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2.75k
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5.51k
AlphaFoldDB
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Q08219
RRT8_YEAST
Regulator of rDNA transcription protein 8
Saccharomyces
MKAGIELISHSQASHATYANSMTLAEKGPQRLKRQFKEHSSSKESNVSRWLKIFIRQFDIWFPETIPTMKVRYELLRKNFIKEIFNSRAFIYPFLGFYEVLTNPVYWKHILLFAVCYALIFVTIAGLFYVTLVPLLVTWAILLLGPLGVILVHIQWILQTNVLTAFVCRTLVLTHITNQIFDISLVLQDQDEFLNEVKVLPKPQKPHRKIDEPDAVRNFNTIKGSRIFKIPRLLFRMFFKVSNFTSLTLLSLIPIVGPILANQLMAPKRTFTYLQRYFLLKGFSKKQAKDFQYEHYASFICFGMSAGLLELIPFFTIVTISSNTVGAAKWCTSLLKGERKKE
Involved in spore wall assembly . May be involved in the modulation of rDNA transcription .
Q08219
Q5L5D3
ISPH_CHLAB
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Chlamydia
MRRVILSNPRGFCAGVVRAIQVVESALEKWGAPIYVKHEIVHNRHVVDDLKRRGAIFIEDLKDVPCGEKVIYSAHGIPPEVREEAKARNLFDIDATCVLVTKIHSAVKLYASKGYQIILIGKKKHVEVIGIRGEAPESVTVVEKVEDVANLPFDIHVPLFFVTQTTLSLDDVAEVTQALKARYPHIITLPSSSVCYATQNRQEALRAVLPRVNFVYVIGDVQSSNSNRLREVAEKRNIPARLVNSPDHISDEILHYSGDIAVTAGASTPEHIIQSCISRLKELIPDLQVEEDIFTTEDVVFQPPKELRT
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Q5L5D3
Q31NM6
SYDND_SYNE7
Non-discriminating aspartyl-tRNA synthetase
Synechococcus
MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLELVDVSDVVADMGFKVFSGAVKSGGKVKILPIPDGNDRISNVRIKPGGDIFKEATEAGAAGLAYIRVRENGEIDTIGAIKDNLSDEQKAEILRRTQAQPGTLLLFGAGSTDIVNKSLDRVRQFLGKELGLIDPEALNLLWVVDFPMVEWNADEKRYEALHHPFTAPNPQDLEDLTTARAQAYDIVLNGLEIGGGSLRIYQRDIQERVFETIGLSHEEAQAKFGFLLEAFDFGTPPHGGIAYGLDRLVMLLTGEESIRDAIAFPKTQQARCLLTEAPADVSDRQLKELYVASTWQPPIKERD
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q31NM6
A3N1D8
ORN_ACTP2
Oligoribonuclease
Actinobacillus
MSKLDNQNLIWIDLEMTGLDPEKERIIEVATIVTDKDLNILAEGPVLTVHQSNDLLNKMSDWCIKTHTENGLIERVKQSKLTERAVELQTIDFLKQWVPKGASPICGNSVAQDKRFLYKYMPDLADYFHYRHLDVSTLKELARRWKPDMLNAFNKKNTHLALDDIRESIEELKFYRTHFINLEK
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
A3N1D8
Q5SD05
ATPE_HUPLU
F-ATPase epsilon subunit
Huperzia
MTLNLRVMTPNRTVWNSEVQEMILSTNSGQIGVLPNHAPLLTALDIGITKIRLNGQWSTMALMGGFAMVDNNQVTILVNEAEEAAGIDPQEAKETFRIAQTNLARAEGKKQVIEANLAFKRAKARLEAIDATLSYASN
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q5SD05
P00919
CAH2_RABIT
Carbonic anhydrase II
Oryctolagus
MSHHWGYGKHNGPEHWHKDFPIANGERQSPIDIDTNAAKHDPSLKPLRVCYEHPISRRIINNGHSFNVEFDDSHDKTVLKEGPLEGTYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVKHPDGLAVLGIFLKIGSATPGLQKVVDTLSSIKTKGKSVDFTDFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPITVSSEQMLKFRNLNFNKEAEPEEPMVDNWRPTQPLKGRQVKASFV
Catalyzes the reversible hydration of carbon dioxide. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Essential for bone resorption and osteoclast differentiation. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.
P00919
A0LU48
DOP_ACIC1
Depupylase
Acidothermus
MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQRQARWDFEEENPLRDARGFEVAREAADPSQLTDEDLGLANVILTNGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWTIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAGRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALRAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMTRDVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKLQLVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFRGRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLLDRCRSATELVAALTGGR
Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-terminal glutamine to glutamate in a variant of the prokaryotic ubiquitin-like protein Pup; however, since Pup from A.cellulolyticus possesses a C-terminal glutamate, this deamidase activity may be of no significance in vivo.
A0LU48
A0A2I6PIZ6
NODD2_HYPPI
Nodulisporic acid biosynthesis cluster protein D2
Hypoxylon
MDSTGRQPLSQDGQPWQALASGLGFPDEDQKYWWSVMAPLLGELMKWANYPVDKQYLVLAFCHEYILPFCGPRPTAEGGIFWPTLITKDGTPFEPSLNFYKNKATLRVGYAPACELSGSNDDPINQRAPIAALEHQKRVLPQQNLKWVDNFKKAWFIDNDDAVALKARVHNELFEQAAVQCLIGYVFSDYTQVKVAMSPLWKSVQTGQQISRVIWDTFRQLGDDASSYLDCLSVLEEYTESKQAKLAQVQPSFVNFDVNLKGDYQQSRLKVYYATPCTAFDTMVQVFTLGGRLKGPEVDHAIECLRVLWPSVLAVPENHPDDQDLPRRYHSVAVTQFNFELWPGAKLPVPQIYLPTNFYGRDELEIAEGLEGFFKTLGWSEPFHAYKQNYIATCATPEGKWKAIQHDVSFSFKDSSPYVSVYYKPELSVLSSPS
Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed . The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB . The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA . NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD-dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable).
A0A2I6PIZ6
Q9MZ13
VDAC3_BOVIN
Outer mitochondrial membrane protein porin 3
Bos
MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLRTKSCSGVEFSTSGHAYTDTGKASGNLETKYKICNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSLGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNEKIETSINLAWTAGSNNTRFGIAAKYKLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFNAGGHKVGLGFELEA
Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules.
Q9MZ13
Q12343
MED4_YEAST
Mediator complex subunit 4
Saccharomyces
MSVQDTKAVEFSMGHIRSSSVSLVAEATSNTNSEDKLSKVQLYEDLCRYEDTLSKLVESVDRFKPNLDIAKDLIRTDEALFENVKLLAEYDNIYRNLQKIDKDSEELDSKTRKILEILNECHDELKALPMLEQVEFEKNTILQQRSKINSTELLDYATKLSKFTKIPPTFDKGAVGPNNFIWPAEDALRRGMLAMASLHSKELTRIPGEEVEETEVPTVPPSQSEEQKGQMAKKEGTPKTDSFIFDGTAKEVGDEADNTKDKEKEENNDDALDLDLDLFDPDDF
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Q12343
A5F3F8
RLMN_VIBC3
tRNA m2A37 methyltransferase
Vibrio
MTTEKVNLLDFDRKGLRTFFAEELGEKAFRAEQVMKWIYHFGCDDFDQMNNINKQLREKLKAKCEIRAPYVSEAQHSADGTIKWAMRVGDQDVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAREIGLEKETGRRPITNVVMMGMGEPLLNMKNLIPALEIMLDDLGFGLSKRRVTVSTSGVVSGLEQMIGQIDVALAISLHAPNDKLRSEIMPINDRWNIEAFLEVVRRYIASSNANRGKVTVEYVLLDHVNDGTEHAHELAELLKRTPCKINLIPFNPYPGSPYKKPSNSRIDRFQKTLMQYEHTVTIRKTRGDDIDAACGQLVGDVIDRTKRTKAKQFDGQAIPVKTL
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
A5F3F8
O76093
FGF18_HUMAN
zFGF5
Homo
MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA
Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation.
