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
|
|---|---|---|---|---|---|---|
Q8RDA2
|
RL31_CALS4
|
50S ribosomal protein L31
|
Caldanaerobacter
|
MKPGIHPTYYHDAVVKCACGNTFITGSTKKEIRVEICSKCHPFFTGQQKIVDTGGRVERFRKRFNLEEK
|
Binds the 23S rRNA.
|
Q8RDA2
|
P24499
|
ATP6_TRYBB
|
F-ATPase protein 6
|
Trypanosoma
|
MFLFFFCDLFWLRLLLCMYYCVSRLCFIVYFNCLMLIFDFLLFCLFDLYLFVGLCLFLLLWFMLFNLYSLILYYCITYLNLYLLFCIVFLLYIAFLFLFCFLCDFFLFNNLLVGDSFMDVFFIRFLLCFLECFSLLCRCLSTFLRLFCNLLSSHFLLLMFFDFFYFIFVFFFYGVFCYFILFIFVFCFCLLFYVFLYLLDLFAAILQLFIFCNMILQLIMDFLLFLLFV
|
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 synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
|
P24499
|
B0UHX7
|
RL7_METS4
|
50S ribosomal protein L7/L12
|
Methylobacterium
|
MADLAKLVDDLSSLTVLEAAELAKMLEEKWGVSAAAAVAVAAGPAAGGAAAPAAEEQTEFTVVLAAAGDKKIEVIKEVRAITGLGLKEAKDLVEGAPKPVKEGVSKDDAAKLKAQLEKAGAKVELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
B0UHX7
|
Q12G79
|
RS11_POLSJ
|
30S ribosomal protein S11
|
unclassified Polaromonas
|
MAKSPSNNAAQRVRKKVRKNVADGIAHVHASFNNTIITITDRQGNALSWASSGGQGFKGSRKSTPFAAQVASEVAGRAAIEQGIKNLDVEIKGPGPGRESSVRALGALGIRINSIADVTPVPHNGCRPQKRRRI
|
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.
|
Q12G79
|
Q3Z5S7
|
RSMH_SHISS
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Shigella
|
MMENYKHTTVLLDEAVNGLNIRPDGIYIDGTFGRGGHSRLILSQLGEEGRLLAIDRDPQAIAVAKTIDDPRFSIIHGPFSALGEYVAERDLIGKIDGILLDLGVSSPQLDDAERGFSFMRDGPLDMRMDPTRGQSAAEWLQTAEEADIAWVLKTYGEERFAKRIARAIVERNREQPMTRTKELAEVVAVATPVKDKFKHPATRTFQAVRIWVNSELEEIEQALKSSLNVLAPGGRLSIISFHSLEDRIVKRFMRENSRGPQVPAGLPMTEEQLKKLGGRQLRALGKLMPGEEEVAENPRARSSVLRIAERTNA
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q3Z5S7
|
Q9FIR9
|
LSU2_ARATH
|
Protein ENHANCED DE-ETIOLATION 6
|
Arabidopsis
|
MGKGGNYVTVAASEVDELRRKNGEMEKAVEEMKKEMLQLWRRTQVAEEAEERLCSQLAELEAESLDQARDYHSRIIFLMNELSRLSSDSASASP
|
May be involved in defense responses monitoring . Probably implicated into osmotic stress signaling .
|
Q9FIR9
|
Q8PGG5
|
ATPA_XANAC
|
F-ATPase subunit alpha
|
Xanthomonas
|
MATTLNPSEISDLIKTRIEAVKLSAESRNEGSVTSVSDGIVRIFGLADVMQGEMIELPNNTFALALNLERDSVGAVVLGDYESLREGDVAKTTGRILEVPVGPELLGRVVNALGEPIDGKGPLGATQTAPVERVAPGVIWRKSVDQPVQTGYKSVDAMIPIGRGQRELVIGDRQTGKTALAIDAVINQKGTGIKCVYVAIGQKASTVANIVRKLEENGALAHTVVVAATASESAAMQYISPYAGCTMGEYFMDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVSEEYVEKFTNGAVTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETDLFNAGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRISLAQYRELAAFAQFASDLDEATRKQLERGQRVTELMKQKQYAPMSIANQALSIYAVNEGYLDDVPVNKLLAFEEGLHAHFANTQGELVSKINSTGGWDNDIEASFKKGIEEFKTTGSW
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q8PGG5
|
Q4J8E4
|
COXX_SULAC
|
Heme O synthase
|
Sulfolobus
|
MSVTLSRKLIDYVKLAKPKVVSLLDVVAIASYILAFKGNWYNLIPVLIGGSIAAGGSMIINGGLEIEKDKVMKRTSWRPTVKGEVGRKEAYMVGGIACALGSLIGLLANPLTAFFILLGSLVYVFVYSYYLKPRTWLNIVIGGFAGSAAAWAGYAAASNSFNLESLLLGLLVFAWTPGHFWALALRYKRDYANAEIPMLPAIVDDKTAARAIAISNILMIPFALGLMLYLNLIYVIITLAATAVLLYFNVRLMRNPTPEESWISYKFSAPYLAIVMIAAVISFIL
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
Q4J8E4
|
Q1Q0T3
|
HZSG_KUEST
|
Hydrazine synthase subunit gamma
|
Candidatus Kuenenia
|
MAREMRLGGKERMKTGVVKIGLVAALGVVGLISAGGVYAGQPRVISTIQTGATWEPLGREEPLTVPEVHFRVKHSPFKSELVRYGQFQFNDAAWSLQGSYSCASCHYERGQTTGLIWDLGDEGWGSWKNTKYIRGGRYLPPFRHEGFTGHPDEIVGATSSLDRVCGRDPGFVFRSENFSPMRLEALICYIRALEFTGSPFRNADGSLTEAQKRGQKIFEDPKVGCLECHPGDPMDPRALFSDAQTHDVGTGRVGVNGFRSTPGKVFNISALEAGEDPYGVESNTPIIGLDLVKEFDTPTLRDIYASGTYFHDGGARTLMDTINNTVNDKDMHGRTSHLKQQELQDLVEYLKAL
|
Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine . The gamma subunit catalyzes the first half-reaction, i.e. the three-electron reduction of nitric oxide to hydroxylamine; it may obtain electrons from the triheme cytochrome c kuste2854 . Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans .
|
Q1Q0T3
|
A9BNB9
|
RS15_DELAS
|
30S ribosomal protein S15
|
Delftia
|
MIASSVKAEVVKSNARSANDTGSPEVQVALLTARINELTPHFKQHAKDHHGRRGLLRMVSRRRKLLDYLKSKDADRYTALIAKLGLRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A9BNB9
|
A7X1F5
|
PYRF_STAA1
|
OMP decarboxylase
|
Staphylococcus
|
MKDLPIIALDFESKEKVNQFLDLFDESLFVKVGMELFYQEGPQLINEIKERGHDVFLDLKLHDIPNTVGKAMEGLAKLNVDLVNVHAAGGVKMMSEAIKGLRKHNQHTKIIAVTQLTSTTEDMLRHEQNIQTSIEEAVLNYAKLANAAGLDGVVCSPLESRMLTEKLGTSFLKVTPGIRPKGASQDDQHRITTPEEARQLGSTHIVVGRPITQSDNPVESYHKIKESWLV
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
A7X1F5
|
A9HHY9
|
NRDR_GLUDA
|
Transcriptional repressor NrdR
|
Gluconacetobacter
|
MRCPFCGHEDTQVKDSRPHEDGAAIRRRRICAACSQRFTTIERVQLRDLYVVKADDRRVPFERDKLARSVRIALRKRPVDEERIERIVNGLVRQLEASGETDIPSRDIGKLVMGTLREVDIVAYIRFASVHWDFRETKDFAAILQSIPGTADGDVPVVPGDAAAAIAAESGPGGVKRR
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
A9HHY9
|
Q8DFD1
|
LIPA_VIBVU
|
Sulfur insertion protein LipA
|
Vibrio
|
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPDWMKIKLPADSQRIQDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPPEAEEPTKLAKTIADMKLKYVVITSVDRDDLRDGGAKHFADCNREIRAQSPHIRIETLVPDFRGRMDVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKEQHPDVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADMQAQGLEVK
|
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.
|
Q8DFD1
|
Q2N9C5
|
RS8_ERYLH
|
30S ribosomal protein S8
|
Erythrobacter
|
MAMTDPLGDMLTRIRNGQQAKKDSVLSPASKLRANVLEVLQREGYIRGYSEDASGKHAALRIELKYFEGEPAIKHVARVSKPGRRIYSGSKELPTVRNGLGITIVSTPKGVLSDNEARTQNVGGEVLAEVF
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
Q2N9C5
|
Q1IC14
|
IF3_PSEE4
|
Translation initiation factor IF-3
|
Pseudomonas
|
MTIKREMRNDKRTAPKAPINENISAREVRLIGADGEQIGIVSIDEALRIADEAKLDLVEISADAQPPVCKVMDYGKHLFEKKKQANEAKKNQKQIQIKEIKFRPGTEEGDYQVKLRNLVRFLSDGDKAKISLRFRGREMAHQELGMELLKRVETDLAEYGTVEQHPKMEGRQLMMVIAPKKKK
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
Q1IC14
|
B7JFI8
|
PPAX_BACC0
|
Pyrophosphatase PpaX
|
Bacillus cereus group
|
MKINTVLFDLDGTLINTNELIISSFLHTLHTYYPNQYKREDVLPFIGPSLHDTFSKIDESKVEELITSYRQFNHDHHDELVEEYETVYETVQELKKQGYKVGIVTTKARQTVEMGLKLSKLDEFFDVVVTIDDVEHVKPHPEPLQKALQLLGAKPEEALMVGDNHHDIVGGQNAGTKTAAVSWTLKGRAYLEAYKPDFMLDKMSDLLPILSDMNRS
|
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
|
B7JFI8
|
Q5E731
|
UREG_ALIF1
|
Urease accessory protein UreG
|
Aliivibrio
|
MQDYKQPLRIGVGGPVGSGKTALLEVLCKTLRDTYQIAVVTNDIYTQEDAKILTQAEALAADRIIGVETGGCPHTAIREDASMNLAAVEELAQRHKNLDVVFVESGGDNLSATFSPELADLTIYVIDVAEGEKIPRKGGPGITKSDLLIINKIDLAPYVGASLEVMESDTARMRPTRPYVFTNLKEGVGLDKIIEFIVDRGMLDAK
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q5E731
|
C3PL36
|
RS11_CORA7
|
30S ribosomal protein S11
|
Corynebacterium
|
MPPKTRSGARRGGRRVVKKNVAAGHAYIKSTFNNTIVSITDPHGAVISWASSGHVGFKGSRKSTPFAAQMAAENAARKAMDHGMKKVDVFVKGPGSGRETAIRSLQAAGLEVSSITDATPQPHNGCRPTKRRKV
|
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.
