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
|
|---|---|---|---|---|---|---|
B8FW28
|
RL25_DESHD
|
General stress protein CTC
|
Desulfitobacterium
|
MSETAIQAVERKEKPKEVRSKGFVPGVIYGKGMDSISVKFDEKRLNKALQGRSQKAKISVQVAGETKQCFVGEIQKDITSGKTIHISMQVVEDDQVVKMKVPITFGGSEALSERKLIVLPYFSELELTGPSADIPEYVAVDVADKSLGDKITVADFMVSPSVSVLDDPEKIIAAITGAR
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
B8FW28
|
Q4A5I9
|
RS11_MYCS5
|
30S ribosomal protein S11
|
Mycoplasmopsis
|
MARKAKKKNISSGVAHIHSSNQNTIITFTDEKGNVIAWSSSGKVGFKGTKKKTSFAASEAAKDAAQMAKEHGISQVRVEMKGLGSGKDSARKQIEVWGIKVTEIKDVTPIPHNGTRPPKRVLKRLRLKK
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
Q4A5I9
|
B1I1H6
|
RECF_DESAP
|
DNA replication and repair protein RecF
|
Candidatus Desulforudis
|
MRLTRIKAGNFRNFQHLDVQPAAGLNIVRGRNAQGKTNFIEAVFFALRGHSFRSLRDRELVTWGQESAFVEAELEGKDGRTRVRAELNPAGKKIVWAGEPVGKAELAVRLGTVLFTPDDLSLIKGGPRERRRFLDLELGIFVPGYLTALQLYRRALEQRNHLLRMGGGRRYSELLDLWTDEVCKYGMMLLSGRLEILKEFAPLACRLFGAWAGEELAVRYRSSVGLSNGVRTPGAGDLRETLAAVRQDEIRAGQTQAGPHLDDLAFMVNGKEGRPFASQGQQRSVVLALKLAQVFLWKRHTGEAPVVLLDDLLFEFDRERRDKVLETLQNDVQVFITTGERVLSGSRVFCVHSGNIQEES
|
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
B1I1H6
|
Q5SQY2
|
BOD1_MOUSE
|
Protein FAM44B
|
Mus
|
MADGAGAGAAGQASGPSGGSSGAGGPVNPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPAMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKEAVPAPPPEPESQDPPAPSQDAS
|
Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles.
|
Q5SQY2
|
Q5P7T7
|
RL13_AROAE
|
50S ribosomal protein L13
|
Aromatoleum
|
MKTFSAKPHEVKRDWFVVDASDKVLGRLAAEVARRLRGKHKAIYTPHVDTGDFIVVVNVEKLRVTGNKALDKKYYRHTGYPGGIYETNFTKLQQRFPERVLEKAVKGMLPKGPLGYAMLKKLKCYAGGEHPHSAQQPQVLEI
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
Q5P7T7
|
A0KAV9
|
LIPB_BURCH
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Burkholderia cepacia complex
|
MSVSPVSIVSTPVAVSASPAGAPDQPVQPVTVRWRGREAYEASFDAMRAFTDTRTADTGDEIWVVEHPPVYTLGQAGDPAHLLVADSGVPLVKVDRGGQITYHGPGQIVVYLLLDLRRRKLMVRTLVTKIEEAVIETLAAYNLASVRKAGAPGIYVASGVHEGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAGLETVDMASLEVAADWNDVAHTLVGRLIANLDGASAAADKPHALEQSND
|
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
|
A0KAV9
|
A7ZCA7
|
YBEY_CAMC1
|
Endoribonuclease YbeY
|
Campylobacter
|
MILCEESYPEILDQICSYLTPGEVELLFINKDEMRELNRSERGIDKTTDVLSFPLELVIHAPLGSIVINKDMVKEKAAELNHSEDAETALLFTHGLLHILGYDHEKDDGQMREKECEVIAKFNLPKSLIVRSEDVRLIDLINKKG
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A7ZCA7
|
A1JJS9
|
CYSD_YERE8
|
Sulfate adenylate transferase
|
Yersinia
|
MDEKRLTHLRQLEAESIHIIREVAAEFGNPVMLYSIGKDSSVMLHLARKAFFPGNLPFPLLHVDTGWKFREMYEFRDHTAKAFGCELLVHRNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELWHNYNGQINKGESIRVFPLSNWTELDIWQYIFLEKIDIVPLYLAKPRPVVERDGMLLMVDDDRIDLQPGEVITQKMVRFRTLGCWPLTGAVESEAQTLPAIIEEMLISTTSERQGRMIDRDQSGSMELKKRQGYF
|
With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
|
A1JJS9
|
Q54YY1
|
SCAI_DICDI
|
Protein SCAI homolog
|
Dictyostelium
|
MEITTKSSTTTDDLNNNNNKTVTPIKSENSATGHTSPPNNSTTTTTSSTSAQPITVLPTEIIKTFEHLLRKSQRLFIGLRDLPQFGRQWQPFFQKTFELYTKLWKFQQQYRSILEDKSKYGLKRCEIGEIASKIGQLYYHYYLRTSDTNYLNESYIFYEAIRLRSYFKDVSLDKTPDMMVKQLRYYARFIVVCLLLNKKKVVFDLIEELLKHVNDYTKIYKPSDAQEWSLVLQEIFSFLQADQCATFSDTNQSPSLTNSGNIINNNSNSNNNNGEHTNNTVQSHRLNHLNCPSPPFPLESTQILQQAILVGSQQNQIKFSEITLDMFRMTQSLEYEPMSEAKENDMKLKQQLTALQQQQQQQAAEAKEKNNGTDQQNTTIPSQPLQQHLHHQQQQQQNGNGSGIKKRNPHKYLLYRPTISQILLFLSYSFKELGDNKAMLLYICADGFTNEDNHVNQHIQPPPSIQQETVPSLIDDSNTNIPITTTATATNPLYNKLFTKGLTLNMQKPSQAINSPTVNNNNNNTTTNVTVPTTTTTATNVTAQTTTTTTTTNSTSTSTTSNIPIYKYNEAPFNTKVESLYPMDLLPFCRKPFFLIVNSQSSDIFNELPTFNQPFVSLLSPQSIPKKLVSNLKCGNLFTFFLHDPISAFCDISCGNKIPSKTFNNISLLAQNSLEIISKLLFECVDLHPSFSFFLLDDFLRSFIIRFIFCHATFYLHKEFQDNIYQVKSNPPLPKSLLYNQSILKSIHQLVSELDVSDQFLGLNENRLVIHEN
|
May function as a transcriptional cofactor with a repressor activity.
|
Q54YY1
|
I3V6B1
|
C80BX_PAPSO
|
Cytochrome P450 80BX
|
Papaver
|
MEIVTVALIAIVFTTFLYLIVRESSPNGLPPGPKPWPIVGNLLQLGEKPHSQFAQLAETYGDLFTLKLGTQTVVVASTPLAASEVLKAHDRTLCGRYVFQSFRVKNHVENSIVWNECNETWKKLRKVCRTQLFTQKMIENQAEVREIKTMEMVKYLKKNEGIEVKIVEVIFGTLVNMFGNLIFSQDIFKLGDESSGSLEMKQHIWRMLELGNSANPGDYVPLLGSLDLFGQRKDVADCLQGVYGVWGAMLKERRIAKRQINGDTKNDFVDVLLDSGLDDQQINSLLLDMFSAGTETTASTIEWALTELTKNPQVTADIRSELLSVVGKRAVKESDILNLPYLQAFVKETLRLHPPTPLLIPRRALETCQVLNYTIPKECQIMVNAWGIGRDPKTWTDPLKFSPDRFLNSSIDFKGNDFELIPFGAGRRICPGVPPGNSVY
|
Involved in the biosynthesis of benzylisoquinoline alkaloids. Probably involved in papaverine biosynthesis since its transcripts are abundant only in cultivars with substantial papaverine accumulation. May catalyze the 3'-hydroxylation of (S)-coclaurine.
|
I3V6B1
|
Q72JP3
|
RUVC_THET2
|
Holliday junction resolvase RuvC
|
Thermus
|
MVVAGIDPGITHLGLGVVAVEGKGALKARLLHGEVVKTSPQEPAKERVGRIHARVLEVLHRFRPEAVAVEEQFFYRQNELAYKVGWALGAVLVAAFEAGVPVYAYGPMQVKQALAGHGHAAKEEVALMVRGILGLKEAPRPSHLADALAIALTHAFYARMGTAKPL
|
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.
|
Q72JP3
|
B9M9X6
|
CAS2_ACIET
|
CRISPR-associated endoribonuclease Cas2
|
Diaphorobacter
|
MRMLVFFDLPVVSKADRRAYTVFRRFLLNDGYDMIQFSVYGRILNGTDAAQKHMQRLLANLPSEGSVRVLTVTEKQFASMKLLVGLPLFQEKKVNAAQIALF
|
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
|
B9M9X6
|
A5GR53
|
MTND_SYNR3
|
Acireductone dioxygenase (Ni(2+)-requiring)
|
unclassified Synechococcus
|
MSQLTIYNAVSEGNDPPLPSLHTTDAAIVAAELSQRGIRFQQWPTHDELDAASSQEEILAAYSAEIAEVQAAGGYQTVDAISLGPDHPQRAELRQKFLSEHTHSEDEVRFFVDGRGLFCLHIGDEVLQVLCERNDWLSVPAGTRHWFDMGERPCFSAIRFFNNQDGWVAQFTGDPIAKRYPLLGS
|
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.
|
A5GR53
|
B6J6A2
|
NUOH_COXB1
|
NDH-1 subunit H
|
Coxiella
|
MTDQLITLIWIIIKIVLILVPLLVAVAFITLAERKVIGYMQSRVGPNRVGFRGLAQPIADIFKLLLKEVIIPTASSRYLYLIAPILSLVPALAAWAVIPFAQGWVLANVNAGLLFLFAMTSLGVYGILVAGWASNSKYAFFGALRSAAQVVSYEIPMGFALVGVLLAAGTMNLQGIVLRQSGGLWHWFWLPLLPLFVTYWITAVAETNRAPFDVAEGESEIVAGFHVEYAGVTFALFFLAEYANMVLVSAIATVIFLGGWLSPFQGIPGLESLFAWVPGIVWFVLKLSLFIFTYFWMRATFPRYRYDQIMRLCWKVLIPVTLVWIIILALAIEFHWTHWL
|
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. This subunit may bind ubiquinone.
|
B6J6A2
|
C0Z4Q5
|
SPED_BREBN
|
S-adenosylmethionine decarboxylase alpha chain
|
Brevibacillus
|
MEQKTEHNVTLHGFNNLTKSLSFNMYDICYTKTKEEREAYIEYIDEQYNAERLTSILKNVSDIIGAHVLNVAKQDYVPQGASVTFLVSEGPVVEVPTESYEESPGPLPENVVLQLDKSHITVHTYPEYHPTEGISTFRADIDVSTCGEISPLKALNYLIRSFDTDLMTIDYKVRGFTRDIHGYKLFIDHDISSIQNYIPEEIKELFHMIDVNVYQDNIFHTKCKRREFDLNNYLFGYTKDRLTPEEQEDITKQLQIEMDEIYYGKNFVN
|
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
|
C0Z4Q5
|
A6UVI4
|
RIFK_META3
|
Flavokinase
|
Methanococcus
|
MLNKLFGRVVSGKGEGKHYMSLPPYKEKFKNILGFEPYEGTLNVKLGYIINLNELNPIEVDDFYYKNNKYYGVKLIPVRICIKDYCVNGAIVYPKKTEHPNNVIELIAPIKLRKYLSLKNNYMVKIRL
|
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
|
A6UVI4
|
B3EFX7
|
GCST_CHLL2
|
Glycine cleavage system T protein
|
Chlorobium
|
MKKTALYSWHEQAGAKIIDFGGYLMPVQYSGIIAEHKAVREAAGLFDVSHMGNFYVRGVRAGEFLQYLTTNDLSKVSDGEAQYNLMLYTDGGVVDDLIIYRIDAETYFLIVNASNAQKDYAWIQKHIGAFEGVSLEDRTDELSLVALQGPMSGAILRKVFPDEDCNTLASFRFRKVYYNGTELLIARTGYTGEQGVEICLPNEAALELWSVLMKAGEEYGIQPIGLGARDTLRLEMGYSLYGHEIDSTVNPLEARLKWVVKMEKGPFIGKEACRQVELNPRYAVAGFSLDGRALPRQHFRLYNSDRQEIGTVCSGTLSPTLQEPIGTCSILREYSRPGTHVMVEIRGTMHQGVIRALPFVQR
|
The glycine cleavage system catalyzes the degradation of glycine.
