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 |
|---|---|---|---|---|---|---|
Q02PS5 | ACCD_PSEAB | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Pseudomonas | MSNWLVDKLIPSIMRSESQKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCDHHMRINARTRLDIFLDEDGREELGADLEPVDRLKFRDSKKYKDRLAAAQKDTGEKDALIAMSGKLQGMPVVACAFEFSFMGGSMGAIVGERFVRAANVALEKRCPLICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFVSVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIVHRAELRPRLANLLSAFTHSPSPVSA | 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. | Q02PS5 |
A1JLU9 | PGSA_YERE8 | Phosphatidylglycerophosphate synthase | Yersinia | MQLNIPTWLTLFRVVLIPFFVLAFYLPFVWAPMVCAIIFVFAAATDWFDGFLARRWKQTTRFGAFLDPVADKVMVAIALVLVAEHYHVWWITLPAATMIAREIIISSLREWMAEIGKRSSVAVSWIGKVKTTAQMGSLVGLLWRPDHNIELASFVLLYIAAVLTFWSMFQYLNAAWKDLLEP | This protein catalyzes the committed step to the synthesis of the acidic phospholipids. | A1JLU9 |
Q7NEK2 | DCUP_GLOVI | Uroporphyrinogen decarboxylase | Gloeobacter | MTQSLLLDAARSKPVARPPVWMMRQAGRYMAEYRALRDKYGFKERCENPDLAVEISLQPFRAFRPDGVIMFSDILTPFDGMGIPFELVESRGPVIDPPIRTREQVEAVRPLDPEASLAFVRTILQTLRREVGEAATVLGFVGAPWTLAAYAVEGKSSKDYALIKQMAFSEPDLLHALLTKFADAIARYVIFQIDSGAQAVQLFDTWAGQLNPADYRAFALPYERRIVEQVRQVHPETPLILYINHSAGLLRHVGESGVDVMSLDWTVDMAEARAILGPDMAVQGNLDPCVLLGDQAQIRSRILDIVEKAGPTGHIMNLGH... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q7NEK2 |
P22389 | EDN2_MOUSE | Vasoactive intestinal contractor | Mus | MVSAWCSIALALLLALHEGKGQAAATLEQPASAPKGRGPHLRFRRCSCNSWLDKECVYFCHLDIIWVNTAGQTAPYGLGNPPRRRRRSLPKRCECSTAGDSACATFCHRRHWPEAVVAPSSQAPAAVLKTGKMWTAEGDLLRKLRDISATKLRFARLQPEVTRKAIPAYSRWRKR | Vasoconstrictor. | P22389 |
Q830Q5 | RL11_ENTFA | 50S ribosomal protein L11 | Enterococcus | MAKKVEKIVKLQIPAGKATPAPPVGPALGQAGINIMGFTKEFNARTADQAGLIIPVVISVYEDRSFTFITKTPPAAVLLKKAAKIEKGSGEPNKTKVATVSSDQVKEIAELKMADLNAADVEAAMRMVAGTARSMGIIVE | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q830Q5 |
B8HTV6 | BIOF_CYAP4 | 8-amino-7-ketopelargonate synthase | unclassified Cyanothece | MDSHPYAWIEAALETVKRAHWYRSVQTIEGRPGAEVELAGQRVLNFASNDYLGLAGDQRLIRAAIQATEQLGTGSTGSRLLTGHRELHRQLERAIAQLKQTEDALVFSSGYLANLGTIAALVGPRDLILSDQYNHSSLKKGASLSGAKVLDYPHLDMGGLAELLQTHRSNYRRCLILTDTVFSMEGDVCPLPQLLAITTAHNAMVLVDEAHATGVLGATGAGAVEHWGCTDQTLIQVGTLSKALGSLGGYVAGTAVLIDFLRNRCPGWIYTTALSPADTAAALAAIAVVQSEPQRRIQLHENVQGVQAQLQNLPQLQEPR... | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | B8HTV6 |
Q39315 | ACBP_BRANA | null | Brassica | MGLKEDFEEHAEKVKKLTASPSNEDLLILYGLYKQATVGPVTTSRPGMFSMKERAKWDAWKAVEGKSTDEAMSDYITKVKQLLEAEASSASA | Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. | Q39315 |
Q2NJ01 | SYP_AYWBP | Prolyl-tRNA synthetase | Candidatus Phytoplasma asteris | MKTMKRVKTVATRLSDFGKWYTDICLKAELIAYSEAKGFIIYLPYGYALWENIQKHLNCTLQKTGHQNVYFPLVFPEKLFHKEKEHIQGFSPEAAMITTTGKKNLSEKLVIRPTSEILFSQYYSKTITSYRDLPKLYNQWCNVVRWEKTTKPFLRGKEFLWQEGHTVHATEQEAMQQTLSILDIYQKLGKDLLALPFVCGKKTETEKFAGALITYSIEALMHDGQALQAGTSHYLGIIFAKSFQIQFQDCDNQKKYAHQTSWGVSTRLIGALIMVHSDDEGLVLPPYVAPMQIVIIPLQTQDESVKQVSENLFSILQKNY... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). | Q2NJ01 |
C0QW63 | ATPD1_BRAHW | F-type ATPase subunit delta 1 | Brachyspira | MKESDKLQILKPTASAIFDIARELGMIKEIYNELSECSKLFQDIDIKKYFFDKSISKKDKKELIDKRLKPILSKETYAFVSILTEHDSIDVLPDIVALYKEIADDYSNIVRVRIITASTIDDKTVEDIIQTVKCFSSNEISYETIVDENIIGGIIVYIGSVVYDYSIKKQIDLLQSKFTYGN | 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. | C0QW63 |
Q630E3 | RLMH_BACCZ | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Bacillus cereus group | MNISIISIGKLKEKYLKQGIAEYLKRLSAYAKVEVIELPDEKAPENLSEAEMLIVKEKEGIRILDKISDDTHVIALAIEGKQKSSEEFAVSLDRLATYGKSKVAFVIGGSLGLSSEVMKRSNESLSFSKMTLPHQLMRLVLLEQVYRAFRINRGEPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q630E3 |
C0RJS3 | COBQ_BRUMB | Cobyric acid synthase | Brucella | MARAIMFQGTGSDVGKSVLVAGLCRVARNRGLKVRPFKPQNMSNNAAVSDDGGEIGRAQWLQALACGVPSSVHMNPVLLKPQTDMGSQLIVQGQVRGEARGRYYQELKPQLMAAVMESFAKVGDGADLVLVEGAGSPAEINLRAGDIANMGFATHADVPVVLVGDIDRGGVIASLVGTHTILPQEDRAMVRGFLINKFRGDISLFDDSLAAITRFTGWRSFGVVPWLKAVSRLPAEDSVVLERAVRGDKKALIVAVPMLPRIANFDDLDPLKAEPAVEVVMVPPGSSLPADAGLVVLPGTKSTIADLLALRENGWDRELV... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | C0RJS3 |
A1AAA8 | DSBB_ECOK1 | Disulfide oxidoreductase | Escherichia | MLRFLNQCSQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALIGAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMARFPEWLPLDKWVPQVFVASGDCAERQWEFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR | Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. | A1AAA8 |
A7ZER3 | LGT_CAMC1 | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Campylobacter | MEIWNDIYNHFNPVAFSIFGFSVHWYGLMYILALVLALAMAKYLVKKDDIPISSQLLDNYFFWVEIGVILGARLGWVLVYSGEAGYYLTQPWQIFNPMHNGEFIGIRGMSYHGAVVGFLLATILFCKRYKQNAWQLLDLCAICIPFGYTFGRIGNFLNQELFGRVTDVPWAINVFGQPRHPSQLYEAFLEGLVIFVILFLYRKYKKFNGELIALYAILYTFARFICEFYREPDSGLGFIIFGLSMGQILSLIMCGFGIFVYIKLYKRFTKI | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | A7ZER3 |
P48548 | KCNJ5_RAT | Potassium channel, inwardly rectifying subfamily J member 5 | Rattus | MAGDSRNAMNQDMEIGVTSQDHKKIPKQARDYIPIATDRTRLLPEGKKPRQRYMEKTGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTITWLFFGFIWWLIAYVRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINEKSPFWEMSRAQLEQEEFEVVVILEGMVEATGMTCQARS... | This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the volt... | P48548 |
