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 |
|---|---|---|---|---|---|---|
C0MDT1 | GLMM_STRS7 | Phosphoglucosamine mutase | Streptococcus | MGKYFGTDGVRGEANVELTPELAFKLGRFGGYVLSQHETERPRVFVARDTRISGEMLEAALIAGLLSVGIEVYKLGVLATPGVSYLVRTEKASAGVMISASHNPALDNGIKFFGSDGFKLADEQELEIEALLDAKKDLLPRPSAEGLGALVDYPEGLRKYERFLVTTGADLDGLKIALDTANGAASVSARNVFLDLNADITVIGENPNGLNINDGIGSTHPEKLQELMTETASDIGLAFDGDSDRLIAVDENGAIVDGDKIMFIIGKYLSEKGLLAKNTIVTTVMSNLGFHKALDSCGIHKKVTAVGDRYVVEEMRQFGYNLGGEQSGHVIIMDYNTTGDGQLTAVQLTKIMKETGKTLSELASEVTIYPQKLVNIRVDNSMKERAMEVPAIAEVIAQMEGEMAGNGRILVRPSGTEPLLRVMAEAPSNEEVDYYVDTIAAVVRAEIGLD | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | C0MDT1 |
B3PC08 | GATA_CELJU | Glutamyl-tRNA(Gln) amidotransferase subunit A | Cellvibrio | MHQFTIAELVKGLRNKDFSSTEITQHYLDRIARLDNTYNSYITVTGDVALQQAAAADKRLAAGNTSALCGVPIAHKDIFCTAGVRTSCASKMLDKFIAPYNATIVENYLKAGVVMLGKTNMDEFAMGSSNETSWYGPVKNPWNTHCVPGGSSGGSAAAVAAHLAPAATASDTGGSIRQPAALCGLTGIKPTYGRVSRWGMIAFASSLDQAGILSRTAEDAALLLNDMASYDPKDSTCIERDVPDYTADLNKPLNGLRIGVPKEYFGEGLNPKTAALVEAAIKVYESLGASIHSVSLPHTHLAVPAYYVIAPAECSANLSRFDGVRYGHRCEDPKDLMDLYMRSRSEGFGAEVKRRILVGTYALSAGYYDAYYSKAQKVRRLIKQDFVDAFHHVDVILGPTSPSPAFEFGSKGKDPVAMYLEDIYTIATNLAGLPGLSIPCGLVDDKPVGLQLIGNFFAEAQLLNAAHQFQQATDFHQQTAPGIE | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | B3PC08 |
Q7KTX7 | PRKN_DROME | E3 ubiquitin-protein ligase parkin | Sophophora | MSFIFKFIATFVRKMLELLQFGGKTLTHTLSIYVKTNTGKTLTVNLEPQWDIKNVKELVAPQLGLQPDDLKIIFAGKELSDATTIEQCDLGQQSVLHAIRLRPPVQRQKIQSATLEEEEPSLSDEASKPLNETLLDLQLESEERLNITDEERVRAKAHFFVHCSQCDKLCNGKLRVRCALCKGGAFTVHRDPECWDDVLKSRRIPGHCESLEVACVDNAAGDPPFAEFFFKCAEHVSGGEKDFAAPLNLIKNNIKNVPCLACTDVSDTVLVFPCASQHVTCIDCFRHYCRSRLGERQFMPHPDFGYTLPCPAGCEHSFIEEIHHFKLLTREEYDRYQRFATEEYVLQAGGVLCPQPGCGMGLLVEPDCRKVTCQNGCGYVFCRNCLQGYHIGECLPEGTGASATNSCEYTVDPNRAAEARWDEASNVTIKVSTKPCPKCRTPTERDGGCMHMVCTRAGCGFEWCWVCQTEWTRDCMGAHWFG | E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Paris, Marf, Opa1, Miro, pnut, Sep1, Tom20 and porin . Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates, depending on the context . Protects against mitochondrial dysfunction during cellular stress, by acting downstream of Pink1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy . Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons . Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires Pink1-mediated phosphorylation of both park and ubiquitin . In depolarized mitochondria, mediates the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of porin/VDAC; polyubiquitination of porin promotes mitophagy, while monoubiquitination of porin decreases mitochondrial calcium influx which ultimately inhibits apoptosis . When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins . Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy . In developing tissues, inhibits JNK-mediated apoptosis by negatively regulating bsk transcription . The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria by mediating the ubiquitination and subsequent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo . This prevents the refusion of unhealthy mitochondria with the healthy mitochondrial network and/or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes . Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma . The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins . Involved in mitochondrial biogenesis via the ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl . Promotes localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs . | Q7KTX7 |
P27182 | ATPL_SYNY3 | Lipid-binding protein | unclassified Synechocystis | MDSTVAAASVIAAALAVGLGAIGPGIGQGNASGQAVSGIARQPEAEGKIRGTLLLTLAFMESLTIYGLVIALVLLFANPFA | 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. | P27182 |
P47632 | CH60_MYCGE | Chaperonin-60 | Mycoplasma | MAKELIFGKDARTRLLQGINKIANAVKVTVGPKGQNVILERKFANPLITNDGVTIAKEIELSDPVENIGAKVISVAAVSTNDIAGDGTTTATILAQEMTNRGIEIINKGANPVNIRRGIEDASLLIIKELEKYSKKINTNEEIEQVAAISSGSKEIGKLIAQAMALVGKNGVITTDDAKTINTTLETTEGIEFKGTYASPYMVSDQEKMEVVLEQPKILVSSLKINTIKEILPLLEGSVENGNPLLIVAPDFAEEVVTTLAVNKLRGTINVVAVKCNEYGERQKAALEDLAISSGTLAYNNEINSGFKDVTVDNLGDARKVQIAKEKTTVIGGKGNKDKIKKHVELLNGRLKQTTDKYDSDLIKERIAYLSQGVAVIRVGGATELAQKELKLRIEDALNSTKAAVEEGIIAGGGVGLLNASCVLTNSKLKERYENETSVENIKEILLGFEIVQKSLEAPARQIIQNSGVDPVKILSELKNEKTGVGFDAETKKKVDMIANGIIDPTKVTKTALEKAASVASSLITTNVAVYDVKERKDNSFSE | 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. | P47632 |
P27439 | MSP1_ASCSU | Alpha-MSP | Ascaris | MAQSVPPGDINTQPSQKIVFNAPYDDKHTYHIKITNAGGRRIGWAIKTTNMRRLSVDPPCGVLDPKEKVLMAVSCDTFNAATEDLNNDRITIEWTNTPDGAAKQFRREWFQGDGMVRRKNLPIEYNL | Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod. | P27439 |
B5Y305 | RL9_KLEP3 | 50S ribosomal protein L9 | Klebsiella | MQVILLDKVANLGSLGDQVNVKAGYARNFLVPQGKAVPATKKNVEFFEARRAELEAKLADVLSAAEARAAQINALESVTIASKAGDEGKLFGSIGTRDIADAVTAAGVKVAKSEVRLPNGVLRNVGEHEVDFQVHSEVFAKVIINVVAE | Binds to the 23S rRNA. | B5Y305 |
Q3A829 | HISZ_SYNC1 | ATP phosphoribosyltransferase regulatory subunit | Syntrophotalea | MNRKITVPEAMLPRGVKDFLPNKAAKLEYLKQSLKDVFHRWAFRPIMPPTLEYLDVLERGLGAGLRDKTFRFDDRQNGKLVAFCPDITPQVARIVATRMKGAPLPQRLCYNGKVLRHTEQQAGKDREIIQSGVELIGLQGPEADAEMIAMAIECLQSLGATEFTVDIGQVEFFHGVMDGLNLPAPQALAVQQAIARKDASGLSELLSELSLDDRKYAEVMALPRLFGGREVLDRAADIVVNDRSRRALENLRQILAVLEAYGVEEHVTFDLGELRGLGYHTGVTFQGFLSGMGTAVCSGGRYDTLTARYGMDAPATGFAFNLLNLLMALDRTLESAAVQPFDVMILQSGPDKRAAQSLARALRDQGYACARDIIERSLQDSLDYGRKMHFRHVMVVADQAGDVRLIRLADGSEQTISLQAVLAGEFRL | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | Q3A829 |
Q9Y6K5 | OAS3_HUMAN | p100 OAS | Homo | MDLYSTPAAALDRFVARRLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKSLNAVYPRAGSKPPSCPAPGPTGAASIVPSVPGMALDLSQIPTKELDRFIQDHLKPSPQFQEQVKKAIDIILRCLHENCVHKASRVSKGGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPRRAEILDEMRAQLESWWQDQVPSLSLQFPEQNVPEALQFQLVSTALKSWTDVSLLPAFDAVGQLSSGTKPNPQVYSRLLTSGCQEGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGKGPAPASLPPAYALELLTIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHGSWELLAQEAAALGMQACFLSRDGTSVQPWDVMPALLYQTPAGDLDKFISEFLQPNRQFLAQVNKAVDTICSFLKENCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGNKRAEIISEIRAQLEACQQERQFEVKFEVSKWENPRVLSFSLTSQTMLDQSVDFDVLPAFDALGQLVSGSRPSSQVYVDLIHSYSNAGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKISKGRGSLPPQHGLELLTVYAWEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNARWDLLAKEAAACTSALCCMGRNGIPIQPWPVKAAV | Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV). | Q9Y6K5 |
P56377 | AP1S2_HUMAN | Sigma1B-adaptin | Homo | MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEAETPRSVLEEIGLT | Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. | P56377 |