|
C3PL36
|
B4SRY7
|
G6PI_STRM5
|
Phosphohexose isomerase
|
Stenotrophomonas maltophilia group
|
MTTNNGFDSLHSHAQRLKGASIPSLLAAEPGRVQELALRVGPLYVSFARQTYDAAALQALLALAAERDVGAAITRLFRGEQVNLTEGRAALHTALRGDVVDAPVAAEAYATARDIRQRMGVLVRALEDSGVTDVVSVGIGGSDLGPRLVADALRPVTGARLRVHFVSNVDGAAMQRTLATLDPAKTAGILISKTFGTQETLLNGQILHDWLGGSERLYAVSANPERAAKAFAIAADRVLPMWDWVGGRYSLWSAVGFPIALAIGFERFEQLLEGAAQMDAHALDAPLERNLPVLHGLTDIWNRNLLGYATHAVMTYDQRLALLPAYLQQLVMESLGKRVQRDGQPVTTDTVPVWWGGAGTDVQHSFFQALHQGTSIIPADFIGCVHNDDPYTINHQALLANLLAQTEALANGQGSDDPHRDYPGGRPSTLILLDALTPQALGALIAMYEHAVYVQSVIWNINAFDQFGVELGKQLASGLLPALQGEDVAVADLMTREILAQLKR
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
B4SRY7
|
B5F5I0
|
GCST_SALA4
|
Glycine cleavage system T protein
|
Salmonella
|
MAQQTPLYEQHTLCGARMVDFHGWMMPLHYGSQLDEHHAVRTDAGMFDVSHMTIVDLHGSRTREFLRYLLANDVAKLTKTGKALYSGMLNASGGVIDDLIVYYFTEDFFRLVVNSATREKDLSWITQHAEPYAIDITVRDDLSLIAVQGPNAQEKAATLFTDQQRHAVEGMKPFFGVQAGDLFIATTGYTGEAGYEIAMPNEKAADFWRALVEAGVKPCGLGARDTLRLEAGMNLYGQEMDEGISPLAANMGWTIAWEPADRDFIGREALEMQREKGHEQLVGLVMTEKGVLRNELPVRFTDAQGNQQEGIITSGTFSPTLGYSIALARVPAGIGETAIVQIRNREMPVKVTKPVFVRNGKAVA
|
The glycine cleavage system catalyzes the degradation of glycine.
|
B5F5I0
|
Q9D529
|
WBP2L_MOUSE
|
WW domain-binding protein 2-like
|
Mus
|
MAVNQNHTVDRRWAAIPHGESLLKKCSEVDLSFPQSPPGSNLFSGTKRGALFLTSYRVIFVTSRADNDPMFSFTMPFHLMNNCTVEQPIFGANYIKGTIQAAPDGGWEGSATFKIVFRKGGAIDFAQLMAKAASAAAQGVPLRVASFWMGPLGIYVITGDRNMYAPQAYQVAYGAPPAGYGASPVGYGVPSAGYGAPPAGYGAPPVGYVAPSPGYDVLPPGYGAVRYGSPPPLYVATPMGYGVPPPGYGPPPVRYGSPPPGYEAPTMEYGAQPPRYGTTPMGSGSPPPRYEAPPMGYGTPPSGRESIPPGSRATSVAQEAPPAGSEAGHPMSVAVQNPEFQASFPSTSSSQVHSPRSKM
|
May play a role in meiotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization.
|
Q9D529
|
B8E2C8
|
HIS6_DICTD
|
ImGP synthase subunit HisF
|
Dictyoglomus
|
MLAKRIIPCLDTIGKKVVKGTSFINVRVVGDAKELARRYEKEGADEIVLLDITASEEGRSTFVDVVTDVASELFVPLTVGGGIKNIEDVRRLLKAGADKVSINTSAVENPDLINQIASEFGSQCLVVAIDVKRRGKKSWEVYIKGGKVPTGIDFKDWVIEVEKRGAGEILLTSIDADGHLSGYDYELLEYALSYSNLPLIASGGAGSLEDLYKALKIGVDAVLAASIFHFGTYSIPEVKRYLREKGIWVRLD
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
B8E2C8
|
Q7V4Q6
|
NDHJ_PROMM
|
NDH-1 subunit J
|
Prochlorococcus
|
MSETPSTPPVPAGPEPGPVSRWLNQQGFEHQLLDPDHLGVEVIGVESMFLQVIVAALKADGFDYLQCQGGYDEGPGQQLVCFYHLVAMAEMVAKMGVGDSSSEAAKVREVRLKVFLSREDIPSLPSIYGLFRGADWQERETFDMFGINFEGHPHPKRLLMPEDWKGWPLRKDYVQPDFYEMQDAY
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
|
Q7V4Q6
|
Q8X954
|
GLAH_ECO57
|
Glutarate 2-hydroxylase
|
Escherichia
|
MNALTAVQNNAVDSDQDYSGFTLIPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRFRVGKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLATAVAHLIGRSNFDAMSGQYYARFVVKNVDNSDSYLRQPHRVMELHNDGTYVEEITDYVLMMKIDEQNMQGGNSLLLHLDDWEHLDHYFRHPMARRPMRFAAPPSKNVSKDVFHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIEISKGILSVPVPVGKFLLINNLFWLHGRDRFTPHPDLRRELMRQRGYFAYATHHYQTHQ
|
Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG). Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
|
Q8X954
|
Q5X521
|
BAMB_LEGPA
|
Outer membrane protein assembly factor BamB
|
Legionella
|
MKIRILVLILCALTQGCTYVDDYMLGKDNTPQPKELKEIQPKVKMAQSWTTPVGKAHKTNEYLNIKPAIRGDVIYTADASGLVQAVNRKDGQIKWSTALKNNIVSGPTVAAGYVAVGTNASTLVLLNQSDGKEIWQNKVSAEVLAPPAISHQKVIAKTIDGKVYAIDAVNGKQLWVADHGAPSLVLKASSSPIIVDDLVLVGFSDGKLDALELQTGRLIWQRSIAYGTGASDVERLVDIDSDPIISNNVAYLATYQGYVGALSLSNGQFIWRKPASVYKNMLLSHNNLYFTDSNDVLWSLNSSTGQVNWKQTSLKARGLTAPALVGGNLAVGDKTGYLHILSTQTGELLGRSQLSGGVTVSPSVSGKNMYVLTNNGMLNQLSVS
|
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
|
Q5X521
|
P54023
|
RL13_METJA
|
50S ribosomal protein L13
|
Methanocaldococcus
|
MTVIDAEGAILGRLASEVAKRVLRGEEIVIVNAEMVVITGNKDWIIKTYQEEREKKNVANPRRFGPKFPRRPDDILRRTIRKMLPYKKPKGREAFKRVKVYVGNPKNLTVDEKISHKLNTTKYITLAELSKHLGAKF
|
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.
|
P54023
|
Q8R010
|
AIMP2_MOUSE
|
Protein JTV-1
|
Mus
|
MPMYQVKPYHGGSAPLHVELPTCMYRLPNVHSKTTSPATDAGHVQETSEPSLQALESRQDDILKRLYELKAAVDGLSKMIHTPDADLDVTNILQADEPTTLATNTLDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCERYRVLSTVHTHSSVKNVPENLVKCFGEQARKQSRHEYQLGFTLIWKNVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKHNAVTLTLIDSWVDIAMFQLREGSSKEKAAVFRSMNSALGRSPWLVGNELTVADVVLWSVLQQTGGSSGAAPTNVQRWLKSCENLAPFSTALQLLK
|
Required for assembly and stability of the aminoacyl-tRNA synthase complex . Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation . Blocks MDM2-mediated ubiquitination and degradation of p53/TP53 . Functions as a proapoptotic factor .
|
Q8R010
|
Q7MY02
|
SELA_PHOLL
|
Selenocysteinyl-tRNA(Sec) synthase
|
Photorhabdus
|
MTHKPCLLYSQLPAIDRLLREPQITPLVEQYGQTLVTATLRRMQEQARINIKQYQALPDWCDNWASALGQQLEQKQALALKPVFNLSGTVIHTNLGRALMAESAIEAVTQVMRSPVTLEYSLNNAERGHRDHALADLLCELTGAEDACIVNNNAAAVLLLLATVASGKQVVVSRGELVEIGGAFRIPDVMVQAGCRLVEVGTTNRTHLKDYRQAINEETALLMKVHTSNYNIDGFTAEVSGRELATLGIASQIPTAIDLGSGSMINMVQYGLPAEPMPQDYLNQGIDLVTFSGDKLLGGPQAGIILGKKHWIEAIQRHPLKRALRADKMTLAALEATLRLYQRPEQLCQQLPTLRLLTRSQQQMHDMAQRLLPQLQAHYGDQFIVRDEPCYSQIGSGSLPVDRLPSWALTFAAVEGQGSSLERLARCWRGLAKPVLGRISGGRLWLDLRCLEDEKALLQALLL
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
Q7MY02
|
Q02910
|
CPN_DROME
|
Calphotin
|
Sophophora
|
MEPGTIPSPVSAPVAAPVTPSAVAAPVQVVSPAAVAPAPAAPIAVTPVAPPPTLASVQPATVTIPAPAPIAAASVAPVASVAPPVVAAPTPPAASPVSTPPVAVAQIPVAVSAPVAPPVAATPTPVAPIPVAAPVIATPPVAASAPTPAAVTPVVSPVIATPPVVPANTTVPVAAPVAAVPAAVPVVAPVLAPAVAPAVAPVVAETPAPPPVAEIPVATIPECVAPLIPEVSVVATKPLAAAEPVVVAPPATETPVVAPAAASPHVSVAPAVETAVVAPVSASTEPPVAAATLTTAPETPALAPVVAESQVAANTVVATPPTPAPEPETIAPPVVAETPEVASVAVAETTPPVVPPVAAESIPAPVVATTPVPATLAVTDPDVTASAVPELPPVIAPSPVPSAVAETPVDLAPPVLPPVAAEPVPAVVAEETPETPAPASAPVTIAALDIPEVAPVIAAPSDAPAEAPSAAAPIVSTPPTTASVPETTAPPAAVPTEPIDVSVLSEAAIETPVAPPVEVTTEVAVADVAPPEAAADLIIEPVEPPAPIPDLLEQTTSVPAVEAAESTSSPIPETSLPPPNEAVASPEVAVAPITAPEPIPEPEPSLATPTEPIPVEAPVVIQEAVDAVEVPVTETSTSIPETTVEYPVAEKVLDPAITEAPVTTQEPDVANINDGAPATEITTPAVEIVTAAAEVSDTAIPLIDPPVPQEIAVAEIPETETKPAEVIVEQSTIPIEAPVPEVSKYAEPVISEAPAAEVPITAGDNPDNTSVGISEVVPTIAEKAVEEVPTSEIPEQSSSPSDSVPVAKITPLLRDLQTTDVSLLAIAATLDAIGEKLKDQKARNQQVMDRLCEIEKILGPPKSN
|
Plays important roles in both rhabdomere development and in photoreceptor cell survival. Might function as a calcium-sequestering 'sponge' to regulate the amount of free cytoplasmic calcium. It binds 0.3 mole of Ca(2+) per mole of protein.
|
Q02910
|
Q9K1Q9
|
MURA_NEIMB
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Neisseria
|
MDKLKISANGPLNGEITVSGAKNAALPLMCAGLLTSGTLRLKNVPMLADVKTTQKLLQGMGARVLTDNISEFEINGGTVNNTCAPYELVRTMRASILVLGPTLARFGEAQVSLPGGCAIGSRPVDQHLKGLEAMGAEIVIEHGYVKAKGKLKGTRVAMDVVTVGGTENLLMAATLAEGTTVLENCAIEPEVVDLAECLVKMGAKISGIGTSTMIVEGVDELQGCEHSVVPDRIEAGTFLCAVAITGGRVVLRNAAPKTMEVVLDKLVEAGAVIEAGDDWIAIDMRQRPKAVDIRTVVHPGFPTDMQAQFMALNAVAEGSCRVVETIFENRFMHVPELNRMGANITTEGNTAFVQGVEQLSGAVVKATDLRASASLVIAGLAARGETVVEQIYHLDRGYENIEKKLGSVGAKIERVSG
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q9K1Q9
|
Q54IM8
|
ACAD8_DICDI
|
Acyl-CoA dehydrogenase family member 8 homolog
|
Dictyostelium
|
MISGLFKLSNKQSVLQNATKLVLQRRTFFNIVPNPSVGLTEDQKQFQSMALDFAQEKMKPFAEKWDKEEYFPRDVMREAAELGFGGIYVREDVGGSGLSRLDASIIIEALASADVSTTAFISIHNMCAGLIDIYGTEEQRKKFLPSLVSMEKIASYCLTEPGSGSDAGSLSTKATKDGDHYILNGSKAFISGGGDSEVYLVMVRTGAEKGPKGISCLLVEKDTPGLSFGKKEEKLGWNTQPTRALIFEDCRVPVGNLIGKEGQGFSIAMNALNGGRINIGACSLGGAQSCLVAARDHVKVRKQFNQPLEHFQAVQFKMADMATKLHASRIMIRNAAAMLDAKDPSAHVYIAMAKLFACDECFKVTDDSLQLFGGYGYLKDYPVERYLRDLRVHRILEGSDAVMRLIISRELSKDDH
|
Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.
