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 |
|---|---|---|---|---|---|---|
Q7NZV7 | CYSG_CHRVO | Sirohydrochlorin ferrochelatase | Chromobacterium | MEFFPIFLKLRHQRCLLVGGGEVALRKARLLLAAGASLQVVAPELAPELADLAERGELEHLPGRYAPALLDGMRLAVAATDDAEVNRAVAADAEARGILVNVVDDAEASRYISPAIIDRSPLMVAVASGGSVPVLARSIRARLESLIPAGYGRLARFGSSFRDAVKARFPDVDARRRFWETVLEGPLADAVMNGDEAAARAEMEKRIAAGGADRAGAVYLVGAGPGNPDLLTFRALRLMQQADVVLYDKLVAPELLELVRRDAERVYVGKARANHALPQDDINQLLVDLARQGKRVLRLKGGDPFTFGRGGEEIATLAEHGIAFEVVPGITSASGAAAYAGIPLTHRDYAQSVTFVTGHKQDGSIDLDWQALTRPQQTVVVYMGVSTAAELCQAFVDNGRAASTPAAAVEWATTERQRTVCGTLAALPGLMASHGIASPALIIVGEVVELADKLSWYRRSENSAVTIQED | Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. | Q7NZV7 |
Q8N264 | RHG24_HUMAN | p73RhoGAP | Homo | MEENNDSTENPQQGQGRQNAIKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLPGNKVSEHPCNEENPGKFLFEVVPGGDRDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGGGIFGQKLEDTVRYEKRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEAGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMISKHDCLFPKDAELQSKPQDGVSNNNEIQKKATMGQLQNKENNNTKDSPSRQCSWDKSESPQRSSMNNGSPTALSGSKTNSPKNSVHKLDVSRSPPLMVKKNPAFNKGSGIVTNGSFSSSNAEGLEKTQTTPNGSLQARRSSSLKVSGTKMGTHSVQNGTVRMGILNSDTLGNPTNVRNMSWLPNGYVTLRDNKQKEQAGELGQHNRLSTYDNVHQQFSMMNLDDKQSIDSATWSTSSCEISLPENSNSCRSSTTTCPEQDFFGGNFEDPVLDGPPQDDLSHPRDYESKSDHRSVGGRSSRATSSSDNSETFVGNSSSNHSALHSLVSSLKQEMTKQKIEYESRIKSLEQRNLTLETEMMSLHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQFFSTFGELTVEPRRTERGNTIWIQ | Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis. | Q8N264 |
Q9ZL42 | RIBA_HELPJ | GTP cyclohydrolase II | Helicobacter | MKRLEVSNQAKLPTQFGEFCIQCFREKGSNGSKDHLVIFTPNFPQNPLVRLHSECLTGDALGSQKCDCGGALQMALERISKEGGLVIYLRQEGRGIGLFNKVNAYALQDKGYDTIQANEMIGFKDDERDYSIAGEILEYYRIKKMRLLTNNPLKIAALEKYAEVTRESLIVCANEHNQGYLEVKKLKMGHLL | Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. | Q9ZL42 |
Q5E9N2 | CNBP1_BOVIN | Beta-catenin-interacting protein 1 | Bos | MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTANEEEFLRTYAGVVNSQLSQLPQHSIDQGAEDVVMAFSRSETEDRRQ | Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. | Q5E9N2 |
Q07QP5 | CAPP_RHOP5 | Phosphoenolpyruvate carboxylase | Rhodopseudomonas | MSSTVLSVEPDALPRSGEDAAAIAEDARLRDDIRLLGRILGDTVRDQEGEDVFDAVERIRQTSIRFHRDNDQPARDELVELFDGLSTPATLRIVRAFSYFSHLANLAEDQNNIRQMRLQNGARPGSLVATLAHARAVGISAKELRHFFETALVSPVLTAHPTEVRRKSTMDREMEIARLLDRRERLQMTPEEIEQHEELLRRAVLTLWQTNMLRRTKLTVLDEVANGLSFYDYAFLHEVPRLHGVLEDKLNDDDGAGEELASFLRMGSWIGGDRDGNPFVTAEVMRGTLRLQSRRALRHYLDELHALGSELSIAAHLADISDELRALAENSPDTSPHRAGEPYRLAVSAIYARLAATAHRLGIDDIRAPVAESAPYAEPAELKADLDVLHRSLVANNSAVIARGRLRSLRRAVDCFGFHLASLDMRQNSAVHERTMAELIDKAMPGKSYMAMNEEARIALLAAELRSPRPLASPFVKYSEETVDELAVFRAAAEAHATFGPAAIPQCIISMTKGVSDLLEVVVLLKEVGLVDPAGRSAINVVPLFETIEDLQAAAGIMDRLLGLHDYRRLVDSRGGVQEVMLGYSDSNKDGGFVTSGWELYKAEIELLKIFEHHGVRMRLFHGRGGSVGRGGGPSYDAILAQPAGAVNGQIRITEQGEIITSKYSNPEVGRNNLEVLAAATLEASLLQPRLGAPCVGYLKAMDEISALAFKAYRGLVYETEGFEDYFWSSTVITEIATLNIGSRPASRKKTHKIEDLRAIPWVFSWAQCRLMLPGWYGFGSAVEAWVKAHPEQGMAYLQELNREWPFFRTLLSNMDMVLSKSSIAIASRYAELVADEKLRAAIFGRIKREWHSSIAALLAIMGHQRLLQGNPRLERSIRHRFPYLDPLNHVQVELLKQHRDHAVDEQALRGIQITINGISAGLRNSG | Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. | Q07QP5 |
A1W118 | NADD_CAMJJ | Nicotinate mononucleotide adenylyltransferase | Campylobacter | MKIALFGGSFDPPHNGHNSVVLEALEKLDIDKLIIMPTYINPFKKSFSADEKQRFLWVKKLWGHLPKVEICDFEIRQKRPVPSIESVKYLYKLYNPSKFYLLIGADHLEKLHLWHDFEKLNSLVEFVIANRNDIGIPKNFKDLKTNKKIASSFIRDTLNTNEVCEEIKDEVKKYYEKLQKN | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | A1W118 |
Q9M3L4 | CEMA_SPIOL | Chloroplast envelope membrane protein | Spinacia | MEKKKVFIPFLYLISIVFLPWWIYLSFQKSLESWVTTWWNTKQSETFLNDIQEKKLLEKFIELEELRLLDEMIKEYPETQLQKLGIGIHNETIQLIKMHNEDCIHMILHFSTNLICFLILGGYSILGNKELILLNSWVQEFLYNLSDTIKAFSILLVTDLCIGFHSPQGWELLIESIYKDFGFADNDQIISSLVSTFPVILDTILKYWIFRSLNRVSPSLVVIYHSMND | May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts. | Q9M3L4 |
A4WE57 | GCST_ENT38 | Glycine cleavage system T protein | Enterobacter | MAQQTPLYEQHTLCGARMVDFHGWMMPLHYGSQIDEHHAVRTDAGMFDVSHMTIVDLRGSRTREFLRYLLANDVAKLKTPGKALYSGMLNASGGVIDDLIVYYFTEDFFRLVVNSATREKDLSWISQHAEKYAVEITVRDDLSLIAVQGPNAQAKAATLFTDEQRHATEGMKPFFGVQAGDLFIATTGYTGEAGYEIAMPNEKAAEFWHALVEAGVKPAGLGARDTLRLEAGMNLYSQEMDETVSPLAANMGWTIAWEPADREFIGREALEMQREKGTDQLVGLVMTEKGVLRNELPVRFTDELGNQREGMITSGTFSPTLGYSIALARVPAGIGETAIVQIRNREMPVNVTKPIFVRAGKPVA | The glycine cleavage system catalyzes the degradation of glycine. | A4WE57 |
P39773 | GPMI_BACSU | Vegetative protein 107 | Bacillus | MSKKPAALIILDGFGLRNETVGNAVALAKKPNFDRYWNQYPHQTLTASGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVNVAIREGEFERNQTFLDAISNAKENNKALHLFGLLSDGGVHSHINHLFALLKLAKKEGLTKVYIHGFLDGRDVGPQTAKTYINQLNDQIKEIGVGEIASISGRYYSMDRDKRWDRVEKAYRAMAYGEGPSYRSALDVVDDSYANGIYDEFVIPSVITKENGEPVAKIQDGDSVIFYNFRPDRAIQISNTFTNKDFRDFDRGENYPKNLYFVCLTHFSETVDGYVAFKPINLDNTVGEVLSQHGLKQLRIAETEKYPHVTFFMSGGREAEFPGEERILINSPKVATYDLKPEMSAYEVKDALVKEIEADKHDAIILNFANPDMVGHSGMVEPTIKAIEAVDECLGEVVDAILAKGGHAIITADHGNADILITESGEPHTAHTTNPVPVIVTKEGITLREGGILGDLAPTLLDLLGVEKPKEMTGTSLIQK | Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | P39773 |
Q9P6Q2 | ENOPH_SCHPO | 2,3-diketo-5-methylthio-1-phosphopentane phosphatase | Schizosaccharomyces | MVKNLLLDIEGTVGSISFVKDKLFPYAASRYESYVNENYESDENLRELGKTPEEALINLRKLHAEGSKERSFKMVQGRIWKKGYESNELTSHLFPDVVPAIQRSLQLGMRVYIYSSGSVPAQKLYFEHSDAGNLLKYFSGYYDTTIGLKTECGSYVKIVGNSNPREWLFLSDNINELKAARKVGLHTGLVVRPGNDPVVDTSGFPVYNSFEILFTE | Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). | Q9P6Q2 |
Q5HQ70 | POTA_STAEQ | Spermidine/putrescine import ATP-binding protein PotA | Staphylococcus | MNPLLSFKDVSKGFEDVQILNEINIDIEPGYFYTLLGPSGCGKTTILKLIAGFEYPDSGDIIYKDKPIGKMPPNKRKVNTVFQDYALFPHLNVFDNIAYGLKLKKLSKSEIKRKVTEALQLVKLSGYEHRQIQGMSGGQKQRVAIARAIVNEPEILLLDESLSALDLKLRTEMQYLLRELQSRLGITFIFVTHDQEEALALSDYIFVMKDGKIQQFGTPIDIYDEPVNRFVADFIGESNIVHGTMVEDFVVNIYGQNFDCVDMGIKENKKVEVVIRPEDISLVSQNDGLFKAKVDSMLFRGVHYEICCKDRKGYEWVIQSTKKANVGSEVGLYFEPEAIHIMVPGETEEEFDKRIESYEDYHHA | Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. | Q5HQ70 |