Q6G2X2 | RL16_BARHE | 50S ribosomal protein L16 | Bartonella | MLQPKRTRFRKQFKGRIHGVSKGGTDLNFGAYGLKAVEPERITARQIEAARRAITRYMKRSGRVWIRIFPDLPVTSKPTEVRMGKGKGSVDYWAARVAPGRIMFELDGIPEDVAREALRLGAAKLPIKTRFIQRIAE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q6G2X2 |
O33570 | CCMA_CERS4 | Heme exporter protein A | Cereibacter | MDLTVTNLACARGGVTVLERVSFRLSRGAALILRGPNGIGKTTLLRTVAGLQPAVAGEISMPPEAVAYAAHADGLKATLTVAENLAFWAAIYGTDRAARAIERMNLAALADRQAQNLSAGQKRRLGLARLLVTGRPLWVLDEPTVSLDAASVALFGDVVRTHLAEGGAALMATHIDLGLAEAEVLDLAPYRAETPAGTEPADDPFAGVTA | Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. | O33570 |
P64688 | AC100_MYCBO | Acyl carrier protein BQ2027_MB0103 | Mycobacterium tuberculosis complex | MRDRILAAVCDVLYIDEADLIDGDETDLRDLGLDSVRFVLLMKQLGVNRQSELPSRLAANPSIAGWLRELEAVCTEFG | Acyl carrier protein that accepts acyl-adenylates (acyl-AMP) from FadD10. | P64688 |
Q9RRB6 | SLPA_DEIRA | S-layer protein SlpA | Deinococcus | MKKSLIALTTALSFGLAAAQTAAPVSAPQVPALTDVPAGHWAKDAIDRLVSRGVILGYPDGTFRGTQNLTRYEAAIIIARLLDQMRDGETPAGMTAEDMTALQNAIQELAADLAALGVRVSDLEANAVSKDDFARLEARIEEVAAAGGEQGATEALQGQIDDLTARVDEYDALRADVDDNASSIAALNDLTVLLNQDILDLQDRVSAVEAAQADFVQRSDFDALGGRVTTVETRVETVNNSLTGRIAALERNAFSVKPSLTIGYSVSRTSRNFDVDRLFPLNADGTVANNAFTSGGIDTDTGAQRRDFGDFGNASDPVVAGAAGLYGFADGVSYTVYFTDGSTATFDGLNPADYKVPTGKVIDTTKGRNGFGFNNLARYKEGSTDIGISLGFDTSGQFSQVTSGTGGSLFSTAGRLQVNQIDLNFGLVTGLPSDAYVDTNGNGKKDDGEATGRGTYLGSGGTAAILRDPAGNVYRPVFFRFKNATTQFSVGNNPVIVTLGQQQKFYFSDYVFDNNYDGRGDGFTVTVDGSNVPVIGAWKPQIKGVYGSRSGLDGTAEAGYGVYYRGVRAQITPVGTLTAGIHYAQEGRDMFGAAQNTTSTPSDVTTYGADLHGKAFGVELHSEYATSRVRPNTANAAVQTSNAFYARVATRKDNLAFDLNTPAAKFGNDTFGVSLYDLNYRKIDAGYNNVAGISEYGYGSYSRTSAQNIAYNPDTGVTAPFANLDRQAYTDANNDGTSDRNADGTVVATNTKIGQMGFGVKAAANLGPVAIGGYYDTSTGANGDNANRMTEAGGSAKVAYSIFSLRGTYNTLDSNRPQIYRDAAGTQIIGDAKVRRYAVQADVTPGLGLFVGAYYRDVNVNGVRSTTDRGLLGRGYLASSFEPGVGNNAYRTGLRCADNNFGTGTRDIDGVGGVLNPAVNLDQSRTATCFTSYGVEAGHAGDNANALVKDLFFRVGYSRVYVPTTATATTGDFSGSVTYGDARYDRKVGVANVRLAGSFSTTNTQLDSRPAGTRGAVGLIVRTDPLENVPFRPQFNGQVGYYTADNRVAAGNYNANATKYGAGVVLNDFLLPQTKIGVRYDGYMAQNRQYTPFDGDGTQGYFSDANNNRRTNLNGVYVEGAYQDLIFSYGTYTLSQKDLNGVEYGSGINNGQPARGQTFKISYKVNF | Major constituent of the S-layer. Plays an important role in the structural organization and integrity of the S-layer . Binds the carotenoid deinoxanthin, a strong protective antioxidant specific of this bacterium, and could be part of the first lane of defense against UV radiation, especially under desiccation . | Q9RRB6 |
Q1INZ5 | GVPA_KORVE | Gas vesicle structural protein | Candidatus Koribacter | MAVERVSGGSSLIDVLDRVLDKGIVIDAWVRISLVGIDLITVEARVVVASIDTYLKYADAVGLTGLVSRPQLTEVVEEPVVVEAPATRRTARPSRRRI | Gas vesicles are small, hollow, gas filled protein structures that are found in several microbial planktonic microorganisms. They allow the positioning of the organism at the favorable depth for growth. GvpA type proteins form the essential core of the structure. | Q1INZ5 |
Q8CE23 | OX26_MOUSE | Pyroglutamylated arginine-phenylalanine-amide peptide | Mus | MRGFRPLLSLLLPLSACFPLLDRRGPTDIGDIGARMNWAQLAEGHPPNSVQNPQPQALLVVAREQQASHREHTGFRLGRQDGSSEAAGFLPADSEKASGPLGTLAEELSSYSRRKGGFSFRFGR | Stimulates feeding and grooming behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland. | Q8CE23 |
A5FY70 | QUEF_ACICJ | PreQ(0) reductase | Acidiphilium | MTDTRYDALQQLGRESRMPDSPEAAVLERVAAPSRGKNYVVRFTCPEFTSLCPITGQPDFAHVVIDYIPDSWIVESKSLKLYLGSFRNHGAFHEACTLMIAERLVDLLAPRWLRIGAYWYPRGGIPIDVFWQTGAPPEGAYLPDQGVPPYRGRG | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | A5FY70 |
Q66EM6 | SGRR_YERPS | HTH-type transcriptional regulator SgrR | Yersinia | MSTSRLQQQFIRLWQRYNGQSTETTLQALAEVLNCSRRHVRSLLGKMQHAGWLDWQAEAGRGKRSQLIFLRSGLALQQQRAEELLEQDHIDQLVQLVGDKKAVRQMLLSQLGRSFRQGKHILRVLYYRPLENLLPGTALRRSETHMVRQIFNGLTRINEENGELEPDLSHHWQAITPLHWRFYLRPAIHFHHGRELEMSDVISSLTRLIPQPLFSHIAEVRSPTPYVIDVYLHSPDHWLPWLLGSVHAMILPQEWETQPDFHRQPIGTGPYSVIRNHHSQLKIQAFDNYFGFRALIDEVNIWVLPELSEELVYSGVQLQADDTGKNELESRLEEGCYFLLFDQRSPQACTPEIRRWLCELITPIALLSHADPFYQRYWSPAYGMLPRWHHNRLTTQEPKPEGLNELTLTFYSEHSEFDAISQTLTQLLAAQGVTLKIQVLDYTRWYQGDAQSDIWLGSANFYLPLEFSLFATLYEMPLLQHCLSEELHQDIESWRNNTLLMADWSQRLVSQHQFHPLFHHWLELYGQHSMRGVRMNTLGWFDFKSAWFTPPEA | Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute-binding domain. | Q66EM6 |
Q8YCY1 | OCD_BRUME | Ornithine cyclodeaminase | Brucella | MMTQPNLNIVPFVSVDHMMKLVLRVGVETFLKELAGYVEEDFRRWQNFDKTPRVASHSKEGVIELMPTSDGTLYGFKYVNGHPKNTRDGLQTVTAFGVLADVGSGYPMLLTEMTILTALRTAATSAVAAKHLAPKNARTMAIIGNSAQSEFQALAFKAILGVDKLRLYDLDPQATAKCIRNLQGAGFNIVACKSVEEAVEGADIITTVTADKANATILTDNMVGAGVHINAVGGDCPGKTELHGDILRRSDIFVEYPPQTRIEGEIQQLPEDYPVNELWEVITGRIAGRKDARQITLFDSVGFATEDFSALRYVRDKLKDTGLYEQLDLLADPDEPRDLYGMLLRHEKLLQSESTKPAA | Catalyzes the conversion of L-ornithine into L-proline with release of ammonia. | Q8YCY1 |
Q5P1F7 | GLMM_AROAE | Phosphoglucosamine mutase | Aromatoleum | MGRKYFGTDGVRGRVGDSTITPEFVMRLGYAAGVTLVGREQLPPGERPAILIGKDTRISGYMLEAALEAGFAAAGVDVMLAGPVPTPAVAYLTRALRLQAGVVISASHNPYDDNGIKFFSANGTKLPDALEEEIEFRVDQPMVCAEASRLGKARRIVDAAGRYVEFCKSAFPNEFDLRGYRIVLDCAHGAAYHIGPSVFHELGAEVIPLGVEPNGLNINDQVGATHPQTLRSAVLANKADFGIALDGDGDRVVMVDGDGELYDGDKLLYVIAASRQAEGRLEGVVGTLMSNLGLERAIGRLGLAFARAKVGDRYVLETMHERGWRLGGENSGHIICLDRHTTGDGIVSALQVIAALIKGQCTLATACADLVFYPQKLINVPLAAGFDWRSDERIDQARSDAELELGEQGRVLLRPSGTEPLLRVMVEGKDGSQVERLARHIADCVRHASV | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q5P1F7 |
Q6NRB9 | EMC1_XENLA | ER membrane protein complex subunit 1 | Xenopus | MAADLCWLSLLLASLALSGAVYEDQVGKFDWRQEYVGRIKFASLESGLGAKKLIAVTDKNIIAALNSRTGDLLWRHVDKDTSEGTVDALMMIGQDAITVSGGRLLRSWETNIGALNWEAALEPGSFQAVSFAGSQDTARYVAVLKNSALSLYFLSNGHLKWSESLPESDTVQYQLLYSPYKGSVHVVGLVPHSHLTILTFSLEDGSISHQVRVLTPWLRTLHGTCGVIGEGVLVCGDVPMASVHIVSLLSGEETTRYSVQSLDIELAEDPTQLDVITAPQNGIGGSLSQFFLQIAPRRFLLMHYHDGVLTPLRDFSQVSLVNFATTGEKTVVAVMQCKTEGNPKSGAESEYLTGQNCAQEPWYCPGHTYSINLYMADSGRRLLETTMSFTLDQICVRPDSFYLQTFLRKDDSVGYRALVQTEDNQLLFLQQPGKLIWLREESLADVVTMETVDLPLTGAQAELEGEFGKKADGLIGMVLKRLSSQLILLQSWSAHLWKMFCDARKPRSQIRNEINVDTLARDDFNLQKMMVMVTASGKLFGIESSSGSILWKFYLHGVHPGSSFKLLVQRTTAHFPHPPQCTLLVKDKVTEKSAMYVFNPIFGKLSQLAPPPLQRPILQSLLLPIMDNDYAKVLLLLDDQHKVIAFPATKYVLQQLQELHSTIFFYLVDVEKGKLSGLRLNKDLSTEEIWEVLLPADQQRITVVKGKRSNEHVHSQGRVMGDRSVLYKYLNPNLLVLVTESTDTHPERCFIGIYLIDGVTGRIIHSSVQRRARGPVQIIHSENWVVYQYWNSKARRNELTVLELYEGTEQYNSTNFSSLDRPLLPHVLQQSYIFPSAIRAMQATITERGITSRHILIGLPSGAILSLPKALLDPRRPEIPNEYTREENLIPYTPDIQIHAERFINYNQTISRMRGIYTAPSGLESTCLVVAYGLDLYQTRVYPSKQFDVLKDDYDYILISSVLIGLVFATMITKRLAQVKLLNRAWR | Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. | Q6NRB9 |