|
Q54IM8
|
Q5A8K2
|
SYA_CANAL
|
Alanyl-tRNA synthetase
|
Candida
|
MIKTLLRRMSSNTTIPTPNGSNHWTASKVRSTFLDYFKKQQHTYVPSSSVVPHNDPTLLFANAGMNQYKPIFLGTVDPASDFASLKRAANSQKCIRAGGKHNDLEDVGRDSYHHTFFEMLGNWSFGDYFKKEAIDYSWELLTKVYGLQEDRLYVTYFGGDEKQGLEPDLEAKNFWLKVGVPEDHILPGSVEDNFWEMGDQGPCGPCSEIHYDRIGGRNASALVNMDDPNVLEVWNVVFIQYNREADGNLRTLPNKHIDTGMGFERLVSILQNKYSNYDTDVFLPIFDKIREITGVRPYTGKFGNEDKDGIDTAYRVIADHVRTLTFAICDGGVPNNEGRGYVLRRILRRGSRYVRKYMNYPIGGFFQQLVDVVIEQNKEIFPEISSGAQDLKEILNEEELSFAKTLDRGEKLFEQYAIIASKTPEQTLSGKDVWRLYDTYGFPVDLTRLMAEEAGLKIDEEGFERAKEESREASKGSGTKDGKTLVKLDVHALSELDQNDAIPKTNDEFKYGLENVKAKVVGIYDGSKFVDSIEDPSIQYGILLDKTPFYAEQGGQEYDTGKLVIDGKSEFNVANVQVYAGYVLHTGNIVDGKLNVGDEIIATYDELRRWPIRNNHTGTHILNFALREVLGDGVDQKGSLVAPEKLRFDFSHKQAVTAKELEKIEAISNKYIKNNDKVYYKDVSLTKAKEINGLRAVFGETYPDPVRVVSIGVSVDDLLADPTNTKWHEISIEFCGGTHVAKTGDIKDLVIIEESGIAKGIRRIVAVTGHDAHHVQKVANEFEQEIDNASSLPFGVAKESKSKELGVALKKLSISVLDKQRLTEKFNKLDKSIKDNLKAKQKEETKKTLDVVNNWLNDKENASSFLVAHVPITANAKAITEAINLIKKQDKTKSIYLLTGETDKVAHGCYVSDEAIAKGINANELAKAVSENIGGKAGGKGNIVQGMGDKPQGINTAIEEVTKLFKEKL
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
|
Q5A8K2
|
Q6CZ45
|
FIEF_PECAS
|
Cation-efflux pump FieF
|
Pectobacterium
|
MNPHYARLVTLAAVSATAVALVLFVMKVFAWWHTGSVSLLASLVDSLVDIAASLVNLLVVRYSLQPADTEHAFGHGKAESLAALAQSMFISGSALFLILTGLQHSLEPQTLHAPEVGMWVTLIALVATLLLVSFQRWVVKHTHSQAVRADMLHYQSDLLMNGAILVALALSWKGITRADSLFALGIGVYILYSALRMGYDAVQSLLDRALPDEEHRAIAEVIVNWPGIRGAHALRTRRSGPTRFIQLHLEMDDALPLAEAHQIADDLEQALRKQFPGADIIIHQDPVSAVPENQRGRLTA
|
Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux.
|
Q6CZ45
|
Q0SVB6
|
PSTB_CLOPS
|
Phosphate-transporting ATPase
|
Clostridium
|
MSDKKTKIQVRDLDLFYASNHALKKINIDIKENEVTALIGPSGCGKSTFLRTLNRMNDLIPIVRIEGEIQVDGKDIYKDDDVIALRTKVGMVFQKPNLFPMSIYDNVAYGPRVHGIKDKKVLDKIVEESLRDAAIWDEVKNRLKSSALGLSGGQQQRICIARAIAMNPEIILMDEPTSALDPISTLKVEELIRKLEDKYTIVIVTHNMQQAARISDKTAFFLNGELVEFSDTNTIFTNPRDKRTEDYITGRFG
|
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
|
Q0SVB6
|
Q8FS36
|
IF1_COREF
|
Translation initiation factor IF-1
|
Corynebacterium
|
MAKEGAIEVEGRVVEPLPNAMFRVELDNGHKVLAHISGKMRQHYIRILPEDRVVVELSPYDLTRGRIVYRYK
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
Q8FS36
|
Q55694
|
MNMG_SYNY3
|
Glucose-inhibited division protein A
|
unclassified Synechocystis
|
MTLRSPVEFQDQFDVIVVGAGHAGCEAALATARLGCRTLLLTLNLDRIAWQPCNPAVGGPAKSQLTHEVDALGGEIGKMADRTYLQKRVLNISRGPAVWALRAQTDKREYAAVMKNIVENQPNLSIREGMVTDLVLGDNDEIQGVQTYFGACFGAQSVVITTGTFLGGKIWIGNKSMPAGRAGEFAAVGLTETLNELGFETGRLKTGTPARVDRRSVDYDKLEPQPPDEQVSWFSFDPEVWVEREQMNCYLTRTTAKTHQLIKDNLHLSPIYGGFIDSKGPRYCPSIEDKIVRFADKESHQIFIEPEGRDIPELYIQGFSTGLPENVQLAMLQTLPGLENCVMLRPAYAVEYDFLPATQCYPSLMTKKVAGLFCAGQINGTTGYEEAAAQGLVAGINAARHCQGKSLIIFSREGSYLGTLIDDLCTKDLREPYRMLTSRSEYRLILRSDNADQRLTPLGREIGLIDDRRWDLFQTKQANITAEKERLYSTRIKEQDAVGKEIVDYTQQKIKGSIVLAELLRRPGFHYPDLEKFQLGNEELKPEEKTSVEIEIKYSGYIKRQQTQIEQVSRHSQKRLPPGLNYMAIETLSMEAREKLTQFQPLTIGQAGRIGGVNPADINALLVYLETQLRRSVSP
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q55694
|
Q4UZF3
|
COQ7_XANC8
|
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
|
Xanthomonas
|
MTQIPPSRLHSPLDRLLVEAQRALDTVFGNPPAERPNPAGDTPDAALAPAQRQHAAGLMRINHVGEVCAQGLYFGQAAVARDDHTRQHLLTAAQEETDHLAWCADRLRELESRPSLFNPLWYAGSYALGAVAGLRGDDWSLGFVVETERQVEAHLDEHLETLPETDQRSRAILRVMKIDEARHADHAEQAGARILPPPIPSAMALASKLMKTIAYRF
|
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
|
Q4UZF3
|
Q3KMZ2
|
KGUA_CHLTA
|
GMP kinase
|
Chlamydia
|
MSVKVISPFSQDGVQCFPKLFIISAPAGAGKTTLTHMLQREFPDAFEKTVSSTTRSARPGEVHGVDYLFVSEDDFKQSLDREDFLEWVFLFGTYYGTSKAEISRVLQKGKHCIAVIDVQGALALKKQMPAVTIFIQAPSQEELERRLNARDSEKDFQKKERLEHSAVEIAAASEFDYVVVNDDLITAYQVLRSIFIAEEHRMSHG
|
Essential for recycling GMP and indirectly, cGMP.
|
Q3KMZ2
|
A7ZIW5
|
GCS2_ECO24
|
Gamma-glutamylcysteine synthetase 2
|
Escherichia
|
MPLPDFHVSEPFTLGIELEMQVVNPPGYDLSQDSSMLIDAVKNKITAGEVKHDITESMLELATDVCRDINQAAGQFSAMQKVVLQAAADHHLEICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCASGDDAIYLLHGLSRFVPHFIALSAASPYMQGTDTRFASSRPNIFSAFPDNGPMPWVSNWQQFEALFRCLSYTTMIDSIKDLHWDIRPSPHFGTVEVRVMDTPLTLSHAVNMAGLIQATAHWLLTERPFKHQEKDYLLYKFNRFQACRYGLEGVITDPHTGDRRPLTEDTLRLLEKIAPSAHKMGASSAIEALHRQVVSGLNEAQLMRDFVADGGSLIGLVKKHCEIWAGD
|
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
|
A7ZIW5
|
O80942
|
ZFP10_ARATH
|
Zinc finger protein 10
|
Arabidopsis
|
MEKPGGFWIPKKSNKESSWEELAFAEDDAAGSLWPPRSYTCSFCRREFKSAQALGGHMNVHRRDRARLKQADDQYLFPKSSSSPEYPSHKDSDNIHETSCYTLVFNTKPNYFKTQHSCVIDLSSSSSLPYLTPSRVSSGLPGKQHTSSSPPSFVVEPSKNSKYIPSSSPWSCPSTVVEQKSCDLYEIPAMEGEKKRKTESDVPKIGHKAKLSLGNTTDLSVSMNLVIHQSFPITAHGSDEEIGRVDIRKRRRRHESPSQQSIFISSLSCKSDIITRNEESKHKGDRFEDLDLELRLGTDPPKGI
|
Probable transcription factor that may regulate cell division and growth.
|
O80942
|
P19956
|
RM44_YEAST
|
YmL44
|
Saccharomyces
|
MITKYFSKVIVRFNPFGKEAKVARLVLAAIPPTQRNMGTQIQSEIISDYNKVKPLVKVTYKDKKEMEVDPSNMNFQELANHFDRHSKQLDLKHMLEMH
|
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
|
P19956
|
P0A9U1
|
YBHF_ECOLI
|
Probable multidrug ABC transporter ATP-binding protein YbhF
|
Escherichia
|
MNDAVITLNGLEKRFPGMDKPAVAPLDCTIHAGYVTGLVGPDGAGKTTLMRMLAGLLKPDSGSATVIGFDPIKNDGALHAVLGYMPQKFGLYEDLTVMENLNLYADLRSVTGEARKQTFARLLEFTSLGPFTGRLAGKLSGGMKQKLGLACTLVGEPKVLLLDEPGVGVDPISRRELWQMVHELAGEGMLILWSTSYLDEAEQCRDVLLMNEGELLYQGEPKALTQTMAGRSFLMTSPHEGNRKLLQRALKLPQVSDGMIQGKSVRLILKKEATPDDIRHADGMPEININETTPRFEDAFIDLLGGAGTSESPLGAILHTVEGTPGETVIEAKELTKKFGDFAATDHVNFAVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGQALVLGMDLKESSGKARQHLGYMAQKFSLYGNLTVEQNLRFFSGVYGLRGRAQNEKISRMSEAFGLKSIASHATDELPLGFKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVEKGVTVMVTTHFMDEAEYCDRIGLVYRGKLIASGTPDDLKAQSANDEQPDPTMEQAFIQLIHDWDKEHSNE
|
Part of the ABC transporter complex YbhFSR that could be involved in efflux of cefoperazone. Probably responsible for energy coupling to the transport system.
