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 |
|---|---|---|---|---|---|---|
Q00874 | DR100_ARATH | DNA damage-repair/toleration protein DRT100 | Arabidopsis | MRKLLASPFSSLLAVVFISVISVVRCCSPKDQTALNAFKSSLSEPNLGIFNTWSENTDCCKEWYGISCDPDSGRVTDISLRGESEDAIFQKAGRSGYMSGSIDPAVCDLTALTSLVLADWKGITGEIPPCITSLASLRILDLAGNKITGEIPAEIGKLSKLAVLNLAENQMSGEIPASLTSLIELKHLELTENGITGVIPADFGSLKMLSRVLLGRNELTGSIPESISGMERLADLDLSKNHIEGPIPEWMGNMKVLSLLNLDCNSLTGPIPGSLLSNSGLDVANLSRNALEGTIPDVFGSKTYLVSLDLSHNSLSGRIP... | This protein is able to complement bacterial recA mutations, but its native function in the plant is not known. | Q00874 |
P28358 | HXD10_HUMAN | Homeobox protein Hox-4E | Homo | MSFPNSSPAANTFLVDSLISACRSDSFYSSSASMYMPPPSADMGTYGMQTCGLLPSLAKREVNHQNMGMNVHPYIPQVDSWTDPNRSCRIEQPVTQQVPTCSFTTNIKEESNCCMYSDKRNKLISAEVPSYQRLVPESCPVENPEVPVPGYFRLSQTYATGKTQEYNNSPEGSSTVMLQLNPRGAAKPQLSAAQLQMEKKMNEPVSGQEPTKVSQVESPEAKGGLPEERSCLAEVSVSSPEVQEKESKEEIKSDTPTSNWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISKSVNLTDRQVKIWFQNRRMK... | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | P28358 |
Q04HV8 | ECFA2_STRP2 | Energy-coupling factor transporter ATP-binding protein EcfA2 | Streptococcus | MGIALENVNFIYQEGTPLASAALSDVSLTIEDGSYTALIGHTGSGKSTILQLLNGLLVPSQGSVRVFDTLITSTSKNKDIRQIRKQVGLVFQFAENQIFEETVLKDVAFGPQNFGVSEEDAVKTAREKLALVGIDESLFDRSPFELSGGQMRRVAIAGILAMEPSILVLDEPTAGLDPLGRKELMTLFKKLHQSGMTIVLVTHLMDDVAEYANQVYVMEKGRLVKGGKPSDVFQDVVFMEEVQLGVPKITAFCKRLADRGVSFKRLPIKIEEFKESLNG | 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. | Q04HV8 |
Q8HY33 | CAH1_MONDO | Carbonic anhydrase I | Monodelphis | MANLNWSYEGENGPEHWSKLYPIANGDNQSPIDIKTKEVKHDASLKPISVSYNPATAKEIVNVSHNFQVNFEDKDNQSVLKGGPFTGSFRLRQFHFHWGTADDHGSEHTVDGVKYSSELHIVHWNSEKYSSFSEAAEKPDGLAIIAVFIKAGQANPGLQKVIDALSSIKTKGKKAPFANFDPSLLIPQSSDYWSYHGSLTHPPLHESVTWIIYREPISASSEQLAKFRSLLSTAEGEKASSILHNHRLPQPLKGRQVKASFK | Catalyzes the reversible hydration of carbon dioxide. | Q8HY33 |
B0S2N4 | LON_FINM2 | ATP-dependent protease La | Finegoldia | MKEYYTISEKKLPIIALRGLWLFPNNIQHFEVGREVSLNALNASLLRNSEIFICTQKDPMLENITKEDFYHTGVLASIKQTIKMPNGNIRVLVEAYDRAKIVDFVENDSFLEANVEVMEYDKTKYHPTDKSLTMIRMIISSFESLAEIIKKPLPQDLLGGLLNEEDPSSLIDTIAMLISLNDKDSILLLETLDMDERIELVYKFVIKEIEFLKIKEDIEERTNKEISDTQKEYFLQEQLRQIKMELGEEYDIEDTDDYANRVKKLKLKKDSEEHVLKEINRLSSMNPNNPESTVIRNYIDQVLDIPWNKKSKSSIDLKVA... | ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small pept... | B0S2N4 |
Q4WF29 | ESTB_ASPFU | Siderophore triacetylfusarinine C esterase | Aspergillus subgen. Fumigati | MGDRPTPVPLPNSEQFYLENDRGEPYLIQVSWPLHWEDKQTGRGPLPIIYIVDGNALFLTATEAAWRRAAASHFAGGGIIVAIGYPLKGKLYDARRRSFDLTPPTACAPVGYGGADVFLDFIENSVRPAVQARFPQVSLAREALYGHSYGGLLALHALFTRPQSFDCYIASSPSIWWNSLCILHEAKAFVETKKVSHDQSPSLMVSWGSWEQHPPRWADELLDHYEARKRTAAELRMADNALDLCAMLHGCSRLHALIKTEYEGEDHTSVMSCSVSRGLTMFFEDWPFHQSG | Displays specific TAFC esterase activity but does not hydrolyze fusarinine C, which has the same core structure as TAFC . Hydrolysis optimizes but is not essential for TAFC-mediated iron uptake .Both extra- and intracellular siderophores have been shown to be crucial for the virulence . Subsequent to chelation of iron ... | Q4WF29 |
Q5FRT1 | NADD_GLUOX | Nicotinate mononucleotide adenylyltransferase | Gluconobacter | MRIGLLGGSFNPAHAGHLMLARRALRALRLDQVWLMVSPGNPLKPSKGMAPFRVRLASAERIADGRRIVATDIESRLGQRFTVKTVGLLKQRFPHVRFVWLMGADGLAQLSHWKRWRRLAAMVPIAVLPRPGSVSPALRGAAASVLRHQRRPSRESPVLAERKGNAWTFLSAPQNDISATALRESGQFRPDSDQE | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | Q5FRT1 |
A0B6F6 | ARGC_METTP | N-acetyl-glutamate semialdehyde dehydrogenase | Methanothrix | MIDIGIVGGSGYTGGELLRLLSVHPSANVVCVTSRKLAGKPVTSVHQHLRGLLDLRFEAPSPAEIAQRCDVVFTAVPHGTAMDWVPELLDNGAKVIDLSADYRLPVDVFEKTYGIKHRAPRDAVFGLPELHPEVAGASLVGNPGCYPTGATLAIAPLAKAGMVDRVVFDSKSGISGAGAEPTETSHYPNLAENIRCYRVTNHRHVPEIKQELSRLQNDIRISFTPHVIPAVRGILTTAHVFVKDSFQDTIQDREFISKLYSDFYRNAKFVRLVEGVPMLGNVRCSNFCDIGFEIEKNSDRIVVISAIDNLVKGASGQAIQ... | Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. | A0B6F6 |
A8AAK3 | HIS6_IGNH4 | ImGP synthase subunit HisF | Ignicoccus | MPLTKRIIPCLDVKDGRVVKGVSFQNLRDAGDPVELAAYYQEQGADEIVFLDISATPEGRETMIEVVRRTAENLSIPLTVGGGVRSLEHIEKLLKAGADKVSINTAAVKNPLLITAAAEEFGSQAVVVAIDAKRKGNGWEVYVSAGKVPTGLDAVEWAKKAEELGAGEILLTSIDYDGTQNGYDLELTRAVSEAVKIPVIASGGAGELEHFYAVLTEGKADAALAASVFHYGKFTVGDVKKYLIQRGVPVRPCCW | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | A8AAK3 |
P83490 | 3NBB_COERA | Alpha-colubritoxin | Coelognathus | QAIGPPYGLCFQCNQKTSSDCTEARRCSPFHEKCYTLYQPDENWMKSSGLSHFGCGKQCPTAGPEGRVTCCLTPRCN | Potent postsynaptic neurotoxin. Displays readily reversible competitive antagonism at the nicotinic acetylcholine receptor (nAChR). | P83490 |
A5EW24 | ENO_DICNV | 2-phosphoglycerate dehydratase | Dichelobacter | MTITISRIHALEILDSRGNPTLQVGVTLSDGSFAQAGVPSGASTGSREALELRDGDAQRYLGKGVQKALANVKNHFAPALIGKPIYDLAALDRIMLAQDGTDFKTHLGANAILGVSLALARAKGASLKKPLYAVLCPQEEYTLPVPMMNIINGGEHADNSVDIQEFMIVPAGFDRFSEALRAGSEIFHTLKKVLKEQGLNTAVGDEGGFAPDLPSNEAAFAVIMQAIERAGYRAGEQIFLAMDAAASEFYREGRYHLASEQKAYTSAEFVDYLADLCRRYPIVSIEDGLHESDWDGWQLLTQSLGERVQLVGDDLFVTNS... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | A5EW24 |