Q8C160 | MSLNL_MOUSE | Pre-pro-megakaryocyte-potentiating-factor-like | Mus | MSRTLRPSAMGSRVGALASPGLALLLSLTAHCSGPQAKGLPKGGLNASEANTWVRNNTSLLQNFWCLPASQLPREQLSSLIRSLASQRVALKAWQLSCLANLAAQLGLQDDFEFHPPNLLLFYDLSQVGDTNCRAFIHHAAQGDTELLTNLPNQRVALQRTALACLGGPHLQLSASDLWLLGVLVCDMEAAQIVTADPSVLRNLLRCPRLTVMQTAALNTLLASGKTQIGPPGSWNLQGLQALGLLATYISPHLWEKVQEAVGLDFFRSVVAACRAGQLSRHDARRFVDNFLESKATSVSSRPKRRTGRSCVRGNITAAT... | May play a role in cellular adhesion. | Q8C160 |
P61988 | CBID_METMP | Cobalt-precorrin-6A synthase | Methanococcus | MGKIDFRLEKTFGYTTGACAAAGAFSALYFLKNNEKLRFVEILNLKGDSLIIPIKNIEKQKNTAISTVEKFSGEDIDITNGMDIKIEVTLEKLDNNSSKSSSVKIIGGDGVGIVTKSGLQVNPGEYAINPKPREMIENNLKSLLENDECVTAKISVPNGDEIAKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLAPQIDVALAYNFENLIFVPGNIGTKHAKILLNAKEDQIIEVSNFWDYMLDKAKEKGVKDITVFGHAGKIVKLAGGIFDTHSRVADARNEILCAYTSLITQDVEMLQKILQSNTTEDIVEILT... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | P61988 |
Q88B46 | TSAC_PSESM | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Pseudomonas | MVSSWRVQQAAQNIRAGAVIAYPTEAVWGLGCDPWDEEAVYRLLAIKLRPVEKGLILIADNIRQFDFLFEDFPELWLDRMASTWPGPNTWLVPHQNLLPEWITGIHETVALRVTDHPTVRELCALVGPLISTSANPAGRPAARSRLRVEQYFRGQINGVLGGSLGGRRNPSVIRDIATGQVMRAG | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | Q88B46 |
B3WEQ7 | DNAK_LACCB | Heat shock protein 70 | Lacticaseibacillus | MSKVIGIDLGTTNSAVAVLEGNQPKIITNPEGNRTTPSVVAFKDGEIQVGEVAKRQAITNPDTIVSIKRHMGEANYKVKVGDKEYTPQEISAMILQYIKKFSEDYLGEPVKDAVITVPAYFNDSQRQATKDAGKIAGLNVQRIINEPTASALAYGLDKGDKDEKILVYDLGGGTFDVSILQLGDGVFEVLSTNGDTHLGGDDFDNKIIDWLVAEFKKDNNIDLSKDKMAMQRLKDAAEKAKKDLSGVTQTQISLPFISAGPNGPLHLERTLTRAQFDEMTADLVAKTKIPVENALKDAKLTNADIDKVILNGGSTRTPAV... | Acts as a chaperone. | B3WEQ7 |
Q381M1 | TUT4_TRYB2 | RNA uridylyltransferase 4 | Trypanosoma | MPPSPAVVGRSLVNSFKQFVSKDLHTRHVDATYRLVLDCVAAVDPLMRLYTFGSTVVYGVHEKGSDVDFVVLNKTDVEDGKGGDAATQVAKGLQADILAKLARVIRQKHLSWNVEEVRRTRVPVVRVKGGGAVDFDITAYRRNGVRNSALLRAYFEQNPPCRWLSMSIKRWSKQTGLNASVIGGSITSYGFNLMVVYYLLQRNHLQFVPPSTIDVSRVEPLPPHLPLEEPADEGLELGTQVLDFLHFFLHEFDSDKQVISLNRPGITTKEELDWTKSAEDFARMNGEKVHYQWCIEDPYELNLNVGRNVTPLKRDFLRRH... | Terminal uridylyltransferase which, specifically, catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U. | Q381M1 |
O46512 | CP19A_HORSE | Estrogen synthase | Equus | MILEMLNPMHYNLTSMVPEVMPVATLPILLLTGFLFFVWNHEETSSIPGPGYCMGIGPLISHLRFLWMGLGSACNYYNKMYGEFVRVWISGEETLVISKSSSTFHIMKHDHYSSRFGSTFGLQYMGMHENGVIFNNNPAVWKALRPFFVKALSGPSLARMVTVCVESVNNHLDRLDEVTNALGHVNVLTLMRRTMLDASNTLFLRIPLDEKNIVLKIQGYFDAWQALLIKPNIFFKISWLSRKHQKSIKELRDAVGILAEEKRHRIFTAEKLEDHVDFATDLILAEKRGELTKENVNQCILEMMIAAPDTLSVTVFFMLC... | A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo... | O46512 |
A0A2I1BSW8 | NVFC_ASPN1 | Short chain dehydrogenase nvfC | Aspergillus | MGSLHDYVLIITGSASGIGLATATIALDEGARVLGVDISSPPRSLIDHSNFKFVEGNLSLEPTPRRVVEACVKAFGGRIDGLLNIAGVMDLNQSVDSLSDTMWESCIAINLTAPVKLMREVIPIMRQQKSGSIVNVASKAALSGAVSGVAYTASKHGLVGATKNVAWRFKQENIRCNAVCPGAVDGTSIHRGLETSQFDSEALGTMSLIHEAHMRDRERGIHIQPEDIARSLLFLVSSRSNGINGAIIPIDNAWSTI | Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one a... | A0A2I1BSW8 |
Q4WVS2 | BCP1_ASPFU | Protein bcp1 | Aspergillus subgen. Fumigati | MGKRKELKDNDVEMGGTGRPVEDDESDEVMDIVNVDFEWFDPQPAVDFHGLKNLLRQLFDADSQIFDLSALTDLILAQPLLGSTVKVDGNESDPYAFLTVLNLQEHKDKPVIKDLTSYLQRKASSNPSLAPLSQLLSQSPIPPIGLILTERLINMPAEVVPPMYSMLLEEIAWAIEDKEPYNFSHYLIVSKTYEEVESKLDMEESRPQKKKKKSGSNVERFFFHPEDEVFERHAICSGSIEYTHKHDDGLSDSKRAFQDLGIKTSGSLILIDGPKLEAAVKDVTDYVKPPV | Involved in nuclear export, actin cytoskeleton organization and vesicular transport. | Q4WVS2 |
Q0AX14 | RUVC_SYNWW | Holliday junction resolvase RuvC | Syntrophomonas | MKVLGIDPGTATTGYGLIRSEAGRVKAITYGTIVTPAQLEMPLRLYQIYRELQALLMEYKPDAVAVEEIFYNRNSKTVITVAQSRGVILMTAAAAGIPVAEYTPLQVKQAVVGYGAAEKKQVQLMVQKILGLQQLPRPDDAADALAVAICHLHSYRLSSFLESSATKAGEKR | Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | Q0AX14 |
A4QLT3 | PSAA_NASOF | PsaA | Nasturtium | MIIRSPEPEVKILVDRDPIKTSFEEWAKPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYSEFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGIK... | PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically... | A4QLT3 |
A9BD87 | RISB_PROM4 | 6,7-dimethyl-8-ribityllumazine synthase | Prochlorococcus | MVSIEGRFNDASNFRIAIVVARFNDLITNKLLSGCIDCLQRHGVDTSESSPQLDIIWVPGSMELPLICQSLASKGKYQVLITLGAVIRGDTPHFEVVINESSKGIASVARENGIPIIYGVLTTDTMQQALERAGIKSNLGWNYALQALEMASLMKALR | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. | A9BD87 |
Q3AW32 | GLMM_SYNS9 | Phosphoglucosamine mutase | unclassified Synechococcus | MVQAAFSPVGPTLGDAIPGFGTDGIRGRVGSVVTPALCLQVGYWVGRVLAVEGPVLIGMDSRTSGSMVASALTAGLTAAGREVWNLGLCPTPAVPLLIRKFGAAGGLMVSASHNPPADNGIKVFGANGAKLAPERQARIEAGLRGEIDHSDHDHSLCAGLRQSSDLMADYRELLLSAVGSHRLDGVPIVLDLCWGSATACAADAFQALGADLTVLHGEPDGSRINVGCGSTALGPLQEAVKERGAVMGFAFDGDADRMLAVDGRGRIVDGDHVMFLWGSVLQEQQALPDQRLVATVMSNLGFQRAWEQRGGILERTPVGD... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q3AW32 |
Q7MYH2 | RS13_PHOLL | 30S ribosomal protein S13 | Photorhabdus | MARIAGINIPDQKHTVIALTSIYGIGKTRSQAICAAAGIAEHVKISELSEEQIDKLRDEVAKYVVEGDLRREVTLSIKRLMDLGTYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK | 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. | Q7MYH2 |
