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 |
|---|---|---|---|---|---|---|
Q981X2 | DADA3_RHILO | D-amino acid dehydrogenase 3 | Mesorhizobium | MPKIVVIGAGIAGVSTAYALLEQGYDVTVVERRRYAAMETSFANGGQLSASNAEVWNHWSTVLKGIKWMLRRDAPLLMNPTPSWHKYSWLLEFVSNISRYRENTIETTRLAIAARKHLFEIADREGIDFDHVRRGILHVYWDKDGFDHALKVNEMLNEGGLDRRSVTPSEFAGIEPALHGKFYGGFYTPSDSTGDIHKYCAGLEKACTKRGAQFIYDAAVTRIERRDRFNIVCATDGADQTLVADGIVVCAGTNSRDIAAMFGDRINIYPVKGYSITVELDGAAADSSAPWVSILDDRAKIVTSRLGAARLRVAGTAEFNGVNFDIREDRIRPLVDWTRMMFPKVATEHVVPWAGLRPMMPNMMPRVGKSRVPGVFYNTGHGHLGWTLSAATSAMLATVVATDLPIDARLAA | Oxidative deamination of D-amino acids. | Q981X2 |
Q75D04 | YEL1_ASHGO | Guanine-nucleotide exchange factor YEL1 | Eremothecium | MRSNHLFFRKVMTRLEVHPLNNSRLFCISDSSSTSLYSEPSKGSTIFAQQALDRFDWDLSIGETAFENMTDDAKMRNDPGMLVGPDGMLITPELLIASPGKIDVFDCASLDDTAGALEGMSLASGEGSNCMQAMRPRSETRSTNTTTSRSVAKQILRNTYGPVRYKDYANYLGSPENREVLREFIALLQPLPVSLLFSLRKLSKSIYFIAEAGAIDAMLEEMSIQWVERHKPLHYQDNYKLVHIVLFSLLILNSDLYNDMAQMKFTSAQFVDNTVYALLRESPTIDKQSFEAELRVYYDLLAMDQLPLHKPPITASHSRDSANPTKKSSVFYSRGHRMERTYSNSSTYSMSTISLQRTTTAIAAKQTAAVASWRFHNFSDLPLIYCKEPFDDEMNNTNDSSWLMDHIIQFQEPLGSVSRAAAASMVSPTAQPRRKLFNWLKKGQPDSIFKSHHEFGSAEGKWYNARVRISEGRLYIFNFKNQPALDPKTADLELCRRRAASYTVQNLFGAMATFVQDNIVYKSNSQTTWNFAITFPKTIDCETERTYQFQTSNMTMAQRFVQAATFWSARITPLPSAQFEMVSNQEYGWGEKLLSRQVAATDVRLTDWMPLIGIDSIYDEIEDSGDLTVDSQLQNLRVFTEHLTQLLDQHNSYKPKMVEIWTQNPSTQQFEMAMENWNRRYLYLNSMYEKHYTYLRALETAFETVTG | Guanine nucleotide exchange factor for ARF3 required for localization of ARF3 to the bud neck and tip and involved in actin patch polarization. | Q75D04 |
A6VJ39 | COFD_METM7 | 2-phospho-L-lactate transferase | Methanococcus | MKITILSGGTGTPKLIQGFKEILPNEDISVIVNTGEDTYIGDIYLSPDIDTVLYTFSDLINDETWYGLKGDTFFCHEQLKNFGFDEVLKIGDKDRALKMHKASSLKNGVKMSEIVDIERKSLLINSKIYPMSNEKVESKVLIEENNEKILLKFHDFWIFRKGNAKVLDIFYENSNYAKAANGVLKAIHESDFVLIGPSNPITSIGPILSISEIKNALKEKLVFAVSPIVGENPVSGPAGTLMNAKGYPVSAVGVYEYYKDIVDVLVLDNSDINKKKDINCEVLYANTIMKTIDDKINLARNILDYYKSR | Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP. | A6VJ39 |
A1VD51 | COXX_DESVV | Heme O synthase | Desulfovibrio | MGRCTIADVAMLIRWRVSLMVAGATFFGAMLAVPHVTITHLLASLATFLLAGGCSAINQVQEADLDAVIPRTASRPIPCGRIGHMYGSLMGLALVTVGWMVLCLAGGLTSLLVGIGIVAVYNGLYTPLKRRTSFALLVGAAAGAMPPVVGWLAVGGHPASPMLVVVYTLYLLWQIPHFWLHAARDREAYRKARLPLPLLSLPHERYARLLKVWFHAYAVAVLMVPAFPLLEGVGMRIMVTLCGIALLFAAMLAVRKRRVALHIADAVLCAVMVVLLIDRLAIPVSLF | Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | A1VD51 |
Q1GK18 | RL24_RUEST | 50S ribosomal protein L24 | unclassified Ruegeria | MAAKLRKGDKVVVLAGRDKGKEGTIASVDPKAGKAVVDGVNMAIRHTRQTQTSQGGRLPKALPIDLSNLALLDSNGKATRVGFREEDGKKVRFAKTTGETV | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | Q1GK18 |
B0U009 | FOLD_FRAP2 | Methenyltetrahydrofolate cyclohydrolase | Francisella | MTLIDGKKLSIDLKERLTDQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEATTEQELLELIDKLNDDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANVGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAHAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVGDVDFEAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | B0U009 |
C5J411 | XYNC_ASPNG | 1,4-beta-D-xylan xylanohydrolase C | Aspergillus subgen. Circumdati | MVQIKVAALAMLFASQVLSEPIDPRQASVSIDTKFKAHGKKYLGNIGDQYTLTKNSKTPAIIKADFGALTPENSMKWDATEPSRGQFSFSGSDYLVNFAQSNNKLIRGHTLVWHSQLPSWVQSITDKNTLIEVMKNHITTVMQHYKGKIYAWDVVNEIFNEDGSLRDSVFYKVIGEDYVRIAFETARAADPNAKLYINDYNLDSASYSKLTGMVSHVKKWIAAGIPIDGIGSQTHLSAGGGAGISGALNALAGAGTKEIAVTELDIAGASSTDYVEVVEACLNQPKCIGITVWGVADPDSWRSSSTPLLFDSNYNPKPAYDAIANAL | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. | C5J411 |
Q32ZH6 | DFB15_RAT | Defensin, beta 15 | Rattus | MKTFLFLFAVFFFLDPAKNAFFDEKCSRINGRCTESCLKNEELIALCQKNLKCCVTVQPCGRDKGDELDEDSGYNRTRG | Has antibacterial activity. | Q32ZH6 |
Q2T0K3 | KDSB_BURTA | CMP-2-keto-3-deoxyoctulosonic acid synthase | pseudomallei group | MTSPLPFVAVVPARLASTRLPNKPLADLGGKPMVVRVAERAREAGAQQVLVASDAQSVLDAVREHGFDAVLTRADHPSGTDRLAEVAAKLGFSDDTIVVNVQGDEPLIDPQLVCDVASHLAAHPSCAIATAAHPIHEAHEVFNPNYVKVVLDANGVALYFSRAPIPWSRDAYLPHWPNIAAMPAPTCPVYRHIGLYAYRARFLRTYPTLAQAPIEAAEQLEQLRAMWHGERIAVLVTEHAPEAGIDTPADLERVQALFRSRAK | Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | Q2T0K3 |
P37326 | INTS_ECOLI | Putative prophage CPS-53 integrase | Escherichia | MLTVKQIEAAKPKEKPYRLLDGNGLYLYVPVSGKKVWQLRYKIDGKEKILTVGKYPLMTLQEARDKAWTARKDISVGIDPVKAKKASSNNNSFSAIYKEWYEHKKQVWSVGYATELAKMFDDDILPIIGGLEIQDIEPMQLLEVIRRFEDRGAMERANKARRRCGEVFRYAIVTGRAKYNPAPDLADAMKGYRKKNFPFLPADQIPAFNKALATFSGSIVSLIATKVLRYTALRTKELRSMLWKNVDFENRIITIDASVMKGRKIHVVPMSDQVVELLTTLSSITKPVSEFVFAGRNDKKKPICENAVLLVIKQIGYEGLESGHGFRHEFSTIMNEHEWPADAIEVQLAHANGGSVRGIYNHAQYLDKRREMMQWWADWLDEKVE | Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. | P37326 |
B5FHV3 | PAT_SALDC | Putrescine--2-oxoglutaric acid transaminase | Salmonella | MNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLIAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV | Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. | B5FHV3 |
P07677 | ATPB_BACP3 | F-ATPase subunit beta | Bacillus | MTRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGQVTLGRVFNVLGEPIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDGLLFIDNIFRFTQAGSEVSALLGRMPSAIGYQPTLATEMGQLQERITSTAKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLVSTSRALAPEIVGEEHYQVARKVQQTLERYKELQDIIAILGMDELSDEDKLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILEGKYDHLPEDRFRLVGRIEEVVEKAKAMGVEV | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | P07677 |
Q9VVF7 | MIP_DROME | MIP-5 | Sophophora | MAHTKTRRTYGFLMVLLILGSACGNLVASGSAGSPPSNEPGGGGLSEQVVLDQLSESDLYGNNKRAWQSLQSSWGKRSSSGDVSDPDIYMTGHFVPLVITDGTNTIDWDTFERLASGQSAQQQQQQPLQQQSQSGEDFDDLAGEPDVEKRAWKSMNVAWGKRRQAQGWNKFRGAWGKREPTWNNLKGMWGKRDQWQKLHGGWGKRSQLPSN | Ligand for the sex peptide receptor (SPR) . Stabilizes sleep and maintains sleep homeostasis to inhibit the activity of wake-promoting circuits, such as those that involve the pigment dispersing factor (pdf) neurons. Regulated by the circadian clock network and pathways associated with a sleep homeostat . May also have a regulatory role in gut motility . | Q9VVF7 |