O60683 | PEX10_HUMAN | RING finger protein 69 | Homo | MAPAAASPPEVIRAAQKDEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVTLHAVLPYLLDKALLPLEQELQADPDSGRPLQGSLGPGGRGCSGARRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRLHVAWFYIHGVFYHLAKRLTGITYLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLYGFRQRQRARKEWRLHRGLSHRRASLEERAVSRNPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKLIYLRHYR | Somewhat implicated in the biogenesis of peroxisomes. | O60683 |
Q88NI1 | MCPU_PSEPK | Methyl-accepting chemotaxis protein McpU | Pseudomonas | MPLRRLSIQWKITLLAGLCLLAIVALLVATSLTQAHRSAALVNQANTAMLEDSARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLKDRGGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQDSHYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETMLGDTSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQVLMTSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLFDGQGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRVAHPFTPIPDTAPWQVVLELPESVLQAPAVALNQRLDAHNQNANLTSLLIGLGTAIAGLLLVWLTARGVTRPILAVAARLEDIASGEGDLTRRLDYAHQDELGQLTGWFNRFLDKLQPVIAQVKGSLQEARNTADQSAAIASQTSDGMQQQHREIEQVATAANEMSATALDVAHNASQAAQAARAADQASQEGLQLVDSTRQGIDRLAAGMNTAMDEARALEDRSGQIGSVLEVIRTIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRGLAQRTQVSVEEIRQVIEGLQQGTQDVVGAMHAGQRQAQDSAARMEQALPALQRIGEAVAVISDMNLQIASAAEEQSAVAEEVNRNVAGIRDVTESLAGQADESARISQALNRLANQQQALMEQFRV | Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpU is a chemoreceptor that binds and mediates chemotaxis to polyamines such as putrescine, spermidine, cadaverine and agmatine . Also binds histamine and ethylenediamine with much lower affinities . | Q88NI1 |
Q71G51 | TBA_NEOCA | Alpha-tubulin | Neospora | MREVISIHVGQAGIQIGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVVDEVRTGTYRHLFHPEQLISGKEDAANNFARGHYTIGKEIVDLSLDRIRKLADNCTGLQGFLMFNAVGGGTGSGLGCLLLERLSVDYGKKSKLNFCSWPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRMDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGYGDEY | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Q71G51 |
Q9PHW9 | HEM3_CAMJE | Pre-uroporphyrinogen synthase | Campylobacter | MKLIIATRKSQLALWQSEHVAQILKNTHQIEVLLEGFKTKGDVLLDSPLAKIGGKGLFTKELEESMLRKEAHLAVHSLKDVPSFFPQGLVLAAVSKREQSNDAMLSQNYKDFLSLPKGAKIGTTSLRRKMQLLLLRPDLEIISLRGNVNSRIEKLKNNDFDAIILAMAGIKRLNLDKQVNFVYEFSKDELIPAASQGALGIESINDEKILELLKCLNDENALIETSIEREFIATLEGGCQVPIGINAELLGDEICVRAVLGLPDGSEILKDKRMIKKNDFKGFGESLAKEFIAKGAKELLKKAESMI | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | Q9PHW9 |
A5EYG3 | DNAK_DICNV | Heat shock protein 70 | Dichelobacter | MGKIIGIDLGTTNSCVAVMDGDSAKVIENSEGTRTTPSIIAFSDGEVLVGQPAKRQAVTNPKNTLYAIKRLIGRRFDEKEVQKDINLVPYNIVKSDNGDAWVEIDGKKMAPPEISARILQKMKKTVEDYLGETITEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAYGIDRGAKDAKIAVYDLGGGTFDISIIETIDLDEEGQQFEVLATNGDTFLGGEDFDRRIIDYLVNEFKKEQGIDLTSDSLALQRLKEAAEKAKIELSSSQQTDINLPYITADASGPKHMNLKLTRAKLESLVADLIERSLEPCRIAMKDAGLSNSDITDVILVGGQTRMPKVQEAVKNFFGKEPRKDVNPDEAVAMGAAIQGGVLGGQVKDVLLLDVTPLSLGIETLGGVMTKLIEKNTTIPTKASQIFSTAEDNQSAVTIHILQGERQQASANKSLGRFDLSDIPPAPRGMPQIEVSFDIDANGILNVSAKDKQTGKEQSIIIKASSGLSDEEVARMVKDAEAHAEEDRKFQERIETKNSAESMINGVEKAISELGDEVTSDEKEKTEAAIKALREVMKGEDSDAIKEKTNALMEAASSIMQKAYAKMTEKQQSDDGAGTQNADHKEDDVVDADFEEVKSDKKD | Acts as a chaperone. | A5EYG3 |
A7M9A9 | CCSA_CUSRE | Cytochrome c biogenesis protein CcsA | Cuscuta subgen. Monogynella | MIVSTLEHILTHISLSIVSILITIELRIFLDDEIKKLYDSSERGMLITFLCITGLLANNWIYLGHFPLSDLSESLIFLSWSFALIHSIGYFTKNLKFLSTITSQSTLFTQGFATSGILTKIQKSSILIPALKSEWLIMHVSLMILGYAALLCGSLLSVALMVITVRNDGKFFFKSNNFLFREISYQNKNFFYAINYYKTQLIKELDFWSYQVISLGFIFLTIGILSGAVWANEAWGSYWSWDPKETWAFITWIVFAIYLHTRININLQSTNSAIVASLGFIIIWICYFGVNLVGLGLHSYGSFPSTSN | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | A7M9A9 |
Q1GJX2 | YIDD_RUEST | Putative membrane protein insertion efficiency factor | unclassified Ruegeria | MRLLARLIALPVRGYRLLFSPWVGFNCRYQPTCSAYALDALERHGPFKGTYLMLRRIGRCHPFGGSGYDPVPGADPKHDRCCGRTP | Could be involved in insertion of integral membrane proteins into the membrane. | Q1GJX2 |
B4K8J8 | SPC25_DROMO | Kinetochore protein Spc25 | Drosophila | MRKRLMAMLQNDISLQQQENALAKQSAKFHSKIAAKHQLIKRQQRKLEKLNQVANERKEDQENRSAFEQSMRDKLLREQQNLSEMQTELATKKQRRDELMGFVRTMSEATNTYINLKALPARVKGVALRPEQGEWIPFNCDAYDLKGLNALWSRLNEPSASTDKWQQLFSAEPTAKEKENANASLSSIIEIDLTSPTAHRSLAKMLEK | Acts as a component of the essential kinetochore-associated Ndc80 complex, which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. | B4K8J8 |
Q1JHB7 | DEOB_STRPD | Phosphodeoxyribomutase | Streptococcus | MSKFNRIHLVVLDSVGIGAAPDADKFFNAGVADTDSDTLGHISETAGLSVPNMAKIGLGNISRPIPLKTVPTEDNPTGYVTKLEEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEEILTKIEEFSGRKIIREANKPYSGTAVIDDFGPRQMETGELIVYTSADPVLQIAAHEDIIPVEELYKICEYARSITLERPALLGRIIARPYVGEPGNFTRTANRHDYAVSPFQDTVLNKLADAGVPTYAVGKINDIFNGSGITNDMGHNKSNSHGIDTLIKTLQLPEFTKGFSFTNLVDFDANFGHRRDPEGYRDCLHEFDNRLPEIIANMKEDDLLLITADHGNDPTYAGTDHTREYIPLLAYSASFTGNGLIPQGHFADISATVAENFGVDTAMIGESFLGHLK | Phosphotransfer between the C1 and C5 carbon atoms of pentose. | Q1JHB7 |
Q9SLF7 | RLA22_ARATH | 60S acidic ribosomal protein P2-2 | Arabidopsis | MKVVAAYLLAVLSGKASPTSADIKTILGSVGAETEDSQIELLLKEVKGKDLAELIAAGREKLASVPSGGGGGVAVASATSGGGGGGGASAAESKKEEKKEEKEESDDDMGFSLFE | Plays an important role in the elongation step of protein synthesis. | Q9SLF7 |
Q9UU89 | ITPA_SCHPO | Nucleoside-triphosphate pyrophosphatase | Schizosaccharomyces | MTILQSILFVTGNKHKLADVKNILGDRFEIKNHDYDLPEIQGSVKEVVLEKCKAAAEIVKGPVLVEDTWLGYKAMNGLPGPYVKWFLNSVGPDGLYRMVSAFDTKEAQAGCTFGYTKGPGKPIHLFEGILDGQVVPPRGSNGFGWNSIFQPNGHKHTYAEMTDEERNSCSHRYLAAMKLRDFLESEKN | Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. | Q9UU89 |
Q6FCR9 | ILVD1_ACIAD | Dihydroxy-acid dehydratase 1 | Acinetobacter | MPDYRSKTSTHGRNMAGARGLWRATGMKDEDFGKPIIAVVNSFTQFVPGHVHLKDLGQMVAEQIQAAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSRDLIADSVEYMVNAHCADAMVCISNCDKITPGMLMAAMRLNIPVVFVSGGPMEAGKVKFRGNEKAIDLVDAMVVAADDSYTDEEVQAFERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSIVATHANRKKLFLKAGELIVSLAKRYYEQDDSSILPRSIATKAAYENAMTLDIAMGGSTNTVLHLLAAASEAEVDFTMDDIDRLSRNVPVLCKVAPAKQDVHMEDVHRAGGIMSILGELDRAKLLNTTVSTVHEKTLQDALNKWDIIRTEDADVYEFFRSSPGGVPTQVAFSQNRYYSTLDGDRENGVIRNAEHAFSKDGGLAVLYGNIALEGCIVKTAGVDESILKFNGTARVFESQDAAVEAILGNEIKAGDVVVIRYEGPRGGPGMQEMLYPTSYLKSKGLGKDCALITDGRFSGGSSGLSIGHISPEAAEGGAIGLVEDGDLIEIDIPNRSMNLKVDDETLAARRKAQDEKGWKPVEERKRKVSKALKVYAMHTTSAAKGAVRIL | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. | Q6FCR9 |
Q8PJZ7 | EFP_XANAC | Elongation factor P | Xanthomonas | MATVGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYWHFMDPDTFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEIIKVDTRSGEYSARVK | Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. | Q8PJZ7 |
