGGEEIVSLLKIGSAYYAPAESALLMIDSYLNDRRLILPCSVYLKGEYGVSNLFVGVPVIIGRNGVEKIIELELTEQEKNIFDNSVKLIKNLVSNV | Catalyzes the reversible oxidation of malate to oxaloacetate. | Q3YS64 |
Q0S3G6 | RL14_RHOJR | 50S ribosomal protein L14 | Rhodococcus | MIQQESRLRVADNTGAKEILCIRVLGGSSRRYAGIGDIIVATVKDAIPGGNIKKGEVVKAVIVRTTKERRRPDGSYIKFDENAAVLIKPDNDPRGTRIFGPVGRELREKKFMKIVSLAPEVL | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | Q0S3G6 |
Q6WN98 | CCR5_MICHU | C-C chemokine receptor type 5 | Mico | MDYQVSSPIYDIDYGPSEPCRKIDVKQMGAHLLPPLYSMVFLFGFVGNMLVVLILINCKRLKSMTDIYLLNLAISDLIFLFTVPFWAHYAAGQWDFGNTMCQFLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGYHYTCSPHFPFSQYQFWKNFETLKMVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTYQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCVNPIIYAFVGEKFRNYLKVFFQKHIAKCF... | Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migrati... | Q6WN98 |
Q5YK47 | MATK_ALBJU | Intron maturase | Albizia | MEEFQVYLELDRSRQHDFLYPLIFREYIFALAYDHGLNSSILVQNLGYDNKSSLLIVKRLITRMYQQNHLIISANNSNKNPFWGYNKNLYSQIISEGLAVSVEIPFSLQFISSLEKAEIIKSYNLRSIHSIFPFFEEKFPYLNYVSDVQIPYPIHLEILIQTLRYWVKDASSFHLLRLFLYEYCNWNSLITPKKRISTFSKSNPRFLLFLYNFYVCEYESIFLFLRNKSSYLRLTSSGVFFERIYFYAKIEHFVEVFDKDFPSTLWFFKDPFIHYVRYQGKSILASKNTPFLMKKWKYYLIHLWQCHFFVWSQPGKIHIN... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q5YK47 |
Q6FPQ3 | MPH1_CANGA | FANCM-like protein 1 | Nakaseomyces/Candida clade | MEDSDFDDAELDELYEKAINRRVNETLIRRSLPVQRDLQNGVVPGQDTYYEEIRTEVTFGPTHHQLNEELLHSYIYPTNFEVRDYQFDIVRKGLLQNILCAIPTGMGKTFIASTVMLNFFRWTKTAKIIFTAPTRPLVAQQIKACLGITGIPHDQTAILLDKTRKNREEIWANKRVFFTTPQVVENDLKRGVLNPKDIVCLVIDEAHRATGSYAYANLVKFINRFNSSYRLLALTATPATDIEGVQEVVNNLNISKIEIRTEESMDIVKYMKKKIKDRVNIQTTVEIENIVEQLGIAILPVLNQAVELGIYESCPPSAIN... | ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked re... | Q6FPQ3 |
P18938 | NU3M_CHICK | NADH dehydrogenase subunit 3 | Gallus | MNTLTFMLSLSFLLSAALTTMNFWLAQMAPDTEKLSPYECGFDPLGSARLPFSIRFFLVAILFLLFDLEIALLLPLPWAIQLAHPMMTLTWATTIIALLTFGLIYEWTQGGLEWAE | 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 of complex I. | P18938 |
Q7U5I8 | RBL_PARMW | Ribulose bisphosphate carboxylase large chain | Parasynechococcus marenigrum | MSKKYDAGVKEYRDTYWTPDYVPLDTDLLACFKCTGQEGVPKEEVAAAVAAESSTGTWSTVWSELLTDLDFYKGRCYRIEDVPGDKESFYAFIAYPLDLFEEGSITNVLTSLVGNVFGFKALRHLRLEDIRFPMAFIKSCYGPPNGIQVERDRMNKYGRPLLGCTIKPKLGLSGKNYGRVVYECLRGGLDFTKDDENINSQPFQRWQNRFEFVAEAIKLSEQETGERKGHYLNVTANTPEEMYERAEFAKELGMPIIMHDFITGGFTANTGLSKWCRKNGMLLHIHRAMHAVIDRHPKHGIHFRVLAKCLRLSGGDQLHT... | 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. | Q7U5I8 |
Q8BXN9 | TM87A_MOUSE | Transmembrane protein 87A | Mus | MAVAAWLQVSPVIFLLLGAQPFPLSFLGAGPAPVFAADRSKWHIPMPSGKGYFNFGKILFRNTTILLKFDGEPCDQSLNITWFLKSADCYNEIYNFKADEIESYLENLKGKKGLSGRYQTSSRLFQNCSELYKAQSFSGDFTHRLPLLGEKQEAKENATNVTFTGDKIAMHEPLQTWQDAPYIFIVHVGISSSKESPKENALSNLFTMTVEVKGPYEYLTLEDYPLMIFFMVMCIVYVLFGVLWLAWSACYWRDLLRIQFWIGAVIFLGMFEKAVFYAEFQNIRYKGESVQNALVLAELLSAVKRSLARTLVIIVSLGYG... | May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN). | Q8BXN9 |
Q9SE97 | FH1_ARATH | Formin-like protein 1 | Arabidopsis | MLFFLFFFYLLLSSSSDLVFADRRVLHEPFFPIDSPPPSPPSPPPLPKLPFSSTTPPSSSDPNASPFFPLYPSSPPPPSPASFASFPANISSLIVPHATKSPPNSKKLLIVAISAVSSAALVALLIALLYWRRSKRNQDLNFSDDSKTYTTDSSRRVYPPPPATAPPTRRNAEARSKQRTTTSSTNNNSSEFLYLGTMVNQRGIDEQSLSNNGSSSRKLESPDLQPLPPLMKRSFRLNPDVGSIGEEDEEDEFYSPRGSQSGREPLNRVGLPGQNPRSVNNDTISCSSSSSGSPGRSTFISISPSMSPKRSEPKPPVIST... | Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes. | Q9SE97 |
A1CNY1 | MDM12_ASPCL | Mitochondrial inheritance component MDM12 | Aspergillus subgen. Fumigati | MSIDINWRTATSGPDGEALAERIRSFIHDRFQQVALPRFIRSVQVHSFDFGTIPPELEIKDFCEPFADFYEEDDDADTSDVSEDLLSEHSSQWDRTHSELNEPPYREESAMNHGLRDPFHEGFPPSPLRSPLGEHLNPHFLPRAGTPGIPGGTSNLGYHLMSLGGLSGTQTPLAAVAGGNPFASGWSDSGMGFGNRGRSERQGPIPQHRPEPEIDTSNSTSRPSTANTLPSHLSESNNLNADGATGRNERGSLHNGDPLADHTCSGHLPLPPRMRERRPEDFQVLCHAKYAGDVRLSLTAEILLDYPMPSFVGLPLKLNV... | Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm12 i... | A1CNY1 |
A6V3A0 | NQRD_PSEA7 | NQR-1 subunit D | Pseudomonas | MAAQPTIREVLFNPVFQNNPIGLQILGICSALAVTSNLKTATVMAIALTLVTGFSNLFISMIRRQIPSSIRMIVQMVIIASLVIVVDQVLKAYAYSLSKQLSVFVGLIITNCIVMGRAEAFAMANPPLVSFFDGIGNGLGYSAMLLVLGFIRELFGAGKLYGISVLPTVNDGGWYQPNGLLLLPPSAFFLIGLIIWALRTWKKDQVEAPAYRMAPQVSSKEAY | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. | A6V3A0 |
B2SXB8 | HEMH_PARPJ | Protoheme ferro-lyase | Paraburkholderia | MRFDLERPSQNASSHRVAVLLINLGTPDAPTPRAVRRYLAQFLSDPRVVEIPALLWQIILRLLILPFRGVASAKKYAAVWMPEGSPLRVNTEKQVEGLRHLLQLNDYTVLVDYAMRYGTPGIPAMLNQLKLAGAERVLLMPMYPQYSSSTTATAFDDAFSALKRMRNQPEIRTVRQYADHPAYIAALAAQVHNYWHQHGRPDFAAGDKLVLSFHGVPKRTLDLGDPYHEQCQQTGALLMQALELTQVECRITFQSRFGKAEWLQPYTAPTLKELGAAGVRRADVFCPGFTADCLETIEEIGMEVRDEFLHAGGKDFHRIP... | Catalyzes the ferrous insertion into protoporphyrin IX. | B2SXB8 |