|
P0A9U1
|
Q8Z9I0
|
LEU1_SALTI
|
Alpha-isopropylmalate synthase
|
Salmonella
|
MSQQVIIFDTTLRDGEQALQASLSAKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARTIKNSRVCALARCVEKDIDVAAQALKVADAFRIHTFIATSPMHIATKLRSTLDEVIERAVYMVKRARNYTDDVEFSCEDAGRTPVDDLARVVEAAINAGARTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGIAVGNSLAAVHAGARQVEGAMNGIGERAGNCALEEVIMAIKVRKDIINVHTNINHHEIWRTSQTVSQICNMPIPANKAIVGSGAFAHSSGIHQDGVLKNRENYEIMTPESIGLNQIQLNLTSRSGRAAVKHRMEEMGYKDTDYNMGHLYDAFLKLADKKGQVFDYDLEALAFINKQQEEPEHFRLDYFSVQSGSSDIATASVKLACGEEIKAEAANGNGPVDAIYQAINRITGYDVELVKYDLNAKGQGKDALGQVDIVVNHHGRRFHGVGLATDIVESSAKAMVHVLNNIWRAAEVEKELQRKAQNKENNKETV
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
Q8Z9I0
|
A4FPT1
|
NUOK_SACEN
|
NDH-1 subunit K
|
Saccharopolyspora
|
MTPTYYLLLSALLFSIGAVGVLVRRNAIVVFMCVELMLNAVNLTLVTFARINGSVDGQVMAFFVMVVAAAEVVVGLAIIMSIFRTRRSASVDDANLLKY
|
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 a menaquinone. 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.
|
A4FPT1
|
Q62G12
|
CHEB1_BURMA
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
|
pseudomallei group
|
MQKKIKVLCVDDSALIRSLMTEIINSQPDMEVCATAPDPLVARELIKQHNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTERGSEITLRALELGAVDFVTKPRVGIRDGMLDYSEKLADKVRAASRARVRQNPQPHAAAAAAAHGHAGAAAPLINNPLVSTEKLIIVGASTGGTEAIREVLTPLPPDAPAVLIAQHMPPGFTRSFAQRLNGLCRISVKEAEHGERVLPGHAYIAPGHAHLLLARSGANYIAHLSDEPPVNRHRPSVDVLFRSAAQHAGKNALGVILTGMGRDGAAGLLEMKKAGAYTFAQDEASCVVFGMPREAIAMGGVDDVAPLSDMSRRIMARLASMGDRVQRV
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q62G12
|
C0PF72
|
ARGJ_MAIZE
|
Arginine biosynthesis bifunctional protein ArgJ beta chain
|
Zea
|
MSPPSVLLLHSRIPLQPRPFRMNSRAAPSRVVVCSVASTEGFISAAPILLPDGPWKQVEGGVTAAKGFKAAGIYSGLRAKGEKPDLALVACDVDATVAGAFTTNVVAAAPVLYCKHVLSTSKTGRAVLINAGQANAATGDLGYQDAVDSADAVAKLLNVSTDNILIQSTGVIGQRIKKEALLNSLPRLVGSLSSSVQGANSAAVAITTTDLVSKSIAVQTEIGGVAIRIGGMAKGSGMIHPNMATMLGVLTTDAQVSSDVWREMIRMSVSRSFNQITVDGDTSTNDCVIAMASGLSGLSGIQSLDSIEAQQFQACLDAVMQSLAKSIAWDGEGATCLIEVTVSGANNEAEAAKIARSVASSSLVKAAIFGRDPNWGRIACSVGYSGIQFDANRLDISLGVIPLMKNGQPLPFDRLTASKYLKDAGDAHGTVNIDISVGSGGGNGKAWGCDLSYKYVEINAEYTT
|
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
|
C0PF72
|
A8AVD7
|
CODY_STRGC
|
GTP-sensing transcriptional pleiotropic repressor CodY
|
Streptococcus
|
MAHLLEKTRKITSILKRSEEQLQEELPYNDITRQLAEIMDCNACIVNSKGRLLGYFMRYKTNNDRVEAFYQTKMFPDDYIRSANLIYDTEANLPVEHELSIFPVETQSDFPDGLTTIAPIHVSGIRLGSLIIWRNDEKFDNDDLVLVEISSTVVGIQLLNFQREEDEKNIRRRTAVTMAVNTLSYSELRAVSAILGELNGNEGHLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVLIPDVFEEIKKRDY
|
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.
|
A8AVD7
|
Q98C21
|
MUTS_RHILO
|
DNA mismatch repair protein MutS
|
Mesorhizobium
|
MNMHSPNEPDAPEVMTTPQPGTAAVTPMMEQFIEIKAANPDSLLFYRMGDFYELFFDDAEKASRALGIVLTKRGKHQGHDIPMCGVPVHAADDYLQKLIGQGFRVAVCEQIEDPAEAKKRGSKSVVRRDVVRLVTPGTITEDKLLAPSESSFLMALGRVKGGSDHSFAIAWIDISTGAFRVAETTADRLLADIFRVDPRELIVAEPVFHDPELRPVFDVLGRVANPQPPSLFDSASATGRIARFFDVATPDSFGTFSRAELSAISGAIAYVEKTQKAERPPLSRPEREEQGSTLFIDPATRGNLELLRTLSGSREGSLFKAIDRTVTGGGARLLADRLMAPLTDPAAIGARLDSVSFFRTETRLCQAVRASLKSVADMPRALSRLALNRGGPRDLGALRAGFEAAGAIVEIFAATALPQELAEAMAAIRALPQALAQHLIQALGEELPLLKRDGGFLRGGYHPELDEMRALRDESRKVIAGLERSLIEETGIRSLKIRHNNVLGYYIEVTANHHAIMTGSDGAKARFIHRQTMANAMRFTTTELAELETKIANAADRALGIELAAFEALTAQAVGEAEKIRAGADALAAIDVSAALALLSESEAWCRPVVDSSLAFEISGGRHPVVEQALRRSGEGPFVANDCDLSPEGNAKNGAIWLLTGPNMGGKSTFLRQNALIAILAQTGSFVPATSAHIGVVDRLFSRVGASDDLARGRSTFMVEMVETAAILNQAGERALVILDEIGRGTATFDGLSIAWAAVEYLHEKNRCRAIFATHFHEMTSLAGKLARLHNVTMRVKEWEGDVVFLHEVGKGAADRSYGVQVARLAGLPEAVVDRAKQVLHQLEEGEVSGKTNRLVDDLPLFSVAMKREAPKPVKSDALGAALGDINPDEMTPREALEALYRLKGLAGK
|
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.
|
Q98C21
|
O25502
|
COAE_HELPY
|
Dephosphocoenzyme A kinase
|
Helicobacter
|
MVLKNAIALTGGIGTGKSTTIKILESQGYKILDADKIAHQLLQEHRFKIAQHFGSDILEKDILNRKKLGAIVFQDAHELKWLEDFLHPLIREHMLKKAYELEKNHQAYFLDIPLFFEVGGKKCYPVSKVVLVYASRALQIERLLERDKLKEAEILQRLACQMDIEQKRAMSDYIIDNSSSLKDLNKQVERFLKTLL
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
O25502
|
A7IAS7
|
NADE_METB6
|
NH(3)-dependent NAD(+) synthetase
|
Methanoregula
|
MAQELGCRMGQVEQMIRYAYWNSKSQGIVVGVSGGVDSALAAAFCCRAIGPEKVLGLSLPASVSNPQDLSDAQELCAMLGMEHRVVLIDPMLAAFKTIPGFVETPYLLGNLMARIRMTVLYYHANRDHRLVCGTSNRSEAMLGYCTKYGDNAADFQPIVHLYKTDVYEMAKEVKIPKAILEKTPSAGLWAGQSDEGEIGLSYAEIDAALKNLEANGWKAGTPSEEKVLSRAQANAHKRLAAPNLLSVP
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
A7IAS7
|
Q8KGG6
|
DNAA_CHLTE
|
Chromosomal replication initiator protein DnaA
|
Chlorobaculum
|
MSDTIQQEAPDNLQVTPTHGRSFAEKVWSACLGLIQENINTLAFKTWFLPIRPLSFSGSELTIEVPSQFFYEWIEENYSVHVKQALRQVIGPEAKLMYSIVIDKSQGQPVTIELPHQIDAAPAERSVRPEAPGQKASAERERLEIARPRFESNLNPKYTFSTLVRGDCNSLAFAASKSIAQNPGQNAFNPLVIYGGVGLGKTHMMQAIGNSVLENRITDAVLYVSSEKFAIDFVNAIQNGNIQEFSAFYRNIDVLIIDDIQFFAGKEKTQEEIFHIFNTLHQSNKQIILSADRPIKEIKGIEDRLISRFNWGLSTDIQAPDYETRKAIIQSKLKQSGVSLDPVVIEFIATNVTSNVRELEGCIVKLLAAHSLDNQEIDLQFAKSTLKDIIRYNTKQLTLETIEKAVCSYFSITSNDLKGKSKKKEIAVGRQIAMYLSKDMTDSSLKTIGLHFGGRDHSTVIHALNTIEKKIAASNEERKKIEELRKRIEIMSM
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q8KGG6
|
Q6CZX7
|
RL16_PECAS
|
50S ribosomal protein L16
|
Pectobacterium
|
MLQPKRTKFRKVHKGRNRGLAQGTDVSFGTFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLEVRMGKGKGNVEYWVALIQPGKVLYEMDGVPEELAREAFQLAAAKLPIKTTFVTKTVM
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q6CZX7
|
B2XWP0
|
RPOC1_FAGEA
|
Plastid-encoded RNA polymerase subunit beta'
|
Fagopyrum
|
MIDQYKHQQLRIGLVSPQQISAWATKILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNFRIIGDETEEPKFCEQCAVEFVDSRIRRYQMGYIKLACPVTHVWYLKRLPSYIANFLDKPLKELEGLVYCDFAFARPIAKKPTFLRLRGLFEYEIQSWKYSIPLFFTTQGFDTFRNREISTGASTIREQLADLDLRTILDSSLSEWKEGPTGNEWEDRKVRRRKDFLVRRMELAKHFIRTNIEPEWMVLCLLPVLPPELRPIIQIDGGKLMSSDINELYRRVIYRNNTLTDLLTTSRSTPGELVMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQTFVIRGLIRQDLASNIGVAKSKIRENEPIVWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPTLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPTQDMLIGLYVLTSGNRRGICANRYNPWSRKNYKNEKWNDHNYKYMKEPFFCNSYDAIGAYRQKRINLDSPLWLRWQLDHRVVASREAPIEVHYESLGTYHEIYGNYLIVRSVKKEIIFIYIRTTVGHISFYREIEEAIQGFYRACSYGT
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B2XWP0
|
B5E8U7
|
PLSX_CITBB
|
Phosphate-acyl-ACP acyltransferase
|
Citrifermentans
|
MRVAVDVMGGDNAPHVEVEGAVAAAREFGVPVTLVGDAEKVRAELARYDCKGLDIEVWHASEVVGMHDSASDAVRKKKDSSIRIAFELVKGGEAVAVVSAGNSGATMAAGMFVLKRMKGIDRAAIAQLFPTVSGKTLVLDVGGNVDCKPIHLVQFAVMGEVYARFVMGVDNPKVGLLSNGEEASKGNELTRETSALLREKPINYIGYVEGRDIFNGSVDVVVCDGFVGNVALKLSEGLAEAVGKMLKAEIKSSFLSQIGYLLSRKAFNNFKKTVDYAEYGGAPLLGINGVGMICHGGSNPKAIKNAIRFAHEYALKGVNGRMAEKLNESFPGDAREREGAPAPDAGTERVAS
|
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
|
B5E8U7
|
A5E8F5
|
HSLU_BRASB
|
Unfoldase HslU
|
unclassified Bradyrhizobium
|
MTDFSPREIVSELDRYIVGQADAKRAVSIALRNRWRRLQLDAGLREEVLPKNILMIGPTGVGKTEIARRLAKLAGAPFLKVEATKFTEVGYVGRDVEQIIRDLVEVAIVQVRERKRKDVAARAQLAAEERVLDALVGANSSAATRDSFRRKLRAGELNDKEIEIETQSSGGGFPMFEIPGMPGAQMGAISIGDIFGKLGGRTKTRRVTVESSHDILIAEESDKLLDNDQLVQEAISVVENNGIVFLDEIDKICVRENRHGGDVSREGVQRDLLPLIEGTTVSTKHGAVKTDHILFIASGAFHIAKPSDLLPELQGRLPIRVELQALTRDDMRRILTEPEASLIKQYVALMKTEGVTLDITDDAIDALADIAVAVNSTVENIGARRLQTVMERVLDEISFTASDRSGETMRVDAAYVQQHIGDLAKNADLSRFIL
|
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
|
A5E8F5
|
Q8Y1H8
|
RISB_RALSO
|
6,7-dimethyl-8-ribityllumazine synthase
|
Ralstonia
|
MDHGFYPTNLEGEGLRIGIVQARFNEPVCEALREACVAELEQLGVAGEDVLLVTVPGALEVPLALQKMAESGQFDALIALGAVIRGETYHFELVSNESGAGITRVCLDFNIAIANGILTTDTDAQAHARTREKGRDCARTAIEMANLTAALDGLQDHGQDDENE
|
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.