|
B3EFX7
|
Q038S1
|
SYD_LACP3
|
Aspartyl-tRNA synthetase
|
Lacticaseibacillus
|
MSKRTCYAGDVTAEYVDQEVTLKGWVQKRRSLGSLIFIDLRDREGIVQLVFSEEFDKDALAVANSVRSEYVIEVQGVVKKRKPQAVNKDMKTGDVEVEVHTITILNKAKTPPFYIEDGVAVTEETKLKYRYLDLRRPEMQKNIFTRAHIMRSVHHFLDDNGFIDVETPTLTASTPEGARDYLVPSRVYPGSFYALPQSPQLFKQLLMGAGFDRYYQIARCFRDEDLRGDRQPEFTQIDLETSFLTAEEIQDITEGLIAKVMHDVKGIDVKLPFDRITWQDAMDKYGSDKPDLRFDMQIQDVSELVKDSDFKVFAGAVQNGGQVRAIVLPGGADKYSRKMIDAQQDYIKRFGAKGLAWLKVTSDGISGPIAKFFGDGADLVKAVGANAGDLVLFVADKAKVVADALGYLRTHFGHDLGLIDEQAFRFCWVVDWPLFEYDEGIQRWVPAHHPFTMPNEEDVHLLDTDPHAAHAQSYDIVLNGYELGGGSIRIHNREIQEKMLKALGFTPERAQKSFGFLLNALDYGFPPHGGLAIGLDRFVMLLTGRDNIRDVIAFPKNSKASEPMTSAPYPVADAQLKDLGIEVRADVDPEKEHEGDENLTE
|
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
|
Q038S1
|
Q7NCS3
|
ATPA_GLOVI
|
F-ATPase subunit alpha
|
Gloeobacter
|
MFTIRPDEISSVIRDQIQKYNTELQVTNVGTVLQVGDGIARVYGLEKCMASELLEFEDGTIGIALNLEEDNVGAVLMGAGRTIEEGSTVRATGRIASIPVGPAFLGRVVNALAIPIDGKGDIVGSETRLLESPAPGIIKRKSVYEPLATGITAIDAMIPIGRGQRELIIGDRQTGKTTIAIDTILNQKGKGVVCVYVAIGQKASTVAQIVEVLRSRGALEYTIIVAANANEPAALQYLAPYTGCTLGEYVMYNGLTLPGSDKKINAALLVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSPDLGEGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLDSGLFNSGLRPAIDAGISVSRVGGAAQTKAMKKVAGKLRLDLAQFSELEAFSQFASDLDKATQAQLARGLRLREILKQPQYSPLSVAQQVAIIYAATNGYLDDIDVKGIQPFKQQFLNYLDSSVSEYGQEIETTKALTDKAVDLLKKALNDFKTTVKK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q7NCS3
|
A7GX33
|
MURC_CAMC5
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Campylobacter
|
MKKVHFIGIGGIGISAIARFLFEKGHKISGSDIKESKTTQELKEQGMDVITPHCKEAIKDQDFVVYSAAIKDDNVELVEARKKGIKCFSRKEILPYVLEDKRVFAVAGAHGKSTTSAMLSSLIEGSVIIGAISKQFGSNMRYAQSDNVVFEADESDSSFLNSNPYLAVVTNAEPEHMEHYDYDLAKFYAAYKGFLERAKVRVINAEDEFLSTLKLDAIRLFPSSDITELAMVVRDYQPYTSFNLKNLGKFEVFGMGQHIAIDASLAILAALHETPLKDIRENLLNFKGIKKRFDILSADKNFILIDDYAHHPTEIRATLNSVFEYAKLLGVSNVTAIFQPHRYTRLSTNLEGFKECFKGVDELVILPVYAAGEKPIEVDMKGAFSEYSPIFTDKVERVGEAIEFTDEFGVKNRLSDGIVVGFGAGDISVQLRGGY
|
Cell wall formation.
|
A7GX33
|
P15090
|
FABP4_HUMAN
|
Fatty acid-binding protein 4
|
Homo
|
MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA
|
Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.
|
P15090
|
Q12NL5
|
LOLD_SHEDO
|
Lipoprotein-releasing system ATP-binding protein LolD
|
Shewanella
|
MKPASTRLLAINAVSKVFHDGACETQVLHEVNLTVHRGEQLAIVGSSGSGKSTLLHIMGTLESPTSGTVLLEGENLHQLSSKRQAQIRNQDLGFIYQFHHLLPEFSALENVAMPAFIQGKNKAQTLAEAKALLERVGLGHRLTHLPSQLSGGERQRVAIARALINKPKLVLADEPTGNLDAVSGEAVYGLIRELAEQLGTAFVVVTHDANLAARMDRQVNMKDGILSQSETHR
|
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
|
Q12NL5
|
A4K2S2
|
KCNS1_LEMCA
|
Delayed-rectifier K(+) channel alpha subunit 1
|
Lemur
|
MLMLLVRGTHFENNWSKLIPPAPLDATVSEPPVPDSGEPDSGVPWRRSDEALRVNVGGVRRRLSARALARFPGTRLGRLQAAKSEEQARRLCDDYDAAAREFYFDRHPGFFLSLLHFYRTGRLHVLDELCVFAFGQEADYWGLGENALAACCRARYLERRVARPRAWDEDSDTPSSVDPNPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVATVAAGRSAEDVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLASVALGGNNHGGTSGEELGHLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEKEEDVGFDTIPACWWWGTVSMTTVGYGDVVPVTLAGKLAASGCILGGILVVALPITIIFNKFSHFYQRQKALEAAVRNSGHREFEDLLSSVDGVSDASLETSRETSQEGRSADLEAPSESPKPQIY
|
Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
|
A4K2S2
|
B2VFY8
|
ENO_ERWT9
|
2-phosphoglycerate dehydratase
|
Erwinia
|
MSKIVKVIGREIIDSRGNPTVEAEVHLEGGFVGLAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVGAVNGPIAEAVTGKDAKDQANIDKIMIDLDGTENKSKFGANAILAVSLAAAKAAAAAKGMPLYEHIAELNGTPGKFSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAKTLKEAVRIGSEVFHNLAKVLKSKGMSTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEDLTKQYPIVSIEDGLDESDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIDKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGNRAPFNGLKEVKGQ
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
B2VFY8
|
Q72IG5
|
TRUD_THET2
|
tRNA-uridine isomerase D
|
Thermus
|
MDLVFRPERYPFLTQDLPGVGGEIRVEPEDFQVEEVPAYLPKGEGEHLYFLLEKEGRTTREVLEFLRDEVGVPEKEIGVAGLKDKRAKTRQWFSIPRKYEDALCLLENLQGVRLLAADLHTNKLRTGHLKGNRFHILIRRPKGGVAEAEAVLKRLAEKGVPNYYGPQRFGLGGLNPVRGYKLVKEGKGRGSPWLKRFLIGSLQSLLFNDWVALRMALGLYDRVVLGDWAKKHATGGEFLVEDPGEAERALRLEISATGPLFGKKYPEAQGEARAIEDEVLARYGLKREEFRARRGARRPIRVPLAEWKVEEAPEGLWLSFFLPKGSYATSLLREVMKVEALDHLEAEPAPEDAEGL
|
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
|
Q72IG5
|
Q3IFH4
|
MDH_PSET1
|
Malate dehydrogenase
|
Pseudoalteromonas
|
MKVAVLGAAGGIGQALSLLLKTGLPAGSELSLYDVAPVVPGVAVDLSHIPTAVKVAGFGADALNEALKDADIVLIPAGMPRKPGMDRADLFNVNAGIIKTLAEGIVASCPKALVGIITNPVNGTVPIVAEVFKKAGTYDAKRVFGITTLDVIRSEAFVAELKGVDVATVKVPVIGGHSGTTILPLLSQVEGVSFTDEEVAALTPRIQNAGTEVVNAKAGGGSATLSMGAAAARFCMSLVKGLQGEDVVDYAYVAVENGDAEYFAHPVRLGKNGVEEILSYGELSAFETKAKNDMLETLKKDIKEGVDFMA
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
Q3IFH4
|
P41653
|
YCF2_PINTH
|
Protein Ycf2
|
Pinus subgen. Pinus
|
MKKRRRPWIIKLEEIQSYQFLCNPWTKSNLIRLLIQILSRRERLIKLFDPRILSTLLLRDLRKSNPYFLVKGIVVLTLSILIYRFNHQSSMIDRKNFYSIKLFPIHNFMELGNETPEEYLKPFTQNWLRFPHLLLSFQLKRYYNRDFDPISLNSGYGKNTNKKDEIISKNQGPSETHSENDEKDINLKIDSTLNSTENEYWKPEKYLCEDPFTRNKTEIEQRRKRSILWDLSFIEREQTKIESDLSSKCLSKDYPISWAKELFTEDQRYTEENSFPLERKRFIENFTKSIRYSFFYILPIDEPCMGGPSATKKPIEDFNLSKRLFKIKKNVFSQDLRDSKSYSLMNRIVDLWKIKTYFEIENPSLNCAMRSFTLPWNLFSAFCDQSKGKYILHKNCLEMTDQFTLSITKPSQVHDKISFFIYYNKNGSLRSDRIFNHREKWKNQSLWVLLNIIDKADDYLDQIIDKQLSQIDSKNCLEIGTPFNNYRTEALGWYESIKYNIDNRYSKNLLNRFYFINRLSRNLKDQIRTNFIENENLNNVTKDTIDRHSSSWKKIKREWFNHSIIRIDKHINRNLNVYKWSNQTEYFMKYLKQVFSKKNYFKIVFDPIELCTNTNRDSIGWSVFLSLSESTVKILNSKFDIISNLNSKFDILISFFDFAFHGLQSMNYRLLNQLLDPIGTLIVRLKKFKTFLLYDHNLSQRSKLLIDEGTIAPFVTNKIPINPLIIDFFDNENNRMESFDNTYFSTISNDRDNWLNPVKLSDQSSLIASFHGANTLQFFDYLHHTRPNYRNRLPSDMKRFYIKRNNFTYGQLFNLLIIHNNLSSLPIGEIGPVHSEKETISFIKSQVSNILLPKYLKRKRSGDQTFVLIYDLYRSFNLLTRLNPFVREKRYLSSIEEISTTPLTKEQIVNFEKNFCQPFFKRSDSEENNFDQCFKRGFSSNVGLIQTRSYQDDLLSEMFSNKNEEIFPRIQDWFVTECLKNKIVNEDIDGRSTLSNSSKEEQNIYRISQIDSIFSKWDLFKTYMPWFFTSAWCKYIENMLLDTLSEILLHGSNPFVSILQNIKHNILLKRNILWELSHPLWEPIQCKLRTNLINKFFFPSNNFKDFFPYCKDFLIEETSDREKSSVPFIWAHMRLLNARGYKYGILIPFFVLGYSILQYFKVISFTFINIKRYFELIKYLKHPSYVIELQKMINPPVPNSFLYYTIDRDRSSSLPQIINSFFSMNMKRKRKTKRKTKNRNIKLLITIIRELNGLCSSMDISEKEMNLLVQFLMTEKALFKFESIFTYSPNLFKNEFGDQIIRQPGLIHLRYLAYTYQKGLINYGFNPFCLAERWVFLAFCQKITSSQILCQTNPTFHGKPFSLHSGSLLSKGILLIGPMGTGRSYLVKSLAADSYVPLIRISLKKLWYGEYLDYPLERIPTEFDPFVKDKMEDFHITLELAKRMSPCIIWIPNIHELNLNDATNYLFGFGFTDLFLSVLMNNLFRFRDGEKDSMRNILVIASTHIPQRVDPALIAPNRLDRSINIRMLVIPQRQREFPILLCSKGLYSVKFPDEFGSITIDYAVRDLAALADEALILSITRNKSVIDTNTIRSAIYRQIFHLQSMDNQVGSSQNDERIIYKVGKAFIQNTLRRNSPMNPLSTKKELWKKRFCYLSEWYLEPSIAETTMKELTILPHILGCLAGSAARDSWSISERNRENWIPFDKLAEHDLDIASSLLESILVEFPFSRLGICRGKSDKDQITFAPQLKMRDNLDLIRFMKEYELKFTPGAKQRDMDEELIKNVVWTPRIWRLSFLRSNRFDHIKTPNSLGSSYQFGSLRKRQMDRSLFPIQYPKQYKYSKKPLFFIGRRFLWDSFLFQEQRPVFSRREFFANEELLKRLYITYGARRLIAQPDFFPKKSIQSFFRRYDSKSTINSVLVMNWWKPLSLRHRHIEHFKRIQAIGIQLERMQPYFPIYSYNRWLTENSRERVDRFQSLIHRQRWLGTNRLLSNESFLYNTLFESYQYLSNLFLSNRMLLDQITKTLLENKWLFPNEIEHSIHTTGLRFDISWENME
|
Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis.