Q5PK78 | MURB_SALPA | UDP-N-acetylmuramate dehydrogenase | Salmonella | MTHSLKPWNTFGIDHCAKHIVCAENEQQLLSAWQQATREGLPVMILGEGSNVLFLENYAGTVILNRLKGIEVNETADAWHLHVGAGENWHQLVRYALDNNMPGLENLALIPGCVGSSPIQNIGAYGVELQCVCDYVDCVELETGKRLRLSAAECRFGYRDSIFKNEYQDRVAIVAVGLRLSKQWQPVLTYGDLTCLDPKTVTAQQVFDAVCHMRTTKLPDPKVNGNAGSFFKNPVVAADIAMELLERFPNAPHYPQADGSVKLAAGWLIDQCQLKGVTIGGAAVHRQQALVLINANDATSKDVVALAHHVRQKVGEKFNV... | Cell wall formation. | Q5PK78 |
O22034 | CFXQ2_CYACA | Protein CfxQ homolog | Cyanidium | MKVNLQTEFKQTQIQQVLDDLDRELIGLQAVKTRIREIAALLLVDRLRQKLGLSSSNPGLHMSFTGSPGTGKTTVATKMADILYRLGYIKKGHLITVTRDDLVGQYIGHTAPKTKQVLKNAMGGVLFIDEAYYLYRPDNERDYGAEAIEILLQVMENQRDDLVIIFAGYKEKMDRFYASNPGLSSRVANHVNFPDYTPEELLMIGKIMLQEQQYQFTPEAEEVFLQYIQRRMQQPHFANARSVRNALDRARLRQANRIFATPGQNLTKYDLVTIQAEDILKCRLFQ | Necessary for the expression of RuBisCO. | O22034 |
P98008 | NORB_PSEST | Nitric oxide reductase cytochrome b subunit | Pseudomonas | MSSFNPHLKFQSQAVAKPYFVFALILFVGQVLFGLIMGLQYVVGDFLFPLLPFNVARMVHTNLLIVWLLFGFMGAAYYLIPEESDCELHSPKLAIILFWVFAAAGVLTILGYLFVPYAALAEMTRNDLLPTMGREFLEQPTITKIGIVVVALGFLYNIGMTMLKGRKTVVSTVMMTGLIGLAVFFLFAFYNPENLSRDKFYWWFVVHLWVEGVWELIMGAMLAFVLIKVTGVDREVIEKWLYVIIAMALITGIIGTGHHFFWIGAPTVWLWVGSIFSALEPLPFFAMVLFALNMVNRRRREHPNKAASLWAIGTTVTAFL... | Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). NorB is the catalytic subunit of the enzyme complex. Shows proton pump activity across the membrane in denitrifying bacterial cells. The mononitrogen reduction is probably coupled to electron transport phosphorylation. | P98008 |
Q6RSH6 | CYB_AKOAL | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Akodon | MKILRKNHPLLKIVNHSFIDLPTPSSISSWWNFGSLLGVCLMIQILTGLFLAMHYTSDTTTAFSSVAHICRDVNYGWLIRYLHANGASMFFICLFIHVGRGIYYGSYVLSETWNIGIILFLTTMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGSTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPSGLNSDSDKIPFHPYYTIKDLLGILLLLLALMILALFFPDILGDPDNFTPANPLNTPAHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILATFPLLNTSKQHGLIFRPI... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | Q6RSH6 |
B7V2X1 | AMIE_PSEA8 | Acylamide amidohydrolase | Pseudomonas | MRHGDISSSNDTVGVAVVNYKMPRLHTAAEVLDNARKIADMIVGMKQGLPGMDLVVFPEYSLQGIMYDPAEMMETAVAIPGEETEIFSRACRKANVWGVFSLTGERHEEHPRKAPYNTLVLIDNNGEIVQKYRKIIPWCPIEGWYPGGQTYVSEGPKGMKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKDQQVMMAKAMAWANNCYVAVANAAGFDGVYSYFGHSAIIGFDGRTLGECGEEEMGIQYAQLSLSQIRDARANDQSQNHLFKILHRGYSGLQASGDGDRGLAECPFEFYRTWVTDAEKARENVE... | Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. | B7V2X1 |
Q0TY47 | RRG9_PHANO | Required for respiratory growth protein 9, mitochondrial | Parastagonospora | MSCHNCARRTLGLFIRSFANVEPTFAPKRTLIRNAQPSRLLHASTARAPYKSDQRDRAAPPTQKEADIEAIAENAENAEDDALPAKYERPAWQAHKAALKEKLNGEAWNPRKKLSPDTMEGIRHLHSTQPDKFTTPVLAQHFKVSPEAIRRILKSKWQPSDEEYEARMERWNKRGERIWTNLVEMGVKPPKKWREMGVGRARGGERPKWKSDRRNLVHVRDSASDSFVMDDGDIIPIVDGTGKARRAPDIPLTRRL | Required for respiratory activity and maintenance and expression of the mitochondrial genome. | Q0TY47 |
Q0WPF2 | PCFS4_ARATH | Polyadenylation and cleavage factor homolog 4 | Arabidopsis | MDSEKILNPRLVSINSTSRKGMSVELPQKPPPPPSLLDRFKALLNQREDEFGGGEEVLPPSMDEIVQLYEVVLGELTFNSKPIITDLTIIAGEQREHGEGIANAICTRILEAPVEQKLPSLYLLDSIVKNIGRDYGRYFSSRLPEVFCLAYRQAHPSLHPSMRHLFGTWSSVFPPPVLRKIDMQLQLSSAANQSSVGASEPSQPTRGIHVNPKYLRRLEPSAAENNLRGINSSARVYGQNSLGGYNDFEDQLESPSSLSSTPDGFTRRSNDGANPSNQAFNYGMGRATSRDDEHMEWRRKENLGQGNDHERPRALIDAYG... | Promotes flowering by suppressing FLC-mediated inhibition of flowering through the regulation of FCA pre-mRNA alternative processing . Regulates mRNA maturation including alternative polyadenylation, splicing or transcription initiation of stress-associated genes . | Q0WPF2 |
B7N6X5 | TRUD_ECOLU | tRNA-uridine isomerase D | Escherichia | MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDLSAFQLEGCQVLEYVRHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQRRVNDKELMITAALPGSGEWGTQREALAFEQAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEI... | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | B7N6X5 |
Q211F9 | RL24_RHOPB | 50S ribosomal protein L24 | Rhodopseudomonas | MAAKIRKGDKVIVLNGRDKGRTGEVFEVRPTENKALVRGVNLVKRHQKQTQAQEGGIISKEAAIHLSNIAIVGKDGKPTRVGFKIQADGKKVRIAKRSGAEIDG | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | Q211F9 |
Q6LY04 | RPIA_METMP | Phosphoriboisomerase A | Methanococcus | MARTKKANDEVATDSDSLKLKVAKQAAKLVKDEMVVGLGSGSTANLFIQELGKRVVEEELYIYGVPTSFDSRMMASNSGIPLISLDQCGEIDIAIDGADEVCKKTLSLIKGGGGCHTMEKIVDYHAKEFVVLADEGKLVESLGDKTAVPLEVIPFAYSTVLNKLLDMNTAPAIRSGSGKMGPVITDNGNMIIDVFINIEDAEETETMLNNIPGVLENGIFSKCDKVLVGTSKKVEILKK | Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. | Q6LY04 |
A5E8J0 | HRCA_BRASB | Heat-inducible transcription repressor HrcA | unclassified Bradyrhizobium | MAHHDPINLMTPPAGLAQLNERSREIFRQIVESYLATGEPVGSRNISRLIAVPLSPASVRNVMADLEQLGLIYAPHTSAGRLPTEAGLRFFVDALMQVGDMTEAERQSIQSQLASVGRAQSVEAALDEALTRLSGLTRAAAVVLTAKSNTRLKHIEFVRLEPERALVVLVGEDGQVENRVLALPPGVPSSALTEASNFLNARIRGRTLAEARLELETALAHDRAELDQLTQKVIAAGVASWSGGDSDDRQLIVRGHANLLEDLHALEDLERVRRLFDDLETKRGVVDLLGRAENADGVRIFIGSENKLFSLSGSSTIVSP... | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. | A5E8J0 |
