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sequence
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2.75k
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5.51k
AlphaFoldDB
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B6YWA4
HIS1_THEON
ATP phosphoribosyltransferase
Thermococcus
MRFVLPKGRLFKGSLEILKKAGIELKPPETRELIVRNGRYELLLARAFDVPVYVEHGIDVGIAGSDVVEERGSDVLVPLELPFGKCRLSLAMPKESAVSVEEMDGFRIATKYPNLARKFFERNGVEVEVIKLHGSIELAPKIGVADAIVDIVETGNTLRANGLVEVEKIMDVSALLLVNRISQKTKFDEINELVLKIKEVVRDGF
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
B6YWA4
P51793
CLCN4_HUMAN
Chloride transporter ClC-4
Homo
MVNAGAMSGSGNLMDFLDEPFPDVGTYEDFHTIDWLREKSRDTDRHRKITSKSKESIWEFIKSLLDAWSGWVVMLLIGLLAGTLAGVIDLAVDWMTDLKEGVCLSAFWYSHEQCCWTSNETTFEDRDKCPLWQKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYINDPNMTRPVDDIPDRPAGVGVYTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFRNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFLDVKDEFTHRTLATDVMRPRRGEPPLSVLTQDSMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMANQDPESIMFN
Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons . The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons . The presence of conserved gating glutamate residues is typical for family members that function as antiporters .
P51793
B9DSX4
RS13_STRU0
30S ribosomal protein S13
Streptococcus
MARIAGVDIPNDKRVVISLTYVYGIGLATSKKILAAAGISEDVRVKDLTSDQEDAIRREIDSIKVEGDLRREVNLNIKRLMEIGSYRGIRHRRGLPVRGQNTKNNARTRKGKATAIAGKKK
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.
B9DSX4
A5FB63
CHIA_FLAJ1
Chitinase ChiA
Flavobacterium
MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAANSTNGLFVAAPRYIVPGCTNPQNPTGTWDGSGACEKSGSIEICDLVGNPVTNSHAYLDPNTMMVTPSAASAGWVRYFDNTTKVPYLYNSTLKQFISYEDKQSMDLKVQYIKSRNLAGGMIWELSQDTRGSIPNSLLNQVDTSFGSVVPGTVSISGSVKNGSALVTDVTVELRNASNAVIQTVVSANGNFAFNNLTSGQNYSLTALKATYTFTPVTLVNVTVNQTAVVINGTQPTYTVSGTVLDGSTPVSGVTVTAVSGSTTLTAVSNASGVYSIAGLTAGLNFTVTAAKSGFSYAPASTVYNAIDSNKTLNFTQGAPVVNYTVSGTVLNSTTPVSGVTVTASFTGGSYAAVTNASGTYSLSLPSGGNYTVTAALTGQTFTPASTVYSNLNANKTLNFTQDVVVSTSKISGTVKNGTNPVAGAKVELVLPWTDNTHNWKSVIATTDAQGKYSFDNSVVDGYTQVLSLKLNSWQNGEVAYYPNNLANFAVPANPTVYNFNTSSTAKSALAAAANLISGTVKNGTTPVAGAKVEIVLPWTDNTHNWKSVLATTDASGNYSFDNSVVAGYTQILSLKLNGWENGDVTYYPNNLANFAVPTTPTIYNFNRQAVVATKPVVTITAPTASAIAINLGSAINFVASVGLSAVDATTISSVVFSLDGQSLSTANSSGTYTAAWTPAANQFSLSHTLTVTATASNGTTDSKTYSFTLTCSGANCPNALPVITWNSPSNTTVYQNTFQVVPISVTAVDSDGTVSGVTITINGGTFNMTAGTNNTYTYNFTPSAYQDYPVVIKATDNKSGVTTLNNTIKIATVSTNRFIPLPSKIILGYAHSWENAGAPFLYFSQMVGSKFNVVDYSFVETVNRDGYTPILTTNDTRYLTNGVFNKQLLKNDIKSLRDSGVPVIVSIGGQNGHVVLDNVTQKNIFVNGLKAIIDEYQFDGVDIDFEGGSMNFNAGGLRDISYAGISAYPRLKNVVDAFKELKAYYGPGFLLTAAPETQYVQGGYTTYTDTFGSFLPIIQNLRNELDLLAVQLYNTGGENGLDGQYYGTAKKSNMVTALTDMVIKGYNIASTGMRFDGLPASKVLIALPACPSAAGSGYLTPTEGINAMHYLRTGTTFSGRTYTMQPGGPYPSLRGLMTWSVNWDASSCGNSSELSKAYAAYFASQTAAKTLVLDDISAKSNATIAYFKNNALSVTNENEDIAQVDVFNVLGQNLVSHRNVQNNKEVLLHNQSFSSKQLFLVVVTDKAGNKKSFKVMNFLN
Major extracellular chitinase, which is essential for chitin utilization.
A5FB63
Q10XP0
COBQ_TRIEI
Cobyric acid synthase
Trichodesmium
MKAIMVVGTTSHAGKSLITTAICRILSRRGWKVTPFKGQNMALNSYVTSTGGEMGHAQAVQAWAAGVTPAIEMNPILLKPQGDMTSQVIIKGKASGTVGAVDYYQQYFDIGWNAIQESLETLSQEFNMIVCEGAGSPAEINLKHRDLTNMRVAKHLNASTILVVDIDRGGAFAHIIGTLELLEPEERNLIKGIVINKFRGQRSLLDSGIHWLEKKTNIPVIGVIPWINEAFPAEDSLSILEQRYNKHTTDITIAIIRLPRISNFTDFEPLEAESSVKIKYIHPNDSLGDPDAIIIPGTKTTINDLLVLQKSGMAEAIKSYQSSGGIVMGICGGFQMLGEVLIDSQGLEGKQGEYKGLELLPLITTITPKKIASQRQVIANYPLGNLPVIGYEIHQGRTIVTKPDIVKPLFNDYDLGFVDSYDSIWGNYLHGIFDNGSWRRSWLNILRHKRGLNSLPTSISNYREQREIILDSIADKVNEHLDLKPVLT
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Q10XP0
P07281
RS19B_YEAST
YS16B
Saccharomyces
MAGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE
Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.
P07281
Q0HTS9
LPXK_SHESR
Lipid A 4'-kinase
Shewanella
MQVLVNKIWYEGHPLRWLLLPFSVLFALITAIRRSLFRLGLKSQTPLPVPVIVVGNITVGGSGKTPTVIYLIELLRQQGFNPGVISRGYGADIQGVKVVTAADSAASVGDEPAMIVARTGVPMVVGAKRVDTAKALLAQFAVDVIICDDGLQHYALGRDIELVVIDGKRGLGNRHLLPAGPLREGAWRLNQVDFVVVNGGPAQANQYEMQLSPSAVLPVNPKAVAVFDPTQPVVAMAGIGHPARFFETLTQQGFQLALSHGFDDHQAYDKEVLCELAASRPLMMTEKDAVKCRDFAQENWWYLAVDAKLSPQFDQQLLSRVRSVAAAKQGKSHGV
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).
Q0HTS9
Q8YJ37
ATPA_BRUME
F-ATPase subunit alpha
Brucella
MDIRAAEISAILKEQIKNFGKEAEVSEVGQVLSVGDGIARVYGLDNVQAGEMVEFPGGIRGMALNLESDNVGVVIFGADRDIKEGDVVKRTGAIVDVPVGPELLGRVVDALGNPIDGKGPIKAKERRRVDVKAPGIIPRKSVHEPMSTGLKAIDALIPVGRGQRELVIGDRQTGKTAIILDTFLNQKPIHDNGPDKDKLYCVYVAVGQKRSTVAQFVKVLEERGALEYSIVVAATASDPAPMQYLAPFAGCAMGEYFRDNGQHALIGYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDENGAGSLTALPVIETQGNDVSAFIPTNVISITDGQIFLETNLFYQGIRPAVNVGLSVSRVGSSAQIKAMKQVAGSIKGELAQYREMAAFAQFGSDLDAATQRLLNRGARLTELLKQPQFSPLKTEEQVAVIYAGVNGYLDKLAVNQVGKFEEGLLASLRTEHKDVLEGICNEKALTDDLKAKLKAAIDAFAKSFA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q8YJ37
Q2YBA4
RRF_NITMU
Ribosome-releasing factor
Nitrosospira
MIAEIKKSAEQKMQKSLEALKLDLGKIRTGRAHTGLLDHVTVDYYGNPTAINQVANISLADARTITVAPWEKKMLGAIEKAIRNSDLGLNPTTVGELIRVPMPPLTEERRRDLTKVVKHEGEAARVAMRNIRRDANAHLKDLLKEKKIAEDEERKGQEDIQKLTDRYIADIDKLLQAKEAELMAV
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Q2YBA4
Q5RE69
NEP_PONAB
Skin fibroblast elastase
Pongo
MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGEPLLKLLPDVYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYKKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.
Q5RE69
Q3K2B0
AROA_STRA1
5-enolpyruvylshikimate-3-phosphate synthase
Streptococcus
MKLLTNANTLKGTIRVPGDKSISHRAIIFGSISQGVTRIVDVLRGEDVLSTIEAFKQMGVLIEDDGEIITIYGKGFAGLTQPNNLLDMGNSGTSMRLIAGVLAGQEFEVTMVGDNSLSKRPMDRIALPLSKMGARISGVTNRDLPPLKLQGTKKLKPIFYHLPVASAQVKSALIFAALQTKGESLIVEKEQTRNHTEDMIRQFGGHLDIKDKEIRLNGGQSLVGQDIRVPGDISSAAFWIVAGLIIPNSHIILENVGINETRTGILDVVSKMGGKIKLSSVDNQVKSATLTVDYSHLQATHISGAMIPRLIDELPIIALLATQAQGTTVIADAQELKVKETDRIQVVVESLKQMGADITATADGMIIRGNTPLHAASLDCHGDHRIGMMIAIAALLVKEGEVDLSGEEAINTSYPNFLEHLEGLVNA
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Q3K2B0
B9L5I6
SUCC_NAUPA
Succinyl-CoA synthetase subunit beta
Nautilia
MNIHEYQAKEIFRKYGVPTPRGGVAFTGPEARRVAEELGGNLWVVKAQIHAGGRGKAGGVKLAKSLDEVEKIAEEMLGMTLVTHQTGPEGKVVKKVYIEEGADIKDELYLGMVLDRALEMPVMMASTEGGMEIEEVAEKTPEKIIKVAIDPAIGFQPFHARKLAFGLGLPKDEQREFIKFASALYNVYMDNDAEMIEINPLIKTGDGKFLALDAKMGFDDNALYKHPEIAEMRDLDEEEPTEVEAKKYGLSYIKLDGNVGCMVNGAGLAMATMDIIKHEGGEPANFLDVGGGANPDTVAKGFEIILSDPNVKSIFVNIFGGIVRCDRIANGILQATEKVEVNVPVIVRLDGTNAEEAAEILRNANIKNIIPAENLKDGAKKAVAAAKGEL
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
B9L5I6
Q5HNZ4
FUR_STAEQ
Ferric uptake regulation protein
Staphylococcus
MNTNDAIKVLKENGLKYTDKRKDMLDIFVKEDKYLNAKHIQQQMDKDYPGISFDTVYRNLHLFKDLGIIESTELDGEMKFRIACTNHHHHHFICENCGETKVIDFCPIEKIKSQLPNVNIHTHKLEVYGICEECQRKAN
Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
Q5HNZ4
B8FP45
GATC_DESHD
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Desulfitobacterium
MKISREEVEHVAFLARLELTEEELVTNTEQLNSILDYAAMLEKLNTDDIKPTAHAVPLHNVLREDQVKPSMAREKVLANAPDAQDGFFKVPRIV
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).