A7I3S9 | GLYA_CAMHC | Serine hydroxymethyltransferase | Campylobacter | MSNLENFDKEIFDLTNKELQRQCDYLEMIASENFTYPEVMEVMGSILTNKYAEGYPGKRYYGGCEFVDEIEQTAIDRCKKLFGCNFANVQPNSGSQANQGVYGAFIKPGDKILGMDLSNGGHLTHGAKVNASGKFYSSFFYGVEMDGRIDYNRVADIAKIVKPKLIVCGASAYPREIDFAKFREIADSVGAFLFADVAHIAGLVVAGEHTNPFPYCHVVSSTTHKTLRGPRGGIIMTNEEEFAKKINSSIFPGMQGGPLVHVIAGKAVGFKHNLSPEWKTYAKQVKANCKILGDTLMKRGFDLVSGGTDNHLILVSFLKKDYSGKDASNALENAGITVNKNTVPGETRSPFVTSGIRVGSAALTSRGMKEKEFEWIANKIADVLNDINNTSLQSKIKAEVKELASKFIIYDKAMF | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | A7I3S9 |
Q8RG36 | RL31_FUSNN | 50S ribosomal protein L31 | Fusobacterium | MKKGIHPEFDLVVFEDMAGNQFLTRSTKIPKETTTFEGKEYPVIKVAVSSKSHPFYTGEQRFVDTAGRVDKFNKKFNLGKK | Binds the 23S rRNA. | Q8RG36 |
A8GDR1 | IHFA_SERP5 | Integration host factor subunit alpha | Serratia | MALTKAEMSEHLFEKLGLSKRDAKDLVELFFEEVRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKE | 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. | A8GDR1 |
Q9HRT6 | RL44E_HALSA | 50S ribosomal protein L44e | Halobacterium | MEMPRRFNSYCPNCDEHHQLEAEKVRSGRSSGMKWDARRTKRANASIGNHGRFSKVPVGNKPTNRTDLKYRCSECGNAHLREGWRAGRLVLQE | Binds to the 23S rRNA. | Q9HRT6 |
A2BWM0 | ARGC_PROM5 | N-acetyl-glutamate semialdehyde dehydrogenase | Prochlorococcus | MNVAIVGATGYGGIQSVNLLKDNKNYKISYLGGYKTSGTKWSDNFPFIKLDSNNLIEKISIDRIADKADVALLCLPNGISSTLTRGLLEKGVKVIDLSADYRYKSLEQWKRIYSNEAAKYKRDDDDLCKEAVYGLPEINNKDISKARLIACPGCYPTSALIPLIPFLSQGIIDNEGIIIDSKSGTSGGGRESSQKLLFSECGDGLSAYGLINHRHTSEIEQIASFISGNDIELLFTPHLLPMIRGMHSTIYGRLRDPGLTSSDCRIILENFYRNYSNIRVLPVDIYPSTKWVKNTNEIHLSVKVDNRNGRIILLSVIDNLLKGQTGQAIQNLNLISGLPLNNGLEMINHYP | Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. | A2BWM0 |
Q2YHJ2 | PA2B_TRIBO | Phosphatidylcholine 2-acylhydrolase | Trimeresurus | MRTLWIMAVLLVGVEGSLLEFGRMIKEETGKNPLFSYISYGCYCGWGGQGQPKDATDRCCFVHDCCYGKLWSCSPKTDIYFYYRKNGAIVCARGTWCEKQICECDKAAAICFRENLGTYKDEYQSYGKSRCTEKSLKC | Snake venom phospholipase A2 (PLA2) that impairs hemostasis. It weakly inhibits ADP-induced platelet aggregation when tested on platelet rich plasma from human and rabbit blood (15-25% of inhibition at 5-10 ug of enzyme), and dose-dependently inhibits blood coagulation, possibly by inhibiting thrombin activation. Exhibits strong hydrolytic activities toward L-dipalmitoyl phosphatidylcholine. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Q2YHJ2 |
Q8EWZ9 | LEPA_MALP2 | Ribosomal back-translocase LepA | Malacoplasma | MDKKYIRNFSIVAHIDHGKSTLSDRIIEFTNTLTTREMKNQILDSMDIERERGITIKLNAVQLIYHNPKDNQDYYFHLIDTPGHVDFTYEVSRSLAACEGALLVVDASQGVEAQTLSNVYLALENNLEIVPVINKIDLPSADIDRVKKQVEDTIGLDCSNAPLVSAKTGLNINQIMEAIIEQIPPPLDSDDNKPLQALVFDSYYDAYKGAVCLVRIKNGQVKVGTKIRFMSNNETFIVSALGVNTPKIVNKEVLVAGEVGWIAASIKNIKSISVGDTITDDANPATTSLPGYKKILPMVYCGLYPIDSTQYELFKEALEKIYLSDSSLTYEYETSQALGFGIRCGFLGLLHMDVIRERLDREFNIALIATAPSVIYKVLLNDGTILEIDSAAKLPDKTLYKEIQEPFAKAEIIVPDDFLGNVMELCQNYRGEYLDLVNVDSTRKKVTYLIPLAEIMYSFFDKLKSCSKGYATLDYEILDYRKQDLVKVDILLNGNKVDALSTIMHREFASDRSRKICLKLKEHIPKHQFEIPIQAVIGGKIIARETVSAMRKNVLAKCYGGDITRKKKLLEQQKEGKKRLKAIGNVSVPHDTFVKILSEE | 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. | Q8EWZ9 |
P85148 | ETC50_ENTFC | Bacteriocin E50-52 | Enterococcus | TTKNYGNGVCNSVNWCQCGNVWASCNLATGCAAWLCKLA | Bacteriocin active against the Gram-negative bacteria C.jejuni, Y.enterocolitica and Y.pseudotuberculosis, and the Gram-positive bacteria S.aureus, S.epidermidis, L.monocytogenes and Listeria spp. When added to the drinking water of chickens, causes a decrease in the levels of C.jejuni and S.enteritidis in the ceca, and in the levels of S.enteritidis in the liver and spleen. | P85148 |
Q2NFV9 | RL2_METST | 50S ribosomal protein L2 | Methanosphaera | MGKRLIIQRRGRGTPTYRSSSHRFRGKVAYRSYDKLEREGSLTGIVIDIIHDPGRSAPVAVVKFDNGEEKLVLAPESIAIDDEIECGVSASIEPGNTLPLSEIPEGTPVFNIENNPGDGGKFVRSSGTYASLITHDVDKTMIEMPSGELKAFNPRSRATVGVVAGGGRKEKPFLKAGNRYHALKAKGKKMMTVRGVAMNAVDHPHGGGNRQHPGRPTTISRHAPAGRKVGSIAAKRTGKRR | 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. | Q2NFV9 |
Q5FS38 | DCUP_GLUOX | Uroporphyrinogen decarboxylase | Gluconobacter | MISENAPSSPSSKPLLRALRGEAVWPPPVWLMRQAGRYLPEFRAMRDRADFLTRCMTPDMATELTIQPIRRYGMDGAILFSDILILPWAMGQSLEFIDGRGPVLGAIRSEADLARLDPKRVQDAVAPVRETLSRLTKELPDVTTLLGFAGSPFTVSCYMVEGGGSRDFAETRRMMQTNPALFDRLIDTLTSSTAEMLCGQIEAGAEAVMLFDSWAGILPPSAFRRYVIEPTRQIVEYIRARHPKTPIIGFPRLGGIMVREYAQKTGVNTLALDTVADPAQISELVSEVRPGLTLQGNMDPMILFSGGETMIREAQAIRDAMRGKPHVFNLGHGVMQHTPPENVAALVEAVRAV | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q5FS38 |
O53561 | ECH19_MYCTU | Enoyl-CoA hydratase EchA19 | Mycobacterium tuberculosis complex | MATVESGPDALVERRGHTLIVTMNRPAARNALSTEMMRIMVQAWDRVDNDPDIRCCILTGAGGYFCAGMDLKAATQKPPGDSFKDGSYGPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTLACDLLLTGRHITAAEAKEMGLIGHVVPDGQALTKALELADAISANGPLAVQAILRSIRETECMPENEAFKIDTQIGIKVFLSDDAKEGPRAFAEKRAPNFQNR | Degradation of the cholesterol side chain involves 3 multistep beta-oxidation cycles, this may be involved in the second cycle (Probable). Hydrates 3-OCDO-CoA ((22E)-3-oxo-chol-4,22-dien-24-oyl-CoA) to make (22R)-HOCO-CoA (3-oxo-chol-4-ene-(22R)-hydroxy-24-oyl-CoA). Also acts on octenoyl-CoA. Not active on (E)-3-OCDS-CoA ((E)-3-oxocholest-4,24-dien-26-oyl-CoA) or 3-OPDC-CoA (3-oxo-4,17-pregnadiene-20-carboxyl-CoA). Hydrates the same substrate as ChsH3, but the 2 enzymes make different stereoisomers of the product . | O53561 |
A3N1B2 | PURT_ACTP2 | Phosphoribosylglycinamide formyltransferase 2 | Actinobacillus | MTTIGTPLRPNATKVMMLGSGELGKEVVIELQRLGVEVIAVDRYENAPAQQVAHRAYTISMLDGAALRALVEKEKPDFIVPEVEAIATATLVELEQEGYNVVPTAKATQLTMNREGIRRLAAEELGLKTSPYRFVDNLEDFKQAVAEIGIPCVVKPIMSSSGHGQSVIKSEDQIQQAWDYSQEGGRAGGGRVIVEGFIKFDYEITQLTVRHVNGTSFLAPIGHRQEDGDYRESWQPQAMSDLALKRAQETAERITTALGGRGIFGVELFVCGDEIIFNEVSPRPHDTGMVTMASQELSQFALHARAILGLPIPEIYQISPAASKAIVVEGKSNNMTFGNLDKVLEEIGTNIRLFGKGEVNGHRRLGVILARDENTEKALAKAERAYAKLAVQL | Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. | A3N1B2 |
Q1MH51 | RRF_RHIL3 | Ribosome-releasing factor | Rhizobium | MSEGIDIKELKRRMDGAISVFKGDIASLRTGRASANILDPVTVEAYGSRMPLNQVANITVPEPRMLSVSVWDKSMVSAVERGIRESNLGLNPIIDGQNLRIPLPELNEERRKSLVKVAHDYAEKSKVAIRHVRRDGMDGLKKAEKDGVIGQDESRAQSERVQKMTDETISEIDRLLGEKEKEIMQV | 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. | Q1MH51 |
A8W3G4 | RR7_CUSEX | 30S ribosomal protein S7, plastid | Cuscuta subgen. Monogynella | MSRRGTAEKKTAKYDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAVKKIQQKTETNPLSVLRQAIRGVTPDITVKARRVGGSTHQVPVEIGSTQGKALAVRWLLAASRKRPGRDMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. | A8W3G4 |