P43914 | EX7S_HAEIN | Exodeoxyribonuclease VII small subunit | Haemophilus | MARKPASSQDFETTLVQLENIVTHLENGDLPLEEALKEFEQGVQLAKLGQERLQQAEQRIQILLQKTEDAPLNDYKGNDYEGNA | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | P43914 |
Q1R5B9 | RSMJ_ECOUT | rRNA (guanine-N(2)-)-methyltransferase | Escherichia | MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALSDITPRPQVVCLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLLATKRVVVKRPDYAPPLANVATPNAVVTKGHRFDIYAGTPV | Specifically methylates the guanosine in position 1516 of 16S rRNA. | Q1R5B9 |
Q4R4U3 | PRPS1_MACFA | Phosphoribosyl pyrophosphate synthase I | Macaca | MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATRVYAILTHGIFSGPVISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. | Q4R4U3 |
Q47JQ1 | RLMH_DECAR | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Dechloromonas | MKLAVLAVGHRQPDWVNEGCAEYLKRMPRELAASVTEIKPEARGSKTREQLLAAEKSRIRDAMAAGSRLVVLDEKGDDLTTLKLAKRLETWMQDGRDVALLIGGADGLDEEFKQQADDRLRLSSLTLPHGMARLLLCEQLYRAVSVLKNHPYHREG | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q47JQ1 |
Q2YWE7 | CRTM_STAAB | Dehydrosqualene synthase | Staphylococcus | MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFLNQIKEDIQSIEKYPYEHHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMFETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFENERIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFRDVMDQIKVFSIEAQPIIELAARIYIEILDEVRQASYTLHERVFVYKRKKAKLFHEINSKYHRI | Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosq... | Q2YWE7 |
A6TG35 | ATPE_KLEP7 | F-ATPase epsilon subunit | Klebsiella | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A6TG35 |
Q700D9 | MYBF_ARATH | Putative Myb family transcription factor At1g14600 | Arabidopsis | MGRCGRSNDGVIGGVRPYVRSPVPRLRWTPELHRSFVHAVDLLGGQYKATPKLVLKIMDVKGLTISHVKSHLQMYRGSRITLLGKPEESSSPSSRRRRRQDNEEDHLHDNLSVHARNDCLLGFHSFNFREQTSATDNDDDDFLNIMNMERTKTFAGNGESIKFQSHHSLEAENTKNIWKNTWRENEHEEEEELSLSLSLNHPHNHQQRWKSNASSSLSETSEAVSSSSGPFIFRDCFASSKIDLNLNLSFSLLHS | Putative transcription factor. | Q700D9 |
Q15040 | JOS1_HUMAN | Josephin domain-containing protein 1 | Homo | MSCVPWKGDKAKSESLELPQAAPPQIYHEKQRRELCALHALNNVFQDSNAFTRDTLQEIFQRLSPNTMVTPHKKSMLGNGNYDVNVIMAALQTKGYEAVWWDKRRDVGVIALTNVMGFIMNLPSSLCWGPLKLPLKRQHWICVREVGGAYYNLDSKLKMPEWIGGESELRKFLKHHLRGKNCELLLVVPEEVEAHQSWRTDV | Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cel... | Q15040 |
M9XB82 | PK23_MEIRD | AMP/ADP-polyphosphate phosphotransferase | Meiothermus | MKKYRVQPDGRFELKRFDPDDTSAFEGGKQAALEALAVLNRRLEKLQELLYAEGQHKVLVVLQAMDAGGKDGTIRVVFDGVNPSGVRVASFGVPTEQELARDYLWRVHQQVPRKGELVIFNRSHYEDVLVVRVKNLVPQQVWQKRYRHIREFERMLADEGTTILKFFLHISKDEQRQRLQERLDNPEKRWKFRMGDLEDRRLWDRYQEAYEAAIRETSTEYAPWYVIPANKNWYRNWLVSHILVETLEGLAMQYPQPETASEKIVIE | Uses inorganic polyphosphate (polyP) as a donor to convert both AMP to ADP and ADP to ATP. Can also use GMP, CMP, UMP, GDP, CDP and UDP. | M9XB82 |
Q9STX5 | ENPL_ARATH | Protein SHEPHERD | Arabidopsis | MRKRTLVSVLFLFSLLFLLPDQGRKLHANAEESSDDVTDPPKVEEKIGGHGGLSTDSDVVHRESESMSKKTLRSNAEKFEFQAEVSRLMDIIINSLYSNKDIFLRELISNASDALDKIRFLALTDKDVLGEGDTAKLEIQIKLDKAKKILSIRDRGIGMTKEDLIKNLGTIAKSGTSAFVEKMQSSGDLNLIGQFGVGFYSAYLVADYIEVISKHNDDSQYVWESKANGKFAVSEDTWNEPLGRGTEIRLHLRDEAGEYLEESKLKELVKRYSEFINFPISLWASKEVETEVPVEEDESADEETETTSTEEEKEEDAEEE... | May have a molecular chaperone role in the processing of secreted materials. Required for shoot apical meristem (SAM), root apical meristem (RAM) and floral meristem (FM) formation, probably by regulating the folding of CLAVATA proteins (CLVs). Also involved in pollen tube elongation . Involved in resistance to tunicam... | Q9STX5 |
Q9C8N5 | STOP1_ARATH | Zinc finger protein STOP1 | Arabidopsis | METEDDLCNTNWGSSSSKSREPGSSDCGNSTFAGFTSQQKWEDASILDYEMGVEPGLQESIQANVDFLQGVRAQAWDPRTMLSNLSFMEQKIHQLQDLVHLLVGRGGQLQGRQDELAAQQQQLITTDLTSIIIQLISTAGSLLPSVKHNMSTAPGPFTGQPGSAVFPYVREANNVASQSQNNNNCGAREFDLPKPVLVDEREGHVVEEHEMKDEDDVEEGENLPPGSYEILQLEKEEILAPHTHFCTICGKGFKRDANLRMHMRGHGDEYKTAAALAKPNKESVPGSEPMLIKRYSCPFLGCKRNKEHKKFQPLKTILCV... | Probable transcription factor. Together with STOP2, plays a critical role in tolerance to major stress factors in acid soils such as proton H(+) and aluminum ion Al(3+). Required for the expression of genes in response to acidic stress (e.g. ALMT1 and MATE), and Al-activated citrate exudation. | Q9C8N5 |
Q969I3 | GLYL1_HUMAN | Glutamine N-acyltransferase | Homo | MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQKQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFSKSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSGLVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRRTGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLVPF | Acyltransferase which transfers an acyl group to the N-terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor. | Q969I3 |
Q149M9 | NWD1_HUMAN | NACHT domain- and WD repeat-containing protein 1 | Homo | MQRGKPCRALPTLKCQTFCQRHGLMFEVVDLRWGIRNIEATDHLTTELCLEEVDRCWKTSIGPAFVALIGDQYGPCLIPSRIDEKEWEVLRDHLTARPSDLELVARYFQRDENAFPPTYVLQAPGTGEACEPEEATLTSVLRSGAQEARRLGLITQEQWQHYHRSVIEWEIERSLLSSEDREQGATVFLREIQDLHKHILEDCALRMVDRLADGCLDADAQNLLSSLKSHITDMHPGVLKTHRLPWSRDLVNPKNKTHACYLKELGEQFVVRANHQVLTRLRELDTAGQELAWLYQEIRHHLWQSSEVIQTFCGRQELLA... | May play a role in the control of androgen receptor (AR) protein steady-state levels. | Q149M9 |
