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 |
|---|---|---|---|---|---|---|
Q562C9 | MTND_RAT | Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1 | Rattus | MVQAWYMDESTADPRMPHRAQPDRPVGLEQLRTLGVLYWKLDADKYENDPELEQIRKTRNYSWMDIITICKDSLPNYEEKIKMFFEEHLHLDEEIRYILEGSGYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTPYNRPADHFDARVQYVKFLEGTA | Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine... | Q562C9 |
A0QKR3 | CH10_MYCA1 | Chaperonin-10 | Mycobacterium avium complex (MAC) | MAKVNIKPLEDKILVQANEAETTTASGLVIPDTAKEKPQEGTVVAVGPGRWDDDGAKRIPLDVSEGDTVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... | A0QKR3 |
P02717 | ACHD_CHICK | Acetylcholine receptor subunit delta | Gallus | MAVLLALFGALVLSGGLCVNQEERLIHHLFEERGYNKEVRPVASADEVVDVYLALTLSNLISLKEVDETLTTNVWVEQSWTDYRLQWNTSEFGGVDVLRLLPEMLWLPEIVLENNNDGLFEVAYYCNVLVYNTGYVYWLPPAIFRSACPINVNFFPFDWQNCTLKFSSLAYNAQEINMHLKEESDPETEKNYRVEWIIIDPEGFTENGEWEIIHRPARKNIHPSYPTESSEHQDITFYLIIKRKPLFYVINIVTPCVLIAFMAILVFYLPADSGEKMTLVISVLLAQSVFLLLVSQRLPATSHAIPLIGKYLLFIMLLVT... | After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | P02717 |
P09373 | PFLB_ECOLI | Pyruvate formate-lyase 1 | Escherichia | MSELNEKLATAWEGFTKGDWQNEVNVRDFIQKNYTPYEGDESFLAGATEATTTLWDKVMEGVKLENRTHAPVDFDTAVASTITSHDAGYINKQLEKIVGLQTEAPLKRALIPFGGIKMIEGSCKAYNRELDPMIKKIFTEYRKTHNQGVFDVYTPDILRCRKSGVLTGLPDAYGRGRIIGDYRRVALYGIDYLMKDKLAQFTSLQADLENGVNLEQTIRLREEIAEQHRALGQMKEMAAKYGYDISGPATNAQEAIQWTYFGYLAAVKSQNGAAMSFGRTSTFLDVYIERDLKAGKITEQEAQEMVDHLVMKLRMVRFLR... | Catalyzes the conversion of pyruvate to formate and acetyl-CoA . In addition, may be involved in the control of the activity of the formate channel FocA, via direct interaction with FocA . | P09373 |
B1KYV1 | SYE_CLOBM | Glutamyl-tRNA synthetase | Clostridium | MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMKELIEAFNYRNINKAPAVFDTKKLK... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | B1KYV1 |
A9AI59 | PROB_BURM1 | Gamma-glutamyl kinase | Burkholderia cepacia complex | MRSIIADSKRLVVKVGSSLVTNDGKGLDHAAIGRWAAQIAALRAQGKEVVLVSSGAIAEGMQRLGWSKRPREIDELQAAAAVGQMGLAQVYESRFTEHGIRTAQILLTHADLADRERYLNARSTLLTLLRLGVVPIINENDTVVTDEIKFGDNDTLGALVANLIEGDALIILTDQSGLFTADPRKDPAATLVAEANAGAPELEAMAGGAGSSLGRGGMLTKILAAKRAAHSGANTVIASGREPDVLVRLAGGEAIGTQLIARTARMAARKQWMADHLQVRGHVVIDAGAVEKLTAGGKSLLPIGVTDVQGAFARGEVIAC... | Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | A9AI59 |
P55678 | FER3_SINFN | Ferredoxin III | Sinorhizobium | MTSHFVTRDGSTWMPQYLTAIDAMTCIGCGRCFKVCSREVMHLHGIDESGEILGACDGEDDDFAGELSRTIMVVDHAGRCIGCGACARVCPKNCQTHVAADEIVA | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | P55678 |
C1CKX8 | UVRB_STRZP | Excinuclease ABC subunit B | Streptococcus | MINHITDNQFKLVSKYQPSGDQPQAIEQLVDNIEGGEKAQILMGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSALLERNDVIVVASVSCIYGLGSPKEYADSVVSLRPGLEISRDKLLNDLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHAFRVEFFGDEIDRIREVEALTGQVLGEVDHLAIFPATHFVTNDDHMEVAVAKIQAELEEQLAVFEKEGKLLEAQRLKQRTEYDIEMLREMGYTNGVENYSRHMDG... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP bindi... | C1CKX8 |
Q49ZE2 | RPOA_STAS1 | Transcriptase subunit alpha | Staphylococcus | MIEIEKPRIETIEISEDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVKYIEIEGVLHEFSAIDNVVEDVSTIIMNIKKLALKIYSEEDKTLEIDVKDEGDVTASDITHDSDVEILNPEIKIATVSKGGHLKIRLVANKGRGYALAEQNKTSDLPIGVIPVDSLYSPVERVNYTVENTRVGQSSDFDKLTLDVWTNGSITPQESVSLAAKILTEHLNIFVGLTDEAQNAEIMIEKEEDQKEKVLEMSIEELDLSVRSYNCLKRAGINSVQELADKSEADMMKVRNLGRKSLEEVKYKLEDLGLGLRKED | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q49ZE2 |
Q9DAQ9 | SPT19_MOUSE | Spermatogenic cell-specific gene 1 protein | Mus | MIITTWIMYIFARKTVGLPFPPRVNSDIEVEESEAVSVVQHWLNKTEEEASRSIREKMSINDSPTHGHDIHVTRDLVKHHLSKSDMLTDPSQEVLEERTRIQFIRWSHTRIFQVPSEVMDDVMQERIDQVRRSVSHLMCDSYNDPSFRTSCSEC | Essential for sperm motility and male fertility . Plays an important role in sperm motility by regulating the organization and function of the mitochondria and is also required for correct sperm midpiece assembly . | Q9DAQ9 |
P20594 | ANPRB_HUMAN | Guanylate cyclase B | Homo | MALPSLLLLVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELEGACSEYLAPLSAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLLTAGAVASGFSAKNDHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTREQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRARED... | Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. | P20594 |
Q5W7F2 | AGD3_ARATH | Protein VASCULAR NETWORK 3 | Arabidopsis | MHFTKLDDSPMFRKQLQSMEESAEILRERSLKFYKGCRKYTEGLGEAYDGDIAFASALETFGGGHNDPISVAFGGPVMTKFTIALREIGTYKEVLRSQVEHILNDRLLQFANMDLHEVKEARKRFDKASLTYDQAREKFLSLRKGTKSDVAAALEQELHTSRSMFEQARFNLVTALSNVEAKKRFEFLEAVSGTMDAHLRYFKQGYELLHQMEPYINQVLTYAQQSRERSNYEQAALNEKMQEYKRQVDRESRWGSNGSNGSPNGDGIQAIGRSSHKMIDAVMQSAARGKVQTIRQGYLSKRSSNLRGDWKRRFFVLDSR... | GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Involved in the spatial control of provascular differentiation. Required for the formation of the normal pattern of continuous secondary veins. Involved in auxin signaling but not in polar auxin transport or in auxin responses. Required for PIN1 interna... | Q5W7F2 |
P50579 | MAP2_HUMAN | Peptidase M | Homo | MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTY... | Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. | P50579 |