O17731 | SAT_CAEEL | Thialysine N-epsilon-acetyltransferase | Caenorhabditis | MKNFEIVTVTPDHAEQLISMIHELAEFEKMKSSVVNTAEKLRKDIENKAVHGFIAFIGEEPAGMNLFYYAYSTWVGQYLHMEDLYIRPQFRRMGLARTLWKKLAELARDKGIVRLEWAVLDWNKNAIALYDTVDYVNLTKSEGWFTFRMDGAAINKFADE | Catalyzes the N-acetylation of the amino acid thialysine (S-(2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur . Substrate specificity: thialysine > O-(2-aminoethyl)-L-serine > S-(2-aminoethyl)-D,L-homocysteine . Does not act on polyamines, such as spermidine and spermine... | O17731 |
Q30SG7 | TRMB_SULDN | tRNA(m7G46)-methyltransferase | Sulfurimonas | MPHLHIAEFKEVEIPSSKDGVSFNFIAKNSSHQEEKLISITVDEDEFFLLAIDENSKKLLKSDKLTRPPSIFNVHKALLSYASATCMNIISSNVPQNQKNIHLREVKALKDINYFATTFPKKEKICIEVGFGSGRHLLHQAQNNPNILYIGIEIHTPSIEQLLKQISIKNIENILVLNYDARLFMELVPSNKIDKIYVHFPVPWDKKPHRRVISTAFIEEARRILNIGGTLELRTDSENYYAYSYETFIAFEKTTLHINKNRDIAITSKYEDRWKRMQKNFYDVTMINSEESPELSLEGDFNFSHVKLNTQEVINLYKKT... | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q30SG7 |
C4JYP8 | RSSA_UNCRE | 40S ribosomal protein S0 | Uncinocarpus | MAPSNLPPVFNATSQDMEMLLAAQCHLGSKNLQVHMDPYLWKTRPDGINVINIGKTWEKIVLAARIIAAIDNPADICVISARPYGQRAVLKFAAHTGAVAIAGRFTPGSFTNYITRSFKEPRLIIVTDPRTDAQAIKEASYVNIPVIALCDTDSPTEYVDVAIPTNNKGRHAIGLVWWLLAREVLRLRGTLATRETEWDVVVDLYFYRDPEAEEAKELEEAKAAGVDEIGPGAVESGFGAEGWEASAGTAFGAAAATTTTTNPATATATWEATGGDWASSAPAEGWAGEAPATEAKW | Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. | C4JYP8 |
Q9SUB1 | DOF42_ARATH | Dof zinc finger protein DOF4.2 | Arabidopsis | MNNLNVFTNEDNEMNVMPPPRVCPRCYSDQTRFSYFNNNKKSQPRYKCKNCCRCWTHGGVLRNIPVTGICDKSNLPKIDQSSVSQMILAEIQQGNHQPFKKFQENISVSVSSSSDVSIVGNHFDDLSELHGITNSTPIRSFTMDRLDFGEESFQQDLYDVGSNDLIGNPLINQSIGGYVDNHKDEHKLQFEYES | Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence. | Q9SUB1 |
Q5E8A2 | RL5_ALIF1 | 50S ribosomal protein L5 | Aliivibrio | MAKLHDYYKSSVVAELTKEFSYTSVMQVPRVEKITLNMGVGEAINDKKLLENAAADMAIISGQKPLITKARKSVAGFKIREGYPIGCKVTLRGERMWEFLERLISIALPRVRDFRGVSAKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTSANTDAEGRALLAAFNFPIP | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement... | Q5E8A2 |
P01129 | CDC10_SCHPO | Start control protein cdc10 | Schizosaccharomyces | MASANFIRQFELGNDSFSYQKRPEDEPSQPLSNRNINKLNDSSTLKDSSSRIFINSQVLRDGRPVELYAVECSGMKYMELSCGDNVALRRCPDSYFNISQILRLAGTSSSENAKELDDIIESGDYENVDSKHPQIDGVWVPYDRAISIAKRYGVYEILQPLISFNLDLFPKFSKQQQIESSSISKNLNTSSFNTRSPLRNHNFSNPSKSSKNGVHTINNMQSSPSPSSSFLLPLTQIDSQNVKRSNNYLSTSPPILEQRLKRHRIDVSDEDLHPSSQLNDNEASSLFPDTPRLNHSLSFVSLVSSLPPLDQNIMQDYHTS... | Major component of the cell cycle transcription factor complex MBF (MCB binding factor, also known as DSC1), that controls G1-S phase specific gene expression. Involved in the control of rRNA production, via interaction with pol5. May be involved in the transcriptional regulation of the cdc22 and cdt1 genes. In fission... | P01129 |
Q9H2A9 | CHST8_HUMAN | N-acetylgalactosamine-4-O-sulfotransferase 1 | Homo | MTLRPGTMRLACMFSSILLFGAAGLLLFISLQDPTELAPQQVPGIKFNIRPRQPHHDLPPGGSQDGDLKEPTERVTRDLSSGAPRGRNLPAPDQPQPPLQRGTRLRLRQRRRRLLIKKMPAAATIPANSSDAPFIRPGPGTLDGRWVSLHRSQQERKRVMQEACAKYRASSSRRAVTPRHVSRIFVEDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTADIQHNTVHYGSALKRLDTFDRQGILHRLSTYTKMLFVREPFERLVSAFRDKFEHPNSYYHPVFGKAILARYRANASREALRTGSGVRFPEFVQYLLDVHR... | Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbe... | Q9H2A9 |
Q4KFT5 | LPXK_PSEF5 | Lipid A 4'-kinase | Pseudomonas | MALSDRLLNAWYNGHPALKLLRPLECLYRRVVTGKRQRFLAGEGAIYQPPVPLIVVGNITVGGTGKTPLILWLVEHCQRLGLRVGVVSRGYGAKPAQLPWRVSAEDCAAVAGDEPLLIVQRCGVPLMIDPDRGRAVQALLAAEPLDLILSDDGLQHYRLARDLELVLIDAARGLGNRRCLPAGPLREPAERLQSVDAVLYNGAVDDRDDGFAFHLKPSVLVNLRSGERRALEHFAPGQALHAVAGIGNPQRFFNTLETLHWRPVPHAFADHAQYSAQALTFTPSLPLVMTEKDAVKCRAFAADDWWYLAVDAQPSPAFVA... | Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). | Q4KFT5 |
Q7VQD2 | RL18_BLOFL | 50S ribosomal protein L18 | Candidatus Blochmannia | MNKKLLRARRALKLRKKLYLLGSVRLVVYRSLRHMYAQIVSEDNCNVLVAASTTEKLIASKLRVTGNKEAAAVVGQVIAERAFKKGIVHVSFDRSGFKYHGRVQILAEYARQFGLKF | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | Q7VQD2 |
Q0HK79 | TRPD_SHESM | Anthranilate phosphoribosyltransferase | Shewanella | MSATSIQPLLDILFQGKALTREQTASLFSTLIQGEMNEAVMAGMLMALKIRGETIAEISGAADAMRAAAKPFPYPSSMRTEGIIDIVGTGGDGFNTINISTTAAFVAAAAGAKVAKHGNRSVSSKSGSSDLLAQFGIDLTMSPELASRCLESLNLCFLFAPHYHGGVKHAVPVRQALKTRTIFNVLGPLINPARPEFMLLGVYSPELVTPIARVLQALGTQRAMVVHGSGLDEVALHGSTQVAELKDGEIIEYQLTPADFGVPQAQMSELEGGEPAQNAQITQSILQGQGSDAHTHAVAINAGCALYLCGLSDSVKAGTA... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q0HK79 |
Q2IL11 | NUOA_ANADE | NUO1 | Anaeromyxobacter | MLTPLQIYFPIGVVLLVAVVLAFTMLGLANVLGPRRPSLVKQTPFECGSEPIGSARERFGVKFYVVALLFIVFDIEAIFLYPWAVLLLPDGQGYPGLGWPGFISMGIFVFTLVAGLVYVWKKGVLDWAD | 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... | Q2IL11 |
P56707 | SMTA_ASTBI | Selenocysteine methyltransferase | Astragalus | MSSPLITDFLHQAGRAAVIAGGLGTELQRHGADLNDPLWSAKCLLSCPHLIRQVHLDYLENGADIIITASYQATIQGFKAKGFSDEEGEALLRRSVEIAREARDLYYQRCAESSSDNGDDSRILKQRPILIAGSVGSYGAYLADGSEFSGNYGDAIKSETLKDFHRRKVQILADSGVDLLAFEAVPNKLEAQAYADLLEEENIITPAWFAFTSKDGNNVVSGDSIEECGSIAESCDKVVAVGINCTPPRFIHDLILLLKKVTAKPIVIYPNSGETYDAIRKEWGQNSGVTDEDFVSYVDKWCESGASLVGGCCRTTPDTI... | Catalyzes the methylation of selenocysteine with S-methylmethionine as donor. Does not methylate cysteine. | P56707 |