Q8KEX2 | NADE_CHLTE | NH(3)-dependent NAD(+) synthetase | Chlorobaculum | MKPQNLHFDYGLVEAILVPFIRNEIRKFGFGSVVLGLSGGIDSAVVCELAVRALGVENVLALMMPYKTSSQESLDHAELMVDRLGIRYEIMPVTEVVDAFFATRPDASRLRRGNVMARSRMLCLYDVSARDGCLVLGTSNKTELMLGYGTMFGDMASAVNPIGDLYKTQIFGLARHLGIPAPLIDKPPSADLWEGQSDEADLGFSYEEVDQLLYMMLEERMDRDAILAEGIDSAFYQRVRSMVVRNQYKRMMPVIAKLSSRTPGIDFRYARDWQEVR | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Q8KEX2 |
A8A5F1 | TUSC_ECOHS | tRNA 2-thiouridine synthesizing protein C | Escherichia | MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLSGQKPDAVLARDYIATFKLLGLYDIEQCWVCAASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | A8A5F1 |
A2BTX3 | EFP_PROM5 | Elongation factor P | Prochlorococcus | MISSNDFRTGTTIEIDGQVWRVVEFLHVKPGKGSAFVRTKLKSVRNGNVVEKTFRAGESVQQAVLEKSNLQHTYVESGDYVFMDMTSFEETRLSSDQIGRGSKYLKEGMEVNVIFYKDKVLEVELPISITLKVTETDPGVKGDTASGGTKPAILETGAQVMVPLFISVGEMIKVDTRNDSYLGREN | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | A2BTX3 |
Q4A734 | TSAD_MYCS5 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Mycoplasmopsis | MIILGIETSHDDSSIAILEDGKVLNMWSISQIDIFKKYGGTIPEIASREHVKNIAILQNFLQEFIDLNKIDHIAYTSEPGLIGCLQVGFLFASALSIALNKPLIKINHLDGHFFSGAIDNKEIKYPALGLIVSGGHSQIIYAKNKFDFQIVGETLDDAIGECYDKVSSRLNLGFPGGPIIDKIHASYKGKYLKLTKPKTSGEFDFSFSGIKTQVLNAFNNKKYESIEQIAASFQEVAINYLIEKFKLAIDKFKPESILLGGGVSANKYLREKFKDLHKNTIFPEIKYATDNGAMIAMCAYLRMKKNS | 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 catalytic role in this reaction. | Q4A734 |
A0A0B4J245 | TVAL1_HUMAN | T cell receptor alpha variable 12-1 | Homo | MISLRVLLVILWLQLSWVWSQRKEVEQDPGPFNVPEGATVAFNCTYSNSASQSFFWYRQDCRKEPKLLMSVYSSGNEDGRFTAQLNRASQYISLLIRDSKLSDSATYLCVVN | V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition . Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens . Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation . The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity . | A0A0B4J245 |
O15998 | ACTM_CIOSA | Actin, muscle | Ciona | MSDSEEDQTALVCDNGSGLVKSGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVMDAGDGVSHNVPIYEGYALPHAIARLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | O15998 |
Q22058 | HRDE2_CAEEL | Heritable RNAi deficient protein 2 | Caenorhabditis | MSQNSDTFDSGLQMEVHKMAEADNSSVQQKFDAIRDYIGRKETTIILCEHDDSRKIKLTLNKQRMESSMFLTEMPDGGIQEKTKFHRNGLAVCSYNAFDEVDLPLADSYIFYGLPSNVEAFPRMLHGIEKSAHKENKIVFIDIVVSILEKIQIKVVSFELYNRKCTVPTWVAELVITYCAPIEEQQQRIEEIRRTRASVPVAISDAANGSAEMVPSNTTGSSGSPMSTAPVPAAKKEKVQYESIRQIRPNAQGRYFVPARMINMDIEMSNDEYSPDESENDENEYDYENAARYDDGYDEGHEYCQ | Plays a role in germline RNA interference (RNAi), and in particular is required for piwi-interacting RNA (piRNA) gene silencing. Facilitates the binding of the argonaut protein hrde-1 to small interfering RNAs (siRNAs) targets that are required for transgenerational epigenetic inheritance and germline immortality. | Q22058 |
Q65Q31 | RHAS_MANSM | L-rhamnose operon regulatory protein RhaS | Basfia | MIQKLLARDFFNNKEQPIILEPRAPQEIFPEHTHDFDELVIVKHGSGRHILNGYPHDLYPGVVLYIQAQDHHSYENLQDLCLTNILIQSNNNFKYLNNIDILLNGLKPENSSYQLINKKTAEYIDSLLEKINAIDESYNLQNECLFFQVLSSIQAHQFNDSGYGNTEEKGRQMIRWLENNFEKEIDWEELAEKFALPIRTLHRYIKSQTGHTPQNYVTKLRLAQAYYQLKYTEKNIINIAYDCGFNDSSYFSTCFKNEYSIAPRELRI | Activates expression of the rhaBAD and rhaT operons. | Q65Q31 |
B8IEX6 | MIAA_METNO | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Methylobacterium | MAGRAILIAGPTASGKSALALGLAQARGGVVINADSMQVYGDLRVLTARPSPEEEEAAPHRLYGHVDGAVNYSVGHYLADAGRVLRDAWAAERLPIVVGGTGLYFKALLEGLSAIPPVPEAVRAAVRAQAEGRETASLHADLARLDPEGAARIAPGDRLRVLRALEIRAATGRPLSAFQGSRQPGPLAGVACEKLFLAPDRAGLRARIDARFLSMMEAGALDEVRRLRARHLDPMLPVMRAHGVPGLIAHLNGALTREEAVARGQADTRRYAKRQVTWFRHQVGEDWRWLTPEEAAREFLPGH | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | B8IEX6 |
A5F649 | SYE_VIBC3 | Glutamyl-tRNA synthetase | Vibrio | MTVKTRFAPSPTGYLHVGGARTALYSWLYAKSQGGEFVLRIEDTDLERSTQAAVDAIIEGMTWLGLEWDEGPYYQTKRFDRYNQVIDQLLAEGKAYKCYAPKELLDEIRAEQEANKEMPRYDANHPKIKAVNDAAKEGEPCCIRFRNPKEGSVVFDDQIRGRIEIRNDQLDDLIIRRTDGTPTYNFCVVVDDVDMGISHVIRGEDHINNTPRQINIYKAMGATIPTFAHCAMILGDDGAKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWGHGDQEIFSRDEMINLFSLNAISKSASAFNTDKLLWLNNHYIKTSEPEYVAKHLEWHFENQGINKATGPALAEVVKLVGERCNTLVELAQQSRYFYEDFAEFDADAAKKHLRGVAKEPLMLALSKIEALTEWNTEALHHVIAQVCEELEIGMGKIGMPLRVAVTGGGQSPSVDAVMNLIGQERVIARIKMALEYIETREANA | 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). | A5F649 |
W4VRU5 | ICK36_TRILK | Toxin ICK-36 | Trittame | MKTIIVFLSLLVLATKFGDAKEGVNQKQKKEVTQNEFREEYLNEMAAMSLVQQLEAIERALFENEAGRNSRQKRCLGENVPCGDNIPCCGKLACEKTAGYGWWYKSPYCVKPTSG | Ion channel inhibitor. | W4VRU5 |
B7VI66 | RS18_VIBA3 | 30S ribosomal protein S18 | Vibrio | MARFFRRRKFCRFTAEGVQEIDYKDVATLKNYITEAGKIVPSRITGTSAKYQRQLARAIKRSRYLALLPYTDKHQ | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | B7VI66 |
Q0AJA9 | ATPE_NITEC | F-ATPase epsilon subunit | Nitrosomonas | MGTIFHLDIVSAEESIYSGPAEFIVAPAVMGEVGIYPQHTPMLTRIKSGVVRVKAPLQDDEEIYVSGGMLEVQPDVVTILADTAVRGQDLDEAKALEAKRKAEEIMKNKTSDIEYARAQAELIEATAQLAAIRKLRKRRH | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q0AJA9 |
Q45251 | HUPD_BRADU | Hydrogenase expression/formation protein HupD | Bradyrhizobium | MPTSSQDNRILVLGIGNILWADEGFGVRAVEEFHRRYAVPDNVTILDGGTQGLYLVNYLEEADRLIVFDAIDYGLEPGRLKLVRDDEVPRFTGAKKMSLHQTGFQEVISAADLLGRCPKHLVLIGCQPLDLEDWGGPLTPPVRDQIAPSIDLACQVLAEWGVTVSRRSAPLAESERLLANDIDHANYEMRPA | Not known. Could be involved in the processing of hydrogenase. | Q45251 |
A3PBV7 | DCUP_PROM0 | Uroporphyrinogen decarboxylase | Prochlorococcus | MGENLPLLLSAALGKKVNRPPVWMMRQAGRYMKIYRDLRERYPSFRERSENPELSYEISMQPFHAFKPDGVILFSDILTPLPGMGINFEIIESKGPIIEDPIRTLNQVENLKELSPSESLSFVGEVLTSLKKDVNNEATVLGFVGAPWTLAAYVVEGKSSKNYSLIKSMAFNKPDLLHKLLDHFAKSIGEYLKYQIKSGAQVVQIFDSWAGQLSPQDYDIFAGPYQKKVVEIVKAEYPETPIILYISGSAGVLERMAKTGVDIISLDWTVDIEEACKRIPRGIGIQGNVDPGILFGNKESIKERIDNTFNKIKDRKYILNLGHGILPGTPEENAQTFFEHGKKLTY | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | A3PBV7 |
A8MG73 | SYG_ALKOO | Glycyl-tRNA synthetase | Alkaliphilus | MATEKTMEKIVSLAKSRGFIFPGSEIYGGLANTWDYGPLGVELKNNVKKAWWKKFIQQSPYNVGLDAAILMNPKTWEASGHIGGFSDPLMDCKKCRSRFRADKLIEDYMHSQNEETVVDGWSNQQMKTYIEEKEIVCPECGAKDFTDIRQFNLMFKTFQGVTEDSSTEIFLRPETAQGIFVNFKNVLRTSRKKVPFGIGQIGKSFRNEITPGNFTFRTREFEQMELEFFCKPGEDLEWFNYWKEFCKNWLLNLNLTEENLRIRDHAEEELSHYSKATTDFEYRFPFGWGELWGVADRTDFDLKQHSEHSGEDFTYQDPITNEKYVPYCIEPSVGVDRVALAFLVDAYDEEVIDEKDTRVVLRLHPALAPFKAAVLPLTKKLKDQALELYETLSENYMVDYDEAGSIGKRYRRHDEIGTPFCITFDYDSLEDQCVTIRHRDSMEQERIQISELTTYLNEKLKF | Catalyzes the attachment of glycine to tRNA(Gly). | A8MG73 |