|
P41653
|
O58686
|
MRE11_PYRHO
|
DNA double-strand break repair protein Mre11
|
Pyrococcus
|
MKFAHLADVHLGYEQFNKPQRAEEFANTFKKALEMCVKESVDFIIIAGDLFNSSRPSPGTIKTAIKLLQIPKENNIPVFAIEGNHDRTQRGPSVLHLLEDLGLLYVIGLRQERVENEYLTSERVGNYWLVKGVYDNLEIHGMKYMSSAWFEANLNFFKGIFRPDEDAILVLHQGIRDITEKVFPSYSAELKLSDLPRGYLYYALGHVHKRFETNYGDSPVVYPGSLERWDFGDYAKRLVWNGVTFREEVGSDKGFYIVEDFTPRFVNIKVRDFIDVVIKGDSEREIKKAVKASLPHIPRNSYVRFNIKWRKPFDVEWIKEIVNAEYLRIHTAIIKDEKSMNGESVDIKSFFTEQEWKVIDLASSDEFESYIEKIVDILSGYEKKEEREKKESKIRKFERPKNPGDLTAWLRGG
|
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
|
O58686
|
P44626
|
LNT_HAEIN
|
Apolipoprotein N-acyltransferase
|
Haemophilus
|
MKNLNRILLSIKFMNKYFTYLIAIISGLLGVFAFSPFDYWPLAYVSLLGLLYVAKNPKKSTALLSTFLWAMGFFCFGVSWLNVSIHQFGGASLGVSYFLVGLLAAYLALYPMLFTYLVHHFKVQSAVIFAVIWTLTEFLRGWIFTGFPWLQFGYTQIDSPFYGIAPIFGVTGLTFFTVWASAVIFNLVSSLFKTKNLKLVLANALLLIIVGGLSAYSSRIHFVKSVEDKAISVTLAQGNIEQNLKWDPNYFYSTLAIYQKLITENLGKTDLIILPESALPTLENAITPFFEGLERAAKETKTEIMVGTVFQDTKSGKLLNSIMTAGNPDFPYQPNTQNRYNKHHLVPFGEYVPLESILRPLNSVFNLPMSAFQSGEAVQPSLIAKKRAFSPAICYEIIFGEQVRQNLKQDTDYLLTLSNDAWFGDSIGPWQHLQMARMRALELGKPLIRATNTGISVFVDAQGKVLAQAPQFIETTLTYKIAPAEGKTPYSVLGNMPLYALSLLFLLLHSMMAFIRRKMNIL
|
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
|
P44626
|
A6UZL2
|
RS4_PSEA7
|
30S ribosomal protein S4
|
Pseudomonas
|
MARYIGPKCKLSRREGTDLFLKSGARALDSKCKAENVPGQHGQRRGRLSDYGLQLREKQKVRRIYGVLERQFRGYYQEASRRKGSTGENLLQLLECRLDNVVYRMGFGSTRAESRQLVSHKAITVNGQTVNIPSYQVKAGDVVAIREKSRNQLRIAQALELCGQRGRVEWVEVDLDKKTGTFKSVPARSDLSADINENLIVELYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
A6UZL2
|
Q2I3H1
|
COX2_ELEMA
|
Cytochrome c oxidase polypeptide II
|
Elephas
|
MAYPLQLGFQDATSPVMEELLHFHDHTLMIIFLISSLVLYIIMLMLTTKLIHTNMMNVQEMEMIWTILPAIILILIALPSLHTLYMMDEINNPLLTIKTMGHQWFWSYEYTDYEDLAFDSYMITTDSLKFGELRLLEVDNRMVLPTDLPVRVLVSSEDVLHSWAVPSLGLKTDAIPGRLNQVTLTSMRPGLFYGQCSEICGANHSFMPIVLELVPLKYFESWSASLA
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
Q2I3H1
|
Q6G9M8
|
KHSE_STAAS
|
Homoserine kinase
|
Staphylococcus
|
MSNVLELTIPASTANLGVGFDSIGMALDKFLHLSVKETSGTKWEYIFHDDASKQLPTDETNFIYHVAQQVASKYSVDLPNLCIEMRSDIPLARGLGSSASALVGAIYIANYFGDIQLSKHEVLQLATEIEGHPDNVAPTIYGGLIAGYYNDVSKETSVAHIDIPDVDVIVTIPTYELKTEASRRALPQKLTHSEAVKSSAISNTMICALAQHNYELAGKLMQQDGFHEPYRQHLIAEFDEVKTIAIQHNAYATVISGAGPTILIFSRKENSGELVRSLNSQVVSCHSELVDINISGVKERIVYQ
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
Q6G9M8
|
A9WT66
|
WHIA_RENSM
|
Probable cell division protein WhiA
|
Renibacterium
|
MALTAAVKEELSRLEVRKSSVRKAEVSAMLRFAGGLHIISGRIVIEAEVDLAATARRVRVAIAELYGHQSEIIVVSGGGLRRGNRYVVRVVREGEALARQTGLLDSRGRPVRGLPSVVVNGSTADAEAVWRGAFLAHGSLTEPGRSSSMEVTCPGPEAALALVGSARRLGIAAKAREVRGVDRVVIRDGDTIAALLTRMGAHETLLVWEERRMRKEVRATANRLANFDDANLRRSAQAAVAAGARVDRALEILGDDVPEHLKYAGELRVAHKQASLDELGRLADPPMTKDAIAGRIRRLLAMADKRASDLGIPSTEANVTLEMLEE
|
Involved in cell division and chromosome segregation.
|
A9WT66
|
Q7YD16
|
CYB_LONCH
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Lonchophylla
|
MTNIRKTHPLLKILNSSFVDLPTPSSLSSWWNFGSLLGVCLAVQILTGLFLAMHYTADTATAFDSVTHICRDVNYGWVLRYMHANGASMFFICLYLHVGRGLYYGSYTYTETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTELVQWIWGGFSVDKATLTRFFAFHFLLPFIVTALVMVHLLFLHETGSNNPTGIPSDPDMIPFHPYYTIKDILGFLIMLTALSTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILVLAIVPVLHTSKQRSMMFRPLSQCLFWLLVATLLTLTWIGGQPVEYPYVIIGQTASVLYFMILLVLMPLTSIVENKLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q7YD16
|
A2RNN4
|
RL15_LACLM
|
50S ribosomal protein L15
|
Lactococcus cremoris subsp. cremoris
|
MELHSLKAAEGSRKVRNRVGRGTSSGNGKTSGRGQKGQKSRSGGGVRPGFEGGQTELFRRMPKRGFLNVNRKEYAIVNLETLNRLEDGATVSAETLVAAKIVKDVKSGVKVLANGELTAKNLTVKVAKVSAAAKAAIEAAGGSVEEA
|
Binds to the 23S rRNA.
|
A2RNN4
|
C6CNE4
|
PAGP_DICC1
|
Lipid A acylation protein
|
Dickeya
|
MRLTLTSRSRLFVLSSLLFISTFDVLSAQAAPANTAPSFWQRAGDNLSDTWHHWQSQDLYVPVMTWHNRWTYDKEKTDRYNERPWGAGYGVSRLDCDGDWHSLYMMAFKDSFNKWEPIGGYGYEKRWRPLEDQDFQLGLGFTAGVTLRDNWNYIPLPVLLPMASLSYQRLSFQATYIPGTYNNGNVFFAWLRWQF
|
Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
|
C6CNE4
|
C4LJL7
|
ATPD_CORK4
|
F-type ATPase subunit delta
|
Corynebacterium
|
MHAASRESMTELATTLDNTVAQSNAAVDGAQIGPELFDVVEVLDSNRDLRVALIDPAASSEKRADLADRVFGEKLNQASRSVLRSAVDKDWSNTRDFRNGLVQLGRRALFRAAEADDKLTTVESELFQLARVLEDAPQLEMLLADRQASADRRRQLLASVLYGKVTSITETLALQAISRAKQRPVEACETLSREAAQLRGYEVAHVVTAGELSDTQRSTLADKLGRIYGHKMSIHGEVDPSILGGMVIRVGDERIDGSTSGKLEKLRRAFA
|
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.
|
C4LJL7
|
Q65HI8
|
FOLD_BACLD
|
Methenyltetrahydrofolate cyclohydrolase
|
Bacillus
|
MTATIIDGKETAKEKRGQLAKEVEELKKQGVTPGLAVILIGDDPASLSYVRGKKKAAEAMGIRFQLDHFDASFTEQELLEVIDQYNQNDDFHGILVQLPLPDHISEQAVIERISPEKDVDGFHPLNVGKMLLGEDTFLPCTPAGIVELLKKTEIDLSGKEVVVVGRSNIVGKPVGQLLLNENATVTYCHSRTADITAHTKKADILIVAVGKANFIKADQIKEGAVVIDVGVNRLDNGKLAGDVDFEEAKEKASYITPVPGGVGPMTITMLAHNTVKSAKRTIQL
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q65HI8
|
Q4JSW2
|
MSHA_CORJK
|
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
|
Corynebacterium
|
MRVAMISMHTSPLEQPGTGDAGGMNVYVKNIAEQLERRGVIVDVFTRATRPLQGEVVNVRPGLRVINCVAGPYEGLSKEELPTQLAAFTGSILAFCREEGVSYDLIHSHYWLSGQVGWLLRDLWQVPWVHTAHTLAAVKNNSLADGDSREPESRRICEQQIVDNADLLIVNTDQEVQDLIEGYDATTCAIRVVPPGADVDRFTPGSDRATERSRRELGIPFRTKVIGFVGRLQRLKGPQVLLRAVAELLDRHPQQQLAVVICGGSSGAGGNELERLQLLAEELGISRCVRFLAPRPPEELVGVYRAADIVAVPSYNESFGLVALEAQACGTPVVATRTGGLPIAVDGGKSGLLVDGHDPSDWADALGKLVLDDDLRIAMGEYAPSHAAKFSWQASAEALHKLYEELPPAGHRGERQPAG
|
Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
|
Q4JSW2
|
Q6FDF6
|
BETT1_ACIAD
|
Osmo-independent choline transporter BetT1
|
Acinetobacter
|
MWSKRDEQKTYPPIRLNPFVFWSSAISISIFGMLFVLFPETSQHGLTWIQQQVNQLFGWYYMLVIILSLGFVAWLAFSQVGNIPLGKAQDKPEFGYLVWTSMLFSAGIGIALLYYGVAEPVDHFLRPPEGQGGTVEAAQNAMMYSFLHWGIHGWVLYALVGVTLGYFAFRRDLPLALRSALYPIFGERIHGLVGHMVDGFGILATIISLVTNLGIGALVMISGISYLFPDLPNTSSTLVVTVIMMMLVATLTTVIGIEKGLAWLSRINLRLLYLLLLFVFLTGPTNHLLNGLVQNTGDYLSHFVQKSFDLYLYDKNATGWLASWTIFYWAWWIAWAPFVGMFIARISKGRTIREVVLGVCLIPLGFTLAWISIFGNTAIDLILNHGQQIIGSLVIQDPALSLFKLLEYLPFHPYVAGIVVVICFVLFLTPVGSGTLMIANLSSQGGSSDSDSPIWLRVFWSIAITIVSIGLLLAGSFSAMQSAVVLCGLPFSVILLLYMFGLAKALKQETQQPVVESHTTETSGSD
|
Sodium-independent high-affinity choline uptake system. Uptake is not proton coupled. May play a role in metabolic adaptation to choline-containing environments.