B9KEE5 | RL22_CAMLR | 50S ribosomal protein L22 | Campylobacter | MSRALIKFIRLSPTKARLIAREVQGMNAELALASLKFMPNKGAKFIANAISSAVANGGFEANEVIVSSCRVDAGAVLKRFRPRARGSASRIRKPTSHILVEVSKAEVSAEKTTKAKKASVKKES | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | B9KEE5 |
Q54HJ2 | PESC_DICDI | Pescadillo homolog | Dictyostelium | MGGIKKFKKGEKGENLKFITRNEAVKKLQISLKIFRKLCILKGIHPRDPKKKFKGKHKTYYYSKDIKYLQNEKVLEIIRARKVFKDREKKLINKKQFGALKNLKENRPMITLDHIIKERYPTFQDALKDLDDCLSLIHLFANMDASAKVRENQILACERLAREFQYYIIQSKSLRKVFVSVKGVYYQADVMGETITWITPLNYLSKKEKEVDYGVMISFLEFYQALMKFVNYRLFTSIGLTYPPTIDDAKLRKCDSLINIFESKPQQQTKTNNTTKKSKSTTAAAAATTPVDPKLKKLEEKISKINSKEEKEIKEQIVEE... | Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. | Q54HJ2 |
P35433 | PUR1_RAT | Glutamine phosphoribosylpyrophosphate amidotransferase | Rattus | MELEESGIREECGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPKFRVHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLMPVSDINDKEKKSSETEGWVVSSESCSFLSIGARYCHEVKPGEIVEISRHGVRTLDIIPRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADL... | Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. | P35433 |
Q84F14 | HPDA_CLODI | 4-hydroxyphenylacetate decarboxylase activating enzyme | Clostridioides | MSSQKQLEGMIFDVQSFSVHDGPGCRTTVFLNGCPLSCKWCANPESWTVRPHMMFSELSCQYENGCTVCHGKCKNGALSFNLDNKPVIDWNICKDCESFECVNSCYYNAFKLCAKPYTVDELVQVIKRDSNNWRSNGGVTFSGGEPLLQHEFLHEVLLKCHEVNVHTAIETSACVSNEVFNKIFNDIDFAFIDIKHMDREKHKEQTGVYNDLILENISNLANSDWNGRLVLRVPVISGFNDSDENISDIISFMHKNNLVEINLLPFHRLGESKWTQLGKEYEYSDKGDVDEGHLEELQDIFLDNGIACYVGHVTAF | Catalyzes activation of 4-hydroxyphenylacetate decarboxylase under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM). | Q84F14 |
B2FK06 | TSAD_STRMK | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Stenotrophomonas maltophilia group | MRVLGIESSCDETGVAVYDTGLSGSAALRAHAVYSQIALHAEYGGVVPELASRDHVRKLLPLVRQTLAEAGLGVGDIDGVAYTAGPGLVGALLVGAGVARSLAWALEVPAVGVHHMEGHLLAPLMEDDPPEAPFVALLVSGGHTQLVAVDAIGQYRLLGETLDDAAGEAFDKTAKLMGLPYPGGPQLARLAEQGTPGAYRFARPMTDRPGLDFSFSGLKTQVLMAWRDSDQSEQTRADIARGFEDAVVETLSIKCERALEAAGTNVIVVAGGVGANKRLRARLQQMAERLGGRACFPRPALCTDNGAMIAFAGALRLQAG... | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct ca... | B2FK06 |
P77348 | MPPA_ECOLI | Periplasmic murein peptide-binding protein | Escherichia | MKHSVSVTCCALLVSSISLSYAAEVPSGTVLAEKQELVRHIKDEPASLDPAKAVGLPEIQVIRDLFEGLVNQNEKGEIVPGVATQWKSNDNRIWTFTLRDNAKWADGTPVTAQDFVYSWQRLVDPKTLSPFAWFAALAGINNAQAIIDGKATPDQLGVTAVDAHTLKIQLDKPLPWFVNLTANFAFFPVQKANVESGKEWTKPGNLIGNGAYVLKERVVNEKLVVVPNTHYWDNAKTVLQKVTFLPINQESAATKRYLAGDIDITESFPKNMYQKLLKDIPGQVYTPPQLGTYYYAFNTQKGPTADQRVRLALSMTIDRR... | Essential for the uptake of the murein peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate. Also transports some alpha-linked peptides such as Pro-Phe-Lys with low affinity. The transport is effected by the oligopeptide permease system. | P77348 |
A1VKS9 | SECB2_POLNA | Protein-export protein SecB 2 | Polaromonas | MPDENKQPLFQIQRVYLKGLSLEQPNSPAIFLEEQSPTLEVAVSTIAEQQADGIFESTVTVSVTAKIRDKVAFLVEAKQSGIFEIRHLPAEQLNPALGIGCPTILYPYLRANIADAITRAGFPPVHLSEINFQAFYLQQQKNKMATQPGQTAEEPAMALEQE | 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. | A1VKS9 |
Q2IID9 | ENO_ANADE | 2-phosphoglycerate dehydratase | Anaeromyxobacter | MTEIINVTAREILDSRGNPTVEVEVAVGTGDVGRAAVPSGASTGEHEALELRDGDKARYLGKGVRKAVANVIDEIAPAVVGLDASDQAALDARMIALDGTPTKSKLGANAILGVSLAAAKAAATAHGLPLYRYVGGAGARTLPVPLMNILNGGAHADSNVDIQEFMVVPLGLPTFAEALRCGAEIFHALKKVLKGKGAATGVGDEGGYAPSLASNEEALAVIMEAIGQAGYEPGKQVALALDCAASEFYDKKAGKYELEGEGKSFDGKGLVEYYAQLAAKYPIVSIEDGCDEDDWATWKLLTERLGGKLQLVGDDLFVTN... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | Q2IID9 |
A9R8D3 | NUDC_YERPG | NADH pyrophosphatase | Yersinia | MELQLTGKESGWWIVSHENKLWLPKGELPQGNAANWSLQGTTARQIGEWQGQSVWLIRQMMPSGMGSVRQLLDVDRGLFQLAGRGVQLAEFYRSHRFCGYCGHEMHASRTEWASLCNHCRERYYPQIAPCVIVAIRRGDEILLAQHVRHRGGINTVLAGFVEVGETLEQAVSREVLEESNIHIKNLRYVTSQPWPFPHSLMMAFMADYDSGELCHDPKELLNAGWYRYDQLPLLPPPGTVARRLIEDTVVLCREHSDLSQ | mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processin... | A9R8D3 |
Q9RVC3 | PYRC_DEIRA | Dihydroorotase | Deinococcus | MTITITNIKRVGSEQTESLTIENGLIKGWNLPAEGEIFDGQGGTLAPALIELHAHLREPGQTEKEDLASGLAAASAGGYGTVVCMPNTRPVIDDPALVRSLIEKARGLGFARLRPAAAVTKGEKGEQLTEMSYLKEAGAVMFTDDGLTNENARVLRLGMEYAKSLGMVISVHAEDDALRAGGVMNEGPVSESLGLPGNPAAAAAARVARDMEIVALTGARLHVQHLSTARELDIVRDAKRRGLPVTCEVCPHHLDLTDESLRTFDAMYKVAPPLRTRADADYLLEGLLDGSVDCIATDHAPHTRAEKERDLLDAPSGIAY... | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Q9RVC3 |
Q0HNG6 | AZOR_SHESM | FMN-dependent NADH-azoreductase | Shewanella | MSKVLVLKSSILGGYSQSALLVDHLIGKWEDQGATITVRDLAGKDVLPMVDGEIASGLRGGDDLTARQQEMLDLSNALVEELKANDTIVITAPMYNFNIPTQLKNWIDFVARAGVTFTYTENGPKGLVEGKRAVLITTRGGAHKDGPTDHIVPFLKTFLGFIGITDVEVVYGEALNMGPEANQKGISEAKQSLDALTV | Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. | Q0HNG6 |
Q55CV0 | NNRE_DICDI | NAD(P)HX epimerase | Dictyostelium | MNAIKFLTQNEAIVMDQLLMGKKYAFSTDSLMELAGLSCASVIQHVYPTISKKVLTICGPGNNGGDGLVASRHLVQFGYDVNIYYPKRTDKELYHNLVTQCKHEGIEFLESMPTNDQLNNDYGLVIDSIFGYSFKGDIRSPFDTIIKDSLNNIKTPIASIDMPSGWDVENGNIKNLFTPDLLISLAAPKLGSKSFKGKHYLGGRFLPKEFLKETNLTIPKFNGSNQFVDITNYQN | Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. | Q55CV0 |