C3PHA2 | LGT_CORA7 | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Corynebacterium | MQIYYLANIPSPPQGVWHLGPVPIRAYAMCIIVGILVALWMTLRRYTARGGNPDVVWDAALVVIPAGIIGGRLYHVITDNDKYFCSTCDPLDALKITNGGLGIWGAVALGAVAVWLMFKVKGIPLGPFADAVAPGLILAQAIGRLGNWFNQELYGRETTVPWALDIYYRVNESGEYAPISGRSTGEVIASVHPTFLYELLWNVAVCVFLLWAHKAFKLGHGRVFALYVAGYTAGRFVVENMRADDATLIFGLRVNVIVSVVCFVVALIVYIRLPRGQETPEEVDPARSTDAGDSVGTADSQR | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | C3PHA2 |
Q47G87 | NIFW_DECAR | Nitrogenase-stabilizing/protective protein NifW | Dechloromonas | MEDTLSLAEAMEDLVSAEDFLDYFAVPYDPAVVHVNRLHILQRFHDYLAKQAPNLPPEESQQRGIYRLWLERAYQDFVTSDSLTEKVFAVFQTVSKPDGGMSSFVSLDKVFRQ | May protect the nitrogenase Fe-Mo protein from oxidative damage. | Q47G87 |
Q06GW5 | RPOA_DRIGR | Plastid-encoded RNA polymerase subunit alpha | Drimys | MVREEVAVSTRTLQWKCVESRTDSKRLSYGRFILSPLMKGQADMIGIAMRRALLGEIEGTCITRAKSDKIPHEYSTIVGIEESVHQILMNLKEIVLRSNLYGTCDASIFVRGPRCVTAQDIISPPSVKMVDTTQHIASLTEPIDLCIGLQIERDRGYRMKTPNNDQDGSYPIPIEAVSMPVRNANHSIHSYGNGNEKQEILFLEIWTNGSLTPKEALHEASHNLIDLFIPFLHGEEEDINLEDSLNRGTLPFFTFQDKLANLRKNKKAIALECIFIDQSELPPRTYNCLKRSNIHTLLDLLSNSQEDLMRIEHLRIEDVKRILDILQKHFTIDLPKNKF | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q06GW5 |
Q9SGU3 | MYB72_ARATH | Myb-related protein 72 | Arabidopsis | MGKGRAPCCDKNKVKRGPWSPQEDLTLITFIQKHGHQNWRSLPKLAGLLRCGKSCRLRWINYLRPDVKRGNFSKKEEDAIIHYHQTLGNKWSKIASFLPGRTDNEIKNVWNTHLKKRLTPSSSSSSLSSTHDQSTKADHDKNCDGAQEEIHSGLNESQNSATSSHHQGECMHTKPELHEVNGLNEIQFLLDHDDFDDITSEFLQDNDILFPLDSLLHNHQTHISTQEMTREVTKSQSFDHPQPDIPCGFEDTNEESDLRRQLVESTTPNNEYDEWFNFIDNQTYFDDFNFVGEVCL | Involved in metal ions homeostasis, including iron ions (Fe) acquisition, via the regulation of NAS4 and NAS2 genes expression. Necessary for plant survival in alkaline soil where iron availability is greatly restricted . Involved in the up-regulation of several biosynthesis genes of secondary metabolites involved in iron uptake under conditions of iron deficiency . Triggers tolerance to nickel (Ni) and zinc (Zn) ions . Required in the roots during early signaling steps of rhizobacteria-mediated (e.g. P.fluorescens WCS417r) and beneficial fungi-mediated (e.g. T.asperellum T34) broad-spectrum induced systemic resistance (ISR) against several pathogens (e.g. P.syringae pv tomato, H.parasitica, P.cucumerina, A.brassicicola and B.cinerea) and implying enhanced callose deposition . Required for the induction of some genes (e.g. BGLU42) upon rhizobacteria-mediated ISR . | Q9SGU3 |
B2J4Q8 | CHEB_NOSP7 | Protein-glutamate methylesterase/protein-glutamine glutaminase | Nostoc | MRIAIVNDTAMAVEALKRVLLTVPGHEISWIARDGTEAVARCARDTPDLILMDLFMPVMDGVEATRQIMKQSPCAIIIVTASVSKNAGKVFEAMGYGARDAVNVPILGTQESSDSAQLLLTKIATIAKLIGKSSPTSTPKPQTAKLTSFSTHSTLLPPLVAIGSSTGGPKALAAILSRLPANFGAAIAIVQHVDMQFSAGLVDWLNQQTALTVQLATVGDRFEKGIVLVAGTNDHLSLHSDLTLHYTKEPIDYPYRPSVDVFFKSLAQYWNAKGTAVLLTGMGQDGAQGLSLLRSRGWHTIAQDEKSSVVYGMPKAAVQLNAAVEILPPEAIATSLIQQIMFRKSGVPKSDTRK | 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. | B2J4Q8 |
Q89AQ2 | MURD_BUCBP | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Buchnera | MTRNYLHKKILIFGMGLTGISCLNFFLSKGIYPKIMDTDKRPKHIEKIIKFKNICYHTGSVNYSWILQSNLIIVSPGITPSHPALKFATKKNIEIIGDIELFVQETKVPIIAITGSNGKSSVTKIVKEIIQKAGFTTYIGGNIGIPALNIVNKFAHFFILELSSFQLERTFSLKAYIATILNITPDHLNRYSSDIKEYEKAKQKIYKNSKICIINVDNPVTINRQAQLTKCISFGVHSGDYHLSHTYTNTWLCYKSLKLINTKKLKLSGRHNYINMLSALAIVHELKISFKISVRILKNFLGLPHRCQKVYKNNNITWINDSKSTNIASTKSAIQSINTKGKIRLILGGDKKSSNLNLLKPILKNNAIVIYCYGKDKKELFNLYPHKSKIFETLQEVMQHISVQVQPGDVVLLSPACSSLDQFSGFEERGNTFVKLIQELIH | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | Q89AQ2 |
Q604M1 | ISPF_METCA | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Methylococcus | MFRIGQGYDAHRFKEGDHIVLCGVKIPFGRGFAAHSDGDVALHALCDALLGAAALGDIGRHFPDTDARYKGIDSRVLLREVRQRIASLGYTVGNVDVTVVAQAPRLAAHIQAMRENLAQDLEIPPDCVNVKATTTEGMGFEGRGEGISAHAVALLARR | 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). | Q604M1 |
A6VQJ6 | LPXA_ACTSZ | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Actinobacillus | MIHSTAKIHPSAIVEEGAKIGENAIIGPFCVVEKDAEIGKGTILYSHVVVRGITKIGEDNRIYQGASIGEINQDLKYQGEATRTVIGNRNRIRENVTIHRGTAQGGWVTNIGDDNLFMVNAHVAHDCQIKNRCILANNATLAGHVELDDFVIVGGMSAIHQFVIVGAHVMLGGGSMVSQDVPPYVMAQGNHARPFGVNIEGLKRRGFDKPTLHAIRNVYKLIYRSGRTLEEVMPEIETYAQTESAVSFFLDFFARSTRGIIR | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A6VQJ6 |
P42077 | RPOC1_PROMD | Transcriptase subunit gamma | Prochlorococcus | EVTKPETINYRTLKPEMDGLFCEKIFGPSKDWECHCGKYKRVRHRGIVCERCGVEVTESRVRRHRMGYIKLAAPVSHVWYLKGIPSYVAILLDIPLRDVEQIVYFNCYVVLDVGDHKDLKYKQLLTEDEWLEIEDEVYAEDSTIENEPVVGIGAEALKQLLEDLDLNQIAEELREEITNSKGQKRAKLIKRIRVIDNFLATNAK | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | P42077 |
A9VG56 | BIOF_BACMK | 8-amino-7-ketopelargonate synthase | Bacillus cereus group | MNQMWRTHLQSKVEQLKEQGQYRNLHVTEKAEETWLIRNEKRMLNLASNNYLGLAGDERLKEAAIACTRKYGTGATASRLVVGNYPLYEEVERSICDWKGTERALIVNSGYTANVGAISALACRHDMIFSDKLNHASIVDGIILSGAEHKRYRHNDLDHLEKMLQIASPEKRKLIVTDTVFSMDGDIAYLRGLVQLKEKYGAIIIVDEAHASGIYGIGGAGLSHVEKDIAQKIDIHMGTFSKALGCYGAYLTGDSIYIEYLQNMMRSLIFTTALPPGTLGAIRKAIEIVKEDNERRERLIENGAYFRTHLQEAGFDIGNSSTHIVPIVVGSNENTLRFSERLQEVGIAAIAIRPPTVPVGSSRVRFAVTSQHTIADLKWAIQHIIRIGKEEGFLV | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | A9VG56 |
Q9ZPI5 | MFP2_ARATH | 3-hydroxyacyl-CoA dehydrogenase | Arabidopsis | MDSRTKGKTVMEVGGDGVAVITLINPPVNSLSFDVLYNLKSNYEEALSRNDVKAIVITGAKGRFSGGFDISGFGEMQKGNVKEPKAGYISIDIITDLLEAARKPSVAAIDGLALGGGLELAMACHARISAPAAQLGLPELQLGVIPGFGGTQRLPRLVGLTKALEMILTSKPVKAEEGHSLGLIDAVVPPAELVTTARRWALDIVGRRKPWVSSVSKTDKLPPLGEAREILTFAKAQTLKRAPNMKHPLMCLDAIEVGIVSGPRAGLEKEAEVASQVVKLDTTKGLIHVFFSQRGTAKVPGVTDRGLVPRKIKKVAIIGGGLMGSGIATALILSNYPVILKEVNEKFLEAGIGRVKANLQSRVRKGSMSQEKFEKTMSLLKGSLDYESFRDVDMVIEAVIENISLKQQIFADLEKYCPQHCILASNTSTIDLNKIGERTKSQDRIVGAHFFSPAHIMPLLEIVRTNHTSAQVIVDLLDVGKKIKKTPVVVGNCTGFAVNRMFFPYTQAAMFLVECGADPYLIDRAISKFGMPMGPFRLCDLVGFGVAIATATQFIENFSERTYKSMIIPLMQEDKRAGEATRKGFYLYDDKRKAKPDPELKKYIEKARSISGVKLDPKLANLSEKDIIEMTFFPVVNEACRVFAEGIAVKAADLDIAGIMGMGFPPYRGGIMFWADSIGSKYIYSRLDEWSKAYGEFFKPCAFLAERGSKGVLLSAPVKQASSRL | Involved in peroxisomal fatty acid beta-oxidation during seed germination. Possesses enoyl-CoA hydratase activity against long chain substrates (C14-C18) and 3-hydroxyacyl-CoA dehydrogenase activity against chains of variable sizes (C6-C18) . Possesses 3-hydroxy-3-phenylpropionyl-CoA dehydrogenase activity and is involved in the peroxisomal beta-oxidation pathway for the biosynthesis of benzoic acid (BA). Required for the accumulation in seeds of substituted hydroxybenzoylated choline esters, which are BA-containing secondary metabolites . Fatty acid beta-oxidation pathway in peroxisomes regulates gene silencing, histone acetylation and DNA methylation . | Q9ZPI5 |