B2S9M3 | DER_BRUA1 | GTP-binding protein EngA | Brucella | MGFTLAIVGRPNVGKSTLFNRLVGRKLALVDDLPGVTRDRRIHDAKLYDLKFQVIDTAGLEEAANDSLEARMRAQTEAAISEADAVLFVIDAKAGITPADSTFAEAVRRSGKPVVLVANKAEARGSEAGMYDAFQLGLGEPCPISAEHGQGMPDLRDAIVELLGEERVFAEERQEEAADEVFTPAAVGALVGDDIEDPDAEEIPAYDATKPLRIAIVGRPNAGKSTLINTMLGEDRLLTGPEAGITRDSISADWEWHGRKINLFDTAGMRRKARVQEKLEKLSVADSLRAIRFAEVVIIVLDATIPFEKQDLQIADLIIREGRAPVIAFNKWDLIEDRQMVLADLYEKTARLLPQVRGLRAVPISGERGQGIDKLMENVVKTHEIWNRRISTGRLNRWLEGVIAHQPPPAVSGRRLKVKYMTQVKTRPPGFVVSCSRPDAMPQSYVRYLINGLRETFDMPGVPIRLSLRTSDNPFAGRAKKKK | GTPase that plays an essential role in the late steps of ribosome biogenesis. | B2S9M3 |
Q8E3J2 | RNH3_STRA3 | Ribonuclease HIII | Streptococcus | MNTIVMQADKKLQEKIRTDLAQHHISNNNPYVVFSAKISGTTVLLYTSGKLVFQGSNASHIAQKYGYIEQKESCSSETQDIPIIGTDEVGNGSYFGGLAVVASFVTPKDHAYLKKLGVGDSKTLTDQKIKQIAPLLEKAIPHKALLLSPQKYNQVVGPNNKHNAVSVKVALHNQAIFLLLQDGFEPEKIVIDAFTSSKNYQNYLKNEKNQFKQTITLEEKAENKYLAVAVSSIIARNLFLENLNKLSDDVGYKLPSGAGHQSDKVASQLLKAYGISSLEHCAKLHFANTKKAQALLK | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q8E3J2 |
B3DTU8 | NUCS_BIFLD | Endonuclease NucS | Bifidobacterium | MRVIVADCSAEYSGRLNASLPLAKRVLLIKADSSLLIFSELGSYKPLNWMTAPCTIREIDPAAKSAQHSRESVAGGAVDGDSATHSPESVAAGEPEKVLRVSADKGSDILEVTLQHIYSDQTYDLGEDPGLIKDGVEDHLQRYLAEQIERIGKGAKLVRREYPTAIGPVDIMAVNAEGEHVAVEIKRHGGIDGVEQLTRYCELLNRDPLLAPVHGIFAAQTITPQAQVLAKDRGFTCLILDYDDMKGTEDDSLRLF | Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. | B3DTU8 |
Q38S26 | COX2_ARVSO | Cytochrome c oxidase polypeptide II | Arvicanthis | MAYPFQLGLQDATSPIMEELTNFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAAILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLCFDSYMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWTVPSLGLKTDAIPGRLNQATLSSNRPGLYYGQCSEICGSNHSFMPIVLEMVPLKYFENWSTSMI | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | Q38S26 |
Q8R070 | G6PT2_MOUSE | Solute carrier family 37 member 1 | Mus | MALLPVGIRFIISFSRDQWYRAFIFMLTFLLYASFHLSRKPISIVKGELHKQCTAGDGPESPFSDPSSSTRHGPTHWLLNNETDCGWAPFDKNNYQQLLGALDYAFLCAYAIGMYLSGIIGERLPIRYYLTFGMLASGAFTALFGLGYFYNIHSLGFYVVTQIINGLVQTTGWPSVVTCLSNWFGKGRRGLIMGIWNSHTSVGNILGSLIAGYWVSTCWGLSFIVPGAIVAAMGIVCFLFLIEHPKDVKCSSTLPTHPRASENGINRFRLQKQTTYSEKNGPLDPELQCLLLSDGKNPLHPSHIVVLPADGNMAAISFTGALRIPGVIEFSLCLLFAKLVSYTFLFWLPLYITSVDHLDAKKAGELSTLFDVGGIFGGILAGVISDRLEKRASTCGLMLLLAAPTLYVFSSVSRMGLEATIAMLLLSGALVSGPYALITTAVSADLGTHKSLKGNSHALSTVTAIIDGTGSVGAALGPLLAGLISPSGWSNVFYMLMFADACALLFLVRLIHKELSCPGPAAGIQAPLKEH | Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. | Q8R070 |
Q0STU9 | FABH_CLOPS | 3-oxoacyl-[acyl-carrier-protein] synthase III | Clostridium | MENAKIIGFGLYTPKNLVENERLQEFLETSDEWIRSRTGIERRYISLDENTSDLAVEASKKALNQAGLSAEEIDLIIVATVTPDNFTPSTACIVQDKLGAKNAWAFDINAACTGFIYALKLGRSLIRSGEAKNALIIGAETLSKALNWEDRGSCVLFGDGAGAIVLTSTEEDCGIKCVNVKSDGSKGDSLVIQGLPLNSPFKDGREVSKNYINMNGREIFKFATKVMEESIVEILEKENIKIEDISAIIPHQANLRIIDYVVKRLGIPREKFVTNLQNYGNTSGASIPIALCESINEGNLKKGDNIIMVGFGGGLTWGAALIKL | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. | Q0STU9 |
B0JQ94 | RL9_MICAN | 50S ribosomal protein L9 | Microcystis | MAKRMQVILNQKVSKLGENGDVVEVAPGYARNYLIPQGVAVLATKGAIKQAEFRKEKERQRLLAEKQEAETRKTAIEKLSPYSIPKQVGENEAIFGTVTSQDVATVILENAKLEIDRRGITVPDIGQLGVYKVQVKLHPEVSADIEIKVIAQ | Binds to the 23S rRNA. | B0JQ94 |
Q3ZC07 | ACTC_BOVIN | Actin, alpha cardiac muscle 1, intermediate form | Bos | MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Q3ZC07 |
A9JRD8 | BTB6A_DANRE | BTB/POZ domain-containing protein 6-A | Danio | MPAAPECRLSNHGRIMKCVTFLLLLPETLKKLKRASKHPGRLSVCYNILTLSLKKRMAAELYPVSDHATLQKSGAVMLSLPEKKRNVEPVSQTTASIATTPTTEQNINNNNVEIPSWHSAHPTLRERNALMFNNEQMADVHFIVGPPGESQRVPAHKYVLAVGSSVFCAMFYGDLAEGDSDIHIPDVEPAAFLILLKYMYSDEIELAPDTVLATLYAAKKYLVSALARACVGFLETSLEARNACVLLSQSRLFEEPELTQRCWEVIDAQAELALRSEGFSEIDLPTLESILHRETLNVKESVVFQAVLGWADAECRRQGLSPTSQNQRSVLGKALHLVRLPSMTLQEFADGAAQVDILTLEETHSIFLWYTAATKPSLGFPVNAREGLTAQRCHRFQSSAYRSNQWRYRGRCDSIQFAVDKRVFIAGLGLYGSSGGKAEYSVRIELKRQGVLLAQNLTKFVSDGSSSTFPVWFEHPVQVEQDAFYTVSAVLDGSELSYFGQEGMTEVQCGKVTFQFQCSSDSTNGTGVQGGQIPELIFYA | Adapter protein for the cul3 E3 ubiquitin-protein ligase complex. Promotes the export of zbtb16/plzf from the nucleus to the cytoplasm and targets zbtb16/plzf for ubiquitination and degradation. Up-regulates neurog1 expression and antagonizes zbtb16/plzf, to promote neurogenesis. | A9JRD8 |
A2BUK4 | AROC_PROM5 | 5-enolpyruvylshikimate-3-phosphate phospholyase | Prochlorococcus | MSSIFGKIFRVSTFGESHGGAVGVILDGCPPKLKINIDLIQNELDRRRPGQSKITTPRKEDDKLEILSGLKEGITLGTPIAMLVRNKDQRPEDYNNLEQVFRPSHADGTYHLKYGIQAGSGGGRASARETIGRVAAGAIAKQLLKTLFNTEILSWVKRIHDIDSQVNKNKLTLSKIDSNIVRCPDEKVATKMIQRIKELQQEGDSCGGVIECLVKNVPSGLGMPVFDKLEADLAKALMSLPATKGFEIGSGFLGTYLRGSEHNDSFVESDDINKLKTKSNNSGGIQGGISNGENIEMKIAFKPTATIGKEQKTVNSDGKEIVMKAKGRHDPCVLPRAVPMVDSMVALVLADHLLLHQAQCSIIK | 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 second double bond into the aromatic ring system. | A2BUK4 |
Q5PCX2 | AROC_SALPA | 5-enolpyruvylshikimate-3-phosphate phospholyase | Salmonella | MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFDGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLEIKDWRQVELNPFFCPDADKLDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGEGFNVVALRGSQNRDEITAQGFQSNHAGGILGGISSGQHIVAHMALKPTSSITVPGRTINRMGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRHRAQNADVKTEIPRW | 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 second double bond into the aromatic ring system. | Q5PCX2 |
B1ZFQ8 | RS6_METPB | 30S ribosomal protein S6 | Methylorubrum | MPLYEHVFLARQDVTAQQVETMVETYKGVIETGGGTIEKIESWGVKSLAYRIKKNRKAHFTLLNISAPPAALAEMERQMQISEDVLRFMTVRVEQLEAEPSAMMQKRDRDDRKDRDRGDRPRRRDDDFGGGDRGDRGDRGDRPERNFGGEN | Binds together with S18 to 16S ribosomal RNA. | B1ZFQ8 |
Q3ALF6 | HIS6_SYNSC | ImGP synthase subunit HisF | unclassified Synechococcus | MVALRLIPCLDVARGRVVKGVNFVGLRDAGDPVELACRYSRAGADELVFLDIAASHEGRGTLIDMVRRTAESVTIPFTVGGGISTVEGITELLRAGADKVSLNSSAVRRPELVREGADQFGCQCIVVAIDARRRDAGGWDVYVKGGRENTGLDVVEWAQRVAGLGAGEILLTSMDGDGTQAGYDLALTRAVADAVPIPVIASGGAGCLDHIAEALDVGPTGGHASAALLASLLHDGVLTVEEIKQDLLSRGLTIRP | 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. | Q3ALF6 |
Q0HM20 | RLMC_SHESM | 23S rRNA(m5U747)-methyltransferase | Shewanella | MSTLVQCGYFERGQCQSCRHIKLPMAQQLAAKTQELQQLLAPFVDNAEPQFLPPVVGDSSGFRNKAKMVALGAAHAPVLGIVSPSGEAVSLCDCLLYPADMQALLHRLERFVQQAGIPPYRVDKAKGELKFILLTRSQVRGEYMLRFVLRSRDAIARIERELPALMAEYPQIKVVSVNLQPVHMAILEGEEEIFLTENTRLEERFNDVPLFIRPKSFFQTNPQVAAKLYQTAREWVADFAPASLWDLFCGVGGFGLHCAAKDIPLTGIEIEAEAIACAKMSAQLMGLDKVQFMALDSTDFAKGDAAQTKPELIIVNPPRRGIGESLCHSLSEFAPKAILYSSCNPKTLAKDLGHIRGYRLTKVQLFDLFPHSDHFEVLALLVKD | Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. | Q0HM20 |