Q93VY3 | NAC72_ARATH | Protein RESPONSIVE TO DESICCATION 26 | Arabidopsis | MGVREKDPLAQLSLPPGFRFYPTDEELLVQYLCRKVAGYHFSLQVIGDIDLYKFDPWDLPSKALFGEKEWYFFSPRDRKYPNGSRPNRVAGSGYWKATGTDKIITADGRRVGIKKALVFYAGKAPKGTKTNWIMHEYRLIEHSRSHGSSKLDDWVLCRIYKKTSGSQRQAVTPVQACREEHSTNGSSSSSSSQLDDVLDSFPEIKDQSFNLPRMNSLRTILNGNFDWASLAGLNPIPELAPTNGLPSYGGYDAFRAAEGEAESGHVNRQQNSSGLTQSFGYSSSGFGVSGQTFEFRQ | Transcription factors that bind specifically to the 5'-CATGTG-3' motif and with bipartite regions with 5'-CGTr-3' and 5'-YACG-3' as cores . Involved in the regulation of metabolic reprogramming during senescence by promoting the chloroplast protein degradation and the catabolism of lysine, phytol and free fatty acids v... | Q93VY3 |
Q1QVH6 | SECA_CHRSD | Protein translocase subunit SecA | Chromohalobacter | MLNTIVRKLVGSKNEREVKRMRKACEAINALEPTFEALDDASLTAKTAEFRQRLEAGESLDKLLPEAFAVVREASKRVMGMRHFDVQMVGGMTLHEGRIAEMKTGEGKTLVGTLAVYLNALTGKGVHVVTVNDYLASRDAEWMRPLYEFLGLSVGTIFSGQSSTQKREAYACDITYGTNNEFGFDYLRDNMAFSLDDKVQRSLHYAIIDEVDSILIDEARTPLIISGPVEENVDMYRRINQLSVQLEECSDEEDPTSGDFILDEKQKQVELTETGHQKLEGLLRDAEMLGQDDSLYSAQNLGLLQHVHSALRARHLYHRD... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | Q1QVH6 |
Q9Y4A8 | NF2L3_HUMAN | Nuclear factor, erythroid derived 2, like 3 | Homo | MKHLKRWWSAGGGLLHLTLLLSLAGLRVDLDLYLLLPPPTLLQDELLFLGGPASSAYALSPFSASGGWGRAGHLHPKGRELDPAAPPEGQLLREVRALGVPFVPRTSVDAWLVHSVAAGSADEAHGLLGAAAASSTGGAGASVDGGSQAVQGGGGDPRAARSGPLDAGEEEKAPAEPTAQVPDAGGCASEENGVLREKHEAVDHSSQHEENEERVSAQKENSLQQNDDDENKIAEKPDWEAEKTTESRNERHLNGTDTSFSLEDLFQLLSSQPENSLEGISLGDIPLPGSISDGMNSSAHYHVNFSQAISQDVNLHEAIL... | Activates erythroid-specific, globin gene expression. | Q9Y4A8 |
Q46YS9 | HTPG_CUPPJ | High temperature protein G | Cupriavidus | MSAPHETMSFQAEVKQLLHLMIHSLYSNKEIFLRELVSNASDATDKLRFEAIANPSLLENDADLAIRIEADTAARTLKITDNGIGMSRDEAIRNLGTIARSGTKEFFQQLSGDQQKDAALIGQFGVGFYSAFIVADKVTVETRRAGVAADEAVRWESTGDGEFTVDAITRAERGTTITLHMREGEDDFLSAWRLKSIIQKYSDHISLPIRMPKEVWDADTSAYKRTDEWESVNQASALWTRPKSDITDEQYIAFYQHIAHDNEAPLSWTHNRVEGRSEYTQLLYIPARAPFDLWDRNHKHGLKLYVKRVFIMDDAEQLLP... | Molecular chaperone. Has ATPase activity. | Q46YS9 |
Q6CZQ8 | AROK_PECAS | Shikimate kinase 1 | Pectobacterium | MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMEFFDSDQEIERRTGADVGWVFDVEGEEGFRDREEKVINELTEKQGIVLATGGGSVKSRETRNRLSARGVVVYLETTIEKQLARTQRDKKRPLLQVETPPREVLEALAKERNPLYEEIADVTIRTDEQSAKVVANQIINMLESN | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q6CZQ8 |
O75486 | SUPT3_HUMAN | SPT3-like protein | Homo | MNNTAASPMSTATSSSGRSTGKSISFATELQSMMYSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVITPEDLLFLMRKDKKKLRRLLKYMFIRDYKSKIVKGIDEDDLLEDKLSGSNNANKRQKIAQDFLNSIDQTGELLAMFEDDEIDEVKQERMERAERQTRIMDSAQYAEFCESRQLSFSKKASKFRDWLDCSSMEIKPNVVAMEILAYLAYETVAQLVDLALLVRQDMVTKAGDPFSHAISATFIQYHNSAESTAACGVEAHSDAIQPCHIREAIRRYSHRIGPLSPFTNAYRRNGMAFLAC | Probable transcriptional activator. | O75486 |
Q1GE49 | COXX_RUEST | Heme O synthase | unclassified Ruegeria | MTDASINASMTREEEASLGDYFALLKPRVMSLVVFTAFVGLMAAPIGVHPVIGFCAILFIAIGGGASGALNMWWDADIDQVMKRTKGRPIPAGKVDKGEALSLGLALSGLSVIMLALATNVFAGAFLAFTIFFYVVIYTMWLKRATPQNIVIGGAAGAFPPVIGWIAATGSMSVEPWLMFALTFLWTPPHFWALALFMRNDYDMADVPMLTVTHGRRSTRKHILVYTVILAAFALTTAFTSVGGPIYLTTAVVLNALFLKGAVQIWRRDEEICESDNFKIERSFFKLSLLYLFLHFGAILAEALLKPYGLGGW | 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. | Q1GE49 |
Q1GT67 | RL11_SPHAL | 50S ribosomal protein L11 | Sphingopyxis | MAKKISGYIKLQVPAGTANPSPPLGPALGQRGVNIMEFCKAFNAATDGLEKGTPTPTIITVYADKSFSFVTKTPPATYLIKKAANLKSGSKEPGKISGGKIARSKLAEIAEIKMKDLNANDIEQATKIIEGSARSMGLEVTEG | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q1GT67 |
O70596 | KCJ14_RAT | Potassium channel, inwardly rectifying subfamily J member 14 | Rattus | MGLARALRRLSGALEPGNSRAGDEEEAGAGLCRNGWAPGPVAGNRRRGRFVKKDGHCNVRFVNLGGQGARYLSDLFTTCVDVRWRWMCLLFSCSFLASWLLFGLTFWLIASLHGDLAAPPPPAPCFSQVASFLAAFLFALETQTSIGYGVRSVTEECPAAVAAVVLQCIAGCVLDAFVVGAVMAKMAKPKKRNETLVFSENAVVALRDRRLCLMWRVGNLRRSHLVEAHVRAQLLQPRVTPEGEYIPLDHQDVDVGFDGGTDRIFLVSPITIVHEIDSASPLYELGRAELARADFELVVILEGMVEATAMTTQCRSSYLP... | Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more posi... | O70596 |
A5UA06 | ATPL_HAEIE | Lipid-binding protein | Haemophilus | METVITATIIGASILLAFAALGTAIGFAILGGKFLESSARQPELASSLQTKMFIVAGLLDAIAMIAVGISLLFIFANPFIGLLH | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | A5UA06 |
Q2GXN6 | KAE1_CHAGB | tRNA threonylcarbamoyladenosine biosynthesis protein KAE1 | Chaetomium | MGLDITQKKRRIALGCEGSANKLGIGVILHEGDTSTVLSNVRHTFVSPAGTGFLPKDTAQHHRAFFVRVAKQALSDAGIRIADIDCICYTRGPGMGGPLASVAVAARTLALLWGKELVGVNHCVGHIEMGRTITGADHPVVLYVSGGNTQVIAYAEQRYRIFGETLDIAVGNCLDRFARALNISNDPAPGYNIEVLARKGGRVLLDLPYAVKGMDCSFSGILTRAEELAAQMKANEGKGTDGEPFTGADLCFSLQETVFAMLVEITERAMAHVGSNQVLIVGGVGCNERLQEMMGLMAADRGGSVYATDERFCIDNGIMI... | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of... | Q2GXN6 |
Q98AV7 | NADA1_RHILO | Quinolinate synthase 1 | Mesorhizobium | MSAVLPSSASLYDRVRRVIPPIEWSVFVEDIDAILNLKRQRNAVILAHNYQTPEIFHCVADIVGDSLALARKAMTVDAEIIVLAGVHFMAETAKLLNPDKTVLIPDLGAGCSLAESITAEDVRLMRQRYPSVPVVTYVNTSAAVKAESDICCTSGNALAVVKSLGAPRVIMLPDEYLAKNIAAQTKVEIIAWKGRCEVHERFTAADIRELREAHPGISVLAHPECPPEVVAEADFAGSTAAMSDYVARHRPARVVLMTECSMSDNVAVEHPEVDFVRPCNLCPHMKRITLANIRTALEENRHVVTIDPHVAERARWAVER... | Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | Q98AV7 |