A2C1Y5 | RUVA_PROM1 | Holliday junction ATP-dependent DNA helicase RuvA | Prochlorococcus | MISWLKGEKVHTWKISSRKGVVLNVGGVGYEIQLLPKQIDKAEVLNEFELWIHQIDREDGTSLYGFIEVNQRDLFREIISVNGIGPQIGMAMLEEFEVPQLVNAIENKESNLLTKTQGIGKRIAERLIVELRNKLQRFTDNDKTIHENKKGIEANQFSKYIDEIYLILNSLGYVDNEIKESIKIITINEKENSLLLNSSSAEEKAELMDKHLKEILMKLSEKTT | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | A2C1Y5 |
Q3BN06 | AROE_XANC5 | Shikimate dehydrogenase (NADP(+)) | Xanthomonas | MPVSRYAVFGHPVAHSLSPAIHTEFGKQTGIALDYTAIDAPLEDFSAALQRFADEGGKGANVTLPLKEAAYALASSLSDRARLAGAVNTLVRNDGQWQGDNTDGAGLVRDLTERQGLDLRGRRVLLLGAGGAARGVAPALLEAGITAMVVVNRSPERADALCDALGEPARVTSRYIEDLRELGDFELIVNATAAGRDRDAGAFALPLGLVNSLTAAVDLNYGDTAIAFLAWARAAQCRYAIDGLGMLVEQAAESFALWHGVRPDTDPVYAALRAREAVLVSAD | 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). | Q3BN06 |
P36091 | DCW1_YEAST | Endo-alpha-1->6-D-mannanase DCW1 | Saccharomyces | MLVNKVIGLLGVLFATRFTNAVELDLDNYESLQNATSLIAYGLMDYYTGNQYGKTVGMFSDPYYWWEAGGAWGCMLDYWFFMDNDTYNDEIIAAMIHQAGDDNDYIPLNQSTTEGNDDQAFWGIAAMTAAERNFTNPPENEPQWLYLAQAVFNTMALRWDADSCGGGLRWQIFVWNSGYDYKNTVSNGALFHIAARLARYTGNQTYVDWAEKVYEWMVGVNLISNGTYKYVYDGVSIDDNCTKVTSYQWTYNQGLLLAGSAYLYNFTGSDLWHTRTKEFLNASQVFFHDGIVYEAACQGPNSCNTDQRSFKAYFARFLGV... | Required for normal synthesis of the cell wall. | P36091 |
Q5FIV0 | PURQ_LACAC | Phosphoribosylformylglycinamidine synthase subunit I | Lactobacillus | MKIAVVVFPGSNCDIDMYEAFHTVCKDDVEYVSYKEKSLDGFDVVVLPGGFSYGDYLRTGAIARFSNIIPAVENMAKEGKLVLGVCNGFQILTEMGLLPGALKKNDSLQFVCKTVTLEVENMHTPFTNEYADKEFIQIPIAHGDGSYYADENVLEELEDNHQVVFRYHGENPNGSLHDIAGICNKEGNVLGMMPHPERAVEEILGGIDGLPLFKSLLKAGVQA | Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three su... | Q5FIV0 |
B7NKU9 | MDH_ECO7I | Malate dehydrogenase | Escherichia | MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSGEDATPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVQQVAKTCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPGEVEVPVIGGHSGVTILPLLSQVPGVSFTEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVRALQGEQGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEKNALEGMLDTLKKDIALGEEFVNK | Catalyzes the reversible oxidation of malate to oxaloacetate. | B7NKU9 |
P15458 | 2SS2_ARATH | 2S seed storage protein 2 large subunit | Arabidopsis | MANKLFLVCATFALCFLLTNASIYRTVVEFDEDDASNPMGPRQKCQKEFQQSQHLRACQKLMRMQMRQGRGGGPSLDDEFDLEDDIENPQGPQQGHQILQQCCSELRQEEPVCVCPTLRQAARAVSLQGQHGPFQSRKIYKTAKYLPNICKIQQVGECPFQTTIPFFPPY | This is a 2S seed storage protein. | P15458 |
Q2FPV1 | HIS6_METHJ | ImGP synthase subunit HisF | Methanospirillum | MTLTRRIIPCLDIKDGRVVKGTNFLGLRDAGDPVELACRYNEQGADEVVFLDITASRENRGMIIDVIQRAADELFLPLTVGGGIRTLDDVQKTLRAGADKVSINTSAVQNPALISEAAQAFGTQCVVVAIDVKRRTSPEPGKTMIPLPDQSSCWYEVVTHGGSQPTGIDAIAWAKEAENRGAGEILLTSMETDGTKEGFDIPITSAISESVGIPVIASGGVGTFDHFYEGFVYGKADAALAASVFHYGEMTIADVKDYLSKKGIAIRPHTQ | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | Q2FPV1 |
Q6DLR9 | NBZA_PSEOL | Type I nitroreductase | Pseudomonas oleovorans/pseudoalcaligenes group | MPTSPFIDDLIRDRRAKRGFLDQPVSIEMVKDILSAAKYAPSSSNTQPWRCYVITGEARERITTAAVEAYRAAPEGLPPEYPFFPQPLHEPYATRFNSFRGQLGDALGIPRSDITLRRRDVERQFRFFDAPVGLIFTMDRRLEWASFICYGCFLQNIMLAAKGRGLDTCTQVFWSMQHPVLRTELNLPDDQMVVAGMSLGWADNSLPENQMSISKMELEEFTTFVHE | Involved in the biodegradation of nitroaromatic compounds . Catalyzes the two-electron reduction of nitrobenzene (NB) to produce a nitrosobenzene (NOB) intermediate, which is immediately reduced to hydroxylaminobenzene (HAB) by a second two-electron transfer . Also active on menadione and nitrofurazone . Replacing NADP... | Q6DLR9 |
A6M317 | UNG_CLOB8 | Uracil-DNA glycosylase | Clostridium | MSDILKNDWKNYLQSEFQKDYYINLRKFLINEYNSKTIYPNMYDLFNALHFTPYNKVKVVILGQDPYHGPGQAHGLSFSVNPGVKTPPSLINIYKELHTDLGCYIPNNGYLRKWADQGVLLLNTVLTVRAGEANSHKNKGWEEFTNEVIKVLNKKETPIVFILWGNNAISKTDFITNPKHLIIKSVHPSPLSASRGFFGSKPFSKTNNFLISTNQEPIDWQIENI | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | A6M317 |
B2UZL0 | METK_CLOBA | Methionine adenosyltransferase | Clostridium | MKRLFTSESVTEGHPDKMCDQISDAILDAILAKDSNARVACETCTTTGLVMVMGEISTNCYVDIPKVVRETVREIGYDRAKYGFDCDTCSVMTTIDEQSADIAMGVDEALESKKGQKDEVEAVGAGDQGMMFGFATNETDAYMPLPIYMAHKLSRRLTEVRKDGTLDYLRPDGKTQVTVEYENNKPKRIDTIVISTQHGEEVSLETIEKDIKEHVINAVVPAELLDAETRYFINPTGRFVVGGPQGDSGLTGRKIIVDTYGGYGRHGGGAFSGKDSTKVDRSAAYAARWVAKNLVAAGIADKLEIQLAYAIGVAKPVSIE... | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B2UZL0 |
Q8SY96 | NFU1_DROME | NFU1 iron-sulfur cluster scaffold homolog, mitochondrial | Sophophora | MSKFLSQAALNTLRNTRLGSRQLVRSFKGISNTRNHRIPAHQESGCGHSVGCGLLELRMPVACRRSMFIQTQDTPNPESLKFLPGVDVLGKGNTYDFPNGTTAHNSPLAKLLFRVEGVKGVFFGADFVTISKQEGAEWSLIKPEVFAVIMDFFASGLPVLNDAQPNADTEILEDDDETVMMIKELLDTRIRPTVQEDGGDIVFMGYEGGVVKLKMQGSCSSCPSSIVTLKNGVQNMLQFYIPEVESVEQVFDEADRMIESEFERFEKNLKTLKQQEPSGGGPH | Molecular scaffold for [Fe-S] cluster assembly of mitochondrial iron-sulfur proteins. | Q8SY96 |