A0KR66 | TSAC_SHESA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Shewanella | MLQLHPSEIKDLVLNGGVIAYPTEAVYGLGCDPDNDTAIQKLLAVKQRPWQKGLILVASEFSQLVDYVDESQLSAEQLEFAFSKWPGPFTFVMPIKPHVSRYLCGEFDSIAVRVSAHDGVRALCQALGKPLVSTSANLAGEDPALSGDEILNAFEGKIDALVLGALGEQRQPSTIIDARSGKILRNGQ | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | A0KR66 |
O03812 | CYB_DELLE | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Delphinapterus | MTNIRKTHPLMKILNNAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTSTAFSSVAHICRDVNYGWIIRYLHANGASMFFICLYTHIGRSLYYGSHTSQETWNIGVLLLLMVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGNTLVEWIWGGFSVDKATLTRFFTFHFILPFIITALVAVHLLFLHETGSNNPTGIPSNMDTIPFHPYYTIKDILGALLLILTLLTVTLFTPDLLGDPDNYTPANPLNTPAHIKPEWYFLFAYTILRSIPNKLGGVLALLLSILILLFIPMLQTSKQRSMMFRPL... | 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... | O03812 |
Q2YUL2 | THIE_STAAB | Thiamine-phosphate pyrophosphorylase | Staphylococcus | MFNQSYLNVYFICGTSNVPSHRTIHEVLEAALKAGITLFQFREKGESALKGNDKLVLAKELQHLCHQYNVPFIVNDDVSLAKEINADGIHVGQDDAKVKEIAQYFTDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKHDAHTPVGPEMIATFKEMNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFFNN | 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). | Q2YUL2 |
Q24Q31 | CBID_DESHY | Cobalt-precorrin-6A synthase | Desulfitobacterium | MGGAADMRKKTKDRHSWKTGFTTGSCAAGAAKAACLLLKGLHQGTEVDIPLPQGERLQLPVHRWDRVEDVAWVSIIKNAGDDPDVTHGLEVVARVQLLSQRGEILIRGGRGIGVVTKKGLQIPPGESAINPVPRSMIQAAVREVFPQEEILVVIEVPEGERLALKTLNPRLGIMGGVSILGTTGIVRPMSEEAFKNSILPELDQAVAYGHKAIVLTPGNYGFKVAREQLMVPEEAIIQMSNFVGFLLEEAAYRKIEKVLLLGHIGKLIKVAGGIFHTHTHVADARMEILVAHAALAGMDQNSLQTIAELPTVEGAAEEIR... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | Q24Q31 |
K0E3U5 | ECDK_ASPRU | Echinocandin B biosynthetic cluster protein K | Aspergillus | MSVLTLDFTKFHSGSEVERRAFGQALLDGFTTTGFVKLINHGFSKEEMADIFNWNQRFFDLPIDRKAAIRNDEGPKPQRGWSSLGAEKTGFLNPGGKLSLARASNNDRQDAKEHFDIGPAEDEEFQNKWPEEQTLPGFQETMNSYFDRSQAITLELLEALALAMDVPKDTFVGLCHGHASELRLNHYPSIPVKTIEEGKTNRIWPHTDFGIITLLAQDDIGGLEIQDRNHPSDFLPVNREDSTEFVVNIGDILERWTNGRLRAGLHQVTTPRSMQQKGNGTLPTRRSVAFFLKPHRQMSVASISHFVPGNQSPRYEDMTA... | 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of echinocandin B, a fungal lipidated cyclic hexapeptide that acts as an antifungal agent . Linoleoyl-AMP, produced by the fatty-acyl-AMP ligase ecdI, is transferred to the initiation carrier domain (T0) of ecdA . The linoleoy... | K0E3U5 |
O31518 | YESO_BACSU | Putative ABC transporter substrate-binding protein YesO | Bacillus | MKKICYVLLSLVCVFLFSGCSAGEEASGKKEDVTLRIAWWGGQPRHDYTTKVIELYEKKNPHVHIEAEFANWDDYWKKLAPMSAAGQLPDVIQMDTAYLAQYGKKNQLEDLTPYTKDGTIDVSSIDENMLSGGKIDNKLYGFTLGVNVLSVIANEDLLKKAGVSINQENWTWEDYEKLAYDLQEKAGVYGSNGMHPPDIFFPYYLRTKGERFYKEDGTGLAYQDDQLFVDYFERQLRLVKAKTSPTPDESAQIKGMEDDFIVKGKSAITWNYSNQYLGFARLTDSPLSLYLPPEQMQEKALTLKPSMLFSIPKSSEHKKE... | May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. | O31518 |
A8GH04 | NUON_SERP5 | NDH-1 subunit N | Serratia | MTITPQQLIALLPLLIVGLTVVVVMLGIAWRRDHFINATLTVIGLNLALLSLYFVGQAGPMDVTPLLRVDGYSMFYTGLVILASLATCTFAYPWLVGYPDNREEFYLLVLIATLGGILLASANHLASLFLGIELISLPLFGLVGYAYRQKRPLEAAIKYMLLSAAASSFLLFGMALLYAESGDLSLAGLGKSLQENMMHQPLVLAGMGMMIVGLGFKLSLVPFQLWTPDVYQGAPAPVSTFLATASKIAIFAVVMRLFLYAPAADNEALRMVLSIIAVCSILFGNLMAISQTNIKRLLGYSSIAHLGYLLVALIAVQTHQ... | 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... | A8GH04 |
B0KP99 | UBID_PSEPG | Polyprenyl p-hydroxybenzoate decarboxylase | Pseudomonas | MQYRDLRDFIRGLEQRGELKRIQVPISPVLEMTEVCDRTLRAKGPALLFEKPTGFDIPVLGNLFGTPERVAMGMGAESVDELREIGKLLAFLKEPEPPKGLKDAWSKLPIFKKVVSMAPKVVKDAVCQEVVVEGDDVDLGALPIQHCWPGDVAPLITWGLTVTRGPNKDRQNLGIYRQQVIGRNKVIMRWLSHRGGALDYREWCEKNPGQPFPVAVALGADPATILGAVTPVPDTLSEYAFAGLLRGNRTELVKCRGSNLQVPATAEIILEGVIHPGEMAPEGPYGDHTGYYNEVDSFPVFTVERITHRHKPIYHSTYTG... | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | B0KP99 |
Q3B5F5 | CH60_CHLL3 | Chaperonin-60 | Pelodictyon | MTAKDILFDADARAKLKVGVDKLANTVKVTLGPAGRNVLIDKKFGAPTSTKDGVTVAKEIELDDAIENMGAQMVREVASKTSDVAGDGTTTATVLAQAIYREGLKNVAAGARPIDLKRGIDRAVKEVVAELRNISRSISGKKEIAQVGTISANNDPEIGELIAEAMDKVGKDGVITVEEAKGMETELKVVEGMQFDRGYLSPYFVTNSETMEAELEDALILIHDKKIGNMKELLPILEKSAQSGRPLLIIAEDIEGEALATLVVNRLRGTLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEEKGYKLENATVNYLGQA... | 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. | Q3B5F5 |
Q54NW4 | LIMB_DICDI | Paxillin-A | Dictyostelium | MANKNVLSEMDDLMAELGLVETTATPTSDQIKQPQQETAPTYLTYKDPNVSTGPGGDFRNLNDNNGGISRGPGLMSTGPGLVSTGPGLMSTGPGLMSKGPGLPNNSINNNISNNNGGGISSGPGLSFGVSSGVSSGVSSGVSSGVSSGVTLVAQNHLARQPSPPLNSQQQQQQQLPTYLDGVGTLQPISLAATTPDGRVVKANGPICGACGDMIIGVCTNALGRSYHPEHFVCTYCKLPFSGSFIEHEEKLYCENDYLELFSPRCFACIKPIEDTCINALGNRYHPECFSCSGCGDKLRGKPYKEEDGEVYCNTCKIARQ... | Regulates and controls rearrangements of the actin cytoskeleton. Required for tip formation, morphogenesis, cell adhesion and motility, chemotaxis and aggregates formation. May function downstream of paxB. | Q54NW4 |
Q5LXR8 | RL16_STRT1 | 50S ribosomal protein L16 | Streptococcus | MLVPKRVKHRREFRGKMRGEAKGGKEVSFGEYGLQATTSHWITNRQIEAARIAMTRYMKRGGKVWIKIFPHKSYTAKAIGVRMGSGKGAPEGWVAPVKRGKVMFEIAGVSEEVAREAFRLASHKLPVKSKFVKREAE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q5LXR8 |