Q9WV50 | NIP7_RAT | kDa93 | Rattus | MRPLTEEETRVMFEKIAKYIGENLQLLVDRPDGTYCFRLHNDRVYYVSEMILKLAANISGDKLVSLGTCFGKFTKTHKFRLHVTALDFLAPYAKYKVWIKPGAEQSFLYGNHVLKSGLGRITENTSQYQGVVVYSMADVPLGFGVAAKSTQDCRKVDPMAIVVFHQADIGEYIRHEETLT | Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. | Q9WV50 |
B8E4M8 | COBT_SHEB2 | N(1)-alpha-phosphoribosyltransferase | Shewanella | MSQSAVSFQISPVSKTQDPLIQQKIDLKTKPPGALGQLESLALQIARVQATDSQQTDQPQNTVLKIVHPTMLVFAGDHGIAAEGVSIAPSEVTRQMVQNFAHGGAAINVFCRQVGFTLEVIDCGILTPVEGVEGIIDQRLGAGTGAIHLEPAMALETVDKGFAMARDLIERHHQAGCNLVAFGEMGIGNTSAAAAIMAAIMQLDVIDCVGRGTGINSETLERKLMLIELALLLHQSALTGPKSVLACLGGFEIVQMTGAMLAAAERKMLVVVDGFIATAAALVAVQIAPNVRDYLIFAHQSDEQGHQRMLEFLQAKPLLS... | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | B8E4M8 |
O33405 | MBHS_AFIC5 | Membrane-bound hydrogenase small subunit | Afipia | MTPTETFYEVMRRQGVTRRSFLKFCSLTATALGLGPAYTSEIAHAMETKPRTPVLWLHGLECTCCSESFIRSAHPLVKDVVLSMISLDYDDTLMAAAGHQAEAALADTIERYKGNYILAVEGNPPLNEDGMFCIIGGKPFVDQLRYAAKHAKAIISWGSCASHGCVQAARPNPTRATPVHQVITDKPIIKVPGCPPIAEVMTGVITYMLTFGKLPELDRTGRPKMFYSQRIHDKCYRRPHFDAGQFVESFDDEGARRGYCLYKVGCKGPTTYNACSTIRWNEGTSFPIQAGHGCIGCSEEGFWDKGSWYARLQDIHQFGI... | This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. | O33405 |
B4RVU1 | RECA_ALTMD | Recombinase A | Alteromonas | MDDNKSKALTAAVGQIEKQFGKGAIMRLGDNQAMDIEAISTGSLTIDIALGIGGLPCGRVVEIYGPESSGKTTLTLQVIAEAQKNGKTCAFVDAEHALDPVYAEKLGVNIDELLVSQPDTGEQALEICDMLVRSGAVDVVIVDSVAALTPKAEIEGDMGDSHVGLQARLMSQALRKLTANIKRSNTLCIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGAVKEGDEVVGNETRVKVVKNKVAPPFKQAEFMIRYGEGISKEAELIDLGVKQKLVDKAGAWYSYKGDRIGQGKANVMKYLKEHPETANEIET... | 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. | B4RVU1 |
D2RXF6 | NNRD_HALTV | ADP-dependent NAD(P)HX dehydratase | Haloterrigena | MGRLQRTLSNISEEEIDNGRIGIVAGAIEYPNQPALVGRAALRTGSDHVRALVADPIYEIVAGQDPNLLVDRYAGEQFEESAVERTREMSEWADALVIGPGLVDADPQAVCEAIDTIDVPMVVDALALEPSLDADLSNAVLTPSGAEVGPIRDEYGSLEAFSEETGAVITLTGDVDEIVADGERLENETGTSAMTVAGTGDTMVGIVASLLGQGMDRREAAELGAWILGKTGELATANHGPGVVATDVIERIPDTIR | Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-depen... | D2RXF6 |
A6TNN7 | HSLO_ALKMQ | Heat shock protein 33 homolog | Alkaliphilus | MSSRIIRATAANSSIRAFVANTTNLVEKARGFHQTSPVASAALGRTLTATSMMGVMLKGEKQKITTKINGGGPLGVILVVGDSEGNVKGYVGNPQVESTNIRPGKLDVGAAVGSDGEITVIKDLGMKKPYVGTAPLVSGEIGEDFATYFLNSEQQPSAVSLGVLIDIDYRIKASGGFIIQVLPNVQEAVLAKLESRIGQLESITVMMEQGMNEVDILNHVLEGMDPKIVETYEVDFECDCNVARFEKGLISIGRQEIREMIEEDENTELVCHFCNKKYHFNKEQLQGLLDEM | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | A6TNN7 |
A4WT69 | NUOB1_CERS5 | NDH-1 subunit B 1 | Cereibacter | MSWTIGRPGAEAPEDRMAASHLFTRLDDLVAWSRKHSLWPFNFGLSCCYVEMATALTPVYDQARFGAEVIRSTPRQADLLIVSGTVFRKMAVPLYRLYQQMREPRWVISMGACANSGGMYDIYSVVQGVDSFLPVDVYVPGCPPRPEALMEALVLLQSKIATEARPLQIRMGETGPARPFDPVPRRDALREGRMSVARLADPEST | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | A4WT69 |
A5GIH4 | PSBH_SYNPW | Photosystem II reaction center protein H | unclassified Synechococcus | MAQRTRLGDLLRPLNSEYGKVVPGWGTTPVMGIFMVLFLVFLLVILQLYNQSLILEGINVNWNGAG | One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a c... | A5GIH4 |
Q4A8N4 | UNG_MESH7 | Uracil-DNA glycosylase | Mesomycoplasma | MESKLSFESFFYNESKKAYFQKLMEKLDEEYEKYQVFPNKKDLFRAIELTNFATLKIVIIGQDPYHRKGQADGLAFSTRTKILPPSLRNLFLEIKNAYPNFSKENGNLENWAKQGVLLLNHVLTVRKSSPNSHKNIGWEVFSSNLINFIVKNKVDIVFLLLGKKAKLAVKNINLEKQKVFAYSHPSPFSFAKSLKNSMVFRKINDFLKEKKRLEINWNL | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | Q4A8N4 |
Q2J8L3 | HIS6_FRACC | ImGP synthase subunit HisF | Frankia | MSVAVRVIPCLDVDAGRVVKGVNFTDLRDAGDPVEMARLYDAEGADELTFLDITASSGDRETTYDIVRRTAEQVFIPLTVGGGVRSVDDVNRLLRAGADKVGINTAAVARPELVRECAHRFGNQCIVISVDARRPPGPDGPRFEVTTHGGRKGTGIDAVAWTARVVELGAGEILLNSMDADGTRDGYDLEMICAVRAEVDVPVIASGGAGDLAHFAPAIDAGADAVLAASVFHFGQLRIGEVKTALRGAGVPVR | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | Q2J8L3 |
Q00763 | COMT1_POPTM | S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase 1 | Populus | MGSTGETQMTPTQVSDEEAHLFAMQLASASVLPMILKTAIELDLLEIMAKAGPGAFLSTSEIASHLPTKNPDAPVMLDRILRLLASYSILTCSLKDLPDGKVERLYGLAPVCKFLTKNEDGVSVSPLCLMNQDKVLMESWYYLKDAILDGGIPFNKAYGMTAFEYHGTDPRFNKVFNKGMSDHSTITMKKILETYKGFEGLTSLVDVGGGTGAVVNTIVSKYPSIKGINFDLPHVIEDAPSYPGVEHVGGDMFVSVPKADAVFMKWICHDWSDAHCLKFLKNCYDALPENGKVILVECILPVAPDTSLATKGVVHVDVIM... | Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins. | Q00763 |
Q5WGC3 | RNZ_ALKCK | tRNase Z | Alkalihalobacillus | MELHFLGTGAGVPAKKRNVSALAIRFLERNGTVWLFDCGEATQHQFLHSPLSLAAVEAIFITHLHGDHILGLPGLLSSRSFQGAETPLDIYGPKGLEAFVIQALETTKTKLRFPIRFHVLAEGRIRDEEKLSVDALALDHPVESYAFRIKEQDKPGTLDAEALKAMGVPPGPLYAQLKKGETVKLADGRIVNGSAFLDESIRGRTVVIAGDTAPVKAMEAFASGADVLVHEATFASNKKDDAHLYGHSTIADACALAKRAAVGQLILTHVSSRYARNENEYRDEAAALLPNVIIAEDLFVFELEKAGRKKRD | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. | Q5WGC3 |
Q52TG6 | MATK_TYPAN | Intron maturase | Typha | MKQLHVQRYLEKVRSRKQHFLYPLLFKEYIYAFAHDYGLNGSIFYEPAEIIGNDNKSSSVLVKRLIIRMYQQNYLINSINHSNQNRFIGHNNYFYSHFFSLMISESFAVIMEIPFSLRLVSSPEEKEIPQFQNLRSIHSIFPFLEDKLSHLNYVSDILIPHPIHFEILVQILQCRIQDVPSLHLLRFFLHEYHNWNSLITSKKSIYVFSKENKRLFRLLYNFYVFECEFVFVFLRKQSSYLRLTSFGTFLERIHFYGKIEHLLVVYRNYFNKTLWFFTDPFMHYVRYQGKAILASKGTHLFMKKWKCYLVNFWQYYFHFW... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q52TG6 |