O76093
Q3SVD4
MUTS_NITWN
DNA mismatch repair protein MutS
Nitrobacter
MMEQYLEIKAANPGLLLFYRMGDFYELFFEDAEIASRALGITLTKRGKHQGADIPMCGVPVERSDDYLHRLIAAGHRVAVCEQTEDPSAARKRGNKSVVRRDVVRLVTPGTLTEDTLLDARANNYLLALARARASSGVDRFALAWIDISTAEFMVTECGANELAATLARINPNEVIVSDTLHGDPDLGALLRELPSVTPLPRDTFDGATAERRLCDYFAVATMDGLSAMSRLEATAAAAAVTYIDRTQIGQRPPLSPPSREASGSTMAIDPATRANLELTRTLAGERRGSLLDAIDRTMTAAGSRLLAQRLAAPLTDTAAITRRLDAVAALTADGAARDDIRAILRTAPDMSRALARLSLGRGGPRDLAGLRDGVMAADQTLARLAGLSDPPEGIAAAMQALRGPSRELARELGNALSENLPLMKRDGGFVREGYDTALDEARKLRDDSRLVVAAMQARYAEETGVKTLKIRHNNVLGYFVEVTAQHANRLMSAPLNATFIHRQTLAGQVRFTTSELGEIEARIANAGERALGLELDIFDRLAAMAIRNGDEIRNAAHAFAQLDVAASFAKLAIDENYTRPDIDASLSFAIEGGRHPVVEQALKRTGQPFIANACDLSPPPPPVEGSGESGQIWLLTGPNMAGKSTFLRQNALIALMAQVGSFVPASRARIGIIDRLFSRVGAADDLARGRSTFMVEMVETAVILNQASERALVILDEIGRGTATFDGLSIAWATIEHLHESNRCRALFATHYHELTALSAKLPRLFNATVRVKEWHGEVVFLHEVLPGAADRSYGIQVARLAGLPPSVIARAKSVLAKLEAQDRGSTVRVLVDDLPLFAVTSRTGESAPTGETSPLIEALKSLHPDEMSPREALDALYALKAKLPKQ
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Q3SVD4
C1D9H2
CCME_LARHH
Heme chaperone CcmE
Laribacter
MHPKRKKRLLIVLAGLAVVAVASGLILNAFRSNLVFFHTPTEIAAGQVDTDRVIRVGGLVEAGSVEREPGGLRVRFVITDTARSVPVRYEGILPDLFREGHGTVVQGRIGTDGVLAATQVLAKHDENYMPPEAADAIQRAGETVVQ
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
C1D9H2
O32377
RECA_ALLVI
Recombinase A
Allochromatium
MDENRKKALAAALTQIEKQFGKGSVMRMGDVGAVRNIEAISTGSLGLDLALGIGGVPKGRVIEIYGPESSGKTTLTLHIIAESQKLGGTAAFVDAEHALDPVYAEKLGVNMTDLLVSQPDTGEQALEITDMLVRSGAVDVVVVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTGNIKRSNCCVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAIKKGDEVIGNETKVKVVKNKVAPPFRQAEFDILYGQGISREGEIIDLGVAEGFIDKSGAWYSYDGNRIGQGKDNVRNFLCENPGIAQAIEARIRDKLLPKGGVEAPAEADVPEPSED
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
O32377
A4W787
RISB_ENT38
6,7-dimethyl-8-ribityllumazine synthase
Enterobacter
MNIIEAAVATPDARVAITIARFNNFINDSLLDGAIDALKRIGQVKDENITVVWVPGAYELPLAAGALAKTGKYDAVIALGTVIRGGTAHFEYVAGGASNGLAHVAQEAEIPVAFGVLTTESIEQAIERAGTKAGNKGAEAALTALEMINVLKAIKA
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.
A4W787
A9LYF6
NDHH_ACOAM
NADH-plastoquinone oxidoreductase subunit H
Acorus
MTVPATRQDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQIPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELIYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLTGIVEYEKLITQNPIFLERVERVGIISGEEAINWGLSGPMLRASGIEWDLRKVDNYECYNEFDWEVQWQKEGDSLARYLVRISEMKESIKIIQQALEGIPGGPYENLEVRRFDKVKDSEWNDFEYRFISKKPSPTFELAKQELYVRVEAPKGELGIFLIGDNSVFPWRWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
A9LYF6
A5GQJ6
YCF3_SYNR3
Photosystem I assembly protein Ycf3
unclassified Synechococcus
MPRSQRNDNFIDKSFTVMADLILKVLPTNQKAKEAFAYYRDGMSAQGDGEYAEALENYQEALRLEEDPNDRAFILYNMALVYASNGEHNRALEQYEQALALNAKMPQVLNNMAVIHHHLGSIAQEKGESDEADRRFDLAADFWSKAIRLAPNNYIEAQNWLKTTGRGSADVYL
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
A5GQJ6
A2YWA6
ZHD2_ORYSI
Zinc-finger homeodomain protein 2
Oryza sativa
MDFDDHDEGDGDEEMPPMPLSSGYDAPMQPGLGGGGGGVPKPGGGVGGGGGGGGGGGGGGARYRECLKNHAVGIGGHAVDGCGEFMASGEEGSIDALRCAACGCHRNFHRKESESPTGVGPAEPSAVSPAAISAYGASPHHQFSPYYRTPAGYLHHQQHQMAAAAAAAAAAAAGGYPQRPLALPSTSHSGRDEGDDMSGMVGPMVIGPMVGMSLGSAGPSGSGSGKKRFRTKFTQEQKDKMLAFAERLGWRIQKHDEAAVQQFCEEVCVKRHVLKVWMHNNKHTLGKKAP
Putative transcription factor.
A2YWA6
B0T192
GATC_CAUSK
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
unclassified Caulobacter
MAIDAATVRKVARLARIATPEDRLEPLAQELNGIMTWIEQLAQVDTDGVEPLTSVVHAGLPLREDVVTMGGDADLITANAPKSTGGFFVVPKVVE
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
B0T192
Q9AKH1
FER2_RICRI
Adrenodoxin-like protein
spotted fever group
MSGKIKVTFIINDGEEKTVEAPIGLSILEIAHSNDLDLEGACEGSLACATCHVILEEEFYNKLKKPTEAEEDMLDLAFGLTDTSRLGCQIILTEELDGIKVHLPAATRNIKL
Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Q9AKH1
Q87LL6
ARGP_VIBPA
HTH-type transcriptional regulator ArgP
Vibrio
MRGLDYKWIEALDAVVYQGSFERAAEHLFVSQSAISQRIKQLEKFLAQPVLIREQPPKPTPIGKKLLGLYRRVRLLEHEILPEIKNDTTTRPVQLSLATNADSLATWLLPALQDVMKTRQVELKLTIYGESRSIEKLKSGEVAGAISLESQAIPNCRADYLGRIDYVCVANPEFYQRYFSEGVNNQTLAKAPAVSYDQYDDLHKKFLTEHFNVRPDSVIHHNISSSEAFLKMALAGVAYCLIPRLQITDELEQGSLIDITPGFLMSYRIYWHHWQLETGVLQEISQAIVNYAQRHLPQ
Controls the transcription of genes involved in arginine and lysine metabolism.
Q87LL6
Q8DW14
PURA_STRMU
IMP--aspartate ligase
Streptococcus
MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPEKVSVIGNGMVVNPKSLVEELDYLHQEGVATDNLRISDRAHIILPYHIKLDQLQEASKGDNKIGTTNKGIGPAYMDKAARVGIRIADLLDKDIFAERLKANLAEKNRLFEKMYESSPVAFDTIFDEYYAYGQKIKDYVTDTSVILNKALDKGRRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDQTGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNCIDVLSGLDIVKICVAYDLDGKRIDHYPASLEQLKRCKPIYEELPGWSEDITGVRSLEDLPENARNYVRRVSELVGVRISTFSVGPDRDQTNILESVWGL
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.
Q8DW14
A4YKF1
PROA_BRASO
Glutamyl-gamma-semialdehyde dehydrogenase
unclassified Bradyrhizobium
MTAPLKAIDGSADLPQLMNDLAKRARAAARVLALAPAEQKNRALEAMERRIRARADVIIAANAEDVAEAKAVGVTPSFVDRLTLTPARVAAMADGIAVVRGVADPVGVVTESWQRPNGMTIERVRVPLGVIGVIFESRPNVAADAGVLCLKSGNAVILRGGSDSFRSCRAIHECLVEGLREAGLPDTAITLVPTRDRAAVGLLLSGLNGGVDVIVPRGGKSLVARVEAEARVPVFAHLEGVNHVYVDGAADLDMAKSIVLNAKMRRTGVCGAAETLLIDRASQDKIKPLVDMLIGAGCEVRGDEAVRAADARVTPANNEDWDTEYLDAIIAAKVVDGVDGAIAHIHAHGSHHTDAIVTQDNKVADKFLNEVDSAIVLHNASTQFADGGEFGFGAEIGIATGKFHARGPVGVEQLTSFKYRIHGTGQTRP
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
A4YKF1
Q8DM00
PRMA_THEVB
Ribosomal protein L11 methyltransferase
Thermosynechococcus
MVQRWWEITVTCQAEAEELVYWRLQSFGCQGTATQLQQGRVLIQGYVPQQRVSLLDIAALGVWIEQDVVAQGYLSPKLHWQLVNEQDWAHSWQAYWHPIPVGDRLLICPAWEMPPLDNTRLVIKLDPGMAFGTGTHETTQLCLEALEMQLDQTFEPLPPTVIADIGCGSGILAIASLLLGAQKAYAVDTSDLAVTATQRNAELNGIRADQLIVHQGSWEQVLELVDGVVCNILAPVIIEILPHLPAIVKPKGWGIFSGILLDQADRVAEQLKRQGWSLGSVWRRNEWCCLNARFERLPD
Methylates ribosomal protein L11.
Q8DM00
O46629
ECHB_BOVIN
Beta-ketothiolase
Bos
MISLLTYTLKNLPNTSKWALRFCMRPLSSSSQLQAAAASQTKSKKTLAKPNIRNIVVVDGVRTPFLLSGTSYKDLMPHDLARAALSGLLHRTSVPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDIPIRHSRKMRKMMLDLNKAKTLAQRLSIISKFRLNFLSPELPAVSEFSTSETMGHSADRLAAAFAISREEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGRDTVTQDNGIRPSSLDQMAKLKPAFIKPYGTVTAANSSFLTDGASAVLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDVFEFHEAFSGQILANLKAMDSDWFAQNYMGRKAKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.
