habdine/Prot2Text-Data · Datasets at Hugging Face

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
F7ZLS5	HYEP_ROSLO	Hydrophobic dipeptide epimerase	Roseobacter	MKVEYHTVYLKKRFPLRISRGVFEGSDNLYISLTENGHTGWGEMAPGGTEGAETAAAGQAMLEQFCATGLSASIHDTWQNAHAAGVAPCALAALDMALWDLRAKQAGVPLYALLGLARRAVVSSVTVGINPPDVVRERVPLLLARGARALKIKLGSPEGIEADQAMFAAVFEAAQGSGAVLRVDANGGWSLKDARRMMGWLAEHDVEYIEQPLVRGAEDQLPDLFKDRAMPIFVDESCRMSGDIATFFQSVDGVNLKLMKCGGITEALRIVATARAFGLKTMIGCMGESSVSIAAGASIGALFDYIDLDSHLNLDPDPATGAPFENGITLPADQPGHGGVLSHA	Dipeptide epimerase with a preference for hydrophobic substrates. Catalyzes the epimerization of L-Ala-L-Thr, L-Ala-L-Met, L-Ala-L-His, L-Ala-L-Phe, L-Ala-L-Tyr, L-Ala-L-Trp, L-Ile-L-Ala, L-Ile-L-Ser, L-Ile-L-Met, L-Ile-L-His, L-Ile-L-Phe, L-Ile-L-Tyr, L-Ile-L-Trp, L-Phe-L-Met, L-Phe-L-His, L-Phe-L-Phe, L-Phe-L-Tyr, L-Phe-L-Trp, L-Phe-L-Ser, L-Phe-L-Thr and L-Phe-L-Lys (in vitro).	F7ZLS5
Q6CQP9	VMA21_KLULA	Vacuolar ATPase assembly integral membrane protein VMA21	Kluyveromyces	MPVDVPRSVIAKLMFFTVAMVVLPVLTFFWLQEHTDNTLVSGGLAAAMANLVLIAYVIMAFQEDSSSSEDDETKKEK	Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.	Q6CQP9
Q46WT0	HEM1_CUPPJ	Glutamyl-tRNA reductase	Cupriavidus	MQLLAIGINHTTAPVSLRERVAFPLEQIKPALGALRTHLAGRNGTEAAILSTCNRTEIYCATDILKPGAEGFEHTLRWLSQHHNVPASDLAPHLYSLPQSEAVRHAFRVASGLDSMVLGETQILGQLKDAVRTAGEAGSLGTYLNQLFQRTFAVAKEVRGQTEIGAHSVSMAAAAVRLAQRIFESVSTQRVLFIGAGEMIELCATHFAAQKPRQVVVANRTVERGEKLAEQLAEQGLTTQAIRLQELGERLHEFDIVVSCTASSLPIIGLGAVERAVKRRKHRPIMMVDLAVPRDVEPEVARLDDVFLYTVDDLGAVVREGNALRQAAVAQAEAIIESRVQNFMHWLETRSVVPVIRELQTAGESIRQAELERARRMLARGDDPEAVLEALSGALTRKFLHGPTHALNHMQGEDREALVRLVPGLFRQSSHSER	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).	Q46WT0
Q9HLV2	PCKG_THEAC	Phosphoenolpyruvate carboxykinase [GTP]	Thermoplasma	MLAIDESELNQHAMKWIEGIKKFTEAEDVVVCDGTPEEFKQISNELIKSGEFIKLNENRYPNSFLYRSDRTDVARSEERTFIAAPDASMAGSLNNHMTLQQVSEVWNKFFRGAYRGKTMFVIPYALGPLNSRFTDYGIEITDSRYVVLNLHYITRMGKQVIGSMPEKFVKGVHATGTLDPGNKFIIHIPWDKPEGVDADILSVNTNYGGNALLSKKCHALRIASVRARKEGWLAEHMLLLEVEDPHGRKVYITGAFPSASGKTNLAMINPPKQYAEAGWKTRLLSDDIAWMKMKDGMLYATNPENGFFAVVPGTNYRTNKNAMITLSRNTIFTNTGMTKTGEPWWEGLDPLQEELYDWKGVLRKPDGEPIAHPNSRFTSPLSNYPFLSDRSEDPEGVPVSAILFGGRRASLVPLVYEAFNWNHGVFMGATMGVEKTAASEGKVGELRRDPMAMRPFCGYNISDYFRHWIEMGRKLSRRPKIFYVNWFRRRQDGSFIWPGFSENFRVIEWILYRLDHNDNAIETPIGYIPENINTDGLNLTKQDMEELFRIDRDGWREEMKSIGDYFSQIGNIPEDLLIEFEMEKRRIS	Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.	Q9HLV2
P47315	PTG3C_MYCGE	PTS system glucose-specific EIIA component	Mycoplasma	MQISLVKIRNKFKQRNRGSFRQWVGKLSNGLMIPIAVLPLAGIFLGIGDAISSNSSGIVGVKFFGEFIKQGGNVVFANLPILFAVAIAITFSQDAGVAGFSAFVFWATMNAFMSSLIIPVDANNTASGYNILYWKAVPQSAIASTLGLNSLSTSVFGGIIVGALTAYLYNKFYAIRLPDVIGFFSGTRFVPIICMTIAIPVALLLLMVWPGVSILLNLIGTGLGILGGRGYGANSLIFGYIERALIPFGVHHAFYAPLWYTSAGGSLQEIANQQVWIRAPGSDYVTRVIGWEDFNTPGKWVIPAALANGTSGMMNGATTTGQDSTSALSKYMSKESTNFLSWKELVDGLTRKGNFDELAKNGLLDGSNKIWIGLNQSGILGKKVLLSDGKDYTITFKTFANTTPTFWSHGAHALLPISGTPSAITNGVTVNGTANSKTYNVSQFTVAVPSLNPAQYSQGKFPFMLIGIPAAGLAMILAAPKGRRKEASSIIGSAAFTSFLTGITEPFEFTFLFLAPWLFYGIHAVLAAVSFWLMNLLSANVGQTFSGSFIDFILYGALPDGRGWLANSYLVPIIGIFLALIYFPTFYFLTIRFNLATPGRGGKLITKKEYLAAKAAQKTDQTTNTNFNQTQIEAGMLLRAYGGSENIAELGACITKLRVTVKNPELVNETIIKDLGAAGVMRTTPTFFVAVFGTRAAVYKSAMQDIIQGKVNWTELQKVLDKNDSTVEKPEIKPTPVLKVQDEIVILSPVNGTLKPLTQVPDDTFKNRLVGDGIAILPSDGHFKAPGDVGVKTELAFPTGHAFIFDVDGVKVMLHIGIDTVKINADKKPGEQLEVFDVKTKQGEYTKLKSESVVEVDLKKLKRKYDPITPFIVMQESLDNFKLVPIRQRGEIKVGQPLFKLIYKDKKS	The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.	P47315
Q92209	KHSE_CANAL	Homoserine kinase	Candida	MSVISFKIKVPASSANIGPGFDVLGIGLQLYLTITVTIDPSIDTSSDPHHALLSYEGDGKVPFESNENLITQTALYVMRCNGIKDFPRGTHIHVNNPIPLGRGLGSSASAIVAGVYLGNEIGNLKLDKYRLLDYCLMIERHPDNIAAAMLGGFIGSYLNELSSEDSQLTTVPLDYILPKVKNGELITPQDKIVSQQPPNNIGQYVEYKWNKKIKCLTIIPNFELSTDLSRSVLPKNYQLPDIVYNLQRIAILTTALTQDPPNHKVIYQSMKDKLHQPYRFGLIPGLNTVLQKITPESYPGLCGICLSGAGPTILCLATDGFEKIANDVIEIFKQEGIECDSKLLDLAYDGATVEYGS	Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.	Q92209
P38623	RCK2_YEAST	CAM kinase-like protein kinase CLK1	Saccharomyces	MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWLNTFDCLPKEGESSQKKAGTSERRHPHKKQFQLFQRDSSLLFSPAAVAMRDAFDIGNAVKRTEEDRMGTRGGLGSLAEDEELEDSYSGAQGDEQLEQNMFQLTLDTSTILQRRKKVQENDVGPTIPISATIRE	Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.	P38623
Q5QYN5	IF3_IDILO	Translation initiation factor IF-3	Idiomarina	MKGGKRTQKAADKNRINEQITGVDEVRLIGTDGEQAGVVSINEALDAAAEAGVDLVEMSPNAEPPVCRLMDYGKFLFEKSKEQKEQKKKQKQIQVKEVKFRPGTDEGDYQVKLRNLRRFLEGGDKTKVTIRFRGREMAHQELGIELLNRVKNDLEEISIVESFPRRAEGRQMIMVLAPNKK	IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.	Q5QYN5
P50266	CYB5R_DROVI	Cytochrome b5-related protein	Drosophila	MVIETWKKSGIATKFPTYRNSAPVTVHSWQKGKRQDVEAEGLWRIKDGIYDFTEFIDKHPGGTFWIRETKGTDITEAFEAHHLTTAPEKMIAKYKVRDAYQRIYTLTLHEDGFYKTLKERVREKLKTIDKRPKRKSDVSDDL	May play a role in muscle cell metabolism.	P50266
Q8FB81	THIG_ECOL6	Thiazole synthase	Escherichia	MLHIADKTFDSHLFTGTGKFASSQLMVESIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIFAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGANAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQAGPGSRSHFAHATSPLTEFLEASA	Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.	Q8FB81
Q8L612	MACP1_ARATH	MACPF domain-containing protein At1g14780	Arabidopsis	MSRDGGDVIETAVKSLGKGFDLTADFRLKYCKDGDGSAGDDRLVVLDQTQNRELHIPGFGVFQNVSADINCDKGERTRFRSDILDFNKMSEYFNQRSSVTGKIPSGNFNATFGFQSGSWATDAANVKSLGLDASVVTLFNLHIHNPNRLRLTDRVRNAVPSSWDPQLLARFIERYGTHVITGVSVGGQDVVVVRQDKSSDLDNDLLRHHLYDLGDQLFTGSCLLSTRRLNKAYHHSHSQPKFPEAFNVFDDKQTVAFNNFSINSQNGITVICAKRGGDGRAKSHSEWLITVPDKPDAINFNFIPITSLLKDVPGSGLLSHAMSLYLRYKPPLMDLQYFLDFSGPRAWAPVHNDLPFGAAPNMASAYPALHINFMGPKLYVNTTPVTSEKNPVTGMRFFLEGKKCNRLAIHLQHLDNTRTTVGEKITDEHIWRGSDQITDNDRYFEPLNGKKFSHVCTVPVKYDPNWIKTTSNHKSQNDVAFIVTGAQLEVKKHGSKSVLHLRLRYTKVSDHYVVQNSWVHGPIGTSQKSGIFSSMSMPLTSGSVHHNMIQKDKNEVVLDSGVFPGGPPVPANNKIVKFVDLSQLCRGPQHSPGHWLVTGVRLYLDKGKLCLHVKFALLHRQRLLVSS	Negatively controls the salicylic acid (SA)-mediated pathway of programmed cell death in plant immunity.	Q8L612