Q28UE7 | RIMM_JANSC | Ribosome maturation factor RimM | unclassified Jannaschia | MTNPDHTCVGAISGSFGVRGEVRLKSFCAEPSDIGSYGPLSTEDGAQTYTITLTRPVKAGYAAMLSGVATKEDADALRGTRLYAPRSALPSLPDDEFYHADLVGLTVLDTGGEVIGTVASVANHGAGDILELSGPGLPSGLLIPFTLAVVPTVDIAAGRVIVDMPDGLIGGDKPDTSDTAPLGQDFD | 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 ribosoma... | Q28UE7 |
Q5Z040 | PROB_NOCFA | Gamma-glutamyl kinase | Nocardia | MSAARQAIASARSVVVKIGSSALTSLEGGLDTTRLDRLADAVEARMRAGSDVVVVSSGAIGAGLAPLGLSRRPRDLATKQAAASVGQLALAHAWGTSFARYGRTVGQVLLSADDFSRREHHRNAQRTLDRLRSLGAVAVVNENDTVATEEIRFGDNDRLAALVAHLVGADALILLSDVEGLYDGDPRKGAATFIPEVRSSADLDGVIAGSGGVLGTGGMASKLSAARLAADAGVPVLLAAAEQAATALGSGTVGTAFAARPVRLSARKFWVRHAADSRGALVLDDGAVQAVAQRRRSLLAAGITAVRGRFHGGDVVDLLA... | Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | Q5Z040 |
P63392 | IRTA_MYCBO | Mycobactin import ATP-binding/permease protein IrtA | Mycobacterium tuberculosis complex | MARGLQGVMLRSFGARDHTATVIETISIAPHFVRVRMVSPTLFQDAEAEPAAWLRFWFPDPNGSNTEFQRAYTISEADPAAGRFAVDVVLHDPAGPASSWARTVKPGATIAVMSLMGSSRFDVPEEQPAGYLLIGDSASIPGMNGIIETVPNDVPIEMYLEQHDDNDTLIPLAKHPRLRVRWVMRRDEKSLAEAIENRDWSDWYAWATPEAAALKCVRVRLRDEFGFPKSEIHAQAYWNAGRAMGTHRATEPAATEPEVGAAPQPESAVPAPARGSWRAQAASRLLAPLKLPLVLSGVLAALVTLAQLAPFVLLVELSRL... | Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT). Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the bacterial cell. Transmembrane domains (TMD) form a pore in the membrane and the ATP-bin... | P63392 |
P92429 | RPOA_AEGTA | Plastid-encoded RNA polymerase subunit alpha | Aegilops | MVREEVAGSTQTLQWKCVESRVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGEIEGTCITRAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRDASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPIDFCIDLQIKRDRGYQTELRKNYQDGSYPIDAVSMPVRNVNYSIFSCGNGNEKHEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHAEEEGTSFEENKNRFTPPLFTFQKRLTNLKKNKKGIPLNSIFIDQLELTSRTYNCLKRANIHTLLDLLSKTEEDLLRIDSFRMEDRKHI... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | P92429 |
Q9V3J8 | WDS_DROME | Protein will die slowly | Sophophora | MVPIGAVHGGHPGVVHPPQQPLPTAPSGPNSLQPNSVGQPGATTSSNSSASNKSSLSVKPNYTLKFTLAGHTKAVSAVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSRLLVSGSDDKTLKVWELSTGKSLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVRTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNMVYIWNLQSKEV... | Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' . In neurons and together with DNA N6-methyl adenine demethylase Tet, plays a role in the maintenance of transcriptional activation for specific sets of genes . | Q9V3J8 |
Q0I143 | RL15_HAES1 | 50S ribosomal protein L15 | Histophilus | MRLNTLSPAEGAKHNAKRLGRGIGSGLGKTSGRGHKGQKARTGGGVRRGFEGGQMPLYRRLPKFGFTSMKSAVTAEVRLNDLAKVEGNIITLDTLKAANVLTKDIRFAKVILAGEVKTAVTIRGLGVTKGAKVAIEAAGGSIEE | Binds to the 23S rRNA. | Q0I143 |
Q9K8L5 | PSTB_HALH5 | Phosphate-transporting ATPase | Halalkalibacterium (ex Joshi et al. 2022) | MALTVKEKKNVEVVVPQPRQKHVIQGEPTVAYETRDLNLWYGKDHALKNINLSIYEKEVTAIIGPSGCGKSTYLKTLNRMVELVPSVRISGNISYRGRNILDKSFQVEELRTRVGMVFQKPNPFPKSIFDNVAYGPRIHGIRNKKILSEIVERSLRGAAIWDEVKDRLHENAYGLSGGQQQRLCIARCLAIEPDVILMDEPTSALDPKSTLKIEELIQELKKEYSIIIVTHNMQQAARISDKTAFFLNGEVVEYDSTDIIFSNPSDKRTEDYITGRFG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Q9K8L5 |
Q0A5K0 | SUCC_ALKEH | Succinyl-CoA synthetase subunit beta | Alkalilimnicola | MNLHEFQAKHLFADYDIPIPQGYVARSSGEAVEAAGRLGGSVWVVKAQVHAGGRGKAGGVKVLKTKEEVEEFTDSLLGSRLVTHQTDAKGQPIHAVLVEQGLDIARELYLGALVDRASKRVTFMGSAAGGMDIEEVAASTPEKILTLAVDPAAGFQAYQGRKMAFALGLEGKQIGQLVKIMKSLYRIFEEKDLSMIEINPLIVTGDGQLLALDAKVNVDDNAVEIGRQPQIADMRDITQEDEAEVQAAEHNLNYITLDGNIGCMVNGAGLAMATMDVVNLHGGSPANFLDVGGGTTTERVTAAFKLILSSDTVEGILVNI... | 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 succinat... | Q0A5K0 |
Q9MZS8 | CATD_SHEEP | Cathepsin D | Ovis | LHKFTSNRRTMSEAMGPVEHLIAKGPISKYATREPAVRQGPIPELLTNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMRQKLVDKNVFSFFLNRDPKAQPGEELMLGGTDSKYYRGSLTYHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLMVGPVDEVRELHKAIGAVPLIQGEYMIPCEKVSSLPQVTLKLGGKDY... | Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. | Q9MZS8 |
Q337Y2 | CADH3_ORYSJ | Probable cinnamyl alcohol dehydrogenase 3 | Oryza sativa | MAPTAASAAAGEEQQAVGLAARDSSGHLSPFAISRRSTGDDDVAIKILFCGICHSDLHCIKNEWKHSIYPLVPGHEIAGVVTEVGKNVTRFKAGDRVGVGCMVNSCRSCESCNNGFENHCPEGVFTYNSVDKDGTVTYGGYSSMVVVHERFVVMFPEAMPLDVGAPLLCAGITVYTPMKYHGLNAPGKHVGVLGLGGLGHVAVKFARAFGLKVTVISSSPGKKREALERLGADAFVVSSSAEEMEAARSTMDGVINTVSANTPMAPYLALLKPNGKMILVGLPENPLEVPPFSLVHGNRTLAGSNIGGMADTQEMIELAA... | Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols. | Q337Y2 |
Q02W76 | SYE_LACLS | Glutamyl-tRNA synthetase | Lactococcus cremoris subsp. cremoris | MNKKIRVRYAPSPTGLLHIGNARTALFNYLFARHHGGDFIIRIEDTDRERHVEDGERSQLENLRWLGMDWDESPETHENYRQSERLPLYQKYIDQLLAEGKAYYSYKTPEELEADHAKQEAAGIPPHYINEYAGMSDDEKAAYIAERKAQNIEPVVRISVDEKAIYKWNDIVKGEIEFEGGNIGGDWVIQKRDGYPTYNFAVVVDDHDMQISHVIRGDDHIANTPKQLVVYDALGWEAPQFGHMTLIINSETGKKLSKRDTNTLQFIEDYRKKGYMSDAIFNFIALLGWNPGGEKEIFSREELIELFDENRLSKSPAAFD... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | Q02W76 |
Q9CPF5 | COAE_PASMU | Dephosphocoenzyme A kinase | Pasteurella | MTYIVGLTGGIGSGKSTIAHLFMALGVPVIDADVVARDIVTKGSELLSKIVDYFGEHILCENGELNRAKLRERIFRHPEDKVWLNQLLHPAIREEMLRQLQIQTYPYVLWVVPLLIENNLTAFCQRVLVVDVEPETQIQRAMQRDNNSIELIQHIMASQVDRQTRLQFADDVIQNDADLKGNLPVLKQKVLELHHQYLQLANAQNA | Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | Q9CPF5 |