O46629
A7GJW3
PTH_BACCN
Peptidyl-tRNA hydrolase
Bacillus cereus group
MKLIVGLGNPGREYELTRHNIGFMAIDELAKRWNISLNEQKFKGMFGAGFVNGEKVILLKPLTYMNLSGESIRPLMDYYKIDLEDFIIMYDDLDLPVGKLRLRMKGSAGGHNGVKSTIAHLGTQEFQRIRMGIDRPKNGMKVVDYVLGRFTAEEMVDVNHAIEKAANACEEWLNKSFLQVMNDFNN
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
A7GJW3
C3P786
DEOC_BACAA
Phosphodeoxyriboaldolase
Bacillus cereus group
MNIAKLIDHTILKANTTKEDVMKVIEEAKEYKFASVCINPTWVKLAAEELAGHDVDVCTVIGFPLGASTTETKAFETKDAIAKGATEVDMVINVGALKDGDNELVEKDIYEVVQAAKGKALVKVIIETCLLTDEEKVRACELSVKAGADFVKTSTGFSTGGATAEDIALMRKTVGPNVGVKASGGVRTREDAEKMVAAGASRVGASASVAIVLNDAKGATDNY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
C3P786
A4X4N7
IF2_SALTO
Translation initiation factor IF-2
Salinispora
MAGKARVHELAKELGVESKTVLAKLKEMGEFVKSASSTVEAPVARRLRNAFVNNTGSPAPAAPPAATPPTPTPTPTPPRTPTPAPPPGGPRVTAKPMPPRRPGAPTPGPKPKGPVPGPPQSATPAAKPASAHDIEVAAAEARAAALKAEQEAAVKAAQAARQQQRDNVRREPPTEGGPRPGPRPGPGAMPPRPGSPAAGRSGGPTPGPGPRSGGRPPARGAGNNPFGIQGGQQRPPAAGAGGPRPSPASMPPRPSPASMPPRPSPASMPSQRPGRPGGPGSGRPGAGAGRPGGGGGGGGGYRGGGGGGGGGYRGGPGGGGGGGGGGGYRGGPGGGGGGFRGGPGGGRPGGGGRGRGGGAAGAFGRPGGRPTRGRKSKKQRRQEFDNLSAPTMSSGAPRGQGQTVRLSRGASLSDFADKINANPGSLVQEMFNLGEMVTATQSCSDDTLLLLGEHLGFVVQIVSPEDEDRELLAQFNIDLDAEVAEDRLVSRPPVVTVMGHVDHGKTKLLDAIRKANVVAGEAGGITQHIGAYQVHVPHDDQDRAITFIDTPGHEAFTAMRARGAQVTDIVILVVAADDGVMPQTIEALNHAKAADVPIVVAVNKIDKPDANPDKVRQQLTEYGLVAEEYGGDTMFVNVAAKPGTGIDSLLEAVLLTADASLELTAPTDGPAQGVAIEAHLDKGRGAVATVLVQKGTLRAGDSIVAGGAHGRVRAMLDENGNQVAEAGPSRPVLVLGLTAVPGAGDTFLAAEDDRTVRQIAEQRQARRRAAAFANSRGRATLETLMEQLKAGEKTSLNLVLKGDVSGSVEALEDALFNLDIPEEVQLRIIHRGVGSITESDVMLASASSEAVTIIGFNVRAANKVREMADREGVEIRYYTVIYQAIEEIEAALKGLLKPEYEEVELGTAEVREVFRSSKVGNISGCIVRSGLLRRNAKARLLRDGAVVADNLTIGSLKRFKDDATEVREGFECGLTLAGYNNVQVGDVIETFEMREKARV
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
A4X4N7
P17867
CISA_BACSU
Stage IV sporulation protein CA
Bacillus
MIAIYVRVSTEEQAIKGSSIDSQIEACIKKAGTKDVLKYADEGFSGELLERPALNRLREDASKGLISQVICYDPDRLSRKLMNQLIIDDELRKRNIPLIFVNGEYANSPEGQLFFAMRGAISEFEKAKIKERTSSGRLQKMKKGMIIKDSKLYGYKFVKEKRTLEILEEEAKIIRMIFNYFTDHKSPFFGRVNGIALHLTQMGVKTKKGAKVWHRQVVRQILMNSSYKGEHRQYKYDTEGSYVSKQAGNKSIIKIRPEEEQITVTIPAIVPAEQWDYAQELLGQSKRKHLSISPHNYLLSGLVRCGKCGNTMTGKKRKSHGKDYYVYTCRKNYSGAKDRGCGKEMSENKLNRHVWGEIFKFITNPQKYVSFKEAEQSNHLSDELELIEKEIEKTKKGRKRLLTLISLSDDDDLDIDEIKAQIIELQKKQNQLTEKCNEIQSKMKVLDDTSSSENALKRAIDYFQSIGADNLTLEDKKTIVNFIVKEVTIVDSDTIYIETY
Putative site-specific recombinase having a very important role in sporulation. It probably plays a role in the recombination of SpoIIIC and SpoIVCB to form sigma K factor.
P17867
A5W9A9
SSRP_PSEP1
Small protein B
Pseudomonas
MAKQKKHPTGTIAQNKKARHDYFIEHKFEAGLVLSGWEVKSLRAGKAHLTDSYVLLKDGEAWLFGSHITPLTTASTHVIADPTRTRKLLLNKRELERVEAAVAQKGYTCVALALYWSKHLIKCEIALGKGKKEFDKRDTMRERDSNRELQRAVRNKGKEE
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
A5W9A9
Q5U1X0
TAF11_RAT
Transcription initiation factor TFIID 28 kDa subunit
Rattus
MDNLGESPTDKAGEPGESEETRATPGAPVSADTEGIPEETDQVGDADSKEAAAEESELKSQDVSDVTAAEREDPSLLTPAAKKLKLDTKDKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKGQIPNSKHKKITFF
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes.
Q5U1X0
Q2YLI7
PROA_BRUA2
Glutamyl-gamma-semialdehyde dehydrogenase
Brucella
MTKDIAQVMAEVGRKAKAAAAPLSIATSEQKNKALNAAADAILEARADILEANRLDLANAEKNGMAASFVDRLTLNEARIDAIAEGIRAIATLPDPVGEVIAEWDRPNGLHIERVRTPLGVIGVIYESRPNVTADAGALCLKAGNAVILRGGSDSAHSSAAIHKALVKGLEAANLPADAIQIVPVTDRAAVGEMLKGLGGAIDVIVPRGGKSLVARVQSEARVPVFAHLEGICHLYIDKSADLDMARRIALDAKMRRTGICGAAETLLVDRAVASTHLAPILGDLAAGGCEIRGSAEVLALYPAAKPATEEDWSTEYLDAIISVALVDGISGAIDHINRYSSHHTEAIVAEDAQTVARFFNEIDSAILLHNASTQFADGGEFGMGAEIGIATGKMHARGPVGVEQLTSFKYRVRGSGQVRG
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Q2YLI7
P69686
PSBD_TOBAC
Photosystem Q(A) protein
Nicotiana
MTIALGKFTKDENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFAVGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL
Photosystem II (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. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
P69686
P33536
RBL_OSMCI
Ribulose bisphosphate carboxylase large chain
Osmundastrum
GIGFKAGVKDYRLTHYTPDYETKDTDILAAFRMTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRSEDSRIPPAYSKTFIGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEALFKAQAETGEIKGHYSNATAGTCEEMMKRAVFARESGAPIVMHDYSTGGFTANTSLAFYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSMPGVFPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLARQGNEIIREAAKWSP
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
P33536
P15241
K2M2_SHEEP
Keratin, type II microfibrillar, component 7C
Ovis
CGFSTVGSGFGSRAFSCVSACGPRPGRCCITAAPYRGISCYRGLTGGFGSRSVCGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKCLNNRFAAFIDKVRFLEQQNKLLETKLQFFQNRQCCESNLEPLFEGYIETLRREAECVEADSGRLSSELNHVQEVLEGYKKKYEQEVALRATAENEFVALKKDVDCAYVRKSDLEANSEALIQEIDFLRRLYQEEIRVLQANISDTSVIVKMDNSRDLNMDCIVAEIKAQYDDIASRSRAEAESWYRSKCEEIKATVIRHGETLRRTKEEINELNRVIQRLTAEVENAKCQNSKLEAAVTQAEQQGEVALNDARCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEQRLCEGVGAVNVCVSSSRGGVVCGDLCVSGSRPVTGSVCSAPCSGNLAVSTGLCAPCGQLNTTCGGGSCSLGRC
Wool microfibrillar keratin.
P15241
A6TCG5
GLYA_KLEP7
Serine hydroxymethyltransferase
Klebsiella
MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGIDESGKIDYDDMAKQAQEHKPKMIIGGFSAYSGIVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDDAVIERVKGKVLDICARFPVYA
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
A6TCG5
P28808
LCRF_YERPE
Thermoregulatory protein LcrF
Yersinia
MASLEIIKLEWVTPIFKVVEHSQDGLYILLQGQISWQSSGQTYDLDEGNMLFLRRGSYAVRCGTKEPCQLLWIPLPGSFLSTFLHRFGSLLSEIGRDNSTPKPLLIFNISPILSQSIQNLCAILERSDFPSVLTQLRIEELLLLLAFSSQGTLFLSALRHLGNRPEERLQKFMEENYLQGWKLSKFAREFGMGLTTFKELFGTVYGISPRAWISERRILYAHQLLLNGKMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSQARLTKIATTG
Transcriptional activator of the thermally regulated virulent yopE gene. LcrF activity could be modulated by the interaction with an inducer molecule serving as a temperature messenger. The availability of the messenger would in turn be controlled by a temperature-responsive process serving as a cellular thermometer.