P25576	POF1_YEAST	Promoter of filamentation protein 1	Saccharomyces	MKKTFEQFRKSNLLFQVLKGPQHLECQKLFVLDSSFNPPHLAHFQLLSQTIKNFKLKDTRSHVLLLLAVNNADKLPKPASFPTRLEMMCLFADYLQEKLPQSVVSVGLTVFSKFIDKDKILHEQFVKGCSADIGYLVGFDTIARIFDEKYYHPLKISDVMESFMSGSQLYCLARGDCHLSAESQLRYASDILEGKFEPVIPREWGARIHVMQNDYPALRNVSSSEIRNKLKNGQVESLKDELPLCIYDYLINNKTIFD	Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Involved in the salvage pathway for NAD(+) biosynthesis via NMN . Involved in the filamentation pathway. Suppresses the filamentation defect of a KSS1 deletion .	P25576
Q18BC9	RNH2_CLOD6	Ribonuclease HII	Clostridioides	MQDKSVREIKEIIETLEVEKYMEYIELLRVDERKSVQGLAIKLAKKLDNIRKEEERLETINIFENEGYDKGYLYIGGIDEAGRGPLAGPVVASVVVFKKDTKIEGVNDSKKLSEAKRDELFEVIKEEALDYGIGIVNNEEIDEFNILNATYMAMKKAINCLKKAPDYLLVDAATIPGIDISQNPIVKGDSKSISIAAASILAKVTRDSIMYQYDRVYPEYGFKSHKGYGTKEHYEAIEKYGITPIHRKSFLKNIL	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.	Q18BC9
Q972C1	GCSPA_SULTO	Glycine dehydrogenase (aminomethyl-transferring) subunit 1	Sulfurisphaera	MDMHPWLPNIKYIEEMLKSIGVNSIDDLFIDVPEEIKLKKELDLDYKKPLSEYEIILKLQELQNKNKRLKMPPFLGGGLCPHYVPEVVKFIIKRSEFYTAYTPYQPEISQGLLQALFEYQSLIAELFEMEVVNASLYDWGSALAEAIMMANRINKKKTVLVPKLMNPYHKEVVKTWTYGKGIKLVEIPPNERGTIDVSKLESMINEDDVSAIYIQQPNFYGIFEDEIEYIVDIAKKKKIITIMGVSPLALGLIKPPGEYEIDITVGDGQELGLSLNFGGPLLGILATRWDGQLVRQMPGRIVGLTKDSEGKRGFTLILQTREQFARREKATSNITTNEALMAIAAAVYLSLLGRNGIKELAKEIYIRSHYAKKRLEELGVNTVYNGDFFEEFAVDFRTDYDIIHSRLLEKNIHGGLKLGKTQALFCVTEVHTKSMIDELIESIREVFSG	The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.	Q972C1
Q4QLG0	MURD_HAEI8	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase	Haemophilus	MNAYQNKNITIIGLGKTGLSCVDYLLSQQANIRVIDTRKKPTGIDKLPQNIPLHTGSLNQEWLLESDMIVISPGLAVKTPEIQTALKAGVEVIGDIELFCRAATKPIVGITGSNGKSTVTTLVYEMAKAAGVKVGMGGNIGIPALSLLNEDCELYVLELSSFQLETTYSLKAAAATVLNVTEDHMDRYMDLEDYRQAKLRIYHNAEVGVLNNEDKLTFGEGENQARQTVSFAENSADYWLKTENGKQYLMVKDEVILPCEEVTLVGRHNYMNILAATALAQAVGINLDSIRTALRHFKGLDHRFQLVHQANGIRWINDSKATNVGSTVAALAGLYIEGKLHLLLGGDGKGADFSELAELINQPHIICYCFGRDGVQLAKFSSQSYLFETMEQAIEFLRPTLQSGDMVLLSPACASLDQFASFEKRGEEFTHLAQYSA	Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).	Q4QLG0
Q3AVC2	ILVC_SYNS9	Ketol-acid reductoisomerase type I	unclassified Synechococcus	MAQLFYDSDADLGLLNGKTVAIIGYGSQGHAHALNLKDSGVNVVVGLYEGSRSAEKAKADGLEVLTVAEASAKADWIMVLLPDEFQKDVYEKEIAPHLKSGKVLSFAHGFNIRFELIKPPADVDVVMIAPKGPGHTVRWEYQNGQGVPALFAIEQDASGNARGLTMAYAKGIGGTRAGILETNFKEETETDLFGEQAVLCGGLSELVKAGFETLVEAGYQPELAYFECMHEVKLIVDLMVKGGLTSMRDSISNTAEYGDYVSGPRLITADTKAEMKRVLADIQDGTFARNFVAECDAGKPEMKKIRDRDAQHPIEKVGKGLRSMFSWLKDA	Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.	Q3AVC2
Q3AJS6	HISZ_SYNSC	ATP phosphoribosyltransferase regulatory subunit	unclassified Synechococcus	MALQPAAGAKDLNPRQVETNRQLTERLASVYRLWGYDEVSPPRVERLATLMAGGAIDSSDIVRLVADDPLGLRPEMTASIARAACTRFADRQRPLRLWASGTVFRTRSADEGGQCIEENLQSGVELFGVSGSEAEMELLSLLMASVQTLGLQTSQKPRLLLGHTALMDLVLRPFNGAVRDQIRTALIDFDRLAIESFDLAYAEKTRLLSLMDCRGTPDQVLAQLSSLYGEQPVFDELRRLCTHLASAAQAQAVTIQLDPTFQPHFELYTGLVFQLVCDGRSSPVVFARGGRYDDLVRRCGATDDRAFGAGFSLAIDPIRELISDLDAAEQQQSDVLIAFSTASNLESAMERQRSWHEQGRTAVMALEPLSSMQEAELQAKAQGGLQLDWVDP	Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.	Q3AJS6
Q9D0C1	RN115_MOUSE	Zinc finger protein 364	Mus	MAEASAAGADAGSAVAAHRFFCHFCKGEVNPKLPEYICPRCDSGFIEEVTDDSSFLGGGGSRTDNSTATHFAELWDHLDHTMFLQDFRPFLSSNPLDQDNRANERGHQTHTDFWGPSRPPRLPMTRRYRSRGSTRPDRSPAIEGIIQQIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVNTGLECPVCKEDYTVEEKVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQTQSSEASASNRFSNDSQLHDRWTF	E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.	Q9D0C1
Q51520	PHZF_PSECL	Phenazine/pyocyanine biosynthesis protein PhzF	Pseudomonas	MHHYVIIDAFASAPLEGNPVTVFFDADDLSATQMQRIAREMNLSETTFVLKPRNCGDALIRIFTPVNELPFAGHPLLGTAIALGAHTDNHRLFLETQMGTIAFELERQNGSVVAASMDQPIPTWTALGRDVELLKALGISDSTFPIEIYHNGPRHVFVGLPSIAALSALHPDHRALSSFHDMAINCFAGAGRRWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHGQIEFGQQIEILQGVEIGRPSLMFARAEGRADQLTRVEVSGNGVTFGRGTIVL	Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.	Q51520
C0MFD9	XERS_STRS7	Tyrosine recombinase XerS	Streptococcus	MKRDLLLTKIEEYKNIMPWYVLDYYQSKLSVPYSFTTLYEYLKEYKRFFEWLIDSDLSKAARIADVDLTTLEHLSKKDMEAFILYLRERPSLNTYSTKKGVSQTTINRTLSALSSLYKYLTEEVENEHGEPYFYRNVMKKVATKKKRETLAARAENIKQKLFLGDETMAFLDYVDKEYEHKLSNRAKASFRKNKERDLAIIALLLASGIRLSEAVNLDLKDVNLNMMLVEVTRKGGKRDSVNVAAFAKPHLEAYLSVRKDRYQAEKQDVAFFLTAYRGLPNRIDASSIEKMVGKYSESFKIRVTPHKLRHTLATRLYDTTKSQVLVSHQLGHASTQVTDLYTHIVNDEQKNALDKL	Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division.	C0MFD9
Q57QP2	CBPA_SALCH	Curved DNA-binding protein	Salmonella	MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPNAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQQHEGQPYNAEDFDDIFSSIFGQHGRHSHHRHAARGHDIEIEVAVFLEETLEEHQRTISYSVPVYNAFGLVEREIPKTLNVKIPAGVSNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVNQDLEVVLPLAPWEAALGAKVSVPTLKERILLTIPPGSQAGQRLRIKGKGLASKKHTGDLYAIIKIVMPPKPDEKTAALWQQLADAQSSFDPRQQWGKA	DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.	Q57QP2
C5B704	UBIA_EDWI9	4-HB polyprenyltransferase	Edwardsiella	MEGCVAQSKWLAYCRLMRIDKPIGSLLLLWPTYWALWLAGGTAPGGKLLLVFTCGVFFMRAAGCVINDFADRHFDGHVKRTCQRPLPCGALSEREAKALFVLLVGLSFALVLTLNAMTIWLSVAALTLAWLYPFIKRFSHLPQVILGMAFGWSIPMAYAAVGESLPLSCWLLFAANICWTVAYDTQYAMVDRDDDLRIGIKSTAILFGRYDRLVIGLLQLATLLLLLWVGDLNQLQGAYYWGVLLAAVLFVYQQQLITRRARTSCFRAFMNNNYVGLILFLGILLAL	Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.	C5B704