|
Q6FDF6
|
B6IPH8
|
DAPE_RHOCS
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Rhodospirillum
|
MAPDPIALARDLIRCPSVTPADAGALDRVQSVLEGLGFTCHRLPFQEPGTERVDNLYARLGDKGPNFCFAGHTDVVPAGDAAAWTVDPFGGEIIDGRLYGRGAADMKGGVAAFIAAVGSFLERNGPPAGSISLLITGDEEGPAVNGTRKVLDWMAAAGERIDACLVGEPTNPRALGDMIKVGRRGSLTATLTALGAQGHTAYPHLADNPLPRLAEALHLLASSPLDMGTPHFQPSTLALTSIDVGNPASNVIPARGTARFNIRFNDLHTPESLEAHIRDVLEEVGGAWELALQTSGVAFLTPPGALSDIVAAAVEAHTGRTPELSTSGGTSDARFIKDHCPVVEFGLVGASMHKVDENVAVADLLELTAIYRTVLERWFAGAEPRT
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
B6IPH8
|
Q5HB44
|
RSMH_EHRRW
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Ehrlichia
|
MYHTPVLLKEMLDILSPQNGGIYVDATFGSGGYSRAILNSADCQVYAIDQDEYTYTFYEKLSNDFPNRIHFFINKFSKIQQILNNVQIKKVDGVVFDIGVSSMQLEDASRGFSFSKNGPLDMRMSTSLSGVDARMFVNTVSEVEMANVIYQYGGEKYSRKIARAIVNARNKNMINTTGELASIIRSVVSRSKNHSIDPATRTFQAIRIWVNKELEELEKGIACAANILNQGGKIIVISFHSLEDRIVKVIFKLLCDGKSVNLLNLGLGFQLINKKIIRPTAEEIHSNPRARSAKLRAILKL
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q5HB44
|
Q6GPK9
|
TAOK2_XENLA
|
Thousand and one amino acid protein 2
|
Xenopus
|
MPSNARAGNLKDPEVAELFFKDDPEKLFADLREIGHGSFGAVYFARDIRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEMEIAAITHGALQGLAYLHNHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITSIELAERKPPLFNMNAMSALYHIAQNESPVLQSNHWSEYFRNFVDSCLQKIPQDRPTSDMLLKHRFLQRERPQTVIMELIQRTKDAVRELDNLQYRKMKKILFQDTQNGPNTETTEEEEEAEQFLHCTGTITSMESSQSVPSMSISASSQSSSVNSLADASDDSGEMAMMQEGEHTVTSNSSVIHRLPAHDNIYDDPYQPEMEAQQSSSAARRRAYCRNRDHFATIRTASLVTRQIQEHEQDSALREQMSGYKRMRRQHQKQLMALENKLKSELDEHQQRLDKELEAHRSNFSAENEKISKKHQAIFEKEAKGGMTEEKKFQQHILGQQKKELTNLLESQKRQYKIRKEQLKEELQENQSTPKREKQEWLLRQKESMQHYQAEEEANLLRRQRQYFELQCRQYKRKMLLARHNLDQDLLREELNKKQTQRDLECAMLLRQHECTQELEFRHLQLLQHTRSELIRMQHQTELGNQLEYNKRREQELRQKHAAEVRQQPKSLKSKELQIKRQFQDTCKIQTRQYKALRNHLLETTPKSEHKSILKRLKDEQTRKLAILAEQYDHSINEMLSTQALRLDETQEAEYQELRIQLQKELELLNAYQSKIKIHTDAQHERELKELEQRVSIRRALLEQRIEEEMLALQTERSERIRSLLERQAREIEAFDSESMRLGFSNMALTGIPAEAFNQGYQAPPPGWPSRPVPRSGSHWSHGVQNTGAPQLWRQPTLLAPPSASWGLHPPGSSSSLSALPSSSSSSSSSPSSSSGGRPGLLLLRNSPQPLRRGGSGGPSEAGLSRSTSVTSQLSNGSHLSYS
|
Activates the JNK MAP kinase pathway.
|
Q6GPK9
|
Q47F82
|
LPXD_DECAR
|
UDP-3-O-acylglucosamine N-acyltransferase
|
Dechloromonas
|
MASLGKVVLTLADIAAQLGGDVLGDSQTPISRVAPLATAGEGDITFLANPKFRSQLSACKASAVILRPDVAEEFPGPRIVTGNPYAYYARVATLLNPYQSGLSGVHASAVVESPVPDSVAIAPNVYIGKDVTLGENVVINAGCVIGDGVSIGAGTVLYANVTVYYGCSIGQQCIIHSGAVIGSDGFGFAPEGQSWIKIPQIGRVVIGNDVEIGANTTIDRGALEDTVIGDGCKLDNLVHIGHNCKIGNNSVLAGCTGVAGSTVFGEHCVVGGAGMISGHLNIAAGTTISGGTTVMKSILNPGVYTSVFPLDTHEEWLRNASHIRRLSKLAERVSELEKKLKEKDIEG
|
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q47F82
|
D7SMN6
|
FULL_VITVI
|
VviFUL2
|
Vitis
|
MGRGRVQLKRIENKISRQVTFSKRRSGLLKKAHEISVLCDAEVALIVFSTKGKLFEYSSDSSMERILERYERYSLSERQLLSTDPDPQGNWSMDYPKLTARIEVLQRNLRHFVGEDLDPLSLRELQNLEQQLDTALKRIRTRKNQLMHESISELQKKEKSLVEQNNALAKKVKEKEKVEQNNRAQWEQQNNIGQNSSAYVVPPPPLQLPSLTIGGSFVGRAVEEDGAEARPSPNTLMPPWMLRHVNE
|
Probable transcription factor involved in flower development.
|
D7SMN6
|
P98023
|
COX2_TRYCR
|
Cytochrome c oxidase polypeptide II
|
Schizotrypanum
|
MSFILSFWMIFLIDSVIVLLSFVCFVCVWICVLLLSTVLFVTKINNIYCTWDFVSSKFVDTYWFVIGVMFIMCLLLRLCLLLYFGCLNFVSFDLCKVVGFQWYWVYFLFGETTIFSNLILESDYLVGDMRLLQCNHVLTLLSLVIYKLWVSAVDVIHSFTLASLGIKVDCIPGRCNEIILFASNNATIYGQCSELCGVLHGFMPIVICFI
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
P98023
|
Q0BYB7
|
RL2_HYPNA
|
50S ribosomal protein L2
|
Hyphomonas
|
MALKTFNPTSPGRRQLVLVDRSALHKGKPVKALTQGLSSKGGRNNQGRITVRHQGGGVKRLYRQVDFKRTRWDIPATVERLEYDPNRTAFIALIKYQDGELSYIIAPQRLEVGDTVITSATADIKPGNTLPLKSIPVGTIIHNIELKPQKGAQMVRSAGTYAQLVGRDSGYAQIKLASGELRMVLDSCLATIGAVSNPDKMNEVSSKAGRNRHLGKRPTVRGVVMNPVDHPHGGGEGKSSGGRHPVSPWGKKTRGPKTRNNKVTDRLIIRRRNAKR
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
Q0BYB7
|
A0A348G5W0
|
TX14A_ODOMO
|
Poneratoxin
|
Odontomachus
|
MKPSSLTLAFLVVFMMAIMYNSVQAEALADADAEAFAEAGVKELFGKAWGLVKKHLPKACGLLGYVKQ
|
This homodimer composed of two cationic amphipathic alpha-helical peptides has antimicrobial activities against E.coli (MIC=3.1 uM), S.aureus (MIC=3.1 uM), and S.cerevisiae (MIC=3.1 uM).It also shows histamine-releasing activity (66.4% at 10 uM) and a weak hemolytic activity (10.5% at 50 uM).
|
A0A348G5W0
|
O93870
|
FCR1_CANAX
|
Fluconazole resistance protein 1
|
Candida
|
MSDDHSIHSHTQGLHHIKKKRVGKACDSCRIKKTKCDGKKPCNRCTLDNKICVFTEKKKTKEKKHPSGYVELLEARLDILTRSLEKLIELSRPHLQFIDDIITEEKSVDQEKSSPASSTPNSSSSDHHDDVEEQNSTGVVAPINKVVSYLIKEQGLLKNIPLEWEQGTEIAANFDPNRNLKSSSRLFAEHKGEAFIGSPVTSPQQMPTSNPFRRTSMFKEELESPSSDHYNESIFSQSVDEPYIKKEPNSAQFSKGTFSPQQQQLQQQQQMLNQFSLNTSRDISDIESDSSNKEDGLNSGSVSPPTSNYRSFSLFSDSNGEPILGKTSSLTSLTNKYENHSLSSPQTAINPVFNNSTTGPILTTLRRNSSSHSQKTLGSIQLQQKPRGSVHKPVRNHSRVSSFDKRMESTATAAATVAAVSGSVQLSQNTTPQNLPHLDNSQNNNYLRDNGMNNIGAGSVGGGLTFGAPSFTQPLSPSDDAIVYPTNQFTNRPATVSTFGGGLDVLVDNSLDPFFNI
|
Transcription factor that acts as a negative regulator of fluconazole resistance in C.albicans. Also confers fluconazole resistance in S.cerevisiae by activation of the PDR5 gene.
|
O93870
|
Q1G3V9
|
EPFL8_ARATH
|
MEPFL8
|
Arabidopsis
|
MDSSRKYKRCGFGAALFVANIFFSLLSLHCISGAHGHQQRMKESVMGSEPPVCATKCRNCKPCLPYLFDIRGAHDDDDDSEPYYPVKWICRCRDRVFEP
|
Controls stomatal patterning.