P28808
P0C0N1
OTC_STAES
Ornithine carbamoyltransferase
Staphylococcus
MKNLRNRSFLTLLDFSRQEVEFLLTLSEDLKRAKYIGTEKPMLKNKNIALLFEKDSTRTRCAFEVAAHDQGAHVTYLGPTGSQMGKKETAKDTARVLGGMYDGIEYRGFSQRTVETLAQYSGVPVWNGLTDEDHPTQVLADFLTAKEVLKKEYADINFTYVGDGRNNVANALMQGAAIMGMNFHLVCPKELNPTEELLNRCERIATENGGNILITDDIDKGVKDSDVIYTDVWVSMGEPDEVWQERLKLLKPYQVNQALLEKTGNPNVIFEHCLPSFHNAETKIGQQIYEKYGISEMEVTDDVFESKASVVFQEAENRMHTIKAVMVATLGEF
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
P0C0N1
Q6LQC0
HMUV_PHOPR
Hemin import ATP-binding protein HmuV
Photobacterium
MTFGPQPNSLTPLINNQICKKKVAIHAQGLNLILGGKTLLDNFDIDINAGEVTALLGPNGAGKSSLLKVLCGEIEATGSIEFFGQNRKQWSAKALAKHLGVLPQHSTLNFAFLAHEVVELGGLPLELSNIQTQQITQEKMALVDVCDLSHRLYPSLSGGEKQRVHFARILTQVSQAGDQCVLMLDEPTSALDLAHQHRTLQVAKELASNGAAVIIVLHDLNLAAQYADRLVIVNHGLIQADGTPWQALQPDIIERVYGWPVYISSHPTGDFPVILSH
Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Q6LQC0
Q21C20
ISPG_RHOPB
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Rhodopseudomonas
MNKLENPLSHDVAGPAPRHKTTQVMVGDVAVGGGAPIVVQSMTNTDTADVAGTVEQVAALTRAGSELVRITVDREEAAAAVPHIRDALRKRGITTPLIGDFHYIGHKLLADYPACAEALDKYRINPGNVGFKNKRDSQFADIVEIAIKNNKAVRIGANWGSLDQELLTKLMDENAVSAKPRDVRAVTREAMVQSALLSAARAEEIGLAKNKMVLSAKVSAVQDLIAVYQDLASRSDYAIHLGLTEAGMGSKGIVASSAALGILLQQGIGDTIRISLTPEPGGDRSLEVQVAQELLQTMGFRTFVPLVAACPGCGRTTSTTFQELARSIQDFIRVEMPAWKTRYPGVENLNVAVMGCIVNGPGESKHANIGISLPGTGETPAAPVFVDGQKFRTLRGANISGEFKALVIDYIEQRYGAGVAAPVTVTAAE
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q21C20
Q6MBU9
RIMO_PARUW
Ribosome maturation factor RimO
Candidatus Protochlamydia
MLPILKNQGVKKDQNHIALKNDSCESSSPCFDHEGNKINFISLGCPRNLVDSEVMLGILLKAGYEVAPTLEEADYLVINTCGFLEASRQESMDTVEEVLSQRKKTAKLIVTGCMVQTHSDALKTTFPSIDYLLGSGDVEGILKAVQSTQKGQIISSARSYLEAGEVPRRLSTPKHYAYLKIAEGCRKRCAYCVIPTIKGPLKSKGKEQILKEFNLLLSQGVKEVILIAQDLGDYGKDQGAKKLTALLNLLQSMLEIKQAFWLRLLYLYPDEITDELIALMKSDSRICPYLDMPIQHVNNQILKSMRRATSKEDIIEIITKLRREIPNVAIRTSLIVGFPGETEEQFQELIQFVQDYPLENVGIFKFSREPGSHAYDLPNQISDEMKEDRYHRLMQVQKKVVKKNLKKMIGKKIAVVVEGYHPETELLMIGRHTGQCPDIDGQVLINDGRKVKAFGEIYTVEITDVADYDLVGHVI
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
Q6MBU9
B5FG22
RS14_ALIFM
30S ribosomal protein S14
Aliivibrio
MAKQSMKAREAKRAKLVAKFAEKRAALKVLISDVNASEEERWDAVLKLQALPRDSSASRQRNRCNQTGRPHGYLRKFGLSRIKVREACMKGEIPGLRKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
B5FG22
A4XL78
RLMN_CALS8
tRNA m2A37 methyltransferase
Caldicellulosiruptor
MKRLIKDFTFDELKKWVEETGEKPFRANQIFEWLYKKNATDVNSFTNIPTQLRKRIEEEFILNSLRVVKYESDGESIKFLLELVDGNAIESVFLPYKYGNAICISTQVGCRMKCAFCASTIGGMIRNLSAGEMVDQIVNIENITKKKISNVVLMGSGEPFDNIENVFKFIDIINSKEGKNIGARHITISTVGIVDGIYKLSEYPKQVNLAISLHAPNNNLRNKLVPMNRKYSIEDILKAVDYYISKTNRRVTFEYALIDGVNDSIECANELAKILSGKLVHVNLIPVNPVNGRNFKKPPKERVKEFYNVLILSGIQVTIRRELGSSIAAACGQLRSRHYNISEK
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
A4XL78
B8HX39
ANMK_CYAP4
AnhMurNAc kinase
unclassified Cyanothece
MHVIGLISGTSVDGIDAALVDLSGTSLDLQVELLAAHTYPYSEPVRSQIISLCKGEAIPLAELALLDEAIAQEFAQAALEIQQGQPAAELIGSHGQTVYHRPVIGNTPAYTLQLGRGAIIAQQTGLPTITNFRVADTNAGGEGAPLVSRIDICLFSHPQQRRCVQNIGGIANLTYLPPLSDVAQIGVGVQGWDTGPGNSLLDLAVQYLSGGRQAYDDKGNWAAQGTPCQALVEQWLSHPYFEQAPPKSTGRELFGWDYLQTCLRDAEPYHLSAEDFLATLTELTAASIVLNYRQFLPALPDQVLLCGGGVRNHYLKQRLATLLTPIPVLSTNEVGLSADAKEAIAFAVLGYWRYLGLPGNVPAVTGARREVLLGELHTYP
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
B8HX39
P58602
CPI4_SOLTU
PCPI-23
Solanum
PVLQVVRDIHGDILTPDSRYIL
Inhibitor of papain (cysteine protease). Does not inhibit trypsin, chymotrypsin nor elastase (serine proteases). May protect the plant by inhibiting proteases of invading organisms.
P58602
P0A3S9
PAL_BRUAB
Outer membrane lipoprotein Omp16
Brucella
MRRIQSIARSPIAIALFMSLAVAGCASKKNLPNNAGDLGLGAGAATPGSSQDFTVNVGDRIFFDLDSSLIRADAQQTLSKQAQWLQRYPQYSITIEGHADERGTREYNLALGQRRAAATRDFLASRGVPTNRMRTISYGNERPVAVCDADTCWSQNRRAVTVLNGAGR
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
P0A3S9
Q9MAP5
SBT33_ARATH
Subtilase subfamily 3 member 3
Arabidopsis
MRSFRSSILLVLLSLITVLNATRARSETESKVHIVYLGEKKHHDPEFVTESHHQMLASLLGSKKDADDSMVYSYRHGFSGFAAKLTKSQAKKIADLPEVVHVIPDGFHELATTRTWEYLGLSSANPKNLLNDTNMGDQVIIGVIDTGVWPESESFNDNGVGPIPRKWKGGCESGENFRSTDCNRKLIGAKYFINGFLAENKGFNTTESRDYISARDFDGHGTHVASIAGGSFVPNVSYKGLAGGTLRGGAPRARIAMYKACWFHEELKGVTCSDSDIMKAIDEAIHDGVDVLSISLVGQIPLNSETDIRDEFATGLFHAVAKGIVVVCAGGNDGPAAQTVVNIAPWILTVAATTLDRSFPTPITLGNNKVILGQATYTGPELGLTSLVYPENARNNNETFSGVCESLNLNPNYTMAMKVVLCFTASRTNAAISRAASFVKAAGGLGLIISRNPVYTLSPCNDDFPCVAVDYELGTDILSYIRSTRSPVVKIQRSRTLSGQPVGTKVVNFSSRGPNSMSPAILKPDIAAPGVRILAATSPNDTLNVGGFAMLSGTSMATPVISGVIALLKALHPEWSPAAFRSAIVTTAWRTDPFGEQIFAEGSSRKVSDPFDYGGGIVNPEKAAEPGLIYDMGPQDYILYLCSAGYNDSSISQLVGQITVCSNPKPSVLDVNLPSITIPNLKDEVTLTRTVTNVGLVDSVYKVSVEPPLGVRVVVTPETLVFNSKTISVSFTVRVSTTHKINTGYYFGSLTWTDSVHNVVIPLSVRTQILQNYYDEN
Serine protease that plays a role in the control of the establishment of immune priming and systemic induced resistance.
Q9MAP5
Q8FK20
ENTS_ECOL6
Enterobactin exporter EntS
Escherichia
MNKQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFVGLMVGGVLADRYERKKVILLARGTCGIGFIGLCLNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVISPMIGGLLLATGGVAWNYGLAAAGTFITLLPLLSLPALPPPPQPREHPLKSLLAGFRFLLASPLVGGIALLGGLLTMASAVRVLYPALADNWQMSAAQIGFLYAAIPLGAAIGALTSGKLAHSVRPGLLMLLSTLGAFLAIGLFGLMPMWILGVVCLALFGWLSAVSSLLQYTMLQTQTPEAMLGRINGLWTAQNVTGDAIGAALLGGLGAMMTPVASASASGFGLLIIGVLLLLVLVELRRFRQTPPQVTASDS
Component of an export pathway for enterobactin.