Q96FG2	ELMD3_HUMAN	RNA-binding protein 29	Homo	MNEKSCSFHSKEELRDGQGERLSAGYSPSYDKDKSVLAFRGIPISELKNHGILQALTTEAYEWEPRVVSTEVVRAQEEWEAVDTIQPETGSQASSEQPGQLISFSEALQHFQTVDLSPFKKRIQPTIRRTGLAALRHYLFGPPKLHQRLREERDLVLTIAQCGLDSQDPVHGRVLQTIYKKLTGSKFDCALHGNHWEDLGFQGANPATDLRGAGFLALLHLLYLVMDSKTLPMAQEIFRLSRHHIQQFPFCLMSVNITHIAIQALREECLSRECNRQQKVIPVVNSFYAATFLHLAHVWRTQRKTISDSGFVLKELEVLAKKSPRRLLKTLELYLARVSKGQASLLGAQKCYGPEAPPFKDLTFTGESDLQSHSSEGVWLI	Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity.	Q96FG2
Q9KQH1	NTPPB_VIBCH	7-methyl-GTP pyrophosphatase	Vibrio	MQNYQLVLASTSPFRQQILAKLKLPFVTAKPDCDETPLIGETPEHLLMRLAENKARSCFLADPSLVIGSDQVCVIDDQIIGKPLTTEKAVEQLLRQSGQAITFYTGLALFNNQTQQTQVLCDTFTVHFRTLSESMARRYVEAEQPLHCAGSFKSEGLGIALFERLEGDDPNSLIGLPLIKLIQLLENEGLNVI	Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.	Q9KQH1
Q2J843	METK2_FRACC	Methionine adenosyltransferase 2	Frankia	MATRLFTSESVTEGHPDKIADQISDSILDAMIKDDPKSRVAVETLITTGQVHVAGEVTTKTYVDIASVVRERILEIGYDSSKKGFDGASCGVSVSIGAQSPDIAQGVDTAHETRVEGSADDEFDRQGAGDQGLMFGFACDETPELMPLPIALAHRLARRLSAVRKEGQIGYLRPDGKTQVTIEYVDGKPARLDTVVVSSQHAADIDLDTLLAPDIAEYVVEPELALLEIATEGRRLLVNPTGRFEIGGPMGDAGLTGRKIIVDTYGGYARHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLASRCEVQVAYAIGKAQPVGLFVETFGTGTVPDIQIQDAVTSVFDLRPAAIIRDLDLLRPVYAQTAAYGHFGRPELDFTWESTARAEALQRAVKG	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.	Q2J843
B0BTN9	RISB_ACTPJ	6,7-dimethyl-8-ribityllumazine synthase	Actinobacillus	MAKITGNLVATGLKFGIVTARFNDFINDKLLSGAIDTLVRHGADENNIDTAWVPGAFEIPLVAKKMATSGKYDAVICLGTVIRGSTTHYDYVCNEAAKGIGAVALETGVPVIFGVLTTENIEQAIERAGTKAGNKGSECALGAIEIVNVLKAI	Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.	B0BTN9
B0REV4	METK_CLAMS	Methionine adenosyltransferase	Clavibacter	MTDLRLFTSESVTEGHPDKICDQISDSILDALLTQDPSSRAAVETLVTTGLVHVAGEVTTSGYVDIPQIVRDRIRDIGYDSSEVGFDGSNCGVTVSIGAQSPDIAQGVDRSYESRSGSASTDAHDLQGAGDQGLMFGYASRDTPVFMPLPIYLAHRLAERLAAVRHSGELSYLRPDGKTQVTIGYEGLVPRTVDTVVLSTQHGPQVSQEDLRREVEEHVIRPVLAAAAEIGIELDSRDATLLINPTGKFEIGGPKGDAGLTGRKIIVDTYGGFSRHGGGAFSGKDPSKVDRSAAYAMRWVAKNAVAAGLADRLEVQVAYAIGKAAPVGLYVEAFGTAHVPEDRIVRAIRETFDLRPAAIVERLDLLRPIYAETAAYGHFGRELPDFTWEALDRVADLQSAAGL	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.	B0REV4
Q5LMK7	DAPA_RUEPO	4-hydroxy-tetrahydrodipicolinate synthase	Ruegeria	MFKGSMPALVTPFRNGELDLEALKRLVEWQIGEGSTGLVPVGTTGESPTLSHEEHETVVAEVVKAAAGRVPVIAGAGSNNTTEAIRFVQFAQRIGADAALVVTPYYNRPTQRGLIAHFTALHDCAEIPIVIYNIPGRSVVDMTPATMGALAKLPRIVGVKDATGDLARVSQQRASCGADFIQLSGEDATALGFNAHGGVGCISVTANVAPRLCAEFQQATLAGDYAKALDYQDRLMPLHEAIFIEPGLVGAKYALSKLGLCSEEVRSPLTGLEDSTKAAIDAAMKHAGLL	Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).	Q5LMK7
B5FEA5	PCP_ALIFM	Pyroglutamyl-peptidase I	Aliivibrio	MKKILITGFEPFGNDKINPALEAVKLIAGRKLNGGEIVICQVPVVRYKSIETVKQAIEEQQPYAVITVGQASGRAAITPERIAINVDDFRIPDNEGIQVIDEPVVAGGPDAYFTTLPIKAMVSEIQAQGIPATVSNTAGTFVCNHLFYGIQHYLKDTNVRHGFVHIPLLPEQSVDGSQPTMKLEQIAEGLAIAAQAIIDNDSDIQQGAGTIC	Removes 5-oxoproline from various penultimate amino acid residues except L-proline.	B5FEA5
A9NNH7	LIAS_PICSI	Lipoic acid synthase	Picea	MSINPAFLRRITWGSKSLHHQFTRCQVRALSSSVEQTPESTTPALSALRERLANGGPTLSDFLTRNLGEEPYSVDVGTKKNPLPKPKWMKAAVPGGDKYTAIKAKLREMNLHTVCEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPNEPTNVAEAIVSWGLDYVVLTSVDRDDLPDQGSGHFAKTVQKLKQLKPKMLVEALVPDFQGNSECVQKVATSGLDVFAHNIETVEELQRVVRDHRANFNQSLEVLKMAKTYSPLGVLTKTSVMLGCGETPAQVIETMEKVREAGVDVITFGQYMRPTKRHMAVSEYVTPEAFEKYQKLGMEMGFRYVASGPMVRSSYKAGEFYIKSMIEDDRKKASSSSI	Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	A9NNH7
A3QEP5	RUVC_SHELP	Holliday junction resolvase RuvC	Shewanella	MPIILGVDPGSRITGYGVIQCQGRQQIYLGSGCIRTQSDDLPSRLKVIFDGISEIIRQYQPDEFAIERVFLAKNADSALKLGQARGAAIVAATNAQLPVAEYSATQIKNAVVGTGRAQKSQVQHMVQQILKLPAAPQADAADALGVALCHFHTYQSLIAMGGKASVRTYGRYR	Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.	A3QEP5
B8H0A0	FTSI_CAUVN	Penicillin-binding protein 3	Caulobacter	MSLSNLGPGGVHSPLWRWVVERVWRLEHAFERSRAAARPEDDTRIRIFLVMGFFGFCFVGVSLGAGWSALFSRAGQGGGYAQGVEGARGDVVDRNGKLLAVDLAHYALYVDPREVWDAKETRAALGRALPQVPAKRLDKAVFGDHRAFVLGGLTPDEKDAIFNLGLPGVTFEEQERRMYPLGPTAAHLIGFVDSGGKGLAGAERALDDPIRKAAGGEGGPAQLSIDVRVQAALEDELRKAAEEFTPKGAVGLVTNVHTGEILGMASWPDYDANKAGGATDDQRLNRAAASVYEMGSTFKAFTVAIGLDTGVATAASTFDAREPYKLGYRTIHDYHATKAVLNLVEVFQHSSNIGTAMLAERVGGQRLSQYFTNLGLTKPAKVELQESARPLTPRKWDQDTVASTSFGHGMNISPLALAQAMNALLNGGEMRPLTIRKLPPGVRPEGRRVLSEHTSAEMLKIMRANVVPGEGGSGGKADVPGLSVGGKTGTGEKYDPAIRRYNHQRQVSSFAATFPTDGPLEADRYFVLILLDEPKGNANSFGFSTGGWVAAPAAGRVIERIAPFLGVKRKTELVTIANSPKNAAPEAGL	Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.	B8H0A0
A1R6G6	Y2084_PAEAT	Nucleotide-binding protein AAur_2084	Paenarthrobacter	MDEATAKSGTEQDGLTPVKPPEAELLVVTGMSGAGRSTASDALEDHGWYVVDNLPPQMLGTLAEIVSHAPKSIPKLAVVVDVRSKDLFTDIQTALGALSASGITFRVLFLDANDDVLVRRFEQGRRPHPLQGGGRILDGIGIEREVLRELREHADVVLDTSEFNVHGLATAITELFSDTGPVTLRLNVMSFGFKYGLPVDANFVADARFIPNPHWVPQLRPHTGLDEDVSDYVLGAEGVQEFVDRYVRALEPVLDGYRQENKHYATLAVGCTGGKHRSVAVAMELSKRLAQYPRVTVTTTHRDLGRE	Displays ATPase and GTPase activities.	A1R6G6
Q4KM33	PLEK_RAT	Pleckstrin	Rattus	MEPKRIREGYLVKKGSVFNTWKPMWVVLLEDGIEFYKKKSDNNPKGMIPLKGSTLTSPCQDFGKRMFVLKITTTKQQDHFFQAAYLEERDAWVRDIKKAIKCIEGGQKFARKSTRRSIRLPETIDLGALYLSMKDPEKGIKELNLEKDKKVFNHCFTGSGVIDWLVSNKLVRNRQEGLMISASLLSEGYLQPASDLSKNAADGIAENPFLDNPDAFYYFPDSGFFCEENSSDDDIILKEEFRGIIIKQGCLLKQGHRRKNWKVRKFILREDPAYLHYYDPAGGEDPLGAIHLRGCVVTSVESNPDGKKSDEENLFEIITADEVHYYMQAATAKERTEWIKAIQVASRTGK	Major protein kinase C substrate of platelets.	Q4KM33