Q9P3A8 | CAND1_SCHPO | Cullin-associated and neddylation-dissociated protein 1 | Schizosaccharomyces | MEEGILLKKYVESSDKDIRYMALSDLAARLNDANHLKNLKLESFPDTLDVLLQALSDASPEVQQEAVRCVAIISSKIPQDKLKSTVENLLSGVAGKKSKNYLSALSLLLSNSNVQPFVNKFYTSTVFPSFLQILKQYNVAQEEFFAILCVVCDSLEIYHSNLSTLLPNNFELCIDVFQKCTTQCQRELIIKKACYLLSDVSLYGPRFAYKYIIEVLDRGLGPSTQMSEVNISIKLLNEILLSSKKEKDSSTSFISTAVADYTNKILSLLKKEEAPDELTQKLLEVLGLLLEYQQVNILKIWPELHGLLISKISYDPNLISDTNDEDDIADFLEEMSDYSSIYEDEEDVSWIVRRESLKVVLSVILSRLEYLPIVLQALGTSVVSKLNDREESVCLISIEVLKQAFLHVPRWIEVYATSNDRKRRYEGLPSDRSAISDTSIYLVSVIGKHVSKLSDKTPLSIVSELLNLVTVIFSSRDLGVQSEFSNLSSIIYRFPDFSTLDIKIKLNLVRLISAIISCGCEEIENMESKMSTILSLAVQNNYPQLSYEALITELSFCKYIHKKQPTNVSTDFSTMIDSSLQLLESKISDLKVRLALIDLVSQYVILFYEPDFDSIFLRRVLIILCKKLQEEPTRSAAARALCDIFMSVTDITKIENGTKIYEEILQDCCRHIDKSGNEFTTAYLELLEVLLKVGQKYLAESLLEHILGLLIETLKRNTENTVAILKCLLIIPLSILLKSKNLLIDTIISHLQSSTIHLNEESVCLLSRIIAVISKEEDLELIINSFTCAQKPVEEMVTLALIAAQLICIFQSKAIVTSLNKSFMSPKSEVRIKVFTTLIFGQLDYGKLTLPANEYFDTIASNLNSPNADVMKAAAIALGSLTSQSEKFIKELCALYVSDAYDKELLLISFLTFLKKSKIDYETADKIWDILSKDIENIKDFSTSPFRTLLSECLGLLICNESSSLYYKLELLSSSEASNHMLLSLSVFRFSLTLDCPKLKAYEKQFFEKAYKLFQNPDLEVSQETLQVIISVIKNRRSCIADVYNELLQGLISKSSVDSSNVHVVQMGPFQHVVDNSINQRQLVFETLYSLLDIPESLNHLTHFLQVSVMGLEDEHYIKLVSLSILEKLVDCSPSIIDEQVDTILEALRKIIELRKTEKTLKTDSDNILDLVRSALRVLFTMKLKCDNPVISEFESQVQKGPYSLEYEGIKNEIKTTIKT | Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor (Probable). | Q9P3A8 |
Q21IY3 | LEUC_SACD2 | Isopropylmalate isomerase | Saccharophagus | MGGKTLYDKLWDDHLVQQRDDGSALLYIDRHIVHEVTSPQAFEGLRLAKRKPWRVDSVVATPDHNVPTTQKERASGVEGIEDPTSRIQVQTLDSNCDELGILEFKINDARQGIVHVVGPETGACLPGMTIVCGDSHTSTNGALGALAMGIGTSEVEHVLATQCLVAKKMKSMLVKVDGKLGAGVTPKDVVLAIIGKIGTAGGTGYAIEFGGEVMRSMSMEGRLTVCNMAIEAGARAGMVAVDDITIDYVKGRSFAPKGEHWEQAVAAWRDLKSDDDAVFDAVVELRGEEILPQVSWGTSPEMVLPVDASIPDPELETDAVKQNGMRRALQYMGLKAGQAIKDIYVDRVFIGSCTNSRIEDIRAAAEVVKGRTKAASVKEAIVVPGSGAVKAQAEAEGLDKIFVEAGLEWREPGCSMCLAMNADKLGDGEHCASTSNRNFEGRQGYGGRTHLVSPAMAAAAAIAGHFVDVREF | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q21IY3 |
A4WSP1 | EFTS_CERS5 | Elongation factor Ts | Cereibacter | MAITAQMVKELRESTGAGMMDAKKALTETDGDMEAAVDWLRTKGLAKAAKKAGRTAAEGLVGVAVSGGTGVAVEVNSETDFVAKNADFQTMVTGFTQAALSVDDVEALKAADMGGKTVETTLQETIAVIGENMTLRRMAKISGDSVAAYVHNAAADGLGKIGVLVAVKGADNGIAKQIAMHIAATSPMALSEADLDPTLVERERAVQTQKALEENAASAKPKPDSVIENNIIPGRMKKFLEENTLLGQKFVINPDVTVAEAAKQAGVEILGFVRMAVGEGIEKEKEDFAAEVAKTLAG | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | A4WSP1 |
B0BUA7 | ERA_ACTPJ | GTPase Era | Actinobacillus | MTEQNQQPKTYCGFIAIVGRPNVGKSTLLNKILGQKISITSRKAQTTRHRIVGIHTEDQYQAIYVDTPGLHIEEKRAINRLMNRAASSAIGDVDLIIFVVEGTKWTDDDEMVLNKLRAAKAPVVLAINKVDNIKEKDELLPHITELSQKFDFAEILPISAQRGKNVHILQKIVRKSLREGVHHFPEEYVTDRSQRFMASEIIREKLMRFTGEELPYSVTVEIEQFKLNERGTYEINGLILVEREGQKKMVIGVKGQKIKTIGMEARADMERLFDNKVHLELWVKVKAGWADDERALRSLGYMDE | An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. | B0BUA7 |
A4YBY0 | RL2_SHEPC | 50S ribosomal protein L2 | Shewanella | MAVIKCKPTSPGRRHVVKVVNTDLHKGKPFAGLLAKKSKSGGRNNTGRITVRHVGGGHKQHYRLIDFKRDKDGIPAKIERLEYDPNRTANIALVLYADGERRYILAAKGMQAGDKIQSGVEAEIKTGNAMPLRNIPVGSVVHAVEMKPGKGAQIARSAGAYVQVVARDGAYATLRLRSGEMRKVPVDCRATFGEVGNAEHMLRQLGKAGAKRWRGIRPTVRGVAMNPVDHPHGGGEGRTSGGRHPVTPWGVPTKGYKTRSNKRTDKYIVRRRNK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | A4YBY0 |
B0TM11 | RL4_SHEHH | 50S ribosomal protein L4 | Shewanella | MELVLKDAQSALEVSEATFGRDFNEALVHQVVVAYAANARQGTRAQKTRAEVTGSGKKPWRQKGTGRARAGTVKGPIWRGGGVTFAAKTQDHSQKVNKKMYRGALKSIFSELVRQDRLIVVESFGVDAPKTKELKAKLDAMQLQDVLIVTPEVDENLFLAARNLYKVDVRDVAGVDPVSLIAFDKVLVTAEAIKQIEEMLG | Forms part of the polypeptide exit tunnel. | B0TM11 |
A2V7M9 | PGAP3_CRIGR | PER1-like domain-containing protein 1 | Cricetulus | MAERTARLLLLTVTVGLAWGSQGDREPVYRDCVLRCEERNCSGDALKHFRSLQPIYMSLAGWTCRDDCKYECMWITVGLYLQEGHRVPQFHGKWPFSRFLFIQEPASAVASLLNGLASLVMLCRYRASVPASSPMYHTCMAFAWVSLNAWFWSTVFHTRDTDLTEKMDYFCASAVILHSIYLCCVRTVGLQHPSVARAFGATLLLMLLLHTSYLSLVRFDYSYNMMANVAIGLVNLAWWLAWCLRNHRRLPHTRKCVAVVLLLQGLSLLELLDFPPLFWVLDAHAIWHISTIPVHVLFFRFLEDDSLYLLKESEAKFKLD | Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. | A2V7M9 |
Q929A9 | ADDA_LISIN | ATP-dependent helicase/nuclease AddA | Listeria | MRLNIPTKPEDALWTDDQWKAIQANGNNILVAAAAGSGKTAVLVTRIIEKLINETENLNVDELLIVTFTNVSAAEMKYRIGKSLEEALVQNPESVHLKKQVALLNYASISTLHSFCLEIIRKHYFEADIDPNFRLIEPIESSMIRDEVLEDLLEKEYSIENNEGFFHLVESFTGDRSDAELHTLISKLYDFSRANPNPDLWLEQMVSFYDTQAITSITELPYFPIIKEDIQLRINQAKSYLLTAIDYANENNGPAPYLSTLENDLAQINTLSSISWDNWQDVKFGFESIDFKRIPALKNKADFDEEYVEEAKKFRDAAKKEVKNVLIDWFSREEENYLSDLEKMKPDIKTLSELVKKFAENFFEEKQQRGVLDFNDLEHLALKILLKNGAPSDVANSYKKQFKEVLIDEYQDTNMVQETILLLVTNSNDTKGNLFMVGDVKQSIYRFRLAEPTLFMAKYQEYQQDGEGSGIRIDLSQNFRSRKEVLDATNFIFHQLMDKHIAEIDYDEAAELTLGASFPEANNMATELLLIDMKSEEKESEDELSPQELQKNQVESRAIATKIREMIDNKFPIYDKKLQQNRPIQYRDIVILARAMTSAPDMEEAMKIKDIPFYANNNSGYFETTEVATMIALMKVIDNPYQDISLAAVLRSPIIGLNEEELGQIRMAKKKGYFFDAMLAYKDITVSDAANKISRFITQLNNWRELSIRENLTALIWQIYQETNFYEFVGGLPGGKQRQANLRALYDRANQYEKTSFRGLFRFVRFVERLEVRGDDLGTAKTLGEKEDVVRMMTIHASKGLEFPVVIVSGLSRKFNMRDIYSKTLLDKDYGFASNYRDIEKMIVYPTIMQQAIKQKKYREMIAEEMRVLYVALTRAEEKLILTATVPDFEKTSKNWLQVSNQQETILPAAIRAKAKCYLDWIGNATIRHSHFKELLCEEKIKTLPTDMKLQVEIKTKEMFLTDDLEKEKSDNWMENVKAHKQVPVKSPYKDEIERFMHYQYKDEEATGIRAKQSVTELKRQFSLQDSWSDTSILKEFQKVSLDRPKFLQQNKLSATEIGTAMHTLMQAVPLDDKPTEKDLVSLLQLMREKDILTEAQIKAINVNQIIAFFESALGKTVLQKKDKVKREVPFSYLLPAAKLYNQTNLDEHVLIQGVVDSMIEEEDSIILIDYKTDKIEGRYDNWEAAEKVMKERYQIQIKLYAEAIQAISRKKVSHAYLYFFDGQHICQINIEEGI | The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities. | Q929A9 |
Q11QA3 | RL10_CYTH3 | 50S ribosomal protein L10 | Cytophaga | MTKEEKAIIIQEVAQKIAGAATFYITDGSGMTVDQVNKFRKLCFSKGVEYKVVKNSLIKKALQQLNIDHTALNGAALKGASGLMFSDTANVPAKLLKQFHKGGVAKPEFKGASVFADFYVGKDKLDALASIKSKEELIGDIIALLQAPAQRVIGGLTNESRVFAEQA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | Q11QA3 |
P60152 | PSBL_PSINU | Photosystem II reaction center protein L | Psilotum | MTQPNPNKQSVELNRTSLYWGLLLIFVLAVLFSNYFFN | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. | P60152 |
Q9AXI1 | OL141_ARAHY | Oleosin 5 variant A | Arachis | MATATDRAPHQVQVHTPTTQRVDVPRRGYDVSGGGIKTLLPERGPSTSQIIAVLVGVPTGGTLLLLSGLSLLGTIIGLAIATPVFTFFSPVIVPAVVTIGLAVTGILTAGACGLTGLMSLSWMINFIRQVHGTTVPDQLDSVKRRMADMADYVGQKTKDAGQQIQTKAQDVKRSSS | May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. | Q9AXI1 |