Q8FK20
C4LEG3
AROA_TOLAT
5-enolpyruvylshikimate-3-phosphate synthase
Tolumonas
MNTLTLEPIARVEGTVNLPGSKSVSNRALLLAALARGTTRLTNLLDSDDIRHMLNALKTLGVSYELSANKTECTVHGLGRAFSSSEPVNLFLGNAGTAMRPLCAALCLSNGEFTLTGEPRMEERPIAHLVDALRQAGAHVHYLKKDGYPPLTIEGKGLWGGEVVIDGSVSSQFLTAFLMAAPLASGDVRIRIRGELVSKPYIDITLHIMKQFGVTVEHDDYQVFYVRGNQTYVSPGTFLVEGDASSASYFLAAGAIKGKVRVTGIGKNSIQGDIRFADVLEKMGAKITWGDDFIEAENVGELQAVDLDMNQIPDAAMTIATAALFANGKTAIRNIYNWRVKETDRLTAMATELRKVGAEVVEGHDFIEITPPAQLKHAAIDTYNDHRIAMCFSLVALSDTKVTINDPGCTSKTFPDYFTKFASVSQR
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
C4LEG3
A2CBN5
MTND_PROM3
Acireductone dioxygenase (Ni(2+)-requiring)
Prochlorococcus
MSRLSIHPEGNTNATSPAEPLLESDDPAVIKAELAKRGIEFQHWPAKVKLHQNSIESDILAAYAVEIARVQADGRYPTVDAIRITPDHPDREALRQKFLAEHTHAEDEVRFFVEGRGLFCLHIGAEVLQVLCEQNDCINVPAGTRHWFDMGSKPQFCAVRFFDNPEGWIASFTGDAIAERFAKLP
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
A2CBN5
Q20EU1
CEMA_OLTVI
Chloroplast envelope membrane protein
Oltmannsiellopsis
MDSESQLLEGAVEKIGLIPRSIIRTINRFQQQLFPDAVEYFIQEFRVSRSQVLVSLQCLLTLIIIPLFIHFFAKTVFLTPCIEYVWNTYKTDIFLNSYQQEQALTEMRNFEEILYFDLLVQSNEEPVTQEGLPFTFLQHSQGSVDEEKTTAPITAYAVSNMGNPETATIAPQHLHGSVGGKLESEFRFTNPSFVGKNNVTGATTITAAIPLQKKLVDLAQSANKQSIAALTNLFADLLTLFSLIILFIRLKSQIIILKSFLIETFYSLNDTTKSFMLIFSTDLLVGFHSPRGWEIFLDFILSRFGLPHDENIILLFVATFPVLLDSVIKYWIFRYLNKISPSTVATYHAMIE
May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Q20EU1
Q0IQN6
DRB8_ORYSJ
dsRNA-binding protein 8
Oryza sativa
MDMPPTPLPPETANTSPAPNGATAGIRVENCYVFKSRLQEYAQKTGLQTPEYHTFKEGPSHEPVFKSTVVINNTSYDSLPGFFNRKAAEQSAAEVALMEIVKSIPANANIPAVQETGLCKNLLQEYAQKMNYAIPSYICTKSASGLAPFICTVEIGGIQYIGAAARTKKDAEIKAARTALLAIQGQSEGSANGATKYIVVPGKRVGKEVEKRPIETPKPLKVKKGGFKKKWNKRKFMKKDGQAVDVEKDEARVAGDAHDSDVLMQPTVITQEASCGTLFLQPCEEAKRVEAEPPRDIEMVQPDKENQHSDAALVQPDDEARVEQEPSRDISVVQPNEEAISGKQEPSIDAAILQPKEEASSVKQEPFIDTAMLQACKEAGSVELGPARDTVISQLNEQDRAVKQEPAGDIVVPQPDVHARVVKE
Binds double-stranded RNA.
Q0IQN6
P85117
TX1_GRARO
GrTx1
Grammostola
YCQKWMWTCDSKRKCCEDMVCQLWCKKRL
Inhibits voltage-gated sodium channels Nav1.1/SCN1A (IC(50)=630 nM), Nav1.2/SCN2A (IC(50)=230 nM), Nav1.3/SCN3A (IC(50)=770 nM), Nav1.4/SCN4A (IC(50)=1290 nM), Nav1.6/SCN8A (IC(50)=630 nM), Nav1.7/SCN9A (IC(50)=15.3-1000 nM) and potassium channels Kv11.1/KCNH2 (IC(50)=4.2 uM).
P85117
P10901
FUCO_DICDI
Alpha-L-fucoside fucohydrolase
Dictyostelium
MKMIIIFFILLILNLIKSQQYGPTWDQINSRPLPGWYDDVKFGIFIHFGIYSVPAFANGGYAEWYWWTLKNPSSDGGATQRYHEKEFGANFTYQDFVSRFDCRLFDANEWASIIEKSGAKYVVLTSKHHEGYTLWNSEQSWNWNSVETGPGIDIVGELTKSVKNMGLHMGLYHSLFEWFNPLYLADAETGKNPTTQVYVDEILMKQLKDIVTTYEPELIWADGDWMQLSNYWKSTEFLSWLYTNSSVKDTVIVNDRWGSECRDKNGGFYTGADHFNPYKLQSHKWENCATIGYSYGYDEYEQATDYQNATELIIDLVTTVACGGNFLLDVGPDAQGTIPNNMVDRLLEIGNWLSINSESIYGSSPWRVQNMTFNIWYTTNTTNGNVYAFVFELPDDGVLILSDPIGNNKTEATLLGLKGEKGVEVSLPIESTKPGITLNIPMVAPQDYPPYVYVFRLTDVE
Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
P10901
B0SC03
TRUA_LEPBA
tRNA-uridine isomerase I
Leptospira
MPNYALLVEYDGTHFNGWQKQKNLPTVQSSIESALGIILRRNPASRLSVAGRTDTGVHALGMVCNFKTEHPIPNFHKLLVSLNALTPTGVSVKNVVEVPSDFHARFSCTGREYIYKLYYSKYESSFVEGRAFWVKGHIDWERVKKQLQVLVGEKDFRSFTKAKSMAGKRAVREILAIQLENLSPEWYQIRIRANGFMHNMVRITVGTLLDIGKGRWESRSIDSILEEKNRTQAGVTLPPDGLYFVRAYYEDHPEIHELYKIPLP
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
B0SC03
P0DL16
CRVP_NAJMO
Cysteine-rich venom protein mossambin
Naja
NVDFNSESTRRKKKQNEIVDLHNSLRRTVN
Inhibits calcium-activated potassium channels (KCa), voltage-gated potassium channel (Kv), and the calcium release channel/ryanodine receptor (RyR).
P0DL16
B7JZP4
ACCA_RIPO1
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Rippkaea orientalis
MSKNERRTFLLDFEKPLWELEARINQIRELAEENNVDVSEQIAQLERRAEELRQEIFSTLTPSQRLQLARHPRRPSTLDYIQAIADEWFELHGDRGGYDDPALVGGVARLGGRPVTILGEQKGRDTKDNVARNFGMASPGGYRKAMRLMERANQFNQPIITFIDTPGAWAGVEAEKLGQGEAIAYNLREMFRLDVPIICTVIGEGGSGGALGIGVGDRLLMLEHAVYMVATPEACAAILWKDAKKSPQAAMALKITSSDLKELGIIDEIVPEPSGAAHSKPLEAANLLKQTLIDTIDELSSLSPEQRRKLRYQKYRQIGVFFES
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
B7JZP4
Q3ZXS0
NUOB_DEHMC
NDH-1 subunit B
Dehalococcoides
MELNFEKPLSLLTLDEIDQQEGGVIQSFRTGHTSPYPDPADWLNGEEPPPGVFITSVEKVLNWSRHYSLWPVMFGLACCAIEMMCMAASRWDLARFGMDIFRASPRQADLMIVAGTLTWKMAPWLKRIYDQMPEPKWVLAMGACGTSGGLFRDSYSVVPGFNLVVPVDVYVPGCPPRPEALMRAIMDIHEKIDKTRILKR
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.
Q3ZXS0
Q256C2
CLPP1_CHLFF
Endopeptidase Clp 1
Chlamydia
MTLVPYVVEDTGRGERAMDIYSRLLKDRIVMIGQEITEPLANTVIAQLLFLMSEDPQKDIKVFINSPGGYITAGLAIYDTIRFLGCDVNTYCIGQAASMGALLLSAGTKGKRYALPHSRMMIHQPSGGIIGTSADIQLQAAEILTLKKHLANILSECTGQPVEKIIEDSERDFFMGAEDAISYGLIDKVVSSAKDTKDKDTIS
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.
Q256C2
Q5FA58
RIMM_NEIG1
Ribosome maturation factor RimM
Neisseria
MTDTQNRVAMGYIKGVFGIKGWLKIAANTEYSDSLLDYPEWHLAKDGKTVSVTLEAGKVVNGELQVKFEGIDDRDSAFSLRGYTIEIPREAFAPTEEDEYYWADLVGMTVVNKDDTVLGKVSNLMETGANDVLMIDGEHGQILIPFVSQYIETVDTGSKTITADWGLDY
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Q5FA58
B8DZY2
RL25_DICTD
General stress protein CTC
Dictyoglomus
MEITEIKVKKRDKIGKQFAKKYRRSNLIPGVVYGAHLKENIHILVEKKDLWSLIKKGHAKEQHLLRLIIENGENTITENAILQDLQIDPIKDEFLHVDFHAITLEELVDVYVPILLVGEAKGIKQGGILQHGVEEILIRALPLDVPPHIEVDITDLEIGESITVGDLKFPENIKVLTPLDEVVVGIIPPKGYTEEVTTGEAQTESQT
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
B8DZY2
Q8BJ03
COX15_MOUSE
Cytochrome c oxidase assembly protein COX15 homolog
Mus
MQRLLLPSLRALTGSRNVGLLVPRVASRTQCGSSCGSQRPLRPGQYSTITEVALQSGKGTVSLPSRAAERAVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSQEEWEAEFQKYQQFPEFKILNHDMTLAEFKFIWYMEYSHRMWGRAVGLAYILPAAYFWRKGWLNRGMKGRVLALCGLVCFQGLLGWYMVKSGLEEKPESYDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPQHKLPETRQLLWLRRFAGGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLLTFSPVLKNVFENPTMVQFDHRLLGVTSVTAITVLYFLSRRIPLPRRTKMAAVTLLALAYAQVALGISTLLMYVPTPLAATHQSGSLALLSGALWLMNELRRVPK
May be involved in the biosynthesis of heme A.