B7J0R6 | MIAA_BORBZ | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Borreliella | MKEDRVVFIFGPTAVGKSNILFHFPKNKAEIINVDSIQVYKEFNIASSKPSKNLMKHIKHHLVDFLDPEKDYTIGIFYEQALKIVKEIRQKKKIPIFVGGTAFYFKHLKDGFPSTPLVTSKIRIYVNNLLELKGKSYLLKELKNVDPIRFNMLNKNDIYRIKRSLEVYYQTGIPISQFQKKQNSEFKNIVIIGLKRSFEDLKTRISIRINEMLNSGLLSEIKGLFSKGYNENTPAFKGIGYNEFLLWKSRPCYGLNDIIGLINKNSFLYAKRQMTFFAKISDVLWLHPEDDLDNILNLIFKVDKEI | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | B7J0R6 |
B6JLI7 | DCUP_HELP2 | Uroporphyrinogen decarboxylase | Helicobacter | MIFIDACFRKETPYTPIWMMRQAGRYLSEYQESRKKAGSFLELCKNSDLATEVTLQPVEILGVDAAILFSDILVVPLEMGLNLEFIPKKGPHFLETITDLKSVESLKVGAYKQLNYVYDTISQTRQKLSKEKALIGFCGSPWTLATYMIEGEGSKSYAKSKKMLYSEPEVLKALLEKLSLELIEYLSLQIQAGVNAVMIFDSWASALEKEAYLEFSWDYLKKISKELKKRYAHIPVILFPKGIGAYLDSIDGEFDVFGVDWGTPLEVAKKILGDKYVLHGNLEPTRLYDKNALEEGVEKILKVMGNQGHIFNLGHGMLPD... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | B6JLI7 |
Q2YIQ2 | ERYB_BRUA2 | D-erythritol 1-phosphate dehydrogenase | Brucella | MAEPETCDLFVIGGGINGAGVARDAAGRGLKVVLAEKDDLAQGTSSRSGKLVHGGLRYLEYYEFRLVREALIEREVLLNAAPHIIWPMRFVLPHSPQDRPAWLVRLGLFLYDHLGGRKKLPGTRTLDLKRDPEGTPILDQYTKGFEYSDCWVDDARLVALNAVGAAEKGATILTRTPVVSARRENGGWIVETRNSDTGETRTFRARCIVNCAGPWVTDVIHNVAASTSSRNVRLVKGSHIIVPKFWSGANAYLVQNHDKRVIFINPYEGDKALIGTTDIAYEGRAEDVAADEKEIDYLITAVNRYFKEKLRREDVLHSFS... | Catalyzes the oxydation of D-erythritol 1-phosphate to D-erythrulose 1-phosphate. | Q2YIQ2 |
Q1DAM1 | PNP_MYXXD | Polynucleotide phosphorylase | Myxococcus | MLKKSVKIGESELSIEVGRLAKQADGSVVVRYGDTMLLVTAVSAREKKDIDFLPLTVEYQEKLYSAGRIPGSYFKREGRLTEKETLASRLVDRSCRPLFPEGYAYETQIIASVISSDPENEGDIHGITGASAALWVSDIPFDGPIAGIRVGRVGGQLVANPTAKQREQSDLDLVMAVSRKAIVMVEGGAEEVSEADMVAALDFGFTTAQPALDLQDELRRELNKQVRSFEKPAAVDEGLRAKVRELAMDGIKAGYGIKEKGARYEALGKTKKEALAKLKEQLGDGYTPLVEKHAKAVVEDLKYEHMREMTVNGGRIGDRG... | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | Q1DAM1 |
Q9VLA2 | GCM2_DROME | Protein glide-2 | Sophophora | MVVINGYSFKTQQLLTQQPDHSQLTQFVQPQSQSTHSVHPGPSPGQQQAGGSMTMPSSSTGKGKREWDINDAIVPHVPDQEFDEFNEWSDGHVRHIYSLHNEEAKKHISGWAMRNTNNHNVNILKKSCLGVLVCSQHCTLPNGSKINLRPAICDKARRKQEGKACPNKSCRGGRLEIKPCRGHCGYPVTHFWRHSGNAIFFQAKGVHDHLRPDPKNSSVSKRAFGRVPLAGKSANGSVAKKSVIAGLVKQAKQQHSLISKVLKRPAVSNPLAHTALDIYQYNACGKCAGYSHCTCSYLDDSTTARSHQLSQSSNYGTNSW... | Transcription factor with a minor role promoting glial cell differentiation and a more significant role in hematocyte differentiation. Gcm2, together with gcm, is required for the proliferation of plasmatocyte precursors, the expression of Croquemort protein, and the ability of plasmatocytes to convert into macrophages... | Q9VLA2 |
Q5ZKC9 | 1433Z_CHICK | 14-3-3 protein zeta | Gallus | MDKNELVQKAKLAEQAERYDDMASCMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVEQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | Q5ZKC9 |
P22813 | HSF_DROME | Heat shock transcription factor | Sophophora | MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYS... | DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. | P22813 |
Q04845 | MTC1_CITFR | N(4)- cytosine-specific methyltransferase CfrBI | Citrobacter freundii complex | MTVKNNYLNRGYLVTSTTQAKKIAKLHLEKLDLADKFSFGLPEVDDRYHVWRVPLVATGHRIGEIVINSKTSTIDYKKSSKSPFLIKKAMEVVHTPKKVKKEKKIISKSPLNNMLLQGNCAETLKKLPDESVNLVFTSPPYYNAKPEYSEYHTYDEYLSLLRSVIKECHRVLSEGRFFVINVSPVLIRRASRNEASKRIAVPFDLHRLFIEEGYEFIDDIHWVKPEGAGWALGRGRRFAADRNPLQYKPVPVTEYILVYRKKTDKLIDWNIRNHHSKEDVFDSKIGDDYEKTNLWKINPSRNRKHPATFPYGLAERVIKY... | A beta subtype methylase that recognizes the double-stranded sequence 5'-CCWWGG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the CfrBI endonuclease. | Q04845 |
Q8PKW5 | PSRP_XANAC | Pyruvate, water dikinase regulatory protein | Xanthomonas | MSTIRPVFYVSDGTGITAETIGHSLLTQFSGFNFVTDRMSFIDDADKARDAAMRVRAAGERYQVRPVVVNSCVDPQLSMILAESGALMLDVFAPFIEPLERELNAPRHSRVGRAHGMVDFETYHRRINAMNFALSHDDGIALNYDEADVILVAVSRAGKTPTCIYLALHYGIRAANYPLTDEDLENEQLPPRLRNYRSKLFGLTIDPERLQQIRQERRANSRYSAAETCRREVAIAERMFQMERIPSLSTTNTSIEEISSKVLSTLGLQREMF | Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. | Q8PKW5 |
C1DD01 | RSMJ_LARHH | rRNA (guanine-N(2)-)-methyltransferase | Laribacter | MHEMIFPCGLSHQRSSADNAPLPRLMVAMFHGLLATPDVSPATLERFAAGYGLSCLATPPDEGYWLAWRAGVLGLESPHHGAVTADFVGGAARHRREFGGGAGQPVARAIGLKGSQRPQVVDATAGLGRDAFVMASLGCRVTLVERSPVAAALLDDALARARLDPATHEIAARMQLVFADAADWLAQQPAGSVDVVYLDPMFPDTGKSAAAKKEMQAFQVVVGDDLDAGRLLLVARQVAGKRVVVKRPRLGALLTGEKPAGQQVGKSTRFDLYAPLPPASA | Specifically methylates the guanosine in position 1516 of 16S rRNA. | C1DD01 |
Q04116 | YHP1_YEAST | Homeobox protein YHP1 | Saccharomyces | MESRNTVLPSLPNIITGTSNSPFQLHTLPNTNFPSDDQGDIRLPPLAASAHIVRPVVNIYKSPCDEERPKRKSPQAVDFLSQRVTTSMTPLSKPKKLSSHSPFTPTVRVCSKEQPPQSMHSYKKVNILTPLSAAKAVLTPTTRKEKKRSFAFITHSQETFPKKEPKIDNARLARRKRRRTSSYELGILQTAFDECPTPNKAKRIELSEQCNMSEKSVQIWFQNKRQAAKKHKNSGNTSHCKVHSNDSMSMISYSDAALEITSTPTSTKEAITAELLKTSPANTSSIFEDHHITPCKPGGQLKFHRKSVLVKRTLSNTGHS... | Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during S late phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Binds the IMEI regulatory regio... | Q04116 |