Q9GMC8 | CP17A_FELCA | Steroid 17-alpha-monooxygenase | Felis | MWELLVFLLFAVAYFLWPKAKCPGAKYPKSLPSLPLVGSLLFLPRSGHPHKNFFKLQKKYGPIYSFRLGTKTTVMVGDHQLAKEVLVKKGKEFSGRPHVVTLDILSDNQKGIAFADHGASWQMHRKLALATFALFKDGDQRLEKIICREISLLCDNLAMQDGQSIDLYLPLFLAVTNIICLICFNSSFKNGDPALKIIQNYNEGILKTLGKDNLVDIFPVLKIFPNKTLEKMKNYVKNRDELLREILEKHKENFSNDSITNMLDVLIQARMNSDNNGAASDQDSKLLSDKHILTTIGDIFGAGVETTTSVVRWTVAFLLHHPQLYKKLQEEIDQNIGFSRTPTMSDRNQLILLEATIREVLRIRPVAPTLIPHKAIMDSSIGEFAVDKGTNVIINLWALHHNEKEWYRPDQFMPERFLDPTRSQLISPSLSYLPFGAGPRSCLGESLARQEVFLFMAWLLQRFDLEVPDDGQLPHLEGNPTVVFLIAPFKVKVKVRQAWREAQAEGST | A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). | Q9GMC8 |
A5F1A0 | CHED_VIBC3 | Probable chemoreceptor glutamine deamidase CheD | Vibrio | MLVVAVRFSIIWDILFMSDSKLATKRKLKQEEAKGQYYRFNHPSDHRHWVKVMPGGVYATSDQEIIHTGLGSCVSACAWDIEMKVGGMNHFLLPFNNQFESQHWHPQALLSDSSRYGCYAMEVLINRLLSMGAERERLKFKLFGGAHLMGYQSLVGEKNVEFVLEYAKREKLNVVAQDLGGAQPRKLLFDPQAGQAWVKRIGFSSAHAIKQDEELYQHSIDKQIPSDDVELFQ | Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. | A5F1A0 |
Q6C0Z6 | CCPR_YARLI | Cytochrome c peroxidase, mitochondrial | Yarrowia | MRSFRAVRNFSTTAKRLSQAPKASTPNASSGNGFVLAFVAAAAGAGAYYYYANSPAAKVETFNATKADYQKVYDAIADKLIEDDDYDDGSYGPVLLRLAWHSSGTYNKSDNKFGSSGGTMRFKPEASHAANNGLVNARNFLKPIHEKFPWISTGDLYTLGGVTAVQELGGPIIPWKRGRVDEPESASPPDGSLPDASQGATHVRNVFNRQGFNDQEMVALIGAHALGRCHKQNSGFEGPWTFSPTMFTNDFYKLLLDDKWQWKKWDGNPQYEDVKTKSLMMLPTDMALATDKNFKKWATAYAKDQDLFFKDFSAAFSKMLNNGVDFPQGTEIWEFKPKNA | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Q6C0Z6 |
Q1G9W7 | RECO_LACDA | Recombination protein O | Lactobacillus | MAADLLDVHGLLFKRQQYKEADLLAKLWTKELGIVTVIAKGGMRPKSQLAAAVLPFTEGTFGILTRYKGISQLRTYKKLSQHDELFTDLDKNAYLSYLFDLADHAFSEYQKLGGYYDLLLVAFNRIVAGQDPEIIAQIVQLQLLDAFGVAPQLGACVICGKEKGIFDYSIAAGGVVCSDHFRSVSRLHLSPKATALIRTLALLPISRLGEIQIGEDLKKESRRAIAQIYQATVDLHLPSLRFLNEVRGS | Involved in DNA repair and RecF pathway recombination. | Q1G9W7 |
A5V6A9 | DXS_RHIWR | 1-deoxyxylulose-5-phosphate synthase | Rhizorhabdus | MNDRPPTPLLDTVSTPEDLRRLKPADLRQLADELRAEMISAVSVTGGHLGAGLGVVELTVALHYVFDTPRDVLIWDVGHQAYPHKILTGRRDRIRTLRQGGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAVANKLANKEGRAIAVIGDGAMSAGMAYEAMNNAKQAGNRLIVILNDNDMSIAPPVGALSAYLAKIVSSRPFLSMRGFAKRVAQKLPRPIHDFAKRSEEYARGMATGGTLFEELGFYYVGPVDGHNLDHLLPILENVRDGDHGPILIHVVTNKGKGYAPAEAAADKYHGVQKFDVVSGVQAKAPPGPPSYTGVFADALVAEAKRDDRICAITAAMPSGTGLDKFGKAFPERSFDVGIAEQHAVTFAAGLAAQGYRPFCAIYSTFLQRAYDQVVHDVAIQNLPVRFAIDRAGLVGADGSTHAGSFDITYLATLPNMVVMAAADEAELVHMVHTAAVHDSGPIALRYPRGNGVGVALPAAPERLAIGKGRIVREGKTVALLSLGTRLGEALRAADQLDALGLSTTVADLRFAKPLDEAMIQTLLTSHEVAVTIEEGAIGGLGAHVLTLASDLGLIDGGLKLRTMRLPDAFQEHDKPEKQYAEAGLDAESIVATVLAALHRNSKGLEESA | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | A5V6A9 |
G0KYB1 | TRI3_TRIAR | Trichothecene biosynthesis cluster protein 3 | Trichoderma | MGSKLPELPKLSPEKHRWEKSNVDPRVLQRRGIGSEAIVGMERSNRRGQYDLYLLATLRTAHVSTSTPLSLLYLKEKLELALLVMRFEHPECACTVTWDDQVPPIIQYASPQNDEEALMWAKSSVHIRTTSQTGFDVRYEIEGKRQDLDQDNMEPSRPIVIYLISNVTNGDAQLTSGATVDVLLHMNHLFWDGISARMFTGDLFRELNKLINSNEQELPKLQWGTEASNLSAPVLDALKINIEELREEFEAASNQFVKALYENYGGWGLEFKSGLGLPRTDIHTSTATESKAIINGVKTRLGPQYTISHLAQAAVVIAMLEIIQPPNLTDKDIFVSPMPVNGRRWLKDGLADHHYSICETGAVIRIENIKSLVLNNNNDKGYRPRCDEKKPGEDVKKSFDQWLGNPYQLALGLAVHTLEASFLTANPMPFDKVAAPFFISDGRNEQFIPASITTTTGEILMTIDNFVFFLNQCLPYLAIRLESWKDASTLSVCYNKANYSQEEATKFLKCVAKYMLIFSQ | Trichothecene O-acetyltransferase; part of the gene cluster that mediates the production of the antimicrobial trichothecene harzianum A (HA) that plays a role in Botrytis cinerea antagonistic activity and plant defense priming . The biosynthesis of harzianum A begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 . Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichodiol . Isotrichodiol then undergoes a non-enzymatic isomerization and cyclization to form 12,13-epoxytrichothec-9-ene (EPT) which is further converted to trichodermol by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation . The last step of HA synthesis is esterification of an octatriendioyl moiety to the C-4 oxygen of trichodermol. The octatriendioyl moiety is probably produced by the polyketide synthase TRI17 and the esterification performed by the trichothecene O-acetyltransferase TRI3 (Probable). | G0KYB1 |
P32090 | MUTT_PROVU | dGTP pyrophosphohydrolase | Proteus | MMDKKKLHIAAGVICDKHNNVFIAQRPLKSHMGGFWEFPGGKLEDNETPEQALLRELQEEIGIDVTQCTLLDTVAHDFPDRHITLSFFLVTEWKNELTEKKGSCRVGHLLCL | Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. | P32090 |
Q83SN2 | SECA_SHIFL | Protein translocase subunit SecA | Shigella | MLIKLLTKVFGSRNDRTLRRMRKVVNIINAMEPEMEKLSDEELKGKTAEFRARLEKGEVLENLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNERCIAEMRTGEGKTLTATLPAYLNALTGKGVHVVTVNDYLAQRDAENNRPLFEFLGLTVGINLPGMPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYKRVNKIIPHLIRQEKEDSETFQGEGHFSVDEKSRQVNLTERGLVLIEELLVKEGIMDEGESLYSPANIMLMHHVTAALRAHALFTRDVDYIVKDGEVIIVDEHTGRTMQGRRWSDGLHQAVEAKEGVQIQNENQTLASITFQNYFRLYEKLAGMTGTADTEAFEFSSIYKLDTVVVPTNRPMIRKDLPDLVYMTEAEKIQAIIEDIKERTAKGQPVLVGTISIEKSELVSNELTKAGIKHNVLNAKFHANEAAIVAQAGYPAAVTIATNMAGRGTDIVLGGSWQAEVAALENPTAEQIEKIKADWQVRHDAVLEAGGLHIIGTERHESRRIDNQLRGRSGRQGDAGSSRFYLSMEDALMRIFASDRVSGMMRKLGMKPGEAIEHPWVTKAIANAQRKVESRNFDIRKQLLEYDDVANDQRRAIYSQRNELLDVSDVSETINSIREDVFKATIDAYIPPQSLEEMWDIPGLQERLKNDFDLDLPITEWLDKEPELHEETLRERILAQSIEVYQRKEEVVGAEMMRHFEKGVMLQTLDSLWKEHLAAMDYLRQGIHLRGYAQKDPKQEYKRESFSMFAAMLESLKYEVISTLSKVQVRMPEEVEELEQQRRMEAERLAQMQQLSHQDDDSAAAAALAAQTGERKVGRNDPCPCGSGKKYKQCHGRLQ | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | Q83SN2 |
A0LIJ7 | RL16_SYNFM | 50S ribosomal protein L16 | Syntrophobacter | MLAPKRVKFRKQQKGRMRGTAFRGSTLSFGDFGLKALECGYITSRQIEAARIAITRHVKRGGKVWIRFFPDKPFTKKPAETRMGKGKGSPEGWHAVIKPGRVLYEIKGVPETIAREALNLAAHKLPIPTRFVSRQDVL | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | A0LIJ7 |
A8ANW0 | ISPF_CITK8 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Citrobacter | MRIGHGFDVHAFGGEGPIIIGGVRIPYDKGLLAHSDGDVALHALTDALLGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTIIAQAPKMLPHIPQMRVFIAEDLGCHMDDVNVKATTTEKLGFTGRGEGIACEAVALLIKAAK | Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). | A8ANW0 |