Q10SU5 | DRM2_ORYSJ | Protein DOMAINS REARRANGED METHYLASE 2 | Oryza sativa | MVDWASDSDNDKFEWDTDGEAETSSAPALRNIDAPGPSTRLPQDANGKANGSGALVAEFMGMGFPKEMILKAIKEIGDTDTEQLLELLLTYQAIGGDASVGNCSASACAPQTLEVDEEEDDTNWDEYDTAGNCDRTPHSDGSGDEDFFQEMSEKDEKMKSLVNMGFPEDEAKMAIDRCGLDAPVAVLVDSIYASQEAGNGYSANLSDYEDTEFSSFGGRKKTRFVDGSKKRKRYGSGPSGNQVPFDGSHEEPMPLPNPMVGFSLPNERLRSVHRNLPDQALGPPFFYYENVALAPKGVWTTISRFLYDIQPEFVDSKYFC... | Involved in de novo DNA methylation. Required for CpG and non-CpG methylation. Required for normal establishment and maintenance of RNA-directed DNA methylation (RdDM) mediated by small interfering RNAs (siRNAs). Regulates proper plant development in both vegetative and reproductive stages through DNA methylation. | Q10SU5 |
Q8FN57 | CLPX_COREF | ATP-dependent Clp protease ATP-binding subunit ClpX | Corynebacterium | MARMQESADLLKCSFCGKSQKQVKKLIAGGAVYICDECIELCNEIIEEELGQAQGQEEEHGELPKPSEISAFLDKYVVGQDQAKRILSVAVYNHYKRLRAHEQIGGRRRRDEEDTELIKSNILLLGPTGSGKTYLAQTLAKLLDVPFAIADATSLTEAGYVGEDVENILLKLLQAADFDVERAQRGIIYIDEVDKISRKSENPSITRDVSGEGVQQALLKILEGTVAAIPPQGGRKHPNQDFIQLDTTNILFIVAGAFSGLEKIIGERRGKKGLGFGVEVASKKDEEKEDIFKDVRPEDLVKFGLIPEFIGRLPVVATVA... | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Q8FN57 |
Q04QV4 | DUT_LEPBJ | dUTP pyrophosphatase | Leptospira | MKIPIKKLRSNAELPVLQTKHAAGYDVHACLDSNLILEPNKVTLVPTGLSFEIPQEYHFEIRPRSGFSTKNQILIPNSPGTIDSDYRGELMIPLFNLGNIPFVIEHGMRIAQLLIRETHYTNWELVSEFTDTTERGTGGFGSTGH | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | Q04QV4 |
Q0I8P6 | CHLN_SYNS3 | Light-independent protochlorophyllide reductase subunit N | unclassified Synechococcus | MSVNLLKETGPREVFCGLTSIVWLHRRMPDAFFLVVGSRTCAHLIQSAAGVMIFAEPRFGTAILSERDLAGLADAQDELDRVARELLERRPEIRTLFLVGSCPSEVIKLDLARAAERLNDELRGRVQVVNYSGSGIETTFTQGEDGALSALVPLLPSTDQRQLLMVGTLADAVEDRLTHLFGRIGIDSVCSLPPRKSTELPAVGPGTTVLLTQPYLTTTARLLRDRGARVLTAPFPLGAEGSRSWMEAAAKDFQINADQVASVLDPLVARAQSALAPHREILNGKRIFLLPESQLELPLARFLQRECGMELVEVGTPYLN... | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Q0I8P6 |
P27814 | KLRBC_MOUSE | Natural killer cell surface protein P1-40 | Mus | MDTASIYLGLKPPRTLGAWHESPPSLPPDACRCPRSHRLALKLSCAGLILLVLTLIGMSVLVRVLVQKPSREKCCVFIQENLNKTTDCSVNLECPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLKITGVTENGSCASILGDKVTPESCASDNRWICQKELNHETPSNDS | Plays a stimulatory role on natural killer (NK) cells cytotoxicity. Activation by cross-linking of the receptor induces Ca(2+) mobilization and interferon-gamma production. | P27814 |
Q5XII0 | EPDR1_RAT | Mammalian ependymin-related protein 1 | Rattus | MLTRAPRRLVQGPRETWLLGGLWVWILCGLGMAGSPGTPQPCQAPQQWEGRQVLYQQSSGHNSRALVSYDGLNQRVRVLDERKALIPCKRLFEYILLYKDGVMFQIEQATKLCAKIPLAEPWDPLDIPQNSTFEDQYSIGGPQEQIMVQEWSDRRTARSYETWIGVYTAKDCYPVQETFIRNYTVVLSTRFFDVQLGIKDPSVFTPPSTCQTAQPEKMKENCSL | Binds anionic lipids and gangliosides at acidic pH. | Q5XII0 |
Q815J4 | Y5156_BACCR | Nucleotide-binding protein BC_5156 | Bacillus cereus group | MTENNDIKMVIITGMSGAGKTVALQSFEDLGYFCVDNLPPMLLPKFIELMADSKGKMNKVALGIDLRGREFFEHLWGALDDLSERTWIIPHILFLDAKDSTLVTRYKETRRSHPLAPTGLPLKGIEAERNLLTDMKARANIVLDTSDLKPKELREKIVHLFSTETEQAFRVNVMSFGFKYGIPIDADLVFDVRFLPNPYYIPHMKPLTGLDEEVSSYVLKFNETHKFLEKLTDLITFMLPHYKREGKSQLVIAIGCTGGQHRSVTLTEYLGKHLKPEYSVHVSHRDVEKRKGH | Displays ATPase and GTPase activities. | Q815J4 |
Q9VCA2 | ORCT_DROME | Organic cation transporter protein | Sophophora | MGYDDVITHLGEFGPYQKRIYYLLCLPAIVCAFHKLAGVFLLAKPDFRCALPYENGSIYELSPHLWNLSYPENERCSYYDVDYTEEYLNGSIPRSSNETKTCSSYVYDRSKYLNSAVTEWNLVCSRSLLSATSDSLFMLGVLLGSLIFGQMSDKLGRKPTFFASLVLQLIFGVLAAVAPEYFSYTISRMIVGATTSGVFLVAYVIALEMVGSSYRLFAGVAMQMFFSVGFMLTAGFAYFIHDWRWLQIAITLPGLLFLCYYWIIPESARWLLMKGRKDEAFVIIEKAAKENKVEVPNEIYEQLVDEVAEKKKQDEMAASQ... | Probably transports organic cations. | Q9VCA2 |
Q7SDY6 | SLU7_NEUCR | Pre-mRNA-splicing factor slu-7 | Neurospora | MPPPPPNRREQATAAPSSTDKSETGAGAARKEDNIYIPSYISKQPFYVSGLDNEEGDSLLHQRARQQEEDKAAQAAALLARGKKAGPARTKWVKGACENCGAMGHKKKDCLERPRKFGAKATGKDIQADRIVRDVKLGYEAKRDVYSAYDPKQYMEVVEEYNMLEEARRALQGDQKTPDGEGADGPEDDKSGFKYDEESDMGRDRATTKQSMRIREDTAKYLLNLDSDSAKYNPKKRALVDAGAIADKSAALFAEESFLRASGEAAEFEKAQRYAWEAQERSGDTSLHLQANPTAGEILRKKESEEREAKRRKRAEELAN... | Involved in pre-mRNA splicing. | Q7SDY6 |
Q9PGR6 | G6PI_XYLFA | Phosphohexose isomerase | Xylella | MHNGFDALQLHANRLRGVTIPDLLAAELKRPEQYARQVGPLYFNFARQKYDCVALEALFALARNHNVAGAFQRMFCGEQVNVTEGRAVLHTALRGDLSGTSVAVAAYTAAAKVRERMYALIAGLDASEVTDIISVGIGGSDLGPRLVVDALRPISQGRFRVHFVSNVDGAAMRRTLDMLDPSRTAGILISKTFGTQETLLNGRILYDWLGGSERLYAVSANPERAAHAFDIVPTQVLPIWDWVGGRYSLWSAVGFPIALAIGSQRFEELLAGAAEFDAYALRVPLEENVAVLHGLTAVWNRNFLGCATYAVMAYDQRLAL... | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q9PGR6 |
B0U8E7 | SECA_METS4 | Protein translocase subunit SecA | Methylobacterium | MLGAIAKKIFGSSNDRRVKGYRPRVAAINALEPEMEALSDEALRARTDALKAEVAAGKSLDDILVPAFATVREAAKRVLGQRHFDVQLIGGMVLHEGGIAEMKTGEGKTLVATLATYLNALAGQGVHVVTVNDYLARRDAEWMGRVYGFLGLSTGIIVHGLDDAERKAAYACDITYGTNNEYGFDYLRDNMKYELGQMVQRGHAFAIVDEVDSILIDEARTPLIISGPIDDRSDLYVAIDALMPRLAREDYDLDEKQRTVSLTESGNEHIEELLREAGVLREGDLYDAHNITIVHHVNQALRAHTLFTRDKDYIVRNDEV... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | B0U8E7 |
P11697 | GGI1_STAHA | Gonococcal growth inhibitor I | Staphylococcus | MQKLAEAIAAAVSAGQDKDWGKMGTSIVGIVENGITVLGKIFGF | Has hemolytic activity and also inhibits the growth of gonococci. | P11697 |