B9M5B4 | ILVD_GEODF | Dihydroxy-acid dehydratase | Geotalea | MRSDMIKKGLERTPHRALLKGTGVPQSQMEKPFIGVATSFTDLIPGHVGMRDLERYIEKGIHSGGGYAFFFGIPGVCDGISMGHKGMHYSLPTRELIADMVESVAEAHRLDGLVLLTNCDKITPGMLMAAARLDIPCIVVTAGPMMSGRGEAGRKYSFVTDTFEAMARYKAGVIDAQELQVCEDNACPGMGSCQGLFTANTMAILTETLGMSLPRCGTALAVSALKRRIAFASGERIVDLVKDNVTPRSILTRAAFENAIRVDLALGGSSNTVLHLLAIAHEAEVELPLETFDILAKETPQLASMNPAGEHFMEDLDTAGGVAGVLMQLGDKIKDNPTVMGLTIKQLAASIANVDETVIRPLSNPVKKEGGIAILSGNIAPKGAVVKQSGVSAAMMNFTGTARCFDSEEAAMAAIMEGKIVAGDCVVIRYEGPKGGPGMREMLAPTAAIMGLGLGDSVALITDGRFSGGTRGPCIGHISPEAAEGGPIALVEEGDRIELDIPGRRLQLLVDDETLAKRRRNWQAPAPKIRTGWLARYAKVVTSANTGAVTSAD | 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. | B9M5B4 |
B1VAM3 | RS7_PHYAS | 30S ribosomal protein S7 | 16SrXII (Stolbur group) | MSRKGHIKKRDVNPDPIYNSKLVTKVINVIMQDGKKGKAQTIFYQALKKVQLMTKREPLEVFRDALNNIMPVLEVRTRRVGGQNYQVPSEIRPERRQSLGLKWLVKFTKQCNEKTMKDKLAKEIVDASLGHGVSVKKREETHRMAEANKAFAHYRW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | B1VAM3 |
B9KFR5 | CMOB_CAMLR | tRNA U34 carboxymethyltransferase | Campylobacter | MQDNALLKQALKHPLYEKIQKLNLKVQNSNYTIDDSFNIFCDEKLDEEIKNIALELKPWRKGPFKINKLFIDTEWQSFIKFNILKPYMQEIKGKVVADIGCNNGYYMFKMLEFNPSKLIGFDPSIKYFLQFFLLNSLAKTPIQYELLGVADVPNYGIKFDVIFCLGVIYHRSDPIAMLKQLKQSLNKDGVVFLDTMYIEDEREIALIPQKTYSKIPNIFFIPSILGLRNWCYRAGFSEFEVITTRQTDFEEQRKTQWIDSYSLDQFLDKNDSNLTCEGYEAPKRVYVKLKV | Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. | B9KFR5 |
B2S684 | RS12_BRUA1 | 30S ribosomal protein S12 | Brucella | MPTVNQLIRKPRTAPVKRNKVPALQANPQKRGVCTRVYTTTPKKPNSALRKVAKVRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHIIRGVLDTQGVKNRKQRRSKYGAKRPK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | B2S684 |
B9DVQ2 | Y1611_STRU0 | Nucleoid-associated protein SUB1611 | Streptococcus | MMNMQNMMKQAQKLQKQMEQKQADLAAMTFVGKSAQDLVTATFTGDKKMVSIDFKEAVVDPDDMETLSDMTTQAINDALAQIDEATKKTMGAFAGKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | B9DVQ2 |
Q6PQZ1 | AQP1_PIG | Water channel protein for red blood cells and kidney proximal tubule | Sus | MASEFKKKIFWRAVVAEFLAMTLFIFISIGSALGFQYPVRNNQTSGAAQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISVLRAVMYIIAQCVGAIVATAILSGITSSLPGNSLGLNSLAPGVDSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGFSVALGHLLAIDYTGCGINPARSFGSAVITHNFQDHWVFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDGDDINSRVEMKPK | Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Q6PQZ1 |
Q8HVV8 | NDHI_AMBTR | NADH-plastoquinone oxidoreductase subunit I | Ambrosia | MFPMVTEFMNYGQQTVRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRVPMSIIDDYTIRTILNLPEIKT | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | Q8HVV8 |
Q6L1F5 | DTDA_PICTO | D-tyrosyl-tRNA(Tyr) deacylase | Picrophilus | MDLIIASRMDEASMLMAEKIIDLYDFNRLNENEYQKDGFKLMFIDDLHIYHNMEKLDFDTLIFLSRHSSSAGVKSLTVHSIGNYRKAELGGYDNKTVLSAPYEMSSSLRSIKELYNDDGYNITFEATHHGPYTKNRSYFIEIGTSGEDWHNDKILEIMARSVIEKNVKRFRSGIGIGGGHYAPKISDYFFNNDINIGHIIPKYVSETIKDNQIIESIENTENCSFILIDWKGSPSRLRSLALDAADKCSLELIKI | D-aminoacyl-tRNA deacylase with broad substrate specificity. 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. | Q6L1F5 |
A6QR20 | SLF1_BOVIN | BRCT domain-containing protein 1 | Bos | MEDDAPKHIIQMTGFKVEEKEALGKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAQSGRWLDETTYEWGYKIEKDSHYSPQMQSAPKRWREELKRTGAPGAFHKWKVVLLVRADKRSDSLVRVLEAGKANVILPKNSPTGITHVIASNARIKAEQEKDDFKAPFYPIQYLEDFLLEKEIHNDEDSQTNSTWKNHSSQEKSNDFRENMGFLEMKGTLKETMCRTQKEMKNHDEDVTISSILTEHQSKERFRDSRKNLKFVKMRNALGRHTYRNQEMKKKDEDIQSIYTLRKKRKKEKERDSRKDIEHDRSTLRKHIYRDQKERKNSVFAGHAKESKTKDIRTNVDIVDLKNALRKHIYRAQAVRYRGIRIDKQPAYNVEVKNAEFPRGILNLIESLIEGQFFKEAIEELSSLQAHYIPPVYLLHALLENILQDNIDTFSGRYFHILSALLHLHPPWKSPAMSTYYLELFQCPTCMKGTWSLIEVLIRSCLFNESFCHQISENIIGSKVLHLTLLKFFFNLIESEVRHLSQKLYDWSDSQSLKITGKAVLLEIFWSGNETSGLLTKPVNMLLEWTIYSHKEKCKSNDVFRHELAYLLTGILGAAIDYWIVLGLNMGRNVMRHMSDDVGSYVSLSCDDFSSQDLEIFISSFSSSWLQMFVAEAVFKKLCLQNSISISSEPLSLQKMVYSYLPALGKTGVRGTRKMQKPKKIGLRPCFESQRALIMLNGAKQKQGEGLPEIPELNLAKCSSSLKRLKKKSEGELSCSKENCPSLVTKINFHKTNLKGETALHRACINNQVDRLILLLSMPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHGGPVLLQQRNSKGELPLDYVVSSQIKEELFAITKIEDTVENFHAQAEKHFYHQQLEFGSFLLSRMLLNFCSIFGLSSESLAFKGLTHLSELLIACQNYKETTSVHTDWLLDLYARNIMTLQKLPNALKELPENVKVCPGVHTEALLVTLEVMCRSVTEIS | Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions. | A6QR20 |
Q6D7I5 | KDPC_PECAS | Potassium-translocating ATPase C chain | Pectobacterium | MRYLRSSLFLFLLLLLVTGLAYPLLTTVLAQWLFPTQANGSLIYRDNAVVGSSLIGQSFSRTGYFQGRPSATSDAPYNALASGGSNLAASNPALDKQIGERAAYWHQAVSNQQPIPAELLTASGSGLDPQISPEAARYQALYVAQARGMSLQQIQQLIDRFTETSKPTFIGQPTVNVLLLNLALDEEKPLP | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex. | Q6D7I5 |
D3UAG5 | 88F1R_MALDO | UDP-glycosyltransferase 88F1 | Malus | MGDVIVLYASPGMGHIVSMVELGKFIVHRYGPHKFSITILYTCGSIVDTASIPVYIRRISHSHPFISFRQFPRVTNNITRNISVPAITFDFIRQNDPHVRSALQEISKSATVRAFIIDLFCTSALPIGKEFNIPTYYFRTSGAAILAAFLYLPKIDEQTKTTESFKDLRDTVFEFPGWKSPLKATHMVQLVLDRNDPAYSDMIYFCSHLPKSNGIIVNTFEELEPPSVLQAIAGGLCVPDGPTPPVYYVGPLIEEEKELSKDADAAEKEDCLSWLDKQPSRSVLFLCFGSMGSFPAAQLKEIANGLEASGQRFLWVVKKPPVEEKSKQVHGVDDFDLKGVLPEGFLERTADRGMVVKSWAPQVVVLKKESVGGFVTHCGWNSVLEAVVAGVPMIAWPLYAEQHMNRNVLVTDMEIAIGVEQRDEEGGFVSGEEVERRVRELMESEGGRVLRERCKKLGEMASAALGETGSSTRNLVNFVSSIT | Glycosyltransferase that possesses phloretin 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Is specific for phloretin and does not possess glycosyltransferase activity toward caffeic acid, catechin, chlorogenic acid, 2-coumaric acid, 3-coumaric acid, 4-coumaric acid, cyanidin, 3,4-dihydroxyhydrocinnamic acid, epicatechin, 3-hydroxybenzoic acid, naringenin, 3,4-dihydroxybenzoic acid, quercetin and rutin. Can glycosylate phloretin in the presence of UDP-glucose, UDP-xylose and UDP-galactose. | D3UAG5 |
Q8LG10 | GAT15_ARATH | GATA transcription factor 15 | Arabidopsis | MLDPTEKVIDSESMESKLTSVDAIEEHSSSSSNEAISNEKKSCAICGTSKTPLWRGGPAGPKSLCNACGIRNRKKRRTLISNRSEDKKKKSHNRNPKFGDSLKQRLMELGREVMMQRSTAENQRRNKLGEEEQAAVLLMALSYASSVYA | Transcriptional regulator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. | Q8LG10 |