Q5ACK7	DRS1_CANAL	ATP-dependent RNA helicase DRS1	Candida	MPDFILTIDSDEEVDVSDSEQLQDINPDFKFQIDGETTNTLEEFDFQENKVKEVDLDEIIKKKGGLKEESDDEELALDGFGMGASKQEEEEEEEEEEVEVPEVKEVVEPEDSAEAIADFYEESSPQQTHTSFQTLQLSRPVLKGIAELKFTKPTPIQSASIPIALLGKDIVAGAQTGSGKTGAYMIPIIERLLYKPSTSTKVIILTPTRELALQVYEFGKKLSHHVNNLNIGLAVGGLNLRQQEEQLKTRPDIVIATPGRLIDHIRNSPSFSVQDIQVLVIDEADRMLEEGFQDELTEILSLIPKHKRQTLLFSATMNTRIQDLIQLSLQKPVRIMIDPPKSVASKLLQQFVRIRKRDQLKPALLYQLLKGVSSRVVVFVARKETAHRLRIVLGLLGLKVSELHGALTQEQRLQNVKNFKSLEVPVLICTDLAARGLDIPKIELVINYDMPKTFEIYLHRVGRTARAGRDGTSITFVGESSQERAIVKSAIVNGKGVAKTVDWKQAEETNKLLESKESVIDEVLEEEKEAKELLRAEMELTKASNLIKHEQEIHSRPKRTWFKGEVMEQLTKHGKKVNSKKRKANEVRKDEGRSYKKTKTDRMKISNKKKSKK	ATP-binding RNA helicase involved in ribosome assembly.	Q5ACK7
Q8ZTY5	IF2A_PYRAE	eIF-2-alpha	Pyrobaculum	MRLVKKEFPDVGELVIGTVKKIAEHGAYVYLDEYDLEAFAPTQEIVQSWFHSIRDYVKEGNKTVFKVISVNPKMRVVEVSLKRVRVDEKEKKLLLYRHRVRVLKLLEIAMKKLNRPAEEALKVMWYLEEQFGDPFKVFEEVVKTGPHVLDDLQLDAKLKEIIIELARQQVELPPTKISGIIKIVSVEGDGVEKIKAALIELEKTLREKFPQISTKIYVVGPPRYRIDLTGQQPKQVEAAFSEAANILQALQKKYKVIGNIQRIEQ	eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.	Q8ZTY5
Q9Y0B7	PP4C_DICDI	Serine/threonine-protein phosphatase 4 catalytic subunit	Dictyostelium	MSSDLDRQIEQLKRCEIIKESEVRALCSKAREILLEEGNVQRVDSPVTICGDIHGQFYDLKELFKVGGDCPQTNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYEECVRKYGSVTVWKYCTEIFDYLSLSALVDGKIFCVHGGLSPSINTLDQIRAIDRKQEVPHEGPMCDLMWSDPEDIPGWNGSPRGAGFLFGEDVVQKFNHDNNLEFICRAHQLVMEGFKYMFNETLVTVWSAPNYCYRCGNVAAILQLDENLKKNFAIFEAAPQESRGAPAKKPAPEYFL	Required for development, chemotaxis and the expression of numerous genes.	Q9Y0B7
A2XSX6	TIF9_ORYSI	Protein TIFY 9	Oryza sativa	MSTRAPVELDFLGLRAAAADADDRHAKSGGSSASSSSSIRGMETSAIARIGPHLLRRVIAAARPPPPPSTAPVPEEMPGAAAAAAPMTLFYNGSVAVFDVSHDKAEAIMRMATEATKAKGLARGNAIVGNFAKEPLTRTKSLQRFLSKRKERLTSLGPYQVGGPAAVGATTSTTTKSFLAKEEEHTAS	Repressor of jasmonate responses.	A2XSX6
Q5F8N2	DPO4_NEIG1	DNA polymerase IV	Neisseria	MSLRKIIHIDMDAFYASVELREQPHLKGRPVVVAWEGARSVICAASYEARQFGLHSAMSVATVKRLCPQAVYVPPHFDLYRQVSAQIHAVFRRYTDLIEPLSLDEAYLDVTRNFKNIPYAGEVAKEIRAAIFAETGLTASAGIAPNKFLAKIASDWRKPNGQFVLPPHKVMAFLETLPLGKIPGAGKVTLKKMQSLGMRTAGDLRRFERGELLNHFGRYGYRLYDLARGTDEHPVKAERERLQISTEITLPEDLPLGQAAGHLPHLAEDLWRQITRKNVEAQSVTLKLKTYDFRIITRTLTYSSVLPDCAALLQAAQMLMARVPPQTEDAFRLIGIGVGRLVPKNQQQDLWA	Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	Q5F8N2
Q31N85	PLSX_SYNE7	Phosphate-acyl-ACP acyltransferase	Synechococcus	MTRARIAVDAMGGDFAPEEIVKGALRAQEELQADVILVGDPDRLRAICQDHAPHLQVRIEAAEEAIAMEDAAVSVRSRPRASINVAMDLVKAGEADAVISAGHSGAVMASALLRLGRIRGIDRPAIGALLPTVIPGKPVLVLDVGANVDCKPRFLEQFAVMGSIYSRDVLGQANPRVGLVNIGEEDSKGNELALASHQLLRNNPRICFVGNAEGRDVLSGQFDVVVCDGFVGNVLLKFAEAVGSVFLEIIRDELPRGMRGKVGSTLLRRNLRRIKQRLDHAEHGGALLLGVNGICIISHGSSKAPSIYSAIRLAVEAAENRVIDHLHQIQEPPSPAADLVTEPVVS	Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.	Q31N85
Q0BYA1	RL1_HYPNA	50S ribosomal protein L1	Hyphomonas	MATKGKRARAIEQTVDKTKAYSVSEAVKLVKSNAKAKFDESIEIAINLGVDPKYADQQVRSVVNLPAGTGKTIRVAVFAKDKKAEEALAAGADIVGADDLFEKVNGGFMDFDRVIATPDMMGLVGRLGKVLGPRGLMPNPKVGTVTPNVAQAVKDAKGGAVEFKVEKAGIVHAGVGKASFSDADIEKNVQAFISAVVKARPSGAKGTFVRKVTLSSTMGTGVAIDLAEAKS	Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.	Q0BYA1
O94886	CSCL1_HUMAN	Transmembrane protein 63A	Homo	MMDSPFLELWQSKAVSIREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSESRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKEKKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVLGCEWEDAISYYTRMKDRLLERITEEERHVQDQPLGMAFVTFQEKSMATYILKDFNACKCQSLQCKGEPQPSSHSRELYTSKWTVTFAADPEDICWKNLSIQGLRWWLQWLGINFTLFLGLFFLTTPSIILSTMDKFNVTKPIHALNNPIISQFFPTLLLWSFSALLPSIVYYSTLLESHWTKSGENQIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFQYEFGAMYAWMLCVFTVIVAYSITCPIIAPFGLIYILLKHMVDRHNLYFVYLPAKLEKGIHFAAVNQALAAPILCLFWLYFFSFLRLGMKAPATLFTFLVLLLTILVCLAHTCFGCFKHLSPLNYKTEEPASDKGSEAEAHMPPPFTPYVPRILNGLASERTALSPQQQQQQTYGAIHNISGTIPGQCLAQSATGSVAAAPQEA	Acts as an osmosensitive calcium-permeable cation channel . Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion .	O94886
B6J1Y7	RNH_COXB2	Ribonuclease H	Coxiella	MAKQEQNIVYLYCDGACRGNPGPGGWGVLLRYNQHERQLHGGVANTTNNQMELTAAIEGLKSLKKPCQVVVTTDSQYLRRGITEWLPVWKRRGWRTSNKKPVKNQPLWETLEREVERHTIVWHWVKGHSGHAENEIADELANRGIDEVLKRGAQ	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.	B6J1Y7
Q6GBS6	SDRC_STAAS	Serine-aspartate repeat-containing protein C	Staphylococcus	MNNKKTVTNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSENKTTEKVDSRQLKDNTQTATADQPKVTMSDSATVKETSSNMQSPQNATASQSTTQTSNVTTNDKSSTTYSNETDKSNLTQAKDVSATPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHLNKDTGKTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTTTYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEVSLGNDTYSEEIIVDYGNKKAQPLISSTNYINNEDLSRNMTAYVNQPKNTYTKQTFVTNLTGYKFNPNAKNFKIYEVTDQNQFVDSFTPDTSKLKDVTNQFNITYSNDNKTATVDLMNGQTSSNKQYIIQQVAYPDNTSTDNGKIDYTLDTDKTKYSWSNSYSNVNGSSTANGDQKKYNLGDYVWEDTNKDGKQDANEKGIKGVYVILKDSNGKELDRTTTDENGKYQFTGLSNGTYSVEFSTPAGYTPTTANAGTDDAVDSDGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKGVKVTLQNEKGEVIGTTETDENGKYRFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDTDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDADSDTDSDSDAGKHTPAKPMSTVKDQHKTAKALPETGSENNNSNNGTLFGGLFAALGSLLLFGRRKKQNK	Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion.	Q6GBS6
B6I7J7	ARNC_ECOSE	Undecaprenyl-phosphate Ara4FN transferase	Escherichia	MFEIHPVKKVSVVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSIIAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKENE	Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.	B6I7J7
Q9ZKB1	6PGL_HELPJ	6-phosphogluconolactonase	Helicobacter	MGYQLFEFENLEDCHKALIERFKEFFNAALKKHHQVSVAFSGGRSPISLLQKLSVLDLKWHECLISLVDERIIEASHEDSNAKLLHDYLLQNNALKASFTPLLPEKISGDTNELLDFANQHFKQPHLAILGMGTDGHTASLFPETSAFLNEEKENIVLTKPTNAPYERLSMSINALENCEKLFLSISGVEKRGVLEKALKENAPYSLPIARILHSKKVTTEVFYAKN	Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.	Q9ZKB1