P68307 | NU3M_BALMU | NADH dehydrogenase subunit 3 | Balaenoptera | MNLLLTLLTNTTLALLLVFIAFWLPQLNVYAEKTSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWAIQSNNLNTMLTMALFLISLLAASLAYEWTQEGLEWAE | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. | P68307 |
C0HLT2 | IBBB6_HYAOR | Bowman-Birk type proteinase inhibitor B6 | Hyacinthus | GRRPCCNECGICDRSLDPMCICEDLVPQCHEGCQACEKVDTGTPMYQCRSFEYYHCGPICY | Serine protease inhibitor . Inhibits trypsin (Ki = 30 nM) and weakly inhibits chymotrypsin (Ki = 550 nM) . Does not inhibit bacterial subtilisin . | C0HLT2 |
A0SE59 | CA13_CONMR | Alpha-conotoxin-like Mr1.3 | Conus | MGMRMMFTMCLLVVLATTVISFTSDRASNGRNAAAKDKASDLNALNVRGCCSHPACRVHYPHVCYGRR | Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. | A0SE59 |
P46663 | BKRB1_HUMAN | B1 bradykinin receptor | Homo | MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLLVFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKANLFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQAVPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRCGGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFFAFTNSSLNPVIYVFVGRLFR... | This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation. | P46663 |
Q9UTN4 | PFS2_SCHPO | Polyadenylation factor subunit 2 | Schizosaccharomyces | MERAENARIIQKPMTRRTVDYGSGLSKYIVNRHLRSNRYHIHVPRPNPNQIINLYPPYEYKYNNTSSLCTKYIHTSANKARHVINVVRWTPDGRRLLTGSSTGEFTLWNGLTFNFELINQSHDYAVRCAEWSTDGRWLISGDGGGMVKYFEPNLNNVKIVQAHEMEVRDVAFSPNDSKFVTASDDGSLKVWNFHMSTEELKLTGHGWDVKTVDWHPSKGLLASGSKDNLVKFWDPRTGTCIATLHGHKNTIMQASFQKNFGSNYLATVSRDSTCRVFDLRAMKDVRVLRGHEKDVNCVTWHPLYPNLLTTGGSDGSVNHY... | Required for 3'-end cleavage and polyadenylation of pre-mRNAs. Also involved in chromosome segregation where it has a role in chromosome attachment to the mitotic spindle. | Q9UTN4 |
A3QEI8 | SYS_SHELP | Seryl-tRNA(Ser/Sec) synthetase | Shewanella | MLDPKFLRTELEATAERLATRGFILDVDRLSKLEEKRKSLQVATEELQASRNAISKSIGQAKAKGEDVAPIMAKVGDLGAELSSKEAELKQLLEELNAIAMSVPNLPDESAPIGADENDNVEIRRWGEPKQFDFDVKDHVDLGEQHAGLDFKSAVKITGSRFIVMKGQIARMHRALTQFMLDLHTTEHGYTETYVPLLVNEDSLLGTGQLPKFGEDLFHTKPATEEGQGLSLIPTAEVPLTNLARDTIIDEDELPIKMTAHTACFRSEAGSYGRDTRGLIRQHQFDKVELVQLVKPEDSMAALESLTQHAETVLQRLGLP... | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). | A3QEI8 |
B7J4D2 | RIMP_ACIF2 | Ribosome maturation factor RimP | Acidithiobacillus | MEDRLYEGIAQQAGIAGCTLVDARMVRTGRAVALQVFIEKDETTAVTIEDCAAVSRQLSLWLDVENPIHGAYRLEVSSPGLDRPLKNLHDFERFKGSQAEIHLHGLTQGRRRLQGELLGVEDQKIVLKNAEGRWTFALDDIHKARLVPQW | Required for maturation of 30S ribosomal subunits. | B7J4D2 |
Q3M704 | CH601_TRIV2 | Chaperonin-60 1 | Trichormus | MAKRIIYNENARRALERGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTNDAAGDGTTTATVLAHAIVKEGLRNVAAGANAILLKRGIDKATGFLVDRIKEHARPVEDSKSIAQVGSISAGNDDEVGQMIAEAMDKVGKEGVISLEEGKSVTTELEITEGMRFDKGYISPYFATDPERMEAIFDEPFLLLTDKKIALVQDLVPVLEQVARAGRPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGQLITEDAGLKLENTKLESLGKAR... | 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. | Q3M704 |
A8A2S4 | MURR_ECOHS | MurPQ operon repressor | Escherichia | MLYLTKIRNAESEFTGNEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASREKTNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEWRSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRLK | Represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). Binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate, the substrate of MurQ, is the specific inducer that weakens binding of MurR to the operator. | A8A2S4 |
A6TAX5 | MINE_KLEP7 | Cell division topological specificity factor | Klebsiella | MALLDFFLSRKKNTANIAKERLQIIVAERRRGDAEPHYLPQLRKDILEVICKYVQIDPEMVSVQLEQRDGDISILELNVTLPETEESKS | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | A6TAX5 |
Q5WEG9 | COAE_ALKCK | Dephosphocoenzyme A kinase | Alkalihalobacillus | MRIGLTGGIASGKSLVATYLEKQGIPVVDADKLARQVVEPGEPALAQIVATFGEHVLQDDGTLDRKQLGAIIFGDEQKRKQLNEIVHPAVRQSMKKQADLYEQRGYTRVVLDIPLLYESNLFHMVNQVWLVYVDEATQLRRLIERDGLTETEAKQRIAAQMPLTAKKAQADVLIDNNGTKENTYRQVYDALAKTAHE | Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | Q5WEG9 |
B9DLM7 | GUAA_STACT | Glutamine amidotransferase | Staphylococcus | MEMAKEQEMILVLDFGSQYNQLITRRIREMGVYSELHDHEISIEEIKKMNPKGIILSGGPNSVYEEGSYTIDPEIYNLGVPVLGICYGMQLTTKLLGGKVERANEREYGKAIIHAKADELFFGLPEEQTVWMSHSDKVIEIPEGFESIADSPSTPYAAIEDKERRIYGVQFHPEVRHTEYGNDILRNFVRRICDCTGEWTMENFIDLEIEKIREQVGDRKVLCAMSGGVDSSVVAVLLHKAIGDQLTCIFVDHGLLRKGEGDMVMEQFGEGFNMNIIRVNAKDRFMDKLKGVSDPEQKRKIIGNEFVYVFDDEASKLEGV... | Catalyzes the synthesis of GMP from XMP. | B9DLM7 |
Q61549 | AGRE1_MOUSE | EMR1 hormone receptor | Mus | MWGFWLLLFWGFSGMYRWGMTTLPTLGQTLGGVNECQDTTTCPAYATCTDTTDSYYCTCKRGFLSSNGQTNFQGPGVECQDVNECLQSDSPCGPNSVCTNILGRAKCSCLRGFSSSTGKDWILGSLDNFLCADVDECLTIGICPKYSNCSNSVGSYSCTCQPGFVLNGSICEDEDECVTRDVCPEHATCHNTLGSYYCTCNSGLESSGGGPMFQGLDESCEDVDECSRNSTLCGPTFICINTLGSYSCSCPAGFSLPTFQILGHPADGNCTDIDECDDTCPLNSSCTNTIGSYFCTCHPGFASSNGQLNFKDLEVTCEDI... | Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development. | Q61549 |
P51641 | CNTFR_CHICK | Growth-promoting activity receptor subunit alpha | Gallus | MANPVPSACCVVLAAVVVVYAQRHSQQDSHIQYERVGADVTMKCGSMDWDAAVTWTANGTDIDDSHLNGSYLILKNVDLTQSGQYSCYEGSSWHLKYQTYLRVGVPPKEPVLMCRSNNYPKGFYCSWHLPSPTYIPNSFNISVIHGTREMVCEKDIFPKNRCHIRYLQLFSTVKYKVTLTVTNALGKNSTTLTFDEFAIVKPDPPESVVAKPVPNNPRRLEVSWQNPSSWPDPESFPLKFFLRYRPLILDQWQHVELSDGTSHTITDAYAGKEYIIQVAAKDNDIGTWSDWSVAVHATPWTEEPKHLTTEVQITETTSTS... | Binds to CNTF (GPA). The alpha subunit provides the receptor specificity. | P51641 |