B8FP45
Q5HQR7
AROD_STAEQ
Type I dehydroquinase
Staphylococcus
MTHVDIAATIAPEDKLSKTLLKDIKVNEESIDIIELRIDQWPSFNKALLNEVIKQLKIFHLKILVTYRTSVQGGKGAVNEQEYLNILGELIECPQFDMIDIEWSSAVKIEKYTHLVQRAQQKGLEVVLSHHNFQETPALDELKFIYFKMQKLNPEYLKLAVMPKCQEDVLHLLEAMSLTAKHTTCRIVGISMSSLGKVSRIAQGVFGGTLSYGCIEEPQAPGQIHVSKLKSMVSFYED
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Q5HQR7
B1JAU1
FABA_PSEPW
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
Pseudomonas
MTKQHAFTREDLLRCSRGELFGPGNAQLPAPNMLMVDRITHISEEGGKYGKGELVAELDITPDLWFFACHFEGDPVMPGCLGLDAMWQLVGFFLGWQGLPGRGRALGSGEVKFFGQVLPTAKKVTYNIHIKRVLKGKLNMAIADGSVSVDGREIYTAEALRVGVFTSTDNF
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
B1JAU1
B7NPB4
LLDD_ECO7I
L-lactate dehydrogenase
Escherichia
MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALGPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQGLGKELPAALAPMAKGNAA
Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.
B7NPB4
A4IYC3
YBEY_FRATW
Endoribonuclease YbeY
Francisella
MDNLNINFINDDEHPIPSQDLLLKCLQLVADKHHISHAEVNLNIVSNDEIQQINKQFRNKDKPTNIISFKFEKPQGLPDDIANDFLGDIVIAPAVLENEAKEQNKELNDHWQHIFIHGLLHLLGYNHQDDQEAEVMENLEIQLLAQLGIANPYIEQENQNGR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A4IYC3
Q02I76
RIMO_PSEAB
Ribosome maturation factor RimO
Pseudomonas
MSTPTPKVGFVSLGCPKALVDSERILTQLRMEGYEVVPTYEDADVVVVNTCGFIDSAKAESLEVIGEAIAENGKVIVTGCMGVEEHTIRDVHPSVLAVTGPQQYEQVVTAVHEVVPPKTEHNPLVDLVPPQGVKLTPRHYAYLKISEGCNHSCSFCIIPSMRGKLVSRPVGDVLSEAERLVKAGVKELLVISQDTSAYGVDLKYKTDFWNGQPVKTRMKELCEALSSMGVWVRLHYVYPYPNVDDVIPLMAAGKLLPYLDIPFQHASPKVLKAMKRPAFEDKTLARIKQWREICPELTIRSTFIVGFPGETEEDFQYLLDWLTEAQLDRVGCFQYSPVEGAPANELGLEPVPDEVKQDRWERFMAHQQAISAARLQLKVGKEIEVLIDEVDEQGAVGRSWADAPEIDGNVFVDSDELKPGDKVRVRITDADEYDLWAELV
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
Q02I76
B1XHY7
ATPG_SYNP2
F-ATPase gamma subunit
unclassified Synechococcus
MPNLKGIRDRIQSVKNTKKITEAMRLVAAAKVRRAQEQVTSTRPFANTLLQVLYSLKSRLRLEEADLPLLKQREVKCVGLLVITGDRGLCGGYNANIIRKAERRAKELAAAGINYKFVLVGRKAVQYFQNRQAPVAKTYAGLEQIPSAAEASDIADELLSLFLSEEVDKIELIYTRFVSLISSQPVVQTLLPLVPEALTNPDDETFNLITRGGKFQVEREKVATEVKELPADMIFEQDPKDILNALLPLYLSNQLLRALQEGAASELAARMTAMNNASDNASDLMKTLTLSYNKARQAAITQELSEVVAGANAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
B1XHY7
Q9S0X4
TAL_METAM
Transaldolase
Methylomonas
MANLFDQLKEFTTIVADTGDVEAIKSVKPYDATTNPSLLLKASTLPQYAPLIDEAIAYAKSQSGDKAQQIEDAADKLAVLIGQEILKHIPGKISTEVDARLSFDTDAMVQKGRKLIKLYADAGISKDRVLIKLASTWEGIKAGEILEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKAKTGENYTSETDPGVLSVRKIYAYYKEHGYKTVVMGASFRNTGEITALAGCDRLTVSPNLLERAEGYRRYLPRVLVDNGATKQRPALLTEKEFRFDQNEDAMATEKLAEGIRGFVVDQNKLEKALAEKL
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q9S0X4
B7MZ04
NORR_ECO81
Anaerobic nitric oxide reductase transcription regulator NorR
Escherichia
MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSNEELRLIAALAAGALSNALLIEQLESQNMLPGDAASFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVDVRVLAATNRDLREEVLAGRFRADLFHRLSVFPLSVPPLRERGDDVILLAGYFCEQCRLRLGLSRVVLSAGARNLLQHYNFPGNVRELEHAIHRAVVLARATRSGDEVILEAQHFAFPEVTLPPPEVAAVPVVKQNLREATEAFQRETIRQALAQNHHNWAACARMLETDVANLHRLAKRLGLKD
Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54.
B7MZ04
Q9CR02
TMA16_MOUSE
Translation machinery-associated protein 16
Mus
MPKGLKGKMVGREKKVIHPYSRKAAQITRESHKQDKKERLKTEKALRLNLIGDKLQWFHSHLDMKKTRYSKKDACELVERYLDRFSSELEQIELQNSIKDRQGRRHHSREAVIKQTLERERQQYEGYGFEIPDILDSNTLQTFREWDFDLKKLPNIKMRKLCADDAVPKKRKQKNILNIEKDLGELELSGPTGATTDGKLEPASESSDTDEEMTPVPVSPH
Involved in the biogenesis of the 60S ribosomal subunit in the nucleus.
Q9CR02
A4TE25
DDL_MYCGI
D-alanylalanine synthetase
Mycolicibacterium
MNARIRVAVVYGGRSSEHAISCVSAGSILRNLDPDRFEVTAVGITPEGSWVLTEGRPETLAITDGKLPGVTGDSGTALTLTADPARRGQLVSLGEAAGEVLASADVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAAGMDKEFTKKLLASAGLPVGDHVVLRARDSTLSLQDRERLGLPVFVKPSRGGSSIGVSRVTAWDELPAAIELARRHDPKVIIEAAVPGRELECGVLEFPDGHLEASTLGEIRVEGVRGREDGFYDFETKYLDDGAELDVPAKVDDDVAEAIRALSLRAFTAIDCQGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMVETALARGTGLR
Cell wall formation.
A4TE25
Q9WYI1
AROE_THEMA
Shikimate dehydrogenase (NADP(+))
Thermotoga
MKFCIIGYPVRHSISPRLYNEYFKRAGMNHSYGMEEIPPESFDTEIRRILEEYDGFNATIPHKERVMRYVEPSEDAQRIKAVNCVFRGKGYNTDWVGVVKSLEGVEVKEPVVVVGAGGAARAVIYALLQMGVKDIWVVNRTIERAKALDFPVKIFSLDQLDEVVKKAKSLFNTTSVGMKGEELPVSDDSLKNLSLVYDVIYFDTPLVVKARKLGVKHIIKGNLMFYYQAMENLKIWGIYDEEVFKEVFGEVLK
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).
Q9WYI1
P81060
PEN3C_PENVA
Penaeidin-3c
Penaeus
MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPFVRPVPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYSG
Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin-binding activity.
P81060
Q2YY57
RECU_STAAB
Recombination protein U homolog
Staphylococcus
MNYPNGKPYRKNSAIDGGKKTAAFSNIEYGGRGMSLEKDIEHSNAFYLKSDIAVIHKKPTPVQIVNVNYPKRSKAVINEAYFRTPSTTDYNGVYQGYYIDFEAKETKNKTSFPLNNIHDHQVEHMKNAYQQKGIVFLMIRFKTLDEVYLLPYSKFEIFWKRYKDNIKKSITVDEIRKNGYHIPYQYQPRLDYLKAVDKLILDESEDRV
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
Q2YY57
B9MFY7
PURA_ACIET
IMP--aspartate ligase
Diaphorobacter
MKASKGRNVVVVGTQWGDEGKGKLVDWLTESAQGVVRFQGGHNAGHTLVINGVKTALHLIPSGIMRPGVKCYIGNGVVLSAGKLFEEIEGLEKAGVEVRSRLRVSEACPLILPFHAALDVAREAAREHGGAEKIGTTGRGIGPAYEDKIARRALRVQDLKYPERFAAKLRELLALHNHVLSTFLGSANFQFGDALKPYITGGQVQFEPVFDEAMRHAEMLKPMMADVSRELNEAHAAGANLLFEGAQGTLLDVDHGTYPYVTSSNCVAGNAAAGSGVGPGHLHYILGITKAYCTRVGGGPFPTELDWETPGTPGYHMSTVGAEKGVTTGRSRRCGWFDAALLKRSAQVNGLSGLCITKLDVLDGLRELSLCVGYELDGERIDLLPMGAEEIARCVPIYENIAGWTESTVGVTRYEDLPSNARRYLERIEQVTGVPIAMISTSPDRDHTILMRHPYAAD
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
B9MFY7
A0A3B1EFQ2
STR9_STRTC
Strobilurin A biosynthesis cluster protein r9
Strobilurus
MAVDRKIRIAVVGGGPGGVIAALALSKSPNVEIDLYEAATAFGDIGLSLGMPWRPWRILRLLGLQGYLAALLPPDQIPKEDVTVPTIHYRKSDQAVGEDIFTCTSLSGYTRFRRSHFHAALLPHLPSNCKTYTSKRLVSYAEPSNASDPIVITFADGTTAECDVLVGADGIKSPTRASMYNYAADEAEKAGRSAEANDLRSKIRAKFSGVEVYRSVISAEQLRAAAPDHHAFRCPTQFLGKEKVRMPTYPIQSENSQFLNCALYICDYSREGEDYPEPWVTDVEAKDLRSSLPDWEPEAQAAVSCMGEVVSRWAICTLSPLPFFQRSRVVLLGDAAVRVTTPFSTFSSDHCQTLACYDELPRCRLRPGDDAYILSEILTHPAVTRDNVQKALEIYSEVRVPMSTHVLESSRRTGMDCALHDEVAAADLKSLGERMQQEMVWAWEWNPEDEKKKALDLVEERLV
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 . Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A . The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore . Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the peroduction of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol . The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self-resistance gene is found within the cluster (Probable).
A0A3B1EFQ2
A4Y7I2
PYRD_SHEPC
Dihydroorotate oxidase
Shewanella
MFYKIAQKVMFQMDPERAHNLAIGSLKMTGNSPLNCFYRQTIAPAPVTFMGLTFPNPVGLAAGMDKDGESIDAFHAMGFGHIEVGTVTPRPQPGNDLPRLFRLKPAKGIINRMGFNNKGVDNLVRNLIAKKSDIMVGVNIGKNKDTPVEQGKDDYLICMDKVYPYAAYIAVNISSPNTPGLRSLQYGDLLDELLSAIKTKQLELAEKHKKYVPIALKIAPDLTIEEIENIADALIKNKFDGAIATNTTLTRDGVSGLANANESGGLSGKPLTELSTKVIRQLAACLKGQIPIIGVGGINSAEDALAKFDAGATMVQIYSGFIYQGPKLIKEIVEAYRLK
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
A4Y7I2
O14236
NOG2_SCHPO
Nucleolar GTP-binding protein 2
Schizosaccharomyces
MGTYKKEKSRIGREGANEKKPGNLRVKGENFYRNAKDVARVNMYRGGKAKYNAAGELVRAAEFQSSEVPKARIQPDRRWFNNTRVIAQPTLTQFREAMGQKLNDPYQVLLRRNKLPMSLLQENTEIPKVRVLESEPFENTFGPKSQRKRPKISFDSVAELAKESDEKQNAYEEKIEERILANPDESDDVMLAARDAIFSKGQSKRIWNELYKVIDSSDVLIQVLDARDPVGTRCGTVERYLRNEASHKHMILVLNKVDLVPTSVAAAWVKILAKEYPTIAFHASINNSFGKGSLIQILRQFASLHSDKKQISVGLIGFPNAGKSSIINTLRKKKVCNVAPIPGETKVWQYVALMKRIFLIDCPGIVPPSSNDSDAELLLKGVVRVENVSNPEAYIPTVLSRCKVKHLERTYEISGWNDSTEFLAKLAKKGGRLLKGGEPDEASVAKMVLNDFMRGKIPWFIGPKGLSSSNDEINSSQKVATQQTEGSDQDGEEAEEEWHGISDDGKADESESTKPVAEGSASESTDESAVDDNKNRS
GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation.