P45378 | TNNT3_HUMAN | Fast skeletal muscle troponin T | Homo | MSDEEVEQVEEQYEEEEEAQEEAAEVHEEVHEPEEVQEDTAEEDAEEEKPRPKLTAPKIPEGEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKELWETLHQLEIDKFEFGEKLKRQKYDITTLRSRIDQAQKHSKKAGTPAKGKVGGRWK | Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. | P45378 |
P00309 | PHEA_MASLA | Phycoerythrocyanin alpha chain | Mastigocladus | MKTPLTEAIAAADLRGSYLSNTELQAVFGRFNRARAGLEAARAFANNGKKWAEAAANHVYQKFPYTTQMQGPQYASTPEGKAKCVRDIDHYLRTISYCCVVGGTGPLDDYVVAGLKEFNSALGLSPSWYIAALEFVRDNHGLTGDVAGEANTYINYAINALS | Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. | P00309 |
Q15661 | TRYB1_HUMAN | Tryptase alpha-1 | Homo | MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP | Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates . | Q15661 |
Q3BUQ7 | SYA_XANC5 | Alanyl-tRNA synthetase | Xanthomonas | MNAPAKFSTSQIRSDFLAFFEGKGHTIVPSAPLVPGNDPTLLFTNSGMVQFKDVFLGAEKRSYVRAADVQRCLRAGGKHNDLDSVGYTARHHTFFEMLGNWSFGDYFKKDAIAWAWELLTQVWKLPADRLLVTVYHTDEEAFALWRDMIGIPESRIVRIGDNKGAPYASDNFWQMADTGPCGPCTEIFFDHGDHIAGGPPGSPDEDGDRFIEIWNLVFMQFDRQPDGTLVPLPAPCVDTGMGLERLAAILQHVHTNYEIDLFQALIGKASALTGITDLENKSLRVIADHIRACSFLIVDGVLPSNEGRGYVLRRIIRRALRHGWMLGVRQPFFSKMVPTLVELMGEAYPELVVAQDTVARALLAEEERFAETLDAGMKIFDEVASRSQDIIPGADAFRLYDTYGFPVDLTADIARERGMRVDMEGFEFAMERQRETARAAGKFGGGVALPADLVASMSPTVFLGYEAYDADALKVVALLKQGRPVERAEAGDEVIVFTDRTPFYAESGGQVGDSGQLSGPGVSINVTDTQKFAGQFHGHVGRISEGALALGDVLAGGIDTQRRGKTILNHSATHLLHAALREVLGTHVQQKGSLVAPDRLRFDFSHFQPFTADELAVIERKVNAEVRANHGVEVHNMAMQEALDFGAMALFGEKYGENVRVLKMGGYSTELCGGTHVTRTGDIGLFKITSEGGVSSGVRRIEAVTGQGALDYVADEERRLLEAANLLGGNTSEVVDKVRALTERQKRLERELESLKAKLASGATADLGASAIDVVGVKVVAVRLEGFDAKALRDAMDRLKQQLGDSVIVLAGASGGKVALVAGVNGSPTGKVKAGELLGHIASQIGGKGGGRPDLAQGGGEDGPALATALDGVPLWVKQHLG | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Q3BUQ7 |
C5CIV6 | ATPA_KOSOT | F-ATPase subunit alpha | Kosmotoga | MKISPSEITKIIEEQLKRSDREIDYFEAGRIIQVGDGIARAYGLKGVMSNELVQFENGEYGLALNLEEDNVGIVVLGDYREIKEGDLVKRTGRIIEVPAGEALLGRVVNPLGIPLDGKGPIEASEHRPVEIKAPGVVMRKPVDTPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKDQGVYCIYVAIGQKTAVLARIIDKLEETGAMEYTTIVAATANDPATLAYLAPYAGAAMGEYFMYSGKDALVIYDDLSKHAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAARLNEEHGGGSLTALPIIETLANDVSAYIPTNVISITDGQIYLDPNLFYAGNRPAINVGLSVSRVGGSAQIKAMKKIAGSLRLDLAQYRELLAFAQFSTELDKATQAQLIRGEKLTELLKQEQYSPMPVEEQIAVLYAGTRGYLDDLPTDKIRQFEKQLLQTMRQKYADVLKAIREKKDMTEEIEAGLKKAVEDVRQAFVS | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | C5CIV6 |
Q9C6B9 | PEAM3_ARATH | Phosphoethanolamine N-methyltransferase 3 | Arabidopsis | MASYGEEREIQKNYWKEHSVGLSVEAMMLDSKASDLDKEERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENINGHYKNVKFLCADVTSPNMNFPNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFFRESCFHQSGDNKRKYNPTHYREPKFYTKLFKECHMNDEDGNSYELSLVSCKCIGAYVRNKKNQNQICWLWQKVSSDNDRGFQRFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSPDFAIYIKKRGYDLHDVQAYGQMLRDAGFEEVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYEDIIGGWKSKLLRSSSGEQKWGLFIAKRN | Catalyzes N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine. | Q9C6B9 |
Q9NZP0 | OR6C3_HUMAN | HSA8 | Homo | MNHTMVTEFVLLGLSDDPDLQIVIFLFLFITYILSVTGNLTIITLTFVDSHLQTPMYFFLRNFSFLEISFTTVCIPRFLGAIITRNKTISYNNCAAQLFFFIFMGVTEFYILTAMSYDRYVAICKPLHYTSIMNRKLCTLLVLCAWLSGFLTIFPPLMLLLQLDYCASNVIDHFACDYFPLLQLSCSDTWLLEVIGFYFALVTLLFTLALVILSYMYIIRTILRIPSASQRKKAFSTCSSHMIVISISYGSCIFMYANPSAKEKASLTKGIAILNTSVAPMLNPFIYTLRNQQVKQAFKNVVHKVVFYANQ | Odorant receptor. | Q9NZP0 |
P0AES2 | GUDD_ECOLI | D-glucarate dehydratase | Escherichia | MSSQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDMDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR | Catalyzes the dehydration of glucarate or L-idarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc) . Also catalyzes the epimerization of D-glucarate and L-idarate . | P0AES2 |
F6M8H7 | SMST_SANMU | Probable sesquiterpene synthase | Santalum | MENQKMPISSVPNLKDLNMISRPIANFPPSIWGDRFINYTCEDENDQTQKERQVEELKEQVRRELAATVDKPLQQLNIIDATQRLGIAYLFENEIEESLKHIYLHTYVENNCFEGSDDLYSVALWFRLLRQNGYKVSCDVFNKFRDNEGNFKNNLMEDAKGLLELYEATHVSIHGEEMLDDALEFTKTRLESVVSHLNYPLAEQVRHALYQPLHRGLPRLEAVYFFRIYEAHASHNKALLKLAKLDFNLLQSFHKKELSDIARWWKSLDFAAKFPFARDRLVEGYFWVLGVYFEPQYSLARKIIIKVFTMISTIDDIYDAYGTLDELKLFTKAMQRWDVGSLDQLPEYMKPCYKSILDVYNEIEEEMANQGSLFRMHYAKEVMKTIVEGYMDEAKWCHEKYVPTFQEYMSVALVTSGYTFLTTISYLGMGEIASKEAFDWLFSHPPVIEASESVGRLMDDMRSHKFEQERGHVASGIECYMKQYGVTEEEAHDEFRKRLVKAWKDINEECLRPYRVPKPLLTRILNLTRVIDVIYKNEDGYTHVKKAMKDNIASLLIDPVIV | Sesquiterpene synthase. | F6M8H7 |
Q9LYC8 | GRXS6_ARATH | Protein ROXY 17 | Arabidopsis | MESVRSLVEDKPVVIFSKSSCCMSHSIQTLISGFGAKMTVYELDQFSNGQEIEKALVQMGCKPSVPAVFIGQQFIGGANQVMTLQVKNQLAAMLRRAGAIWV | May only reduce GSH-thiol disulfides, but not protein disulfides. | Q9LYC8 |
Q51834 | RNZ_PORGI | tRNase Z | Porphyromonas | MAAFSVHILGCGSALPTTHHHPSSQVIDLRDKLYMIDCGEGVQRQFRHEKLHFGRLIHIFISHLHGDHCFGLPGFISTLGLLGRTGTLHVHGPEGIERFLSPILEQFCHRMPYQVEIHTIDASRHALVHEDKSVKVYSIPLSHRIPAVGYLFEEKCRARHLNKAAAEFYNIPLAEYPLIIEGSDYTTPDGRIIPNRHLTTPGTPPRRYAYCSDTEFCPSIVPIIQGVDLLYHEATFMEEDRARAKETFHSTAKEAAEIARQAGAKRLLIGHYSGRYKDVQGLLEEAQSVFKPTIAANERMRIDL | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. | Q51834 |
A8YTF6 | Y401_LACH4 | Nucleoid-associated protein lhv_0401 | Lactobacillus | MSRRPNFGGMGMGGMNMQQMMKQAKKLQAQMAQEQENITAQEFTGKSADDLVVATFTGDRKLKDIKIDKEAIDPDDPDMLQDLVIDAVNKGLSQIDEATQASLGKYTKGLM | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A8YTF6 |
B8NM79 | USTS_ASPFN | Ustiloxin B biosynthesis protein S | Aspergillus subgen. Circumdati | MTKTEESPLHFFDIFSTLPGTSKSWSSNVLKIRMVLNYKGIPYTQSFHSYPDIAPLLQSLSVPPHKQGRFKYTLPAICHPSSVKSSPSGAMMDSLPIACHLDETYPDPPLFPSGEASYALALAIGKLMVPAALKTCDLLLPKAEEVLDDRGKEYFVRTRTEIFGKPLSELRPKTEEGVRAIVDGMKADMEVFISMLRGRGEGKKSGPFLEGEKPGYADFILVTFLSWSHRFDMELWREIMDMGNGEFRALWHASVQWLEGQGEEKEWAVPQLSTVD | Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide . First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-Lys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) . Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI . To process the precursor peptide further, at least two peptidases are necessary to cleave the N-terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline . One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH . Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F . For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization . UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations . N-desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H . The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H . Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B . | B8NM79 |