Q03MP9 | DTD_STRTD | Gly-tRNA(Ala) deacylase | Streptococcus | MKIVIQRVQSASVAIEDSTVGTIKQGLLLLVGVGPEDTKEDLDYAVRKIINMRIFSDEDGKMNLSVKDIGGQILSISQFTLFADTKKGNRPAFTGAAKPDMASQFYDDFNQSLSSYVPVERGRFGADMQVSLVNDGPVTVILDTKNR | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | Q03MP9 |
Q3IYM7 | DNAK_CERS4 | Heat shock protein 70 | Cereibacter | MAKVIGIDLGTTNSCVAIMDGAQPRVIENSEGARTTPSIVGFTDSERLVGQPAKRQAVTNPSNTVFAVKRLIGRRVGDAEVEKDKKLVPYSIVNGGNGDAWVEVRGEKYSPSQISAFILQKMKETAEAYLGESVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKDTKTIAVYDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVNYLADEFKKEHGVDLTLDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDRNTGQPLHMVMKLTRAKLESLVGDLIKKSLKPCEAAL... | Acts as a chaperone. | Q3IYM7 |
P45288 | SAPD_HAEIN | Peptide transport system ATP-binding protein SapD | Haemophilus | MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEISGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSPNKRRKLVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTAPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIKQHEFS... | Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. | P45288 |
P19177 | H2A_PETCR | Histone H2A | Petroselinum | METAGKAKKGFGGRKGGPRKKSVTRSVKAGLQFPVGRIGRYLKKGRYAQRVGTGAPVYLAAVLEYLAAEVLELAGNAARDNKKTRIIPRHLLLAVRNDEELGKLLAGVTFAHGGVLPNINPVLLPKKTAEKAAKEPKSPSKAGKSPKKA | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated v... | P19177 |
Q8W9N5 | NU2M_DUGDU | NADH dehydrogenase subunit 2 | Dugong | MNPLILSMILTTLAMGTMATMLSSNWLLAWMGLEMNMLAMIPILTMNPNPRSTEAATKYFLTQATASMLLMMAIMINFMLSGQWSITKLPNTTVSSMALAALMMKLGLAPFHFWVPEVTQGTSLTSGMILLTWQKLAPLSILYQIDTSVDITILTVSGLLSILVGGWGGLNQTQLRKILAYSSIAHMGWMLIIMPYNPSLTILNLLIYILMTLSIFMIMMNNHSTSTLTLALLWNKAPMMMILLTITLLSLGGLPPLSGFMPKWLIIHELTKNDSIILPMSMAMFALLNLYFYMRLIYSSSLTMFPSTNNMKMKWHFTNR... | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. | Q8W9N5 |
Q657C0 | HFA6B_ORYSJ | Heat stress transcription factor 1 | Oryza sativa | MLKPQTPRARRAAHPNSHMASSSSSSSLCRLLIPRPTTRRFSGGGGEGGMAAAAPVKREVKPEAGEGWGGGDLGVVPPPPRPMEGLGEAGPAPFVAKTYEMVADAATDAVVSWGPGGSGASFVVWDPHALAAGVLPRFFKHANFSSFVRQLNTYGFRKVTPDRWEFANEAFLAGQKHLLKNIKRRRVSKPLVDSQLRNKASVVFGQPEAPGEVVSLKRDRAALRAEVIMLKQQYNACKSQLIAMEEMVRNIERRQQQTIGFFAKVLTNPAFVQQVLLNYVNKNGLRGAAKRQRLMENEEQHADSPLNKGMEAASVMEADV... | Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE). | Q657C0 |
Q1ACI3 | EFTU_CHAVU | Elongation factor Tu, chloroplastic | Chara | MAQEVFQRTKPHVNIGTIGHVDHGKTTLTAAITMTLAVNSTCTPKKYDEIDAAPEERARGITINTAHVEYETASRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPSIVVFLNKEDQVDDEEILQLVDLEVRESLINYEFPGDKVPVVAGSALMALQALTEKPNTLRGENKWVDKIYELMDAVDSYIPTPKRDIEKPFLMPIEDVFSIQGRGTVATGRIERGILKLGDIVELIGLNEKIRSTVVTGLEMFRRLLEQGFAGENIGVLLRGIEKKDIERGMVIAQPGTIEPHTRFEAQV... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q1ACI3 |
B8E9X5 | FLGH_SHEB2 | Basal body L-ring protein | Shewanella | MARYLVLAVALLLAACSSTQKKPLADDPFYAPVYPEAPPTKIAATGSIYQDSQASSLYSDIRAHKVGDIITIVLKESTQAKKSAGNQIKKGSDMSLDPIFAGGSNVSIGGVPIDLRYKDSMNTKRESDADQSNSLDGSISANVMQVLNNGSLVIRGEKWISINNGDEFIRVTGLVRSQDIKPDNTIDSTRMANARIQYSGTGTFADAQKVGWLSQFFMSDWWPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | B8E9X5 |
Q9V8Y2 | OB56A_DROME | General odorant-binding protein 56a | Sophophora | MNSYFVIALSALFVTLAVGSSLNLSDEQKDLAKQHREQCAEEVKLTEEEKAKVNAKDFNNPTENIKCFANCFFEKVGTLKDGELQESVVLEKLGALIGEEKTKAALEKCRTIKGENKCDTASKLYDCFESFKPAPEAKA | Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid. | Q9V8Y2 |
Q5HME5 | ALR_STAEQ | Alanine racemase | Staphylococcus | MSEKFYRATYLNVNLDAILANYQNFNQLHANKTVISVIKANGYGLGSVKIAQHLMRHGATFFAVATLDEAIELRMHGVDAKLLVLGVVPTEDIEKAIQHRVALTVPSKAWLKETIKQIPDDNQKNLWLHVKLDTGMGRIGMKDIDEYKEVVDLINKRDHLVFEGVFTHFASADEPGSSMNEQYTLFKEMVNQVEKPIYIHCQNSAGSLLMDGQFCNAIRLGISLYGYYPSEYVKDNVKVHLRPSAQLVSETVQVKTLKVGETVSYGRTFIADEEMTIAILPIGYADGYLRSMQGAFVNVNGSQCEVIGRICMDQMIVKVP... | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | Q5HME5 |
B0R2T2 | PSA_HALS3 | Proteasome core protein PsmA | Halobacterium | MQGQNQQQAYDRGITIFSPDGRLYQVEYAREAVKRGTASIGVRTPEGVVLVVDKQTRSPLLEGSSVEKLHKIDDHVGAASAGHVADARQLVDFARQQSQVERVRYDEPIGVRTLTKSVTDHIQQYTQVGGARPFGVALLIAGVEGGEPRLFETDPSGTSNEWKAVAIGSNRGDIQEFLEDEYDAGLSVDDGIDLALRALNEGREDALSGDGVGVGIVDADTGTYRELAADESQSYIDDIEDAADDSDDDDDEE | Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. | B0R2T2 |
A8GG04 | FLIT_SERP5 | Flagellar protein FliT | Serratia | MERQQQLLAAYQQIHSLSSQMIALAQTERWEDLVELELAYVTAVESTAAFTGQAGPSMALQELLRNKLQQILDNETELKRLLQQRMDQLKELIGQSTRQNVVNSTYGQFNDRALLLGEPQIR | Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promo... | A8GG04 |
Q5LLL2 | METK_RUEPO | Methionine adenosyltransferase | Ruegeria | MSRQNYIFTSESVSEGHPDKVCDRISDAVLDAFLTEEPEARVACETFATTNRVVIGGEVGLSDQAKLREYMGRIDQIARDCIKDIGYEQDKFHHETVEITNLLHEQSAHIAQGVNAAEGKDEGAGDQGIMFGYATTETPALMPAPIQYSHAILRRLAEVRKNGTEPALGPDAKSQLSVIYRDGMPVGVSSLVLSTQHLDPDLTSADIRAIVEPYIREVLPEGWLSADTVWHVNPTGKFVIGGPDGDAGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLADKCTIQLSYAIGVSKPLSIYA... | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q5LLL2 |