P48556 | PSMD8_HUMAN | p31 | Homo | MFIKGRAPRAPPRERRRATRGGLRQVVAPPRALGSTSRPHFRRASVCRRRCRKSGGLLAASRKMAAAAVNGAAGFSSSGPAATSGAVLQAATGMYEQLKGEWNRKSPNLSKCGEELGRLKLVLLELNFLPTTGTKLTKQQLILARDILEIGAQWSILRKDIPSFERYMAQLKCYYFDYKEQLPESAYMHQLLGLNLLFLLSQNRVAEFHTELERLPAKDIQTNVYIKHPVSLEQYLMEGSYNKVFLAKGNIPAESYTFFIDILLDTIRDEIAGCIEKAYEKILFTEATRILFFNTPKKMTDYAKKRGWVLGPNNYYSFAS... | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions ... | P48556 |
Q95LB0 | APOH_PANTR | Beta-2-glycoprotein I | Pan | MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPITCPPPSIPTFATLHVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTI... | Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Q95LB0 |
C1A9H6 | EFP_GEMAT | Elongation factor P | Gemmatimonas | MAFSATQIRRGMVLVFEGDPCRVIEFRHHTPGNLRAMVQAKLKNLRTGSNFEHRFRAADTIVKADMETHELEFMYQGGDTYHFMNSENYDQLELDDEALGDSAPWMQPGLKILAEYYNGRPIGIQLPNSLVFEIVETAPVVRGATKTASSKPAKLENGVTVNVPEFVEQGTRVRVNPSTGEYLDRAKD | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | C1A9H6 |
A0A0D4BS77 | IND1_STRGR | S-adenosylmethionine: indolepyruvate 3-methyltransferase | Streptomyces | MTRTDFAQSAVASIFTGAIASHAAVLADDLGLFDALAKGKLRNRDLDRSPWLRNRIRISGALEALCRVGAVQRCTDGYELTDVGTELAGQVPVFRLWLGGYASVLAGQISIGADPATGVHGGIVAESSGAIGARYLDETIVNLLESLRPEGRICDIGCGTGARLLRVCRRVNQPGIGYDLSAKAVEAARETVDEARRIGVDIDVRQGDATALTQDHPDVDIVTQAFMTHHIAPDEYCAAVLRSYRSRFPRARYLVIFDTVPSQDSEEPEIFAPGFDYIHALQNMEPRSRGAARRMFTEAGYICREEVELAVPNSYAWVLE... | Involved in the biosynthesis of the antibiotic indolmycin, an inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to position 3 of the aliphatic side chain of (indol-3-yl)pyruvate to yield 3-methylindolepyruvate. | A0A0D4BS77 |
Q8TXZ3 | IF1A_METKA | Translation initiation factor 1A | Methanopyrus | MGKRIDDETLKKIRLPKEGEIFGVVEKMLGNDRVQVRCVDGKTRVARIPGKMRKRVWIREGDVVLVKPWEFQPERADVTWRYTRVQVDWLKRKGKLDERVTKLLEEIIPGA | Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits. | Q8TXZ3 |
C6DH15 | RNFC_PECCP | Rnf electron transport complex subunit C | Pectobacterium | MLKLFSAFKKDRIWDFDGGIHPPEMKTQSSRTPLRQIPLPEQFIIPLKQHLGPEGEICVSVGDKVLRGQPLTRGRGRTLPVHAPTSGTVNAIRQHTTAHPSGLSELSIIIVPDGEDRWSDRQTLADYQTQSTDTLLAHLHQAGIAGLGGAGFPTAAKLQGGMRGIETLIINGAECEPYITADDRLMQECADEIIQGVEILSFLLQPKRILIGIEDNKPEAISALRLALGKRSDMQLRVIPTKYPSGGAKQLTKILTGKEVPFGKHSAAIGVLMQNVGTAFAIKRAVIDGEPLTERVVTLTGEALRQPGNVWARLGTPVRH... | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | C6DH15 |
P82282 | BMNH1_BOMVA | Bombinin-H1/H3 | Bombina | IIGPVLGMVGSALGGLLKKIG | Has antimicrobial and hemolytic activities. | P82282 |
Q1CTX0 | ACCA_HELPH | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Helicobacter | MAIYLDFENHIKEIQNEIELALIRGDEDAKEILEKRLDKEVKSIYSNLTDFQKLQLARHPDRPYAMDYIDLILKDKYEVFGDRHYNDDKAIVCFIGKIDNVPVVVIGEEKGRGTKNKLLRNFGMPNPCGYRKALKMAKFAEKFNLPILMLVDTAGAYPGIGAEERGQSEAIAKNLQEFASLKVPTISVIIGEGGSGGALAIAVADKLAMMEYSIFSVISPEGCAAILWDDPSKTEVAIKAMKITPRDLKEAGLIDDIILEPSKGAHRDKFSAANTIKEYFLDALRTIQQDPHFLENRYQKLMSLGSFVESMN | 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. | Q1CTX0 |
Q8DHK2 | THIE_THEVB | Thiamine-phosphate pyrophosphorylase | Thermosynechococcus | MQNLAPASEGQRLRRILDANLDRAREGLRVIEEWCRFGREDAALSAECKDLRQTLGRYHTEELRAARQTDQDPGTALSHPQERDRPTLNAVLTANFARVQEALRVIEEYGKLTDTELSETAKALRYRVYILEQALTLNPLQARLRQLQGAKLYLVTAPSDRLLEIVEAALKGGLPLVQYRDKTSDDHTRLTTARQLQALCQRYGALFLVNDRVDIALGANADGVHLGQMDIPMELARQILGRDRLVGRSTTNAQELERAIAEGADYVGVGPIFATPTKPGKAAVGFDYLQYARKHAPMPQFAIGGIDLSNIEEVIKAGAT... | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | Q8DHK2 |
Q9C9K5 | PILS3_ARATH | Auxin efflux carrier-like protein 3 | Arabidopsis | MVKLLELFITSSKPVVEILLITSVGFYMALDGVNLLGHDARKYLNNIVFYVFSPSLIGSRLADSVTYESLVKMWFMPVNVLLTFIIGSLLGWIVIVITKPPSHLRGLILGCCAAGNLGNMPLIIIPAVCKEKGGPFGDPESCQKYGMGYVALSMAMGSIYIWTYVYNLMRVLSNSPVETPPSVESNYDSYKVPLISSKEEENNQKAGRWEKVKRRLVSLSQKVNLKTIFAPSTIAAMIALVIGLITPLRKLIIGTEAPLRVLQDSVTLVGDGAVPAMTMIIGGNLLKGLRSSGMKMSSIIGVLVARYVLLPMSGVLIVRG... | Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling. | Q9C9K5 |
Q5HC01 | RNH2_EHRRW | Ribonuclease HII | Ehrlichia | MPDFSIENEILKLKNNKECIIVGVDEVGYGSLAGPVVSAAVFFPNYNNETTQDINDSKKLTPKTRQKIYNKIITRVKWSIGFAHIFEIDEYNILNATHIAMKRALTGLNAHIDIDYVIIDGNKIPNIPWNAQAIIGGDTISTSIAAASIIAKVTRDRLMETLHIQYPQYNWNKNKGYGTKDHITSLYKYGKTIHHRNTFTPISKISYMFKNS | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q5HC01 |
A1AVF0 | ORN_RUTMC | Oligoribonuclease | Candidatus Ruthia | MNKKTNLIWIDLEMTGLIPEKDVIIEIATIVTNVQLHIIAQGPSLVIHQNDEILSNMDQWNTEHHTSSGLLRRVRESSLSCKQAEAQTLEFLKKYVHTGASPMCGNTICQDRRFLYNYMPTLERFFHYRHIDVSTLKELVIRWKPNAKMIFEKDSAHLALSDIQDSIDELKHYRNVFINV | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | A1AVF0 |
C6KYS2 | SYMPP_STHOU | Symplectin | Sthenoteuthis | YVRPVSSWKVAVFEHQVIPPKTDMETREEALDALKLNSDVYHEAVLESRSKGVKMIVFPEYGLYDINTLTRTRMDLMAEKVPHPKHGHRNPCDEPEYQTQSSEMLRTFSCMAKENDMYMVVNMAGREPCRRATEPECPGDKQLLYNTNVAFNNEGDVVARYYKTHLFWEEGWFNSSKNYEMALWDTPIGKFGTFMCFDFQAVQLIEQYNVRHIAYPASWVNLPPIYQSIQSHSAFARFAKINLLAASVHRLETSTYGSGIYSPNGAEIFYFRPDIPKSKLLVAEILPIHVKKPEQTVVNFDNPVFPSEDDDVQDLFDRGD... | Monovalent ion-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of monovalent ion trigger the intramolecular oxidation of the chromophore, didehydrocoelenterazine, with the emission of light. | C6KYS2 |