|
Q8Y1H8
|
P01558
|
ELTB_CLOPF
|
Heat-labile enterotoxin B chain
|
Clostridium
|
MLSNNLNPMVFENAKEVFLISEDLKTPINITNSNSNLSDGLYVIDKGDGWILGEPSVVSSQILNPNETGTFSQSLTKSKEVSINVNFSVGFTSEFIQASVEYGFGITIGEQNTIERSVSTTAGPNEYVYYKVYATYRKYQAIRISHGNISDDGSIYKLTGIWLSKTSADSLGNIDQGSLIETGERCVLTVPSTDIEKEILDLAAATERLNLTDALNSNPAGNLYDWRSSNSYPWTQKLNLHLTITATGQKYRILASKIVDFNIYSNNFNNLVKLEQSLGDGVKDHYVDISLDAGQYVLVMKANSSYSGNYPYSILFQKF
|
This enterotoxin is responsible for many cases of a mild type of food poisoning.
|
P01558
|
A7ZCG7
|
APT_CAMC1
|
Adenine phosphoribosyltransferase
|
Campylobacter
|
MKILDQKGKEFLLNSIRCINDFPKPGIVFRDITTLLNNKEAFNFLIDHLAARYEDANIDYIAGIESRGFIFGAALAARLRLPFVPIRKPKKLPFITLSQKYSLEYGVDEVQIHIDAFGEKAGARVLLMDDLIATGGTAKASVELINQTNATCVEACFLIDLVDLKGSEKLKSLTKIYSVLEV
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
A7ZCG7
|
P33036
|
NRLA_ACISA
|
Nitrilase
|
Acinetobacter
|
VSYNSKFLAATVQAEPVVLDA
|
Acts on many kinds of nitrile compounds such as aliphatic, aromatic, and heterocyclic mononitriles or dinitriles. Prefers S-(-)-2-(4'-isobutylphenyl)-propionitrile to R-(+)-2-(4'-isobutylphenyl)-propionitrile as the substrate.
|
P33036
|
Q5RCR3
|
RL4_PONAB
|
60S ribosomal protein L4
|
Pongo
|
MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKARNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMINTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVDKAAAAAAALQAKSDEKAAVAGKKPVVGKKGKKAAVGVKKQKKPLVGKKAAATKKPAPEKKPAEKKPTTEEKKPAA
|
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
|
Q5RCR3
|
A0AJ38
|
ARGB_LISW6
|
NAG kinase
|
Listeria
|
MENIIVIKLGGTASDNLTENFFQKITEWQGAEKKIVLVHGGGHYITKMMEALQIPVETKNGLRITNQQALEVTKMVLIGQVQPTITSAFQKRGISVIGLNAGDTGLLEAERLNDRDLGLVGKITKVKTNLIEQLLAGNIITVIAPLGIDNTYNWLNVNADTAACEVASALKAEALYLLTDVPGVKNESEIISEINTTEINKLQTSGVIKGGMIPKLESAAFAAKHGVGQVIITDSLENAGTKIRSKVAIG
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
A0AJ38
|
Q9Y366
|
IFT52_HUMAN
|
Protein NGD5 homolog
|
Homo
|
MEKELRSTILFNAYKKEIFTTNNGYKSMQKKLRSNWKIQSLKDEITSEKLNGVKLWITAGPREKFTAAEFEILKKYLDTGGDVFVMLGEGGESRFDTNINFLLEEYGIMVNNDAVVRNVYHKYFHPKEALVSSGVLNREISRAAGKAVPGIIDEESSGNNAQALTFVYPFGATLSVMKPAVAVLSTGSVCFPLNRPILAFYHSKNQGGKLAVLGSCHMFSDQYLDKEENSKIMDVVFQWLTTGDIHLNQIDAEDPEISDYMMLPYTATLSKRNRECLQESDEIPRDFTTLFDLSIFQLDTTSFHSVIEAHEQLNVKHEPLQLIQPQFETPLPTLQPAVFPPSFRELPPPPLELFDLDETFSSEKARLAQITNKCTEEDLEFYVRKCGDILGVTSKLPKDQQDAKHILEHVFFQVVEFKKLNQEHDIDTSETAFQNNF
|
Involved in ciliogenesis as part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia . Required for the anterograde transport of IFT88 .
|
Q9Y366
|
E8N5I8
|
SECD_ANATU
|
Protein translocase subunit SecD
|
Anaerolinea
|
MKRYYFTLALIVLLLGLTIWFNVPGHPQIKIGNFERSMDLIQGLDLQGGVQVLLEADLPAETPIDPQALEDARTILENRTNALGVSENLFQVAGERRIVAEFPGLSDPEKVLAVIKETGLLEFVDLQDNPENLQEGNLILTDFGQTSTSTQPTETTTAPATEGQESLASTTVYHTIMTGKDLKSVVVSRNPNTGEVVIDFTLSDEGAKIFDEYTSNNIGKILAIVLDKKIISAPRVQGRIPSGQGQITGNFTLETANNLAIQMRYGALPIPFKVVESRVIGPTLGRDSLQKSLLAGYIGFTIVILFMGIYYRLPGVMADLSLIVYALITLTLFRFIPVTLTLPGIAGFLLSTGSALDANILIFERLKEELRAGRTFSQALDLAWKRALPSIRDSNIATLITVVILFIFGSQFGATIVKGFAFTLGVGIFVSLFCAMVVTRTFMYILVDRMKPQAKHLKWFGILD
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
|
E8N5I8
|
P19175
|
RPOB_PSEPU
|
Transcriptase subunit beta
|
Pseudomonas
|
MAYSYTEKKRIRKDFSKLPDVMDVPYLLAIQLDSYREFLQAGSIQGSLPRRRLHAAFKSVFPIISYSGNAALEYVGYRLGEPAFDVKECVLRGVTFAVPLRVKVRLIIFDKESSNKAIKDIKEQEVYMGEIPLMTENGTFVINGTERVIVSQMHRSPGVFFDHDRGKTHSSGKLLYSARIIPYRGSWLDFEFDPKDCVFVRIDRRRKLPASVLLRALGYSTEEVLNTFYTTNVFHISGEKLSLELVPQRLAGEVAVMDIHDETGKVIVEQGRRITARHINQLEKAGVKQLDVPMEYVLGRTTAKAIVHPATGEILAECNTEMTTELLIKVAKAQVVRIETLYTNDIDCGPFISDTLKIDTTSNQLEALVEIYRMMRPGEPPTKDAAETLFNNLFFSAERYDLSPLGRMKFNRRIGRTEIEGSGVLSKEDIVEVLKTLVDIRNGKGIVDDIDHLGNRRVRCVGEMAENQFRVGLVRVERAVKERLSMAESEGLMPQDLINAKPVAAAVKEFFGSSQLSQFMDQNNPLSEITHKRRCSALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLAAYARTNQYGFLESPYRVVKEGVVSDDIVFLSAIEEADHVIAQASAAMNDKKQLIDELVAVRHLNEFTVKAPEDVTLMDVSPKQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLRADKPLVGTGMERNVARDSGVCVVRRRGGVIDSVDASRIVVRVADDEVETGERRVDIYNLTKYTRSNQNTCINQRPLVSKGDKVQRGDIMADRASTDMGELALGQNMRIAFMAWNGFNFEDSICLSERVVQEDRFTTIHIQELTCVARDNKLGPREITSGIPNVGEAALNKLDEAGIVYVGAEVGAGDILVGKVTPKGHTQLTPEEKLLRAIFGEKASDVKDTSLRVPTGTQGTVIDVQVFTRDGVERDSRALAIEKMQLDEIPQDLNEEFRIVEGATFERLRSALNGQVVDGGAGLKKGTVITDEVLDGLDDGQWFKLRMAEDALNEQLEKAQQYIVDRRRLLDDKFEDKKRNVQQGDDLAPGVLKIVKVYLAIRRRIQPGDKMAGRHGNKGVVSVIMPVEDMPHDANGTPVDVVLNPLGVPSRMNVGQILETHLGLAAKGLGEKIDRMLEEQRKAAELRVFLTEVYNEIGGRQENLDEFTDEEILALANNLKKGVPMATPVFDGAKEREIKAMLKLADLPESGQMVLFDGRTRNKFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGDHRMEPGMAESFNVLIKEIRSLGIDIDLETE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
P19175
|
B5XTQ8
|
GLGX_KLEP3
|
Limit dextrin alpha-1,6-maltotetraose-hydrolase
|
Klebsiella
|
MTSLAAGKPAPLGASYDGKGVNFALFSAHAERVELCVFDEQGNEQRVDLPARSGDIWHGWLDAAGPGLRYGYRVHGPWDPAQGHRFNPAKLLLDPCAYRVEGDLPDDERLHGGMWEPDHRDSAAIAPKSQVVDLHYDWRGDKPPRTPWGETVIYEAHVKGLTLLHPQLPEAIRGTYKALGHPVMIAYFKSLGISALELLPVAQFASEPRLQRMGLSNYWGYNPLAWFALDPRYASDPARALDEFRDAVKALHAAGIEVILDIVLNHSAEIDLEGPTVSLRGIDNRSYYWVREDGDYHNWTGCGNTLNLSHPGVVEWARQCLRFWVDECHVDGFRFDLASVMGRTPEFRQDAPLFEAIRRDSVLSQVKLIAEPWDIGPGGYQVANFPPLFAEWNDHFRDISRRFWLQQNVSLGDFAQRFAASSDLFARDGKRPSATVNLVTAHDGFTLRDCVCFNQKHNEANGEENRDGTNNNYSNNHGIEGLDANLAVIERRRASVHALLTTLLLAQGTPMLLAGDEQGHSQHGNNNAYCQDNALTWLDWRQANPGLTAFTAALIHLRRRIPALTRNRWWQEGDGNVRWLNRNAQPLTAGEWQLGAACMQIQLSDRWLLTLNATAEVVDMVLPEGEWRAVPPFAGEDNPVIMAVWHGPAHGVCVFQRS
|
Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.