P07306 | ASGR1_HUMAN | Hepatic lectin H1 | Homo | MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL | Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. | P07306 |
O31678 | QUEF_BACSU | PreQ(0) reductase | Bacillus | MTTRKESELEGVTLLGNQGTNYLFEYAPDVLESFPNKHVNRDYFVKFNCPEFTSLCPKTGQPDFATIYISYIPDEKMVESKSLKLYLFSFRNHGDFHEDCMNIIMNDLIELMDPRYIEVWGKFTPRGGISIDPYTNYGKPGTKYEKMAEYRMMNHDLYPETIDNR | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. | O31678 |
O60512 | B4GT3_HUMAN | UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3 | Homo | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. | O60512 |
Q1C2C4 | FADB_YERPA | 3-hydroxyacyl-CoA dehydrogenase | Yersinia | MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTKTVANLGEALNVLEKQSELKGLLLRSAKTALIVGADITEFLSLFNAPPEKLHQWLVFANTIFNRLEDLPVPTISAINGYALGGGCECILATDFRIASPEARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIATGKDVTANDALKIGLVDAVVDPEKLVGSALTMLKQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGRVMQVAGKHYPAPLTAVKTIEAAAKFGRTEALNLETNSFVPLAGSNEARALVGIFLNDQYVKAQAKKLSKGVAAPKLAAVLGAGIMGGGIAYQSALKSVPVIMKDINENSLDLGMNEAAKLLNKQLERGKVDGLKMASILATIRPTLDYAGIERAQVIVEAVVENPKVKAAVLAEVEALIGEDTVLASNTSTIPIDQLAKSLKRPENFCGMHFFNPVHRMPLVEIIRGAKTSDKTLAAVVAYATQMGKTPIVVNDCPGFFVNRVLFPYLAGFGMLVRDGGDFHQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPERMNKDYRDAVDVMFDNQRFGQKNGQGFYRYTQDAKGKPRKENDEQVDKLLAEISQPLQEFSDEDIIARTMIPMINEVVRCLEEGIIASAAEGDMALVYGLGFPPFHGGVFRYLDTLGSANYVEMAQRYAHLGALYHVPAGLRAKAEHNESYYPVAAALLDVSTNQPA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. | Q1C2C4 |
Q08460 | KCMA1_MOUSE | Slowpoke homolog | Mus | MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLVSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQNRKEMVYR | Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX). | Q08460 |
A0B9M2 | UPPP_METTP | Undecaprenyl pyrophosphate phosphatase | Methanothrix | MDALQALVLGALQGITEWLPVSSEGQTMLAMISWLGMRPTDALSCSIFLHTGTMLAVLVRFRSRLLGMLNTESKLMRTVIVATLFTGITGVPLYMLFRDRFTGGEQATLLIGSLLIATGLMLRLRSSSTKDMEEISTKDMVLLGLAQGFSILPGVSRSGTTLTVLLMRGVKQDDALMVSFIISVPAVLGAIALDCLAGSPLSIRSLPGAVMLASSFITGYATMDVLMRFSRNVSFSWFCITMGMITLALTALPEVQ | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). | A0B9M2 |
F4JSV3 | EDA40_ARATH | RING-type E3 ubiquitin transferase EDA40 | Arabidopsis | MMNGLRRTFWSSIHKKKDNNRVDDSLDRQKPTTTSRFGFFSNPSTPRSETRPDSVTCSPTIPCQSWSATAISTPSPSLPASPKLQCDTSGDVTPTRNRSPLSFLSVSSSSSTPSSPKSPASFSLLKSKLCFTKVRILNRNNQVNIFKNNSKLTFLRLCYEQSSISSSKCGICLQSAKAGRGTAIFTAECSHTFHFPCVASRAGDRNLLSDCPVCGASWRETSLLPLSLSSSLHESGSESDSKIRESKNNNKSLRVYNDDEPLISSPISRTGFNTIPESNEDEEEEDNDDGEFKGFYVNTPSPLTTKKMLTDSVTGHVDVKLSSEAAIVAVGRGNETYSVLMKIKSPSLPTARRSPVDLVTVIDVSGGNIEMVKRAMRQVISSLRETDRLSMVSFSSSSKRLTPLRRMTANGRRLARRIVDDISGDGDGMSVNDAVKKAAKVIEDRRQKNLFTTIFVLTDRNRNSAHQAQLAQPDFVTSTRFSHLEIPTHTIWLGACNHALPEDVFAKRIKSLLSLSVQDLTLNLGLVSGSGQGKVTSVYSLSGRPVWLGSGLIRLGDMYGDEEREVLVELKSPSSSRSQRIMTVRSRHVDPTTQEIKNYEDRALMIPRPTTVRSSDPSIARLRNLHVSTRAVAESRRLVEVNDYSGAERMLTSARALLVQYGLSSSDSCLRGLEAELADLNRLRGRHVAVKSPEPVVQKSEPLTPTSAWRAAERLAKVAIMRKHMNRVSDLHGFENARF | Probable E3 ubiquitin-protein ligase involved in female gametophyte development. Required for fusion of polar nuclei in the embryo sac. | F4JSV3 |
B8E8D7 | SELO_SHEB2 | Protein adenylyltransferase SelO | Shewanella | MKFKQDFFTQLPEFYSQVYPQGITKPEWLAWSDDAAQLIGLSQPTDELLLGLSGNAAVDGATYYAQVYSGHQFGGYTPRLGDGRSIILGEAIGPNGAWDVALKGGGPTPYSRRGDGRAVMRSAVREFLVSEALHHLHVPTTRALAVIGSDLPVWRESQETAAITVRLARSHIRFGHFEFFCHSERGRADKLIQLLNFTITQHYPHLSCDAAGYKAWFLQVVQDTAKMIAHWQAVGFAHGVMNTDNMSILGDSFDFGPFAFLDTFQEDFICNHSDPEGRYAFGQQPGVGLWNLQRLAQALTPVIPSDDLIAILNQYQEALVQPYLRLMRAKLGLSAVDVPSVEQDKQDLDLIGRFTVLMEKNQLDYTQTWRQLGKLDPTSKHSALRDDFIDVSQFDTWYQAYQQRLGAVADIPAWQTERNSVNPKYILRNYLAQEAIIAVEEGNLAPLHLLQKILTQPFAEHAEHEDLAKRPPDWGQGLIMSCSS | Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). | B8E8D7 |
Q2NHD1 | RADB_METST | DNA repair and recombination protein RadB | Methanosphaera | MKTLSDISESVLIPTNSSLDKLLGGGIEKGCITQFYGPPGSGKTNIALKILYEATKNGSKAIYMDTEGGLSLERIQQIAGTDFGSISKNIYILEPKSFDEQILDIQNIEDILKKDKSIDMLIIDSIVALYRVEDGDPSEINKRLGRLMAKLLRLSREYNVAIVITNQIYSPFDSDDLIIEPIGGTVLKYWSKIIIEIEKSVDSLKRTATLQRHKTKAPGQSIKFEIIDRGII | Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange. | Q2NHD1 |
O67502 | TRPA_AQUAE | Tryptophan synthase alpha chain | Aquifex | MGRISDKFTELKEKREKALVSYLMVGYPDYETSLKAFKEVLKNGTDILEIGFPFSDPVADGPTIQVAHEVALKNGIRFEDVLELSETLRKEFPDIPFLLMTYYNPIFRIGLEKFCRLSREKGIDGFIVPDLPPEEAEELKAVMKKYVLSFVPLGAPTSTRKRIKLICEAADEMTYFVSVTGTTGAREKLPYERIKKKVEEYRELCDKPVVVGFGVSKKEHAREIGSFADGVVVGSALVKLAGQKKIEDLGNLVKELKEGLRE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | O67502 |
Q2NCP2 | NHAA2_ERYLH | Sodium/proton antiporter NhaA 2 | Erythrobacter | MFYTAATALRDFLKQESAGGIVLMFAAVLALIFANTALADTYFSVLATEIAVTVGGGGIEKPALLWINDGLMAVFFFLVGLEVKREVLTGQLSSWKQASLPLIAAFGGIVLPALVFYGINSGTPENLSGWAIPAATDIAFALGILALLGKRVPVALKALLLAIAVIDDIAAIAIIAIFYTPGVELAMLGAAAITLLILSAFGRAKAGSSIPYIVLGIVLWYFVLKSGVHATLAGVALAMTVPLIDRKGNHMLEHMEHALHSWVAFLVVPIFALANAGVSFEGVELSALFAPLPLGIALGLIVGKQVGIFGFAWLAVKTGFAQLPSSVGWLQVWGLSLVAGIGFTMSLFIGNLAFADPAQINAVKIGVLSGSLIAALVGIAILVLGAKAPAAKSADERVQAPA | Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. | Q2NCP2 |
Q9D1I2 | CAR19_MOUSE | Bcl10-interacting CARD protein | Mus | MTDQTYCDRLVQDTPFLTGQGRLSEQQVDRIILQLNRYYPQILTNKEAEKFRNPKASLRVRLCDLLSHLQQRGERHCQEFYRALYIHAQPLHSHLPSRYSPQNSDCRELDWGIESRELSDRGPMSFLAGLGLAAGLALLLYCCPPDPKVLPGTRRVLAFSPVIIDRHVSRYLLAFLADDLGGL | Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. | Q9D1I2 |