P18004 | TRAC_ECOLI | Protein TraC | Escherichia | MNNPLEAVTQAVNSLVTALKLPDESAKANEVLGEMSFPQFSRLLPYRDYNQESGLFMNDTTMGFMLEAIPINGANESIVEALDHMLRTKLPRGIPLCIHLMSSQLVGDRIEYGLREFSWSGEQAERFNAITRAYYMKAAATQFPLPEGMNLPLTLRHYRVFISYCSPSKKKSRADILEMENLVKIIRASLQGASITTQTVDAQAFIDIVGEMINHNPDSLYPKRRQLDPYSDLNYQCVEDSFDLKVRADYLTLGLRENGRNSTARILNFHLARNPEIAFLWNMADNYSNLLNPELSISCPFILTLTLVVEDQVKTHSEAN... | Required for the assembly of mature F-pilin subunits into extended F pili. | P18004 |
A7FNV6 | FEOC_YERP3 | Probable [Fe-S]-dependent transcriptional repressor | Yersinia | MASLLQLRDAIALNGSAEASQLSRQLAIPLPLVNAMLEKLTAMGKIERIELDHSGCLTGSCKSCPEGHQHCNTVIYQLKEPHAHQ | May function as a transcriptional regulator that controls feoABC expression. | A7FNV6 |
A1U0X1 | ACCD_MARN8 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Marinobacter | MSNWLDKIMPSKIRSESRQRTGVPEGLWKKCPKCGAFLYKPELEKNLDVCPKCNHHLRVSARRRLDIFLDKDGREELAAHLEPSDRLKFKDSKRYKDRLAAAQKSTGEKDALIAMRGTTMGVPLVACAFEFNFLGGSMGQVVGEKFVQAANVALEHRIPLVCFSASGGARMQEAILSLMQMAKTAAVLEKLKQEGIPYISVMTDPVFGGVSASLAMLGDLNIAEPYALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMILHRHQMRERIAHLLAKFTAQEKPGTEAPIEFEVTEKPDVDEPEGQ | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | A1U0X1 |
B1ZJ23 | KDSB_METPB | CMP-2-keto-3-deoxyoctulosonic acid synthase | Methylorubrum | MSDPLILIPARLAATRLPSKPLADIAGEPMIVHVWRRAVEAGIGPVVVATDTDAIAAAIEAQGGLAVMTQPDHPSGSDRLAEALEIVDPDGNHDVVVNVQGDLPTIDPAIIAASVTPLADPQVDIATLCAVIHRPEEMDDPNVVKIIGHTVGPNRLRALAFTRARAPWGEGPLFHHIGLYAYRRKALARFVALPQGELERREKLEQLRALEAGMRIDAMIVEDLPLGVDTPADLERARTLLAIRRLN | Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | B1ZJ23 |
O79210 | CYB_OCEFU | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Oceanodroma | MAPNPRKSHPLLKMINNSLIDLPTPPNISAWWNFGSLLALCLMTQILTGLLLAMHYTADTTLAFSSVAHTCRNVQYGWLIRNMHANGASFFFICIYMHIGRGFYYGSYLHKETWNTGVLLLLTLMATAFVGYVLPWGQMSFWGATVITNMFSAIPYIGQTIVEWAWGGFSVDNPTLTRFFALHFLLPFMIAGLTLIHLTFLHESGSNNPLGIVSNCDKIPFHPYYSLKDILGLALLLLPLTTMALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLSPLLHKSKQRTMAFRP... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | O79210 |
Q1LS04 | GLMU_CUPMC | Glucosamine-1-phosphate N-acetyltransferase | Cupriavidus | MNIVILAAGMGKRMNSALPKVLHPVAGQPMLSHVLDTARTLSPSRLVVVVGHGAELVRKAVGADDVAFAEQAQQLGTGHAVMQALPLLDDSQPTLVLYGDVPLTSVDTLKGLVQAAGAERLGVLTVEMPDPTGYGRIVRDAAGNIVRIVEQKDASEDVRAIREINTGIIVCPTAHLRQWLATLRNDNSQGEYYLTDTIERAVNDGVEVVSAQPAALWETLGVNSKVQLAEIERIHQRNIAQRLLEAGVTLLDPARIDVRGELTCGRDVTIDVGCVFEGRVHLEDGVSVGAHCVVRNTTIGAGARIQPFCHFEDAKVGPDG... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | Q1LS04 |
Q95EA5 | MATK_BROHE | Intron maturase | Browningia | MEEFQRYIELDRSWQHNFFYPLIFQEYIYGFAYDHGLNKSILLENAGDKKYSLLIVKRLINRMYQQTHLIISANHSNQNDFFGHKHKKNLYYQIISEGFAVIVEIPFSLLLISSLEAKEKKIVKSHNLRSIHSIFPFFEDKFLHLNYVLEILIPYPIHLEILVQTLRYWVKDASSLHLLRFFLYEYRNWNSLITPQKSISIFSNQRLFLFLYNFYVCEYESIFVFLCNQSSHLRSTSFGALLERNYFYGKLEYLVKVKTNTKDFCVILWLFKDPFLHYVRYRGKSILASKGTSLLMHKWKYYLFNFWQCHFSLWSPPRRI... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q95EA5 |
Q9HVW9 | HISX_PSEAE | Histidinol dehydrogenase | Pseudomonas | MTAPFAIRRLNAADPDFGRHLDHLLSWESVSDDSVNQRVLDIIAAVRSRGDAAVVEFTQRFDGLQAASMADLILPRERLELALTRITVAQREALEVAAERVRSYHEKQKQGSWRYTEADGTVLGQQVTPLDRAGLYVPGGKASYPSSVLMNAIPAKVAGVSEVVMVVPTPRGEINEIVLAAACIAGVDRVFTIGGAQAVAALAYGTESVPRVDKIVGPGNIYVATAKRHVFGQVGIDMIAGPSEILVVCDGQTDPDWIAMDLFSQAEHDEDAQSILVSPDAAFLDRVADSIARLLPTMERAEIIRTSLEGRGALIQVADQ... | Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. | Q9HVW9 |
A0A0D9S1R0 | APOE_CHLSB | Apolipoprotein E | Chlorocebus | MKVLWAALLVTFLAGCQAAADAPIKVEQPVEPETEPELRPQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPS... | APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amp... | A0A0D9S1R0 |
Q96HA1 | P121A_HUMAN | Pore membrane protein of 121 kDa | Homo | MSPAAAAAGAGERRRPIASVRDGRGRGCGGPARAVLLGLSLVGLLLYLVPAAAALAWLTVGATAAWWGLSREPRGSRPLSSFVRKARHRRPLSSFVRKARHRRTLFASPLAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAAAPEGQDLRDRPGRRPPARPAPRSPPPRSPPPRSPPPSPPTHRAHHVYPSLPTPLLRPSRRPSPRDCGTLPNRFVITPRRRYPIHQAQYSCLGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKE... | Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). | Q96HA1 |
D5DNA8 | GPMI_PRIM3 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Priestia | MSKKPVALIILDGFALRDEDKGNAVTHAKKPNFDRFWNEYPHATLQASGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVNVAIREGEFEQNETLLAAVKHAKEKGTNLHLFGLLSDGGVHSHIEHLYALLRLAKSEGLEKVYIHGFLDGRDVAPQSAETYLKELNEKIEEYGVGEIATLSGRYYSMDRDKRWERVEKSYRAMVYGEGPSYTSAEECVKDSYENGIYDEFVLPSVITKEDGSPVATIQDEDAVIFYNFRPDRAIQISNTFANEDFRSFDRGEKHPKNLHFVCLTHFSETVDGYVAFKPNNLDNTLGEV... | Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | D5DNA8 |