O27518 | FAEHP_METTH | D-arabino-3-hexulose-6-phosphate formaldehyde lyase | Methanothermobacter | MYRIGEALIGSGNEVAHIDLIIGDKEGNAGAAFANGLTNLSLGHTPLLSVVRPNLMTKPATLIVPKVTVSCLEDADKVFGPAQTAVARAVADSVEEGIIPEEKAEDLVVIVSVFIHPEAEDYRKIYQYNYGATKLALRRAMEGYPSVRKVLSEKDRGSHPIMGFRAVRLWNPPYLQVALDLDSMEEMERIINTLPDRERILLEAGTPLVKKFGVGVVRRIRELRRDAFIIADLKTLDVGRIEVKMAADETADAVAISGLGTVESIEKAIHEAQKQGIYSILDMMNVENFVDKLRGLKYKPDIVLLHRNVDLETLRAERGE... | Catalyzes the reversible formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. | O27518 |
P44123 | QUED_HAEIN | Queuosine biosynthesis protein QueD | Haemophilus | MFKISKEFSFDMAHLLDGHDGKCQNLHGHTYKLQVEISGDLYKSGAKKAMVIDFSDLKSIVKKVILDPMDHAFIYDQTNERESQIATLLQKLNSKTFGVPFRTTAEEIARFIFNRLKHDEQLSISSIRLWETPTSFCEYQE | Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. | P44123 |
Q3APJ7 | RS13_CHLCH | 30S ribosomal protein S13 | Chlorobium | MRLAGVNLPLNKHAVIALTHVYGIGRTSAENILRKAGIAYDKKISELSDEEAHAIREIIAEEYKVEGQARGEQQTAIKRLMDIGCYRGLRHRRSLPVRGQRTRTNARTRKGKRKTVAGKKKAVKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q3APJ7 |
Q2GCU8 | CCME_NEOSM | Heme chaperone CcmE | Neorickettsia | MLLLRWKRFWFLSLGILLFSGVVSLMLFNLSESISFFYLPSDVARVVASNREIKVGGIIKAIKKSKDGVRFLLSDGAAEIEVLYEGILPSLVQDGINVVVVARFEGGLLLAKRVLVKHDERYYPPEDFIKSVRGE | Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. | Q2GCU8 |
A7HHV3 | PIMT2_ANADF | Protein-beta-aspartate methyltransferase 2 | unclassified Anaeromyxobacter | MLARSLLPALALLLAATAGGDACADRGHPSAERSTPETERRRMVEEQLAARGIRDRRVLEAMGKVPRERFVPEQWRSLAYLDEPLPIGRGQTISQPYVVAFMAQALALRGGERVLEVGSGSGYAAAVLAHLAGAVYGIELEPELHARSVETLAELGYGNVHLRRGDGFLGWPERAPFRAIVVSCAMEEIPAPLWEQLVQGGRIVYPKGPEGEVQLLVVVTKTARGPREEHLAPVRFVPMRRGG | Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. | A7HHV3 |
Q59MJ2 | MCH1_CANAL | Probable transporter MCH1 | Candida | MHKHLHHVSHTIKSYLSTLIALENLKVVAFLISLLSCLVAGSILLFTLYTSSFHEVLGLSYLQINMISSLSALGMYFCLPVLGYLADSYGPALLSLFSIWFFCPSYFVNSYLVSTQSGSVIGFCVCFCFIGLATSSLYFSSLITCARICPDHKGLAISLPITCYGLSALLGAQILKLPYFHRHDVLDLEVVFSFFAWLYLVVGIASFVSSSIVIVESELLFGVTPDEETALLELTPTRSLEPPNHRQRFVSFVKDPSAWILLVSLILNIGPMESYQNNLSSILKHTNGADLPNQVSIMAASSTGARLLLGVLSDYSSKYV... | Probable transporter. | Q59MJ2 |
B2A2K6 | RLMN_NATTJ | tRNA m2A37 methyltransferase | Natranaerobius | MINHKQSLKDLTLNELQEYFSRKGWQQFRAKQIFDWMYIQQVDSIEVMSNIPKKLRQELMENCTINDLELDSNNIYTSPTDGTIKFLSVLKDGIGVETTIMKYDYGNTVCISSQAGCNMNCVFCASTTGGKERDLSPGEMIDQVLMANKVLPGSESINNIVVMGSGEPLENYQHLIKFLKIVNDGKGLNIGMRHITVSTCGLVPEIYNLAEEELQLNLAISLHAPNDELRNKLIPLNKIYPIHELLEACQVYFQKTGRRITFEYVLIKDFNDSIDLAKELSETLTALKMPVHVNLIPFNPVEETKFTAPPSSRISDFKNN... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | B2A2K6 |
Q03220 | CTL1_YEAST | mRNA 5'-triphosphatase | Saccharomyces | MSDQPETPSNSRNSHENVGAKKADANVASKFRSLHISETTKPLTSTRALYKTTRNNSRGATEFHKHVCKLAWKYLACIDKSSISHIEIEMKFGVITDKRTHRRMTPHNKPFIVQNRNGRLVSNVPEQMFSSFQELLRSKSENPSKCAPRVVKQVQKYTKDSIYNCNNASKVGKLTSWRCSEDLRNKELKLTYIKKVRVKDFLIRYPQSSLDAKISISLEVPEYETSAAFRNGFILQRTKSRSTYTFNDKMPLHLDLTKVTTTRRNSHQYTSHEVEVEMDPIFKETISANDREKFNEYMCSFLNASDLIRKAAERDNMLTT | Probably involved in an RNA processing event other than mRNA capping. Releases gamma-phosphate from the 5'-end of RNA to produce a diphosphate terminus. | Q03220 |
Q6L1S1 | IDI2_PICTO | Type 2 isopentenyl diphosphate isomerase | Picrophilus | MIENRKEEHIKIAENENVVSEHNFWDDIRIVHRAIPEVDFNDIDTGVKFLGKQFNYPILISSMTGGTETAKIINKNLAMTAEHFKIGMGVGSMRVAVKNKNTADTFSVINDYKIPAKFANIGAPQLVRQDSDSLSDNDIEYIYNLINADFLIVHFNFLQEMVQPEGDRNSKGVIKRLKDIAGSYNVIAKETGSGFSKEDALSLLDAGVKAIDVGGLGGTSFAAIEYYRAQKANDEIKMHTGKAFWNWGIPSPASIKYCSLGEPVIGSGGLRNGLDLAKAIMFGATLGGFARELLKDANTSFDDVKRQMEMIINDLKITMM... | Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | Q6L1S1 |
O00212 | RHOD_HUMAN | Rho-related protein HP1 | Homo | MTAAQAAGEEAPPGVRSVKVVLVGDGGCGKTSLLMVFADGAFPESYTPTVFERYMVNLQVKGKPVHLHIWDTAGQDDYDRLRPLFYPDASVLLLCFDVTSPNSFDNIFNRWYPEVNHFCKKVPIIVVGCKTDLRKDKSLVNKLRRNGLEPVTYHRGQEMARSVGAVAYLECSARLHDNVHAVFQEAAEVALSSRGRNFWRRITQGFCVVT | Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and includes regula... | O00212 |
B7LTZ5 | TATD_ESCF3 | DNase TatD | Escherichia | MFDIGVNLTSSQFAKDRDDIVTRAFAAGVNGLLITGTNLRESQQAQKLARHYPHCWSTAGVHPHDSSQWQAATEEAIIELAAQPEVVAIGECGLDFNRNFSTPEEQERAFVAQLRIAAELNMPVFMHCRDAHERFITLLEPWLEKLPGAVLHCFTGTREEMQACVARGIYIGITGWVCDERRGLELRELLPLIPAEKLLIETDAPYLLPRDLTPKPTSRRNEPAYLPHILQRIAQWRGEDAACLAATTDTNVKTLFGISF | 3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair. | B7LTZ5 |
Q9XZT1 | MED18_DROME | dp28b | Sophophora | MAIVSSARESLSHAMNNRFLPNLEYLLQGSILDSAVEHLMHRLKGLCDNVDTSPEPFHDLEVCMSLRQPNANQPLLLRVRRALGRDAPFQMRYLGNPEVDLRRPTLVRSCMDCACTNGILEFLTEMGFRLEFEYIAKGYMFRKGRMKITVSKLIKIVPGKQQDMANEPISQSYIVELSVVAPTGQENVGEEMRVFAEQLKPLVQLEKIDYKRLGGMP | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters... | Q9XZT1 |
Q68FW4 | STX18_RAT | Syntaxin-18 | Rattus | MAVDITLLFRASVKTVKTRNKALGVAVGGGADGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTMSEYGRMTDTERDQIDQDAQIFMRTCKDAIQQLRTEAHKEIHSQQVKEHRTAVLDFVEDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPHTKRKEPASEKSSHNASQDSEEKPAAEDLPEKPLAESQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLV... | Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. | Q68FW4 |
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