Q8BJ03
C1KVD5
NADD_LISMC
Nicotinate mononucleotide adenylyltransferase
Listeria
MKHKVGILGGTFDPPHLAHLRMAEEAKKQLGLEKILFLPNKIPPHKHISGMASSDERVEMLQLMIEGIDSFEIDTRELMRAGKSYTYDTMRDMISEQPDTDFYFIIGGDMVEYLPKWYHIDDLVKMVTFVGVNRPSYQTEVPYDIVKINMPETTISSTEIRNNIENASTFLPEKVWSYIKEHQLYGKK
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
C1KVD5
Q92AH4
PYRK_LISIN
Dihydroorotate oxidase B, electron transfer subunit
Listeria
MLQTEMKVIQQTEIADKVYELILSGECVADMSPGQFLMLKPSRSDLLMRRPISICSYDKTAKTCILLYRVEGDGTKDFSSLSKGDSIDVLGPLGKGFDLNTIPAPKTALLIGGGIGVPPMYQLGKELADKGVQVTFVNGFQSEKDSFYEKEMTEYGTVHIATVDGSYGTQGFVTDITKNFPEEPDVIYSCGPKAMLQAVKASFPETKTYLSLEERMACGIGACYACVCPKAGDTKKQFKVCEDGPVFRADEVSL
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Q92AH4
P58182
O12D2_HUMAN
Olfactory receptor OR6-28
Homo
MLNTTSVTEFLLLGVTDIQELQPFLFVVFLTIYFISVTGNGAVLMIVISDPRLHSLMYFFLGNLSYLDICYSTVTLPKMLQNFLSTHKAISFLGCISQLHFFHSLGSTESMLFAVMAFDLSVAICKPLRYTVIMNPQLCTQMAITIWVIGFFHALLHSVMTSRLNFCGSNRIHHFLCDIKPLLKLACGNTELNQWLLSTVTGTIAMGPFFLTLLSYFYIITYLFFKTRSCSMLCKALSTCASHFMVVILFYAPVLFTYIHPALESFMDQDRIVAIMYTVVTPVLNPLIYTLRNKEVKGALGRVIRRL
Odorant receptor.
P58182
Q22RG7
H34_TETTS
Minor histone H3 variant
Tetrahymena
MARTKQTARKSTSIKAPRKQLAAKAARKSAPISGGIKKPHKFRPGTVALREIRKYQKTTDLLIRKLPFQRLVRDIAMEMKSDIRFQSQAILALQEAAEAYLVGLFEDTNLCAIHARRVTIMTKDLHLARRIRGERF
Macronuclear replacement variant which replaces conventional H3 in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Functions redundantly to H3.3. H3.4 deposition is mainly transcription-associated, DNA replication-independent. Although not essential for vegetative growth, minor H3 variants are required for producing viable conjugation progeny by affecting late developmental stages of conjugation.
Q22RG7
B2JFK6
ACPS_PARP8
4'-phosphopantetheinyl transferase AcpS
Paraburkholderia
MAIYGIGTDIVQVSRVAAVMQRTNGRFAEKVLGPDELRVYHARHARSQARGLAFLATRFSVKEAFSKAIGLGMRWPMTWRALQTLNEPSGRPTCVASGELADWLAERGITSRVTLSDERDYAVSFVIAETPDTAD
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
B2JFK6
Q884C8
SYE_PSESM
Glutamyl-tRNA synthetase
Pseudomonas
MTTVRTRIAPSPTGDPHVGTAYIALFNYCFAKQHGGEFILRIEDTDQLRSTRESEQQIFDALRWLGIEWSEGPDVGGPHGPYRQSERGDIYQKYAQQLVELGHAFPCFCTAEELDEMRAEQQAKGETPRYDGRALLLSKEEVQRRLDAGEPHVIRMKVPTEGVCVVPDMLRGEVEIPWDRMDMQVLMKTDGLPTYFLANVVDDHLMGITHVLRGEEWLPSAPKLILLYEYFGWDKPQLCYMPLLRNPDKSKLSKRKNPTSVTFYERMGFMPEAMLNYLGRMGWSMPDEREKFSLQEMVDHFDLSRVSLGGPIFDIEKLSWLNGQWLRELPVEEFASRLQTWALNPEYMMKIAPHVQGRVETFSQVAPLAGFFFAGGVTPDVKLFEHKKLSPDQVRQVMQLILWKLESLRQWEKERIMGSIQAVVEHLELKLRDAMPLMFAAITGQANSVSVTDAMEILGPDLTRFRLRQALDLLGGVSKKENKEWEKLLGAIA
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Q884C8
C0QWN8
ACKA_BRAHW
Acetokinase
Brachyspira
MNVLVINSGSSSIKYQLFAMPEAKVLAKGLLEKIGEEISALKHTAVEKGKEKKIEQKVADHKAGMSLIFSLLTDKEVGVIADMNEISAVGHRVVHGGEAFNKSILITDEAIKAIEACCDIAPLHNPAGLQGISACKEILKDVKMVGVFDTSFHQTIPDYAYMYAVPHEWYDKYKIRRYGFHGTSHKYVYGEFCKVTNKPNANVIVCHLGNGASVTAVKNGESIDTSMGLTPLEGLVMGTRSGDMDPAVPTFVMAKENLSAKEMDNILNKKSGLLGVSGVSNDMRNLEEAAKTNPKAELAITMFCYRVKKYIGAYMAALGHLDGIVFTGGIGENSAYIRGRILEGLDELGIKCDADKNSKARGCANFEKDGAAIKLYVIATDEEKAIAMDTYNLAK
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
C0QWN8
Q32I48
UVRB_SHIDS
Excinuclease ABC subunit B
Shigella
MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKAMLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTVGMIIDQRAILRRLAELQYARNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQIVSTIPRFTIYPKTHYVTPRERIVQAMEEIKEELAARRKVLLENNKLLEEQRLTQRTQFDLEMMNELGYCSGIENYSRFLSGRGPGEPPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEKSGGDVVDQVVRPTGLLDPIIEVRPVATQVDDLLSEIRQRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKAILYGDKITPSMAKAIGETERRREKQQKYNEEHGITPQGLNKKVVDILALGQNIAKTKAKGRGKSRPIVEPDNVPMDMSPKALLQKIHELEGLMMQHAQNLEFEEAAQIRDQLHQLRELFIAAS
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Q32I48
Q9V4I1
CP9B2_DROME
CYPIXB2
Sophophora
MALIEICLALVVIGYLIYKWSTATFKTFEERKLYFEKPYPFVGNMAAAALQKSSFQRQLTEFYERTRQHKLVGFFNMRTPMITLNDPELIKKVCVKDFDHFPNHQPFITSNDRLFNDMLSVMRDQRWKHMRNTLTPVFTAAKMRNMFTLMNESFAECLQHLDSSSKTLPGRKGFEVDMKVMCNKLSNDIIATTAFGLKVNSYDNPKNEFYEIGQSLVFSRGLQFFKFMLSTLVPKLFSLLKLTIFDSAKVDYFARLVVEAMQYREKHNITRPDMIQLLMEAKNESEDKWTDDEIVAQCFIFFFAAFENNSNLICTTTYELLYNPDVQERLYEEIVETKKALNGAPLTYDAVQKMTYMDMVISESLRKWTLAAATDRLCSKDYTLTDDDGTKLFDFKVGDRINIPISGLHLDDRYFPEPRKFDPDRFSEERKGDMVPYTYLPFGVGPRNCIGNRYALMQVKGMLFNLLLHYKIEASPRTIKDLWGSASGFNFTPRSGFWMHLVPRK
May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Q9V4I1
Q981J9
CH605_RHILO
Chaperonin-60 5
Mesorhizobium
MAAKDVKFSRDARERMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTNDIAGDGTTTATVLAQSIVQEGHKAVAAGMNPMDLKRGIDLAVADVVATLIKNAKKIKTSEEVAQVGTIAGNGDSSVGSMIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNADKMVADLEDAYILLHEKKLSNLQAMLPILEAVVQTSKPLVIISEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGQVISEDLGIKLENVGLNMLGRAKKVSISKENTTIVDGAGKKAEIQGRVAQIKQQIEETTSDYDKEKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALNATRAAVEEGIVPGGGVALLRASLSINAVGANSDQTAGISIVRRALQAPARQIAANAGAEASIVAGKILENKGATYGYNAQTGEYGDMIAMGIVDPVKVVRTALQDAASVAGLLVTAEAMIAEAPKKESAGGGMPGGMPGGGMGGMGGF
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.
Q981J9
Q9MUS0
PSBK_MESVI
Photosystem II reaction center protein K
Mesostigma
MNIGFDMILAKLPEAYAMFDPLVDVLPVIPLLFLLLAFVWQASVSFR
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.