Q7P1G2 | GLPK_CHRVO | Glycerokinase | Chromobacterium | MTDQYVLALDQGTTSSRAILFNRSGDIVSLAQKEFRQIYPQPGWVEHDPQEIWGGQVGVAAEAVAKAGIDGRSIAAIGITNQRETTIVWDRETGQPVYNAIVWQDRRTAEFCDELKARGLGELIRSKTGLLVDAYFSGSKIKWILDNVPGARDRAREGKLAFGTVDSWLIWNFTHGKVHVTDVSNASRTMLYNIHTLQWDAELLDIMGIPASMLPEVKSSSEVYGHTHAAHLGVEIPIAGVAGDQQAALFGQQCTTPGMVKNTYGTGCFMMLNTGDKPIESSNNLLTTIAWKVDGKVQYALEGSIFIGGAVVKWLRDGLG... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | Q7P1G2 |
A8LWI0 | FOLD1_SALAI | Methenyltetrahydrofolate cyclohydrolase | Salinispora | MTATLMDGRTLSRQLLESTAERVTGFHRSHGRRPCLATVLVGEDPASHTYVRIKVNRCTEVGIDSRRFDLPTLTTTEQLVRVLRDLSSDSAVDGILLQHPTPPQIDEHAAFEAIDPSKDVDGVTGTSFAAMAFGYRGFASCTPAAIMRLLDAYDVPLSGQRAVVVGRSAILGKPIGMLLLARDATVTYCHSRTTDLAAHVAEADLVVAAVGVPHLVRGEWIKPGAVVVDAGYNAGNVGDVQAATAANRASLITPVPGGVGPMTIAVLLAQTVDAAERHG | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | A8LWI0 |
D3RNJ4 | CYSH_ALLVD | Thioredoxin-dependent 5'-adenylylsulfate reductase | Allochromatium | MTERRQPSLSTDTLPTREAAAIELLSQVCRELDSIVFATSLGAEDMVLTEIIRRERLPIRIFTLDTGRLPTETLELIEVVERHYGTRIERYAPHPDAIADYVSRYGLDGFYDSVPARQACCRVRKLEPLKRALAGQSAWVTGLRAEQSVTRAELPAREWDAANGLEKINPLADWSEHEVWAFIRHHRVPYNPLHNQGYPSIGCAPCTRAITVGEDVRAGRWWWENPETKECGLHRREFAPRQPSAHPAIERDRSAA | Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor. | D3RNJ4 |
Q5L3X5 | Y018_GEOKA | Nucleoid-associated protein GK0018 | Geobacillus thermoleovorans group | MMRGGMGNMQKMLKQMQKMQKEMQKAQEELAEKTVEGTAGGGMVTVVANGHKQILEVKIKEEVVDPDDIEMLQDLILAATNDALKKADELANEMMGQFTKGLNIPGLF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q5L3X5 |
A7FY07 | DTD_CLOB1 | Gly-tRNA(Ala) deacylase | Clostridium | MRAVVQRVISSKVEVDGRVIGSIGKGLNVLLGISKEDTEEDIKYLKEKIINLRIFEDENEKLNKSLLDIGGDIIIVSQFTLYGDCRKGRRPSFIEALGGEEAYILYNKFVESIKKEVNNVATGEFGADMKVYIENDGPVTILLDSKKTF | 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... | A7FY07 |
A8ALD3 | CLCA_CITK8 | H(+)/Cl(-) exchange transporter ClcA | Citrobacter | MNTDTPTFEAQQVVRLRRGDLIRRLLQRDKTPLAILLTAAVVGTVTGLIGVAFEKAVTWVQNLRIGALVQTADYAILVWPLAFILSALLAMVGYFLVRKFAPEAGGSGIPEIEGALEELRPVRWWRVLPVKFVGGMGTLGAGMVLGREGPTVQIGGNIGRMVLDLFRMRSAEARHTLLATGAAAGLSAAFNAPLAGILFIIEEMRPQFRYNLISIKAVFTGVIMSSIVFRIFNGEAPIIEVGKLSNAPVNTLWLYLILGMIFGCVGPLFNHLVLRTQDMFQRFHGGEIKKWVLMGGAIGGLCGILGLIEPEAAGGGFNLI... | Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. | A8ALD3 |
Q5N667 | ILVC_SYNP6 | Ketol-acid reductoisomerase type I | Synechococcus | MARMYYDADANLDLLNGKTVAIIGYGSQGHAHALNLRDSGVNVVVGLYPGSKSAAKAEAEGPKVLPVAEAAQAADWIMILLPDEFQKSVFENEIRPALSAGKVLAFAHGFNIHFAQIVPPADVDVVMIAPKSPGHLVRRTYEQGQGVPCLFAIYQDASGQARDRAMAYAKGIGGTRAGILETSFREETETDLFGEQAVLCGGLSALIKAGFETLVEAGYQPELAYFECLHEVKLIVDLIVEGGLAAMRDSISNTAEYGDYVTGPRLITEETKAEMKRVLADIQQGRFALDFVQECGAGKPVMTATRRLEAEHPIESVGKD... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q5N667 |
P01509 | CECB_ANTPE | Cecropin-B | Antheraea | KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAKAL | Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. | P01509 |
Q02328 | SLAP2_CAEEL | Actin-binding protein SLA2 homolog | Caenorhabditis | MDHRAQAREVFVRAQLEAVQKAITKNEVPLKPKHARTIIVGTHKEKSSGIFWHTVGRIQLEKHPVLTWKFCHLVHKLLRDGHRKVPEETYRYVNRFTQLSQFWKHLNTSGYGPCIESYCKLLHDRVTFHNKYPVVPGKLDLNDSQLKTLEGDLDNMFEMTIDMLDQMDALLVLQDRVYEMMNSLRWNSLIPQGQCMLSPLIIAILDTSKFYDYLVKMIFKLHSQVPPDALEGHRSRFRTIFERTKKFYEESSNLQYFKYLVSIPTLPSHAPNFLQQSDLESYRTPHAYLHSEGSEDGTSLNGHDGELLNLAEAEPQQASP... | Regulates pre-synaptic vesicle recycling at neuromuscular junctions of mechanosensory neurons. Plays a role in maintaining a normal defecation cycle. | Q02328 |
Q9FRG8 | GRF9_ORYSJ | Transcription activator GRF9 | Oryza sativa | MFADFSAAAMELGEVLGLQGLTVPSTKEGDLSLIKRAAAGSFTQAAAASYPSPFLDEQKMLRFAKAAHTLPSGLDFGRENEQRFLLSRTKRPFTPSQWMELEHQALIYKYLNAKAPIPSSLLISISKSFRSSANRMSWRPLYQGFPNADSDPEPGRCRRTDGKKWRCSKEAMADHKYCERHINRNRHRSRKPVENQSRKTVKETPCAGSLPSSVGQGSFKKAKVNEMKPRSISYWTDSLNRTMANKEKGNKAAEENNGPLLNLTNQQPTLSLFSQLKQQNKPEKFNTAGDSESISSNTMLKPWESSNQQNNKSIPFTKMH... | Transcription activator that plays a regulatory role in gibberellin-induced stem elongation. | Q9FRG8 |
Q8XXF4 | IXTPA_RALSO | Nucleoside-triphosphate pyrophosphatase | Ralstonia | MRRIVLASNNPGKLAEFNALLAPLGLDVAPQGELGIPEAEEPHATFVENALAKARHASRLAGLPALADDSGICAHALGGAPGVYSARYAQLAGGPKSDAANNARLVRELAGHADRGAHYVCVLVYVRHADDPQPIIAEGSWFGEVIDAPRGDGGFGYDPHFLLPALGKTAAELSKAEKNAVSHRAQALAQLVERLRLFENA | Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical p... | Q8XXF4 |
P10982 | ACT1_ABSGL | Actin-1 | Absidia | MSMEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKSNREKMTQIMFETFNAPAFYVSIQA | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | P10982 |
A7H9V5 | NUOD2_ANADF | NDH-1 subunit D 2 | unclassified Anaeromyxobacter | MNDHKGLGGLDTEATPGSFGAGEPPRALGQAGLAAENELDAPLASKLMTVNLGPSHPAMHGVTRAVVELDGEMIRSMKLDIGFLHRGFEKSCENVTWTQCFPYTDRLNYVSSIMNNVGFALAVEKLCKLDVPERAKYLRVVTSEIHRICDHLTLVGAMAMELGAMTVFLYAIEARDIIYDRLAELCGARLTSNYGRIGGVARDTPDGWIEKTEKTLDRVKGYVDEIDQLVSRNRIFIDRTRGTGVVPRADAIELGFTGPCLRASGEPYDLRKAAPYLVYDRIDFDIPVGTNGDNFDRFQMRMEEMRQSDRIIRQCFAQME... | 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... | A7H9V5 |