|
Q1G3V9
|
Q9XP84
|
CYB_SMIGI
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Sminthopsis
|
MINLRKTHPLMKIINHSFIDLPAPSNISAWWNFGSLLGICLVIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNYGWLIRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLAEWIWGGFAVDKATLTRFFAFHFILPFIIMALVIVHLLFLHETGSNNPSGINPDSDKIPFHPYYTIKDALGLMFLLLVLLSLALFSPDSLGDPDNFSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASILILLIIPFLHTANQRSMMFRPVSQTLFWILTANLITLTWIGGQPVEQPFIIIGQLASILYFTLLLVLMPLAGMFENYMLEAQR
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q9XP84
|
Q9SVP6
|
PILR2_ARATH
|
Pinoresinol-lariciresinol reductase 2
|
Arabidopsis
|
MKETNFGEKTRVLVVGGTGSLGRRIVSACLAEGHETYVLQRPEIGVDIEKVQLLLSFKRLGAHLVEGSFSDHQSLVSAVKQVDVVVSAMSGVHFRTHNIPVQLKLVAAIKEAGNVKRFLPSEFGMDPSRMGHAMPPGSETFDQKMEIRNAIKAAGISHTYLVGACFAAYFGGNLSQMGTLFPPKNKVDIYGDGNVKVVFVDEDDMAKYTAKTLNDPRTLNKTVYVRPTDNILTQMELVQIWEKLTEKELEKTYVSGNDFLADIEDKEISHQAGLGHFYHIYYEGCLTDHEVGDDEEATKLYPDVKYKRMDEYLKIFV
|
Reductase involved in lignan biosynthesis . Unlike conventional pinoresinol reductases that can reduce both pinoresinol and lariciresinol, PRR2 shows a strict substrate selectivity for (-)-pinoresinol . No activity with (+)-pinoresinol or lariciresinol . Abstracts the 4R-hydride from the NADPH cofactor during catalysis .
|
Q9SVP6
|
Q6A7P6
|
PNP_CUTAK
|
Polynucleotide phosphorylase
|
Cutibacterium
|
MEGPGLEFTEAIIDNGKLGKHVVRFEAGLLAQQADGSAAVYLDGDTMLLSATTAAKTPRDSIDFFPLTVDVEERMYAAGRIPGSFFRREGRPSEGAILACRLIDRPLRPSFVKGLRNEVQVVVTVMALNPAVYYDVVAINAASMSTQLAGLPFSGPIGGVRMALIDDQWVCFPSVDQRKESTFDMVVAGRVLADGDVAIMMVEAESTPATWGLVRGGRTAPTEEVVATGLEAAKPFIKVLCDAQVALAAKLPKETYDFPVFKDYEDDVYAAVEEKAADELSRIEQIAAKLERQEAESELKARIKAELAETFPEREAEISGAFKAVMKKIVRKRVLDEGVRIDGRGPRDIRSLSAEVGIIPRVHGSALFQRGETQILGVSTLNMLDMEQKLDTLSPENTRRYMHNYNMPPYSTGETGRVGSPKRREIGHGNLAERALIPVLPTREEFPYAIREVSEAIGSNGSTSMGSVCASTLALLNAGVPLRASVAGIAMGLMSETDEDGKTKYLALTDILGAEDALGDMDFKVAGTSEFVTALQLDTKLDGIPADVLAGALKQAKEARTAILEVMNEAIDSPDEMAPTAPRIITVHIPVDKIGEVIGPKGKMINQIQDDTGANISIEDDGTIFIGADNGDSAESARSMINAIANPQMPEVGERYLGTVVKTTSFGAFVSLLPGKDGLLHISKMRDLNDGKRVEAVEDVLSVGQKIQVEIAEVDDRGKLSLVLASDEDDADE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q6A7P6
|
Q8QGQ7
|
BMAL2_CHICK
|
Brain and muscle ARNT-like 2
|
Gallus
|
MAEAGVGSAEGAEEERRAVEENFPVDGNSCIASGVPSLMNPITKPATTSFNNSVVEIPRKRKGSDSDNQDTVEVDGDPQKRNEDEEHLKIKDFREAHSQTEKRRRDKMNNLIEELSAMIPQCNPMARKLDKLTVLRMAVQHLKSLKGSTSSYTEVRYKPSFLKDDELRQLILRAADGFLFVVGCNRGKILFVSESVCKILNYDQTSLIGQSLFDYLHPKDVAKVKEQLSSSDVSPREKLVDGKTGLQVHTDFQAGPARLNSGARRSFFCRIKCSRTTVKEEKECLPNPKKKDHRKYCTIHCTGYMKNWPPSEVGVEEENDVEKNSSNFNCLVAIGRLHPYIVPQKSGEIKVKATEFVTRFAMDGKFVYVDQRATAILGYLPQELLGTSCYEYCHQDDHNHLAEKHKEVLQNKEKVFTNSYKFRAKDGSFITLKSQWFSFMNPWTKELEYIVSNNTVVLGHNESAEEQVSYGSQPAEGAVKQSLVSVPGMSSGTVLGAGSIGTEIANEILELQRLHSSPPGELSPSHLLRKSPSPALTVNCSNVPNKELIQLCPSEAEVLETSEQNQGAIPFPSNEPLLGGNSQLDFAICENDDTAMTALMNYLEADGGLGDPAELSDIQWAL
|
Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL binds to the half-site 5'-GTGA-3'.
|
Q8QGQ7
|
A8M0Z1
|
RL21_SALAI
|
50S ribosomal protein L21
|
Salinispora
|
MYAIVKTGGKQYKVAEGDVIEVEKLAGAPGDAVQLAAVLLVDGDDLVTDAAKLAEVEVSGEIAAHTKGPKIRIHKFKNKTGYHKRQGHRQPLTQVKVTGISSGK
|
This protein binds to 23S rRNA in the presence of protein L20.
|
A8M0Z1
|
P04927
|
SANT_PLAFF
|
S-antigen protein
|
Plasmodium (Laverania)
|
MNRILSVTFYLFFIYLYIYETYGKVKNTDKELSDIYGTKYYLRSGFFNSKKCKGHKYEDLQAEGEGENDKEEDSNNEEMNIDEENGLIEGQGESEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGLEDPAKASQGGAEGHGKHAPNKENKNKNKESIKNIMNMFI
|
S antigens are soluble heat-stable proteins present in the sera of some infected individuals.
|
P04927
|
Q8EQV2
|
EFTS_OCEIH
|
Elongation factor Ts
|
Oceanobacillus
|
MAITAQMVKELREKTGAGMMDCKKALQETNGDIEQAIDFLREKGMAKAAKKADRVAAEGLTHIEVEGNKAAIIEVNCETDFVTKNDQFKQLLSELGKHIVANEPATVEEALQQKLHGDGETVESVITNAVAKIGEKISLRRFEVLEKTDNDAFGAYLHMGGTIGVLSLLEGTTDEQVGKDIAMHVAAVNPRYVTRDEVAEEEVNREREVLKTQALNEGKPENIVEKMVEGRLGKFFEDIVLLEQSFVKDPDQKVKKYVADKGAAVKTFVRYEVGEGMEKREENFAEEVMSQIKK
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
Q8EQV2
|
Q8DZL4
|
GUAC_STRA5
|
Guanosine 5'-monophosphate oxidoreductase
|
Streptococcus
|
MFNDIPVFDYEDIQLIPNKCIISSRSQADTSVKLGNYTFKLPVIPANMQTIIDEEVAETLACEGYFYIMHRFNEEERKPFIKRMHDKGLIASISVGVKDYEYDFVTSLKEDAPEFITIDIAHGHSNSVIEMIQHIKQELPETFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKVKTGFGTGGWQLAALRWCSKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHLESPGKLVEVEGQQFKEYYGSASEYQKGEHKNVEGKKILLPVKGRLEDTLTEMQQDLQSSISYAGGKELDSLRHVDYVIVKNSIWNGDSI
|
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
|
Q8DZL4
|
P0DTZ6
|
O1634_CONCL
|
O1_cal6.34
|
Californiconus
|
MKLTCVLIVAVLILTACQVIAADSSCWFCSTGFNKCCESTGDCMTYPSEYNASCPEA
|
Probable neurotoxin.
|
P0DTZ6
|
Q5V468
|
MCT_HALMA
|
Succinyl-CoA:mesaconate CoA-transferase
|
Haloarcula
|
MGALDDLRVLDLTQVLAGPYCTMLLADMGADVVKVERPGGDLIRSNPPFVSDGDEEAYGGYFQSVNRGKRSLELNLGTDEDREAFLSLVERADVVVENFKAGTMEKFDCGYETLREHNPDLIYSSIRGFGDPRTGETHRQGQPSFDLIAQALGGVMEITGQSDGPPTKVGPGVGDLFTAVLNAVGILAAVHHRERTGEGQYVDTAMYDSMVSLCERTVYQYSCDGESPTRQGNSHPTLFPYDSFEAADGHVVIAAFADGHWEALCEAMERPDLAAEYPDAGSRIANRESLRAEIAEWTTAIDSETLLDLLEGRVPAAPVQNTADIFDDPHIHDREMLAEVDQPGADDQMTIAGSPIKMTETMPSPGGRAPLLDEHKTELLDEAGVDTGTNRVESDD
|
Involved in the methylaspartate cycle. Catalyzes the transfer of the CoA moiety from succinyl-CoA to mesaconate to generate mesaconyl-CoA (2-methylfumaryl-CoA) and succinate.
|
Q5V468
|
Q1Q8F6
|
ANMK_PSYCK
|
AnhMurNAc kinase
|
Psychrobacter
|
MDDLNYATLTDALEQTVFENFDDGLYIGMMSGTSLDGMDAVLCQFSEKDNTQQPMHVLATHSQDFPPRLREVLLALCQPNGIQALTPSDDEPNSELDWFGWASKEYAEFSSDVVNTLLQQSNTDSESVLAIGCHGQTVRHRPQMGFSLQLVDANIIAERTGISVVSDFRRRDMAVGGQGAPLVPAFHQALFAVPDSTRVLLNLGGIANIAVLPAISNDLVDSNEHSENQPSDSVVGYDTGPANLLLDAWTTLHTDKDYDAGGTWAQSGQVVEPLLNQLLEHPFFKKTYPKSTGREDFNLAWLQDELQKFDQASADVRYSSADVQATLTELTAISASAQINLFINASSSNAVYVCGGGALNNYLMTRLQVHLQRCKVETTASLGLEPTWVEAVAFAWLARQTLMGETGNLPAVTGASKGVVLGQVCFA
|
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.
|
Q1Q8F6
|
P49587
|
PCY1_PLAFK
|
Phosphorylcholine transferase
|
Plasmodium (Laverania)
|
MDSSNYFHDCKTMLSEHNESIESSNNDINGKQKEHIKKGNSENQDVDPDTNPDAVPDDDDDDDDNSNDESEYESSQMDSEKNKGSIKNSKNVVIYADGVYDMLHLGHMKQLEQAKKLFENTTLIVGVTSDNETKLFKGQVVQTLEERTETLKHIRWVDEIISPCPWVVTPEFLEKYKIDYVAHDDIPYANNQKKKKKKKSKGKSFSFDEENEDIYAWLKRAGKFKATQRTEGVSTTDLIVRILKNYEDYIERSLQRGIHPNELNIGVTKAQSIKMKKNLIRWGEKVTDELTKVTLTDKPLGTDFDQGVENLQVKFKELFKIWKNASNKLITDFTRKLEATSYLTSIQNIIDYEIENDDYASSNFDDETSS
|
Controls phosphatidylcholine synthesis.