A1VZ42 | FLGH_CAMJJ | Basal body L-ring protein | Campylobacter | MKKVLFYVLPFAFFGCSATVDPQISMKPPAYVEELAPKQSNNVESAPGSLFGKGDNPLFSDKKAMNVNDLVTVVIQESTTQSTQANKATSRTNTSNLGGGALTGSSGVVANALNKVNAYSNIGFQTNSSNKYTGTGSQSRNESFNTTISTRVIKILSNGNYFIEGSRELLINGEKQIIQLSGVIRPYDIGQDNTIDSKYIADAKILYKTEGEVDRSTRKPWGSKVIEAIWPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | A1VZ42 |
Q38W81 | IF2_LATSS | Translation initiation factor IF-2 | Latilactobacillus | MGKKRIYELAKEINVASKDILETANKKGYDLKNHMATIDDNQEKTLRAAFQTKATPAASKPATPAAPKASEKSESGKIKINKTAIRRRPEADKKPAQHSNNRPQANANRNGQASNGQNRTNNARPNNNSARPNNSRPNTNSRPNNNSQNRSTSANHPMSLQEQISQANARRQRTQERIQQQREQREADEKKRREQANRPRPTRNNASNNRPSNGKPTNGARPTTNSPRPTVTKDGRPLGSSRPNNNNSARPNTTNNRPTNSRPATTPSRPVSAQEMQQKMQANTVSASKPASNNTASKPKNFGPDKKRGGGYNSYGNSQQ... | 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. | Q38W81 |
P10333 | MS2A_DROME | CP3-C | Sophophora | MNQILLCSPILLLLFTVASCDSEQQLDSAMHLKSDSTKSASLKNVAPKNDETQAKIAKDDVALKDAKKGDYIMDIDISDLPLDDYPINRSKSLKSSSIDLNNIPFNKGLDDFPAKEKNQGSNQSALKALQQRLLTEQNNSLLLRNHSIYLMKEIEARKTDIIKVRQLNLDLELELNTVNRRLLELNGQLQNTRKSTKPCKKRSSKDSAPPAANQFQEANVRNTYRNKYLTLLKELSQKINNEIAKVATDVPTETNPSQGNLPTL | Male seminal peptide which is able to enhance ovulation in female Drosophila. | P10333 |
C1F460 | MURD_ACIC5 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Acidobacterium | MELKGKKVLVVGLGKSGLAAALFLRRRGAQVTVSDIRSAEALSKDIPALIEQGIAVEAGGHGLLTFRRQDLIVVSPGVPLDTPELVQVRKFGLPIIGEVELAARFLKGKTLAITGSNGKTTTTSLCGAILERAHQHVQVGGNIGLPVIALVDDSRDDGWSVLEISSFQLETTERFRPGIAVILNITPDHLDRHGSFENYVAAKERIFAAQTHDDALILNADDDAASRAAARASSRIFWFSRNRVIRQGAFVHEGNILFRAAEDAATEPILPLSEIPLKGAHNVENVLAAVCAARLAGVSAEAIRDAVRDFRAVEHRLEFV... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | C1F460 |
Q9SEZ4 | MY105_ARATH | Protein LATERAL ORGAN FUSION 2 | Arabidopsis | MEMVHADVASLSITPCFPSSLSSSSHHHYNQQQHCIMSEDQHHSMDQTTSSDYFSLNIDNAQHLRSYYTSHREEDMNPNLSDYSNCNKKDTTVYRSCGHSSKASVSRGHWRPAEDTKLKELVAVYGPQNWNLIAEKLQGRSGKSCRLRWFNQLDPRINRRAFTEEEEERLMQAHRLYGNKWAMIARLFPGRTDNSVKNHWHVIMARKFREQSSSYRRRKTMVSLKPLINPNPHIFNDFDPTRLALTHLASSDHKQLMLPVPCFPGYDHENESPLMVDMFETQMMVGDYIAWTQEATTFDFLNQTGKSEIFERINEEKKPP... | Probable transcription factor that involved in boundary specification, meristem initiation and maintenance, and organ patterning. Functions in both lateral organ separation and axillary meristem formation. | Q9SEZ4 |
Q9UTT1 | UBP21_SCHPO | Ubiquitin-specific-processing protease 21 | Schizosaccharomyces | MVLSNVDAEEVNMDSSMELEESSQEPLRADNYEEIYNSLVHHEPDLEEAAHASYSWVVKNFSTLEDKTYSPLFKAGHTTWRIVLFPKGCNQTEYASVFLEYLPQCKVEAIRKYEAELAAGKTPTIDPEIVNDETYSCCAQFALSLSNVQDPTVMQINTSHHRFRSEVKDWGFTRFVDLRKIAVPTPEFPVPFLENDEICISVTVRVLQDPTGVLWHSFVNYNSKKETGYVGLKNQGATCYMNSLLQSLFFTNIFRKTVYKIPTDNDDSRDSVAYALQRVFYNLEKQREPVSTTELTRSFGWNSFDSFMQHDIQEFNRVLQ... | Involved in regulating the steady-state levels of proteins including prp4. | Q9UTT1 |
B2A713 | UVRB_NATTJ | Excinuclease ABC subunit B | Natranaerobius | MNEFKLQSDFSLEGDQPKAVDELCESLNGGNSHQTLLGVTGSGKTFTMANVIQRLQRPTLVIAHNKTLAAQLCGEFKEFFPENAVEYFVSYYDYYQPEAYIPQTDTYIEKDASINDEIDKLRHSATSALFERRDVIIVASVSCIYGLGSPEEYREQVLSLRCGMEKDRDEILKGLVDIQYSRNDVNFTRGTFRVRGDVIEVFPASYTETAVRIELFGDEIERITEIDTLTGEILGERNHVAIFPASHFVTRRSKLEKAIESIQEELHEQLEYLKRQGKAVEAKRLEQRTNYDLEMLQEMGFCQGIENYSRHLIGRPAGSR... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP bindi... | B2A713 |
Q8R4H9 | ZNT5_MOUSE | Solute carrier family 30 member 5 | Mus | MEEKYGGDARPGPGGGLGPVDVPSARLTRYILLLCLTKCLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKPITKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGVADHKGGVLLLVLALCCKVGFHTASRKLSIDVGGAKRLQALSQLVSVFLLCPWVIVLSVTTESKVESWFSLIMPFTTVIFFVMILDFYMDSVCSVKMDVSKCARYGSFPIFISALLFGNFWTH... | Zinc ion:proton antiporter mediating zinc entry into the lumen of organelles along the secretory pathway. By contributing to zinc ion homeostasis within the early secretory pathway regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosy... | Q8R4H9 |
P0CP75 | PLB1_CRYNB | Lysophospholipase | Cryptococcus neoformans species complex | MSIITTAFALSLLATTAFAVPPETPRIELQAERGLGDQSYAPWQVDCPSNVTWIRNATTGLGTGERAYIEAREKLVQPAIEQMMAARGLETPPRTPVIGVALAGGGYRAMLTGLGGIMGMMNESTEASQSETGGWLDGVSYWSGLSGGSWATGSFMSNGGQLPTTLLENLWNIDSNLVFPDDGKLSFYTNLYTETNAKSDLGFPVQITDIWGLAIGSHVLPEPYQLSNTPNLTFSSLPSVVAALGNASLPMPIIVAADRKRREAGELVIAENATVWEFTPYEFGSWAFGSQYKSPGAFTPIEYLGTSVDDGSPNGTCWKG... | Exhibits phospholipase B (PLB), lysophospholipase (LPL) and lysophospholipase/transacylase (LPTA) activities. | P0CP75 |
P0DO33 | ILID_NEOS2 | Pericyclase iliD | unclassified Neonectria | MTSTEAAGTGKAPAIRANPALQTYYESQESYLVYEVVLRGSHHFGFYEKDTYWPFPVGRSLERMEAKLLSALALPSGSQILDAGCGFGPVAISMAKKGMRVTAIDIIDHHVTKARRNVEKAGLPKGQVTVEKMDYQHLESIASESHDDAKAAATGFFRILKPGGRIAFFEAQRSRTSGDYDEGDELAGHLKLVNEYTAMPTNELSREDYFKDLLEDAGFVDVEFTLPPGTREPREHWSYSALKA | S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IliD catalyzes the Diels-Alder reaction that converts the acyclic ... | P0DO33 |
O53333 | HIGA3_MYCTU | Putative antitoxin HigA3 | Mycobacterium tuberculosis complex | MTMARNWRDIRADAVAQGRVDLQRAAVAREEMRDAVLAHRLAEIRKALGHARQADVAALMGVSQARVSKLESGDLSHTELGTLQAYVAALGGHLRIVAEFGENTVELTA | Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB3. | O53333 |