Q80ZG1 | RIC8A_RAT | Protein Ric-8A | Rattus | MEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITFDSVKREVDEEDAALYRYLGTLLRHCVMADRAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSRMRTPTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRLIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD | Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation. | Q80ZG1 |
A5UCY6 | ENGB_HAEIE | Probable GTP-binding protein EngB | Haemophilus | MSEIKLNYHKTHFLTSAPNIRSIPEDTGIEIAFAGRSNAGKSTALNALTNQKNLARTSKTPGRTQLINLFEVEPNYKLVDLPGYGYAAVPEQMKIQWQKSLGEYLQKRECLSGLVVLMDIRHPLKDLDQQMIEWAVSADLPILLLLTKADKLSQSARSKQVKMVREAILPFQGDIQVEAFSAQNKIGIDKLAAKLDFWFSPLFAK | Necessary for normal cell division and for the maintenance of normal septation. | A5UCY6 |
Q6D163 | GLNE_PECAS | Adenylyl transferase | Pectobacterium | MSILPLPALPVLLTEQSQRALSRLREAAPDEPITDSDSAVLALSDFVSDALALHPDWWQGIHQQPPQPEEWQHYADWLSNALVDVNDENALMAALRRFRRHMLARIAWSQALQTSTTEHSLRQLSELAEVIIVAARSWLYQVCCHEWGTPCNAKGVAQPLLILGMGKLGGGELNFSSDIDLIFVYPENGHTQGGRRELDNAQFFTRLGQRLIKVLDQPTVDGFVYRVDMRLRPFGDSGPLVLSFAAMEDYYQEQGRDWERYAMVKARLMGGMDDAYSQELRSTLKPFVFRRYIDFSVIQSLRNMKGMIAREVRRRDLRNNIKLGAGGIREIEFITQVFQLIRGGREPGLQGRSLLPTLQHVGALGLLTPQQVLDLSTSYLFLRRLENLLQAIADEQTQTLPSDELNQQRLAWGMGFDSWDTLQSMLSQHMQAVRHVFDELIGDDAPDNNDIPEHSSYSSLWQDTLDDGDLAPLTPHLTETVREKLMRTIVEFRNDVAKRTIGPRGRDVLDQLMPCLLAEVCARQEADTVLSRLTPLLLGIVTRTTYLELLLESRAALAQLIRLCAASPMVASQLARYPLLLDELLDASTLYQPTAPGAYADELRQYLMRVPEDDEEQQLEAVRQFKQSQQLRIAAGDIGGVLPVMKVSDHLTYLAEAIIAAVVQQAWGLMVERYGQPSHLQHREGRGFAVIAYGKLGGWELGYSSDLDLVFLLDCPSDVMTDGERSIDGRQFYLRLAQRVMHLFSTRTSSGILYEVDARLRPSGAAGMLVSTVEAFDDYQRNEAWTWEHQALVRARMVYGESGVQQTFESIRRSILCAERDADTLRTEVREMREKMRQHLANKDKSRFDIKTDAGGITDIEFITQYLVLRYAAQEPRLTHWSDNVRILELMAQYGVMEESEANALKLAYVTMRNELHHLALQELSGRVSKDRFVAEREQVLVSWNKWLMGA | Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. | Q6D163 |
P10620 | MGST1_HUMAN | Microsomal GST-I | Homo | MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAKKYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL | Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity. | P10620 |
Q1LSL0 | TRUB_BAUCH | tRNA-uridine isomerase | Candidatus Baumannia | MCFSLNINSHNINGIILLDKQEGLSSNYLLHKVKRLFRVQKAGHTGALDPLASGMLPICLGEATKFSKYLLDADKRYIVSAKLGEKTNTYDATGIIINTRPVTINQAMIEHIMEQFYGDIYQIPPMFSSIKYQGRALYKYARKGINIPRSARLVHIYNLQILDWDNTHIELQIHCSKGTYIRTIIDDIGELLGCGAHVTMLRRLAVAHYHTARMITLESLQTAITLALRQTPNTLVQLNKLLLPIDSAVANFPAIKLSKDSVARVRKGQMVAVDQCWQSGLVRMCENKGETTYFFGIGEITQPGVLKPKRLLAEKYV | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q1LSL0 |
Q2RVG7 | EFP_RHORT | Elongation factor P | Rhodospirillum | MKMQANQIRPGQVLEHQGKRWTVLKIQLIQPGKGGAFIAVEMRDVDSGNKTNERWRTADTVERLEVREIDCQYLFKDDTGYTFMDKETFEQFSMAADALGEQAGFLQESMEVTVDCIEGSPVSVNLPSQVILQVVEADAVVKGQTASSSYKPGLLENGMKVMIPPFIEAGTRIVVSTVDCSYIERAK | 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. | Q2RVG7 |
B5EXA8 | LLDD_SALA4 | L-lactate dehydrogenase | Salmonella | MIISAASDYRAAAQRTLPPFLFHYIDGGAYAEYTLRRNVEDLSQVALRQRVLKNMSDLSLETTLFNETLSMPVALAPVGLCGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYWQAVMHPKWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAYLYALATAGKAGVANLLDLIEKEMKVAMTLTGAKSISEISGDSLVQELGKSLPAALAPMSKGDAA | Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain. | B5EXA8 |
Q3K6Y7 | HEMH_PSEPF | Protoheme ferro-lyase | Pseudomonas | MTDHALLLVNLGSPASTSVADVRRYLNQFLMDPYVIDLPWPVRRLLVSLILIKRPEQSAHAYASIWWDEGSPLVVLSRRLQQQMKAQWTHGPVELAMRYGEPSIETNLLKLVAAGHKRITLAPLYPQFADSTTTTVIEEAKRVVREKKLDVQLSVLQPFYDQPEYLDALVASARPHLQQDYDHLLLSFHGLPERHLTKLDPTGNHCFKNEDCCKNASAAVLATCYRAQCLRTAALFAERMGLPDGKWSVSFQSRLGRAKWIEPYTEARLDELAKSGVKKILVMCPAFVADCIETLEEIGDRGKEQFREAGGEELVLVPCLNDDPQWAKALATLCERAPLAL | Catalyzes the ferrous insertion into protoporphyrin IX. | Q3K6Y7 |
B0KC91 | PANC_THEP3 | Pantoate-activating enzyme | Thermoanaerobacter | MIVTDKISNVRNIIKEQKLSGKKIGLVPTMGYLHEGHLSLVRIAKKHSDFVAVSIFVNPIQFGPNEDFDRYPRDLERDLKLLEKEGCDLVFAPSVEEMYPSELLTTVNVDKITEKLCGAFRPGHFKGVTTVVAKLFNIFTPDIAVFGQKDAQQVAVIKKMVEDLNFPVEIIKAPIVRESDGLAMSSRNVYLNPEERKAALILSKSLKEAEKLLLNGERNANTIIKKVNEVLNSEPLCKVQYVSCVHPDTLEDLTYIKDKALIAIACFIGTTRLIDNLLWGENI | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | B0KC91 |
Q46LU1 | GLGA_PROMT | Starch [bacterial glycogen] synthase | Prochlorococcus | MRILFAAAECAPMIKVGGMGDVVGSLPPALKKLGHDVRLIIPGYGKLWTLMDIAPEPIFRSNTMGVDFSVFETKHPSNGLPIYLVGHPCFDSERIYGGEDEDWRFTFFASAVSEFAWNSWKPQVLHCHDWHTGMIPVWMHQDPEISTVFTIHNLKYQGPWRWKLDQITWCPWYMHGDHTMASAMLYADRVNAVSPTYSREIRTSEYGEKLEGLLNYISGKLRGILNGVDLDEWNPATDNSLPAKFSVDNISGRAINKRVLQERMGLEVNPDKYLMGMVGRLVDQKGIDLLLQVANRLLSYTDSQVVVLGTGDRYLESSLWQLAIEYPGRFSVFLTYDDALSRLIYGGADAFLMPSRFEPCGISQLLAMRYGAIPIVRKVGGLVDTVEPYNPMNETGSGFCFDRYEPIDFYTSLVRSWEEYRHQKSWKQLQLRAMSNKYSWDRSAKEYELMYKDVCGIKEPSPDAAEVEKFSYGQEADPSRKGKKIKL | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | Q46LU1 |
Q5LIJ3 | MURE_BACFN | UDP-N-acetylmuramyl-tripeptide synthetase | Bacteroides | MKLKEILTSIQPVKITGNQDIEITGVDIDSRQVESGHLFMAMHGTQTDGHAYIPAAVEKGATAILCEELPAELAEGVTYIQVADSEDAVGKAATTFYGNPSSKLELVGVTGTNGKTTIATLLYNTFRYFGYKVGLISTVCNYIDDEAIPTEHTTPDPITLNRLLGRMADEGCKYVFMEVSSHSIAQKRISGLRFAGGIFTNLTRDHLDYHKTVENYLKAKKKFFDDMPKNSFSLTNLDDKNGLVMTQNTKSKVYTYSLRSLSDFKGRVLESHFEGMLLDFNNHELAVQFIGKFNASNLLAVFGAAVLLGKKEEDVLVALSTLHPVAGRFDAIRSPQGYTAIVDYAHTPDALVNVLNAIHGVLEGKGKVITVVGAGGNRDKGKRPIMAKEAARASDRVIITSDNPRFEEPQDIINDMLAGLDTEDKKKTLSIADRKEAIRTACMLAEKGDVILVAGKGHENYQDIKGVKHHFDDKEVLKEIFSLTV | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q5LIJ3 |
Q5HAA6 | COXX_EHRRW | Heme O synthase | Ehrlichia | MGIQSSTMKLPLIHEISDYWHLLKPKIMYLVVLTGVTGIIIAPGNIHPLIAVISTLCIALGSGAAGAINMWYDSDIDALMTRTKTRPIPAGKISRSSALEVGLVLSFISVTIMMIAVNYISGILLAISIGFYIYVYTMYLKRRTPQNIVIGGAAGALPPIIGWTSVTGSISIESLVLFLIIFMWTPPHFWALSLLNYHEYEKAKIPMLPVTHGIFTTKIHILVYSILLFPITLLPGLFLKDPVLYEITAIPLGLMFVVQAFQVFKSSISYHYRVMFTYSIIYLFILFTCIMLSSF | 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. | Q5HAA6 |