O14236
Q8UIQ2
LEPA_AGRFC
Ribosomal back-translocase LepA
Agrobacterium tumefaciens complex
MSTNSTRTPLDHIRNFSIVAHIDHGKSTLADRLIQSTGGLAERDMSEQVLDSMDIERERGITIKAQTVRLHYKANNGETYVLNLIDTPGHVDFAYEVSRSLSACEGSLLVVDASQGVEAQTLANVYQAIDNNHELVTVLNKIDLPAAEPERIKEQIEEVIGIDASDAVMISAKTGLGIPDVLEAIVNRLPPPKSDVGENGPLKALLVDSWYDTYLGVMVLVRVIDGVLTKGQQIRMMGSGAKYGVERVGVLTPKMVNVDSLGPGEIGFITASIKEVADTRVGDTITDDKRPTAQALPGFKPAQPVVFCGLFPVDAADFEDLRAAVGKLRLNDASFSFEMESSAALGFGFRCGFLGLLHLEIIQERLEREFNLDLVATAPSVVYEMTLTDGTEKELHNPADMPDVVKIKEIREPWIKATILTPDEYLGGILKLCQDRRGLQTELTYVGNRAMITYELPLNEVVFDFYDRLKSISKGYASFDYNIIDYREGDLVKMSILVNGDPVDALSMLVHRSAADRRGRGMCEKLKELIPPHMFQIPIQAAIGGKVIARETVRALRKDVTAKCYGGDATRKRKLLDKQKEGKKRMRQFGKVEIPQEAFIAALKMNDE
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q8UIQ2
P31743
GSPF_AERHY
General secretion pathway protein F
Aeromonas
MTEGDSARQVRQQLREQGLTPLEVNETTEKAKREANRFVLFRRGASTSELALITRQLATLVGAGLTIEEALRAVAEQCEKAHLRSLVATVRSKVVEGYSLADSLGAFPHVFDQLFRSMVAAGEKSGHLEKVLNRLADYTEQRQHMRTKLLQAMIYPIVLTLVAVGVISILLTAVVPKVVAQFEHMGQQLPATTRFLIGTSELMQHYGLWFLLLLFIGGFVWRWWLTDEKRRRHWHQVVLRLPVIGRVSRGLNTARFARTLSILNASAVPLLEGMKIAGEVLSNDFARTRIGEATERVREGTSLRKALDETKIFPPMMLHMIASGEQSGELDSMLERAADNQDREFETQVNIALGVFEPLLVVSMAGVVLFIVMSILQPILELNNMVNL
Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
P31743
Q68X16
NUOA_RICTY
NUO1
typhus group
MLQNSELLHEYLPIAIFFGIAVLVSGLIMMLPNLLSTKKYNKDKLEPYECGFAPFSDARSKFDIRFYLVAILFIIFDLEITFLVPWAISLNTIGKIGFFSMMFFLFVLIIGFIYEWTKGALDW
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.
Q68X16
Q8L4H4
NORK_MEDTR
Symbiosis receptor-like kinase
Medicago
MMELQVIRIFRLVVAFVLCLCIFIRSASSATKGFESIACCADSNYTDPKTTLTYTTDHIWFSDKRSCRQIPEILFSHRSNKNVRKFEIYEGKRCYNLPTVKDQVYLIRGIFPFDSLNSSFYVSIGVTELGELRSSRLEDLEIEGVFRATKDYIDFCLLKEDVNPFISQIELRPLPEEYLHGFGTSVLKLISRNNLGDTNDDIRFPDDQNDRIWKRKETSTPTSALPLSFNVSNVDLKDSVTPPLQVLQTALTHPERLEFVHDGLETDDYEYSVFLHFLELNGTVRAGQRVFDIYLNNEIKKEKFDVLAGGSKNSYTALNISANGSLNITLVKASGSEFGPLLNAYEILQARSWIEETNQKDLEVIQKMREELLLHNQENEALESWSGDPCMIFPWKGITCDDSTGSSIITKLDLSSNNLKGAIPSIVTKMTNLQILNLSHNQFDMLFPSFPPSSLLISLDLSYNDLSGWLPESIISLPHLKSLYFGCNPSMSDEDTTKLNSSLINTDYGRCKAKKPKFGQVFVIGAITSGSLLITLAVGILFFCRYRHKSITLEGFGKTYPMATNIIFSLPSKDDFFIKSVSVKPFTLEYIEQATEQYKTLIGEGGFGSVYRGTLDDGQEVAVKVRSSTSTQGTREFDNELNLLSAIQHENLVPLLGYCNEYDQQILVYPFMSNGSLLDRLYGEASKRKILDWPTRLSIALGAARGLAYLHTFPGRSVIHRDVKSSNILLDQSMCAKVADFGFSKYAPQEGDSYVSLEVRGTAGYLDPEYYKTQQLSEKSDVFSFGVVLLEIVSGREPLNIKRPRIEWSLVEWAKPYIRASKVDEIVDPGIKGGYHAEALWRVVEVALQCLEPYSTYRPCMVDIVRELEDALIIENNASEYMKSIDSLGGSNRYSIVMDKRALPSTTSTAESTITTQTLSHPQPR
Involved in the perception of symbiotic fungi and bacteria. Part of the perception/transduction system leading to nodulation or mycorrhizal infection . Phosphorylates PUB1 .
Q8L4H4
O86418
RBCX_NOSS1
RuBisCO chaperone RbcX
Nostoc
MNLKQIAKDTAKTLQSYLTYQALMTVLAQLGETNPPLALWLHTFSVGKVQDGEAYVKELFREQPDLALRIMTVREHIAEEVAEFLPEMVRSGIQQANMEQRRQHLERMTHLSLSNPSPESEQQTISDTDWDH
When rbcL-rbcX-rbcS or rbcL-rbcS were overexpressed in E.coli no change in reconstituted RuBisCO activity was observed, which suggests RbcX plays no role in RuBisCO assembly in this system . However in PubMed:8472962 E.coli chaperones groL and groS were also overexpressed, which may compensate for lack of rbcX (Probable).
O86418
C6E7U2
HEMH_GEOSM
Protoheme ferro-lyase
unclassified Geobacter
MSSKTALLLLQMGGPDSLDAVHPFLMKLFTDRDIIKIGPAFLQPFIARRIVNKRAPKVEEYYRQIGGKSPIRELTEAQGEGLQQLLGEDFRSFVAMRYSRPSTIDALAAIKRAGIERVIALSLYPHYSRATTGSSVNELKRVLNESGAKFEISYIDRFYNHPLYIKALSEKVVQGLAAFPDSKDVEIVFSAHSLPQSFIEEGDPYLDHIQETVRLVMEQVGEGSHTLCFQSKASRVKWLEPSTEATIEQMAKAGKKNLLMVPLSFVSDHIETLYEIDIQYGEEAKALGIERFIRTESLNSSPLFLECLADLVKTAAK
Catalyzes the ferrous insertion into protoporphyrin IX.
C6E7U2
A4VUJ6
RIMM_STRSY
Ribosome maturation factor RimM
Streptococcus
MNYFNVGKIVNTQGLQGEMRVLSVTDFAEERFKKGAKLALFDDKDQFAMEVEIASHRKAKNFDIIKFKGMYHINDIEKYKGFSLKIAEENLTDLEDGEFYYHEIIGLDVYENDILIGQIKEILQPGANDVWVVKRKGKKDLLLPYIPPVVLNIDIPNNRVDVELLEGLDDEN
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
A4VUJ6
P49513
PSBK_TRICV
Photosystem II reaction center protein K
Trieres
MESLLLARLPEAYVVFSPIVDVLPIIPVFFLLLAFVWQAAIGFR
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
P49513
B5CY73
BAGA_PHOPM
Glycosyl hydrolase 16 family protein A
Phocaeicola
MKRKLFTICLASLQFACAAENLNNKSYEWDIYPVPANAGDGMVWKLHPQSDDFNYIADEKDKGKEFYAKWTDFYHNHWTGPAPTIWQRDHVSVSDGFLKIRASRPEDVPLKKVVSGPNTKELPGTYTGCITSKTRVKYPVYVEAYAKLSNSTMASDVWMLSPDDTQEIDIIEAYGGDRDGGGYGADRLHLSHHIFIRQPFKDYQPKDSGSWYKDDKGTLWRDDFHRVGVFWKDPFTLEYYVDGELVRTISGKDIIDPNNYTGGTGLVKDMDIIINMEDQSWRAVKGLSPTDEELKNVEDHTFLVDWIRVYTLVPEE
Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
B5CY73
Q8D370
PYRD_WIGBR
Dihydroorotate oxidase
Wigglesworthia
MIYKIINFILSKKDHEEKKDLLLKIMKFFNKTPLNFLIKNKFPNNNISCMGLNFKNILGLAAGLDKNGDYIKLFSDIGFGFIELGTVTLKPQHGEKKPRLFCFPNVYGIINRMGFNNNGIENLIENIKNEKNVKSILGINIGKNKDTLIEKAKDDYLICINKAYYYSDYISINISSPNTKDLRKLQFGELFSDLLKSIKEEQNKLNKIYNKYVPILIKISPDINNSEIIQISDCLLSYNIDGVIATNTTVNKDIIMRCCNNCEKGGLSGAPLNENSTRIIKKLSKELKGKIPIIGSGGIISVKSAKEKIKAGASLIQIYSGLVFFGLKIIKKLIKSF
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Q8D370
A9ISM8
LPXA_BART1
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Bartonella
MSGTKIHPTALVEKGAQLGENVRVGPFCHISSEAVIGDECSLTSHVVIMGKTMLGAKSKVFSHAVLGADPQNNKHKGGATILSIGKNCMIREGVTMHRGSDSSTGMTVVGDNCQFFCYAHIAHDCHVGNHVTFANNAMIAGHVTVGDYVIIGGGAAVHQFVRVGHHAFIGGVSALVGDLIPYGTAVGVQAKLAGLNIIGMKRAGLERQDIHALRHAVAMLFDHSKPFKERVNDVASCYSSSRSVADVVRFIKEEGKRFYCTPKFGGDRIK
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A9ISM8
B0K754
GLPK_THEP3
Glycerokinase
Thermoanaerobacter
MAKYIMAFDQGTTSSRAIIFDRSGKIIASLNQEFKQIYPKAGWVEHDPMEIWGTQIGVAKGVIEKAGINPEDIAAIGITNQRETTVVWDKNTGKPIYNAIVWQCRRTAPICDELKNKGFDKKIREKTGLVVDAYFSGTKIKWILDNVEGAREKAEKGELLFGNIDTWLIWNLTRGKVHVTDYSNASRTMIFNIHELKWDKEILAELNIPEQMLPEVKPSSYVYGYTDKSIFGVEIPIAGDAGDQQAALFGQACFKPGMAKNTYGTGCFMLMNTGEKAVPSNTGLLTTIAWGIDGKVEYALEGSIFIAGAAIQWLRDELRIIDNSPQSEEYAMKVEDTNGVYVVPAFVGLGAPYWDMYARGTIVGLTRGAKREHIIRATLESIAYQTRDVLEAMQEDSGIRLQALKVDGGASANNFLMQFQSDILGVPVDRPQVIETTALGASYLAGLAVGFWNSREEIEKNWNVDKHFEPAMDNEKREKLYKGWKKAVERAMKWAEE
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
B0K754
Q59WU8
KAR5_CANAL
Karyogamy protein 5
Candida
MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEKNEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSIFNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMKVVDID
Required for nuclear membrane fusion during karyogamy.