P04845 | OMPA_SERMA | Outer membrane porin A | Serratia | MKKTAIALAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFYGNGYQNGIGNGPTHKDQLGAGAFLGYQANQYLGFELGYDWLGRMPYKGSVNNGAFKAQGVQLAAKLSYPIADDLDIYTRLGGMVWRADSKANYGRTGQRLSDHDTGVSPLAAVGVEYALTKNWATRLDYQFVSNIGDAGTVGARPDNTMLSLGVSYRFGQDDVVAPAPAPAPAPVVETKRFTLKSDVLFNFNKSTLKAEGQQALDQLYTQLSSMDPKDGSVVVLGYTDAVGSDQYNQKLSEQRAQSVVDYLVSKGIPSDKISARGMGEADAVTGNTCGYKSGRATKAQIVCLAPDRRVEIEVKGIKDVVTQPQG | With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | P04845 |
Q5M869 | SIT1_RAT | Suppression-inducing transmembrane adapter 1 | Rattus | MSRENNCTTADLAWGIPSITQAWGLWALFGVVTMLLLISLAALLSQWTRGRRRTQEEQGPPSGRSVEEVPLYGNLHYLQTGRLSEESRSEEQDPSSGGLARGAEEATCYTSLQLRPAQGRIPSSGTPIKYCEVVLDSEPKPQASGPEPELYASVCAQTRRARASFPDQAYANSQPAPS | Negatively regulates T-cell antigen receptor (TCR)-mediated signaling. Involved in positive selection of T-cells. | Q5M869 |
Q6MSM5 | RS10_MYCMS | 30S ribosomal protein S10 | Mycoplasma | MAESKMRIKLKGYDHAIVDQSIVKIIQAAEGTGAKVRGPIPLPTEKQVITILRAVHKYKDSREQFDMRTHKRLLEILNPTAATMDILKRVQLPSGVDIEIKL | Involved in the binding of tRNA to the ribosomes. | Q6MSM5 |
Q2S2F9 | MIAA_SALRD | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Salinibacter | MEPLSEPDASDPILTITGPTAVGKTAVSLEAAEQLNAEIVSVDSRQVYEELTIGTAKPSPSEQRRAPHHFIGERSLHEPFSAGAYAKAANDRIRAVLERGRRPLVVGGATLYLHALQYGLADIPDVDDEVRDELNQRLESEGQDALYEELQQVDPRQAAETDPTKTQKVIRALEVYHGTGKPLSYYYENQPEPPFDYVTVVLNRDREKLYDRINQRVDRMLDAGLLDEVRDVMDIDGVQLDEPPLSTIGYREPIQHLKGDIDYDEMVRLVKRNTRRYAKRQLTWFRRYDEYHWRAAPETRAEDLIEVLKNALDPTHSAAEGSAR | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | Q2S2F9 |
Q0RRS9 | RPOC_FRAAA | Transcriptase subunit beta' | Frankia | MLDVNFFDELRIGLATADDIRQWSHGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWECYCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDLAPKDLEKVIYFAAYMITKVDAEARHRDLPTLEARMGVEKQQLEDKKNADVETRQKRLETDLAQLEAEGAKGDARRKVRESAEREMRQIRDRAQRKIDDLDRVFDRFKNMKVQDLEPDELLYRELRDRFGQYFDGGMGAEALQRRLADFDLAAEAESLRETIRSGKGQKKARALKRLKVVSAFLNTRNSPMGMVLDCVPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPEIIVNNEKRMLQEAVDALFDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKQMALELFKPFVMKRLVDLNHAQNIKSAKRMVERARPVVWDVLEEVITEHPVLLNRAPTLHRLGIQAFEPQLVEGKAIQIHPLVCTAFNADFDGDQMAVHLPLSAEAQAEARILMLSSNNILSPASGRPLAMPSLDMVTGVFHLSTLAEGAVGEGRAFSSVAEAQMAFDAREIALQARISVRLRDTTPPSDWVPPADWVTGDVFTLETTFGRCLLNEALPEGYPFINAQLNKKAQAAIVNDLAERYPKIQVAATLDALKSAGFYWATRSGVTVAIEDVVAPPNKAEILDDYEQRADRVQKQFDRGFLSDEERRSELVQIWTEATNKIAEAMEKNFPQTNPVYVLVNSGAAGNMMQIRQLAGMRGLVSNPKGEIIPRPIKANFREGLTVLEYFISTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREEDCGTERGILTRIARRGADGVLVRDRYAETSAYARTLASDAVDEHGEIIVPAGTDAGDVAIGQIIEAGIESVRVRSALTCESRMGVCAQCYGRSLATGKLVDVGEAVGIVAAQSIGEPGTQLTMRTFHSGGVAGDDITQGLPRVVELFEARSPKGKAPITEVSGRVKIEETEKTFKVVVVPDDGSEEIAYPVSRRSRLRVREGDRIEVGNQIVDGAVDPHEVLRILGPRQVQLHLVDQVQEVYRSQGVSIHDKHIEIIIRQMLKRVNVLESGETNLLPGELCERARFESENRRVVESGGQPASARPVLMGITKASLATESWLSAASFQETTRVLTDAAINARSDSLVGLKENVIIGKLIPAGTGISRYRNIRVEPTEEARAAMYSVGAYEDGGSVEYGAFGTGSGQAVPLDEFDYRSSGDFR | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q0RRS9 |
P48633 | HMWP2_YERE8 | High-molecular-weight protein 2 | Yersinia | MISGAPSKDSLLPDNRHAADYQQLRERLIQELNLTPQQLHDESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWNQLMLSRSPENAEEETLPDESSWPNMTESTPFPLTPVQHAYLTGRMPGQTLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNRHRLHVNIDLLIMDASSFTLFFDELNALLAGESLSAIDTRYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPLVCEPATLREVRNTRRRMIVPATRWHAFSNRAGEYGVTPTMALATCFSAVLARWGGLTRLLLNITLFDRQPLHPAVGAMLADFTNILLLDTACDGDTVSNLARKNQLTFTEDWEHRHWSGVELLRELKRQQRYPHGAPVVFTSNLGRSLYSSRAESPLGEPEWGISQTPQVWIDHLAFEHHGEVWLQWDSNDALFPPALVETLFDAYCQLINQLCDDESAWQKPFADMMPASQRAIRERVNATGAPIPEGLLHEGIFRIALQQPQALAVTDMRYQWNYHELTDYARRCAGRLVECGVQPGDNVAITMSKGAGQLVAVLAVLLAGAVYVPVSLDQPAARREKIYADASVRLVLICQHDASAGSDDIPVLAWQQAIEAEPIVNPVVRAPTQPAYIIYTSGSTGTPKGVVISHRGALNTCCDINTRYQVGPHDRVLALSALHFDLSVYDIFGVLRAGGALVMVMENQRRDPHAWCELIQRHQVTLWNSVPALFDMLLTWCEGFADATPENLRAVMLSGDWIGLDLPARYRAFRPQGQFIAMGGATEASIWSNACEIHDVPAHWRSIPYGFPLTNQRYRVVDERGRDCPDWVSGELWIGGIGVAEGYFNDSLRSEQQFLTLPDERWYRTGDLGCYWPDGTIEFLGRRDKQVKVGGYRIELGEIESALSQLAGVKQATVLAIGEKEKTLAAYVVPQSEAFCVTDHRNPALPKAWHTLAGTLPCCAISPEISAEQVADFLQHRLLKLKPGHTAGADPIPLMNSLAIQPRWQAVVERWLAFLVTQRRLKPAAEGYQVCAGEEREDEHPHFSGHDLTLSQILRGARNELSLLNDAQWSPESLAFNHPASAPYIQELATICQQLAQRLQRPVRLLEVGTRTGRAAESLLAQLNAGQIEYVGLEQSQEMLLSARQRLASWPGARLSPWNADTLAAHAHSGDIIWLNNALHRLLPEDPGLLATLQQLAVPGALLYVMEFRQLTPSALLSTLLLTNGQPEALLHNSADWAALFSAAAFNCQHSDEVAGLQRFLVQCPDRQVRRDPRQLQAALAGRLPGWMVPQRIVFLDALPLTANGKIDYQALKRRHTPKAENQAEADLPQGDIEKQVAALWQQLLSTGNVTRETDFFQQGGDSLLATRLTGQLHQAGYEAQLSDLFNHPRLADFAATLRKIDVPVEQPFVHSPEERYQPFALTDVQQAYLVGRQPGFTLGGVGSHFFVEFEIADLDLTRLETVWNRLIARHDMLRAVVLDGQQQVLEQTPPWVIPTHTLHTPEEALRVREKLAHQVLNPEVWPVFDLQVGYVDGMPARLWLCLDNLLLDGLSMQILLAELEHGYRYPQQLLPPLPVTFRDYLQQPSLQSPNPDSLAWWQAQLDDIPPAPALPLRCLPQEVETPRFARLNGALDSTRWHRLKKRAADAHLTPSAVLLSVWSTVLSAWSAQPEFTLNLTLFDRRPLHPQINQILGDFTSLMLLSWHPGESWLHSAQSLQQRLSQNLNHRDVSAIRVMRQLAQRQNVPAVPMPVVFTSALGFEQDNFLARRNLLKPVWGISQTPQVWLDHQVYESEGELRFNWDFVAALFPAGQVERQFEQYCALLNRMAEDESSWQLPLAALVPPVKHAGQCAERPPRVCPEHSQPHIAADESTVSLICDAFREVVGESVTPAENFFEAGATSLNLVQLHVLLQRHEFSTLTLLDLFTHPSPVALADYLAGVATVEKTKRPRPVRRRQRRI | Unknown. May be involved in the nonribosomal synthesis of small peptides. | P48633 |
P0C1N8 | M3B_CONTE | Tx3.3 | Cylinder | MSKLGALLTICLLLFSLTAVPLDGDQHADQPAQRLQDRIPTEDHPLFDPNKRCCPPVACNMGCKPCCG | Intracranial injection into mice causes scratching, hyperactivity and circular motion. | P0C1N8 |
A9M752 | MASZ_BRUC2 | Malate synthase G | Brucella | MGSAEKRNYVEIEGLAVAPELVEFLAKEAAPGTGVEPEKFWKGFAAIIRDLAPKNRALLAKRDELQARIDAWYKENRDKGYSQADYQQFLKDIGYLLPEGGAFSVSTTNVDPEITHIAGPQLVVPVMNARYALNAANARWGSLYDALYGTDAISEADGAEKGKGYNPKRGEKVIAWAKNFLDESAPLSTGKWADVAGLAVNDGKLEIRLTDGSATTLKDESQFKGYNGDAASPTNVLLAKHNMHVDIVINADHPIGKTDPAHIADVVLESAISTIQDCEDSIAAVDAEDKVAVYRNWLRLMNGKLEDTFEKNGKQMTRRLNGDRTYTAPDGSTLTLKGRSLMLVRNVGHLMTNPAILDAEGNEVPEGIMDAAFTSLIALHDIGPNGRHMNSREGSVYIVKPKMHGPEEVAFANEIFTRTEEMLGMKPNTLKIGIMDEERRTTVNLKEAIRAAKDRVVFINTGFLDRTGDEIHTSMEAGPMIRKGDMKQAAWIGAYEQWNVDIGLECGLSGHAQIGKGMWAMPDMMAAMLEQKIAHPKAGANTAWVPSPTAATLHATHYHKIDVAAVQEKLKSRPRAKLDDILSVPVAVRPNWTPDDIQHEIDNNAQGILGYVVRWIDQGVGCSKVPDINNVGLMEDRATLRISAQHIANWLYHGVVSEAQVMETMKRMAAIVDKQNEGDPLYRPMAADFDKSIAFQAACDLVFKGREQPNGYTEPVLHRRRLELKQAS | Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. | A9M752 |