Q7SY06 | HACD3_DANRE | Protein-tyrosine phosphatase-like A domain-containing protein 1 | Danio | MSALTPHVYWAQRHGEIYLRVEISDAQDLSIGVEENILQFRGQGHGAKGENEYEFSLEFLKPVKPEVKHKSTQRQVNITVRKQEEVWWNRLTKQEKKPLFLAPDFDRWLDESDAEMELREKEEKINKVSFESRVRKDPFLGLKKGFLFMYNLVQFLGYSWIFVNMTVRLFILGQDSFYDTFHTIADVMYFCQMLAIMEVINPAVGLVKTGVMPAFIQVMGRNFILFVIFGSLEDMQNKPVVFFVFYLWSTIEIFRYPFYMLACIDTEWKLLTWLRYTIWMPLYPLGVLAEAVAVIQSIPIFDETKLLSIPLPKATGLSLSFSYILQLYLVVMFLGLFINFRHLFKQRTRRFRTKKRKAN | Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Involved in Rac1-signaling pathways leading to the modulation of gene expression. | Q7SY06 |
Q2S3F9 | RUVB_SALRD | Holliday junction ATP-dependent DNA helicase RuvB | Salinibacter | MSTSRSDALKAEADRSDNDVEKLLRPQSLDEFVGQEKIKENLNVFMKAALQRGETLDHVLLSGPPGLGKTTLAHIIANEMGARIRTSSGPVLEKPADIAGVLTNLEEGDLLFIDEIHRLSSVVEEYLYSAMEDYRIDIVIDQGPNARTVQIDLPPFTMVGATTRKGLLTAPLRARFGIDFRYDYYTADLLQEITQRSARILDVETTPDGAYEIARRSRGTPRVANRLLRRTRDFAEVEGDGEITKAIADRALNALDVDEEGLDDMDARILLTLIDNFDGGPTGLKNLAVSVGEESGTLEEVYEPYLIQEGFMERTPQGRVALQRAYDHFDRSSPAADQDLFDQE | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | Q2S3F9 |
Q6YXH5 | ZHD1_ORYSJ | null | Oryza sativa | MDFDDHDDGDEEMPPMPVSSSYETPPQHGLAGGGMAPKPPGEIGSRVKGPSCGGGRYRECLKNHAVGIGGHAVDGCGEFMAAGEEGTIDALRCAACNCHRNFHRKESESLAGEGSPFSPAAVVPYGATPHHQFSPYYRTPAGYLHHHQHHMAAAAAAAAAAAGGYPQRPLALPSTSHSGRDDGDDLSGMVGPMSAVGPLSGMSLGAGPSGSGSGKKRFRTKFTQEQKDKMLAFAERVGWRIQKHDEAAVQQFCDEVGVKRHVLKVWMHNNKHTLGKKLP | Putative transcription factor. | Q6YXH5 |
P80916 | ACP_ACICA | Acyl carrier protein | Acinetobacter calcoaceticus/baumannii complex | MSDIEQRIKQAVAEQLGMRAEEIKNE | Carrier of the growing fatty acid chain in fatty acid biosynthesis. | P80916 |
A0ZZZ0 | OBG_BIFAA | GTP-binding protein Obg | Bifidobacterium | MSDFVDRVTVHVKGGDGGNGSAGIRREKYKPLAGPNGGNGGDGGSVIFMADSNANSLLDYRFMPHREAESGTMGLGDTKDGSKGADLILPVPVGTVVFEAKGPQGKPKHPGEQLADLRHAGDKFVVAAGGNGGLGNAALANRTRRAPGFALLGEPGEERDVILELKSIADVALVGFPSAGKSSLIAAMSSAKPKIADYPFTTLVPNLGVVVAGDMRYTIADVPGLIPGASQGKGLGLEFLRHIERTEIIAHVIDCATLEPGRDPMSDYQALEHELAEYAGKLELPLGAIPIPERPRIIILNKVDVPEAKELAEFVKPEFEKLGLKVHIISTASHEGLKELNWALADLVTNMRAEVAKREQAEEEARVVIKPLEEPRNRRRRNDEGGNALDFTVERKENGNGEVWYEVLGTKPERWVMQTNFDNDEAVGYLADRLAKLGVEDELRHKGAKPGDEVRIGRGDRAVEFDWDPTIAAGAEMLDGTQLGARGVDLRLQESDGRAQRRSNTERRRQYHEMMDARQAVREAMMAERKAGHWADPSVDDDRHDETSLFGRGETADDEDVEQ | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | A0ZZZ0 |
Q85FX7 | PETN_CYAM1 | Cytochrome b6-f complex subunit VIII | Cyanidioschyzon | MHLDLISITWGCLMATFTASLALVIWARNGL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | Q85FX7 |
A0JN80 | DI3L1_BOVIN | DIS3-like exonuclease 1 | Bos | MLQKREKVLLLRTFHGRTLRIVREHYLRPSVPCNSPLCPQPATCHNDGKLLSSDVTHYMVPDWKVVQDYLEILEFPELKGIVFMQTACQAVQHQRGRRQYNKLRNLLKDARHDCVLFANEFQQSCYLPRERGESMEKWQSRSIYNAAAWYYHHCQDRMPIVMVTEDEEAIQQYGSETGGVFVISFKNYLDNFWPDLKAAHELCESILQSRRERENESQESHGKEYPEHVPLEVLEAGIKSGRYIQGTLNVNKHRAQIEAFVRLQGASSKDSDLVSDVLIHGMKARNRSIHGDVVVVELLPKSEWKGRTTALGENDGDDKALGESPSEPMPTGRVVGILQKNWRDYVVTFPSIEEVQSQGKNAQKILVTPWDYRIPKIRISTQQAEALQDFRVVVRIDSWESTSMYPNGHFVRVLGRIGDLEGEIATILVENSISVVPFSEAQMCEMPVNTPENPWKVSSQEEREREDLRKTHLVFSIDPSGCEDVDDTLSVRALDNGNLELGVHIADVTHFVAPHSYIDIEARTRATTYYLADRRYDMLPAILSADVCSLLGGVDRYAVSVMWELDKTSYEIKKVWYGRTIIRSAYKLFYEAAQDLLDGNFSVVKDIPEFKDLDEKSRQAKLEELVWAIRKLTDIARHIRAKRDSCGALELEGVEVRIQLDEKKNIHDLIPKQPLEVHETVAECMILANHWVAKKIWESFPHQALLRRHPPPHQEFFSELRECAKAKGFFIDTRSNKALADSLDNANDPNDPIVNKLLRSMATQAMSNALYFSTGSCAEEEFHHYGLALDKYTHFTSPIRRYSDIIVHRLLMAAISKDKKMEIQENLFSNKDLEELCRHINNRNRAAQHSQKQSTELFQCMYFKDKDPETEERCISDGVIYSIRTNGVLVFIPRFGIKGAAYLRNKDGLVVSCGPDGHSEWKPGSLQRFQNKITCTTTGGESVTFHLFDHVTVRISVQTSRCHSDTIRLEIISNKPHMTPDTELLQQCSLLLKSDLVKEVTRSVEEAQLAQEVAVNITEDYQKYCQTKGRSLYTLLEEIRDLALLDVSNSYGI | Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. | A0JN80 |
Q8RXG3 | M2K5_ARATH | Mitogen-activated protein kinase kinase 5 | Arabidopsis | MKPIQSPSGVASPMKNRLRKRPDLSLPLPHRDVALAVPLPLPPPSSSSSAPASSSAISTNISAAKSLSELERVNRIGSGAGGTVYKVIHTPTSRPFALKVIYGNHEDTVRRQICREIEILRSVDHPNVVKCHDMFDHNGEIQVLLEFMDQGSLEGAHIWQEQELADLSRQILSGLAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLNHGRYDGYAGDVWSLGVSILEFYLGRFPFAVSRQGDWASLMCAICMSQPPEAPATASQEFRHFVSCCLQSDPPKRWSAQQLLQHPFILKATGGPNLRQMLPPPRPLPSAS | Mitogen-activated protein kinase kinase (MAPKK) which regulates abscisic acid (ABA) responses in a MAPKKK20-MKK5-MPK6 cascade involved in root growth (e.g. root cell division and elongation) and stomatal response, probably via MAPK6 activation by protein phosphorylation . Involved in the second phase of hydrogen peroxide generation during hypersensitive response-like cell death. Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. Activates by phosphorylation the downstream MPK3 and MPK6. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the guard mother cell (GMC) is specified. This MAPK cascade also functions downstream of the ER receptor in regulating coordinated local cell proliferation, which shapes the morphology of plant organs. MKK4 and MKK5 participate in the regulation of floral organ abscission. Target of the Pseudomonas syringae type III effector HopF2, that inhibits the activation of the downstream MPK6 and PAMP-triggered immunity. Plays a critical role in high light stress tolerance by the mediation of the Cu/Zn SODs CSD1 and CSD2 gene expression. Phosphorylates BZR1 in vitro. | Q8RXG3 |
Q48V07 | NRDI_STRPM | Protein NrdI | Streptococcus | MAELIIVYFSSKSNNTHRFVQKLGLPAQRIPVDNRPLEVSTHYLLIVPTYAAGGSDAKGAVPKQVIRFLNNPNNRKHCKGVISSGNTNFGDTFALAGPIISQKLQVPLLHQFELLGTATDVKKVQAIFARLKHHTHDKQKQINNLITERTHPCHKPMRHTSH | Probably involved in ribonucleotide reductase function. | Q48V07 |
Q2FZ95 | FTSL_STAA8 | Cell division protein FtsL | Staphylococcus | MAVEKVYQPYDEQVYNSIPKQQPQTKPEKKTVSRKVVVQLTKFEKVLYITLITVIAMLSIYMLSLKMDAYDTRGKIADLDYKIDKQSSENSALQSEIKKNSSYERIYEKAKKQGMSLENDNVKVVRSNGEAKN | Essential cell division protein. | Q2FZ95 |
Q728G0 | HTPG_DESVH | High temperature protein G | Desulfovibrio | MATAPASHAFRTEVRKMLHIITHSLYTNREIFLRELVSNASDALDKLRFIRSRGDAVVAPDLAPGIDISVDKEARILTIADTGVGMTRQELMDNLGTIARSGSEQFVADLAAAENAKDADAASIIGRFGVGFYAVFMVADRVEVTSRSYIEGEAAHTWTSDGLGEFTVEEATGDIPQRGTVIKAHLREDAAEFLEKYRIEGILRKHSQFISFPIRVDGEQVNTTPALWREPKFSITDEQYADFYKHLTFDTEAPLRTLHVSVDAPVQFTGLVFVPPHGQEVFSMGRDRWGLDLYVRRVLIQRENKDLLPEYLGFLKGIVDTEDLPLNISRETLQENVVVRKIGQTLTKQVLADLARLAADDAEAYATFWRQHGKVFKLGYSDYANREKFAPLLRFNSSHHDDAQGLTSLDDYISRAREGQKEIWYIAAPGREAARLDPRVEVFRRKGLEVLYLLEPIDEFVLETLDSYSDFSFKAVEHADGEKLAQFEDTGPARDVTPLTEDEDAAFARLIERMKALLGDAVEDVRISHRLADSPACLVQPGGASTSSMDRLLRVLHKDESVPRKVFEVNRDHPILRNLLKVFTSDASDPLVEDTTRQLFATSLMLDGYLKDPHELAAMMHRLMEKSGDWYKAVRGL | Molecular chaperone. Has ATPase activity. | Q728G0 |