Q9QZY7 | CD1C2_CAVPO | T-cell surface glycoprotein CD1c2 | Cavia | MLFLQFLFVDVVLGGSITENVVQENISLYLMQISSYANQSWTQNLGSAWLDQLQTHSWDSESGTIIFLHAWSRGNFSNEEVTDMQLLLRVHFAELTLDVHQQASQLQFKYPFDIQVRLGCELHSRETTKSFLHVAFNGLNFLSFQHKSCVPSPEGETRAQKACDILNTYEATKEIAYYVMNDICPRLLLSLLEAGKMDLQRQVRPEVWLSSSPNLEPGRLLLACHVSGFYPKPIWVMWMRGAQEQLETKQGDILPHADGTWYLRVTLNVVAEEAAGLSCRVRHSSLRDQDIILYWGHGLSVILIALAVIVPLVLLIVLVLLCKKRCTYQGIP | Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. | Q9QZY7 |
A7MKE8 | NUDL_CROS8 | Uncharacterized Nudix hydrolase NudL | Cronobacter | MENSPLTLDRFLSRFQLLRPQMSRSSLNQRQAAVLVPVVRRPEPGLLLTKRAATLRKHAGQVAFPGGAVDDTDASLIAAALREAQEEVAIPPEAVDVIGVLPPVDSVTGFQVTPVVGIIPPDLPYHASEDEVAAVFEMPLAEALRLGRYHPLDIHRRGNHHRVWLSWYQHYFVWGMTAGIIRELALQIGEKP | Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. | A7MKE8 |
Q886V0 | TRMD_PSESM | tRNA [GM37] methyltransferase | Pseudomonas | MASLRIEVISLFPEMFSAISEYGITSRAVKQGLLQLTCWNPRDYTTDRHHTVDDRPFGGGPGMVMKIKPLEDALVQARQAAGDAAKVIYLSPQGRQLNQAAVRELAQEEAIILIAGRYEGIDERFIEAHVDEEWSIGDYVLSGGELPAMVLIDAVTRLLPGALGHVDSAEEDSFTDGLLDCPHYTRPEVYADQRVPDVLLSGNHAHIRRWRLQQSLGRTYERRADLLESRSLSGEEKKLLAEYIRERDDS | Specifically methylates guanosine-37 in various tRNAs. | Q886V0 |
Q6YQX2 | PNP_ONYPE | Polynucleotide phosphorylase | Candidatus Phytoplasma asteris | MLKKVFETTNLKDSFQVEIGTYARNVDASILVRYQDTVVLTTTVFSRKPNNLDFLPLTVIYQEKLYAAGKIPGSFLRREGRSNDHEILTSRLIDRSLRPLFPDYFQQEVQVINTVLSLDPDFKSELASMLGSSLSLLISEIPFFEAISGVYVGKINDKFIINPTLQQLANSTLHLMVAGTKHNVTMIEAHANEVSEQDFLEAINFAHQYIKKLCLFQENIKQQFAPAKITNTLHQTEQTQQQAFFAKHQSQVKQAILSCNSKNDLQQLKEQILDQAKQTPFFKTIDTATVFDYEAHKKHLQTTETLFQKLSKQETRSLILQEKIRPDKRGLEEIRTLESQIDLLPRAHGSALFTRGQTQSLAAVTLGCLSESKIIDGLSDEQNKRFMLHYNFPPFSVGAVGRYTAPSRREIGHGTLAEKAISQVLPEEKDFPYTIRVVSEILESNGSSSQATVCASSLALMASGVPLKKAVAGMSVGLVFDQATNKYVILSDIQGLEDHVGDMDLKIAGTNKGITALQMDLKIQGIHFKILQEAFLQAKKGRLHILEHMSQTISQPRLEVSKYAPKVCMMQIKPEKIRDIIGSGGKIINQIIESHDGVKIDIEQDGRVFVMHSNLETVKKTVAFIESLIQEIQIGTCYQASILRFLSDKQGKMIGAVAQVCPGIEGLIHVNQKKFQKITDVLKIGETVSVKCTKINDRGRIDFLLLPKNTQEKNS | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | Q6YQX2 |
Q601U7 | TRUB_MESH2 | tRNA-uridine isomerase | Mesomycoplasma | MADTLDLGSSAFGCKGSSPFLRTTMIGQPCVDFFFFFFFFFKKKKKKMITFLYKPKKISSAKFLRQWSKTNLIKKAGHAGTLDPLASGLLLVATEDDTKLLQYLDQKTKTYLAKIQFGFWSTTYDAEGQIYGVEQPIKVTKDNLEQALNRLSESQKQVPPVFSSKKVSGKSAYHYARQGKQIELKPISIKISKTILINFDEKLQNCVIMWQVSRGCYIRSLADDLGKMLKTRAYLSDLERTKIGNFDKKFLNQSLKPQDLFDLQQVKLDLENLELLLQGKKINYFAKNSELNTLIFKDEVVGFGKIINNVLITKKLFGNRIKKIINT | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q601U7 |
Q6AF47 | WHIA_LEIXX | Probable cell division protein WhiA | Leifsonia | MALTADVKDELTKVEVSKTTVRAAELATILRFSGGLHLIGGRIAVESELDTPELARRVRKDLAELYGVRGVVSVISTSGVRRASQYLVRVLDGGETLARQTGLLDAHRRPIRGLPNRLTTGSREELAAVWRGAFLASGSLTDPGRSAALEVTCPGNEAAMALVGAAGRIGVAAKAREVRGVHRVVIRDGEAISAMLVQMGAAQTVSNWEELRQRREVRATANRLVNFDDANLRRSAQAAVAACARVERALEILGDDIPEHLQYAGRLRLAHRDASLDELGHYADPPMTKDAVAGRIRRLLAMADKRASDLGVPSTEASLPADFDEV | Involved in cell division and chromosome segregation. | Q6AF47 |
A7I9I6 | IF6_METB6 | Translation initiation factor 6 | Methanoregula | MERTTTFAGDPNIGVFARVAGNIAVIPPEAPEEFRNAIREGLGVELLVTTIQGSAIIGSLVAGNSRGLVVSGLATDEELAVLKKHRKVMLLCETMNAAGNVIMANDTFAAVHPDLPAEVAEEIGAFLGVEVIHLTLGGVRTTGMAGVATNKGVIVHPRATAQEIARLETVSGIPVGTGTINMGSGLVGTGLLVNDTGYLAGNATSGFELGRVEDVFGFLE | Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex. | A7I9I6 |
P70981 | YBAC_BACSU | Probable aminopeptidase YbaC | Bacillus | MIPEKKSIAIMKELSIGNTKQMLMINGVDVKNPLLLFLHGGPGTPQIGYVRHYQKELEQYFTVVHWDQRGSGLSYSKRISHHSMTINHFIKDTIQVTQWLLAHFSKSKLYLAGHSWGSILALHVLQQRPDLFYTYYGISQVVNPQDEESTAYQHIREISESKKASILSFLTRFIGAPPWKQDIQHLIYRFCVELTRGGFTHRHRQSLAVLFQMLTGNEYGVRNMHSFLNGLRFSKKHLTDELYRFNAFTSVPSIKVPCVFISGKHDLIVPAEISKQYYQELEAPEKRWFQFENSAHTPHIEEPSLFANTLSRHARHHL | Probable aminopeptidase. | P70981 |
B5F138 | LFTR_SALA4 | Phenyalanyltransferase | Salmonella | MRLVQLSRHSIAFPSPEGALREPNGLLALGGDLSPARLLMAYQHGIFPWFSPGDPILWWSPDPRAVLWPEKFHLSRSMKRFHNASPYRVTLNYAFDRVIDGCANHRDEGTWITRGIEEAYRRLHELGHAHSIEVWRDRELVGGMYGVSQGALFCGESMFSRQENASKTALLVFCAEFTRHGGKLIDCQVLNSHTASLGAIEIPRRDYLDHLAALRQQPLASRFWVPRTLFLPRK | Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | B5F138 |
Q8FFK3 | NUON_ECOL6 | NDH-1 subunit N | Escherichia | MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGVYLVGYLFSSLGAFGVVSLMSSPYRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSAIGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM | 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 translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q8FFK3 |
B3E2K5 | KTHY_TRIL1 | dTMP kinase | Trichlorobacter | MFITFEGIEGCGKSTQIALLAASLQQAGQRVLLTREPGGCPIADQIRSVLLDAANTALVPMAELMLYAASRAQHLAEVVSPALAEGVIVLCDRFSDATRAYQSFGRGIDRQVIETLNSLACDGISPDLTVLLDCPVETGLGRARQRIDSTSGPREERFELESLAFHQRVRDGYLQLAAEEPGRFVIVDATVQPAQVASAISDAVLSRLAVPV | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. | B3E2K5 |
A1TND9 | ORN_ACIAC | Oligoribonuclease | Acidovorax | MSDTAPVSVPPVLPKSDLNFVWLDCEMTGLDPEKDRLLEIAVVVTGPELEPRVEGPVFAIHQSDALLDGMDAWNKGTHGRSGLIEKVRASTVTEAEAEQAILEFLARYVRKGVAPMCGNSIGQDRRFLVRYMPKLEAFFHYRNVDVSTLKELSRRWKPEVYASFKKAQKHTALADVHESIEELAHYRKHLLVP | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | A1TND9 |
P13564 | GLNA2_HORVU | Glutamate--ammonia ligase | Hordeum | MQVRRDDDGAGGCAGDAVPGGGEGQDGVPARQPAGRVWGVSRAARATSGFKVLALGPETTGVIQRMQQLLDMDTTPFTDKIIAEYIWVGGSGIDLRSKSRTISKPVEDPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNILVICDTYTPQGEPIPTNKRHMAAQIFSDPKVTSQVPWFGIEQEYTLMQRDVNWPLGWPVGGYPGPQGPYYCAVGSDKSFGRDISDAHYKACLYAGIEISGTNGEVMPGQWEYQVGPSVGIDAGDHIWASRYILERITEQAGVVLTLDPKPIQGDWNGAGCHTNYSTLSMREDGGFDVIKKAILNLSLRHDLHIAAYGEGNERRLTGLHETASISDFSWGVANRGCSIRVGRDTEAKGKGYLEDRRPASNMDPYTVTALLAETTILWEPTLEAEALAAKKLALKV | The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration. | P13564 |
P48210 | CH60_BORPE | Chaperonin-60 | Bordetella | MAAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQIIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVAKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAKRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELMENKPAAAPAMPGGMGGMGGMDF | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | P48210 |