Q59WU8
A9ADK9
RL18_BURM1
50S ribosomal protein L18
Burkholderia cepacia complex
MDKTQSRLRRARQTRIKIAELQVARLAVHRTNTHIYAQVFSPCGTKVLASASTLEAEVRAELADKSGKGGNVAAATLIGKRIAEKAKAAGIESVAFDRSGFRYHGRVKALAEAAREAGLKF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
A9ADK9
A3DHB8
Y2143_ACET2
Nucleoid-associated protein Cthe_2143
Acetivibrio
MAKGGFPGFGGNINNLVKQAQKMQRDMERVQEELKEKTVEASAGGGAVTVVATGRKDIKEITIKPEVVDPDDVEMLQDLILAAVNEALRKADEMVTAEISKITGGLGGIPGLF
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
A3DHB8
Q12N25
RNFE_SHEDO
Rnf electron transport complex subunit E
Shewanella
MSQYQEIAKQGLWHNNPGLVQLLGLCPLLAVTATVTNALGLGFATLLVLVGSNMLVSLVRDYVPKEIRIPVFVMIIAALVTSVQLLINAYAYGLYLSLGIFLPLIVTNCVIIGRAEAFASRNNLAHSAFDGLMMGIGFTCVLVVLGAGRELLGQGTLFEGADLLLGDWAKALVMQVWQVDTPFLLALLPPGAFIGMGLLIAGKNVIDARLKARQPKTQAEPVARVRITKVS
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Q12N25
Q0AGI1
ISPF_NITEC
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Nitrosomonas
MKKIRIGQGFDIHQLAAGRELVIGGVTIPYEKGLLGHSDADVLLHALCDALLGAAALGDIGKHFSDTDARYKDIDSRKLVCKVHRLLAETGYRVVNIDATIIAQAPKMAPHISGMIANIAQDLAMPAGNINIKAKTAEKLGAVGRGEGIVAEVVCLIANSDEGEAQP
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q0AGI1
Q9QZH6
ECSIT_MOUSE
Protein SITPEC
Mus
MSWVQVNLLVRSLSRGWGGLCRPALSGTPFAQVSLQALRGLHCSAATHKDEPWLVPRPPEPQRKPIKVPAMHEDLFKPSGNRERDKASFLNAVRSFGAHNVRKRGHVDFIYLALRKMPEFGVERDLSVYNLLLDVFPKEVFRPRNVIQRIFVHYPRQQECGVAVLEQMERHGVMPSAETEFLLIQIFGRKSYPMLKFLRMKLWFTRFKNINPYPVPRDLPQDPLDLAKLGLRHMEPDLSAKVTVYQMSLPSDSTGMEDPTQPHIVGIQSPDQQAALARHNPSRPVFVEGPFPLWLRNKCVYYHILRADLPPPEEEKVEEIPEEWELYYPQKLDLEYSRSGWDDYEFDVDEVTEGPVFAMCMAGAHDQATLIKWIQGLQETNPTLAQIPVVFRLARSTGELLTTSRLEGQSPPHSPPKGPEEDDETIQAEQQQGQS
As part of the MCIA complex, involved in the assembly of the mitochondrial complex I.
Q9QZH6
Q39QM7
HEM3_GEOMG
Pre-uroporphyrinogen synthase
Geobacter
MAPKQLRIGTRASQLALWQANWVKGELEKRYPGMAVELVKIKTMGDKILDVPLAQVGGKGLFVKEIEEAMLRGEIDIAVHSMKDVPTEFPEGLGLYCITEREDPRDAVISRGVKFADLPQGARIGTSALRRQAQILKVRPDLQMVVIRGNVETRIRKLTDENLDAVILAAAGLNRLGFADQVSEYLPVELSLPAIGQGALGIECRLDDETIKDTIAFFNHPDTAHAVRAERALLWRCEGGCQVPIAAHGQVSGDTLTLTGFVASVDGTRSVKDTISGPVTECEKLGIALAEKLLADGAHEILAEVYQREVAREKEIPV
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Q39QM7
Q9JZQ2
METE_NEIMB
Methionine synthase, vitamin-B12 independent isozyme
Neisseria
MTTLHFSGFPRVGAFRELKFAQEKYWRKEISEQELLAVAKDLREKNWKHQVAANADFVAVGDFTFYDHILDLQVATGAIPARFGFDSQNLSLEQFFQLARGNKDQFAIEMTKWFDTNYHYLVPEFHADTEFKANAKHYVQQLQEAQALGLKAKPTVVGPLTFLWVGKEKGAVEFDRLSLLPKLLPVYVEILTALVEAGAEWIQIDEPALAVDLPKEWVEAYKDVYATLSKVSAKILLSTYFGSVAEHAALLKALPVDGLHIDLVRAPEQLDAFADYDKVLSAGVIDGRNIWRANLNKVLETVEPLQAKLGDRLWISSSCSLLHTPFDLSVEEKLKANKPDLYSWLAFTLQKTQELRVLKAALNEGRDSVAEELAASQAAADSRANSSEIHRADVAKRLADLPANADQRKSPFADRIKAQQAWLNLPLLPTTNIGSFPQTTEIRQARSAFKKGELSAADYEAAMKKEIALVVEEQEKLDLDVLVHGEAERNDMVEYFGELLSGFAFTQYGWVQSYGSRCVKPPIIFGDVSRPEAMTVAWSTYAQSLTKRPMKGMLTGPVTILQWSFVRNDIPRSTVCKQIALALNDEVLDLEKAGIKVIQIDEPAIREGLPLKRADWDAYLNWAGESFRLSSAGCEDSTQIHTHMCYSEFNDILPAIAAMDADVITIETSRSDMELLTAFGEFQYPNDIGPGVYDIHSPRVPTEAEVEHLLRKAIEVVPVERLWVNPDCGLKTRGWKETLEQLQVMMNVTRKLRAELAK
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Q9JZQ2
Q3K107
KUP_STRA1
Probable potassium transport system protein kup
Streptococcus
MQHVNHSSFDKASKAGFIIALGIVYGDIGTSPLYTMQSLVENQGGISSVTESFILGSISLIIWTLTLITTIKYVLVALKADNHHEGGIFSLYTLVRKMTPWLIVPAVIGGATLLSDGALTPAVTVTSAVEGLKVVPSLQHIFQNQSNVIFATLFILLLLFAIQRFGTGVIGKLFGPIMFIWFAFLGISGFLNSFAHPEVFKAINPYYGLKLLFSPENHKGIFILGSIFLATTGAEALYSDLGHVGRGNIHVSWPFVKVAIILSYCGQGAWILANKNAGNELNPFFASIPSQFTMHVVILATLAAIIASQALISGSFTLVSEAMRLKIFPQFRSTYPGDNIGQTYIPVINWFLFAITTSIVLLFKTSAHMEAAYGLAITITMLMTTILLSFFLIQKGVKRGLVLLMMIFFGILEGIFFLASAVKFMHGGYVVVIIAVAIIFIMTIWYKGSKIVSRYVKLLDLKDYIGQLDKLRHDHRYPIYHTNVVYLTNRMEGDMIDKSIMYSILDKRPKKAQVYWFVNIKVTDEPYTAEYKVDMMGTDFIVKVELYLGFKMRQTVSRYLRTIVEELLESGRLPKQGKTYSVRPDSKVGDFRFIVLDERFSSSQNLKPGERFVMLMKSSIKHWTATPIRWFGLQFSEVTTEVVPLIFTANRGLPIKEKIELTTTGD
Transport of potassium into the cell.
Q3K107
Q6Q2J0
AOFA_PIG
Monoamine oxidase type A
Sus
MERQEKANNAGHMVDVVVIGGGISGLSAAKLLNEYGINVLVLEARDRVGGRTYTVRNENVDYVDVGGAYVGPTQNRILRLSKELGLETYKVNVNECLVQYVKGKSYPFRGAFPPVWNPIAYLDYNNLWRTMDDMGKKIPADAPWESPHAEEWDKMTMKDLIDKICWTKTAKRFASLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMHLLGDRVKLRCPVTYVDQSGDNIIVETLNHELYECQYVISAIPPTLTAKIHFRPELPSERNQLIQRLPMGAIIKCMMYYKEAFWKKKNYCGCMIIEDEEAPISITLDDTKPDGSLPAIMGFILARKADRLAKVHKEVRKRKICELYAKVLGSQEASHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATQWSGYMEGAVEAGERAAREILNALGKVSKKDIWLREPESEDVPAFEITRTFWERNLPSVTGLLKIIGFSTSVTALWLAVYKFRLLTRS
Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline.