Q9MUS0
P05630
ATPD_BOVIN
F-ATPase delta subunit
Bos
MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
P05630
Q165E3
GLGC_ROSDO
ADP-glucose synthase
Roseobacter
MNREEQRLAQQTMAFVLAGGRGSRLYELTDRRAKPAMYFGGKSRIIDFPLSNAVNSGIRRIGVATQYKAHSLIRHLQRGWSFFRAERNESLDILPASQQMNDENWYKGTADAVAQNKDIIEGYGPKYIIILAGDHIYKQDYAEMIRHHVESGADVTVGCIEVPRMEASGFGVMKVDTEDRILDFIEKPGDPPAMPGHPDQALASMGIYVFETEYLFKIMEECAAVPGYSHDFGGDIIPTIVRGGKAVAHPFSRSCVRTVNEEAPYWRDVGTVDAFWQANLDLTDFKPALDLYDTEWPIWTYSELTAPAKFIHNEEGRRGSAVSSMVSGGCIISGSSLERCLLFTGVRTHSFSQLNGVVSMPYAIINRNARLTNVVVDRGVVIPQGLVVGEDPALDAQRFRRTDSGVCLITQPMIDKLDM
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Q165E3
B1Y222
MNMC_LEPCP
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Leptothrix
MRRSNPITPARLGRSAEGLPFSEDFGAPYHPSAGALAQAEQVFLRGTDLPARWAGQARHVILETGFGLGHNFLATWAAWRRDPRRCERLVYLAIDKHPPAPADLADVHRDSPLADLAAQLIAAWPLATPDLHLLDFEGGRVQLMLALGDIHDVLPGLQAEAHSLYLDGFVPARNPAMWSADVFKRIARLAAPGAMAASGHADSAVRDGLVRQGFEVRATGADATVARYAPRFQPEPPRGWRWPHAAAREALVIGGGLAGCAVAQALALQGWRSTVIDRQAGPAQETSGNAGGLMHGIFNAPDSPHARWFRAAAMHTARNAAAGLAAGELAGTLAGFLRLDERLNTTQAEAQLSAVGLPRAWLAWLDVAGARAAAGLELPCGAWHYGAAGWLDPAGYSRWMLQSAGDSARWIGGTGVAALRGPRDGAADHHGGWQAIDRHGRVIASAPVLVLANALDAARLLPAHCPPPGLSAVRGQVTRIPAGTPGLRPPRLTVAGQGYALRLDNGDVLVGATTQDEPVGIDGAALRLADQQRNLQRAAGLGVLDATAAEFGTTLLPGRAGWRAVTADRLPLVGPPIDLAQLAQARGGRVRLDAHRHQPRCVDDRSGLYLCTGLGSRGITSAALAGRLLAAWVSGAPAPVDADLRNALDPARLSK
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
B1Y222
Q1D5J5
NHAA1_MYXXD
Sodium/proton antiporter NhaA 1
Myxococcus
MAQTPPTSEARPRPPVPTLFRVALAPIQAFFRLEAASGILLALCAVAAMVWANSPWAATYSAVFDARMTVGLAGVHAGFTIREFINDGLMTLFFFVVGMEIKRELSSGELRTFSRAVLPLIAAMGGMIVPAALYAAFNQGTPAQAGWAIPMATDIAFSIGCLTLVKTRVSHGLVVFLTALAIFDDIGGILVIALFYGSGLHVSWLVGALGVLAVLACLNHFQVRNGVAYALAGAALWYTMHHGGIHATLSGVVLGLFMPARPLRPGRHVLEELRLYVDRALQTAMDEATRGAQILYLEERLEELEPPLNRFVHLWHVPVAYGIVPLFALANSGISLEGMGWADLLRPLPLGIIAGLFVGKQVGIFLFTWGSLKLGVADRPGGATLPQLHGVAVVAGIGFTVALFVAGLAFPTQPELLTEAKLGILVGSLLSAVVGYALLRFVAKPAVPA
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Q1D5J5
Q9FJ74
WAXS3_ARATH
Wax synthase 3
Arabidopsis
MEEELKNFIKLWISAIISISYCYYLSTGIKAGVFRLLSVLPVCALFLVFPLFFSYVHFSGCMAFFLSWLANFKLILFSFDQGPLSPLPRTLSRFICITCFPIKPQQNPNIQNYKIPIWLFAIKVVIFVVLLQMYEYKQYLSPALLLVFNSLHIFLELEIVFMLVKALVFITLGCDLEPQSNEPYLATSLQDFWGRRWNLMVPAILRPAVYLPARRMACRKVNSDQAMFLGVFAAFLVSGAVHEMLFFYLTREVPTGEVTWFFLLHGVCTVAEVAVKKSTFVRRWWRVSPTVSRLLTVGFVVVTSGWFFFPLIRSGIIERLASEALMCIDFVKHKFLLLLLGD
Catalyzes the final step in the synthesis of long-chain linear esters (waxes).
Q9FJ74
P12018
VPREB_HUMAN
V(pre)B protein
Homo
MSWAPVLLMLFVYCTGCGPQPVLHQPPAMSSALGTTIRLTCTLRNDHDIGVYSVYWYQQRPGHPPRFLLRYFSQSDKSQGPQVPPRFSGSKDVARNRGYLSISELQPEDEAMYYCAMGARSSEKEEREREWEEEMEPTAARTRVP
Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.
P12018
A2SPS3
COFD_METLZ
2-phospho-L-lactate transferase
Methanocorpusculum
MITVFSGGTGTPKLIRGLRQILHDHEITVVVNTAEDLWMSGLYVSPDIDTVQYLFSGLLNTDSWWGIRGDSFETFHAMEKLGYTELLPLGDKDRATNIARAEFLRQGMTLTEATEKIAKGYGVSARILPMSDQNVASYVVCEDDSLMHYQEYWVGKRGNVNIKGVVRKTTDGLPLKTTPEVISAIEESDGVIIGPSNPVTSIGPILECAGVREALQNTFTAAVSPFIGNRPVSGPAAALMKAWGYESTSYGTWQVYKDVVDLFIQDVRDTAIEVPGAHRLDTMMTNEKKAESLAWDLLSYFPRK
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.
A2SPS3
Q4JBV4
LIPA_SULAC
Sulfur insertion protein LipA
Sulfolobus
MKSEVVVRINENFKKLSRIVSEKGISTVCEEALCPNIMECWGSGTATFMIMGDICTRGCRFCYVKKGKPVLLDHEEPIKVAEAVREMGLDYVVITSVDRDDLADGGASHFSQVVKAVKEMNPDVIVEVLTPDFMGNKELVEKVIGSGVDVFAHNVETVRSLTPLVRDARASYEQSLRVLSYAKNVVKKSSILLGLGESLEEVVETMKDLRNVGVDILVLSQYMRPSIKQLEVKKRYNMEEYKELEKIAYSLGFSYVVALPHARTSYRAKEAYLRAMANVKNNNRWS
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Q4JBV4
B1KZM3
ERA_CLOBM
GTPase Era
Clostridium
MFKSGFVTIVGRPNVGKSTLLNAIMKEKLSIVSCRPQTTRNNIQTILTEDNYQLVFVDTPGIHKPKHKLGEYMVKSASDAMKDVDLVLFLINPDEKPGRGDLFIIEQLKEVKVPVFLVLNKIDENPQEKVAETLKTYSELMEFEEIIPISALKGKNIDLLKELMFKYIPEGPQYYPEDMIIDQNERFIVAEIVREKALRLLSEEVPHGIAVEILQMKRNEKGTYHIEGNILCEKNSHKPIIIGKGGSKLKKISQYARQDIEAFLQSKVYIRLWVKVKEEWRDNQSLLKELGYKNMK
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.
B1KZM3
Q08465
YNG1_YEAST
ING1 homolog 1
Saccharomyces
MEHLANENSDSDIRYSFLSTLDHLPCELIRSLRLMQTIDLFKNEEDEPGMERACRDLLLVATYINDLVDDQIHFLKQHKKELEIQKSVTKNFNSSLENIKSKLTLEEPGAYKEPKLLLKINLKKAKSRERKESITSPTIGINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLKQAPKGKWYCSKDCKEIANQRSKSKRQKRRK
Histone-binding component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. YNG1 is required for the HAT activity of NuA3 but not for its integrity. Mediates the interaction of SAS3 with nucleosomes.
Q08465
C0R2E2
PURA_BRAHW
IMP--aspartate ligase
Brachyspira
MASVIIVGTQWGDEGKGKIVDYLAENCEYVVRSQGGSNAGHTVVVDNIKYKLRLLPSGILHKDKVCVIGNGVVIEPKVFLSEIDSLIEKKVNISNLKISDRAHVLMPYHKILDELQEEDLGENKLGTTKNGIGPCYMDKSSRLGIRIVDLMNKETFAKKLKFNVELKNKLLKKLYNHDGVNYDELLKEYLGYAEKLRPFVADTTTILNKAIKEKKNILFEGAQATMLDLDHGTYPFVTSSYPAAGGACTGSGVGPRKIDNVIGVVKAYATRVGEGPFPSELFDDVGQFIRDKGGEYGTVTGRARRCGWLDACVVKYASYVNGLDSIAITRLDILDELDKLKICVAYKYNSEILEGYPADLDILSKVEPVYEEFEGWKTSTRDIREYDKLPENAKKYLKRLSEVIETDISIVSVGAGRDETIIVKKIF
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.
C0R2E2
P54997
DSZB_RHOSG
Dibenzothiophene desulfurization enzyme B
Rhodococcus
MTSRVDPANPGSELDSAIRDTLTYSNCPVPNALLTASESGFLDAAGIELDVLSGQQGTVHFTYDQPAYTRFGGEIPPLLSEGLRAPGRTRLLGITPLLGRQGFFVRDDSPITAAADLAGRRIGVSASAIRILRGQLGDYLELDPWRQTLVALGSWEARALLHTLEHGELGVDDVELVPISSPGVDVPAEQLEESATVKGADLFPDVARGQAAVLASGDVDALYSWLPWAGELQATGARPVVDLGLDERNAYASVWTVSSGLVRQRPGLVQRLVDAAVDAGLWARDHSDAVTSLHAANLGVSTGAVGQGFGADFQQRLVPRLDHDALALLERTQQFLLTNNLLQEPVALDQWAAPEFLNNSLNRHR
Catalyzes the third and final step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Oxidizes 2-(2'-hydroxyphenyl)benzene sulphinate (HBPS) to 2-hydroxybiphenyl (HBP) plus sulfite . The rate-limiting step of the '4S' desulfurization pathway . The pathway substrate specificity has been augmented using mutagenesis, however no mutations allowed use of alkylated thiophenes .