Q1QN35 | RS12_NITHX | 30S ribosomal protein S12 | Nitrobacter | MPTINQLIASPRVIQKSRKKVPALQQSPQKRGVCTRVYTTTPKKPNSALRKVAKVRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHILRGVLDTQGVKNRKQRRSKYGAKRPK | 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 com... | Q1QN35 |
Q7TX84 | MOAA1_MYCBO | Molybdenum cofactor biosynthesis protein A 1 | Mycobacterium tuberculosis complex | MSTPTLPDMVAPSPRVRVKDRCRRMMGDLRLSVIDQCNLRCRYCMPEEHYTWLPRQDLLSVKEISAIVDVFLSVGVSKVRITGGEPLIRPDLPEIVRTLSAKVGEDSGLRDLAITTNGVLLADRVDGLKAAGMKRITVSLDTLQPERFKAISQRNSHDKVIAGIKAVAAAGFTDTKIDTTVMRGANHDELADLIEFARTVNAEVRFIEYMDVGGATHWAWEKVFTKANMLESLEKRYGRIEPLPKHDTAPANRYALPDGTTFGIIASTTEPFCATCDRSRLTADGLWLHCLYAISGINLREPLRAGATHDDLVETVTTGW... | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | Q7TX84 |
Q9X9U0 | THIC_STRCO | Thiamine biosynthesis protein ThiC | Streptomyces albidoflavus group | MTIKDARTPASTQNTAQADTAENTDTAEDTEAGKSIGWHKAYVEGSRPDLRVPVRQVHLTNGQSVTLYDTSGPYTDPLVDTDVRRGLAPLRENWIIARGDTEEYAGRPVRPEDDGIKHTSPRGGLRNLDAVFPGRPRQPRRGRDGNAVTQLAYARRGEITPEMEYVAVRENVSPEVVREEIAAGRAVLPANINHPEIEPMIIGKRFLVKVNANIGNSAVTSSIEEEVDKMTWATRWGADTVMDLSTGRNIHTTREWVLRNSPVPIGTVPLYQALEKVDGRAEELTWEIYKDTVIEQAEQGVDYMTVHAGVRLPYVPLTAN... | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | Q9X9U0 |
C5CQI8 | MURA_VARPS | UDP-N-acetylglucosamine enolpyruvyl transferase | Variovorax | MDKLLIRGGRQLRGEVLISGAKNAALPELCAALLTDQPVTLHNVPRLQDVSTMLKLVRNMGVAAERDDNGTVRLDAGDLSIPEAPYELVKTMRASVLALGPLLARFGHAKVSLPGGCAIGSRPVDQHIKGLQAMGAEIVVEHGYMIASLPAGRTRLKGARILTDMVTVTGTENFLMAAALAEGETLLENAAQEPEIVDLAEMLIRMGARIEGHGTSHIRIQGVEKLHGCEHAVVADRIEAGTFLCAVAATGGDVFLRHARADHMDAVIDKLRDAGCTVAAQEGGVRISSSAPACEHLKAQSFSTTEYPGFPTDMQAQFMA... | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | C5CQI8 |
Q9SS04 | GSOX1_ARATH | Putative flavin-containing monooxygenase 3 | Arabidopsis | MAPTQNTICSKHVAVIGAGAAGLVTARELRREGHTVVVFDREKQVGGLWNYSSKADSDPLSLDTTRTIVHTSIYESLRTNLPRECMGFTDFPFVPRIHDISRDSRRYPSHREVLAYLQDFAREFKIEEMVRFETEVVCVEPVNGKWSVRSKNSVGFAAHEIFDAVVVCSGHFTEPNVAHIPGIKSWPGKQIHSHNYRVPGPFNNEVVVVIGNYASGADISRDIAKVAKEVHIASRASESDTYQKLPVPQNNLWVHSEIDFAHQDGSILFKNGKVVYADTIVHCTGYKYYFPFLETNGYININENRVEPLYKHVFLPALAP... | Catalyzes the conversion of methylthioalkyl glucosinolates into methylsulfinylalkyl glucosinolates. Able to S-oxygenate both desulfo- and intact 4-methylthiobutyl glucosinolates, but no activity with methionine, dihomomethionine or 5-methylthiopentaldoxime. | Q9SS04 |
Q8NG04 | S2610_HUMAN | Putative solute carrier family 26 member 10P | Homo | MRLDLASLMSAPKSLGSAFKSWRLDKAPSPQHTFPSTSIPGMAFALLASVPPVFGLYTSFFPVLIYSLLGTGRHLSTGTFAILSLMTGSAVERLVPEPLVGNLSGIEKEQLDAQRVGVAAAVAFGSGALMLGMFVLQLGVLSTFLSEPVVKALTSGAALHVLLSQLPSLLGLSLPRQIGCFSLFKTLASLLTALPRSSPAELTISALSLALLVPVKELNVRFRDRLPTPIPGEVVLVLLASVLCFTSSVDTRYQVQIVGLLPGGFPQPLLPNLAELPRILADSLPIALVSFAVSASLASIHADKYSYTIDSNQEFLAHGA... | Chloride/bicarbonate exchanger. | Q8NG04 |
G8GTN7 | COCH_PEA | Protein COCHLEATA | Pisum | MSLEDSLRSLSLDYLNLLINGQAFSDVVFSVEGRLVHAHRCILAARSLFFRKFFCGPDPPSGLDPSGNRVNSSTRSGVIPVNSVGYEVFLLMLQFLYSGQVSIVPQKHEPRPNCGDRGCWHTHCTSAVDLALDTLSAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMHQLWTTCSHLVAKSGLPPEVLAKHLPIDIIAKIEELRMKSSLSRRSLIPHHHHNPHHHHDHLTAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALPYAVESCSREVVKALLELGAADVNFPAGPTGKTPLHI... | Involved in the promotion of leaf and floral meristem fate and determinacy . Promotes normal stipule growth and development . Down-regulates UNI expression in primordia of leaves and secondary inflorescences, and thereby controls their sizes and/or structures . Involved in the coordination of the symbiotic nodule devel... | G8GTN7 |
A5UQN2 | ATPE_ROSS1 | F-ATPase epsilon subunit | Roseiflexus | MPIHLEIVTAERVVLSDDVDMINAPTKDGRVGILPRHAPLLTILEVGELDIVKDGVTTPFAISGGFMEVLPNRVTILADTAERADEIDEARAEAARRAAEQRIAERKSAQDLALAEAELRRALVQLKVAQLKKIRRERD | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A5UQN2 |
B8ZNH8 | RPIA_STRPJ | Phosphoriboisomerase A | Streptococcus | MENLKKMAGIKAAEFVKDGMVVGLGTGSTAYYFVEEIGRRIKEEGLQIIAVTTSSVTTKQAEGLNIPLKSIDQVDFVDVTVDGADEVDSQFNGIKGGGGALLMEKVVATPSKEYIWVVDESKLVEKLGAFKLPVEVVQYGAEQVFRRFERAGYKPSFREKDGQRFVTDMQNFIIDLALDVIENPIAFGQELDHVVGVVEHGLFNQMVDKVIVAGRDGVQISTSKKGK | Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. | B8ZNH8 |
A8ALP3 | RAPA_CITK8 | ATP-dependent helicase HepA | Citrobacter | MPFTLGQRWISDTESELGLGTVVAMDARTVTLLFPATGENRLYARSDSPVTRVMFNPGDTITSHEGWQLQIDEVKEENGLLAYTGTRLDTEETAVTLREVLLDSKLVFSKPQDRLFAGQIDRMDRFALRYRARKFQSEQYRMPWSGLRGQRTSLIPHQLNIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIIVPETLQHQWLVEMLRRFNLRFALFDDERYTEAQHDAYNPFETEQLVICSLDFARRNKQRLEHLCDAQWDLLVVDEAHHLVWSEDAPSREYMAIEQLAERVPGVLLLTATPEQLG... | Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on line... | A8ALP3 |
Q4ZYD2 | CHED_PSEU2 | Probable chemoreceptor glutamine deamidase CheD | Pseudomonas syringae | MNTPVGVAEIVLGPGEVVFQTRPTRLRTLLGSCVAITFWHPWRRIGGMCHFMLPGRIRRHQPLDGRYADEAMEILIRHALANGTLPEEYQVKLFGGGEMFPAHRHDPHMRNVADSNVHAALALAEQNRLKLMAQDLGSTGHRSIIFDLWDGNVWVRHQPMEAMEKDAKQKNQRTAGR | Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. | Q4ZYD2 |
B9JG70 | HSLV_AGRRK | ATP-dependent protease subunit HslV | Agrobacterium tumefaciens complex | MTTIVTIRKGGKVVMAGDGQVSLGQTVMKGNARKVRRIGKGDVIAGFAGATADAFTLLERLEKKLEQYPGQLMRAAVELAKDWRTDKYLRNLEAMMLVADKSVTLAITGNGDVLEPEHGALAIGSGGNYALAAARALMDTDKSAEDVARRALDIAADICVYTNHNVVIETLDAEA | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | B9JG70 |