Q8P243	PCP_STRP8	Pyroglutamyl-peptidase I	Streptococcus	MKILITGFDPFGGEAINPALEAIKKLPATIHGAEIKCIEVPTVFQKSADVLQQHIESFQPDAVLCIGQAGGRTGLTPERVAINQDDARIPDNEGNQPIDTPIRADGKAAYFSTLPIKAMVAAIHQAGLPASVSNTAGTFVCNHLMYQALYLVDKYCPNAKAGFMHIPFMMEQVVDKPNTAAMNLDDITRGIEAAIFAIVDFKDRSDLKRVGGATH	Removes 5-oxoproline from various penultimate amino acid residues except L-proline.	Q8P243
P60209	KAX94_HOTTA	BTK-2	Mesobuthus	VGCAECPMHCKGKMAKPTCENEVCKCNIGKKD	Blocker of human voltage-gated potassium channel Kv1.1/KCNA1 .	P60209
C6L862	AHLL_MICTS	N-acyl homoserine lactonase	Microbacterium	MILAHDVSGSGPLLVLLHGITEDRRSWDPVDFTDGFTVVRVDLRGHGASAAEEPYDIPTLATDVHDTLAQLAENDVIPGELPVIVGHSMGGIVATAYGALFPARAIVNVDQPLQLAGMQGQVQQAEGMLRGADFPLFIHGMFAQMAGGLDAEELARVNGIRSPRQDVVLGMWRPLLEDSPEELAALVSGLTRIPEDVPYLVITGLDAGPEYAAWLQREIPQAVQEVWQPPTHYPHLVDPARFVERVEAFVR	Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3. Has slight activity towards L-homoserine lactone, and no activity towards gamma-butyrolactone.	C6L862
Q6YPI8	ACP_ONYPE	Acyl carrier protein	Candidatus Phytoplasma asteris	MVFEKIKALIATQLSLDASTITLDTRFKEDLGLDSLDALELVMEVEKTFQINISDATLQNFKTVQDIVFYITKNTP	Carrier of the growing fatty acid chain in fatty acid biosynthesis.	Q6YPI8
Q07532	IWR1_YEAST	Interacting with RNA polymerase II protein 1	Saccharomyces	MSTISTTTAPEFIRVKRRRDEDSVQALLIDEGKRVKKQKFIFKLSKTVSSESYQSEQESSTPLLKLAHEDHRHFVLEQRKKSRRDSDDEKSQQRLAAEGSTVDDDGLPPEINQMVNDYLKLNKGVEKTERKKPSRKYFTGDSAKIASLPSLDYVFDIYHLEKIHDDEVARYNNEKNIGFVKIIEHIDLALDEESDPNEARSDDEDSNDENYYQNDYPEDEDDDRSILFGSEGEDIAALGEEIVIGVNKSRFSSWNDDKIQGSNGYHDVEEEYGDLFNRLGGKSDVLKSINSSNFIDLDGQEGEIEISDNEDDSDEGDDIEYPRNEFFPTDVDDPLAHHRDRIFHQLQKKINRS	Directs RNA polymerase II nuclear import. Binds RNA polymerase II in the active center cleft between the two largest subunits in the cytoplasm. Then uses an N-terminal bipartite nuclear localization signal that may be recognized by karyopherin alpha to direct the polymerase II complex nuclear import. In the nucleus, is displaced from polymerase II complex by transcription initiation factors and nucleic acids, enabling its export and recycling.	Q07532
P56833	MRAY_STRCO	UDP-MurNAc-pentapeptide phosphotransferase	Streptomyces albidoflavus group	MKQILFAGVIGLFLTLVGTPLLIKLLARKGYGQYIRDDGPREHASKRGTPTMGGIAFILATVAAYFLAKGITSYLDPDIDAGPTFSGLLVLGLMVGMGLVGFLDDYIKIVKRRSLGLRARAKMIGQLTVGIAFAVLSLQFADNRGNTPASTKLSFITDFGWTIGPVLFVVWALFMILAMSNGVNLTDGLDGLATGASVLVFGAYTFIGVWQFQESCANALTLTNPGACYEVRDPLDLAVVASALMGSCLGFLWWNTSPAKIFMGDTGSLALGGVLAGLAICSRTELLMAILGGLFVLITMSVVIQVGSFRLTGKRVFRMAPLQHHFELKGWSEVLVVVRFWIIQGICVIVGLGLFYAGWATDK	Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.	P56833
A0A0R4I987	CDII_YERPY	Immunity protein CdiI-YPIII	Yersinia	MNDIVKSAWASVKMNTDFICVDTYSGYRSNQLDPLGVQHLSSPDVSDLDLGEMVKDALSHSRFVLPAPRTDIWIHPEVTFDLDLYDSRRTVERYDEWVKKLMVHYGYKTKRALFKDMKSCDICCNHDAITISPTRHEKLEVWGGTGLKGSDNVILSVDSSPTEIGAGLRLALSRCKG	Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Neutralizes the toxic activity of cognate toxin CdiA-YPIII (residues 954-1077). Does not inhibit toxic activity of CdiA from other toxin-immunity modules.	A0A0R4I987
O55208	FIGLA_MOUSE	Transcription factor FIGa	Mus	MDTAPASPEPFLVTPQAEVLEELIQAQMGPLPRLAAICRLKRLPSGGYSTTDDLHLVLERRRVANAKERERIKNLNRGFAKLKALVPFLPQSRKPSKVDILKGATEYIQILGCVLEEAKVSEKQSPEEQTHSGRPSDPHVSSTRELLGNATQPTSCASGLKKEEEGPWAYAGHSEPLYSYHQSTVPETRSYFTH	Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters.	O55208
Q6AAU3	GLYA_CUTAK	Serine hydroxymethyltransferase	Cutibacterium	MSDPRAVDPTARDIAEKLAPAYRTMLDAIAQVEPRIAEATRAELTDQRHSLKLIASENYASLPVLATMGTWFSDKYAEGTAGHRFYAGCQNVDTVETIAAEHACALFGAEHAYVQPHSGIDANLTAYWTILAHHIETPALSEFGARTVNDLTQVDWDTLRHRFNDQRAIGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPQTGLLDYDKVAELAREFKPLVIVAGYSAYPRRVNFAKMREIADEVGAVLMVDMAHFAGLVAGKVFTGDENPIPHAQVVTTTTHKSLRGPRGGMVLTTKDYADDVDRGCPMVLGGPLSHVMAAKAVALAEARTQTFRDYAQRVANNAKALAEGLMKRGVKLVTDGTDNHINLLDVTTSFGLTGRQAEAALLDAGVVTNRNSIPTDPNGAWYTSGIRIGTPALTSRGFGPDEFDQVAELIVTTLEATTPMTASTGKPGKAKYQIADGVAQKVHDAADELLGNFPLYPGLDLA	Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.	Q6AAU3
Q0HEW2	MDH_SHESM	Malate dehydrogenase	Shewanella	MKVAVLGAAGGIGQALALLLKTQLPAGSQLSLYDIAPVTPGVAVDLSHIPTAVEIKGFAGEDPTPALVGADVVLISAGVARKPGMDRSDLFNINAGIVRNLIEKVAVTCPKALVGIITNPVNTTVAIAAEVLKKAGVYDKNRLFGVTTLDVIRSETFIAELKGLNVADVKVNVIGGHSGVTILPLLSQVEGVTFSDEEVASLTKRIQNAGTEVVEAKAGGGSATLSMGQAACRFGMSLVRGLQGEANIVECAYVDGGSEHAEFFAQPVLLGKNGIEKVLPYGEVSAFEANARDSMLDTLKGDIKLGVDFVK	Catalyzes the reversible oxidation of malate to oxaloacetate.	Q0HEW2
C6DGY3	CLSA_PECCP	Cardiolipin synthase A	Pectobacterium	MSTFYTVISWLLVFGYWLLIAGVTLRILMKRRAVPSAMAWLLVIYILPLVGIVAYLSFGELHLGKRRAERASKMWPSTAKWLRELKEYRRIFATENSEVASALFQLCERRQGVGGVKGNQLQLMTTFDDTIKALLRDIELARSNIEMVFYIWQPGGLVEQVSSSLIAAARRGVHCRILLDSAGSVQFFRQHHPELMRTAGIEVVEALKVNLFRAFLRRMDLRQHRKIILIDNRIAYTGSMNMVDPRFFKQDAGVGQWIDLMARIEGPVATTLGIIYCCDWEMETGKRLLPPPPDVNVMPFEQESGHTIQVIASGPGYPEEMIHQALLTSVYSARKQLIMTTPYFVPSDDLLHAICTAAQRGVDVSIIVPHKNDSVLVGWASRAFFTELLAAGVKIYQFKDGLLHTKSVLVDGQLSLVGTVNLDMRSLWLNFEITLVIDDAGFGSDLACVQEDYIARSRLLNATQWQNRPYWQRIVERLFYFFSPLL	Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.	C6DGY3
B2A4D5	RS7_NATTJ	30S ribosomal protein S7	Natranaerobius	MSRKGPAPKRDVNPDPIYNSKMVTKFINKLMLDGKKGLSQRIFYKALELVGERTNEEPLEVFETAVKNVMPVLEVKARRVGGATYQVPVEVEPNRKQVLAIRWIVNYARERGERAMSERLAGELIDAYNNTGGAIKKKEDTHKMAEANKAFAHYRW	One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.	B2A4D5
A0PJR5	ECHD3_DANRE	Enoyl-CoA hydratase domain-containing protein 3, mitochondrial	Danio	MLLRGFSELLKCRGVMMKMRMKMSGDSSSLTLTEQQGGIRRIILNNPRKRNALSLQMLESLRENILTDADNPELHVIIISAVGPVFSSGHDLQELSSAEGSDLPRRVFHSCSELMMLIQDLPVPVIAMVNGVATAAGCQLVASCDVAVASEKSTFATPGVNVGLFCSTPAVAIGRTVPRKIAMQMLLTGRPLSAQQALQHGLLSAVFSEERLEDETLAIARRVCESSRPVVSLGKQIFNTQMSQSRDAAYSTAGAAMLDNLRLRDGQEGIRAFLEKRKPVWSNTDDCIH	May play a role in fatty acid biosynthesis and insulin sensitivity.	A0PJR5