|
B5XTQ8
|
P10952
|
TETO_CAMJU
|
Tetracycline resistance protein TetO
|
Campylobacter
|
MKIINLGILAHVDAGKTTLTESLLYTSGAIAELGSVDEGTTRTDTMNLERQRGITIQTAVTSFQWEDVKVNIIDTPGHMDFLAEVYRSLSVLDGAVLLVSAKDGIQAQTRILFHALQIMKIPTIFFINKIDQEGIDLPMVYREMKAKLSSEIIVKQKVGQHPHINVTDNDDMEQWDAVIMGNDELLEKYMSGKPFKMSELEQEENRRFQNGTLFPVYHGSAKNNLGTRQLIEVIASKFYSSTPEGQSELCGQVFKIEYSEKRRRFVYVRIYSGTLHLRDVIRISEKEKIKITEMYVPTNGELYSSDTACSGDIVILPNDVLQLNSILGNEILLPQRKFIENPLPMIQTTIAVKKSEQREILLGALTEISDCDPLLKYYVDTTTHEIILSFLGNVQMEVICAILEEKYHVEAEIKEPTVIYMERPLRKAEYTIHIEVPPNPFWASVGLSIEPLPIGSGVQYESRVSLGYLNQSFQNAVMEGVLYGCEQGLYGWKVTDCKICFEYGLYYSPVSTPADFRLLSPIVLEQALKKAGTELLEPYLHFEIYAPQEYLSRAYHDAPRYCADIVSTQIKNDEVILKGEIPARCIQEYRNDLTYFTNGQGVCLTELKGYQPAIGKFICQPRRPNSRIDKVRHMFHKLA
|
Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.
|
P10952
|
P31398
|
HEMO_MANSE
|
Protein P4
|
Manduca
|
MVSKSIVALAACVAMCVAQPVEKMPVLKDQPAEVLFRESQATVLECVTENGDKDVKYSWQKDGKEFKWQEHNIAQRKDEGSLVFLKPEAKDEGQYRCFAESAAGVATSHIISFRRTYMVVPTTFKTVEKKPVEGSWLKLECSIPEGYPKPTIVWRKQLGEDESIADSILARRITQSPEGDLYFTSVEKEDVSESYKYVCAAKSPAIDGDVPLVGYTIKSLEKNTNQKNGELVPMYVSNDMIAKAGDVTMIYCMYGGVPMAYPNWFKDGKDVNGKPSDRITRHNRTSGKRLFIKETLLEDQGTFTCDVNNEVGKPQKHSVKLTVVSGPRFTKKPEKQVIAKQGQDFVIPCEVSALPAAPVSWTFNAKPISGSRVVASPSGLTIKGIQKSDKGYYGCQAHNEHGDAYAETLVIVA
|
Insect-immune protein with antimicrobial activity . Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.
|
P31398
|
A2RM26
|
FABZ_LACLM
|
Beta-hydroxyacyl-ACP dehydratase
|
Lactococcus cremoris subsp. cremoris
|
MTEVNINVTEIMEALPHRYPFLLVDRVIDIAEDEITAIKNVTINEEFFQGHFPQYPVMPGVLIMEALAQAAGVLELSKPENKGKLVFYAGMDNVKYKKQVTPGDKLVLHAKFIKRRGPIAVVEAEATVDGKLAAKGTLTFALGR
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
A2RM26
|
L8FLZ2
|
Y78_MYCSE
|
Uncharacterized protein D806_0078
|
Mycolicibacterium
|
MVTIQPDASEYGGQTVTGAAWPNIDESVLASAASDLEAVANHLRDNVVPSAGRQKMKLADSWEGKGADSALDEANAIIGEHEQNEVEAREAAAKLRRMEFAVAVAKTLANQTAEQVQNDCQRIMDEGQPSEGEDTRFERVATRIREGYDDNVRMVAEVSHQLAADLGIVPPEPWGHPGSPARTPQTPDQHPDGQLGTVDSGSSAPAPPPSLFAPPPPSRNADRPSQLGTEVAAKAEPTPSLETVQSGSPVPPDPLVGGEAPARSNPPFAQPHSDAPSTSGASTPPAVGPAPAPTTGSGTMRPQAPAQALPPGHLDSLSPATSNEISSNAVSPSAFGAKSGTPLEQFQKGLADAAKTGGSPQTLSTAPSQPLGAPPTTQPLGAAPPTAGPAAPPTTGGPPAPVAQAAGGPGGGAGPAPVAPPLSGGVPGGAVPLGPPPTPPPAAPVTTPPLASGAPVAPTGAAAGAAGGGGAQVAPIPVSAARAERDLAQRAVRRSGVDPMETARRIAAALNAPGMTNVEDFKFFWVTGLTADGKIVVANNYGIAYIPQQVHLPEQVYMASADESISPAERASWVNEPIVAVQRWAEHNGRVLRAVIATEDQLKNSDAGVHHEVLRPEDIPENGKMAGRDRLQVIAPDVSSQLAKIGDADLVSVLPPAPADSNPPEDRRKSLWDNVWKPLASRSAKRGERHLTAFVAYAAHAQEHALYAAHTAALPDEQRQAIREFIYWQHVGQLTADALAPA
|
May be involved in the ESX-1 / type VII specialized secretion system (T7SS), which exports several proteins including EsxA and EsxB (Probable). Involved in DNA conjugation in the recipient strain .
|
L8FLZ2
|
Q9ZVA0
|
LSH7_ARATH
|
Protein ORGAN BOUNDARY 7
|
Arabidopsis
|
MASHSNKGKGIAEGSSQPQSQPQPQPHQPQSPPNPPALSRYESQKRRDWNTFCQYLRNQQPPVHISQCGSNHILDFLQYLDQFGKTKVHIHGCVFFGQVEPAGQCNCPLKQAWGSLDALIGRLRAAFEENGGLPERNPFAGGGIRVFLREVRDSQAKARGVPYKKRKKRKKRNPMKSHDGEDGTTGTSSSSNLAS
|
Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light.
|
Q9ZVA0
|
Q7X7X4
|
C99A2_ORYSJ
|
Cytochrome P450 99A2
|
Oryza sativa
|
MQFFAKQNCQVNLLTNNPSSNPRFIMEINSAATLTLVSLLTLPILLALLTRKSSSKKRRPPGPWNLPLVGGLLHLLRSHPQVALRELASKYGPVMFLRMGQIDTVVVSSPAAAQEVLRDKDVMFASRPSLLVSEIFCYDNLDVGFAPYGAYWRMLRKLCTVELLSTKVVRQLAPVRNDETLTLVRNIKAASSGHGGGGGKKPVTLARLLTTCTNTITAKAAFGQACGVELQEQFLTALDVGLKFSGGFCFGDLFPSLRFIDAMTGLRSRLWRARGQLDSVFDKIIAQCEEHQGDSLVNVLLRIRDQGDLEFPFGTTNIKAIILDMFTGGTETTSSAAEWVMSELMRNPEVMAKVQAEVRRVFDNKSPQDHEGLIDNLRYMKMVIKETMRLNPVLPLLMPHLCRETCDIGGYEVVEGTRVVINSWAMARSPEYWDDAEEFKPERFEDGMADYKGSRFEYLPFGTGRRRCPGDTFGMVLLELIVARLLYYFDWSLPAGMQPDDVDMDFVVTATTRRKNHLQLVASPYKLAPIQI
|
Involved in momilactone phytoalexins biosynthesis. Participates in the biosynthetic steps between 9-beta-pimara-7,15-diene and 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide.
|
Q7X7X4
|
P51665
|
PSMD7_HUMAN
|
Proteasome subunit p40
|
Homo
|
MPELAVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLRDIKDTTVGTLSQRITNQVHGLKGLNSKLLDIRSYLEKVATGKLPINHQIIYQLQDVFNLLPDVSLQEFVKAFYLKTNDQMVVVYLASLIRSVVALHNLINNKIANRDAEKKEGQEKEESKKDRKEDKEKDKDKEKSDVKKEEKKEKK
|
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
|
P51665
|
A2SL48
|
NADK_METPP
|
ATP-dependent NAD kinase
|
Methylibium
|
MASRFRHAALVGKYQAPGSRQVLASVAEFLTNQGLEVSLDTTTAMAVGLPDYGALDAAQIGKHCDLAVVVGGDGTMLGTARQLARYGVPLIGINQGRLGFMTDIPMAEFRETIAPMIAGDYEEEHRTMLEGCVKRPSGDEFDVIYETFAVNDVVVSRGASAGMVELRVDVQDQFVANFRADGLIISSPTGSTAYALSAGGPILHPGISGWLMVPIAPHALSNRPIVLPDDSEVRIEIVAGRDASVNFDHQSLASLLHGDRICVRRSEHRVRVLHPRGWNFYATLRRKLHWNEGVLPDGAHS
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
A2SL48
|
C5D486
|
EFP_GEOSW
|
Elongation factor P
|
unclassified Geobacillus
|
MISVNDFRTGLTIEVDGDIWRVMDFQHVKPGKGAAFVRSKLRNLRTGAIQEKTFRAGEKVNRAQIDTRKMQYLYANGDQHVFMDMETYEQIELPAKQIEHELKFLKENMEVYIMMYQGETIGVELPNTVELKVVETEPGIKGDTASGGSKPAKLETGLVVQVPFFVNEGDTLIINTADGTYVSRA
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
C5D486
|
Q47GJ8
|
IHFB_DECAR
|
Integration host factor subunit beta
|
Dechloromonas
|
MTKSELIAQLAERFPQLVAKDADFAVKMILDAMSEALVRGDRIEIRGFGSFALNYRPPRVGRNPKSGEKVSVPAKWVPHFKAGKELRERVDQAI
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
Q47GJ8
|
C6E2F4
|
DCTA_GEOSM
|
C4-dicarboxylate transport protein
|
unclassified Geobacter
|
MKTKKFYQHLYFQVLTAISFGVALGYYLPDTGTAMKPLGDGFIKMIKMIITPIIFCTVVTGIAGMDDMKKVGRVGGKALLYFEAVSTLALGIGLVVINIIQPGVGMNADVTKLDTKGLDTYTATAAKGHSFVDFVLGVIPNSVVDAFAKGEILQVLFFAILFGLALSAMGEKGKPVYRLIDEVAHAFFGVVNIIMKFAPIGAFGAMAFTIGKFGLGSLTKLGMLMGSFYLTCLLFVFVVLGTIGKLCGFNIFKFISYIKEELLIVLGTSSSESALPRMMAKLENLGCSKSVVGLVIPTGYSFNLDGTSIYLTMAAVFVAQATNTPLDLTQTLTILGVLMLTSKGAAGVTGSGFVTLAATFAAIPTIPVAGLALILGIDRFMSEARALTNLVGNGVATVVVSRWENELDVARMSQVLNKELDEADGEADLLMMDPEPEEA
|
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane.