P54997
Q39255
SKP1A_ARATH
UFO-binding protein 1
Arabidopsis
MSAKKIVLKSSDGESFEVEEAVALESQTIAHMVEDDCVDNGVPLPNVTSKILAKVIEYCKRHVEAAASKAEAVEGAATSDDDLKAWDADFMKIDQATLFELILAANYLNIKNLLDLTCQTVADMIKGKTPEEIRTTFNIKNDFTPEEEEEVRRENQWAFE
Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1. SCF(UFO) is required for vegetative and floral organ development as well as for male gametogenesis. SCF(TIR1) is involved in auxin signaling pathway. SCF(COI1) regulates responses to jasmonates. SCF(EID1) and SCF(AFR) are implicated in phytochrome A light signaling. SCF(ADO1), SCF(ADO2), SCF(ADO3) are related to the circadian clock. SCF(ORE9) seems to be involved in senescence. SCF(EBF1/EBF2) may regulate ethylene signaling. Plays a role during embryogenesis and early postembryonic development, especially during cell elongation and division. Contributes to the correct chromosome segregation during tetrad formation.
Q39255
Q10198
NDC80_SCHPO
NMS complex subunit ndc80
Schizosaccharomyces
MQDSSSYARRYSQAPSSSNLRTTTFGFNGLGTSRTSLAPQRTLVNARQSIDPDGLSSRVLTPTMRPSLAPNTRRSSVRVSNASFISQTPNITSIKDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIFKHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVEQNSLDDHLVDKVLFDYLVRTYHLYLDESPEESEPEKELKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQKFNSLAYRIGIVPIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQIAHACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDLKMDYQKELDDLSRSEL
Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Q10198
A0T0H9
RK4_PHATC
50S ribosomal protein L4, chloroplastic
Phaeodactylum
MTIQKFITYTPLDLNGKQLNFNHELKLNILETSGNYLVHKDLIRHFGSQRQATSSSKTRSEVRGGGRKPWRQKGTGKARAGSNRSPLWKGGGVIFGPKPKKISLKLNKKERQLALQTLIYNKKNNILIIENLETGMTEPKTKAFVKICQDCQINLEQKVLLVVTDKTSVLKLATQNLKNVELLAASSLNTLSILKARQIILTSAAINHIKESYCD
Probably binds the 23S rRNA.
A0T0H9
A5CX29
RNH_VESOH
Ribonuclease H
Candidatus Vesicomyosocius
MMNRIVIYTDGGCRCNTGIGGWGVWLKYGDYDKKLKGNEKKTTNNRMELTATIKALEEIKSNQIGIDLFTDSKYVITGINEWMKNWKVKNWETSKKRPVKNVDLWQRLDVLNKQHDVIWYWVKSHSNNKGNDIADELANLAMDKISLS
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A5CX29
P65861
CRTB_MYCBO
Phytoene synthase
Mycobacterium tuberculosis complex
MTEIEQAYRITESITRTAARNFYYGIRLLPREKRAALSAVYALGRRIDDVADGELAPETKITELDAIRKSLDNIDDSSDPVLVALADAARRFPVPIAMFAELIDGARMEIDWTGCRDFDELIVYCRRGAGTIGKLCLSIFGPVSTATSRYAEQLGIALQQTNILRDVREDFLNGRIYLPRDELDRLGVRLRLDDTGALDDPDGRLAALLRFSADRAADWYSLGLRLIPHLDRRSAACCAAMSGIYRRQLALIRASPAVVYDRRISLSGLKKAQVAAAALASSVTCGPAHGPLPADLGSHPSH
Involved in the biosynthesis of carotenoids. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield phytoene (Probable).
P65861
A1S1K8
AROE_SHEAM
Shikimate dehydrogenase (NADP(+))
Shewanella
MTDRFAVFGNPISHSKSPQIHAMFAKETGQTLTYEAILAPLDGFAEAVTAFMAAGGCGANVTVPFKEQAFTLCDELSDDARIAGAVNTLIKLPDGRLRGDNTDGMGLVADLIRHGVELNNKRVLLVGAGGAARGALLPLVRAGAKLTISNRTLSKAEALAALCPKVNVEVISGSHIRSPFDVIINSTSASLSGDLPVIAANAIDNQTVCYDMMYGAKPTVFNEWARSLGAKICIDGLGMLVGQAAESFYLWRRVRPNAAPVLQTLRQSLISGV
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
A1S1K8
Q31AD1
TRHO_PROM9
tRNA hydroxylation protein O
Prochlorococcus
MKGKNYKIVSLYSFFPFQENLIIDLKSKLLEIGYENDLSGLLIFASEGINGTICAEKNVIDIVINLLNKYADNRNLNIKVNFSKKKVFKKLKIKIKKEIVTMGVPEINPSENNGTYIDSANWNKLIKNQNTIVIDTRNHYEVSVGTFQNSINPNTRNFSEFPKWVDDQLDTHLENKESTNIAMFCTGGIRCEKATSLLKKKGYKNIYHLQGGILQYLDDIPKEKNLFEGECYVFDKRVALDQELEKGSYSICHACGMPVSIQDQERKEYRKGIQCHFCIDQFSDDDRKRFEERQKQIDRLKVGNHKIFKD
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q31AD1
P04816
LIVK_ECOLI
Leucine-specific-binding protein
Escherichia
MKRNAKTIIAGMIALAISHTAMADDIKVAVVGAMSGPIAQWGDMEFNGARQAIKDINAKGGIKGDKLVGVEYDDACDPKQAVAVANKIVNDGIKYVIGHLCSSSTQPASDIYEDEGILMISPGATNPELTQRGYQHIMRTAGLDSSQGPTAAKYILETVKPQRIAIIHDKQQYGEGLARSVQDGLKAANANVVFFDGITAGEKDFSALIARLKKENIDFVYYGGYYPEMGQMLRQARSVGLKTQFMGPEGVGNASLSNIAGDAAEGMLVTMPKRYDQDPANQGIVDALKADKKDPSGPYVWITYAAVQSLATALERTGSDEPLALVKDLKANGANTVIGPLNWDEKGDLKGFDFGVFQWHADGSSTAAK
This protein is a component of the leucine-specific transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids in E.coli.
P04816
A9IW04
RS5_BART1
30S ribosomal protein S5
Bartonella
MAQKERGEREERDNEFVDRLVHINRVAKVVKGGRRFGFAALVVVGDQKGRVGFGHGKAREVPEAVRKATESAKRGMIYVPLRSGRTLHHDLEGRHGAGRVLLRSASAGTGIIAGGPMRAIFEALGMQDVVAKSLGSSNPYNMVRATFDALKHQMHPRDIAAQRGIKYSTLQARRRHLVDVEG
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A9IW04
Q5YTM8
RPOZ_NOCFA
Transcriptase subunit omega
Nocardia
MSDTKTAPAYDTPIGLTNPPIDELLERTSSKYALVIYAAKRARQINDYYNQLGDGILEYVGPLVEPGLQEKPLSVALREIHADLLEHSEGE
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Q5YTM8
Q52873
TRA5_RHIME
Transposase for insertion sequence element ISRM5
Sinorhizobium
MTKTEGKTASAAVKDILLSNPDGLREVIRTVMQEVLEAEMDEALGAAKGERTPERLGYRSGHYGRTLITRVGKLELRVPQDRSGHFSTELFERYQRSERALVATLAEMYVQGVSTRKVKAITEELCGHAFSASSISAINKRLDESLKAFAERSLEEPFAYLILDARYEKVREAGVVMSQAVLIAVGIDWDGRRQILSVEMAGRESRSAWKDFLVRLKGRGLKGVELVVSDDHAGLVAAIGEVIPEAAWQRCYVHFLRNALDHLPRKHGDDCLQELRWLYDRRDLDEAKADLAAWLGKWSVRYPRLTSWVEETIEQTLTFFRLPRQHHKHLKSTNMLERLNEEIRRRTYVVRIFPNTESCLRLVRALAVETHENWMEANRYINMDDLREHKKLALRQAA
Required for the transposition of the insertion element.
Q52873
Q0AXL3
DEF_SYNWW
Polypeptide deformylase
Syntrophomonas
MSVYQVITVPNDILRGKALPVKEINAGVLRVLDNMRDTMYAADGVGLAAPQIGIPKRMIVVDIGENLLELINPEILKQEGNQLGSEGCLSVPGIVGRVNRAKKVLVKGLDRNGQELNFAAVDLLAKVLQHEIDHLEGILFIDKAIETRIEKL
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Q0AXL3
Q6TH22
DDI2_DANRE
Protein DDI1 homolog 2
Danio
MLLTVFCAPRDRSETTFALDVSPELELRDFLALCELESGIPAGEIQIIYAEQPLQDPTRALGNYGLKDGDVLVLRQAERLRAPPQPTVPGLPRIDFSSIAVPGTSSGQNRNRPQQAQRPSTTQPPPPQATTSPGSGVSPQGLDNPALLRDMLLANPHELSLLKERNPPLAEALLSGDLERFTKVLMEQQQDRARRDQERIKLLTADPFDLDAQAKIEEEIRQHNIEENMTIAMEEAPESFGQVVMLYINCKVNGHPVKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGIAKGVGTQKIIGRVHLAQVQIEGDFLPCSFSILEDQPMDMLLGLDMLKRHQCSIDLKKNVLLIGTTGTETRFLPEAELPECARLAYGPEGREEPRPDEIADRELAEAIQRSVQDSGKMHDM
Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane. Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1. Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2. Required for cellular survival following replication stress.
Q6TH22
P00553
KKA4_NIACI
Neomycin-kanamycin phosphotransferase type IV
Niallia
MNESTRNWPEELLELLGQTELTVNKIGYSGDHVYHVKEYRGTPAFLKIAPSVWWRTLRPEIEALAWLDGKLPVPKILYTAEHGGMDYLLMEALGGKDGSHETIQAKRKLFVKLYAEGLRSVHGLDIRECPLSNGLEKKLRDAKRIVDESLVDPADIKEEYDCTPEELYGLLLESKPVTEDLVFAHGDYCAPNLIIDGEKLSGFIDLGRAGVADRYQDISLAIRSLRHDYGDDRYKALFLELYGLDGLDEDKVRYYIRLDEFF
Resistance to butirosin and structurally-related aminoglycosides, including kanamycin and amikacin.
P00553