A5CS07 | RUVA_CLAM3 | Holliday junction ATP-dependent DNA helicase RuvA | Clavibacter | MISSLRGTVLSVSGQTLLLEVHGVGYGVSVTPRHALELRNGSEATVLTSLVVREDSLTLFGFPGPDELRAFELLCGVTGVGPKSALAVLEHLDPEAMAQAVAAEDDAAFRRVSGIGPKTAKLIVLQLAGKLFVTQPRARSATSAASTVTADVVTALIGLGWSERVARTAVDDAAAAAADQGLPADMPRLLRVALGMLGPQQPAGAAPTGQAADR | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | A5CS07 |
C1BYA3 | MTNB_ESOLU | APAF1-interacting protein homolog | Esox | MVSSQEKMASISDIIQKDEDSGSEKTESQDKEHPRVLIPELCRLFYKLGWVTGTGGGISLRHGDQIYIAPSGVQKERLQPEDMFVCDVEERDICVPPAWKNLKKGQCTPLFMNAYTMRAAQAVIHTHSKAAVMATLFYPGKEFRITHQEMIKGIRKCTSGTNYRYDETLVVPIIENTPEEQDLKERMALAMEQYPESCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVKMKQCGLDPSAQPVEENLYYYVQQA | Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway. May play a role in apoptosis. | C1BYA3 |
P0AGE3 | SSB_SHIFL | Single-stranded DNA-binding protein | Shigella | MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF | Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | P0AGE3 |
Q7RVM2 | ARF_NEUCR | ADP-ribosylation factor | Neurospora | MGNTLSIFGKLFDGLFGKKEMRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNIQFTVWDVGGQDKIRPLWRHYFQNTQGIIFVVDSNDRDRVVEAREELQRMLNEDELRDALLLVFANKQDLPNAMNAAEITDKLGLSSLRQRSWYIQATCATTGDGLFEGLDWLSTELKKKSP | GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. | Q7RVM2 |
P49208 | RK1_PEA | CL1 | Pisum | IPLFLHLLLMSRKLLMKRRTKVVRRMNLMLLLTLLLSPLSLRQGKLHWRLKSDRVRSKRFLEIQKLRELKKEYDLKTAISLVKETAKTKFVETVEAHFRLNIDPKYNDQQLRATVSLPKGTGKPIKVAVLTQGERFDEAKNAGADLVGGEDLIEQIKGGFMEFDKLIASPDMMPKVASLGKILGPRGLMPNPKAGTVTANIPQAIAEF | This protein binds directly to 23S ribosomal RNA. | P49208 |
Q46ZI7 | DER_CUPPJ | GTP-binding protein EngA | Cupriavidus | MKPVIALVGRPNVGKSTLFNRMTRSRDALVADLPGLTRDRHYGEGRIGDRPFIAIDTGGFEPVVKEGIVAEMAKQTRQAVVEADVVIFIVDGRLGLAPQDRAIADYLRKTGRRVMLAVNKAEGMKYTSVAADFYELGMGDPYAISAAHGDGVRELVDEALELAVQERPELAEEDADSGKGVKIAIVGRPNVGKSTLVNTLIGEERVIAFDMPGTTRDAIYVEFERGGKPYTLIDTAGLRRRGKVFEAIEKFSVVKTLQSIADANVVILLLDAQQDISDQDAHIAGFIVESGRALVVGVNKWDGLDGHTRDRIKHDLERKLQFLSFANFHFVSARERTGIGALMRSVDDAYAAAMVKLPTPQLTRVLQEAVEFQQPKRAGVSRPKLRYAHQGGSNPPIIVIHGNALSSVSETYRRYLENRYRAAFKLKGTPLRIEFRTNKNPYADSKD | GTPase that plays an essential role in the late steps of ribosome biogenesis. | Q46ZI7 |
Q09147 | FGFR2_DROME | dFGF-R1 | Sophophora | MAKVPITLVMIIAIVSAAADLGCDYGHHRCYIDVTVENSPRQRHLLSDMDITLQCVRPMAKWFYEDKFQLRATLLRLERAQSGNSGNYGCLDSQNRWYNISLVVGHKEPVGNDIASFVKLEDAPALPESDLFFQPLNESRSLKLLQPLPKTVQRTAGGLFQLNCSPMDPDAKGVNISWLHNDTQILGGRGRIKLKRWSLTVGQLQPEDAGSYHCELCVEQDCQRSNPTQLEVISRKHTVPMLKPGYPRNTSIALGDNVSIECLLEDSALEPKITWLHKGNADNIDDLLQRLREQSQLPVDVTRLITRMDEPQVLRLGNVLMEDGGWYICIAENQVGRTVAASYVDLYSPSDTTTVRTTTTTTVASPIPTASTGEDNDDDVENPAAEASGGVGPPVFRKELKRLQHSLSGNTVNLACPVYGKANITWTKDKKPLNRELGVYVQKNWTLRFVEATSEDSGLYNCKVCNAWGCIQFDFSVQINDRTRSAPIIVVPQNQTVKVNGSLVMKCTVYSDLHPTVSWKRVVLKNASLDGLKSVEIQNLNFTVTNDSVVLTLRNVTFDQEGWYTCLASSGLGRSNSSVYLRVVSPLPPLEIYALLHAHPLGFTLAAITIVALFLLGSAFITFMLRRLRREKLLKLRIETVHQWTKKVIIYRPGGEEGSGCSSGDLQMPVIRIEKQRTTVSTTGTGGTDPAQGFNEYEFPLDSNWEIPRQQLSLGSILGEGAFGRVVMAEAEGLPRSPQLAETIVAVKMVKEEHTDTDMASLVREMEVMKMIGKHINIINLLGCCSQGGPLWVIVEYAPHGNLKDFLKQNRPGAPQRRSDSDGYLDDKPLISTQHLGEKELTKFAFQIARGMEYLASRRCIHRDLAARNVLVSDGYVMKIADFGLARDIQDTEYYRKNTNGRLPIKWMAPESLQEKKYDSQSDVWSYGVLLWEIMTYGDQPYPHILSAEELYSYLITGQRMEKPAKCSLNIYVVMRQCWHFESCARPTFAELVESFDGILQQASSNPNDAYLDLSMPMLETPPSSGDEDDGSDTETFRETSPLRYQYTYKFN | May be required for patterning of muscle precursor cells: generation of mesodermal and endodermal layers, invaginations of various types of cells, and CNS formation. Essential for the ability of the migrating tracheal and midline cells to recognize external guiding cues. | Q09147 |
A0A0G2K6Z9 | ODAPH_RAT | Odontogenesis-associated phosphoprotein | Rattus | MAPGFHFSWLLVSWLVVTTVKGQDVMTPPGSQNNVNPTDCQIITLTPPPTTRNQLTRAQPVTRTPTFYFPPRRPGFYPRFPNIPFFPPNNRRFQLWPFYPPRGRLIPWRFFLGRRQLQSSSSEESLE | May promote nucleation of hydroxyapatite. | A0A0G2K6Z9 |
P43619 | NADC_YEAST | Quinolinate phosphoribosyltransferase [decarboxylating] | Saccharomyces | MPVYEHLLPVNGAWRQDVTNWLSEDVPSFDFGGYVVGSDLKEANLYCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPSKNDSGKIVVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARSTGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKWNGKKHFLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKLAH | Involved in the catabolism of quinolinic acid (QA). | P43619 |
Q9ZMQ6 | ALF_HELPJ | Fructose-1,6-bisphosphate aldolase | Helicobacter | MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASEGAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIEDNISVDEKDAVLVNPKEAERFVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAIPDDVRKSYLDAGGDLKGSKGVPFEFLQESIKGGINKVNTDTDLRIAFIAEVRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | Q9ZMQ6 |
A1RVE1 | AROB_PYRIL | 3-dehydroquinate synthase | Pyrobaculum | MRRFFYRHTRGVTEVVVGRGLPYGEYIERPVVLAEEGLRPPIPGAPTLVLRGGEEVKSLEVLTKVYSFLKEVGADRSTTLVAVGGGALLDLATFAAGTYMRGIRLVHIPTTLLAMVDAALGGKGAVDWGPVKNLVGVFYQPAAILCDLSWLETLPERVYRSAFAEVVKYGLALDGDFYSWVRENAKALLARDWGALEYAVYRSLQLKAGVVEVDEFEERGIRQVLNVGHTVGHAVERVLGLLHGEAVAVGIVAELRLSSELGYLRESHVAEAAEVLSSLGLPTSVKATEQQLAEAAALVKFDKKRRGGHIYIPLVVRPGRWILEKIAVEEVEKAVRYVLHQGG | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | A1RVE1 |
Q8EER2 | LOLA_SHEON | Outer-membrane lipoprotein carrier protein | Shewanella | MKKLLCAVLLSPLLYSNAVLADDAKQLRETLTGTESLKADFKQTVTDVNKKVIQSGAGVFALAHPNQFYWHLTAPDESKIVADGKDLWIYNPFAEEVVIMDFTQAITASPIALLVHRDDATWSQYAVTKKQDCYEIKPKATDAGISAVNVCFNKGTLNKFNVLDDKGNLSQFDLSNQHSISTGDKALFKFVLPDNVDVDDQRIKTQ | Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Q8EER2 |
Q2S2H7 | PLSY_SALRD | Lysophosphatidic acid synthase | Salinibacter | MWSLTVILLISYFLGSIPGALWSSKALHGVDIRNHGSHNCGATNAFRVVGWQAGALATVVDFGKGFLAAGVVASVIRIDPIPSGLSLFGGDPFVVLGLLAGVGAVIGHMYPIFARFEGGKGVNTAAGMLFALTPLTMAITLAVFVAVLLSSRYVSLSSITAAVAFPTIVALRRFGFGADLDPSLLVFGGLLALSIVVAHRSNIQRLLNGTESQISSFEPAQGMLGRGEL | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q2S2H7 |
B2VL52 | SECB_ERWT9 | Protein-export protein SecB | Erwinia | MSEQNNTEMSFQIQRIYTKDISFEAPNAPQVFQKEWEPEVKLDLDTASSQLADDVYEVVLRVTVTATVGEDSAFLCEVQQAGIFSVGGIDGTQMAHCLGAYCPNILFPYARECITSLVARGTFPQLNLAPVNFDALFMNYLQQSEGAAQQQDA | One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. | B2VL52 |