|
P49587
|
A5D6D2
|
PDXT_PELTS
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Pelotomaculum
|
MKVGVLALQGAFREHQKVLAACGAESVQVRKPEQLEDISALVIPGGESTTIGKLLLEFNLFEPLVKLGQGGLPVFGTCAGMILLAREIAGSGQPRLGLMDISVERNAFGRQVESFEADLDIPVLGEEPFRAVFIRAPYIIEAGGGVEVLARFGEKIVMARQGRCLAAAFHPELTGDLRIHRYFLEKCVRAGQNCKG
|
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
|
A5D6D2
|
A8EXK5
|
RL1_RICCK
|
50S ribosomal protein L1
|
belli group
|
MSNKKDIAVKNSGGKKIREAREKVKSDTLYNLTNAVERLKSASYVKFDPTLEIVMKLGIDPRHSDQMIRGVVNLPAGTGKTVRVAVICKAERVEEAKSAGADLVGSTSIIDEIKAGKINFDVCIATPDMMAAIGSVARILGPKGLMPNPKLGTVTLDIKNAIKNAKSGQVEYRAEKAGIIHAGLGKLSFSDQDLLQNLNEFIEAVIKAKPAGLKGSYLKAMYLSSTMGASVQIDLTSIA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
A8EXK5
|
Q7NJT1
|
GLPK_GLOVI
|
Glycerokinase
|
Gloeobacter
|
MVFASAGAAVSGAILALDLGTTGIRALLFDPSGAVAAGAYREVPQIYPQPGWVEHDPQTIWQLTCEVVAEVQAQSAARIAAVGLTNQRETCLLWDAATGTPHGNAIVWQDRRTAALCQKLRAEGWEAPIRQRTGLVIDAYFSATKLAWLLAHRRPYYPGLKAGTIDSWIIWKLTGGRVHATDTSNASRTMLFNLHTRDWDPELLELLAIPAEILPAIKPSLGVLAETDVRVLGYSAPIAGILGDQQAALFAHGCDRPGLVKCTYGTGSFLVAHTGDRPIRSRHQLLTTVAWSDRTSTGYALEGALFTTGASVQWLRDGLGIIETADESEALAASVPDSGGVYFVPALSGLGAPHWDMGARGLLIGLTRGSGRGQIARAVLEAIAFQTREVTDALAADMGTPLTRLKVDGGAVRNNLLMQLQADVLGVPVERPQLIDTTAQGAAFAAGLGTGFWGDYAELVAARPIDRVFESGERQLVLQAHYAVWQRAVERSREWVR
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
Q7NJT1
|
Q8D4N8
|
RIMO_VIBVU
|
Ribosome maturation factor RimO
|
Vibrio
|
MTVQTFTPNQTTTLDTAKKTIEQQSQELTPSGGNKIGFVSLGCPKNLVDSERILTQLRTEGYEIVNSYHDSDVVIVNTCGFIDSAVQESLDTIGEALKENGKVIVTGCLGAREDEIREVHPGVLGITGPHAYENVLEHVHQFAPKPEHNPFTSLVPDHGVKLTPKHYAYLKISEGCNHRCTFCIIPSMRGDLVSRPVGEILSEAERLKNAGVKELLVISQDTSAYGVDSKHSLGFANGSPVRQNIKALSEELGKMGIWVRLHYVYPYPHVDDLIPLMAEGKILPYLDIPFQHASPNVLKAMKRPGRAERTLDQIKKWREICPELVIRSTFIVGFPGETDEDFEMLLEWLKEAQLDRVGCFKYSPVEGAAANDIDDQISEEVKQERFECFMLVQQEISAAKLQKRIGSTMKVIIDEVDEEGAIGRTYADAPEIDGLVYLNGETSLKAGELVDVLIEHADEYDLWGSLVRA
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
Q8D4N8
|
A0LZ30
|
DAPA_GRAFK
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Gramella
|
MEAFVGTGVALITPFKEDLSIDTEALSNLVKYQIENGIEYLVVLGTTAESATLTQDEKELIKKVVKEANAGELPLVLGVGGNNTAGVVEELQIADLDGFDAILSVSPYYNKPTQEGIYRHFEAISKASPLPIILYNVPGRTSSNVLPETINRIARNLKNVIGVKEAAGDIVQAMKMISLVPDDFKVISGDDMITLPMTLAGGKGVISVIGQGLPKEFSNMVRAGLEGKVSEAYQLHYKIAPSIEFIFAEGNPAGIKTLLAKKGIISNTLRLPLVEATETLQSKINSFVDNF
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
A0LZ30
|
Q756C3
|
CEF1_ASHGO
|
Pre-mRNA-splicing factor CEF1
|
Eremothecium
|
MPAVPIYVKGGVWSTVEDEILRAAVQRYGTHAWNKVASLLPRKSGKQCRARWEESVRPTRQGAWTAAEDATLAALARGGPQWRSVGAALGRPAAACAARWAELTGDQAVAGPAAGERIPGAEGLPAVPEEDEREMVAEARARLASTQGKKAARRARERQVEESRRVARLQKRRALLQAGVNSALPLPRAVRGQLDPNADVLYELAPAEGVFETANEAARDRAAREAYERQIEARGKRTARKQSRAPARAPATEQPALQVRRAIPRPPLELPVPEALLKNSAAPTAAVRRALARLWQGLPAAKNDFDVAPESEDEQPSGSADAAVQSTDMEVLLPWEPPLRQDLPPPPPPPPGLLAEHYRALAAAAAGGPACYDTPDVLRQREAIERALAAEPSPAMLHPQCELPRLPSLDALRAAAQPRPQRRLAAHAATDAGSRLLAYELLPDLATKQREYYVRYTAYELERTAVATRVRRLTAGR
|
Involved in mRNA splicing and cell cycle control.
|
Q756C3
|
C5BF98
|
MDH_EDWI9
|
Malate dehydrogenase
|
Edwardsiella
|
MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKVCGFGGEDASPALVGADIVLISAGVARKPGMDRSDLFNVNAGIIRNLIGQVARTSPNACIGIITNPVNTMVPIAAEVLKKAGVYNPNKLFGVTTLDIIRSNTFVGELKHLDPATLDIPVIGGHSGVTILPLLSQIPGVSLSEREVAELTKRIQNAGTEVVEAKAGGGSATLAMGQAAARFALSLVRAMQGDENVVECGYVESDGEYARFFAQPLLLGKAGLVQRLSIGTLSAFEQDALESMLEVLRKDIALGEDFINK
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
C5BF98
|
P46377
|
FAS5_RHOFA
|
Uncharacterized oxidoreductase ORF5 in fasciation locus
|
Rhodococcus
|
MSGIWHTDDVHLTSAGADFGNCIHAKPPVVVVPRTVADVQEALRYTAARNLSLAVRGSGHSTYGQCQADGGVVLDMKRFNTVHDVRSGQATIDAGVRWSDVVAATLSRQQTPPVLTDYLGTTVGGTLSVGGFGGSSHGFGLQTDNVDSLAVVTGSGDFRECSAVSNSELFDAVRGGLGQFGVIVNATIRLTAAHESVRQYKLQYSNLGVFLGDQLRAMSNRLFDHVQGRIRVDADGHLRYRLDLAKYFTPPRRPDDDALLSSLQYDSCAEYNSDVDYGDFINRMADQELDLRHTGEWFYPHPWASLLIPADKIEQFIETTSSSLTDDLGNSGLIMVYPIPTTPITAPFIPIPHCDTFFMLAVLRTASPGAEARMIASNRLLYEQARDVGGVAYAVNAVPMSPGDWCTHFGSRWQAIARAKRRFDPYRILAPGYRMSFD
|
The FAS-operon encodes genes involved in cytokinin production and in host plant fasciation (leafy gall).
|
P46377
|
A5GAU3
|
RS13_GEOUR
|
30S ribosomal protein S13
|
Geotalea
|
MARIAGIDLPRNKRIEIALTYIYGIGRSTAQKILADAGVDSNTRSDNLTESEIARIRENIDKNVKVEGDLRRDISMNIKRLMDLGCYRGLRHRKGLPVHGQRTKTNARTRKGPARTVAGKKK
|
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.
|
A5GAU3
|
Q077R2
|
WFAP_ECOLX
|
UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfaP
|
Escherichia
|
MELVSIIIAAYNCKDTIYATVESALSQTYKNIEIIICDDSSTDDTWDIINKIKDSRIICIKNNYCKGAAGARNCALKIAKGRYIAFLDSDDYWVTTKISNQIHFMETEKVFFSYSNYYIEKDFVITGVFSSPPEINYGAMLKYCNIACSTVILDRTGVKNISFPYIDKEDYALWLNILSKGIKARNTNLVDTYYRVHAGSVSANKFKELIRQSNVLKSIGIKAHHRIICLFYYAINGLIKHCFSYRDKRNA
|
Catalyzes the addition of Glc, the second sugar moiety of the O56-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol.
|
Q077R2
|
Q0AEI9
|
ATPA2_NITEC
|
F-ATPase subunit alpha 2
|
Nitrosomonas
|
MSVLDDVTEQQFEQNFNAWLDSLSTGATPTPVLTETGTVTEVADGVAIVSGLARALADELLVFASGVHGIVLDLEPGRLGIILLGPSEQIHLGETVYRTRKVVSVPVGSALLGRVIDAMGRPRDTLGPIDAIAEHPIEAEAPSILNRTQIFRPLATGLKAIDAAIPVGLGQRELIIGDRQTGKTSIAIDTMLNQARSDVLCIYCAVGQRGDAVARVIRALKDGEMLQRCIVMSAGDEEAPGLSYIAPYAAMTMAEYFSAQGQDVLVIFDDMTHHARSYRELSLLLRRPPGREAFPGDIFYVHARLLERAGQFGADIGGGSITTLPVVETQAGNLSAYIPTNLISITDGQIYLSPQLVRKNQFPAVDLGLSVSRVGSKAQNRTLRGVSGNLRVTLSQFEELEDFARFGTRLDDVTRARLARGSAVRTALRQAERDPMSALEQLAVLIAAMEGLFDQFNEQKINDAMRLVRDAAQQQLAVIEQRIIDNQTLQDDDHTLIVNCAQKALSIFDQPATNTK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q0AEI9
|
Q9FXA7
|
RGXT3_ARATH
|
Rhamnogalacturonan xylosyltransferase 3
|
Arabidopsis
|
MAQQSQRPISNRHISLLNRNGLILLLLLALFVILGVFLPLTKSSLFMFPNTTSSSLSPSSSLSVSDWRDYSLAQAVKFVAKNETVIVCAVSYPFLPFLNNWLISISRQKHQEKVLVIAEDYATLYKVNEKWPGHAVLIPPALDPQSAHKFGSQGFFNLTSRRPQHLLNILELGYNVMYNDVDMVWLQDPFDYLQGSYDAYFMDDMIAIKPLNHSHDLPPLSRSGVTYVCSCMIFLRSTDGGKLLMKTWVEEIQAQPWNNTQAKKPHDQPAFNRALHKTANQVKVYLLPQSAFPSGGLYFRNETWVNETRGKHVIVHNNYIIGYDKKMKRFQDFSLWLVDDHALESPLGKLEIYQEQNTTTEGKNLTKIVRKQRKNRGKKHKLP
|
Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose onto L-fucose. Probably involved in the biosynthesis of rhamnogalacturonan II (RG-II) through xylosylation of the internal fucose moiety of the A-chain of RG-II, a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues such as roots and pollen tube growth and elongation.
|
Q9FXA7
|
Q9JJC9
|
HERP2_MOUSE
|
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein
|
Mus
|
MDQSGMEIPVTLIIKAPNQKYSDQTISCFLNWTVGKLKTHLSNVYPSKPLTKDQRLVYSGRLLPDHLQLKDILRKQDEYHMVHLVCASRSPPSSPKSSTDRGSHEALASSTSSNSDHSDSTTPSPSQESLSLVTGSSEGLRQRTLSQAQTDPAQSHQFPYVIQGNVDHQFPGQGVPPAFPVYPALSPLQMLWWQQMYAHQYYMQYQAAVSAQATSSAGSAQRAASSPLNLAHVPGEEPPPAPNLVAQENGPMNENVQMNAQGGPVLNEEDLNRDWLDWVYTFSRAAVLLSIVYFYSSFSRFIMVMGAMLLVYLHQAGWFPFRQEGGQQQAPNNVDANNDGHNANNLELEEMERLMDDGLEDESGEDAGEDASAAQRPGLMASAWSFITTFFTSLIPEGPPQVAN
|
Could be involved in the unfolded protein response (UPR) pathway.