G3XCX3 | PILU_PSEAE | Type IV pilus ATPase PilU | Pseudomonas | MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQA... | ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers . Functions as a PilT-dependent retraction ATPase,... | G3XCX3 |
A0A009IHW8 | ABTIR_ACIB9 | TIR domain-containing protein in A.baumannii | Acinetobacter calcoaceticus/baumannii complex | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide . In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which the cyclizing bond is unknown . | A0A009IHW8 |
Q3AW72 | RS13_SYNS9 | 30S ribosomal protein S13 | unclassified Synechococcus | MARIAGVDIPRDKRVEVSLTYIYGIGLTRAKAILAKAGVNPDIRVKDLEDGDIQKLRGATEAFTIEGDLRRQEGMALKRLQDIGCVRGRRHRMSLPVRGQRTRTNARTRRGARKTVAGKKK | 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. | Q3AW72 |
A6GYU2 | RL10_FLAPJ | 50S ribosomal protein L10 | Flavobacterium | MTREEKSIAIGDLTEKLAGTNILYVADISGLNAETTSNLRRACFKAGIKLEVVKNTLLVKAMEASDKDFGDLPLTLKGNTSIFFADVANGPAKIIKDFRKKSDKPLLKGAFINDEIYIGDNLLDSLVNLKSRDEVIGEIIGLLQSPAKRVIAALLNNAESKGEVAE | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A6GYU2 |
Q3AUW7 | RL22_SYNS9 | 50S ribosomal protein L22 | unclassified Synechococcus | MTSSTSTAATAQAHGRFIRGSVSKVRRVLDQIRGRTYRDALIMLEFMPYRSTGPITKVLRSAVANAENNLGLDPASLVISSASADMGPSMKRYRPRAQGRAFQIKKQTCHISIAVAVQTDS | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | Q3AUW7 |
Q5FF40 | SYY_EHRRG | Tyrosyl-tRNA synthetase | Ehrlichia | MKLKSGFLGLLYSRGYFNQCTDLAELDQLMSKECVIAYIGFDCTARSLHIGSLMQIMILRYLQKCGHKPIVLLGNGTTKIGDPSGKDKSRTLLSSSDIQENTLGIRKVLEKFIVCGDGVSDALLVYNAEWLDKLNYIDFLRNIGRHFSVNNMLTFDSVKLRLEREQNLSFLEFNYMLLQAYDFIELNQRYNCLLQIGGSDQWGNIVNGVELGRKLKLPQLFGLTTHLLLTSTGEKMGKTANGAVWLDGEMYSPADYWQYFRNVKDEDVGRFLRLFTELPLTEIEKLENLKGYEINEAKKILATEATRICHGEKIAQDIAY... | 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). | Q5FF40 |
A6W7G8 | ATPG_KINRD | F-ATPase gamma subunit | Kineococcus | MAGQLRAYRRQIRSVQATKKITRAMELIAASRIIKAQANVRASTPYARALTRAVSAAASNSSLDHPLITEKTEVKRAAVLLCSSDRGLAGAYSSSVLREGERLTATLRAEGKEIAPYLVGRKAAAFYNFRRRAVVDQWAGFTDSPSYEDAKTIGDRLVADFGKEFADGGVDEIHVVYTHFVSMVTQEPRVIRLLPLEVVEGVEAPSDGELQPLYEFEPSADAVLDALLPQYVNSRIYNCLLQAAASELAARQRAMKSATDNADELIKKLTRLANNARQADITQEISEIVGGADALASSGSRA | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | A6W7G8 |
A4J122 | RL24_DESRM | 50S ribosomal protein L24 | Desulforamulus | MPKVHVRKGDTVMVITGKDAGKKGKVVTVEPAKNRVIVEGVNIVKRHRKATPQMPQGGIVEKEAPIHSSNVMLFCNKCNKATRIQKKVLDNGNKERICKHCGETLS | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | A4J122 |
A9W5L3 | PTH_METEP | Peptidyl-tRNA hydrolase | Methylorubrum | MRLIVGLGNPGARYARNRHNIGFMAVDEIARVHRAAPFRRRFQGEAAEVMLGSERAILLKPQTFMNESGRSVGEAQRFFKIPLADVIVLHDELDLAPAKLRVKLGGGNAGHNGLRSITALCGNEYRRVRLGIGHPGDKALVHAYVLNDFAKSEEPWVEDLCRATADHAPLLAAGEDASFQNKVHLAMAGRGWETVKTPAEAGKAKARDAN | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | A9W5L3 |
Q9CER9 | ATPG_LACLA | F-ATPase gamma subunit | Lactococcus | MGASLNEIKTKIASTKKTSQITGAMQMVSAAKLQKAESHAKAFQIYAEKVRKITTDLVSSDKEPAKNPMMIKREVKKTGYLVITSDRGLVGGYNSNILKSVMNTIRKRHANESEYTILALGGTGADFFKARNVKVSYVLRGLSDQPTFEEVRAIVTEAVTEYQAEEFDELYVCYNHHVNSLVSDARMEKMLPISFEESGQQKPSLETFELEPDRETILNQLLPQYAESMIYGSIVDAKTAEHAAGMTAMRTATDNAHSVINDLTIQYNRARQASITQEITEIVAGASAL | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | Q9CER9 |
Q1MTQ5 | MUG89_SCHPO | Meiotically up-regulated gene 89 protein | Schizosaccharomyces | MPEALNENVSDTASNGPVAKTRAPPNTSFRQQRIKSWQPLLTPKIVLPLFFVLGIIFGPLGGGLLYASSIVQELVVDYTDCETLASYDEFSAVPSKKYTASFDQSGTIGFDKESTYWKLEKILDKDLDMDVNYCIIRFTVPSVLKAPIFIYYRLTNFFQNHRRYAKSVDEKQLQGVALTADEVKGGNCFPLEVNEDDKPYYPCGLIANSLFNDTFSSLRLLDDNSVYTFSTKNIAWASDKRRFLKTNYSPDDVAPPPNWVLRYPDGYTESNMPDLSTMENLQVWMRTAGLPTFSKLAMRNDNDDIFPGTYEIKIGLFFPV... | Has a role in meiosis. | Q1MTQ5 |
Q12MU6 | SERC_SHEDO | Phosphohydroxythreonine aminotransferase | Shewanella | MSRIYNFCAGPAMLPAAVMQKAQQELLDWNGLGVSVMEISHRSKEFIALAEQAEVNLRQLMNIPNHYHVLFMHGGGRSQFSNVVNNFLGDHGRALYLVSGQWSQSAVEEAQKLAGEAQIDALNIVTKADGLNQVTLPDLHSIKKDYRYVHYCTNETVDGIEIFDELDSPWPIVADLSSTIMSREIDVSRYGLIYAGAQKNIGPSGLSIVIVRDDMLKLASLPQSSVMDYRIAAENGSMFNTPPTFAWYLAAEVFNWLKGLGGVEVIAQVNQQKAQLLYACIDDNSFYRNGVAKQNRSQMNVTFQLADDSLDSRFLAEAER... | Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. | Q12MU6 |
Q5FGQ8 | DNAJ_EHRRG | Chaperone protein DnaJ | Ehrlichia | MSKSDYYDLLGLSKNATPEEIKKAYRKMALKYHPDKNPGDKAAEEKFKELSEAYDVLIDKDKRAAYDRYGHSAFSDGSGRGGFDFNSGFSTDFSDIFNDLFGGGFRGGRSSSKRQDGGTVGSDLRLDIEITLEDSFNGTKVPINYVTHVKCSSCSGSGSEGSVKSVQCNTCHGAGNTRTQQGFFTIERTCHVCNGEGEIIKNKCKKCSGSGRVRDEVNLLVTVPKGIESGDKIRLNGKGEAGYRGAQSGDLYVYPNIKKHKFFTRNGADLYCNVPIKMILATLGGHIEMPSIDGTWTKVKVPEGSQNGDKLRLKEKGMPV... | 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 bou... | Q5FGQ8 |
Q8G2P9 | URE21_BRUSU | Urea amidohydrolase subunit beta 1 | Brucella | MIPGEIITLEGDIELNQGQPTVTMRVANTGDRPIQVGSHFHFYEVNAALSFDREKARGQRLDIAAGTAVRFEPGQERDVTLVPIRGHREIYGFRQMIMGKL | Disrupting the ure1 operon causes loss of urease activity, decreased resistance to low pH killing in vitro and decreased pathogen survival when inoculated in BALB/c mice by gavage. | Q8G2P9 |
P0C8W4 | KBX2_TITST | beta-Ktx | Tityus | MVATNRCCVFALLFALLLVHSLTEAGKGKEILGKIKEKIIEAKDKMKAGWERLTSQSEYACPAIDKFCEDHCAAKKAVGKCDDFKCKCIKL | Blocks voltage-gated potassium channels (Kv). | P0C8W4 |