Q6Q2J0
A5UKU8
RL10_METS3
Acidic ribosomal protein P0 homolog
Methanobrevibacter
MAHVAEWKKEEVNELKSLIDKYDVIGIVDLLNIPAKQLQEMRKSLHNKAVIRMSKKNLIDLALEDCNASKNNIVDLSEHMEGQVAVIATEMNPFKLYKILEDSKTSAPAKPGAIATDDIVIPEGDTGFEPGPFLGELQQVGIPAKIDKGKIVVSKETVLVEAGEEVSAAVASTLSRMDINPMEVGIDLRAVYEEEAIYTSEVLAIDEEQTLADVQNAFRNAFNLSVNAAIPTEETISTIITLAYTRAINVGVDAAIMTSETSEPIIGLAQAKMLALASEVSGTEGALDDELAEKLSNVAVAAAPVVEETVEEEEEEEEEEDAEEEAAAGLGALFG
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
A5UKU8
Q93ZS1
LPAH2_ARATH
Protein LOW PHYTIC ACID 1 homolog 2
Arabidopsis
MMTEATKVLYIVVREEGDDDDNNGDDSFRYTRPVLQSTLQLMGCKARHAFKISRRVFELIRSEGSCNTSPENGKEPEFAKEVGGSTCVEKLNCLVVAGDVDKNKSKPFEMYKRRTTVVVSREIFVDVVCDALAEYKYVGRDQRADLILACRIRERKESVTVLLCGTSGCGKSTLSALLGSRLGITTVVSTDSIRHMMRSFADEKQNPLLWASTYHAGEYLDPVAVAESKAKRKAKKLKGSRGVNSNAQKTDAGSNSSTTELLSHKQMAIEGYKAQSEMVIDSLDRLITTWEERNESVVVEGVHLSLNFVMGLMKKHPSIVPFMVYIANEEKHLERFAVRAKYMTLDPAKNKYVKYIRNIRTIQDYLCKRADKHLVPKINNTNVDKSVATIHATVFGCLRRRETGEKLYDTTTNTVSVIDDEHRNQCAANSLTSKGMFQVIQRQGSSRRFMALCNTDGTVAKTWPVASVGKIRKPVVNTEMDDGTEHQLHKAEPVNLQFGHFGISAWPSDGATSHAGSVDDLRADIIETGSRHYSSCCSSPRTSDGPSKELMEEQSVNGSDEDDEEGDDDFHEPDSDEDLSDNNDERNRDEIGSVDEESTKSDEEYDDLAMEDKSYWTDNEEEESRDTISMVSQNNHNEASKTNKDDKYSQNLDLFLKTTNQPLTESLELTSEYRNRMGVAASDKAKMRKRSLSIPPVGKHGSIIDDQILANQTDSVL
May be not required for the accumulation of phytic acid in seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Q93ZS1
Q71VZ1
GSHAB_LISMF
Glutathione synthase
Listeria
MLDSFKEDPKLRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDSVYEWLENLHNIVSLRSENELLWPSSNPPILPAEEDIPIAEYKTPDSPDRKYREHLAKGYGKKIQLLSGIHYNFSFPEALIDGLYDKISLPEESKQDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFSKTKHDESLPDGSSALRDGISLRNSNAGYKNKEALYVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAEHGVEYLEIRSIDLNPLESNGISKDELAFIHLFLIKGLLSEDRELCSNNQQLADENENNIALNGLAQPALKNCDNEEISVVEAGLLELNKMSDFIQSLRPEDTKLQAIIEKQKERLLHPEKTIAAQVKQQVTKEGYVDFHLNQAKTYMEETEALAYKLIGAEDMELSTQIIWKDAIARGIKVDVLDRAENFLRFQKGDHVEYVKQASKTSKDNYVSVLMMENKVVTKLVLAEHDIRVPFGDSFSDQALALEAFSLFEDKQIVVKPKSTNYGWGISIFKNKFTLEDYQEALNIAFSYDSSVIIEEFIPGDEFRFLVINDKVEAVLKRVPANVTGDGIHTVRELVEEKNTDPLRGTDHLKPLEKIRTGPEETLMLSMQNLSWDSIPKAEEIIYLRENSNVSTGGDSIDYTEEMDDYFKEIAIRATQVLDAKICGVDIIVPRETIDRDKHAIIELNFNPAMHMHCFPYQGEKKKIGDKILDFLFE
Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Q71VZ1
Q16AD5
RS17_ROSDO
30S ribosomal protein S17
Roseobacter
MPKRILSGVVTSDANDQTVSVSVERRFTHPVLKKTIRKSKKYRAHDENNTFKKGDAVRIVECAPKSKTKRWEVLQAAEV
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Q16AD5
C3K1N5
QUEA_PSEFS
Queuosine biosynthesis protein QueA
Pseudomonas
MRVADFTFELPDSLIARHPLAERRASRLLTLDGVSGALAHRQFTDLLEHLRPGDLMVFNNTRVIPARLFGQKASGGKLEILVERVLDSHRVLAHVRSSKSPKPGSSILIDGGGEAEMVARHDALFELKFAEEVLPLLERVGHMPLPPYIDRPDEDSDRERYQTVYSQRLGAVAAPTAGLHFDQPLLDAIAAKGVETAYVTLHVGAGTFQPVRVDNIEDHHMHSEWLEVSQDVVDAVEACKARGGRVIAVGTTSVRSLESAARDGVLKPFSGDTDIFIYPGRPFHVVDCLVTNFHLPESTLLMLVSAFAGYPETMAAYQAAIDNGYRFFSYGDAMFITRNPAPRGPEEQL
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
C3K1N5
B3Q6W6
PURA_RHOPT
IMP--aspartate ligase
Rhodopseudomonas
MANVVVVGAQWGDEGKGKIVDWLSEQADIVVRFQGGHNAGHTLVINGQTYKLALLPSGVLRPSKLAVIGNGVVFDPQAFLDEVKKLQGQGVAISPENLRIAENVTLILPLHRELDATRENAAKAGAIGTTQRGIGPAYEDKVGRRAIRLMDLADLDTLPTKIERLLAHHNALRRGLGQPEIDAGQILADLSAMAPHLLPYAESVWRLLDIKRREGKRILFEGAQGALLDVDHGTYPYVTSSNTVAAQAATGTGMGPGAVGYVLGICKAYTTRVGAGPFPTELTNEIGEEIGRRGKEFGVNTGRKRRCGWFDAVLVRQTVRTCGIHGLALTKLDILDGFDSVEVCVGYKLDGKEIDYLPAGEGAQARVEPIYETIEGWKEPTANARSWAELPAQAIKYVRRIEELVGCPVALLSTSPEREDTILVQNPFEA
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
B3Q6W6
O78422
RRP3_GUITH
Probable 30S ribosomal protein 3, chloroplastic
Guillardia
MPKFTLKVLWLDNNVAVAVDQIIGNGTSPLTCYFFWPRNDAWEQVKAELESKPWIEEKERIELLNKTTELINCWQEQSKKYSFKEIQSKFPDFIFAGAN
Probably a ribosomal protein or a ribosome-associated protein.
O78422
H6VGI3
KARG0_SCYPA
Arginine kinase Scy p 2.0101
Scylla
MADAAVIEKLEEGFKKLEAATDCKSLLKKYLTKSVFDQLKGKKTSLGATLLDVIQSGVENLDSGVGVYAPDAEAYTLFAPLFDPIIEDYHKGFKQTDKHPNKDFGDVNQFVNVDPDGKFVISTRVRCGRSMEGYPFNPCLTEAQYKEMESKVSSTLSNLEGELKGTYYPLTGMTKDVQQKLIDDHFLFKEGDRFLQAANACRYWPTGRGIYHNDNKTFLVWCNEEDHLRIISMQMGGDLGQVYRRLVSAVNEIEKRVPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYSLQVRGTRGEHTEAEGGVYDISNKRRMGLTEFQAVKEMQDGILELIKIEKEMQ
Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine.
H6VGI3
A1JP52
PURR_YERE8
Purine nucleotide synthesis repressor
Yersinia
MATIKDVAKHAGVSTTTVSHVINKTRFVAENTKAAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEVIEAVENSCYSKGYTLILCNSHNNLDKQKAYLAMLAQKRVDGLLVMCSEYPEQLLGMLEDYRNIPMVVMDWGTARGDFTDSIIDNAFEGGYLAGRYLIERGHRDIGAIPGQLSRNTGGGRHQGFLKALEEANITLREEWVVQGDFEPESGYKAMHQILTQKHRPTAVFCGGDIMAMGAICAADELGLRVPQDISVIGYDNVRNARYFSPALTTIHQPKERLGETAFAMLLDRIVSKREDPQTIEVHPKLVERRSVADGPFRDYRR
Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.
A1JP52
B3E600
ADE_TRIL1
Adenine aminohydrolase
Trichlorobacter
MNLTNIPRQALPELLCRMPKAELHIHIEGSLEPELIFALAERNRLQLAYPTIESLRAAYAFTNLQSFLDIYYAGASVLQTEQDFFDMAWAYLLRAKADNVVHAEIFFDPQTHTARGIPFATIINGLDRAIQQGRNELGISAALILCFLRHLTEADAFTVLEEALPFRDKFIGVGLDSGEKGNPPEKFSRVFARCRELGLRLVAHAGEEGTAEYIWHALDLLQAERIDHGVHCLDDPQLVTRLVQQQVPLTVCPLSNVKLRVFPDLAAHNIARLLACGIRATINSDDPAYFGGYLNQNYLETFAALPELGAAEAYQLARNSFEASFVDAEVKAGWIRELDQFFQQQCDKI
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
B3E600
E1B7Q7
TRIPC_BOVIN
Thyroid receptor-interacting protein 12
Bos
MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSVVIVPQPEDPDRANTSEKQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPKALQHTESPSETSKPHSKSKKRHLDQEPQLKSAPSPSTSKAHTRKSGAAAGSRSQKRKRTESSCIKSASVSEATGAEERSAKPTKLASKSAASAKAGCSTITDSSSAASTSSSSSAVASASSAVPPGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASASRRGSGLGKRGAAEARRQEKMADPEGNQETVNSSAARTDETPQGAAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEQINEDTGTARAIQRKPNPLANTNTSGYSELKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSLGSTPSVNSGTATAATNASADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGSRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSAQSNSNNIEPARTAGVSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPIERVEPVGNAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGTGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSIQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESNKDCVGGKRGRAQTAPTKTSPRNAKKHDELWNDGVCPSVSNPLEVYLIPTAPENITFEDPSLDVILLLRVLHAVSRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSLEIMREKLLMAAREGQQSFHLS
E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex.
E1B7Q7
A8F3S6
RUVC_PSELT
Holliday junction resolvase RuvC
Pseudothermotoga
MIIFGVDPGFGILGYGVLSVSGNSFQHVSHGTIQTEKQQNIALRLKVLYEELSNVIDNFKPSEIAMEKLFFSRNITTAISVGEARGIVLLLAAQRNIPVFEYTPHEIKKAVTGSGKASKKDVQQMIKILLNLKELPKPDDAADGLAIAWCHCAVRNITRRFS
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.
A8F3S6
A7MWI6
RL2_VIBC1
50S ribosomal protein L2
Vibrio
MAIVKCKPTSPGRRHVVKVVNADLHKGKPYAPLLEKNSKNGGRNNNGRITVRHIGGGHKHHYRVVDFKRTKDGIPATVERLEYDPNRSANIALVLYKDGERRYILAPKGVNAGDVIQSGVDAPIKAGNTLPMRNIPVGSTVHNVELKPGKGGQLARSAGAYAQIVARDGAYVTIRLRSGEMRKVLSEGRATIGEVGNSEHMLRELGKAGASRWRGVRPTVRGVVMNPVDHPHGGGEGRTSGGRHPVSPWGMPTKGFKTRKNKRTDKYIVRRRNK
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.
A7MWI6
O32522
PTHB_ERWAM
Glucitol/sorbitol-specific phosphotransferase enzyme IIB component
Erwinia
MANTIEIRKGESGWGGPLSINVTAGKKIVYITAGTKPAIVDHLVALTGWEAVDGFKQGEPPAEEIGVAVIDCGGTLRCGLYPKRRIPTINIHATGKSGPLAQFITEDIYVSGVRVADIRVANDAEAAPPEVAVADVAVNAGKGTGRDYDTSKKITEQSDGLLAKVGMGMGSAVAILFQSGRETIDTVLKTILPFMAFVSALIGIIMASGLGDFIAHGLTPLANSPVGLVTLALICSFPLLSPFLGPGAVIAQVIGVLVGVQIGQGTIPPHLALPALFAINAQAACDFIPVGLSLANARQETVRVGVPAVLVGRFITGAPTVLLAWAASSFIYH
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport.