|
Q9JJC9
|
P0C5K8
|
SCX5_TITBA
|
T-alpha* NaTx3.4
|
Tityus
|
MNDFVFLVVACLLTAGTEGKKDGYPVEGDNCAFVCFGYDNAYCDKLCKDKKADSGYCYWVHILCYCYGLPDKEPTKTNGRCKPGKK
|
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission.
|
P0C5K8
|
Q7VR45
|
LPXK_BLOFL
|
Lipid A 4'-kinase
|
Candidatus Blochmannia
|
MLFNIWFGSSLCYLFLLPFSWVYGFFSTLNRISYKYGWRKVYRFSVPIIVIGNLTIGGNGKTPMVLWLIDQLKTRGWRVGVVSRGYGGRSDKYPIIINSTSCSKKCGDEPLLIWRRTGVLVSVSPNRVKAVSALLKKQPLLDIIISDDGLQHYALFRDIEWVVVHSLRRFGNGCWLPAGPMRERITRLNTVQAIIINGLSNDIQSGAILMQLCPRSIINLVTGEIRPIQPLKDVVAIAGIGYPKQFFMTLQDYGIFPIKTIEFSDHHMYSEIMLSSLTSGNEMLLMTEKDAIKCLDFAHENWWYVHIDVNIHQEDTKKLLSKIESTIQYYKNN
|
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).
|
Q7VR45
|
A4VRE8
|
METK_PSEU5
|
Methionine adenosyltransferase
|
Pseudomonas
|
MSEYSIFTSESVSEGHPDKIADQISDAVLDAIIAEDKHARVACETLVKTGVAIVAGEVTTSAWVDLEQLVRDVIVDIGYNSSEVGFDGATCGIINIIGKQSVDIAQGVDRTKPEDQGAGDQGLMFGYASNETDVLMPAPIRFSHALVERQAEARKNGLLPWLRPDAKSQVTCRYENGQVVGIDAVVLSTQHNPDVKQSDLREAVMELIIKHSLPAELLHKDTQYHINPTGQFVIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLADRCEIQVSYAIGVAQPTSISLNTFGTGKLGDDKIIALVREHFDLRPYAITRMLDLLHPMYRATAAYGHFGRTPYEMTVGADTFTAFTWEKTDKADALRAAAGL
|
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
|
A4VRE8
|
A0A1D8PC43
|
MVD1_CANAL
|
Mevalonate-5-diphosphate decarboxylase
|
Candida
|
MYSASVTAPVNIATLKYWGKRDKSLNLPTNSSISVTLSQDDLRTLTTASASESFEKDQLWLNGKLESLDTPRTQACLADLRKLRASIEQSPDTPKLSQMKLHIVSENNFPTAAGLASSAAGFAALVSAIAKLYELPQDMSELSKIARKGSGSACRSLFGGFVAWEMGTLPDGQDSKAVEIAPLEHWPSLRAVILVVSDDKKDTPSTTGMQSTVATSDLFAHRIAEVVPQRFEAMKKAILDKDFPKFAELTMKDSNSFHAVCLDSYPPIFYLNDTSKKIIKMVETINQQEVVAAYTFDAGPNAVIYYDEANQDKVLSLLYKHFGHVPGWKTHYTAETPVAGVSRIIQTSIGPGPQETSESLTK
|
Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway . MVD1 converts diphosphomevalonate into isopentenyl diphosphate . The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
|
A0A1D8PC43
|
Q6AD21
|
RPOA_LEIXX
|
Transcriptase subunit alpha
|
Leifsonia
|
MLIAQRPTLTEENISEFRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFSTVPGVKEDVTEIILNIKGLVVSSEHDEPITAYLRKTGAGQVTAADISAPAGVEIHNPELVIATLNDKAKFEVELTIERGRGYVSAQQNRNEYSEAGQIPIDSIYSPVLKVTYRVEATRAGERTDFDRLVVDVETKPAISPRDAIASAGRTLVELFGLARELNSAAEGIEIGPAPVDQVLSSELSMPIEDLDLSVRSYNCLKREGINTVSELVSLSETQLMNIRNFGQKSVDEVKDKLTEMGLSLKDSVPGFDGAHFYSGYDEDESTTI
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q6AD21
|
Q1QDH1
|
RL6_PSYCK
|
50S ribosomal protein L6
|
Psychrobacter
|
MSRVAKAPVTLPNGVSVTLNDRQVEVKGKNGNMSLRLHELVELKQEDDAIIFSPTVDSKEAMMHTGTMRSLLNNLVIGVNEGFEKRLQLIGVGYRAQAAGNKVTLNVGYSHPVEYTLPEGVSAETPTQTEIVLKSNDKQQLGQAAADIRGFRPPEPYKGKGIRYSDEHVIRKEAKKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
Q1QDH1
|
A4QN56
|
MFS4B_DANRE
|
Major facilitator superfamily domain-containing protein 4B
|
Danio
|
MSPAEAAPRKKHVRFARMEGDVDHDDQEENTLFDKQKDVKEGLKSVLKGGKGILSQGSGQVDVVRPGRSKTGTCWRWLVSLALCASFLGLGMAISVLGPTFEDLAINVNKNISNLSYIFVGRASGYIGGSLLGGILFDFVNPHLLLGFALLTTAFGMSGTPFCKKAWVLTVLMSSVGVSMGVLDTGGNVLILNTWGEQAGPHMQALHFSFAAGAFASPIIAKLLFGHHNSSTNTSLMSGHASKTIDAVLPFSHPKGTSTIDLPWMWAYIVIGAFVLLVSLLFFSLYFCISTNSNRTKTASGKQQFSKHHNTLIILLSMFFFFYVGSEVAYGSFIFTYGKDYVHMEETEAAGLNSLFWGAFAAGRGLAIFFAACLHPGTLILLSLVGTTVSSLLLCLFSQNYPMLWACTALYGISMSTTFPSGISWVEQYTTVTGRSAAIFVVGAALGEMVLPALLGFLLGHVQNYPLLMYLTLCTATFTSILFPVLYKLASPEGNVTLRKSSGKCTIKDADDSEYRQALLENMEEQEENESEADLCNDADFEVIEMDDASLLSSPKSSPPADVAASVPDVHLVASPLSEPNMLSFSTDSPRSKL
|
May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney.
|
A4QN56
|
C3RT18
|
GGN2_LIMKU
|
Gaegurin-LK2
|
Limnonectes
|
MFTMKKSLLLIFFLGTINLSLCEEERNAEEEKRDGDDEMDVEVQKRFLGPIIKMATGILPTAICKGLKKC
|
Has antimicrobial activity against Gram-positive bacteria S.aureus ATCC 2592 (MIC=2.5 uM), S.aureus ATCC 43300 (MIC=2.5 uM) and B.subtilis (MIC=20.0 uM), against Gram-negative bacteria E.coli ML-35P (MIC=50.0 uM), P.aeruginosa PA01 (MIC=10.0 uM) and P.aeruginosa ATCC 27853 (MIC=5.0 uM) and against fungus C.albicans ATCC 2002 (MIC=5.0 uM).
|
C3RT18
|
B2TY23
|
EFP_SHIB3
|
Elongation factor P
|
Shigella
|
MATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK
|
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
|
B2TY23
|
Q88PC0
|
GATB_PSEPK
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Pseudomonas
|
MQWEVVIGLEIHTQLATQSKIFSGSATTFGSEPNTQASLVDLGMPGVLPVLNEQAVRMACMFGLAIDAEIGKRNVFARKNYFYPDLPKGYQISQMDLPIVGKGHLDIALEDGTIKRIGVTRAHLEEDAGKSLHEDFSGSTGIDLNRAGTPLLEIVSEPDMRSAKEAVAYVKAIHALVRYLGICDGNMAEGSLRCDCNVSIRPKGQTEFGTRCEIKNVNSFRFIERAINSEIQRQIDLIEDGGKVVQETRLYDPNKDETRSMRSKEEANDYRYFPDPDLLPVVIEDSFLETIRAGLPELPPQKVERFQTQYGLSAYDANVLASSREQADYFEEVVKIGGDAKLAANWVMVELGSLLNKLGVEIDQAPVSAAQLGGMLLRIRDNTISGKIAKTVFEAMAAGEGDADSIIESKGLKQVTDTGAIDKMLDEMLAANAEQVEQYRAADEAKRGKMFGFFVGQAMKASKGKANPGQVNQLLKAKLEG
|
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).
|
Q88PC0
|
Q0WT48
|
DNJ21_ARATH
|
Translocation protein SEC63 homolog ERDJ2A
|
Arabidopsis
|
MAASEENSALFPIFILTIMAIPLVPYTMVKLSGALSKKQRTIHCQCLECDRSGKYKRSLFKKISNFSTWSNLTLVLLWVVMIFLIYYTKNMSREAQVFDPFSILGLEPGVTDSEIKKAYRRLSIQYHPDKNPDPEANKYFVEFISKAYQALTDSVSRENFEKYGHPDGRQGFQMGIALPQFLLDIDGASGGILLLWIVGVCILLPLVIAVIYLSRSSKYTGNYVMHQTLSAYYYLMKPSLAPSKVMEVFTKAAEYMEIPVRRTDDEPLQKLFMSVRSELNLDLKNMKQEQAKFWKQHPAIVKTELLIQAQLTRESGVLSPALQGDFRRVLELAPRLLEELLKMAVIPRTAQGHGWLRPAVGVVELSQCIVQAVPLSARKSSGVSSEGISPFLQLPHFSDAVVKKIARKKVKSFQDLQEMRLEDRSELLTQVAGLSATDVEDIEKVLEMMPSITVDITCETEGEEGIQEGDIVTLQAWVTLKRPNGLVGALPHAPYFPFHKEENYWVLLADSVSNNVWFSQKVSFLDEGGAITAASKAISESMEGSGAGVKETNDAVREAIEKVKGGSRLVMGKLQAPAEGTYNLTCFCLCDTWIGCDKKQALKVKVLKRTRAGTRGLVSDEGAIAEEGMEEEDEIEEEDYDDDYESEYSEDEDEKKDMDEKRGSKKANGSVKQKKESSSEESGSEEE
|
Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
|
Q0WT48
|
B9E1I7
|
CODY_CLOK1
|
GTP-sensing transcriptional pleiotropic repressor CodY
|
Clostridium
|
MSTLLDKTRKLNKILQKSGVEPVVFDDICKILSEVLGCNVYVISRKGKVLGYNFPDGFECSTVKNKIISEMRFPEQYNNKLLNAHETLPNLSNHGICVFEDGTPCDLEDKVTTIVPIIGNRERLGTLLLASFGEKFTDEDLVLGEYSATIVGLEILKSKNDEIEEEARKKAVVQLAIGTLSYSELEAVEHIFNELDGKEGLLVASKIADKVGITRSVIVNALRKFESAGVIESRSLGMKGTHIKILNDKLLDELKKIK
|
DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor.
|
B9E1I7
|
B4ER10
|
IFNL3_CHICK
|
Interleukin-28B
|
Gallus
|
MVCYGVTIILVGTLGSLLVGAFPQVTPKKSCSLSKYQFPAPLELKAVWRMKEQFEDIMLLTNRKCNTRLFHRKWDIAELSVPDRITLVEAELDLTITVLTNPTTQRLAETCQQPLAFLTQVQEDLRDCLALEAPSHQPSGKLRHWLQKLKTAKKKETAGCLEASAILHIFQVLNDLRCAAQREDCT
|
Cytokine which plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Exhibits antiviral activity against the H5N1 influenza A virus. Induces the expression of the antiviral MX protein in epithelial-rich tissues, such as intestine, trachea and lung.