|
C6E2F4
|
Q9ABV2
|
GLMS_CAUVC
|
L-glutamine--D-fructose-6-phosphate amidotransferase
|
Caulobacter
|
MCGIIGIVGKEPVADRLIESLKRLEYRGYDSAGVAGVVGGKVERRRAQGKIKALEAVLADEPLTATTGIGHTRWATHGAPNVRNAHPHTAGRVTLVHNGIIENFAELKAELAGMGRTFESDTDTEVIAQLIDVALAKGLAPLDAFKATLDRLTGAYALAVLIQGEADLLLGARRGSPLVVGEGQGEMFLGSDALAVGPFTNRVIYLEEGDYVALDHDSRRIFDASGARVERPVRVVPTSSVMLEKGNYRHFMEKEIHDQPEGCQRTIAAYVDTLTSKAAVPGDIDFATLDRIQIVACGTSYIAGVIGKYLIEQLADLPVDVEIASEFRYRTPALRPGSLVVAMSQSGETADTLAALRYCKAKGMKSAVVVNAQESTMAREVDVVWPIHCGPEIGVASTKAFTAQVSVMIALAIAAAKARGTIDAAEEQRLVKVLLEAPRLIAEAIGLEDAIKEIAADVAKARDVLYLGRGPMSALALEGALKLKEISYIHAEGYAAGELKHGPIALVDDQTPIVILAPYDSYFEKSASNMSEVMARGGQVIFITDTEGVKHAPAGAKVVVTAPASDPLVSTLVMSAPIQLLAYHVAVVKGADVDQPRNLAKSVTVE
|
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
|
Q9ABV2
|
F8VQB6
|
MYO10_MOUSE
|
Unconventional myosin-10
|
Mus
|
MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLAELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEEYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQQTLDLGLQEKTSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQQGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVITAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQIPFKTALGRSADLLGLDPTQLTDALTQRSMILRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQVVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPDDIRGKCTVLLQVYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKKFLHLKKAAIVFQKQLRGQLARRVYRQLLAEKRELEEKKRREEEKKREEEERERERAQREADLLRAHQEAETRRQQELEALQKSQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGEELSELAESASGEKPNFNFSQPYPAEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASMQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTSKENGIDIILADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTPHTSIPPLEEVYSVQRLRARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGSVVRQKAEEEQMLDMWIKEEVCSARTSIIDKWKKLQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSVSSQGSSR
|
Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion.
|
F8VQB6
|
C3N509
|
FAU1_SULIA
|
RNA-binding protein FAU-1
|
Sulfolobus
|
MKGRVRIRGIYATALTSIFSSLSYEIVQQSVEIAERFMREVNNLPADITIKDFEYDRGKIIVMGNGTIEEDLHDVFKYSFHWKSPIKLYSVIEADESCTYGNFKVEPCLEEGIVIKPPYDGKIVLSETKAVSKYAMVWRGKGVTTFSEHINNEEERLRLLTLSSPLNRKGYNVKWRSNAKYATLNELKEDLERLVLRYENREFRDQGEDFYLITLSLPDKLHLDEVRKSIVNTVKYHHMLKLSYNREVDSLEKDKEGSPVKLLEALISDFMKIEHIKADGKAIYLRGGKVIEKEVNNDGYRITLRREINGNGVLDGIGKRIENGDYDIVEYNSDKWYQIHRYYSGIDNSLKGIYINISTPPELLKGKIRYLDLEIDIAIRDSEIIVLDEDELNKKSIYMHSSLVNKAKEVANYLIDCIQQNKLI
|
Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Binds to RNA in loop regions with AU-rich sequences.
|
C3N509
|
Q41407
|
RBLL_SYMSP
|
Uncharacterized ribulose bisphosphate carboxylase-like protein
|
Symbiodinium
|
LEQSSRYADLTLDEAGSLRNGEHVLVAYIMKPKMGYDYLATAAHFAAESCTGARSTDDAKESANAVVYYIDADSQEMRIAYPTVLFDSNLTDGRDMVRSFLTLAIGNTQGMEDVEFGKIYDFYLPPSFLRLQESPSVNTMWRILDKGASNGGLAAGAMKPKLGMQPKPFRAASYALWQGGAYTTADVQANQAPTQASEGIPEVVKAMRSCVQGTDVAKRHSGGNYTDEPKEMDARGKYVLSQFGPFSGNCVSLVAGYAAGGSARHTFPRQFVHYHRAGQASTSSPQTQRGYSAFVHTKISQVISTTSIHADTMSFGKTQGDSPDKSIAVMLQDDAADARLCNQEWEGMRQNAPIISGSMNALRLPAFFETLGNSNVILTADSGSFGHKDGPASGAIACRQVEEAWKAWRSGQYGNVSLSDGVVEFAKTHEEIKGAFLTFPKDADEIYPGWKEKLGCTAEASVPPASFVNAKISTASSAAVATARTTMNAAKMASQSTAGSAVNPYTGGLKSIHPASSSNTARTVLLSRQGREAALQD
|
Unknown. Probably does not have RuBisCO activity.
|
Q41407
|
Q7MSR3
|
LPXK_WOLSU
|
Lipid A 4'-kinase
|
Wolinella
|
MRFIERYFYRPSPVQKGVALALLPLSLLYCTIATTRRALSLKREFPATLISIGNLVVGGTGKTPFLIALAKEYEDRVAVVSRGYKRGSKGLLVVSHEGKILEETPKSGDEAMLIAQKLPKATVIVSEDRAKGINKAIELGKDIIFLDDGFRFPYNKLNILLRPLLEPHFKLCIPSGAYRERPSLYQSADILAKEGKEYRREVNISNPTPRMLLVTAIASPSRLERFLPEVVGKIAYKDHAFFDIKTLQKAMKEHEASSLLVTEKDEVKLKESGLPLSVMRLEFFIDEEIRAHVREFVASRSPKLS
|
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).
|
Q7MSR3
|
Q7VQV6
|
ATPB_BLOFL
|
F-ATPase subunit beta
|
Candidatus Blochmannia
|
MSIGKIIQVIGAVIDVEFQYNDIPNLYHALEVNIDNGNSHQVLILEVVQQLGRSIVRCIAMGSTNGLKRGLDVTNLKHGIQVPVGKETLGRVMDVLGNPIDMKGPINSIEKWSIHRSAPLYEELSSNQELLITGIKVIDLMCPFIKGGKIGLFGGAGVGKTVNIMELIRNIAIEHAGYSVFVGVGERIREGNDFYHEMIHSGILDKVALVYGQMNEPPGNRLRVALTGLTIAEKFRDEGHDVLLFIDNIYRYTLAGTEVSALLGRVPSAVGYQSTLSEEMGMLQERIASTKSGSITSVQAIYVPADDLTDPSPTTTFAHLDATIVLSRQIAALGIYPAVDPLDSYSKQLDPCIVGQEHYDIANNVKSILQRYQELKDIIAILGMDELSEEDKLIVLRSRKIQRFLSQPFFVAEVFTGFSGSYVSLEDTIAGFKEIIDGKYDHLPEQSFYMVGSVKEAIEKSKIL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q7VQV6
|
B8JB71
|
RL7_ANAD2
|
50S ribosomal protein L7/L12
|
Anaeromyxobacter
|
MADLNAIVEQLSGLTIMEAAELVKQLEEKWGVSAAAAPVMVAAGGGAAAAAPVEEKTEFTVVLVDAGANKINVIKEVRAITGLGLKEAKDLVEGAPKEVKAGVAKAESEELKKKLEAAGAKVEVK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
B8JB71
|
A1S6T3
|
GLO2_SHEAM
|
Glyoxalase II
|
Shewanella
|
MLDIRPIPAFADNYIWMIVLPDGGAVVVDPGDAMPVINTLQRLNLQLTAVLLTHHHRDHNGGINQLRDWAKSNGQSFTVYGAVTSDYSDVLCRDGDTVDISGLTSPVRVLSVPGHTLDHLAFVVDNALFCGDTLFSGGCGRLFEGDAGQLYDSLAKLASLPDDTLVYCAHEYTLSNLRFALAVEPQNQCLQDYVKQVNNLREANKPSLPSTLGTEKAINPFLRVDTATVHAAVAAQAGQKVPDEVTCLALLRRWKDNF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
A1S6T3
|
Q9RXX0
|
CRCB_DEIRA
|
Putative fluoride ion transporter CrcB
|
Deinococcus
|
MSFPLWLWLALGGAVGAVCRQAAVLLLAPLVARTGFPAAVLLINVLGSFLLGLTLALTGRGVWPEAVRMTFGTGVLGAFTTFSTFSTELDGLLLRGQGGLALAYAALSVGLGLTAAVAGRVLGARL
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
Q9RXX0
|
Q8XZV4
|
TRUB_RALSO
|
tRNA-uridine isomerase
|
Ralstonia
|
MTEQRPSQQAKQPRRDVHGVLLLDKPIGWSSNDALIRAKRLLWAKKAGHTGTLDPLATGLLPLCFGEATKFSQDLLEADKTYEAVVRLGIRTSTADAEGEVLSERPVAVTPEQLRAAIGRFVGEIDQVPPMHSALKKDGKPLYEYARAGQTVERAARRVTIRAIDVLATDLDAAAPTVTLRVCCSKGTYIRTLGEDLGEALGCGAHLVALRRTQVGSLTLDGAVTLEALEAASEDQRAALLAPVDALLQTLPRVELGAEDSRRFLHGQRLPLQLSLPSAEQVRVYGARGEAGASLLGVAAWQGGVLRPERLVHL
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q8XZV4
|
Q5FUK8
|
G6PD_GLUOX
|
Glucose-6-phosphate 1-dehydrogenase
|
Gluconobacter
|
MEHFQQVEPFDYVIFGATGDLTMRKLLPALYNRLRMGQIPDDACIIGAARTELDREAYVARARDALERFLPSDILGPGLVERFLARLDYVTLDSSREGPQWDALKSLLAKAQPDRVRVYYFATAPQLYGSICENLNRYELITPTSRVVLEKPIGTNMATATAINDGVGQYFPEKQIYRIDHYLGKETVQNVLALRFANPLMNAAWSGEHIESVQITAVETVGVEGRAAYYDTSGALRDMIQNHLLQVLCLVAMEAPDSLEADAVRNAKLAVLNALRPITDATAATETVRAQYTAGVVDGENVPGYLEELGKPSATETYAAIRAWVDTPRWKNVPFYIRTAKRSGKKVSEIVVTFRPAATTMFGATPASNRLVLRIQPNEGVDLRLNVKNPALDVFNLRTADLDTSIRMEGGLPFPDSYERLLLDAVRGDPVLFIRRDEVEAAWRWVEPILEAWKHDKAPMQTYSAGSYGPEQATQLLASHGDTWHEASE
|
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
|
Q5FUK8
|
Q48NZ3
|
RS6_PSE14
|
30S ribosomal protein S6
|
Pseudomonas
|
MRHYEIIFLVHPDQSEQVGGMVERYTKLIEEDGGKIHRLEDWGRRQLAYAINNVHKAHYVMLNVECTGKALAELEDNFRYNDAVIRNLVIRRDEAVTGQSEMLKAEENRSERRERRDRPEHSDSADGDDGDNSDVSDNADE
|
Binds together with S18 to 16S ribosomal RNA.
|
Q48NZ3
|
Q9A9W0
|
ISPG_CAUVC
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Caulobacter
|
MAADHTHVRPWRMITRRQSRKIRVGSVEVGGDAPISVQSMTNTLTSDAAATLEQIRQLEEAGADIVRVSCPDVESTAAFKTIAREAKVPLVADIHFHYKRGIEAAQAGAACLRINPGNIGSPDRVRDVIQAARDHGCSMRIGVNAGSLERELLEKYGEPCPDAMVESALNHARILQDHDFHEFKISVKASDPFMTVAAYYQLAEAIDCPLHLGVTEAGATRTGTVKSAIGIGAMLWAGIGDTIRVSLAADPVEEIKVGFDILKSLGLRHRGVNIIACPSCARQGFNVIKTVEALEERLAHISTPMSLSIIGCVVNGPGEALMTDIGFTGGGAGAGMVYMAGKPDHKQSNEGMIDHIVDLVEKKAAEIQAAKAQDEAAQTVAAE
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q9A9W0
|
Q8PXE6
|
AROE_METMA
|
Shikimate dehydrogenase (NADP(+))
|
Methanosarcina
|
MKQVFGVFGDPVGHSLSPAMHNAAFSALGMDCIYHAFRVTPEKLEKAILGAEAMGFGGINLTVPLKEKALKLDFVKPDPLAKRIGAVNTLVFGKKGDIQGYNTDGPGAKQALLDTGVEIRGSRMVVAGAGGAARAVAFQLAADGADITVINRTEERAVGLAREISAADLPGKIRGTGLSGLKELLRDADVLINTTTLGMHPNTDATIVTAEELHSGLTVFDIVYNPLETRLLREARTSGAKTISGVLMLVYQGAEAFRLWTGVEPPLELMKKTVLEALQA
|
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).