O32522
Q3AMN6
RS3_SYNSC
30S ribosomal protein S3
unclassified Synechococcus
MGHKINPTGLRLGITQEHRSRWYASSKNYPALLQEDDRIRKFIHKKYGSAGISDVLIARKADQLEVELKTARPGVLVGRQGSGIEELRSGIQKTIGDSSRQVRINVVEVERVDGDAFLLAEYIAQQLEKRVAFRRTIRMAVQRAQRAGVLGLKIQVSGRLNGAEIARTEWTREGRVPLHTLRADIDYATKVASTTYGVLGIKVWVFKGEVLSEQAQPMPVGAAPRRRASRRPQQFEDRSNEG
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Q3AMN6
A4IKW7
ADDA_GEOTN
ATP-dependent helicase/nuclease AddA
Geobacillus
MNATFRPKPAGSRWTDEQWKAIAAGGRDILVAAAAGSGKTAVLVERIIQKVTAEEGAVDIDRLLVVTFTNAAAAEMKARIGEALERELANRPHSLHLRRQLSLLNRASISTLHSFCLDVIRKYYYLLDLDPSFRIADETEIELLKEDVLEELLEEEYGKADNERFFAVVDAYTGDRSDAELQEMILALYEFSRSHPAPDEWLADLVSMYDVDEQTNVETLPPARYIAQHAAMELAAAKRFIGLALALAEKESGPKPYEKRLREDMDLIADLERRLSGSWDELYHALQSLSFGRLPPCRGDGFDAELIDEAKSLRDQAKKKIEALRDNVFSLHPSAWLRHMREMKPVVETIAALVRRFSAMFEAAKREKGIVDFSDLEHYCLRILRQYDPETGEWQPSSAALEYQAQFDEVLVDEYQDTNLVQETILQLVKKGSERTGNLFMVGDVKQSIYRFRLAEPMLFLDKYKRFTADGEAGGMKIDLASNFRSRAEVLDGTNFLFAQIMGEAVGEMVYDEAAQLKYGADYPEGTDAVPEVMIIDRQRTSEEDEEETAELEAAELESRLMAEKIKEIVSRPFYVYDRSSGQQRRAMYRDIVVLVRSMTNAPQMIEQLQAQGIPAAADLSSGYFQATEISVMLSLLKVIDNPYQDIPLAAVLRSPLFRFDENELAMIRLSDPKGTFFEALQAFCQKTAETGEEENAKEKAISFLNKLEEWRTMARRRSLADLIWQLYRDTQFYDFVGALPGGKQRQANLRALYDRARQYESTSFRGLFRFLRFIERLQERGDDLGAARPLGDQEDVVRVMTIHSSKGLEFPIVFLVGLARPFYTRDLHSPYLLDKELGFAARFVHPRLRISYPTLPLLAIQVKKRLELLAEEMRILYVALTRAKEKLYLLASVNDADKEIEKWKGVAAESGWLLPDDVRASARSYLDWIGRALIRHRDGRSLVEVNRPDEIASHPSVWRFEIVSAAKLRNAEVSTDREDGGALVALEQGRPVPTQGEWEEEARRRLLWRYRYGKETVVRAKQSVSELKEQQALFGEQADEWLPRKGTAPLFSRPRFMQEKTLTPAEKGTALHVVMRHLDLHAPMDESSIRSQIIRLVEKELLSAEQAETVDAAAIVAFFATDIGRRLCAAREVYREVPFSLGLPADELYGSEGMESGRRLLVQGVVDCVFADERGYVVIDYKTDEVTGRFAGQKEEATRFLLGRYGGQMRLYRRAIEQIWRVPVAECYLYSFDGEYFLAVE
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
A4IKW7
Q9A5C1
SYA_CAUVC
Alanyl-tRNA synthetase
Caulobacter
MPSLNEIRSTFLDYFGKADHAVTPSAPLVPQNDPTLLFVNAGMVPFKNVFTGAETPAHPRAASSQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEQAILHAWTLLTAEFKLPKDKLLVTVYHTDDEAADLWKKIAGLGDDRIIRIPTSDNFWSMGDTGPCGPCSEIFFDHGPHIAGGPPGSPDEDGDRFIEIWNLVFMQFEQLAGGERISLPKPSIDTGMGLERIAAVLQGQHDNYDIDLFKALIAASVELTGVKAEGAQAPSHRVIADHLRSSSFLLADGVSPSNEGRGYVLRRIMRRAMRHAYLLGASEPLMHRLAPTLVREMGQAYPELRRAEALIVETLRQEEERFRTTLGRGMGLLDEATANLAAGGVLDGETAFKLYDTYGFPLDLTQDAVRAKGLTVDTDAFDAAMQKQREMARANWAGSGQQGAAAAWFSIKEKAGATDFVGYETTETTGVVKAIVVDGAEVESASAGQTVEVLLDRTSFYAESGGQAGDTGVIEAHGRESRVLDTQKQAGELHVHRVELASDLKVGDQVVASVDADRRNTTRSNHSAAHLVHAALHHVLGPHVAQKGQMVDGERMRFDFSHGGPLTAEELDRIEAEVNEVIRQNVPAETKEMAPQEAIEAGAVALFGEKYGDSVRVLTLGKSLADEAKAYSVELCGGTHVARTGDIALFKIVSEQGVAAGVRRIEALTGEAARRFLLDQAGVAKALADQFKTPVAEVATRVDALIADRKRLEKELAEAKKQLALGGGGAASGPEDVNGTALIARVLDGVGGKELRGVAEEFKKQLASGVVALVGTSDGKAAVTVAVTADLTGKFSAADLAKAAVIAMGGQGAGGKADFAQGGAPDDSKAEEGLAAVKALLAG
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q9A5C1
P24504
NUP3_PENSQ
Endonuclease PA3
Penicillium
WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASIASWADEYRLTSAGKWSASLHFIDAEDNPPTNCNVDYERDCGSSGCSISAIANYTQRVSDSSLSSENHAEALRFLVHFIGDMTQPLHDEAYAVGGNKINVTFDGYHDNLHSDWDTYMPQKLIGGHALSDAESWAKTLVQNIESGNYTAQATGWIKGDNISEPITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDSVIDTIELQIAKGGYRLANWINEIHGSEIAK
Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases.
P24504
Q9NYW3
TA2R7_HUMAN
Taste receptor family B member 4
Homo
MADKVQTTLLFLAVGEFSVGILGNAFIGLVNCMDWVKKRKIASIDLILTSLAISRICLLCVILLDCFILVLYPDVYATGKEMRIIDFFWTLTNHLSIWFATCLSIYYFFKIGNFFHPLFLWMKWRIDRVISWILLGCVVLSVFISLPATENLNADFRFCVKAKRKTNLTWSCRVNKTQHASTKLFLNLATLLPFCVCLMSFFLLILSLRRHIRRMQLSATGCRDPSTEAHVRALKAVISFLLLFIAYYLSFLIATSSYFMPETELAVIFGESIALIYPSSHSFILILGNNKLRHASLKVIWKVMSILKGRKFQQHKQI
Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Q9NYW3
Q6G543
ILVD_BARHE
Dihydroxy-acid dehydratase
Bartonella
MPSYRSRISTHGRNMAGARSLWRATGMKESDFGKPIIAIANSFTQFVPGHVHLKDLGQLVAQQIVASGGIAKEFNTIAIDDGIAMGHDGMLYSLPSREIIADSVEYMINAHCADALVCISNCDKITPGMLMASLRLNIPTIFVSGGPMEAGKIKWKDQDLTVDLVDAMVAAAAENNSEEEVAEMERAACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSMLATHADRQMLFEEAGRQIVTLVKRYYEKGDETVLPRSIASRKAFENAMTVDISMGGSTNTVLHLLAAAQEGEVDFTMTEIDRLSRRVPVLCKVAPAVANVHMEDVHRAGGIMGLLGELDAVGLIDTSAYTVHAKTMKEALCRWDVKRTNEPKTHEFYRAAPGGISTQTAFSQSRRYDSLDLDREKGIIRDKEHAYSQDGGLAVLYGNLAKDGCIVKTAGVDQSILTFKGPARIFESQDSAVSAILNDTIQSGDIVLIRYEGPRGGPGMQEMLYPTSYLKSKGLGKVCALITDGRFSGGTSGLSIGHVSPEAAEGGAIALVEEGDIIEIDIPNRTIHMLVEDDELMHRRVKMEAKGKAAWQPTEKRKRKVSKALKAYAAMTTSAAKGAVRNI
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Q6G543
O04019
PS6AB_ARATH
Tat-binding protein 1 homolog B
Arabidopsis
MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRADILDPALMRSGRLDRKIEFPHPTEEARGRILQIHSRKMNVNADVNFEELARSTDDFNGAQLKAVCVEAGMLALRRDATEVNHEDFNEGIIQVQAKKKASLNYYA
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
O04019
A3LVL1
RCF1_PICST
Respiratory supercomplex factor 1, mitochondrial
Scheffersomyces
MVIRSKEQPVVPLGALATTGAIILAARSMKRGEKLRTQVYFRYRVVFQLITLVALVAGGVMMQQESAEQKKTREDKLREKAKQREKLWIEELERRDALIQERKRRLEESRAELKKMAEEGFKQENDNSKGK
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
A3LVL1
A1WLI3
IF2_VEREI
Translation initiation factor IF-2
Verminephrobacter
MSSNTVAEFATELKKSPATLLDQLKAAGVGKAALSDALTESDKQRLLAYLQASHGTTSVDRKKITLVKKSTSEIKQADATGKARTIQVEVRKKRTFVKRDDAQEGAADGAGSAAFAEPEHPAPAAQHDVPEAPAEQAQADAAPAADGAAPALSSEDQELARREEQARHQAELIRRQEAELAAKRAAREAREKREREAEERAAAYAAQEAEKKAAASAVKQVATREQAAEATARNAAQLQARAKAAAESKARSDEEAARAADLDARRRKAEAEAAAIRSMLATPKKAVMVAKKPEPPPKPVPKPAAAAGDAKKGTLHKPAVGATRTAAGAARAGAAAGAPGAGKEVKSAKLSSSWAGDPAKKKEIKTRGDSSGGVGRNNWRGGPRGRRGDSRDQRDEHLQAAPAETRIIEVHVPETITVAEVAHKMSIKASEVIKALMKMGQMVTINQPLDQDTAMIVVEELGHKAVVAALDDPEAFADDDVAQQSIEVLPRAPVVTVMGHVDHGKTSLLDYIRRAKVAASEAGGITQHIGAYHVQTPRGMVSFLDTPGHEAFTAMRARGAQATDIVILVVAADDGVMPQTREAIKHAKAAGVPIVVAITKADKPDANLDRVKQELIGEQVVPEDYGGDSPFVAVSSKTGQGIDALLEHVLLQADVMELKAPVDALAKGLVIEAQLDKGRGPVATVLVQSGTLKVGDVVLAGQTFGRVRAMLDENGRPAKTAGPSIPVEIQGLTEVPQAGDEFMVLTDERRAREIATYRAGRFRNTKLAKQQAAKLEHVFADMTAGEVKMLPIIVKADVQGSQEALAQSLLKLSTDEVKVQLVYAAVGAISESDINLAIASKAVVIGFNVRADAGARKLAEGNGVALHYYSIIYDAVDELRVAMSGMLAPEQREEIIGTAEIRTVFTASKIGTVAGSYITSGMVHRNARFRLLRANVVVHTGEVDSIKRLKDDVREVKEGFECGIKLKNYSDILEGDQLEFFDIKQIARTL
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
A1WLI3
Q54VX4
MCFJ_DICDI
Mitochondrial substrate carrier family protein J
Dictyostelium
MSSSHTIQETKEVHTKTNKRIQWDDLDPKRYYFYNFLLGGSIDLLMFPLDVIRTRLQVQGSQNVIQSFPQYNGTFDGFKKLIRLEGKRALYKGFLTSECGYLCSRAIYFGSYEFVKQGFLKGRSDSDSDLLFVTTISGAISEALASVIWVPFDVATQSVQIQGSLSKPKYKGGSDVFKKIYGERGIKGLYKGFGATIIRNVPYSGIWWGTYEISKSKLTQFNIRQKLGLKERSSHSLAVSAEIDKNNPSHEVENEDPIIHFISGFFAAVFATSITNPLDVAKTRLQTGVFPENEKPNFYTIIKSTIRKEGIRALWKGLVPSLLTSTPYSMISIFLYEEVKKLSLK
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Q54VX4
Q0HDV7
AROB_SHESM
3-dehydroquinate synthase
Shewanella
MTQQIQVDLGERSYPIYIGQSLMSDSETLSRYLLKKRILIVTNETVAPLYLKQIQDTMASFGEVSSVILPDGEQFKDLTHLDSIFTALLQRNYARDSVLVALGGGVIGDMTGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQIVIIDTECLQTLPAREFAAGMAEVIKYGIMWDAEFFQWLENNVQALKSLDTQALVYAISRCCEIKADVVSQDETEQGVRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKSMGLIDESIVRRIVQLFHAFDLPITAPESMDFDSFIKHMRRDKKVLGGQIRLVLPTAIGRADVFSQVPESTLEQVICCA
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Q0HDV7
Q9R1K5
FZR1_MOUSE
Cdh1/Hct1 homolog
Mus
MDQDYERRLLRQIIIQNENTVPCVSEMRRTLTPANSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEHKGLFTYSLSSKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNADQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLKWSTDHQLLASGGNDNKLLVWNHSSLSPVQQYTEHLAAVKAIAWSPHQHGLLASGGGTADRCIRFWNTLTGQPLQCIDTGSQVCNLAWSKHANELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLAMSPDGEAIVTGAGDETLRFWNVFSKTRSTKESVSVLNLFTRIR
Substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. Acts as an adapter for APC/C to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, may play a role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR).