Q0KI28 | BL1S5_DROME | Protein Muted | Sophophora | MKIMISQVGRELYKVPLRILDHRVFVNGEIEAFLENFEVRRNDSEVEKLFQVTETVGSLKYDLSRCSATGRGSGAENLAQLDTEVSHLLDGVNALLAKAKVERTASTQLQEARLAREQRRAEFLTNLEHGYRRIENSFEEKEEEIAELYSDLQLKLNIAK | Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis. | Q0KI28 |
P81494 | CATB_COTJA | Cathepsin B heavy chain | Coturnix | LPDTFDSRKQWPNCPTISEIRDQGSVSVEVSAEDLLSCCGFECGMGCN | Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. | P81494 |
B0RTU1 | PANB_XANCB | Ketopantoate hydroxymethyltransferase | Xanthomonas | MSSHADSKPWTVPALAQAKRDGRKLVMLTAYDAGFARTFDANGVDLILVGDSLGMVVQGHESTLPVTTADMVYHTAAVARVLERALLVADLSFQADATPERALDAATQLLQAGAEMVKIEGAGHKLDVIRYLVEREIPVCSHLGLTPQSVLRFGGYKVQGRGEAGEQLRRDAQAAVDAGVSLIVLECVPTPIAAQISAELRVPTIGIGAGPGCDGQVLVMHDMLGLDSGHRRPKFVKDFLAEGGSVAGAVQAYAQAVRDGSFPDAEHAYAA | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | B0RTU1 |
B5XV34 | ISPD_KLEP3 | MEP cytidylyltransferase | Klebsiella | MAATFPGVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHAVAALLANACVQRVVIAVSPGDRRFSQLPLAQHPQITVVDGGAERADSVLAGLKALPEAQWVLVHDAARPCLHQDDLSRLLALSETSRVGGILAAPVRDTMKRAEPGKTAIAHTVDRNDLWHALTPQFFPRELLVDCLTRALNEGATITDEASALEYCGFHPQLVAGRADNIKVTRPEDLALAEFYLTRSRHQEKA | Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | B5XV34 |
A3N0B0 | AROC_ACTP2 | 5-enolpyruvylshikimate-3-phosphate phospholyase | Actinobacillus | MAGNSIGQLFKVTTFGESHGIALGCIVDGVPPNMALSEADIQPDLDRRKPGTSRYTTPRREDDEVQILSGVFEGKTTGTSIGLIIKNADQRSKDYGDIADKFRPGHADYTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLREQFGIEVRGYLSQIGNVKINPETVADISKIDWQQVASNPFFCPDPVAVEGFGELIRELKKDGDSIGAKLTVVAENVPVGLGEPVFDRLDADLAHALMSINAVKAVEIGDGFDVVEQRGSEHRDEMTPQGFVSNHAGGILGGISSGQPIIAHIALKPTSSIMVPGRSVNLNNEQV... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | A3N0B0 |
Q3KR86 | MIC60_RAT | Mitofilin | Rattus | MLRACQLSGVTVAAQSCLCGKFVLRPLRPCRRYSTSSSSGVTAGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFGMVLGSAPYTVPLPKKPIQSGPLKISSVSEVMTDSELPMAQTQETNGDTPASAAGDPAPEVEHEDTINTECPNTDEGTSTFVTAALAKSLEDALNQTATVTRQTITAQNAAVQAVKAHSSTLKTAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDAKKREIAGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDD... | Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and th... | Q3KR86 |
Q9TKI7 | ATPB_MEDSA | F-ATPase subunit beta | Medicago | MRLTPTTSDTEVSGLEKKNLGRITQIIGPVLDVVFSPGKMPNIYNALIVQGRDTVGQEINVTCEVQQLLGNNRVRAVAMSATDGLKRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTGTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGTLQERITSTKEGS... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q9TKI7 |
Q57G60 | DNAT_SALCH | Primosomal protein I | Salmonella | MSSRILTSDVIGIDVLLHDHHAVLAKSTGGAVAVFANNAPAFYAVTPARMAELLALEEKLSRPGSDVALDAQFYEEPEAAPVAIPCGKFAMYPAWQPDADFQRQAALWGVALREPVTAEELAAFIAYWQAEGKVFHHIQWQQKLARSVQISRSSNGGMPQRDINSVSEPDNHIPPGFRG | This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by p... | Q57G60 |
Q9UXA8 | RL3_SACS2 | 50S ribosomal protein L3 | Saccharolobus | MGHRKLASPRRGSAGLRPRKRSSELLPTPRTWPQINSQNPKLLGFVGYKVGMTHVFMIDDWPNSPTNGKEIYMPVTVLEVPPIIPLALRAYAIDGKGEPNVITEYWSSSSLQFLDITRRIHSISSFLKDDESKKKFDERFNTKLDLIKSNLDRIVYFRLLVSTQPRKIPSLGKKAPDLVEIQIGGGEKKSQLDYALNILGKEITIRDVFKEGQLIDVVGVTKGKGFAGVIKRYSVVELPRWHKHRKGSRKIGTRGPSLGTPSYTPQPGQLGFHRRTEYNKRIIKIGDEPKEINPAGGFVRYGIVRNTYVLLEGSILGSKK... | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q9UXA8 |
B9K8A0 | RS8_THENN | 30S ribosomal protein S8 | Thermotoga | MWSDPIADMLTRIRNANMVFKEYTDIPASNLKRKICEILKREGFIADYKYIEDGKQGILRVYLKYKGGRKNRERVIHGIVRVSHAGRRVYVDKDHIPKVKNGLGIAILTTSKGVLTDKEARQLGVGGEVIAYVW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | B9K8A0 |
Q65EW6 | AZOR2_BACLD | FMN-dependent NADH-azoreductase 2 | Bacillus | MTKTLYITAHPHDERASYSMAAGKAFIESYKEAHPDDEVIHLDLYRENIPQIDADVFSGWGKLQSGSGFEQLSEHEKAKVGRLNELSEQFIAGDKYVFVTPLWNFSFPPVMKAYFDAVAVAGKTFKYTEQGPIGLLTDKKALHIQARGGYYSEGQAAELEMGHRYISIMMQFFGVPEFEGLFIEGHNAEPDKAEEIKQNAIVRAKELGRTF | Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. | Q65EW6 |
B2UER8 | LOLB_RALPJ | Outer-membrane lipoprotein LolB | Ralstonia | MAMRFAHALGALMLGAGCALFSGCASLRPANDLFAGTQDADTNITRYQGRFSARYTQNNAEQSAVGSFLWRERGPDVQLELMSPLGQTLAIVSQSNQGATLELPNQPPRRAPEVDTLMQDALGFSLPVSGLRDWLRARPAPGTPARVARDAQSRPETIEQNGWTVHYVAWTDDGNNTDGAKVGIRRLDLDRPQGTNGPLSVRLVLDQ | Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | B2UER8 |
Q9PLV4 | QUEF_CAMJE | PreQ(0) reductase | Campylobacter | MRYGEKEIKEFDVENMEIWPNDAKNDYIIKITLPEFMCCCPRSGYPDFATIYLEYMPDKFVVELKAIKLYINTFMYRNVSHEASINEIYNTLKDKLKPKWIKVVGDFNPRGNVHTVIECRSDMVVPK | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | Q9PLV4 |
A4G043 | HPRT_METM5 | Hypoxanthine/guanine phosphoribosyltransferase | Methanococcus | MSRLLEESLKTCPIVKRGEYHYFIHPISDGVPLVEPELLRDISTRVIKMIDTEVDKIVTAEAMGIPIVTAVSIATDIPYVIMRKREYLLEGEIPVHQETGYSKGELYLNGINKGDKVVILDDVISTGGTLVAIINALKRAGADIRDVLCIIDRGNGQNIVEEKTGYKVKTLVKIEVVDGKVQILK | Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis. | A4G043 |
Q895L1 | EFTS_CLOTE | Elongation factor Ts | Clostridium | MITAKMVKELREITGAGMMDCKKALTETNGDTEKAVEVLREKGLAAAAKKSGRIAAEGLVETYIAEDKKNASIVEVNCETDFVAANEEFKGLVANIAKQAANTKAEDVDSFIEEKYIGSEEGTIKDAVTALVAKLGENMSVRRFKQLSVENGIIESYIHGDGKIGVLVELECEKESEVLSEVAKDVAMQVAAVNPPFLDRTFVDEETLDKEREIYRVQALNEGKPEKIVDKMVEGRIQKYYKENCLVEQVWVRNSDYTIDKYVKEKSKEVGADIKVANFVRFEKGEGIEKKEEDFAEEVKKQMQ | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | Q895L1 |