A7N2Q0	BETB_VIBC1	Betaine aldehyde dehydrogenase	Vibrio	MDMKAHYIDGAMHLGCSEEHFTTYNPANGEPLANVKQANQQDMQAAIESAKRGFAIWSAMTATERSRILLKAVALLRERNDELAALEVADTGKPIQEANCVDIATGADVIEYYAGLAPSMHGEQQPLNESQFFYTRREPLGICAGIGAWNYPIQIAMWKSAPALAAGNAMIFKPSEETPLTALKLAEIYSEAGLPDGVFNVIQGDYRVGQMLTAHPDIAKVSFTGESGTGKVVMGDSAATLKQVTMELGGKSPMIIFDDAKLDDAVSAAMVANFYTQGEVCTHGTRVFVHEGIYDEFVVQLKKRTELLVVGDPLDEQTQIGALISKEHESKVLSAIEQAKASKATLLTGGYKVTENGLASGNFVVPTVFIDCEDDMPHVQQEIFGPVMSVLKFSDEDEVIARANNTDYGLAAGVFTQNLSRAHRVIHQIQAGICWINTWGDSPAEMPVGGYKLSGIGRENGVETLTHYTQTKSVLVHLGDFDSPYA	Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.	A7N2Q0
P08228	SODC_MOUSE	Superoxide dismutase [Cu-Zn]	Mus	MAMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.	P08228
P33711	SOMA_CANLF	Growth hormone	Canis	MAASPRNSVLLAFALLCLPWPQEVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF	Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.	P33711
B5YKP5	MTIP_THEYD	5'-methylthioinosine phosphorylase	Thermodesulfovibrio	MHNKQQVKIGIIGGSGLSESEAKKEIITIKTPYGEPSCPYEIEKIDDIEVLFLRRHGQKHSIPPHKVNYRANIYGFKNFGIERIFGVFATGSLTENIPPGSIVIPNQIIDFTQGMRANTFYEEKKVVHIDFTEPFCSEIRHYLLETARKIGINVISHATYICVNGPRLETAAEIKFFKNIGADIIGMTIMPEASLAREVEICYAAVAVVANYAAGISKFPLTVKEVIETMEDSLDAVGFLIKETIKKLPEERKCLCKHALKNASF	Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.	B5YKP5
A5WGS6	TGT_PSYWF	tRNA-guanine transglycosylase	Psychrobacter	MQFTLHKTAAGESRARRGTVTVNHGEIRTPAFMPVGTYGTVKGMLPRDIEDIGADIILGNTFHLWLRPGTEVIDKFGGLHQFMNWNKPILTDSGGFQVFSLGAMRKITEEGVAFKSPIDGAKVFLSPEKSMQIQYSLNSDIVMQFDECTPYPATYSEAQKSLELSLRWGQRCVDEHKKLGNTNALFGIVQGSMYEDLRRQSMDGLLEIGFDGYAIGGLSVGEPKEEMISVLNYMPELMPADKPRYLMGVGKPEDILEAVRRGVDMFDCVMPTRNARNGHYFVTGNEDNQGIVRIRNSQYREDQGPLDPECDCYCCQNFSRAYLYHLNKCKEMLGAQLATIHNLRYYQRLMQGIRDAIDEDRFDEFVADFYHRRGQDVPPLELK	Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).	A5WGS6
O78516	FTSH_GUITH	ATP-dependent zinc metalloprotease FtsH	Guillardia	MKISWKNILLTLIPLGLISFLVWQGFNNTTNPQFTKNIASSRMTYGRFLEYLDLGWVKKVDLYDEGHTAIVEAIGPELGNRIQRIRVELPATAPELITKLRKANVDLDAHATNDSTPAWSLIGNLIFPILLIAGLAFLFRRSSNLPGGPGQAMNFGKSKARFQMEAKTGVTFNDVAGVDEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENSPCIVFIDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGIIIIAATNRVDVLDAALLRPGRFDRQVTVDVPDVKGRLEILNVHARNKKLDLSISLELIAKRTPGFSGADLANLLNEAAILTARRRKKQITISEIDASIDRVIAGMEGKALVDSKTKRLIAYHEVGHAIIGTLLKHHDPVQKVTLVPRGQAKGLTWFTPSEDQSLISRSQILARIMGALGGRAAEEVVFGLPEVTTGAGNDLQQVTSMARQMVTRFGMSNIGPLSLESQNSDPFLGRTMGSSSQYSEDIASRIDMQVRAIIQHCHTETVQIIKDNRVVIDKLVDLLIEKETIDGDEFRQIVGDFTSLPEKIDYKSQLKST	Acts as a processive, ATP-dependent zinc metallopeptidase.	O78516
O62327	GPX2_CAEEL	Glutathione peroxidase 2	Caenorhabditis	MASVHGITVKNAQGEDTPLSNYQGKVLIIVNVASQCGLTNSNYNQFKELLDVYKKDGLEVLAFPCNQFGGQEPSCEIDIAAFVADKFKFEPTLFQKIDVNGDNTAPLYKFLKQEKGGFLVDAIKWNFTKFLVGRDGHVIKRFSPTTEPKDMKKDIEAALQAKL	May constitute a glutathione peroxidase-like protective system against oxidative stresses.	O62327
Q6S5L9	SHC4_MOUSE	Src homology 2 domain-containing-transforming protein C4	Mus	MRERSQDSQAGLTLYVGLFGHLGMLHRTKYSRFRNESITSLDEGSPGGSVGNKGSSPPPYPALAPHLPTEDATVSSQESPTALCTLIPRMASMKLANPITFLGLKTFCLGTKQVSRLKLQENQDQTPSRPASPESNLNRTGPAPAPDPDQVGRRPTSLRPDTCPLPGPGEPSPRSKQDGPPLQHLLGNGLNYCVRYMGCIEVLQSMRSLDFGMRTQVTREAISRLCEAVPGAHGAIKKRKAPVKFLTTVLGKSNLQFSGMNIKLTVSTSSLTLMNLDNQQIIANHQMQSISFASGGDPDTTDYVAYVAKDPVNQRACHILECRSGMAQDVISTIGQAFELRFKQYLKNPSLNTWEREEVLVDGAPEDRDHDYYNSIPGKQPPEGGISDVRIQAQATDQMAYCPIRCEKLCYLPGNSTCSGVYKNCMGRSRPIGIPHERAGQGDTPSLRHFWRVDLFDDPCYVNTQALQSMHSYAGNQSSALPQGSPWHLGKAPETVQPGATAKPGSALALPHIRQQLWDEECFHGKLSRGAAEKLLVKDGDFLVRESVTSPGQFVLSGLQGGQAKHLLLVDPEGKVRTKDHVFDNVGHLIKYHMDNNLPIISSGSEVRLKQPIRKYDNTGLLPPKK	Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1.	Q6S5L9
B0SA31	RL18_LEPBA	50S ribosomal protein L18	Leptospira	MINKTAKNTKRLRRAERVRYKLRQTSERPRLVFNKTNRYLTAQIIDDAKGVTLVYATTLEKDFPKHENSKKSKSAATELGKVVADKAKKAGVSQVVLDRSGMVYHGRIAAFADSAREGGLEF	This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.	B0SA31
Q9UJ71	CLC4K_HUMAN	Langerin	Homo	MTVEKEAPDAHFTVDKQNISLWPREPPPKSGPSLVPGKTPTVRAALICLTLVLVASVLLQAVLYPRFMGTISDVKTNVQLLKGRVDNISTLDSEIKKNSDGMEAAGVQIQMVNESLGYVRSQFLKLKTSVEKANAQIQILTRSWEEVSTLNAQIPELKSDLEKASALNTKIRALQGSLENMSKLLKRQNDILQVVSQGWKYFKGNFYYFSLIPKTWYSAEQFCVSRNSHLTSVTSESEQEFLYKTAGGLIYWIGLTKAGMEGDWSWVDDTPFNKVQSVRFWIPGEPNNAGNNEHCGNIKAPSLQAWNDAPCDKTFLFICKRPYVPSEP	Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.	Q9UJ71
Q9W5B6	MTU1_DROME	Mitochondrial tRNA-specific 2-thiouridylase 1	Sophophora	MIRNVVVGVSGGVDSAVSAHLLAEQGFKVLGVFMRNWDEADEVGRCSGEADLKDAEWACRQLGVELRQVNYVREYWTAVFSQFLDDYQMGLTPNPDILCNRHIKFDLFHKHALENLGYDAVATGHYARNSLGNYLEGIASNNDARLLIPADTFKDQTFFLAGISRKALQRTMFPLGDFQKSQVKDLAKKIGFQRLAKKKESTGICFVGKRNFKDFIQEYITSKRGPFLDIDSGAVVGHHEGIHQWTVGQRCRLSSFLQPYFVARKEAASNTIYVASGHNHPALLSTHIAVDPPNWLCSKSQQILSDTGSLRCRFRFQHTKPLVDCQLSISPSNTFLVELDAPLRAITPGQYAVFYDDTACLGSARILSANPLKKKNAQTQQAQAANLVS	Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.	Q9W5B6
A5IN99	PANC_THEP1	Pantoate-activating enzyme	Thermotoga	MKIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARDENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRKLLEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKVKIDYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTILG	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.	A5IN99