Q9R1K5
Q1H361
ISCS_METFK
Cysteine desulfurase IscS
Methylobacillus
MTVRTPIYLDYSATTPIDPRVAEKMIPYLTEHFGNPASRSHAFGWTAEKAVENAREEVARLVNADPREIVWTSGATESNNLAIKGAANFYSPSKGKHIVTVQTEHKAVIDTVRELERLGYEATYLIPEPNGLIDLDKFKAALRPDTVLASVMLVNNEIGVIQDIEAIGNICREQGVIFHVDAAQATGKVHIDLQKLPVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLATHQIVGMGEAFRIAREEMDSENVRIRQLRDRLLKGLQEIEEVYVNGDLEHRVAHNLNISFNFVEGESLIMAVKDIAVSSGSACTSASLEPSYVLRALGRSDELAHSSIRFSIGRFTTEEEIDYTIQLMKSKIGKLRELSPLWEMHLEGVDLNAVAWATH
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Q1H361
B9M7S3
RECF_GEODF
DNA replication and repair protein RecF
Geotalea
MKLNKIYLQSFRNLQETMLMPAQHFNIFYGNNGQGKTNLLESIFIMATMKSFKTARSSDLVRWGAISSLLKGWVERDGVTREIAVFLDNQGKKIRVDQKAVTRIDDFFGHLNVVVFTPEEVNMVKGLPELRRKYLDRAVFSSDITYLSVYHAYSKILKNRNMLLKRGEKASFDIWTEKLVEQGKNIILSRLAYLDALRDLLKRFYREISGNEEAVDISYRPYHMDLADCRGDVADAFAEALAKTATEEERRGTTLAGPHRDDVEFILNGRPLKQFGSQGQQKSYVLALKMAETEYLQKKFHSQPIFLLDDLSSELDQERKKNLMEFLKKRDMQVFITTTSLQNINVDEIENYRTYRIEEGKVLH
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.
B9M7S3
Q9XA10
CRGA_STRCO
Cell division protein CrgA
Streptomyces albidoflavus group
MPKSRIRKKADYTPPPSKQATSIKLTSRGWVAPVMLAMFVIGLAWIVVFYVTDGSLPIDSLGNWNIVVGFGFIAAGFGVSTQWK
Involved in cell division. Coordinates growth and cell division. May act as an inhibitor of Z-ring formation.
Q9XA10
Q891R5
SYV_CLOTE
Valyl-tRNA synthetase
Clostridium
MNDNINIAKTYDPKEFEERIYKMWEEGEYFTPKVDKDKKPYTIVMPPPNITGKLHLGHALDNSMQDFLIRVKRMQGYSTLWLPGQDHASIATEVKVENELLKTGLKKKEMGREAFLERVWEWSEEYRGRIRDQLKKLGSSADFTRESFTMDDNLDKAVRAVFVKLYEEGLIYKGNRIVNWCPKCMTALSDAEIEYEENYGNFWHVKYPLVDSEEYLEIATTRPETMLGDTAVAVNPNDERYKHLIGKKLMLPLVNREIPIVADDYVDVEFGTGAVKITPAHDPNDYEVGKRHDLEEIIIMNENGTINELGGKYSGMDRYEARKAIVEDLKKEGFLVKVKEHIHNVSCHDRCNTIIEPMISKQWYVKMKELAKPAIEVVKSGEIKFVPERFDKTYFNWMENIQDWCISRQLWWGHRIPVWYCKDCGETIVSLEEAKKCSKCSSENLIQDEDVLDTWFSSALWPFSTLGWPDKTEDLEYFYPTDVLATGYDIIFFWVARMIFSGLHNMKEIPFKTVLIHGIVRDSEGKKMSKSLGNGVDPLEVIDKYGADALRFMLITGNAPGNDIRFYEERVESARNFANKIWNASRYVMMNLDKNLMEKYKDCKDYNIADTWILSRLNEVIKEVTDNIEKFELGMASQKVYDFMWNEFCDWYIELSKPVLYGEDEKAKGVTFNVLFNVLTSGLKLLHPIMPFITEEIFINIQEEEKTITTSKWPEFKEELKNEEVEKKMSHVIEAIKAIRNVRIEMDVPPSRKAKIMIYALDGIDAFKDGKIYFEKLASASEVEFLNSKEEAPENAVSAVTKGAEIYIPLFDLVDLEKEMERLNKEREKLEKEIERVDKKLSNENFVKKAPEAVVNEEKAKGEKYKEMLEAVLERIKSLK
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Q891R5
B4U609
MURD_HYDS0
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
unclassified Hydrogenobaculum
MAYLVWGKGRSGLAAFNLLKAKGFKAYIGDDKEDKNLWQDVWNEIDTVVLSPGIPPFHPLWKEAIKSSKEVIGETELAYRFYKGKNIIAVTGTDGKSTTVHLIHHFTSFKEGGNFGTPFSEIVLDNDKENVALEASSFQGKTLDTFRPNVGVFLNFSKDHLDWHPSLEDYLLSKQKIFKNQTQEDILILNAQKPVCDTPSLAKKIFFGENGDLKVVGSDVYYKDELLIENISHPSLKGLHNLYNIAVASFVAFSMGISLEEIKKNLETFEALPFRYQYLGNFEGIDICNDSKSTTVNALMSALESTKAPILLIAGGIDKGGDFSSIEAYKDKIKAVFLYGKDKNLIKDQIEHFLKVYVLEDLESALLKVKEQARKGDTILFSPACASFDMFESYKHRGEVFNELVKKHFNS
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
B4U609
Q42850
PORB_HORVU
NADPH-protochlorophyllide oxidoreductase B
Hordeum
MALQAATSFLPSALSARKEGAAKDSAFFGVRLADGLKLDATSLGLRTKRVNTSSVAIRAQAAAVSAPTATPASPAGKKTVRTGNAIITGASSGLGLATAKALAESGKWHVIMACRDYLKTARAARAAGMPKGSYTIVHLDLASLDSVRQFVKNVRQLDMPIDVVVCNAAVYQPTAKEPSFTADGFEMSVGVNHLGHFLLARELLEDLKASDYPSKRLIIVGSITGNTNTLAGNVPPKANLGDLRGLAAGLNGVGSAAMIDGAEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGVTFASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGYVSEEEAGKRLAQVVSEPSLTKSGVYWSWNKNSASFENQLSEEASDTEKARKVWELSEKLVGLA
Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Q42850
C5CBJ8
RISB_MICLC
6,7-dimethyl-8-ribityllumazine synthase
Micrococcus
MSGAGAPTFTPDPAAASGLNVAIVAAQWHTEIMDGLIAGAQAAAADLGLEPVLVRVPGTVELTVAAARLAERFDVVVVLGVVVRGDTPHFDYVCQSVTQGVTEVSVRTGVPVGFGVLTVDTEQQARDRAGLPGSREDKGREALEAAVLTELALRRAGA
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.
C5CBJ8
Q9P6L8
SRB8_SCHPO
Suppressor of RNA polymerase B srb8
Schizosaccharomyces
MSNRDSANPPGFNDAVPLAICYIDSSTSSHDEYLTLLQSKVSAPDKNFRDETVDGAPFLAGDAISKGHRYSPPVRSDRASAQGLLQQHLEKSSTLENLKRYSSTLLGRQNDAVIDEPFAPFRPPPRVTLSESRRDRWLQGLSDPMVPLSSLIKTIPHGLWGEDILRMLVKFRVPFTRAIWFIRCAGVNEARSFLRKVQTTDITEWVKNWTDVAAGFLISFISSFLNADIYSFADDYTYLLKLFGRLLAEELVSPKHFLLRIVSFSGDSSLKSFSLHFFALQFFSTSLIQYTHICRKCVITILQSYQQLIVDQPANLLKFSLLSKKVSHFLFTLAQKNIESFFFPTEWDKLKPTIILLWKDFPNYSTLLSIMQERNSKAMYMYKPVTSSIRFLQIISCLSFPVGWRTLAKDLFKLLPVYTGVPLLLHWCINCRSIFSGDRNFIVSSIFDNANFDRNLIVDLTLSFVLKLHPLEYNECVAAAQLLDHLAACGYFFFSKYIARLASLGYLRESMLNSSFMDDQRKILVQLPILRMSQQLKNKIYYILSKGNYFVDWSICDEYVKRFKEDHFSFMFKKEENYAIITLSLVKIASTPMSKLYEDYLVMLFAFHYSMFQVMTKLIADNLVHFSFQSCACQTLFFICSVVPKTESQKLLLNEMGKLFQVELNFSYDSPDVNLLIEQFYEITSYESNYDDAFVEYKDATVANRKDFIEFLFHNITVSSKHTAVIFTSDLLMVLKIALNHPPYFDDLATTTFSSLLKRDECTILSFFKILQFYGCKLLSVDQIWAVVSDVYEAQDNNTTLKQFFNYLLDESTWPEGYLEERHWRSILCKEARKHDSGLKLFKLGIKLCTRNEQIMKTIWSFIHVHDCNVISEVIPDQRFLRTLTEHFMIDLRQLDIVTCLKKALVTLDEFSAPLYATWLTTLDDDELSELTDDVVQKKVLESLDNYKSGIWKLVLSGLPNCKTVFEHLLLFSLEERLDLPAAFLQDLIGASAYVMEQVPDSWFLEKLPCPLTQSLQSFSHLSNHIEVLDSTRQSRLTFLCHLILHMHGFVELTDQLATLESLTIRKCIYRNQELLDLLLFSIHLVKPNVETNDEVCNTLKAWENIESRPYTIDFPEALQQYSPRIVLYEPTFW
Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Q9P6L8
Q9TL12
PSAI_NEPOL
Photosystem I reaction center subunit VIII
Nephroselmis
MVTSFLPSLFVPLVGLVFPAVAMASLFLYIEKDEIA
May help in the organization of the PsaL subunit.