P9WG96 | TATC_MYCTO | Sec-independent protein translocase protein TatC | Mycobacterium tuberculosis complex | MRAAGLLKRLNPRNRRSRVNPDATMSLVDHLTELRTRLLISLAAILVTTIFGFVWYSHSIFGLDSLGEWLRHPYCALPQSARADISADGECRLLATAPFDQFMLRLKVGMAAGIVLACPVWFYQLWAFITPGLYQRERRFAVAFVIPAAVLFVAGAVLAYLVLSKALGFLLTVGSDVQVTALSGDRYFGFLLNLLVVFGVSFEFPLLIVMLNLAGLLTYERLKSWRRGLIFAMFVFAAIFTPGSDPFSMTALGAALTVLLELAIQIARVHDKRKAKREAAIPDDEASVIDPPSPVPAPSVIGSHDDVT | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. | P9WG96 |
B4T2Q0 | FRDC_SALNS | Quinol-fumarate reductase subunit C | Salmonella | MTTKRKPYVRPMTSTWWKKLPFYRFYMLREGTAVPAVWFSIELIFGLFALKHGAESWMGFVGFLQNPVVVILNLITLAAALLHTKTWFELAPKAANIIVKDEKMGPEPIIKGLWVVTAVVTVVILYVALFW | Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones. | B4T2Q0 |
A3CVD3 | ECFA_METMJ | Energy-coupling factor transporter ATP-binding protein EcfA | Methanoculleus | MHLLETRDLTHIYRGDVHALEGVNFTAERKSRIAVIGPNGAGKSTLFKHFNGILKPTSGEVLVRGEPITKENVREVRKFVGIVFQNPDDQIFSPTVEQDIAFGPINLGLDEATVAHRVEEALHLLGIEELRERVPHHLSGGEKKRVAIAGILAMEPQVLVLDEPTAGLDPQGVADLVAFVNRLPEEYGMTVVFSTHHLDLVAEMADYIYVMDKGRVVGSGTVEEVFTRPELLTQTRLDVPPIPKLIRSLRENGVAIDMAYTYEDAKKSFLDAYARRA | ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. | A3CVD3 |
A8FYS8 | RLME_SHESH | rRNA (uridine-2'-O-)-methyltransferase | Shewanella | MSGKKRTASSSRWMQEHFDDHYVKLAQKRGFRSRAAFKIEEIQEKDKLIRPGMTVVDLGAAPGGWSQVAVKLAGDNGKVIACDILPMDPIVGVDFLQGDFREEKVLDALLTRVGDAKVDVVLSDMAPNMSGTGGVDQPRAMYLVELALDMCHQVLAPNGCFAVKVFQGEGFEEYMKSVREAFKTVKTRKPDSSRARSREVYLVATGYKL | Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. | A8FYS8 |
Q07YF5 | KATG2_SHEFN | Peroxidase/catalase 2 | Shewanella | MKHPLFNQKVLAGFVSMLLISGSAFASNNEKSEMTKPKGAVGTGVALENQARTNQFWWPDQLNLSALRDHDKRSNPYGENFDYAKAFNSLDLDKVKLDINALLTTSQDWWPSDYSNYGPFFIRMTWHSAGTYRTLDGRGGAGGGQQRFEPLNSWPDNASLDKARRLLWPIKMKYGEAISWSDLIVLAGNVSLENMGFKTYGFAGGRHDDWEPDMVYWGPEIEMLASDREDNGGKLQRPLGATHMGLIYVNPEGPKGVPDPLGSAKNIRVAFERMAMNDEETLALIAGGHTFGKMHGAHKPKDCLGAEPAAAGIEEQGLGWKNKCGKGHSEDTITSGLEGAWTQAPTKWTSLYLSNLLTFEWKQTRSPAGAIQWIPTDESLHKAVPDAHVKGKFHAPVMTTADLALKYDPEYRKIAERFLADPEEYRLAFAKAWYKLTHRDMGPSRNFLGKEVPKESLIWQDPIDDKTQSNIDADGVQELKAQILKSNLTVSELVRVAWASAASYRHSDMRGGANGARIALSPQKDWSVNNPAETAKVIKTLKAIQEDYNDSLFSKSKVSLADLIVLGGTAAIEKAAKDAGFTVSVPFNAGRGDATQAMTDINAFSLLELTSDGFRNYFDAQQSYKSPVDMLVDKADQLNLSVPEMTVLVGGLRALDANYKGLKHGVLTSTPGTLNNDFFVNLLDMSTVWKKSSTDGIYEGFDRQSGHKKWTATSVDLVFGSNSELRAVSEVYAFDTSKQKFVEDFAAAWTKVMNLDR | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. | Q07YF5 |
A5ELM3 | RS19_BRASB | 30S ribosomal protein S19 | unclassified Bradyrhizobium | MVRSVWKGPFVEASLLKKADAARASGRHDVIKIWSRRSTILPQFVGLTFGVYNGQKHVPVAVNEEMVGHKFGEFSPTRTFHGHSGDKKAKKA | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | A5ELM3 |
P34716 | RECA_ACIFA | Recombinase A | Acidocella | MDEPGGKIEFSPAFMQIEGQFGKGAVMRAGDKPGINDPDVKSTGSLGLDGALGQGGLPRGRVVEIYGPESSGKTTLTLKAIASAQAEGATPAFTDAEHALDPGFASKLGVNVKRLLISQPDTGEQALEIADMLFRSGAVDVIVKDSVAALTPKAEIEGEMGDSHQGLHARLMSQALRNKTANISRWNKLVIFKKQIRMKMGVYGRPETTTGGNALKFYASVRLDIRRMGAMKKSATKSYDWSTRVKVVKNKVAPPFRQAELAIYYGEGIYRGSEPVDLGVKLENVEKSGGWYSYPGRRIGQGKANARQYLRVKPEFPGIFEQGIRGAMAAPHPLGFGERRDVQQESGEPYGNNG | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | P34716 |
Q6N6B8 | RECO_RHOPA | Recombination protein O | Rhodopseudomonas | MEWSDEGIILGVRRHGESAAIVELLTRGHGRHLGMVRGGASARMRPLLQPGNSVLASWRARLDEHLGYYQLEATKMRAATLLGSSHAVYGVTHLASLARLLPERDPHEEIYQRLVLTLDDFDDFGVAAAHLIRFELAILAELGFGLDLSACAATGSTTELIYVSPKSGSAVSRSAGEPWRDRLLRLPAFLRDDEAESGHGWSGQDLFDGFELTGRFLLRNVLEPRGQSHSDARAGFINAITRALQRPAES | Involved in DNA repair and RecF pathway recombination. | Q6N6B8 |
B1ISA3 | UXUA_ECOLC | D-mannonate hydro-lyase | Escherichia | MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIVEDAGLVWSVVESVPIHEDIKTHTGNYEQWIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAVRFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRPILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNPKTFHEAAHLNGDVDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGTGTGSGA | Catalyzes the dehydration of D-mannonate. | B1ISA3 |
P38454 | CCMB_MARPO | ORF 277 | Marchantia | MKRVREENETLHLENARRSPPLASTHFLGFPCISLFYSQHKSTKKNIYLDLKTKKKELLPMVFALRAFKIFLKLFYQHILLNLSTLITTFSLFLLYIVVTPLMIGFSKDFLCHFHLGLIWICLLFSFLPERFFQNDFEDGTLELYYLSGYCLQKILLSKLYGHWVLQISGVFCSFPVLQLLYQFDQSKMNWFTIIIGSQIFTLMCGIHSCLALGITSNGWNSLQNLTTLPTLLPLIVFCTSIETEWFHVILLMGYLLLFLFFYPILVSITLQTLLAK | May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes. | P38454 |
Q2H137 | BCP1_CHAGB | Protein BCP1 | Chaetomium | MGKKRSRDADGQGDVEMADPAVTKRDDDDSSDDENMDIVNVDFELFNYDSQIDFHGVKTLLRQLFDTDAQLFNLSALSDLIIEQNTIGSTCKVDDKANDAYAFLTVLNLQEHRAKQPVAQLIEYLTDRAKSNDSLAGVLPELLASDKHVGLVLAERLLNMPAEVIPPMWTCMIDEIEAAVEDKEPYEFSHYLVVSRTYREVASSLDQSERKQKKAREEAELQFFHPEDDEMRKHAVASGAYDFTKEGEAVADSKRAFQEMGIKPCGFMMLIEASKFQGAVQAIAEYIGTAT | Involved in nuclear export, actin cytoskeleton organization and vesicular transport. | Q2H137 |
B2TNM9 | DCDB_CLOBB | DCD-DUT | Clostridium | MILSGKEILKHIGEDIVIEPFSEERINPNSYNLTLFNELLVYKNETLDMKIPNETEKLIIPEEGLLLEPGKLYLGRTNEFTQTNKYVPMLEGRSSTGRLGLFIHVTAGFGDIGFAGYWTLEIFCVQPIKIYPNTEICQIYYHNIDGEYDLYNSGKYQNNNGIQPSLMYKDFEK | Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. | B2TNM9 |
O33114 | ILVC_MYCLE | Ketol-acid reductoisomerase type I | Mycobacterium | MFYDDNADLSIIQRRKVGVIGYGSQGYAHSLSLRDSGVQVRVGLPEGSKSRPKAFEQGLDVDTPAEVAKWADVIMLLVPDTAQADVFENDIEPNLQPGDALFFGHGLNIHFELVKPSGDVTVAMVAPKGPGYLVRRQFVDGKGVPCLIAVNQDPTGTGEALALSYAKAIGGTRAGVIKTTFKDETETDLFGEQAVLCGGTEELVKAGFDVMVEAGYPPEMAYFEVLHELKLIVDLMYEGGIARMNYSVSDTAEFGGYLSGPRVIDADTKERMRGILRDIQDGSFVKKLVANVEGGNKQLEVLRKENAEHPIEVTGKKLRDLMSWVDRQSTETA | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | O33114 |
A4IKT9 | HPR_GEOTN | Protease production regulatory protein Hpr | Geobacillus | MKSTEQHYSIKEAMLFSQRIAQLSKALWKSIEKDWQQWIKPFNLNINEHHILWIAYHFKGASISEIAKFGVMHVSTAFNFSKKLEEKGLLSFSKKQDDKRNTYIELTEKGEEVLMKLMETYDPTRNAVFNGALPLRELYGKFPEILEMMCIVRNIYGDDFMEIFERAFENIKEDFVEQDGKLVKRAPKAEEHEKELASPG | Negative regulator of protease production and sporulation. | A4IKT9 |
P95988 | RS11_SACS2 | 30S ribosomal protein S11 | Saccharolobus | MSSRREIRWGIAHIYASQNNTLLTISDLTGAEIISRASGGMVVKADREKSSPYAAMLAANKAASDALEKGIMALHIKVRAPGGYGSKTPGPGAQPAIRALARAGFIIGRIEDVTPIPHDTIRRPGGRRGRRV | Located on the platform of the 30S subunit. | P95988 |
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