|
Q8PXE6
|
P14716
|
SPOR2_IPOBA
|
Clone PIM0535
|
Ipomoea
|
MKAFALFFVLSLYLLPNPTHSKFNPIRLRPAHETASSETPVLDINGDEVRAGENYYMVSAIWGAGGGGLRLVRLDSSSNECASDVIVSRSDFDNGDPITITPADPEATVVMPSTYQTFRFNIATNKLCVNNVNWGIKHDSESGQYFVKAGEFVSDNSNQFKIEVVNDNLNAYKISYCQFGTEKCFNVGRYYDPLTRATRLALSNIPFVFVIKPTDM
|
Major tuberous root protein.
|
P14716
|
A4IH17
|
BAG6_XENTR
|
HLA-B-associated transcript 3
|
Silurana
|
MEVTVKTLDSQTRTFTVDAEITVKEFKTHISSDVGISPEKQRLIYQGRVLQEDKKLKEYNVDGKVIHLVERAPPQTQPSTGGPSTSSSTSPSSSNAANVPGAGAPERNGNSYVMVGTFNLPHVMSGLGEASRGPRVSTVSGNDGSTLDVHINLDQQLPVQSEPRVRLVLAQQILQDIQRILDRLEGQPVNEQTAEPMDTAVSEGEASSRETLPQTTQNTDGQSNTAPTSHPSPSEYVEVLQSLSRVEERLAPFMQRYREILSSATSDAYENQEEREQSQRIINLVGESLRLLGNALVAVSDLRCNLSSASPRHLHVVRPMSHYTGPMLLQQAAIPIQINVGTTVTMTGNGTHAGQMPSDGNAAHTPTNTSEPQRSNSDNQPPSSGERPASEIPPTSVPHPHPRVVRITHQTVEPVMMMHMNIQDSGPGGPTNIPPPTAGHGGSAHIHMPGLPPEFMQAISHQITQQAVAAASGQQIPGFQAPPRFVFTRPAAPSFPPQPGVATTPPGPGGATTAVPGATVGPAGNASLAQMISGLVGQLLMHPVIVAQGGSNTPSSTSTPTSTSSSSSSSSSTVTTSTTTTSSTSFPTVSSGPSPQPPPGTDQHLSQLLGSLLGTAGSGMSNFAMGSPSITVTVPGMPAFLQGVTDILQATQTVPVSTSPPQSASQAPPPSSPSPPPAHSSPPPAAAPESLPPEFFTSVVQGVLSSMLGSLSAADQSGTESIAAFIQRLSGSHNIFQPDAEGPGGFFGDLLTLICHNFSLVDMVMLLHGHSQPLQNLQPQLRSFFLQEYLHQADPTPNNIQMASRNLTNGLEEYIRESFASVTVRDDVDITRTNLEFLQDQFNRITTHILHCADSTFGQRLLEMCNQSLFEWLALNLYCLRGDQSALTSVINERIRRLSLDVSPVLVSWVTSVLSLRLQVLLGQMPVTEGEIQRHIRRVGDVPQAPEASSQDQPMETTPVDCQNGAASPVPATTVEEVLFLPPQSSVPTICTDSEHPTQEDTGSEQWAASVPPEWVPVIRQDMQNQRKMKQQPPLSDAYLSGMPAKRRKTMQGEGPHLSLSEAVSRAMKATGAKPESSTDCVRRELDNSEAQGRYREQLCQDIQNILQDNESYSAQRFPNTQRAFRGDP
|
When nuclear, may also act as a component of some chromatin regulator complex.
|
A4IH17
|
A5DAD0
|
PAN2_PICGU
|
Poly(A)-nuclease deadenylation complex subunit 2
|
Meyerozyma
|
MEGWEEVSILAAILYSFPASKDPVTSLLFDSVHNLLWCGDSSGSARSFTPNAGYPFQLYPYTKFPATTSPLPVVQQRNHSRGILSLSQNCVNLNSRRGLSQATFTAASVTDSANVLRNLSCMTTLGTGNDIIVGGTHSLGSLDMQKCVATGFDHSGNLSFVDSVAKTLVLGTTDGTVELFDTASNSSVKSFPAHSGLLSDMAVQGNYIATCGYSARRRYDHKNSSAAGGTSYITDPLVHLIDTRMMKSLSPIPFPNGASFVRFHPKLPNIVIVASSTGVLEFVDIFDQSKLNVYQVNMSPASPGISRMEISDNGEYICCSEGRSLHLWSFTSDTNFVNFPAPLEEQDIPAPLPPPFEVDDPVPLSSVGMPYYKDYLLSNYATDMVFTKELSKVPAEVDTSLGHGAFVPYDRTAHGPRNISQPYQSLREPPGSNSNAPRFISERDGESNENMIHAENSIFHLKSPTSVPHCYSRLQIQYSKFGVDDFDFDYYNKSNGACSGLENHLDNSYTNALLQLYRAAPAFYNSVVESLLPEYLPNGPEIISWNPQGSSLLIELGYLFDMMHKAEGRNVKIANFSQLLTQSASAASAGVINTDEEKSLNADGLREIIIRFNHYLLSELTSNQRERRHTNSEKIEDIMGIKLEMQIKSQCTETETHTGSQLIFDLTSPPEQYLNKLAMLRRAEKTEITILSYMDYFMDQYKSASCRECEARGRPHAVNARQRVVRLPKVLSINLSMTNFELQQIHNCRGWLVPEFHIGEDERFVDAGRGRKYELLGYVCEISHGPGVKRGAHNLVSFVKIKGQWYLFNDFLVMPIAQEEALNLSYSWKKPVIIVYSEPGQDFSYFETSTFKKIQDLDTSIIYRDHFVRAAREGHRQEYKLLTKQEAPEIGTLIAIDAEFVVSEPEQLEIRYTGTRKLIKPKKLTLARVSVLRGNGPNIGVPFIDDYIVWTGHIEDYLTSFSGIEPGDLDPEVSKKALVTLQTVYRKLWLLLNMGCVFVGHGLQNDFRCINLVVPKTQVRDTADLFYLPEFKRKLSLKFLAYVLLKEKVQTGNHDSVEDAYTALMLFQKHEELTRTGDLETVLYQVYMEGQQRRFRAP
|
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
|
A5DAD0
|
P13691
|
IAA2_HORVU
|
Alpha-amylase inhibitor BDAI-1
|
Hordeum
|
MGAMWMKSMLLVLLLCMLMVTPMTGARSDNSGPWMWCDPEMGHKVSPLTRCRALVKLECVGNRVPEDVLRDCCQEVANISNEWCRCGDLGSMLRSVYAALGVGGGPEEVFPGCQKDVMKLLVAGVPALCNVPIPNEAAGTRGVCYWSASTDT
|
Could be involved in insect defense mechanisms. Inhibits insect-type alpha-amylase.
|
P13691
|
D2Y2C8
|
H17A3_CYRHA
|
Peptide F2-20.97
|
Haplopelma
|
MTTVGVSLFRRSPEKITMKIATFLGLSFLLIASYFLICEAQHPGFQELLILEENMRDPENSKERSCAKPRENCNRMNILCCRGECVCPTFGDCFCYGD
|
Inhibits with low potency Kv1.2/KCNA2 and Kv1.3/KCNA3 voltage-gated potassium channels.
|
D2Y2C8
|
Q2LR42
|
YQGF_SYNAS
|
Putative pre-16S rRNA nuclease
|
Syntrophus
|
MRILGLDYGEKRIGVALCDELGLTAQALTTVIRKSWRNDVGIIASLVRTYDVEKIVIGYPLRLDGTEGIQCEKVVRFARRLEAALGIPVIRWDETLTTKEAEEILSRSGVPPRKRRGVVDRLAASLILQSYLDAISQEKIPSDACDANES
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q2LR42
|
Q5AFI4
|
DFI1_CANAL
|
Defective in filamentous invasion protein 1
|
Candida
|
MEKLSINNNNNNRRYQSRRFDGITIIRIVVLVFIVTVSTYFVNSYTCNQPHHNHSTRPSHYLPINGTHGLMNNDDSLHNKGAIGHYNTTVSLERRADENNSTTNGLFPSTSSSTFIFTPSSSSSSTFQQSRSSPQTTSTSSFVATTSSFQQETSQTSIPDTTTDFSFSSFSEAPTTSTTSSTSEFSSTPQETSNTVTSTSSTSTSSSSSPTSSPATTSASQHVTTFSSVDNGKTIVVTRTSVISSSPTASNSNNNKNNDNGGGLSHTNRIVVGVVVGVGGSILIGLLAVLFYLRKRNNRDYEGGWTFWRKNEKLGSDEFFNGELGVRDRNINQGSNF
|
Cell-surface associated glycoprotein that acts as a plasma membrane receptor-type protein which senses the presence of matrix. Binds to calmodulin in response to environmental conditions and initiates a signaling cascade that activates CEK1, thus promoting invasive filamentation. Involved in the maintenance of the cell wall.
|
Q5AFI4
|
A8IMX7
|
QUEC_AZOC5
|
Queuosine biosynthesis protein QueC
|
Azorhizobium
|
MSADAGPGSGALVLFSGGQDSTTTLAWALDRFERVETLGFDYGQRHRIELDCRVKVRAAMAALNPAWAAKLGEDHTLALDALGAVSDTALTRDVAIEMTEGGLPNTFVPGRNIVFLTFAAALAYRRGLKHIVGGMCETDFSGYPDCRDDTIKALQVALNLGMDRRFVLETPLMWIDKAETWRLAERLGGRALVDLIVEDTHTCYLGERGPRHPWGHGCGTCPACQLRAEGFARYEAARVSE
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
A8IMX7
|
Q1BZ40
|
DTD_BURCA
|
Gly-tRNA(Ala) deacylase
|
Burkholderia cepacia complex
|
MIALIQRVTRADVRVGGRTTGEIGAGLLALVCAERGDTEAAADKLLAKLLGYRVFSDAAGKMNLPVSNIDGEGRAGGLLLVSQFTLAADTNSGLRPSFTPAAPPDEGARLFDYFVAAARARHPIVETGEFGADMQVSLVNDGPVTFWLQVRP
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q1BZ40
|
Q3ALB5
|
DDL_SYNSC
|
D-alanylalanine synthetase
|
unclassified Synechococcus
|
MPSSPITVGLVFGGRSGEHDVSIRSAATVVRGLRSGENTERYTVQPIYIDRDGRWWGTDLAEATLTSEVAPELTTPRPPSGFQGFPEGCDAIDLWYPVLHGPNGEDGTIQGLFQLTGKPFVGAGVLGSAVSMDKQAMKSAFSSAGLSQVPYVALHASELEDAKSRSALLDRIERELNYPCFVKPANLGSSVGISKVRSRQELEAGLEQAAALDPRLVVEQGVNAREVECAVLGRRTLEASVIGEVRFDADWYDYETKYTAGRSTTLIPAPLPDPVRDRIREQALQACAAVGVHGMSRVDFFYDETNDQLWINEINTLPGFTAQSMFPMLWAASGVTLEQLVHKLIQTAGE
|
Cell wall formation.
|
Q3ALB5
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.