B4U081 | CH60_STREM | Chaperonin-60 | Streptococcus | MAKDIKFSADARESMVRGVDILADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAATTTAVEALKAVAQPVSGKEAIAQVASVSSRSEKVGDYISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLENPFILITDKKISNIQDILPLLEEVLKTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGGTVITEDLGLELKDATMAALGQAAK... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | B4U081 |
P75712 | ALLP_ECOLI | Allantoin transporter | Escherichia | MEHQRKLFQQRGYSEDLLPKTQSQRTWKTFNYFTLWMGSVHNVPNYVMVGGFFILGLSTFSIMLAIILSAFFIAAVMVLNGAAGSKYGVPFAMILRASYGVRGALFPGLLRGGIAAIMWFGLQCYAGSLACLILIGKIWPGFLTLGGDFTLLGLSLPGLITFLIFWLVNVGIGFGGGKVLNKFTAILNPCIYIVFGGMAIWAISLVGIGPIFDYIPSGIQKAENGGFLFLVVINAVVAVWAAPAVSASDFTQNAHSFREQALGQTLGLVVAYILFAVAGVCIIAGASIHYGADTWNVLDIVQRWDSLFASFFAVLVILMT... | Uptake of allantoin into the cell. | P75712 |
C5YUK3 | FEN11_SORBI | Flap structure-specific endonuclease 1-A | Sorghum | MGIKGLTKLLADNAPKAMKEQKFESYFGRKIAIDASMSIYQFLIVVGRTGMETLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPDMKKEELAKRFSKREDATNDLKEAVEAGDKDAVEKLSKRTVKVTAQHNDDCKRLLRLMGVPVVEAPSEAEAECAALCKNDKVFAVASEDMDSLTFGAPRFLRHLMDPSSKKIPVMEFDVAKVLEELELTMDQFIDLCILCGCDYCDSIKGIGGQTALKLIRQHGSIESILENLNKDRYQIPEDWPYQEARRLFKEPNVTLDVPELKWTPPDEEGLISFLVKDNGFNEDR... | Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It ente... | C5YUK3 |
Q8D303 | ACPS_WIGBR | 4'-phosphopantetheinyl transferase AcpS | Wigglesworthia | MAIIGIGIDIVNLERINKIILCYGNKFVKKILSFNEKKKYYELKNKKKNISVNFLAKRLAAKEAASKAFGLGMKKGLYFSQFEVLNNNLGKPYFKFNNTAKNLIKALNITNIHLSLTDERKYACATVIFEDNRTNIILS | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | Q8D303 |
Q6D037 | ORN_PECAS | Oligoribonuclease | Pectobacterium | MVDENNLIWIDLEMTGLNPDHDRIIEIATLVTDANLNVLAEGPVLAVHQSDSQLALMDDWNVRTHGASGLTDRVKVSTADERAAELETLAFLQKWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEIMAGFKKQGTHQAMDDIRESLAELVYYRENFLRL | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | Q6D037 |
Q9STQ6 | SOT3_ARATH | Cytosolic sulfotransferase 3 | Arabidopsis | MEKWMNLRDEDLTEETKTLISSLSSEKGYLGRNLCKYQGSWYYYNFLQGVLNFQRGFKPQDTDIIVASYPKSGTLWLKALTVALFERTKNPSHDDPMSHPLLSNNPHNLLSSSSPRLFSTHTPFHTLQVAVKDSPCKVVYICRDAKDSLVSRWHIVCRSLNKEEDRTILESMFESFCSGVCLFGPFWDHILSYWKASLEKPKQVLFMRYDEIKTDPHGQLKKLAEFLGCPFSKEEEKNGSLNKILEMCSLPNLSSLEVNKTGKSINGIEYKNHFRKGIVGDWKNHLTPEMGSKIDMIMKEKLKDYSEVWFENAL | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. | Q9STQ6 |
C3MZS1 | HEM1_SULIA | Glutamyl-tRNA reductase | Sulfolobus | MTSNEELLQNYCSILFTYKTIGISNLHLYYFRETEIKSLRQLINAEFAILQTCNRVEIYLYSNTNTISEINKMIQYLNNVHNEPIGNQARVICGKDSIKHLFLVASGADSLSIGEYEILSQIRSTIDMFKKLGFSGKYLQILFERAIKVGRKVREETSISKGKVGIYSLAIDEAKRQFNNFYDRKIVIVGAGEMGQKIANMLYNEGVKNVTIMNRTVEKAKQLALKFGYNYEKLDLDKLGSFDIAFISISHENLRLENKWNTLIVDITVPPLFTGNNVITLEELEKISKLNFKAREEELVKINKLVEDGIDELIYDYKKE... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | C3MZS1 |
A5IKS2 | PLSX_THEP1 | Phosphate-acyl-ACP acyltransferase | Thermotoga | MRYRSDRVKIAIDVMGGDRAPDEILKGALLASKEVEGEIVLIGPEEIVRNKGLPFVSAFEIVKMDDPPLEVLRKKNSSMHVGLKLLSEGKVDAFVSAGATGPLFLGATSIVGKLEGIERPALGVAVPSLKGATVLIDAGANAKVRPEHLVDFAFMGIAYSKVLGAENPRVGLLNMGSEENKGPDDIKRAYQLLKEFLGDTFFGNIEGHDINLGTVDVVVADGFSGNVALKTMEGTAKLVTSVLKESIKDGGFLSLLGALLMKRSFDKMKEKLDPRSYGGTFILGVKGIVVKAHGSSDAKAIKHAIKVAEKGIRMNIVQEI... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | A5IKS2 |
Q4FVG6 | Y118_PSYA2 | Nucleotide-binding protein Psyc_0118 | Psychrobacter | MKVNQDTHNAQPKLIDSNESVGDRLNILVVSGRSGSGKTSVLNILEDLGFYSIDNLPLSLVPEAVQKLVCDSGIKRIALGVDIRTPRADLSNFAAIHDSLKQAYGEEAVTVMYVTAQEETLVARFNATRRIHPLMVLDTKGVENTAYNLPAAIEKEIQLLQPICKYADIKIDTSMLNIHQLKERLRDYVGVDNQIVINLLSFGFKYGSPIDADFVFDVRILPNPHWNPTLRAATGLDAEVGEFFADYPEVTEMTGDIATFLNRWLPDFLHNNRHTVTVAIGCTGGKHRSVFITKHLQDSLQNSLPEGLTVTAKHREKHRW | Displays ATPase and GTPase activities. | Q4FVG6 |
Q4FLP6 | PANC_PELUB | Pantoate-activating enzyme | Candidatus Pelagibacter | MFYLLIFLLQMKLIKLKTDLIKAIELDRRLGFVPTMGSLHEGHKTLIKTSQKNCKKTLVSIFINPTQFNNKKDYKTYPKNLKQDLSYLKKLKVDYVYLPTIKQIYWKKNNEIKLNKSQKILCAKFRKGHFEGVLNVLDRFIELISPQKMFMGEKDFQQFFLVKNYIENKYNTKVHVCKTVREKNKLALSSRNSLLNKKSFINSGIIAKKLLSLKNEIKKNKKNYKKMIFYLKEELSKNFDIKIEYLECRNTHNLSTNIMNKPFKLFVAYYINNVRLIDNF | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q4FLP6 |
A6LPM3 | KTHY_CLOB8 | dTMP kinase | Clostridium | MKKGLFIVFEGGEGTGKTTAIDAIYDWITENNFECIKTREPGGIKISEQIRQVILSKDNKEMDAKTEALLYAAARRQHLVEKVIPALNQGVIVLCDRFIDSSLAYQGYARNLGIEEVLSINKFAIGEYMPDISVLFDLDPKIGLARIANNDCREVNRLDIEKLEFHERVREGYDIVYKNNNHRIVKIDANNTKENVINQIKNILRPKIWTNIK | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. | A6LPM3 |
Q6DCT2 | ARMD3_XENLA | Armadillo-like helical domain-containing protein 3 | Xenopus | MAQIEKKVGLLRKSSASKKPLKEKVVLMYDEIFTKEDPTKSNPRFWDELFLMKVNIEYLESKLESLDGEELMKLKDNINSLFQHCIHALRAEHQIRVVNSLQTLCALIRGVHQKNKPTSGFDIINMLMGFDKAELRMKNLMESLDLLLCGDGSESLKSLCLKLLLCLVTVTDNISQNTILEYVMINSIFEAILQILSNPLSRRQHGYDAVVLLALLVNYRKYESVNPYIVKLSIVDDENTLNGMGLVIARALFEYNRQYTDKEEENQTGFFSALTNMVGSMFIADADEKISVQTNEAILLALYEAVHLNRNFITVLAQSH... | May be involved in Golgi maintenance and protein secretion. | Q6DCT2 |