Q5L3R4 | RS13_GEOKA | 30S ribosomal protein S13 | Geobacillus thermoleovorans group | MARIAGVDIPRDKRVVISLTYIYGIGKPTAQKILKEAGVSEDTRVRDLTEEELGRIREIVGRLKVEGDLRREVSLNIKRLMEIGCYRGLRHRRGLPVRGQNTKNNARTRKGPRRTVANKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q5L3R4 |
Q136C2 | LEXA_RHOPS | LexA repressor | Rhodopseudomonas | MLTRKQFELLKFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPDLGGNTGGGRRGFTPSVIEGTLGKVRPPSHSHAEDESDRNVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVEAGILDGDMALIQRNESAETGDIVVALIDEEEATLKRFRRRGASIALEPANAAYEVRILPPNRVRIQGKLIGLYRKY | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | Q136C2 |
P57834 | LOLB_PASMU | Outer-membrane lipoprotein LolB | Pasteurella | MVMKKQHFLLPIIASFFLFACTLDTERPTDVKYISHTDPTWQQHLSQLKKIRDYTNQGQLGYISQKERFSTRFDWQYQNPTNYRLTLSSTLSPTTLSIEVRHNVMHLSDNKGPLRSAQDAKRLLKEIVGMDLPLDQFALWLKGQPDESREYRVAENHLLAHFSYPIDNQQWTADYLSYHQLPLPLPKDILLKTEGQTLKIRIDNWTY | Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | P57834 |
A9IMW7 | MIAB_BART1 | tRNA-i(6)A37 methylthiotransferase | Bartonella | MNKVNPKNTSPVAPKKVFIKTYGCQMNVYDSQRMTDSLSSQGYVTTQTPNDADLILVNTCHIREKAAEKLYSDLGRLRVMRQERTPDKPLTVGVTGCVAQAEGSEILRRAPIVDLVIGPQMYHRLPELLEKAKQGKKIIETDYAVEDKFAHLPPHNKRAVRKRGVSAFLTVQEGCDKFCTFCVVPYTRGAEISRSVEQITEEARQLIEAGVKEITLLGQNVNGWHGQSADGKTWRLGDLLYHLAKLDGLKRLRYTTSHPRDMDDSLIAAHRDLDMLMPYLHLPVQSGSDRILKAMNRQHKSSYYLHLIEKIRAARPDIAFSGDFIVGFPGETDEDFEETIKLIQQVQYSSAYSFKYSPRPGTVGATMKNHVDESVKDARLQHLQVLLLEQQNTFLRSKIGQKTDVLIEKPGRHSGQMVGRSPWLLPVVVDTESSTGSVVEIHIKNASSNSFVGEMTNR | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | A9IMW7 |
B5RE15 | GCSH_SALG2 | Glycine cleavage system H protein | Salmonella | MSNVPAELKYSKEHEWLRKEADGTYTVGITEHAQELLGDMVFVDLPEVGATVSAGDDCSVAESVKAASDIYAPVSGEIVAVNDALSDSPELVNSEPYAGGWIFKIKASDESELESLLDATAYEALLEDE | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | B5RE15 |
Q3Z3K7 | MSBA_SHISS | Lipid A export ATP-binding/permease protein MsbA | Shigella | MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDNLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAIDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFGQ | Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. | Q3Z3K7 |
Q146K5 | BIOB_PARXL | Biotin synthase | Paraburkholderia | MTQLNIAPASTDTAAASNNNAAAGTKQLARWRVADIVSLYELPFNDLMFQAQQTHREHFDANTVQLSTLLSIKTGGCEEDCAYCPQSVHHDTGLQADKLMPVDEVLAAAKVAKENGATRFCMGAAWRNPKDRHLEPIKDMIRGVKAMGLETCVTLGMLETHQAQGLREAGLDYYNHNLDTSPEFYGQIISTRTYQDRLDTLERVRDAGINVCCGGIVGLGESRRERAGLIAQLANMDPYPESVPINNLVQVEGTPLTGTEAIDPFEFVRTIAIARITMPRAMVRLSAGREQMNEALQAMCFLAGANSIFYGDQLLTTSNPQAEADRKLLERLGIRAEAAQQMPLDQSGCEHGCDKHAAPN | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | Q146K5 |
Q6A7F0 | CLPP1_CUTAK | Endopeptidase Clp 1 | Cutibacterium | MNAEQAEQAAPGGLAPAGPRNDYYIPQWEERTSYGVRRVDPYTKLFEDRIIFLGTPVTDDIANAVMAQLLCLQSMDADRQISMYINSPGGSFTAMTAIYDTMNYVRPDIQTICLGMAASAAAVLLAAGAKGQRLSLPNSTVLIHQPAMGQATYGQATDIEILDDEIQRIRKLMENMLATATGQSVEQISKDIDRDKYLTAQGAKEYGLIDDILTSL | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | Q6A7F0 |
Q8DF67 | DNAJ_VIBVU | Chaperone protein DnaJ | Vibrio | MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGHARPQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCEGTGAKKGTSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGERGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPSETQTGRMFRMRGKGVKGVRGGAIGDLIVKLVVETPVNLSSRQKELLKEFEESCCGEAATKHKPKSEGFFNGVKKFFDDLTS | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. | Q8DF67 |
Q21WQ0 | NADD_ALBFT | Nicotinate mononucleotide adenylyltransferase | Rhodoferax | MKRIGVFGGAFDPPHVAHAALVKAALAELQLDELRVVPTGEAWHKTRTLSPAPHRLAMAQLAFAELPHVVVDPRELERVGPSYTVDTLREFKALWPTAEFFLILGEDQAQALPSWHDWQEILQLAIICVATRACSTGAGAKFDLETTHKSRFRRLLMPALNVSATDIRARFAAHLSVADMVFEPVARYIAHHHLYQTA | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | Q21WQ0 |
F4IE66 | PRP22_ARATH | Protein ROOT INITIATION DEFECTIVE 1 | Arabidopsis | MPSMAQGELKSFVQNSRPNPKSPTVSPFSMRQKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVSEKTEFGNVASQVQTTTRDANGPQQNGVLKGYQGRKLSPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYTVHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDEIESVERLVQERLQNIPEDKRKLLPLAIFSALPSEQQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEIKRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLENPVGYQMSRLPLEPVYSKALILANQFNCLEEMLITVAVLSVESIFYDPREKREEARTSKNHFASVEGDHLTYLSVYRESDEFLEKRKAAGSGNNIDKIMKKWCKENYVNSRSLKHARDIYRQIREHVEQIGFNVSSCGNDMLAFRRCLAASFFLKAAQRQLDGTYRALESGEVVHIHPTSVLFRAKPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPHHFQTAE | Involved in pre-mRNA splicing. Plays a role during development in processes such as meristem maintenance, leaf morphogenesis and root morphogenesis. | F4IE66 |
Q894H0 | DXS_CLOTE | 1-deoxyxylulose-5-phosphate synthase | Clostridium | MINTLDRYKDVYDIKNMSLDELNLLSRELRNFIIESVSQNGGHLASNLGVVELTLSLYNVFDFSYDKLIWDVGHQCYVHKILTGRRSGFQNLRKINGLSGFPKRCESKFDHFETGHSSTSISSALGMARARDLKGENYNVVAVIGDGALTGGMALEALNDVGDNKTKLTIILNDNQMSIGKNVGGLSTYLSSLRIDPNYNKFKRDVEGIIKKIPNIGKGVAKNLERVKDGVKQVLVPGMLFENMGIKYFGPIDGHNIKQLSKVMDKAKNMKEPVIIHVVTTKGKGYKFAEQNPDKFHGIGSFDYMTGCSKKSKGVTYSKAFGKAMVSIASKDKRVVAITAAMKDGTGLNEFSNKFKNRIFDVGIAEQHAVTMAAGMATAGLRPVFSVYSTFLQRAYDQVLHDVCIQNLPVVFAIDRAGLVGEDGETHQGVFDMSYLSHMPNMTIMAPKCVEELEFMLNWALSQESPIAIRYPKGESRLNLKPIKNFQKGKWEVLEDKGKISIIATGRMVEKAFNVKETLKERNIDIGLINATFVKPIDKEMLNKIIDEEKTIITLEDNVILGGFGNSVLNYVRDTNSNIKVVNLGFKDEFIPHGKVDDLFKMYGLDEEAILKEVMKLM | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | Q894H0 |
P48039 | MTR1A_HUMAN | Melatonin receptor type 1A | Homo | MQGNGSALPNASQPVLRGDGARPSWLASALACVLIFTIVVDILGNLLVILSVYRNKKLRNAGNIFVVSLAVADLVVAIYPYPLVLMSIFNNGWNLGYLHCQVSGFLMGLSVIGSIFNITGIAINRYCYICHSLKYDKLYSSKNSLCYVLLIWLLTLAAVLPNLRAGTLQYDPRIYSCTFAQSVSSAYTIAVVVFHFLVPMIIVIFCYLRIWILVLQVRQRVKPDRKPKLKPQDFRNFVTMFVVFVLFAICWAPLNFIGLAVASDPASMVPRIPEWLFVASYYMAYFNSCLNAIIYGLLNQNFRKEYRRIIVSLCTARVFFVDSSNDVADRVKWKPSPLMTNNNVVKVDSV | High affinity receptor for melatonin. Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. | P48039 |
A5UA08 | ATPD_HAEIE | F-type ATPase subunit delta | Haemophilus | MSELTTIARPYAKAAFDFAIEQSAVEKWTEMLGFAAAVAEDETVKAYLSSSLSAQKLADTVISICGEQLDQYGQNLIRLMAENKRLSAIPAVFEEFKHHVEEHQAIAEVEVTSAQPLNATQIEKIAAAMEKRLARKVKLNCNVDNALIAGVIIRTEDFVIDGSSRGQLTRLANELQL | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | A5UA08 |