O50143 | ATPE_RUMA7 | F-ATPase epsilon subunit | Ruminococcus | MAVFKLRVLTPEKIFFEGDAEQLIAKTTSGYVGILKGHAPYVASIVPSEMKIRSDGSFRSAAISDGIVKVSEDSMVTVLTSAIEWSDEIDVARAERSKARAEKQLKAETSRTEFDLAERQLKRAVNRISVANKK | Produces ATP from ADP in the presence of a proton gradient across the membrane. | O50143 |
Q5RAY7 | CMTR2_PONAB | FtsJ methyltransferase domain-containing protein 1 | Pongo | MSKCRKTPVQQLASPTSFSPDILADIFELFAKNFSYSKPLNNEWQLPDPSEIFTCDHTEFNAFLDLKNSLNEVKNLLSDKKLDEWHEHTAFTNKAGKIISHVRKSVNAELCTQAWCKFHEILCSFPLIPQEAFQNGKLNSLHLCEAPGAFIASLNHYLKSHRFPCHWSWVANTLNPYHEANDDLMMIMDDRLIANTLHWWYFGPDNTGDIMTLKFLTGLQNFISSMATVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFVLKMFTMFEHCSINLMYLLNCCLDQVHVFKPATSKAGNSEVYVVCLYYKGREAIHPLLSKMTLNFGTEMKRKALFPHHVIPDSFLKRHEECCVFFHKYQLETISENIRLFECMGKAEQEKLNNLRDCAVQYFMQKFQLKHLSRNNWLVKKSSIGCSTNTKWFGQRNKYFRTYNERKMLEALSWKDKVAKGYFNSWAEEHGVYHPGQSSILEGTASNLECHLWHILEGKKLPKVKCSPFCNGEILKTLNEAIEKSLGGAFNLDSKFRPKQQYSCSCHVFSEELIFSELCSLTECLQDEQVVEPSNRIKCLLVGFSTLHNIKMHIPLEVRLLESAELTTFSCSLLHDGDPTYQRLFLDCLLHSLRELHTGDVMILPVLSCFTRFMAGLIFVLHSCFRFITFFCPTSSDPLRTCAVLLCVGYQDLPNPVFQYLQSVNELLSTLLNSDSPQQVLQFVPMEVLLKGALLDFLWDLNAAIAKRHLHFIIQREREEINSLQLQN | S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs. | Q5RAY7 |
Q8YWF0 | MURE_NOSS1 | UDP-N-acetylmuramyl-tripeptide synthetase | Nostoc | MKLRELLATVDSVENLPPVLADAEVKGIKTNSHACGAGDLFIGMPGTRVDGGEFWPSAIASGAIAAIVSPQAVEKNPPHDEAVVISSNNMTKACAAIAAAFYGYPGQKLKLVGVTGTNGKTTTTHLIEFFLTKAKLSTALMGTLYTRWPGFEQTATHTTPFAVELQQQLAQAVNAGCEFGVMEVSSHALAQGRVLGCPFEVGVFSNLTQDHLDYHSDMEDYFAAKALLFSPEYLKGRAIINADDTYGQRLIKALSPEKVWSYSVNDSSADLWMSDLSYEPNGVTGTIHTPEGNVSFRSPLVGQYNLENLLAAVGAVLHLGLNLQLIANAIPEFPGVPGRMERVQINPDQDISVIVDYAHTPDSLENLLKAARPFIPGRMICVFGCGGDRDRTKRPKMGKIVAELADLAFVTSDNPRTEDPDRILDDILAGIPDTVQPTVIGDRAIAIRTAILQAQPGDGVLLAGKGHEDYQILGTEKIHFDDREHARAALTEREKL | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q8YWF0 |
Q49406 | EX53_MYCGE | 5'-3' exonuclease | Mycoplasma | MKKAILIDGNSLAYRAYFATWKQVEYAKQNNLPFNNAIRTMLLMCWNLIKANVYQYGIVSFDTKAPTFRDQIYEGYKQKRVKTPVELLVQIPLIKQALVYLGFLVCEKDGFEADDLIGSYANLFTKQEITVDIYSSDRDMLQLVNAFTNVFLCIKGTKEMVMYNNENFKSLFYGLAPYQVVEYKGLVGDNSDNLAGIKGIGPIKGIELLQQYGTIDNIYTNFNNLPNQLQKLLNNQKEIAKTFSFLAKIKTDIELDQNIDLTGLKPIQKQALIQLLSENKINTLVEKFSKI | 5'-3' exonuclease acting preferentially on double-stranded DNA. | Q49406 |
Q82ZQ1 | ALLB_ENTFA | Allantoin-utilizing enzyme | Enterococcus | MQAELVIKNGLVILETGEVITDVAVQGGKIVAIGQDLSGERVIDATGLVVSPGMVDAHVHITDPGGGYRDEWEGYVTGTAACAKGGVTTFMEMPLNQIPATVDKTSLEIKYKAGENKLKVDVGSFGGVVPTNLADGIQELDEGGVSGYKCFLGTCGDRSIEGDFQNVDDYSLYEGMKQVAKTGKVLAIHAENAPITDKLGAVAYQNGETTLAAYVATRPVFTEVEAIQKAILFAKETGCRIHICHVACQEGVEEVLKAQAEGVDVTCETCTHYLYFTTDELDAIGPVVKCSPPIRDADQQAALWNHVQTGGIAFVTSDHSPCTPDLKDTTNAFEAWGGISGVQNNVDVLFDEAVQKRGLSLKQFADMIAANPADRYHLAQKGRISIGKDADFVLIKPNAPYILKAEDLEYRNKISPYIGREIGAQVIQTILRGETIYAQETGVTEAFNGVFIKN | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. | Q82ZQ1 |
C6E105 | RS20_GEOSM | 30S ribosomal protein S20 | unclassified Geobacter | MANHKSAMKRIKQTAKRTERNKHERSTLRTFIKRVREAVATKDQEAAKAALAVAIPVIDGAATKGIIHSSNASRNVSRLTKLVNTLG | Binds directly to 16S ribosomal RNA. | C6E105 |
Q57457 | LPTE_HAEIN | LPS-assembly lipoprotein LptE | Haemophilus | MINSIKTLLLIATLAILSACGWHFQQSVTMPSEWRTLALESDDSYNDFTVIMRRKLQENQVNVVNLEQNIPILRINKQITSDQVASIFKHGREAEKLLMLEVEATFRLANGESYPINAKVNRTFFDNARAALAKSEEREVIWNDMREQVARQLIVKIIALQNQIKRK | Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. | Q57457 |
A4XLQ7 | IF1_CALS8 | Translation initiation factor IF-1 | Caldicellulosiruptor | MSKEDVIELEGTVIEALPNAMFQVQLDNGHKVLAHVSGKLRMNFIRILPGDRVVVQLSPYDLTRGRIVWRSK | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. | A4XLQ7 |
Q9M815 | PCR8_ARATH | Protein PLANT CADMIUM RESISTANCE 8 | Arabidopsis | MGRVTTPSEEDSNNGLPVQQPGTPNQRTRVPVSQFAPPNYQQANVNLSVGRPWSTGLFDCQADQANAVLTTIVPCVTFGQIAEVMDEGEMTCPLGTFMYLLMMPALCSHWVMGSKYREKMRRKFNLVEAPYSDCASHVLCPCCSLCQEYRELKIRNLDPSLGWNGILAQGQGQYEREAPSFAPTNQYMSK | May be involved in heavy metals transport. | Q9M815 |
P08319 | ADH4_HUMAN | Alcohol dehydrogenase class II pi chain | Homo | MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGVAAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDKISEAFDLMNQGKSVRTILIF | Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol . Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate . Also catalyzes the reduction of benzoquinones . | P08319 |
A0A0H2VFI8 | ETTA_ECOL6 | Translational regulatory factor EttA | Escherichia | MAQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNETNELFIPPGPRLGDKVLEVSNLRKSYGDRLLIDSLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRIAK | A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase. | A0A0H2VFI8 |
Q9UTE3 | SEB1_SCHPO | Rpb7-binding protein seb1 | Schizosaccharomyces | MSGIAEFDGILDSLEHSKTGISGSKILKLTNLSMENVSENAQFVASVYKYAKRAPVTHKLGALYILDSIVRSFQDGAKKNNESFENPVDASFSGGWCKAAEITDSLVADAIQHAPSAHLPKILKLCDIWEKASTFPPEKLESLRSKLKDAMASTEPVSVDSAAAPSQSTNPEGNGGSVGSQAAAPTSRPVENDAASILEALAAFAQKAPVPSAAEESVSTPPQPAVAPSVSAVVPNLPVHPATAINAQSQSGNPLSNPLFQPSNVPQSIPSGPMGMKTGSVNDTQSQQITLMNVLASQNVPPAQIDSIMKAAFPNYNAPFQPAGVGSVPLPAPTSSQSLRLGSLHRSRSPSPRSGRPRRSPSPSHLSIPSTLPPADGVPKPTPDGFPRRFERDPTIPPDSIKVYSRTLFLGGITRSVREPVLRSMFERFGSVQSLILNHNYRHGFLKMFRRDAAEKAQVAMENVPFADTTIRTKWGVGFGPRECSDFSTGISVIPIRLLTDADRTWLVTAEYGGTGGLPITPGIALDEPDIEIGLGISSKAISKRGKDFAMRRDERFRGRKPYRGGPPIHHGERHFDSGNDWHGNPSTVPPPTNPYNPGYPYMDPNYSSGYVSQPPWQPQ | Involved in the processing of pol II transcripts. | Q9UTE3 |
Q8VCL2 | SCO2_MOUSE | Protein SCO2 homolog, mitochondrial | Mus | MLLALGPKAWPKLSQFKPLLRISGGETLHRNSRHWAGQGQRQGPGLRTRLLITALFGAGLGWAWLAARAEKEQWRQQQRTEALRQAAVGQGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPDLPLVQPVFITVDPERDDVAAMARYVQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAAFHSVLP | Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2. | Q8VCL2 |
P35304 | HSP1_CAVPO | Cysteine-rich protamine | Cavia | MARYRCCRSPSRSRCRRRRRRFYRRRRRCHRRRRRCCRRRYTRRCKRY | Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. | P35304 |
Q08831 | VTS1_YEAST | VTI1-2 suppressor protein 1 | Saccharomyces | MKHPYEEFPTGSKSPYNMSRGAHPGAVLLSPQSSAINKNNPGSNSGNNQGNSSVTANVLSPQSHSMSLNDMLDQQSFMLDTAGTRAQPLQQQQQQQQQQQQASLPSLNIQTVSSTAAGSAIVSPMMQSPKALQSTLSSTSMYLDSFQRSPNNILGIPSQSGSIPLPQSRQSQQQSQSQKNDPNMGTNFSQDINQLCSWISMLNSSQQNTVMDNILSILNDDVLKYTKLKIETLTNTPFISPPLPAIASPIPNRDDTQILNIDSVFSSSPITNDPENTDNLLYQNWSPQPHSIPISQPIYDNITDASQRSKSAEPHVNSSPNLIPVQKQFNNGNSTKYKKLPSENPNYLSHSLSSSHSFFQPKKRSNMGNEYNSHHHHSLHHPLHNTTSYFSNTSRPSGTDLNKSNQNVFNNTITHPNAGPTSATSTSTSSNGNTPLSSNSSMNPKSLTDPKLLKNIPMWLKSLRLHKYSDALSGTPWIELIYLDDETLEKKGVLALGARRKLLKAFGIVIDYKERDLIDRSAY | RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. | Q08831 |