|
B4ER10
|
B0KHR5
|
TRMA_PSEPG
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Pseudomonas
|
MSAAFDPSSYATQLDAKVARLRELLAPFGAPEPAVFDSPREHYRLRAEFRLWREDGQRHYAMFAQGDKHKAILIDDFPIASQRINALMPRLKAAWQASEELGNRLFQVEFLTTLAGDAMITMCYHRPLDEAWEVEARQLAEALGVSVIGRSKGKRLVIGRDYAIEELDVAGRVFSYRQPEGAFTQPNGAVNQKMLSWAFEAIGEREDDLLELYCGNGNFTLPLATRVRQVLATEISKTSVNAALSNLDENAVDNVRLVRLSAEELTQALNEVRPFRRLEGIDLKSYEFGTVFVDPPRAGMDPDTCELTRRFERILYISCNPETLAANIAQLQDTHRIERCALFDQFPYTHHMESGVLLVRR
|
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
|
B0KHR5
|
Q6K4N0
|
RSZ21_ORYSJ
|
RS-containing zinc finger protein 21
|
Oryza sativa
|
MARLYVGNLDPRVTSGELEDEFRVFGVLRSVWVARKPPGFAFIDFDDKRDAEDALRDLDGKNGWRVELSRNSSSRGGRDRHGGSEMKCYECGETGHFARECRLRIGPGGLGSGKRRSRSRSRSRSPQYRKSPTYGRRSYSPRDRSPRRRSVSPVRGRSYSRSPRGRGGSPYADGRDGGRYRRSRS
|
Involved in pre-mRNA splicing.
|
Q6K4N0
|
B4SG10
|
RPOC_PELPB
|
Transcriptase subunit beta'
|
Pelodictyon
|
MIFSQGASPLKGEFSRIKFSIASPESILAHSRGEVLKPETINYRTFKPERDGLMCEKIFGPTKDWECYCGKYKRVRYKGIICDRCGVEVTTKSVRRERMGHIALAVPVVHTWFFRSVPSKIGALLDLSTKELERIIYYEVYVVINPGEPGEKQGIKKLDRLTEEQYFQIITEYEDNQDLEDSDPDKFVAKMGGEAIHMLLKNIDLDASAIHLRKVLKESNSEQKRADALKRLKVVEAFRKSYEPHKKTRKKPQGLFPEDELPEPYVYEGNKPEYMVMEVVPVIPPELRPLVPLEGGRFATSDLNDLYRRVIIRNNRLKKLIDIRAPEVILRNEKRMLQEAVDALFDNSRKANAVKTGESNRPLKSLSDALKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHECGLPKSMAIELFQPFVIRRLVDRGIAKSVKSAKKLIDKKDPIVWDVLEKVIDGRPVLLNRAPTLHRLGIQAFQPLLIEGKAIQIHPLVCTAFNADFDGDQMAVHIPLSQEAQLEASLLMLSSHNLILPQSGKPVTVPSQDMVLGMYYLTKSRSRDLGEGQIFYSPQDVLIAYNEERVGLHAQIFVQYDGEIDQKFDSLRVLDTMTDLTAEKSAWLKAQIEKKCILLTTVGRVIFNQNVPKEIGFINRVIDKKVAKELIGRLSSEVGNVETAKFLDNIKEVGFHYAMKGGLSVGLSDAIVPETKARHIKSAQRDSTKVVKEYNRGTLTDNERYNQIVDVWQKTSNIVAEESYQKLKKDRDGFNPLYMMLDSGARGSREQVRQLTGMRGLIARPQKSMSGQPGEIIENPIISNLKEGLTVLEYFISTHGARKGLSDTSLKTADAGYLTRRLHDVAQDVIVTIDDCGTTRGLYVHRNIEEETSGQIKFREKIKGRVAARDIIDTLNNNVIVNSGEIITEELAELIQETAGVEEAEIRSVLTCESKIGICSKCYGTNLSVHELVEIGEAVGVIAAQSIGEPGTQLTLRTFHQGGTAQGGISETETKAFYDGQIQFEDIKTVEHTAINEDGVADLRIIVIQKNGKINIADPESGKILKRYLVPHGAHLHCKNGSLVKKDQVMFSSEPNSTQIIAEIPGIIKFADIEKGITYKEEVDPQTGFSQHTIINWRSKLRATETREPRLMIIDASGEVRKTYPVPIKSNLYVEDGQKVEPGDIMAKVPRNLDRVGGDITAGLPKVTELFEARIPTDPAIVTEIDGYVSFGSQRRSSKEIKVKNDFGEEKVYYVQVGKHVLANEGDEVKAGDPLTDGAVSPQDILRIQGPNAVQQYLVNEIQKVYQINAGVEINDKHLEVIVRQMLQKVRVEEPGDTDLLPGDLIDRSAFVESNQSVAEKVRITEKGDAPARIQDSQLHKVRDITKLNRELRKNSKNMIAFEPALQATSHPVLLGITSAALQTESVISAASFQETTKVLTDAAVAGKVDYLAGLKENVIVGKLIPAGTGLKRYKAIKLTGEGQESNATERVVEEPATREGFANER
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B4SG10
|
A9A3X2
|
RNZ_NITMS
|
tRNase Z
|
Nitrosopumilus
|
MKLVFLGTSAAQPTENRGLSCICLEREGEVLMFDAGEAAQISYMKSGLGWNKKMKIFVTHLHGDHCVGILGLLQTMSMQNRTESLEIFGPSGIEEFIAANIKVLNFGLSFPILINTIKDEKIFEDEKFLIRTCKANHSIIAFSYLFEEKDKPGRFNVEKAKELGIPEGELWNKLQNGNEITVNEKIIKPEQVLGERRPGKKIGISGDTMPTKELEEFFEECDYLVFDSTFLEAEKQKAQDTCHSTAKQAATVAKNAKVKNLVLTHFSARYRDEVEHLREAKEIHDSVITAKDLLEIEIK
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
A9A3X2
|
Q2JIF9
|
ATPD_SYNJB
|
F-type ATPase subunit delta
|
unclassified Synechococcus
|
MISSTMAEKVVDPYAEALIALGSGQGLLDTFAADMRFIAEVLRATPELGQFLANPVIKAEAKKNLLQQVFADQIHPLLLNALKLLTDRRRIMFLGTVCRRFLDLQRKLQNIVLAEVTTAIPLTEAQQQSIRERVMDFTQASGVELQATQDPELLGGVVIKIGSQVIDLSLRGQLRRLALQLA
|
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.
|
Q2JIF9
|
Q7MAE8
|
PYRF_WOLSU
|
OMP decarboxylase
|
Wolinella
|
MQLCIALDLPSQEENLKLLESLVGLPVWIKVGLRSYIRDGKEFLGRIRQIDPRFELFLDLKLHDIPNTMGDAAEEIASLGVGMFTLHASSGGEAMREVAARLARFPRRPLAFAVTALTSFGEEGFREIYNASLESKALDMAMLAAQNGMDGVVCSVFESQRIKSYVAQDFLTLTPGIRPFGEPSGDQKRVADLHEAKSASSDFIVVGRPVYKHPRPREAVEKILEGIA
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
Q7MAE8
|
A5I7K8
|
EFTU_CLOBH
|
Elongation factor Tu
|
Clostridium
|
MAKAKFERSKPHVNIGTIGHVDHGKTTLTAAITTVLAQKGGASATKYDEIDKAPEEKERGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLASRVGVQYIVVFLNKADQVDDPELIELVEMEVRELLNEYGFPGDDTPIVVGSALEVLENQDNAEKTKCIDELMEAIDSYIPTPERATDQPFLMPVEDVFTITGRGTVATGRVERGVLHTGDEVELIGMKQEVSKTVCTGIEMFRKILDEAMAGDNIGALLRGIQRDEIQRGQVLAKPGSVTPHKKFVGQVYVLKKEEGGRHTPFFNGYRPQFYFRTTDVTGSINLPEGVEMVMPGDHIDMAVELITPVAMHENLRFAIREGGRTVGSGVVTTISE
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
A5I7K8
|
A4SSZ3
|
RS14_AERS4
|
30S ribosomal protein S14
|
Aeromonas
|
MAKTSMKAREAKRAKLVAKFATKRTELKAIIVDMNASEEARWDAVLQLQQLPRDSSPSRQRNRCNITGRPHGFLRKFGLSRIKVREHAMKGEIPGLKKASW
|
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.
|
A4SSZ3
|
Q1ICK1
|
ZIPA_PSEE4
|
Cell division protein ZipA
|
Pseudomonas
|
MEIGLREWLILIGIIVIAGILFDGWRRMRGGKGKLKFRLDRSYANAPDDEGGAEVLGPSRVLETHKEPELDESDLPSVSAPARERERDPKPAKASKRGKRNHSEPQQGDLNLAAEAREPDLFADDKDDFVADNNRHGAAATPSTPVKELPPAEEVLVISVISRDEGGFKGPALLQNILESGLRFGEMDIFHRHESMAGHGEVLFSMANAVKPGVFDLDDIDHFSTRAVSFFLGLPGPRHPKQAFDVMVAAARKLAHELDGELKDDQRSVLTAQTIEHYRQRIVEFERRALTQKR
|
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
|
Q1ICK1
|
Q2RXI5
|
GUAA_RHORT
|
Glutamine amidotransferase
|
Rhodospirillum
|
MTDRTSVSATDRILIIDFGSQVTQLIARRVRESGVYSEIQPFNTVTAASIAAFAPKGVILSGGPASVTAADTPRAPIELFTMGLPVLGICYGQQTMVAQLGGRVEAPDHREFGRAFVEVTAGCALFDGVWTPGERDQVWMSHGDRVDAIPEGFSVVAVSEGAPYAAIADEARHFYGVQFHPEVVHTPKGAALLRNFTHGICGCGGDWTMAAFKDQAIARVREQVGSGRVICGLSGGVDSSVVAALIHEAIGEQLVCVLVDHGMMRQGETEQVVRVFRDRFNITLVHRDASELFLGKLDGVVDPEAKRKIIGATFIDVFDEEARKVGGADFLAQGTLYPDVIESVSFTGGPSVTIKSHHNVGGLPERMKMALVEPLRELFKDEVRDLGRELGLPDEMVGRHPFPGPGLAIRIPGQPLTREKLDILRRADAIYLEEIRNAGLYDVIWQAFAVLLPVRTVGVMGDARSYDFALALRAVTSTDGMTADYYPFDHTFLGRVANRIINEVKGVNRVVYDITSKPPGTIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q2RXI5
|
Q03FS2
|
RBFA_PEDPA
|
Ribosome-binding factor A
|
Pediococcus
|
MARQYRSDRLSQEIEKEVSDILRRRVRDPRVEGVTITGVDVTGDLQQAKIYYSILSDKASDDQKTKAGLEKASGLIRKELGSRLSIYKTPELSFIRDESVQYGDKIDQLLNKLNRD
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One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
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Q03FS2
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Q9Z856
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DAPAT_CHLPN
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LL-diaminopimelate aminotransferase
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Chlamydia
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MRRNPHFSLLKPQYLFSEISKKLAQFRKENPEISVIDLSIGDTTQPLCRSITQAIKEFCVSQEKQETYRGYGPETGLEKLRTKIASEVYENRISPEEIFISDGAKPDIFRLFSFFGSEKTLGLQDPVYPAYRDIAHITGIRDIIPLACRKETGFIPELPNQQSLDILCLCYPNNPTGTVLTFQQLQALVNYANQHGTVLIFDAAYSAFVSDPSLPKSIFEIPEAKYCAIEINSFSKSLGFTGMRLAWNVIPKELTYDNNEPMINDWKRLFATTFNGASLLMQEAGYYGLDLFPTPPAISLYLTNAQKLKKSLETAGFSVHGGDHAPYLWVELPEGISDEEAFDFFLHQYHIAVTPGHGFGSCGQGFVRFSALTQPQNIALACDRLCTASLKETMVLA
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Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
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Q9Z856
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