Q10133	RHO2_SCHPO	GTP-binding protein rho2	Schizosaccharomyces	MLQSQPIRRKLVVVGDGACGKTSLLSVFTLGYFPTEYVPTVFENYVSDCRVDGKSVQLALWDTAGQEEYERLRPMSYAKAHIILVGFAIDSPDSLENVSTKWIEEINTLCPNVPFILVGMKADLRSDPVAIEEMRRRNQNFVKSQQAELVAQRIGARKYMECSSLTGDGVDDVFEAATRAALTVRDSENDKSSTKCCIIS	Involved in cell morphogenesis, the maintenance of growth direction, control of polarity and of cell wall integrity. Regulates the synthesis of alpha-D-glucan through activation of pck2.	Q10133
Q8R6T8	PURA_CALS4	IMP--aspartate ligase	Caldanaerobacter	MSVTVIVGAQWGDEGKGKITDYLAERSEVVVRYQGGNNAGHTVEKDGVQYKLHLIPSGILYPDKICVIGNGVVVDPSALLKEIEDLKAKGVEVKEDNLKISDRAHVVFPYHIKEDELEEKGKGDEDLGTTKKGIGPCYRDKTERIGIRMCDLMNAEVFREKLKKNLERKNKIFKDIYGEDGFDFEQIFETYREYAERLRPYVTDTSVLLYNLAKEGKKILFEGAQGTLLDLDFGTYPYVTASHPVAGGATIGAGIGPTMIDNVIGVVKAYTTRVGKGPFPTELKDEIGDFLREKGYEYGTTTGRPRRCGWIDIVMLRYAVRVSGITSLALTKLDTLTGLEKIKICTGYKINGKIIEDFPASLEELKMCEPIYEEMEGWSENIQDVRSFEDLPLNAKKYVKRLEELVGVEFSIISVGPEREETIVLRNF	Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.	Q8R6T8
Q67PR8	RPOZ_SYMTH	Transcriptase subunit omega	Symbiobacterium	MIKPSLDQLMHLVDSKYTLVILAARRARDLQDGKHQMVESKSNKPVTIALEELAAGKLFFERGKPTPLG	Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.	Q67PR8
P02163	MYG_ROUAE	Myoglobin	Rousettus	MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGQHEAQLKPLAQSHATKHKIPVKYLEFISEVIIQVLQSKHPGDFGADAQGAMGKALELFRNDIAAKYKELGFQG	Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.	P02163
Q6LU31	GUAA_PHOPR	Glutamine amidotransferase	Photobacterium	MTTSTNIHDQRILILDFGSQYTQLIARRIREIGVYCELWSWDVDEADIRDFNPNGIILSGGPESVTGDESPRAPQYVFEAGVPVFGVCYGMQTMAEQLGGKVAGSSMREFGYAQVEIVEPTSFFKNIEDAVAEDGNGLLDVWMSHGDKVVEIPSDFVKVAQTDTCPFAAIANEEKHFYGVQFHPEVTHTRQGMRIIENFVLNICGCENLWTSANIIEDAIANIKEQVGDDEVILGLSGGVDSSVVAMLLHRAIGDKLTCVFVDNGLLRLNEGEQVMDMFGDHFGLNIVHVKAEDRFLNALAGENDPEAKRKIIGHAFIDVFDEESKKLKNAKWLAQGTIYPDVIESAASKNGKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHSADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVDGISRVVYDISGKPPATIEWE	Catalyzes the synthesis of GMP from XMP.	Q6LU31
Q88PD5	SODF_PSEPK	Superoxide dismutase [Fe]	Pseudomonas	MAFELPPLPYAHDALQPHISKETLEYHHDKHHNTYVVNLNNLVPGTEFEGKTLEEIVKSSSGGIFNNAAQVWNHTFYWNCLSPNGGGQPTGALADAINAAFGSFDKFKEEFTKTSVGTFGSGWGWLVKKADGSLALASTIGAGCPLTSGDTPLLTCDVWEHAYYIDYRNLRPKYVEAFWNLVNWAFVAEQFEGKTFKA	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.	Q88PD5
P42111	YXAL_BACSU	Uncharacterized protein YxaL	Bacillus	MVKSFRMKALIAGAAVAAAVSAGAVSDVPAAKVLQPTAAYAAETVFSQNNGASGFLPGRYDVQAMAPAMFNWSRESRFAGNTDGTLKWQNDIRTTPQNGAGAVIDGDGTVYLHSRDGEMKAFNPDGSVKWVTGNLGKTYTQSPVLGTNGVIYLASYDKKIYFIDKETGEILTTVPLSGGPSSETVIGSDGTLYFSTLDNYVHAIKPTSKSTWTERWKLKTNGVVSSVPVLAKNGTVYVGTYNYVFYAINSGTGQVKWSRTTSNAFKGYPVIDKDGNIYAGNQDGQLYAYTSTGSLKWTFPLNGFSSSSPAIDHNGNIYIGSGSGELFSISKNGDMNWSFYTDGPVRTAPLIDAKGTVYFGSDDMKVYAADANGNELWSYQTDSNVVSSPQLAEDGTLYIGSYTKLMAFGK	Increases the processivity of the PcrA helicase, but does not bind to DNA.	P42111
A4W7Z0	MTNK_ENT38	Methylthioribose kinase	Enterobacter	MSQYRTFTAQDAVEYAKQFGGLDNPSSLVEAQEIGDGNLNLVFKIFDAQGVSRIIVKQALPYVRCVGESWPLTLDRARLEAQTLVEHYQHSPQHTVKIHHYDPELAVMVMEDLSSHKIWRGELISGVYYPQASRQLGEYLAHTLFHTSDFYLHPHAKKAQVAKYINPEMCEITEDLFFNDPYQIHERNNYPAELEADVAALRSDDQLKIAVASLKHRFFSQAEALLHGDIHSGSIFVAEDSLKAIDAEFGYYGPIGFDIGTAIGNLLLNFCGLPGHLGIRDAAAAREQRLTDIQELWNTFSERFQALATEKTRDAALSVPGYASQFLKKVWTDAIGFCGTELIRRSVGLSHVADIDTIKDDAMRHECLRHAITLGKALIVIADRIDSAEALVARVRQYS	Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.	A4W7Z0
Q8U1R2	PANB_PYRFU	Ketopantoate hydroxymethyltransferase	Pyrococcus	MREITPKRIMEMKGKEKITMITAYDYPSALLADKAGFDIVFVGDSLGMVVYGEQNTLNVTMDQMIFHTRAVAKAVKRALVLADMPFGSYEVSVEEGVKNAIKLIQAGADAVKIEGGYDHRKLVKKLVRMGIPVMGHTGLTPQRYLRLGGYRIMGENEEEVEEILRDAKALEKAGAFAVVLEFVLADVAKLVTEEVSIPTIGIGSGPYVDGQVLVWHDVLGLYESSPPFAKRYANLREEILRAISEFRKEVKEGKFPGKEHYWEYQDKETFNRIKENVMRKLRL	Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.	Q8U1R2
Q5L3Z4	RL2_GEOKA	50S ribosomal protein L2	Geobacillus thermoleovorans group	MAIKKYKPTSNGRRGMTVLDFSEITTDQPEKSLLAPLKKKAGRNNQGKITVRHQGGGHKRQYRIIDFKRDKDGIPGRVATIEYDPNRSANIALINYADGEKRYIIAPKNLKVGMEIMSGPDADIKIGNALPLENIPVGTLVHNIELKPGRGGQLVRAAGTSAQVLGKEGKYVIVRLASGEVRMILGKCRATVGEVGNEQHELVNIGKAGRARWLGIRPTVRGSVMNPVDHPHGGGEGKAPIGRKSPMTPWGKPTLGYKTRKKKNKSDKFIIRRRKK	One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.	Q5L3Z4
Q5YXQ1	MAIA_NOCFA	Maleate cis-trans isomerase	Nocardia	MGIRRIGLVVPSSNVTVETEMPALLSRHPGAEFSFHSTRMRMHTVSPEGLAAMNAQRERCVLEIADAAPEVILYACLVAVMVGGPGEHHRVESAVAEQLATGGSQALVRSSAGALVEGLRALDAQRVALVTPYMRPLAEKVVAYLEAEGFTISDWRALEVADNTEVGCIPGEQVMAAARSLDLSEVDALVISCCVQMPSLPLVETAEREFGIPVLSAATAGAYSILRSLDLPVAVPGAGRLLRQDSAVTAS	Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Shows a strict specificity for maleate, with no activity detected toward structurally related substrates including citraconate, mesaconate, dimethylmaleate, and maleamide.	Q5YXQ1
Q9C8H0	AB12C_ARATH	Multidrug resistance-associated protein 13	Arabidopsis	MGFEALNWYCKPVADGFWEKAVDGAFGAYTPCAIDSLVMLVSHFVLLGLCFYRIWIIFHNTKAQIYVLRKKYYNCVLGLLACYCVVEPVLRLVMGISLFDMDEETDFPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEFRWYVRFGVLYVLVADAVLLDLVLPLKNSINRTALYLFISSRCSQALFGILLLIYIPELDPYPGYHIVNNEPLDNVEYDALRGGEHICPERHASIFSRIYFGWITPLMQLGYRKPITEKDVWQLDKWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGGRFWLAGIFKIGNDLSQFVGPVILSHLLRSMQEGDPAWVGYVYAFIIFVGVTLGVLCEAQYFQNVWRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQISQQLHGLWSAPFRIIVSMILLYQQLGVASLFGSLILFLLIPLQTLIISKMRKLTKEGLQWTDKRVGITNEILSSMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTVVSFGVFVLLGGDLTPARAFTSLSLFAVLRFPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGTPAISIKNGYFSWDSKTTKPTLSDINLEIPVGTLVAIVGGTGEGKTSLISAMLGELSHAETTSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDATALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVAHQVFDSCMKDELRGKTRVLVTNQLHFLPLMDKIILVSEGMIKEEGTFVELSKSGILFKKLMENAGKMDATQEVNTNDENILKLGPTVTVDVSERNLGSTKQGKRRRSVLIKQEERETGIISWNVLMRYKEAVGGLWVVMILLACYLATEVLRVSSSTWLSIWTDQSTSKNYSPGFYIVVYALLGFGQVAVTFTNSFWLITSSLHAARRLHDAMLSSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLQNGNTNNQAGFASTMGLLLSYTLNITSLLSGVLRQASRAENSLNSVERVGNYIDLPSEATDIIENNRPVCGWPSGGSIKFEDVHLRYRPGLPPVLHGLTFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEVEKGRIMIDDCDVAKFGLTDVRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAGLWEALHRAHIKDVISRNPFGLDAEVCEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLSNLVFERRENGMSVGG	Pump for glutathione S-conjugates.	Q9C8H0