Q2JD96 | RUVC_FRACC | Holliday junction resolvase RuvC | Frankia | MRVLGVDPGLTRCGLGVVDGGLGIRAHLVEVGVVRTPATAEVAERLCAVSDGIDAWLDRTRPEAVAVEKVFSQANMRTVMGTAQAGAVAIVLAARRGLPVGLYTPSEVKAAVTGSGRADKAQVSFMITRLLGLTEAPRPADAADALALALCHLWRGPALARFRSAAPGGPTR | Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | Q2JD96 |
Q9ZBA9 | DAP_BRUAN | D-aminopeptidase | Brucella | MSKFDTSALEAFVRHIPQNYKGPGGVVAVVKDGEVVLQHAWGFADLRTRTPMTLDTRMPICSVSKQFTCAVLLDAVGEPELLDDALEAYLDKFEDERPAVRDLCNNQSGLRDYWALSVLCGADPEGVFLPAQAQSLLRRLKTTHFEPGSHYSYCNGNFRILADLIEAHTGRTLVDILSERIFAPAGMKRAELISDTALFDECTGYEGDTVRGFLPATNRIQWMGDAGICASLNDMIAWEQFIDATRDDESGLYRRLSGPQTFKDGVAAPYGFGLNLHETGGKRLTGHGGALRGWRCQRWHCADERLSTIAMFNFEGGASE... | Hydrolyzes N-terminal residues in D-amino acid-containing peptides. | Q9ZBA9 |
Q8PC59 | EFTU1_XANCP | Elongation factor Tu-A | Xanthomonas | MARAKFLREKLHVNVGTIGHVDHGKTTLTAALTKIGAERFGGEFKAYDAIDAAPEEKARGITISTAHVEYESAVRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLSRQVGVPHIVVFLNKADMVDDAELLELVEMEVRELLSKYDFPGDDTPIIHGSARLALEGDQSDIGVPAILKLVEALDTFIPDPTRDVDRPFLMPVEDVFSISGRGTVVTGRIERGIIKVGDEIEIVGIRDTQKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRDDVERGQVLCKPGSIKPHTEFEAEVYVLSKDEGG... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q8PC59 |
Q2SYE1 | UPPP1_BURTA | Undecaprenyl pyrophosphate phosphatase 1 | pseudomallei group | MDWILICKALALGIVEGLTEFLPVSSTGHLIVAGSFLRFHPEQAKTFDVVIQFGAILAVCWEYRRRIVDVVTGLPAQREARRFTMNVVIATLPAIALALLFEKTIKSVLFAPVPVAVALVVGGAVILWVEGRQRERGKPSRVQSIDALTPLDALKVGLAQCFALIPGVSRSGSTIIGGMLFGLERRVATEFSFFLAIPVIFGATLYETAKDWHAFNVDSIGLFAIGLAAAFVSAFACVRWLLRYVASHDFTAFAWYRIVFGLFVLLVGYSGWIEWI | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q2SYE1 |
A4FZP2 | KHSE_METM5 | Homoserine kinase | Methanococcus | MKKVKVCSPGTSANLGPGYDIFGLALSKPYDILEVEKTEKGIIISVEGEKAEEIPTNVDENTAGVVAKKMMEDFNIQSGIHIHINKGIKPGSGLGSSSASCAGVAFALNELFELKLSKLELVKYSSLGEAVAAGAPHADNVAPAIFGGFTLTTSYDPLEVLHIPVDIEVLVALPNIQVSTKTAREILPKEIPIKYMVNNVGKAAGMVYALYNNDLELFGRYMSKDCVVEPCRANLIDGYAEVKEKVKDLVYGITISGSGPAIITIPKKEHVIDIENIFKEVWNCPVYYTKVGPGCYVEEIE | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. | A4FZP2 |
Q6BL01 | DML1_DEBHA | Protein DML1 | Debaryomyces | MSEVINLSLSQRANHLSAHLYNNQEAHLPYSKTATVDYDNSVFLSTSKNPNGTVNYSPRSLNYDLTRGYGSLGKYEYYESKADILGQYEVIQTGEKMDKNEYQKALDKGMNKSNTLNVNNTKYWTDYNKLIYSPKSLNQLNNWEYKPHDFGINRSFPNLKFDTFNKGKEEYHQYSEDSLENFRNTLEQCDLIQGVNLISELDSAWGGFTNELLVDLKDEFFNNGINSKYNIWVHGLINHNLNPKLNQLYSRINSIIELSFNSTLFFPMNLNSSSECLGVKMSVIEDELLRGFDKRNIVNEIKIHKNKQASNDFGMVDIDR... | Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance. | Q6BL01 |
Q07KN7 | RL15_RHOP5 | 50S ribosomal protein L15 | Rhodopseudomonas | MKLSEIADNAGSRKKRMRVGRGIGSGKGKTAGRGGKGQTARSGVRIKGFEGGQMPLHRRLPKRGFNNIFRLDFAEINLDRLQEAIDAKAVDAGAVINAEVLVAAGVVRRAKDGVRLLGRGELKSKLTIEVYGASKPAIAAVEKAGGTVKILAPVKDEGEAA | Binds to the 23S rRNA. | Q07KN7 |
B7STY1 | ATRA_TAPPA | Nonribosomal peptide synthase atrA | Tapinella | MAPTAVFSNPATNPVANLKASVKTAEGVPATLNDLLLQATEMYPSHELSFITSSAHDSSVQARTFQDFNQRVRNLASALAAWKKPAGEVVVVYLTEHEDNMSAVWACLLAGLVPCLQPALSAQQEHKEGHIAHIRKLFGSATWLTNDAGAMQLDTIKGLDVHLFSDLLASAEKSSVAANYVARQSQPDDEAILFLTSGSTGFSKAVVHTHRTIINACIAKGANYRLTPQTNILNWVGFDHVAGSLEMHIAPLLYGCSQLHVHASAILSDPLLLLRLIDERSIDIAFAPNFLLAKMVRDLEKRTDLHGKFDLSSLRRMNSG... | The L-tyrosine:2-oxoglutarate aminotransferase atrD and the atromentin synthetase atrA catalyze consecutive steps to turn over L-tyrosine into atromentin, which represents the generic precursor molecule for the entire terphenylquinone and pulvinic acid family of pigments, which are widely distributed secondary metaboli... | B7STY1 |
Q93132 | ACTM_BRAFL | Actin, muscle | Branchiostoma | MSDEEEEATPLVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDAYVGDEAQSKRGILTLKYPVEHGIVTNWDDMEKVWHHTFYNELRIAPEENPCLLTEAPLNPKANREKMTQIMFETFNSPAMYVCIQAVLCLYASGRTTGIVLDSGDGVSHTVPIYEGYAMPHAILRLDLAGRELTNYLMRVMCDRGYAFVTTAEREIVRDIKEKLGYVALDFEQEMLTAATSTSLEKSYELPDGQVITIGNERFRCAEALFQPSFLGMESAGVHETVYNSIMKCDIDVRKDLYANNVLSGGTTMFPGIGDRMQKEM... | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Q93132 |
Q6APU2 | GUAA_DESPS | Glutamine amidotransferase | Desulfotalea | MDIHKEKIIILDFGSQTTQLIARRVREMKVYSEIHPFSLPLEKLKELNPTGIILSGGPCSVYDDDAPHSDAGLFELGVPVFGICYGAQLMIQQLGGSVEKAEKREFGKAEIQILNDSDLFAGLDVARSHQVWMSHGDRVEVIPDQFEVSAESAHSPYAALRHRSKPFVAVQFHPEVVHSIIGTDLLRNFVFGLCKCQATWTMQGFIESNVAAIKEKVGDAHVICALSGGVDSSVVAAMIHKAIGSQLTCVYVNNGLMRIGESEGIIKFFKENTDLHLIDVDASDYFLGKLEGVTDPEVKRQHIGLGFIKIFEEEAHKIDG... | Catalyzes the synthesis of GMP from XMP. | Q6APU2 |
H2KZ49 | HRDE4_CAEEL | null | Caenorhabditis | MNTYFRFEWINGEENPCEYNLWRMFQIEPKPKSGANFMKPNLPNTENFSTASSSKIRQLSEQPSCSNSYKKLRHEMGSDNSNIDDPLDDYDDRKKKLAKKKAAFKAKKGYTTGQNKSDNSFEFEVEKSMDRKEPENGDEEESTEDDYRHAYSSVEKSLRKISLLPIQRPSHHTFCVFCSESYPPVEFHFCIFMTAAQKEVNQSVNEFLGKADTINKKMLESLKKFIHTSKVDTIAKHSRMENTSMKKNSDSPKKLKRPSTDPNPISKRFRHISDESTSSSSLAKNKSRSVTPDALPFAMIDSQEHRTQSGRVVKRPNLFC... | May play a role in transgenerational epigenetic inheritance. | H2KZ49 |
Q980P7 | PURP_SACS2 | 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase | Saccharolobus | MIIATIGSHSALQILHGAKKEGFQTMVITDNKRENFYKNFSFIDNIYAYASLDEAVSIINGIKDYGILIPHGSLVEYLGKERVDKIETKIFGNKKIFEWEADQKKKMELLRKSNIKIPEIFERPEDVDRLVIVKLNGAKGGKGYFLARNKSEVKEGIQKLIESKMIRDENEVIIQEYVVGVPMYFQFFYSDIINRTEIFGIDIRYETNIDGLRRLPFEYMKELKINPTFVVVGNIPAVARESLLPVALEYANNFVRTTKELVPPGMIGPFCLESIITDNSDIVVFEFSGRIVAGTNLYVNGSPYSWLYWDEPMSIGRRIA... | Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates. | Q980P7 |