B0T1I5 | GLYA_CAUSK | Serine hydroxymethyltransferase | unclassified Caulobacter | MTAPASNITADKNAFFGADLAAADRDIFDRIGLELNRQQNQIELIASENIVSRAVLEAQGSILTNKYAEGYPGKRYYGGCEYVDEIETIAIERAKALFGAGFANVQPHSGSQANQSVFMALLQPGDTFLGMDLAAGGHLTHGSPANQSGKWFKPVSYTVRQQDQLIDYDAVEEVAQASKPKLIIAGGSAYSRQIDFARFRQIADSVGAYLMVDMAHFAGLVAGGVFPSPIPHAHVVTTTTHKTLRGPRGGMVLTNDEAIIKKVNSAVFPGLQGGPLEHVIAAKAVAFGEALQPAFKAYAQAVIDNARALAEALQTQGVNI... | 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 a... | B0T1I5 |
Q15GI4 | EGS1_OCIBA | Eugenol synthase 1 | Ocimum | MEENGMKSKILIFGGTGYIGNHMVKGSLKLGHPTYVFTRPNSSKTTLLDEFQSLGAIIVKGELDEHEKLVELMKKVDVVISALAFPQILDQFKILEAIKVAGNIKRFLPSDFGVEEDRINALPPFEALIERKRMIRRAIEEANIPYTYVSANCFASYFINYLLRPYDPKDEITVYGTGEAKFAMNYEQDIGLYTIKVATDPRALNRVVIYRPSTNIITQLELISRWEKKIGKKFKKIHVPEEEIVALTKELPEPENIPIAILHCLFIDGATMSYDFKENDVEASTLYPELKFTTIDELLDIFVHDPPPPASAAF | Catalyzes the synthesis of the phenylpropene eugenol from coniferyl acetate . Phenylpropenes are produced by plants as defense compounds with antimicrobial and antianimal properties, or as floral attractants of pollinators . Eugenol is a characteristic aromatic constituent of spices . | Q15GI4 |
Q4FQB2 | CMOB_PSYA2 | tRNA U34 carboxymethyltransferase | Psychrobacter | MLNNTILHAERELYLTLLAWAQQQPNAYEWLTQLPTWLNDIKDKANYAHAPAYQASVARLPTLTVDNVQLNSDILTIDAQLSDSERKQATALLKQLMPWRKGPFKIGSSQNEGEQAEPIFIDTEWHSDWKWQRVAPHLGNLKGRRVLDVGGGSGYHGWRMAGAGADTVIIIDPSCLFYHQFMAIRHFVGSADAHDIGRYRTHYIPVPLEALPDNSQLFDTVFSMGVLYHRQSPFEHLQQLKGQLVKGGELVLETLVIEGDANTVLVPHDRYAQMNNVYFLPSVAALIGWLEKAGFTEVRCVDVAVTSTDEQRKTEWMNYH... | 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. | Q4FQB2 |
B2ISX5 | XERDL_STRPS | Tyrosine recombinase XerD-like | Streptococcus | MRDRISAFLEEKQGLSVNSKQSYKYDLEQFLDMVGERISETSLKIYQAQLANLKISAQKRKISACNQFLYFLYQKGEVDSFYRLELAKQAEKKTEKPEILYLDSFWQESDHPEGRLLALLILEMGLLPSEILAIKVADINLDFQVLRISKASQQRIVTIPTALLSELEPLMGQTYLFERGGKPYSRQWAFRQLESFVKEKGFPSLSAQVLREQFILRQIENKVDLYEIAKKLGLKTVLTLEKYR | Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site. | B2ISX5 |
Q93MH2 | CH10_RHOPL | Chaperonin-10 | Rhodopseudomonas | MAFKPLHDRVLVRRVQSDEKTKGGLIIPDTAKEKPAEGEVVACGEGARKDSGELIAMSVKAGDRVLFGKWSGTEVTIDGAELLIMKESDILGILS | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... | Q93MH2 |
P48291 | RECA1_MYXXA | Recombinase A 1 | Myxococcus | MSKLAEKLKAVAAAVASIEKQFGRGSVMTLGGEAREQKVAVIPSGSVGVDRALGVGGYPRGRVVEVFGNESSGKTTLTLHAIAQVQAAGGVAAFIDAEHALDVSYARKLGVRVEELLVSQPDTGEQALEITEHLVRSGAVDLIVVDSVAALVPRAEIEGEMGDAHMGVQARLMSQALRKLTGAVSRSGTCIIFINQIRMKIGVMFGNPETTTGGNALKFYASVRMEIRRTGNIKDGDAVVGSKARVKVVKNKVAPPFQEAEFDLMYGSGIHRVGEVLDLGVATGLIEKSGSYFSLRGERIGQGRERAAEWLREHPDVLEA... | 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. | P48291 |
Q88XP6 | GATB_LACPL | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Lactiplantibacillus | MNFVTTIGLEVHVELKTNSKIFSPSPVQFGSEPNANTNVIDWGYPGVLPTPNKGVVEAGIKAATALHAEIEHHTYFDRKNYFYPDNPKAYQITQHEKPIAHDGWIEIEVDGKKKKIGIEEMHIEEDAGKNTHENDYSYVDLNRQGTPLIEIVSKPDIASPEEAYAYCEALRQRIQFTGVSDVKMEEGSMRVDVNISIRPAGSDKYGVKTEMKNLNSFNYVRKSLEYEEQRQQQVLMAGGKIQQETRRFDETTGQTILMRVKEGSDDYRYFPEPDIPAVDIDDDWIASVKKTIPEMPGSRRERYINEFGLTAYDAGVLTQT... | 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 ... | Q88XP6 |
B5L5Q3 | IVBS5_OXYSC | Scutellin-5 | Oxyuranus | MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFYELPADIGPCEDFTGAFHYSPREHEYIEFIYGGCEGNANNFNTLEECET | Serine protease inhibitor. | B5L5Q3 |
Q2NEZ9 | COBQ_METST | Probable cobyric acid synthase | Methanosphaera | MKYIMFQGTSSNAGKTLTVAALCNLLSRKGYRVTPFKSQNMSLNSYTTVDNDEMSIAQVMQSEAAGIEPNCNMNPILLKPKEDFTSQVIVQGKPAGNMRFDDYQNNFRTQAIKAIEESLEYLKEDYDITVIEGAGSPAEINMYDKDLANMLIARMTDADVILVADIDQGGVFASIVGTYFLIPEEDRKRIKAVIINKFRGNADVLKPGIEKIEELTNIPVIGIIPYDETLNLPEEDSASLSTHHFSENEKITIGTLRLPRISNFTDIDPLDYEEDIGIKLVSIYDDLEDLDALIIPGTRNTVNDLVELKKSGAFDKIKKI... | 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. | Q2NEZ9 |
Q6L1T9 | MBD_PICTO | Bisphosphomevalonate decarboxylase | Picrophilus | MNDLNVYGEKIRNMLLELGIYNKSDDYSPDIKYNKTFHANGYPITGLYKFLGYYDRDNNIANFPSISFTTNFSSCDVTCRVLRSGNDRIIFNGKNNEKYYKRAEKALSFLRKKYRIDAAFEFNIRINRRYRDAKGLGESAAVASATARAVAAAVFGMDAAKDRGFVSYLARHVSGSGTRSAAGNLSMWLSYPGIDDLSSIGFEIRKDDLFHFYAIPMRSRIETLNAHDYASSSIFYNAWVKSKFFDIIDIIENKFNTRMMLEYSMKDMYRLQALLISSGYIIYEKHYLDIIRKLRSSLNNYKNVYFTSDTGTSIVVMSTS... | Catalyzes the ATP-independent decarboxylation of (R)-mevalonate 3,5-bisphosphate to isopentenyl phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate. Shows no detectab... | Q6L1T9 |
A5VWL3 | TRPB_PSEP1 | Tryptophan synthase beta chain | Pseudomonas | MTQSQYRPGPDANGLFGSFGGRYVAETLMPLVLDLAREYEAAKADPKFLEELAYFQRDYIGRPNPLYFAERLTEHCGGAKIFFKREELNHTGAHKVNNCIGQVLLAKRMGKKRLIAETGAGMHGVATATVAARFGLPCVIYMGATDIERQQANVFRMKLLGAEIVPVTAGTGTLKDAMNEALRDWVTNVEDTFYLIGTVAGPHPYPAMVRDFQSIIGKETRAQLQEKEGRLPDSLVACVGGGSNAMGLFHEFLEEPSVQIIGVEAGGHGVHTDKHAASLNGGVPGVLHGNRTYLLQDQDGQITDAHSISAGLDYPGIGPE... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A5VWL3 |
Q56XY2 | QQT1_ARATH | Protein QUATRE QUART 1 | Arabidopsis | MVFGQVVIGPPGSGKTTYCNGMSQFLSLMGRKVAIVNLDPANDALPYECGVNIEELIKLEDVMSEHSLGPNGGLVYCMEYLEKNIDWLESKLKPLLKDHYILFDFPGQVELFFIHDSTKNVLTKLIKSLNLRLTAVQLIDSHLCCDPGNYVSSLLLSLSTMLHMELPHVNVLSKIDLIGSYGKLAFNLDFYTDVQDLSYLEHHLSQDPRSAKYRKLTKELCSVIEDYSLVNFTTLDIQDKESVGDLVKLIDKSNGYIFAGIDASVVEYSKIAIGQTDWDYNRVAAVQEKYMEDEEIQD | Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition . Is crucial for normal d... | Q56XY2 |