Q9TL12
Q7U7I0
GLMU_PARMW
Glucosamine-1-phosphate N-acetyltransferase
Parasynechococcus marenigrum
MLAVAVLAAGKGTRMKSALPKVLQPLAGATLVERVLASAANLQPDRRMLIVGHQADRVEEQLAAIGLLEFVLQQPQNGTGHAVQQLLPVLQGFEGELLVLNGDVPLLRAETIESLVNGHRESGADVTLLTARLEDPTGYGRVFVDADGKVSAIVEHRDCSEEQLSNNLTNAGIYCFNWQALAEVLPKLSTDNDQGELYLTDTVAMLPKAMHVEVADPDEVNGINNRKQLAQCEAVLQQRLRDHWMAEGVTFVDPGSCTLSENCCFGRDVVIEPQTHLRGSCRIGDNCRLGPGSLLENAELGSDVSVLHSVVREATVGNGVAIGPFAHLRPAADIADGCRIGNFVEVKKSQVGAGSKINHLSYIGDASLGENVNVGAGTITANYDGVRKHRTVIGDGSKTGANSVLVAPVTLGAKVTVGAGSTITKDVPDGALAIGRAKQLSKEGWADRPA
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q7U7I0
B0VRV3
FPG_ACIBS
DNA-(apurinic or apyrimidinic site) lyase MutM
Acinetobacter calcoaceticus/baumannii complex
MPELPEVETTKTSLFPLLNQKVLSVEVRNPSLRWPIPDNVQKLVGQRLIGLNRRSKYILAEFEQDQMLWHLGMSGSFRLCQPNDELRKHDHLIIQFEDQQLRYHDPRRFGCILWLNPETQGKLIDTLGPEPLSTDFHAEYLASKLKNKSVGIKIALMDNHVVVGVGNIYATESLFNVGIHPAQPAGDLTMQQIEKLVVEIKRILKSAIDLGGSTLRDYSNAMGENGYFQQTLLAYGRAREMCVNCETTLENLKLGQRASVFCPQCQPLKKLRKP
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
B0VRV3
B2GJ30
ACPS_KOCRD
4'-phosphopantetheinyl transferase AcpS
Kocuria
MIVGTGVDIVDIARFERQLERTPRLRERLFVPHERELAPRSLAARFAVKEAAAKALLAPPGMIWQDCWVSNDEHGAPHLHTTGTVARQQRARGVDTWHVSISHDGGMAVAFVVAEAQEGSRDD
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
B2GJ30
Q2GK70
SYP_ANAPZ
Prolyl-tRNA synthetase
phagocytophilum group
MRLSEFYSPTVKNVSSDVVSASHKYSIRAGIVSQTASGIYTLLPLGLMVLRKVENIIREEINAVGFSEILMPTMQPADLWKESQRYDSYGQELIRIHDRGGREMVLGPTHEEVVTDLVRSSLKSYRDLPVNLYQIQWKFRDELRPRNGILRSREFLMMDAYSFDTDFEKAMKTYDAVFRAYRKAFKRMNLQTIALKADMGAIGGSVSHEFHVLTPTGESTVYYDERALELSEMNDYGIEELKEVYAATDDMHDEKSCGIAPEDLKTARGIEVGHIFYLDDRYSRTMNVKFCNTDGHSGTHVKMGCYGIGISRLIGALIEVFHDDAGIKWPLSVAPFKVGIVNLFSKNEECKRVSERIHSVLPNDSLYDDRDDTPGVKLSRMDLIGLPWQVIVGNSFIKDGVLELKNRATGDIELLSVDDVVSRISV
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Q2GK70
A0B8Q8
PURA_METTP
IMP--aspartate ligase
Methanothrix
MFTIITGAQFGDEGKGKIVDLLAEKYDIIARFQGGDNAGHTVKVGDKTYKLHLVPSGVLFDKRLLIGPGVVLNPKVLWEELQTLWGMGMKVDLGIDPKTSIIMPYHIEMDALREKARTAKIGTTRRGIGYAYIDKIAREEVQMADITDPEMLKRKLEEIAPAKESAIKEMGGDPSVVRDEAQLRAYLEIGRALKNNLTDVSLEINRALDEDKMVLAEGAQGAFLDVIHGTQKFVTSSFTTAGSACANLGVGPVRVDNVVGVVKAYITRVGEGPMPTELKDEIGDRLREAGGEYGTTTGRPRRCGWFDAVLGRKAVYLNGYTELALTKLDVLTGLRRIKICVAYELDGEILEYPPESTYELARCVPVYEEMEGWSESISEALDYSDLPQNARAYVERIQELMDVDIAAISVGPAREQTIYME
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
A0B8Q8
P59522
RSMH_BUCBP
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Buchnera
MKNNFSHTPVLLNETIQNLDIKNDGIYIDATFGYGGHSKEILKHLGKNGKLYSIDQDPYAIKIANKLKNDTRFNIIHGKFSNILKYSNKNKIRGKVNGILLDLGMSSMQINNPNRGFSFISDGPLDMRMNPNTGIPAYMWLKKTNLTTLYHVLKKYGEEPFSKKIAYNIIAYNKKKTITRTLELSKIITNSIPIKKYRKHPARRVFQAIRIYINHEIYELQQALEHVLNILIPGGKLLILSFHSLEDRTVKKFMIKYSKPPFVPPGLAITETQLKSLANKQLKIITKIFPSTIEIRKNPRAHSAILRVAQKNNNE
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
P59522
Q28ZT4
CLP1_DROPS
Protein CLP1 homolog
Sophophora
MSDHQNRGQDFSLEADSELRFEIEQKDAKVLVTLVNGFAELFGTELVKKKKYEFGMGAKVAIFTYQGCVLHVTGKMDVCYISKETPMVQYVNCHAALEQFRTEAEEKDRRGPVAMVVGPTDVGKSTLCRILLNYAVRVGRRPLYADLDVGQGAIAISGNVATILIERPASVEEGFPKTAPLVYHFGHKSPSGNSVLYNAVVSKMAEVTLQSLNGNKRTKSSGIIVNTCGWVKGHGYAHLLHAARAYGACAIFVLDQERLYNELLRDVPSSVHVVLLPKSGGVVERSKELRHECRDQRIKEYFYGNARAPFYPFSFEVKFQELRLYKIGAPPLPDSCMPIGMKAEDNKTKVVAVTPTPALIHHVLALSFAESVDDDVIGTNIAGFCCVTEVDMERQVVMLLSPQPRPLPPNALLLWSELQFMDNHT
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Q28ZT4
Q8CSS7
RNY_STAES
Ribonuclease Y
Staphylococcus
MNLLSLLLILLGIILGVVVGYIVARNLLHQKQVQARQTADDIVSYANKEADNIKKEKLLEAKEENQILKEQAENELRERRGELQRQETRLLQKEENLDRKSDLLDKKDEILEQKESKLEERQQQVDAKESSVQTLIMKHEQELERISGLTQEEAVKEQLQRVEEELSQDIAILVKEKEKEAKEKVDKTAKELLATTVQRLAAEHTTESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIRDAGEQATFEINVHNMHPDLVKILGRLNYRTSYGQNVLKHSIEVAHLSGMLAAELGEDVTLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYNENNIIINAIHSHHGDVEPTSIISILVAAADALSAARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVVVSPEEIDDLKSYRLARDIKNQIEEELQYPGHIKVTVVRETRAIEYAK
Endoribonuclease that initiates mRNA decay.
Q8CSS7
O59264
RF1_PYRHO
Translation termination factor aRF1
Pyrococcus
MSKMTRHDAQLYELKKKIEELKKIRGRGTELISLYIPAGYDLSKVMQQLREEYSTAQNIKSKTTRKNVLGALERAMQHLKLYKQTPENGLALFVGNVSEIEGNTDIRLWAIIPPEPLNVRLYRCDQTFVTEPLEEMLRVKDAYGLITVEKNEATIGLLRGKRIELLDELTSNVPGKTRAGGQSARRYERIREQETHEFMKRIGEHANRAFLPLLEKGELKGIIIGGPGPTKEEFVEGEYLHHELKKKILGVVDISYHGEYGLRELVEKASDILRDHEVIREKKLVNEFLKHVVKDTGLATYGEREVRRALEIGAVDVLLISEGYNKVRVRVKCNHCGWEELKTMSEEEYEVYRKKITKCPKCGSQNLTIEKWDVAEELIKMAEEAGSDVEIISLDTEEGQQFYRAFGGLGAILRFKI
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
O59264
Q9DEQ4
SFRP1_CHICK
Secreted frizzled-related protein 1
Gallus
MGVGRSEGGRRGAALGVLLALGVALLAVGSASEYDYVSYQSDLGPYPGGRFYTKPHQCVAIPADLRLCHSVGYDKMVLPNLLDHETMAEVKHQASSWVPLLNKNCHMGTQVFLCSLFAPVCLDRPVYPCRWLCEAVRDSCEPVMQFFGFFWPEMLKCDQFPQDYVCIAMTTPNATEVSRPKGTTVCPPCDNEMKSEAIVEHLCASEFALKMTIKEVKKENGDKVIIPRKRKALKLGPIRKKNLKKLVLLLKNGADCPCHQLDNLGHHFLIMGRQVKTQHLLTAIYKWDKKNKEFKKFMKKVKAPDCPTFPSVFK
Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types.
Q9DEQ4
Q9HCE6
ARGAL_HUMAN
GrinchGEF
Homo
MASSNPPPQPAIGDQLVPGVPGPSSEAEDDPGEAFEFDDSDDEEDTSAALGVPSLAPERDTDPPLIHLDSIPVTDPDPAAAPPGTGVPAWVSNGDAADAAFSGARHSSWKRKSSRRIDRFTFPALEEDVIYDDVPCESPDAHQPGAERNLLYEDAHRAGAPRQAEDLGWSSSEFESYSEDSGEEAKPEVEVEPAKHRVSFQPKLSPDLTRLKERYARTKRDILALRVGGRDMQELKHKYDCKMTQLMKAAKSGTKDGLEKTRMAVMRKVSFLHRKDVLGDSEEEDMGLLEVSVSDIKPPAPELGPMPEGLSPQQVVRRHILGSIVQSEGSYVESLKRILQDYRNPLMEMEPKALSARKCQVVFFRVKEILHCHSMFQIALSSRVAEWDSTEKIGDLFVASFSKSMVLDVYSDYVNNFTSAMSIIKKACLTKPAFLEFLKRRQVCSPDRVTLYGLMVKPIQRFPQFILLLQDMLKNTPRGHPDRLSLQLALTELETLAEKLNEQKRLADQVAEIQQLTKSVSDRSSLNKLLTSGQRQLLLCETLTETVYGDRGQLIKSKERRVFLLNDMLVCANINFKPANHRGQLEISSLVPLGPKYVVKWNTALPQVQVVEVGQDGGTYDKDNVLIQHSGAKKASASGQAQNKVYLGPPRLFQELQDLQKDLAVVEQITLLISTLHGTYQNLNMTVAQDWCLALQRLMRVKEEEIHSANKCRLRLLLPGKPDKSGRPISFMVVFITPNPLSKISWVNRLHLAKIGLREENQPGWLCPDEDKKSKAPFWCPILACCIPAFSSRALSLQLGALVHSPVNCPLLGFSAVSTSLPQGYLWVGGGQEGAGGQVEIFSLNRPSPRTVKSFPLAAPVLCMEYIPELEEEAESRDESPTVADPSATVHPTICLGLQDGSILLYSSVDTGTQCLVSCRSPGLQPVLCLRHSPFHLLAGLQDGTLAAYPRTSGGVLWDLESPPVCLTVGPGPVRTLLSLEDAVWASCGPRVTVLEATTLQPQQSFEAHQDEAVSVTHMVKAGSGVWMAFSSGTSIRLFHTETLEHLQEINIATRTTFLLPGQKHLCVTSLLICQGLLWVGTDQGVIVLLPVPRLEGIPKITGKGMVSLNGHCGPVAFLAVATSILAPDILRSDQEEAEGPRAEEDKPDGQAHEPMPDSHVGRELTRKKGILLQYRLRSTAHLPGPLLSMREPAPADGAALEHSEEDGSIYEMADDPDIWVRSRPCARDAHRKEICSVAIISGGQGYRNFGSALGSSGRQAPCGETDSTLLIWQVPLML
Acts as guanine nucleotide exchange factor (GEF) for RHOA, RHOB and RHOC.
Q9HCE6
Q5F5B4
PRMC_NEIG1
Protein-glutamine N-methyltransferase PrmC
Neisseria
MFKPHRRQTGRKMTFDEWLGLSKLPKIEARMLLQYVSEYTRVQLLTRGGEEMPDEIRQRADRLAQRRLNGEPVAYILGVREFYGRRFTVNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISTPALETARKNAADLGARVEFAHGSWFDTDMPSERQWDIIVSNPPYIENGDKHLSQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVEILPDLAGLDRVTLGKYMKHLK
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Q5F5B4