P9WGB6 | METB_MYCTO | O-succinylhomoserine (thiol)-lyase | Mycobacterium tuberculosis complex | MSEDRTGHQGISGPATRAIHAGYRPDPATGAVNVPIYASSTFAQDGVGGLRGGFEYARTGNPTRAALEASLAAVEEGAFARAFSSGMAATDCALRAMLRPGDHVVIPDDAYGGTFRLIDKVFTRWDVQYTPVRLADLDAVGAAITPRTRLIWVETPTNPLLSIADITAIAELGTDRSAKVLVDNTFASPALQQPLRLGADVVLHSTTKYIGGHSDVVGGALVTNDEELDEEFAFLQNGAGAVPGPFDAYLTMRGLKTLVLRMQRHSENACAVAEFLADHPSVSSVLYPGLPSHPGHEIAARQMRGFGGMVSVRMRAGRRA... | Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. | P9WGB6 |
Q06FX0 | RPOC1_PELHO | Plastid-encoded RNA polymerase subunit beta' | Pelargonium | MIDKYQEPKHHQLRIGLVSPQQIMAWANKTLPTGEIVGEVKNYRTFSYDRDSETYKPERDGLFCERIFGPIKSGVCACGESRKIGDEKEKRTFCEKCGVEFVDSRIRRYQMGYIKLASPMAHVWYLKRIPSYIANLLDEKIKDLENLVYRDFIFAGPLTKKPTLLRLRGSFPESKTKFSGSRDILSQFLKTKSFQKLRDREFSAGAGAIRKRLANLDLEVIIYSSLAEWKKRKEQKAEIEIKPTRTERTEEEDRKIEKIKRRMRVLVRRMELAKHFLETNVKPEWMILRLLPVLPPELRPIFKISEVQFISSDLNTLYKE... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q06FX0 |
Q9A8I5 | PLSX_CAUVC | Phosphate-acyl-ACP acyltransferase | Caulobacter | MSQSLVISVDAMGGDHGPSIVVPGIAQALQALPGVRFLLHGDGAAIEAELAKHPGAKAVSEVRHCDKAIGMDEKPAQAMRRGKGSSMWNAVEAVRENEAQACVSAGNTGALMAISKLILRMGAELERPAIVANWPTMKGVTTVLDVGANVESDASQLVEFAIMGAAFHHAVHGSKRPTVGLLNVGSEDQKGHEEVREAHAILRETTLDFDYHGFVEGNDIAYGTVDVVVTDGFTGNVALKTAEGLARFFSNEIKSTLTSGPLAMLGALIASGALKKMRHRLDPSRVNGAPLLGLNGIVVKSHGGADANGFASAIRVATNL... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q9A8I5 |
Q8Z699 | ISPE_SALTI | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Salmonella | MMTHWPSPAKLNLFLYITGQRADGYHTLQTLFQFLDYGDTLHIEPRHDGEIHLLTPVTGVENEDNLIVRAARLLMKVASESGRLPAGSGADISIEKRLPMGGGLGGGSSNAATVLVALNHLWQCGLSIDELATLGLTLGADVPVFVRGHAAFAEGVGEILTPVNPPEKWYLVAHPGVSIPTPVIFKDPQLPRNTPKRSIDTLLKCEFSNDCEVIARKRFREVDAALSWLLEYAPSRLTGTGACVFAEFDTESCARQVLEQAPEWLNAFVAKGVNLSPLHRELL | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q8Z699 |
Q3SH96 | TYSY_THIDA | Thymidylate synthase | Thiobacillus | MKPYLDLMRHVLEHGTRKDDRTGTGTLSVFGWQTRYDLAAGFPLVTTKKCHLRSIVHELLWFLQGDTNIRYLKENGVSIWDEWADENGDLGPVYGHQWRSWPKADGGVIDQIAEAVKTLRTNPDSRRIIVSAWNVADLDRMALAPCHAFFQFYVAEGRLSCQLYQRSADIFLGVPFNIASYALLTLMMAQVTGLKPGDFVHTLGDAHLYVNHLEQAREQLSREPRPLPTMTLNPDVTDIFGFRFEDFTLGGYDPHPAIKAPVAV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracell... | Q3SH96 |
Q8FFM1 | ARNA_ECOL6 | UDP-glucuronic acid dehydrogenase | Escherichia | MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPDNVNHPLWVERIAQLSPEVIFSFYYRHLICDEILQLAPRGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQLRVAIAPDDIAITLHHKLCHAARQLLEQTLPAIKHGNILEIAQRENEATCFGRRTPDDSFLEWHKSASVLHNMVRAVADPWPGAFSYVGNQKFTVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQGSRLNSQPACAARRRTRVLI... | Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A an... | Q8FFM1 |
B2J711 | EFP_NOSP7 | Elongation factor P | Nostoc | MISSNDFRPGVSIVLDGSVWRVLEFLHVKPGKGSAFVRTKLKNVQSGSVMEKTFRAGETVPQATLEKSTMQHTYKEGDEFVFMDMETYEEGRLTRTQIGDRVKYLKEGMEAEVIKWGDQVLGVELPKSVVLEIVQTDPGLKGDTATGGSKPATLETGAIVMVPLFISQGERIKVDTQEDKYISRE | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | B2J711 |
A8Z681 | RL6_SULMW | 50S ribosomal protein L6 | Candidatus Sulcia | MSRIGNIPVLIPNNVFVKKQDNIIYINGPLGKLNQKIIGDINIIINNNNIIVKRKHNDKKNRALHGLYRMLIYNMIKGVYNGFKKKLELIGVGFRAKNNSNILDLNIGYSHNIIIKLPKSITLEVKMEKNKNTQIILKSYDKQLLGIVAAKIRSLRKPEPYKGKGIRYINEYVIKKTGKSAK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | A8Z681 |
Q6K2E1 | UGE4_ORYSJ | UDP-galactose 4-epimerase 4 | Oryza sativa | MAGGEVVAVAAAAAGTSRTVLVTGGAGYIGSHTVLQLLAAGFRVVVADSLGNSSELAVRRVAALAGDKARNLSLHKVDIRDKGGLEKVFSSTRFDAVVHFAGLKAVGESVQKPLLYYDHNVAGTIILLEVMAAHGCKKLVFSSSAAVYGSPKNSPCTEEFPLTPHNPYGRTKLIAEEICRDIYHSDSEWSIILLRYFNPVGAHPSGYLGEDPCGIPNNLMPFVQQVAVGRRPSLTIFGNDYATKDGTGVRDYIHVVDLAEGHIAALRKLFESSIGCQAYNLGTGKGTSVLEIVNAFEKVSGKKIPLVIGPRRPGDAEILF... | Catalyzes the interconversion between UDP-glucose and UDP-galactose. | Q6K2E1 |
Q568F6 | PURA2_DANRE | IMP--aspartate ligase 2 | Danio | MSDSGDAQPQDGGNSSSSRGKSPSVGNRVTVVLGAQWGDEGKGKVVDLLAQDADMVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPKVTAFIGNGVVIHLPGLFEEAEKNVRKGKGLEGWESRLIISDRAHIVFDFHQAVDGVQEQERQQQAGKNLGTTKKGIGPVYSAKAARSGLRICDLLADFQEFSERFKHLASQYKSMYPSLEIDVDGELEKLKSYVDRIKPMVRDGVFFMYEALHGDPKRILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQSNETGELL... | Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q568F6 |
Q9I5Q3 | SYY2_PSEAE | Tyrosyl-tRNA synthetase 2 | Pseudomonas | MKSVEEQLALIQRGADEILVEAELVAKLKRGQPLRIKAGFDPTAPDLHLGHTVLINKLRQFQDLGHQVIFLIGDFTGMIGDPSGKSVTRPPLTREQVLENAETYKSQVFKILDPAKTEVAFNSTWMDQLTPADFIRLASQYTVARMLERDDFSKRYASNQPIAIHEFLYPLVQGYDSVALKADVELGGTDQKFNLLMGRELQRAYGQEAQVILTMPLLEGLDGVKKMSKSLGNYIGIQEAPGVMYSKLVSIPDTLMWRYFELLSFRSLDEIDSFRKDVEAGANPRDIKIKLAEEIVARFHGEEAAASAHKSAGNRLKEGE... | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | Q9I5Q3 |
Q46Z22 | ACPS_CUPPJ | 4'-phosphopantetheinyl transferase AcpS | Cupriavidus | MIYGVGTDIIEIARVQGVMERTRGRFAEKVLGADELAKYHARKARSERRGLAFLATRFAAKEAFSKAIGLGMRWPMTWRAMELMNLPSGEPTPICHGELAQWIAERGITVRVSVSDERDYAVAFAIAERGGHAAVPENPA | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | Q46Z22 |
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