Q8E3P5 | GATB_STRA3 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Streptococcus | MNFETVIGLEVHVELNTNSKIFSPSSAHFGQEQNANTNVIDWSFPGVLPVMNKGVVDAGIKAALALNMDIHQNMHFDRKNYFYPDNPKAYQISQFDEPIGYNGWIEIELEDGTRKKIRIERAHLEEDAGKNTHGTDGYSYVDLNRQGVPLIEIVSEADMRSPEEAYAYLTALKEIIQYTGISDVKMEEGSMRVDANISLRPYGQEEFGTKAELKNLNSFNNVRKGLIHEEKRQAQVLRSGGQIQQETRRFDETTGETILMRVKEGSSDYRYFPEPDLPLFDISDEWIDQVRLELPEFPQERRAKYVSSFGLSSYDASQLTATKATSDFFEKAVAIGGDAKQVSNWLQGEVAQFLNSESKSIEEIGLTPENLVEMISLIADGTISSKIAKKVFVHLAKNGGSAEEFVKKAGLVQISDPEVLIPIIHQVFADNEAAVIDFKSGKRNADKAFTGYLMKATKGQANPQVALKLLAQELAKLKEE | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). | Q8E3P5 |
Q8RQQ0 | NPHA1_RHOSO | Two-component 4-nitrophenol hydroxylase | Rhodococcus | MTTSAFVDDRVGVPNDVRPMTGDEYLESLRDGREVYFRGERVDDVTTHPAFRNSARSVARMYDALHQPEQEGVLAVPTDTGNGGFTHPFFKTARSADDLVLSRDAIVAWQREVYGWLGRSPDYKASFLGTLGANADFYGPYRDNALRWYKHAQERMLYLNHAIVNPPIDRDKPADETADVCVHVVEETDAGLIVSGAKVVATGSAITNANFIAHYGLLRKKEYGLIFTVPMDSPGLKLFCRTSYEMNAAVMGTPFDYPLSSRFDENDAIMVFDRVLVPWENVFAYDTDTANGFVMKSGFLSRFMFHGCARLAVKLDFIAGCVMKGVEMTGSAGFRGVQMQIGEILNWRDMFWGLSDAMAKSPEQWVNGAVQPNLNYGLAYRTFMGVGYPRVKEIIQQVLGSGLIYLNSHASDWANPAMRPYLDQYVRGSNGVAAIDRVQLLKLLWDAVGTEFGGRHELYERNYGGDHEAVRFQTLFAYQATGQDLALKGFAEQCMSEYDVDGWTRPDLIGNDDLRIVRG | Utilizes the flavins supplied by NphA2 to catalyze the degradation of 4-nitrophenol (4-NP) via 4-nitrocatechol (4-NC) which is used as the sole carbon, nitrogen, and energy source. Can also degrade phenol and 4-chlorophenol as rapidly as 4-NP. | Q8RQQ0 |
A1EA34 | PSBB_AGRST | Protein CP-47 | Agrostis | MGLPWYRVHTVVLNDPGRLLAVHIMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITDSWGGWSISGGTVTNPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFSDERTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQAVNPAWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSNGLAENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPVFRDKEGRELFVRRMPTFFETFPVVLVDEEGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRSQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGTFQKVGDPTTRKQAV | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. | A1EA34 |
Q68XE1 | PARE_RICTY | Topoisomerase IV subunit B | typhus group | MSDLFSFNNKEKKNKIIYTNYSAKDIEVLDGLEPVRKRPGMYIGGTDSNAMHHLVSEVLDNAMDEAVAGFASIIMIKMHQDHSITIFDNGRGIPIDNHPKFPNKSALEVILTTLHSGSKFSNNVYHTAGGLHGVGISVVNALSKHLKIEVYQQGKLYSQSYSKGEKLTDLISTEVSKRLRGTSINFTPDPEIFSETLHFNPKKIYEIARSKAYLYRGVSIEWECEVEVPSDIPKKALINFPNGLKDYLSSKISLDNLVIPEIFSGNIESTMDAIKLEWAICWQNNDTSAFMKSYCNTVPTPQGGTHEQGLKSAILRGLKAYSEMIGNKKSANLTIEDIFETASVVLSVFIVEPSFQGQTKEKLVSNGVSKLVENIIKDHFDHFLSSDKVLATHLLEHVIAISEFRRNKKNERNISRKNATQKLRLPGKLADCTRTSAEGTELFIVEGDSAGGSAKQARNRETQAVLPLWGKVLNVASSTLEKIINNQAIQDLEIALACGSLKNYKKENLRYEKIIIMTDADVDGAHIASLLMTFFFLRMPQLVKEGHLYLAKPPLYRLTQSNKIYYACDEEEKIKLTYKLSKTSKAKIEVGRFKGLGEMMPAQLKETTMHPEKRSLLKVTLEDVQNVDKIVDDLMGKKPEKRFQFIYEQALVKMDQIINKLDI | Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. | Q68XE1 |
Q6GEV0 | ALF2_STAAR | Fructose-1,6-bisphosphate aldolase | Staphylococcus | MPLVSMKEMLIDAKENGYAVGQYNINNLEFTQAILEASQEENAPVILGVSEGAARYMSGFYTIVKMVEGLMHDLNITIPVAIHLDHGSSFEKCKEAIDAGFTSVMIDASHSPFEENVATTKKVVEYAHEKGVSVEAELGTVGGQEDDVVADGIIYADPKECQELVEKTGIDALAPALGSVHGPYKGEPKLGFKEMEEIGLSTGLPLVLHGGTGIPTKDIQKAIPFGTAKINVNTENQIASAKAVRDVLNNDKEVYDPRKYLGPAREAIKETVKGKIKEFGTSNRAK | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | Q6GEV0 |
A8GMX9 | TOLB_RICAH | Tol-Pal system protein TolB | spotted fever group | MRNIIYFILLLLFSFKGYALETINIEHGQAAPTPIAVNKFNIDSSADYVLGNDVVKVISNDLKLSGVFCPISSASFIEERTGIEYKPLFAAWRQINASLLVNGEIKKLESGKLKISFILWDTLLEKQLAGEILEVPENLWRRAAHKIADKIYEKITGDAGYFDTKIVYVSESTSLPKIKRIALMDYDGANNKYLTNGRSLVLTPRFARSADKIFYVSYATKRRALVYEKDLKTGKESVVGDFSGISFAPRFSPDGRKAVMSIAKNGSTHIYEIDLATKRLHKLTDGFGINTSPSYSPDGKKIVYNSDRNGVPQLYIMNSDGSDVQRISFGGGSYTAPSWSPRGDYIAFTKIIRGAEGKTFNIGIMKAYPQDDENRERIITSGYLVESPCWSPNGRVIMFAKGWPSGAKAPGKNKIFAIDLTGHNEREIITPEDASDPEWSGVLN | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | A8GMX9 |
A6T306 | HSLV_JANMA | ATP-dependent protease subunit HslV | Janthinobacterium | MEQFHGTTILSVRRGNIVALGGDGQVTLGNIVMKGTARKVRKVYNGKVLVGFAGGTADAFTLLERFESKLEKHQGHLMRASVELAKDWRTDRMLRRLEAMLLVADKETTLIITGNGDVLEPNDGIGAIGSGGTYAQSAAKALQENTDLSPEDIVKKSLTIAGELCIYTNLSHIIETLD | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | A6T306 |
Q0AD66 | FPG_NITEC | DNA-(apurinic or apyrimidinic site) lyase MutM | Nitrosomonas | MPELPEVEVTRRGIDAHLAGRYITQVKIRNYALRWPVSPELITLLPGQRINTITRRAKYLLFACSKGTLIIHLGMSGSLRVLPVSTPSLLHDHFELWLDNEKMLRFRDPRRFGVILWWDGDVRQHPLLQKLGPEPLSDAFNGLFLHEKIQRRSISIKEALMNQHIVVGIGNIYANEALFHAGISPLIAAGSLSTALCARLVDAVKMTLQRAIEAGGSSLRDFTDCDGSPGCFQQQYWVYGRTGQPCRKCGALVSKTRQGQRSSFFCAQCQK | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | Q0AD66 |
Q2JLR0 | DAPF_SYNJB | PLP-independent amino acid racemase | unclassified Synechococcus | MTPRLSFHKYQGLGNDFILVDNRWQSQPCLSPEEAVALCNRRFGVGADGVIFLLPGQEGADFSMRLFNSDGSEAEMCGNGIRCLARFLQDLGIPGRDGAYQIHTLAGRIVPQVRADGLVTVDMGIPRLLAKQIPTTLVEPDEKVIRQPLAVAGREWRVTAVSMGNPHCVVFLEEEGSLEELDLAAVGPLFEHHPAFPERTNTEFVQVLSPTRLRLRVWERGAGATLACGTGACAVLVAAVLEERAESQATVELPGGNLEIRWDPSTQHVWMTGPALHVFSGTTAG | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | Q2JLR0 |
Q6DIP3 | RN126_XENTR | RING finger protein 126 | Silurana | MAEALPEAGRYFCHSCTAEIIPRLPEYTCPRCDSGFIEELPETRNSENNSSNNSGTDQNRPSFENLESAQFTLPSGYGQVTFGIFNEGLDFPIFGTSGPVEEPRDGESRREHQSRQRYGARQPRARLSTRRAAGRNEGVPTLEGIIQQLVNGIIAPTAMSNLGVGPWGVLHSNPMDYAWGANGLDTIITQLLNQFENTGPPPADTEKIQALPTIQITEEHVGSGLECPVCKEDYTVGESVRQLPCNHLFHNDCIIPWLEQHDTCPVCRKSLSGQNTATNPPGLTEMTFSSSSTSSSSSTSPTDENNAANNS | E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome. | Q6DIP3 |
Q25145 | TPM_HALRU | Tropomyosin | Haliotis | MDAIKKKMLAMKMEKENAVDRAEQNEQKLRDTEEQKAKIEEDLNNLQKKCANLENDFDSVNEQVQVAMAKLETSEKRVTEMEQEVSGTTRKITLLEEDLERNEERLQTATERLEEASKLPDESERGARVLESRSLADDERIDQLEAQLKEAKYIAEDAERKYDEAARKLAITEVDLERAEARPKAAEAKILELEEELKVVGNNTKSLEISEQEASQREDSYEETIRDLTQRLKDAENRATEAERTVSKLQKEVDRLEDELLAEKEKYKAISDELDQTFAELAGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q25145 |
O15287 | FANCG_HUMAN | DNA repair protein XRCC9 | Homo | MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGNRDTYFHLLQTLKRLDRRDEATALWWRLEAQTKGSHEDALWSLPLYLESYLSWIRPSDRDAFLEEFRTSLPKSCDL | DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene. | O15287 |
Q8CN17 | RBSD_STAES | D-ribose pyranase | Staphylococcus | MKKTAVLNSHISSAISTLGHYDLLTINDAGMPIPNDDKRIDLAVTKSLPRFIDVLETVLTEMEIQKVYLAEEIKTANAQQLKAIKKLINDDVEIKFIAHSEMKEMLKSPLNKGNIRTGEITPFSNIILESNVTF | Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. | Q8CN17 |
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