B0YPR6 | RR19_ANEMR | 30S ribosomal protein S19, plastid | Aneura | MTRSLGKGPFVANHLLKEIEILNFGGSEEVVVTWSRASTIVPVMIGHTIAIHNGREHLPIYITDRMVGHKLGEFAPTRTFRGHARNDKKSRR | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | B0YPR6 |
B7ID58 | BIOF_THEAB | 8-amino-7-ketopelargonate synthase | Thermosipho | MFDYSIFSKELENLKEQGLYTYIKTLESPQGAWLTINGKKVLNLCSNNYLGFANEERLKKAAIEAIEKWGVGPGAVRTIAGTFSLHNELEKTLAEFKKVEATIFLQSGFVANQAVIPAITNEEDAILSDELNHASIIDGVRLSKAKRYVWKHRDVKDLEEKLKEAKDARRKLIITDGVFSMDGDLAPLPEIVELAEKYNAMVMVDDAHGEGVLGSHGRGIVDHFGLHGRVDIEIGTLSKAFGVLGGYVAGKKELIDYLKQKARPFLFSSPLSPADTAAALEATKILQESDDRVKRLWDNAKYFKEEMKKLGFDTGESETP... | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | B7ID58 |
Q58G53 | LAZY2_ARATH | Protein NEGATIVE GRAVITROPIC RESPONSE OF ROOTS 1 | Arabidopsis | MKFFGWMQNKLNGDHNRTSTSSASSHHVKQEPREEFSDWPHALLAIGTFGTTSNSVSENESKNVHEEIEAEKKCTAQSEQEEEPSSSVNLEDFTPEEVGKLQKELMKLLSRTKKRKSDVNRELMKNLPLDRFLNCPSSLEVDRRISNALSAVVDSSEENKEEDMERTINVILGRCKEISIESKNNKKKRDISKNSVSYLFKKIFVCADGISTAPSPSLRDTLQESRMEKLLKMMLHKKINAQASSKPTSLTTKRYLQDKKQLSLKSEEEETSERRSSSDGYKWVKTDSDFIVLEI | Involved in the regulation of root gravitropism . Functions redundantly with LAZY3 and LAZY4 in the control of root gravitropism . Functions redundantly with LAZY1, LAZY3 and LAZY4 to control plant architecture by coupling gravity sensing to the formation of auxin gradients . Involved redundantly with LAZY1 and LAZY4 i... | Q58G53 |
Q45968 | TRA1_COXBU | Transposase for insertion sequence element IS1111A | Coxiella | MDPPLKDGVIMRQHRISIFKKRRRSMKDIKILGVDIAKDVFQLCGIDEWGKVIYTRRVKRAQYVSTVASLKVGCVVMEACGGANHWYRTFMGMGIPTQLISPQHVKPYVKSNKNDRNDAQAIAEAASRASMRFVQGKTVEQQDVQALLKIRDRLVKSRTALINEIRGLLQEYGLTMARGAKRFYEELPLILASEAVGLTPRMKRVLNCLYTELLNRDEAIGDYEEELKAVAKANEDCQRVQSIPGVGYLTALSVYASVGDIHQFHRSRQLSAFIGLVPRQHSSGNKEVLLGISKRGNVMLRTLLIHGARALLRHVKNKTD... | Required for the transposition of the insertion element. | Q45968 |
A2RP07 | RUVA_LACLM | Holliday junction ATP-dependent DNA helicase RuvA | Lactococcus cremoris subsp. cremoris | MFEYLNGKLVKISPTNIVIDLSGIGYLISVANPYAWSALMNTEVKIYVHQVIREDAHSLYGFVNESEKALFLRLISVSGIGPKSALAIIAAADNEGLINAIDNSDIKYLTKFPGVGKKTAMQMVLDLAGKFDATGAVGISLLDAAPASNLALEEAIEALQALGYKATELKKIEKKLAQEAGLTSEEYIKSALKLMMK | 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... | A2RP07 |
A1CND4 | XYND_ASPCL | Xylobiase xlnD | Aspergillus subgen. Fumigati | MSAIKSIATVLAAILPSVLAQANTSYADYNTEANPDLTPQSVATIDLSFPDCDNGPLSKTIVCDTLTSPYDRAAALISLFTLEELVNATGNTSPGVPRLGLPPYQVWNEALHGLDRAYFTDEGQFSWSTSFPMPILTMSALNRTLINQVASIISTQGRAFSNAGRYGLDVYSPNINSFRHPVWGRGQETPGEDAYCLSSAYAYEYITGIQGGVDPKSLKLVATAKHYAGYDIENWDGHSRLGNDMNITQQDLSEYYTPQFLVAARDAKVRSVMCSYNAVNGVPSCANSFFLQTLLRDTFGFVEDGYISSDCDSAYNVFNP... | Xylan 1,4-beta-xylosidase 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. | A1CND4 |
Q4KIG0 | GLMM_PSEF5 | Phosphoglucosamine mutase | Pseudomonas | MTKKYFGTDGIRGRVGEFPITPDFMLKLGWAAGMAFRSMGACRVLVGKDTRISGYMFESALEAGLSAAGADVMLLGPMPTPAIAYLTRTFHAEAGIVISASHNPHDDNGIKFFSGEGTKLPDEVELMIEELLDAPMTVVESSKLGKVSRINDASGRYIEFCKSSVPSSTSFAGLKVVLDCAHGATYKVAPSVFRELGAQVTVLSAQPNGLNINENCGSTHMSQLQAAVLAEHADLGIAFDGDGDRVLMVDQTGAIVDGDELLFIIARDLHERDKLQGGVVGTLMSNLGLELALADLGIPFVRANVGDRYVIAELLERNWL... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q4KIG0 |
B1YMR8 | ATPF_EXIS2 | F-type ATPase subunit b | Exiguobacterium | MNLTYRAAEGVAESNHLLLANMIVTIVVFLLLLILLKKFAWGPLVNMMKAREEHVASEINSAEKSRKDAEVYVEQQQAELNKARTEARDLLEASRRQAEAEQARAMEQARVETELSKEEARRAIERERAEAQAALKNDVALQAIAAARHVMKTQLATDEAAQRALVDQFLADTKGTN | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | B1YMR8 |
Q3APR5 | QUEF_CHLCH | PreQ(0) reductase | Chlorobium | MKLEILESFENKYPNRDYTIEIVNPEFTSVCPITGLPDFGTITIRYVPNQRCVELKSLKYYFFEFRNAGIFYENITNKVLDDMVALLEPRSISVITEWKARGGITETVSVHYTSQS | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | Q3APR5 |
Q39EA2 | UPP_BURL3 | UPRTase | Burkholderia cepacia complex | MKQDSRFPNLFITDHPLIQHKLTHMRDKDTSTRTFRELLREITLLMGYEITRNLPITTKRVETPLVEVDAPVIAGKKLAIVPVLRAGIGMSDGLLDLVPSARVGHIGVYRADDHRPVEYLVRLPDLEDRIFILCDPMVATGYSAVHAVDVLKRRNVPAANIMFVALVAAPEGVQVFQDAHPDVKLFVASLDSHLNEHAYIVPGLGDAGDRLFGTKN | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q39EA2 |
B1ZA43 | NUOD_METPB | NDH-1 subunit D | Methylorubrum | MSEHNIRNFSINFGPQHPAAHGVLRLVLELDGEVVERVDPHIGLLHRGTEKLIEHKTYLQATPYFDRLDYVSPMNQEHAFCLAIERLAGIEVPRRAQLIRTLFCEIGRLLSHLLNVTTQAMDVGALTPPLWGFEEREKLMIFYERASGARLHANYFRPGGVHQDLPPALIDDIEAFCDPFLKVVDDLDNLVMANRIFKQRNVDIGIVSVDEAMAWGFSGVMVRGSGIPWDLRKSQPYECYEEMDFDIPVGKNGDTYDRQVIRMEEMRESVKIMRQCCAKLREPSGQGPIASIDGKFAPPPRREMKRSMEALIHHFKLYTE... | 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... | B1ZA43 |
Q96511 | PER69_ARATH | ATP3a | Arabidopsis | MGRGYNLLFVLVTFLVLVAAVTAQGNRGSNSGGGRRPHVGFYGNRCRNVESIVRSVVQSHVRSIPANAPGILRMHFHDCFVHGCDGSVLLAGNTSERTAVPNRSLRGFEVIEEAKARLEKACPRTVSCADILTLAARDAVVLTGGQRWEVPLGRLDGRISQASDVNLPGPSDSVAKQKQDFAAKTLNTLDLVTLVGGHTIGTAGCGLVRGRFVNFNGTGQPDPSIDPSFVPLILAQCPQNGGTRVELDEGSVDKFDTSFLRKVTSSRVVLQSDLVLWKDPETRAIIERLLGLRRPSLRFGTEFGKSMVKMSLIEVKTGSD... | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. | Q96511 |
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