B0XM00 | LIS1_ASPFC | Lissencephaly-1 homolog | Aspergillus subgen. Fumigati | MSQLLTARQAEELHKSIIAYLASVNLTESSAALRAELGDSVSIDDATLKKYEGLLEKKWTSVVRLQKKIMDLESRCAALQSELDSATPTSLLRKNQDPTSWLPRSPARHILEGHRNPVTCVAFHPVFSSLASGSDDTTIKIWDWELGELERTVKGHTKAVLDVDYGGPRGGTLLASCSSDLTIKLWDPSDNYKNIRTLPGHDHSVSSVRFIPSGAAGSPMSGNLLVSASRDKTLRIWDVTTGYCVKTLSGHVDWVRAVAPSIDGRFLLAAGDDRIPRLWDLSSAETKSTFLGHEHVIECVAIAPAASYPHLAVLSGLKKPPPASSSAEFFATGSRDKTIRLWDSRGNLIKTLVGHDNWVRALAFHPGGKHLLSVADDKTIRCWDLTQECKCVRVISDAHGHFVTCLRWAPPLIKDGGANGEAETNGTPAATSTTNGVRPDPNVATKISIRCVIATGSVDQKVRIFAT | 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 (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. | B0XM00 |
Q2I2Q5 | CM31_CONLT | Lt3a | Elisaconus | MLKMGVLLFTFLVLFPLTTLELDTDRPVERHAAIKQDLKPQERRGIRLHAPRDECCEPQWCDGACDCCS | Iota-conotoxins bind to voltage-gated sodium channels and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. This toxin enhances tetrodotoxin-sensitive sodium current in rat dorsal root ganglion neurons. | Q2I2Q5 |
Q8FMB0 | PURA_COREF | IMP--aspartate ligase | Corynebacterium | MAAIVIVGAQWGDEGKGKATDILGGLVDYVVKPNGGNNAGHTVVVGGEKYELKLLPAGVLSETATPILGNGVVINLEALFEEIDGLEARGADASRLRISANAHLVAPYHQIMDRVQERFLGKRAIGTTGRGIGPTYQDKVGRVGIRVQDIFDESILRQKIESALDVKNQVLVKMYNRKAIVAEETVQYFLSYADRLRPMVIDATLELNKALDEGKHVLMEGGQATMLDVDHGTYPFVTSSNPTAGGACVGSGVGPTRITSTLGIIKAYTTRVGAGPFPTELFDKWGEYLQTVGGEVGVNTGRKRRCGWYDSVIARYASRVNGFTDYFLTKLDVLTGIGEIPICVAYEVDGVRHDEMPMTQSDFHHAKPIFETMPAWDEDITGCRTFEELPQKAQDYVRRLEELSGARFSYIGVGPGRDQTIVLHDVMES | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q8FMB0 |
B7LLI6 | CRCB_ESCF3 | Putative fluoride ion transporter CrcB | Escherichia | MLQLLLAVFIGGGTGSVARWMLSMRFNPLHQAIPLGTLAANLLGAFIIGMGFAWFSRMTNIDPVWKVLITTGFCGGLTTFSTFSAEVVFLLQEGRFGWAMLNVLVNLLGSFAMTALAFWIFSASTAN | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | B7LLI6 |
Q9M1U4 | TCP16_ARATH | Transcription factor TCP16 | Arabidopsis | MDSKNGINNSQKARRTPKDRHLKIGGRDRRIRIPPSVAPQLFRLTKELGFKTDGETVSWLLQNAEPAIFAATGHGVTTTSNEDIQPNRNFPSYTFNGDNISNNVFPCTVVNTGHRQMVFPVSTMTDHAPSTNYSTISDNYNSTFNGNATASDTTSAATTTATTTV | Required during early processes in pollen development. | Q9M1U4 |
B5YHP1 | KAD_THEYD | Adenylate monophosphate kinase | Thermodesulfovibrio | MRLVFLGAPGAGKGTQAKRLVEKYGIPQISTGDLLRAAVAAGTPLGKEAKAYMDRGELVPDKVVLGMVKERLSQNDCKKGFILDGFPRNVAQAEALDKMLSEMNMPLDLALNLDVPFDDLMKRLTGRRTCKSCGQMYNVYYSPSKVEGKCDKCGGELFQRDDDKEETIRKRLEVYRAQTEPLIDYYSKKGILKSVSGTGSIDEIFNSICAILEKK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | B5YHP1 |
Q9B5Q7 | CYB_CEPSP | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Cephalophus | MTNIQKTHPLMKIVNNAFIDLPTPSNISSWWNFGSLLGICLILQILTGLFLAMHYTADTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYAYTETWNIGVILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFIFPFIIAALAMVHLLFLHETGSNNPTGISSDADKIPFHPYYTIKDILGALLLILALMILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILVLMPLLHTSKQRSMMFRPISQCLFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLLILVLMPMASTIENNLLKW | 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 then used for ATP synthesis. | Q9B5Q7 |
O27231 | MTRE_METTH | N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E | Methanothermobacter | MDPMITGLGVVALMGAAATIAGAAEDLESDVGSQSNPNSQVQLAPQMGHLHRIINKAVSGEPVAYGTWCGIAGSVAYVLMQSMQLPVIMAIAVGAVIAAMVHTTYAVTSHMGRIVSQSQFNQPLFMDMLVQHLGPIAGHGFIVTFCIVGLSYLMTLPIPGFAHPFPLPLLAVLWGITIGAIGSSTGDVHYGAEREYQQYPFGGGIPVAIHGDITTKAELGARNSMDVVHFCAKYGGPLTGFAFGAIVFLSFWNTIVFGITGGIISGLIIVLLLIILNNRLEVFARNRYGPYKEDE | Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. | O27231 |
Q11QB9 | RL16_CYTH3 | 50S ribosomal protein L16 | Cytophaga | MLQPKRTKYRKQQKGRVTGVATRGHRIAFGSFAIKSLEGGWITARQIEAARIAMTRAMKREGQVWIRVFPDKPITQKPAEVRMGKGKGAPEYWVACIKPGTILFESGGVSIETAQESLRLAAQKLPFKTKFIVRPDYVAS | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q11QB9 |
P0DMZ9 | TX9A2_ANEVI | Peptide toxin AV-2 | Anemonia | MKSIFLVFFAVCLVKAEAGKGRKREPNIINPPCRECYVQDSSGNCVYDKWGCGGARKREPNIINPPCRECYVQDSSGNCVYDKWGCGGARKREPNIINPPCRECYVQDSSGNCVYDKWGCGGARKREPNIINPPCRECYVQDSSGNCVYDKWGCGGARK | Inhibits ion channels. | P0DMZ9 |
P13738 | NHAA_ECOLI | Sodium/proton antiporter NhaA | Escherichia | MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNMLLWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPALLYLAFNYADPITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLSMASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLKEKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLQGVTLDGLTSILPLGIIAGLLIGKPLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINWAKLGILVGSISSAVIGYSWLRVRLRPSV | Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons . Plays an important role in the regulation of intracellular pH, cellular Na(+) content and cell volume . Catalyzes the exchange of 2 H(+) per Na(+) . This stoichiometry applies at both neutral and alkaline pH values . In addition, can also transport lithium and is involved in lithium detoxification . Binding of the Li(+) and H(+) ligands to NhaA is coupled and antagonistic . | P13738 |
Q7ZU13 | SPNS1_DANRE | Spinster-like protein | Danio | MSQADADITPFFADDNEGEGPVENGVGSPLPEDEEEESPSGVTDRRAIMTVIVLCYINLLNYMDRFTVAGVLPDIEHFFGIGDGTSGLLQTVFICSYMFLAPLFGYLGDRYNRKLIMCVGIFFWSVVTLASSFIGKDHFWALLLTRGLVGVGEASYSTIAPTIIADLFVKEKRTNMLSIFYFAIPVGSGMGYIVGSKVDTVAKDWHWALRVTPGLGLLAVFLLMLVVQEPKRGAIEAHPEHTLHRTSWLADMKALCRNPSFILSTFGFTAVAFVTGSLALWAPAFLFRAGVFTGVKQPCFKAPCDDSDSLIFGAITVVTGILGVASGVQASKLLRTRTPRADPLVCAAGLLLAAPFLYLSIMFAQASTVATYVFIFLGETFLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAISPYLIGVVSDSIKESNSYMWEFRSLQMSLLLCSFVAVAGGAFFLATAVFIEKDRDLAENYVPSDDAPIVVPRSGRSTKVSVSSVLI | Sphingolipid transporter. | Q7ZU13 |
C3PMH4 | RL1_RICAE | 50S ribosomal protein L1 | spotted fever group | MSNKKDVAVKISGGKKIREAREKVKSDTLYNLTNAVERLKSASYVKFDPTLEIVMKLGIDSRHSDQMVRGVVNLPAGTGKTVRVAVICKEEREEEAKSAGADLVGSTNIIDEIKAGKINFDVCIATPDMMVAIGSVARILGPKGLMPNPKLGTVTLDIKNAIKNAKSGQVEYRAEKAGIIHAGLGKLSFSDQDLLKNLNAFIEAVIKAKPAGLKGSYLKAMYLSSTMGASVQIDLTSIA | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | C3PMH4 |
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