Q8YZZ2 | MEND_NOSS1 | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase | Nostoc | MPIAYKNINQLWAYIFTETLKRLGLAYAVICPGSRSTPLAVAFAQQAPNIEAISILDERSAAFFALGIAKATNRPVAIVCTSGTAGANFYPAVIEAQESRVPLLLLTADRPPELRDCHSGQTIDQMKLYGSYPNWQAELALPVSDMGMLAYLRQTLVHSWYRMQAPTPGPVHLNIPFRDPLAPIPDGTDLSYLLAKFHPEEFFAGITDTTPLPHHSPLSIPPEWLQSQRGIIIAGVAQPQQPQEYCRAIARLSQTLQWPVLAEGLSPVRNYADFNPYLISTYDLILRNQQLATRLAPDMVIQIGDMPTSKELRNWIDTHQ... | Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). | Q8YZZ2 |
C6Y4C2 | SPO2_SCHPO | Sporulation-specific protein 2 | Schizosaccharomyces | MSITMSDSSAYGEELMRERFEHLLKAYEKMALMVAEQEEFNAKIEDMALKLLSEKYDNEAYQAELFYRLSNCVEKVLHNKISITDLKTEYEEILEQTLKKECKAYERSCIENVKLKKRTEQATAYYASSSSEP | Involved in sporulation. Plays a significant role in modification of the spindle pole body prior to spore formation and is required for initiating forespore membrane formation. Assists in the localization of spo13 to the outer surface of the SPB. | C6Y4C2 |
B1VIZ8 | RS6_CORU7 | 30S ribosomal protein S6 | Corynebacterium | MRQYEVMIIVDPSQDERTVAPSLDKYLNIVREEKGSVDKVDVWGKRRFEYPIQKKEEGVYIVLDLTCESDTVRELDRVLNLNDNVLRTKVLRKDK | Binds together with S18 to 16S ribosomal RNA. | B1VIZ8 |
A9KIE9 | DRDI_LACP7 | 5-deoxyribose 1-phosphate isomerase | Lachnospiraceae | MENVTLSPDGKSVVIIDQTKLPNAIEYLTLSTSRQMYDAIFALKVRGAPAIGICAGFSIYCLAQTIEETEYDAFLLKFREYKDYLDSSRPTAVNLSWALKRMGKVVLDAKDKSIDEILSLLKAECIAIKEEDIKICKAISEYGLEFLKDGDGILTHCNAGPLATSQYGTALGPLILGKERGMNFKVFADETRPLLQGARLTAFELHEAGIDVTLICDNMASIVMKNGFINACFVGCDRVAENGDTANKIGTSGVAILAKHYGIPFYVMCPTSTIDLNCKTGDDIEIELRSEDEIKSKWYEKPMAPSDVKCYNPAFDVTDH... | Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. | A9KIE9 |
Q81ZF5 | METN2_BACAN | Methionine import ATP-binding protein MetN 2 | Bacillus cereus group | MISFNNVSKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSTKELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLKLAKVPKNEIKERVNELLKFVGLEDKANNYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTTTTQNFVRSVINDHLPESVLAKIQNGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQREIQK... | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. | Q81ZF5 |
P0DKQ5 | M7G_CONCN | Omega-conotoxin-like CnVIIB | Pionoconus | MKLTCVVIVAVLLLTACQLITADDSRGTQRHRALRSDTKLSMSTRCKGKGASCRRTSYDCCTGSCRSGKCG | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). | P0DKQ5 |
B9DM32 | RL6_STACT | 50S ribosomal protein L6 | Staphylococcus | MSRVGKKIIEIPSDVTVDIKGNVITVKGPKGELTRTFDDSMSYKLEDNTLEVVRPSDSQKDRTVHGTTRALINNMVQGVSKGFEKTLELIGVGYRAQLQGSNLVLNVGYSHPVEFKPEDGITFTVEKNTTVKVEGISKELVGATASNIRAVRPPEPYKGKGIRYQGEYVRRKEGKTGK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | B9DM32 |
A8L7B6 | UREG_FRASN | Urease accessory protein UreG | unclassified Frankia | MHLEHDRPLGGGGAPAASGGAGPRWQSPPGTPAGPAPTDRALRVGVGGPVGSGKTALVAALCRALAGRIRLGVVTNDIYTTEDADFLRSAGVLDPGRIRAVETGCCPHTAIRDDITANLDAVEDLESDLGRLDLILVESGGDNLTATFSYGLVDRQIFVIDVAGGDKVPRKGGPGVAGSDLLVVNKTDLAPLVGADLAVMARDAAAMRGGRADRPVLFTSLRSDAGASDVADWVLAQLPSPARPQ | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | A8L7B6 |
A6S8E0 | S2538_BOTFB | Solute carrier family 25 member 38 homolog | Botrytis | MSNGGNAGKKSSSYFHFGAGLGSGILSAVLLQPADLLKTRVQQSNHASLFTTIRELSQSPNSIRSFWRGTVPSALRTGFGSAIYFTSLNALRQNVARSNLLRTIGVVEQKSMVHSSSLPKLSNLANLTTGAVARAGAGFILMPMTIIKVRYESNLYAYKSIAGAGRDIFLTEGFRGFFSGFGATAIRDAPYAGLYVLFYEELKKRLSHIVHSSPQVEGLAEKVDLGLSKNMKGSTSASINFGSGVLAAGLATAITNPFDAIKTRIQLQPKKYTNLVMAGKKMVGEEGVKSLFDGLGLRMGRKAVSSALAWTIYEELIRRA... | Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. | A6S8E0 |
C6DJR2 | RHAA_PECCP | L-rhamnose isomerase | Pectobacterium | MSTPIETAWQLAKARYASLNIDVEAALEQLDQIPVSMHCWQGDDVAGFENTGGPLTGGIQATGNYPGKASTPDELRADLEQAFALIPGPKRLNLHAIYLESAQPVARNEIAPEHFRTWVEWAKRHQLGLDFNPTCFSHPLSADGFTLSHPDEKVRRFWIEHCQASRRISAYFGRELGTPSVMNIWVPDGMKDLTIDRLAFRQRLLSALDEIIAEPLDQAHHIDAVESKLFGIGAESFTVGSNEFYLGYAASRGTALCLDAGHFHPTEVISDKISSAILYVPRLLLHVSRPVRWDSDHVVLLDDETQAIAHEIVRHKLLNR... | Catalyzes the interconversion of L-rhamnose and L-rhamnulose. | C6DJR2 |
J9VQ06 | CHS2_CRYNH | Chitin synthase 2 | Cryptococcus neoformans species complex | MAYHYSHDSDRRQPHGGYNYPSNYSNPSQYSIPDSVYSGHSTNTPRVPSPGGYHQQPSPTTRAVNPAYYQPQPTASSMTSHDLMYGRPSPGPNQYGAAPADVVRGPGATTVPLSQQAPYQPYPSHTDYSDEDKSFASTTHLVSPQKEWGVGSVVPVTTIPPVNQLPYQPYQAYPPRPSPSPITHRGGTSHWHAMRKQLLERRVIKQIPLHNGNLVMDVPVPKGVIPSTKGLGVMDGEMDSMRYSAATCDPDDFMGSKFSLRQYLYGRKTELFIVMTMYNENSELLLRTLNAVIKNIAHLTTRTRSKTWGPDSWKKVVVCI... | Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. | J9VQ06 |
O25254 | HSLU_HELPY | Unfoldase HslU | Helicobacter | MSKLNMTPREIVAYLDEYIIGQKEAKKSIAIAFRNRYRRLQLEKSLQEEITPKNILMIGSTGVGKTEIARRIAKIMELPFVKVEASKYTEVGFVGRDVESMVRDLVNNSVLLVENEHKEKLKDKIEEAVIEKIAKKLLPPLPNGVSEEKKQEYANSLLKMQQRIAQGELDSREIEIEVRKKSIEIDSNVPPEILRVQENLIKVFHKEQDKVKKTLSVKEAKEALKAEISDTLLDSEAIKMEGLKRAESSGVIFIDEIDKIAVSSKEGSRQDPSKEGVQRDLLPIVEGSVVNTKYGSIKTEHILFIAAGAFHLSKPSDLIP... | ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before... | O25254 |
Q1QTL1 | RLMN_CHRSD | tRNA m2A37 methyltransferase | Chromohalobacter | MTLDTVTPRTNLLGLTREEMESFFVSLGEKKFRAAQVMKWIHHEGCADFASMTNLSKALRTRLEELAEIRGPRVVYEGTSQDGTRKWVLEVEDGSYVETVLIPAEGGKRRTLCVSSQVGCSLDCSFCSTGKQGFQRNLTSAEIIGQVWVASNSFGARRDTTNRPVTNVVMMGMGEPLLNYDNVVPAMKLMLDDNGYGLSKRRVTLSTSGVVPKLDQLGDELDVSLAVSLHAANDELRNELVPLNRKYNIATLLDACRRYLAKCDDTRMLTIEYTLIKDVNDQQHHAEELAALLADLPSKINLIPFNPFPHSGYEKPSRNQ... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | Q1QTL1 |
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