B0KDB8	ADDB_THEP3	ATP-dependent helicase/nuclease AddB	Thermoanaerobacter	MGIRFIYGRAGTGKTYFCLREIKEKINDGNSHPLILLVPEQFTFEAEKYLLETVEKDRKMRAQVLSFKTLANRVFTEVGGLTRQHVNSCGRSMVIYKIMEDLKENLKVYYKASRQQGFIKKISEVITEFKRFEVTPEKLMDTAESIQKEGLREKLRELSLIYGKFDELLHQKYIDEEDALTLLAEKLEYSEQFKGAEFWIDGFTGFTPKQYKVLEKLLKKAARVSVTLTMDTSKDSIDNTDLFYTTKKTEDKLLKICYENNISYEKPVDLNEGVPKRFEKNEEMAFLEKHLFSYPYKIYSKDTKNISLFKAVNVYSEVEETAREIIRLVRDENLRYSDIVVTARDLKRYHKLIKTIFSHYGIPHFIDLKLDIKNNPIIVYITSLFEIYLKNWSYESVFRHLKTGFTNLNKEDISFLENYVLANGIKGGKWKEEWKYSFRNRLDKLFDDQDEKEALEKVNTIKNGISEPLNKFYKDFSNANTVREACEILYNFLVERDIPQRIENLIREFKENKEFEIANQYSQIWDIVVDVLDQMVEVMGEEKINIDLFSKILDIGFEAYQIGSIPPALDEVLVTSVDRMKSHNAKALFVIGANDGIFPASSFEEGILTDEDRQILTSYEVELDRDTKAKVFEEQFLVYTALTSTSKFLRISYPIADHEGRSLRPSIIISRFKRIFPQITQFSNVIEMDTDEENLHRVSSPDPTFNEMIKSFKEWDIKDKINSLWLDVYNWYSNKEVWRKRIEKVLEGFNYSNQVRVIPSAKIKRLYKDEINFSVSRLEKYAACPFAYFVQYGLKAKERKIYSFDPPDLGIFMHNVLNEVSKALEKEDKTWEDLDREYCDEVVNIVVDNMLKGVSEHILKSSPRYEYLSKRLTRVLSNAVWVISEHIKRSSFIPSGHEVAFGENQMYPPIKIILSNGEEINLIGRIDRVDVFEKGEESYIRIIDYKSGNKELKLEDVFYGLELQLLIYLDAILESADKENTDIKPAGIFYFRIDDPIVKADKDITDEELQKEILKKLRLDGLVLKDAEIIKEMDKSINGTSYIIPASINKDGTIGKKTKGATKEQFELLRKHVKNMIKDLAEQMINGNISITPYRKGKETACKYCPYSSVCKFETNFEGNKYMFIKEQKEEEIWNMLQKEVNKDGDKVD	The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.	B0KDB8
Q26972	SEM1A_TRICF	Semaphorin-I	Tribolium	MVVKILVWSICLIALCHAWMPDSSSKLINHFKSVESKSFTGNATFPDHFIVLNQDETSILVGGRNRVYNLSIFDLSERKGGRIDWPSSDAHGQLCILKGKTDDDCQNYIRILYSSEPGKLVICGTNSYKPLCRTYAFKEGKYLVEKEVEGIGLCPYNPEHNSTSVSYNGQLFSATVADFSGGDPLIYREPQRTELSDLKQLNAPNFVNSVAYGDYIFFFYRETAVEYMNCGKVIYSRVARVCKDDKGGPHQSRDRWTSFLKARLNCSIPGEYPFYFDEIQSTSDIVEGRYNSDDSKKIIYGILTTPVNAIGGSAICAYQMADILRVFEGSFKHQETINSNWLPVPQNLVPEPRPGQCVRDSRILPDKNVNFIKTHSLMEDVPALFGKPVLVRVSLQYRFTAITVDPQVKTINNQYLDVLYIGTDDGKVLKAVNIPKRHAKALLYRKYRTSVHPHGAPVKQLKIAPGYGKVVVVGKDEIRLANLNHCASKTRCKDCVELQDPHCAWDAKQNLCVSIDTVTSYRFLIQDVVRGDDNKCWSPQTDKKTVIKNKPSEVENEITNSIDEKDLDSSDPLIKTGLDDDSDCDPVSENSIGGCAVRQQLVIYTAGTLHIVVVVVSIVGLFSWLYSGLSVFAKFHSDSQYPEAPFIEQHNHLERLSANQTGYLTPRANKAVNLVVKVSSSTPRPKKDNLDVSKDLNIASDGTLQKIKKTYI	Plays a role in growth cones guidance.	Q26972
P39683	NPT1_YEAST	Nicotinate phosphoribosyltransferase	Saccharomyces	MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKFSKIICYSDSLNVEKAITYSHAAKENGMLATFGIGTNFTNDFRKKSEPQVKSEPLNIVIKLLEVNGNHAIKISDNLGKNMGDPATVKRVKEELGYTERSWSGDNEAHRWT	Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate . Essential for growth under anaerobic conditions .	P39683
P0AD98	LIVJ_ECO57	Leu/Ile/Val-binding protein	Escherichia	MNIKGKALLAGCIALAFSNMALAEDIKVAVVGAMSGPVAQYGDQEFTGAEQAVADINAKGGIKGNKLQIVKYDDACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLILRTTGLDSDQGPTAAKYILEKVKPQRIAIVHDKQQYGEGLARAVQDGLKKGNANVVFFDGITAGEKDFSTLVARLKKENIDFVYYGGYHPEMGQILRQARAAGLKTQFMGPEGVANVSLSNIAGESAEGLLVTKPKNYDQVPANKPIVDAIKAKKQDPSGAFVWTTYAALQSLQAGLNQSDDPAEIAKYLKANSVDTVMGPLTWDEKGDLKGFEFGVFDWHANGTATDAK	This protein is a component of the leucine, isoleucine, valine, (threonine) transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids.	P0AD98
Q8L765	BPM1_ARATH	Protein BTB-POZ AND MATH DOMAIN 1	Arabidopsis	MGTTRVCSEVSSGSSKSLSQSLTVSTSTTETVNGFHEFKICGYSLAKGVGVGKYVASDTFMVGGYSWAIYFYPDGKSPEDNSSYVSLFIALASEGADVRALFELTLVDQSGNGKHKVHSHFGRALDSGPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRVGVVKSVTEGPRYYNIPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLCEGVAINTVATTLALAEQHHCLQLKAVCLKFVALPENLKAVMQTDGFDYLKESCPSLLTELLQYVARLSEHSVIVSGHRKEIFADGCDASGRRVKPRLH	May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.	Q8L765
Q145X4	PTH_PARXL	Peptidyl-tRNA hydrolase	Paraburkholderia	MIKLIVGLGNPGAEYTATRHNAGFWLVDQLAREAGTTLRDERRFHGFYAKARLHGEEVHLLEPQTYMNRSGQSVVALAQFFKILPDEILVAHDELDMPPGSVKLKLGGGSGGHNGLKDITAHLSSQQYWRLRIGIGHPRDLIPESARAGARPDVANYVLKPPRREEQDVIDASIERALAVMPQVIKGELERAMMQLHRNP	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.	Q145X4
A0A023GPI8	LECA_CANBL	Lectin gamma chain	Canavalia	ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGRDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSSDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN	D-mannose/D-glucose-binding lectin . Has anti-inflammatory activity in animal models when applied intravenously . Has antinociceptive activity in mice when applied intravenously .	A0A023GPI8
A6X0C8	RL14_BRUA4	50S ribosomal protein L14	Brucella	MIQMQTNLDVADNSGARRVMCIKVLGGSKRRYASVGDIIVVSIKEAIPRGRVKKGDVMKAVVVRTAKDIRRPDGSVIRFDNNAAVLIDNKKEPIGTRIFGPVPRELRAKNHMKIISLAPEVL	Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.	A6X0C8
Q5SK67	PYRC_THET8	Dihydroorotase	Thermus	MILIRNVRLVDARGERGPADVLIGEGRILSLEGGEAKQVVDGTGCFLAPGFLDLHAHLREPGEEVKEDLFSGLLAAVRGGYTDLVSMPNTKPPVDTPEAVRALKEKAKALGLARLHPAAALTEKQEGKTLTPAGLLREAGAVLLTDDGRTNEDAGVLAAGLLMAAPLGLPVAVHAEDAGLRRNGVMNDGPLADLLGLPGNPPEAEAARIARDLEVLRYALRRSPATPRLHVQHLSTKRGLELVREAKRAGLPVTAEATPHHLTLTEEALRTFDPLFKVAPPLRGEEDREALLEGLLDGTLDAIATDHAPHTLAEKEKDLLRAPFGIPSLEVAFPLLYTELHLKRGFPLQRLVELFTDGPRRVLGLPPLHLEEGAEASLVLLSPKERPVDPSAFASKARYSPWAGWVLGGWPVLTLVAGRIVHEALK	Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.	Q5SK67
Q4UWC9	ACCD_XANC8	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta	Xanthomonas	MSWLSKLMPSGIRTENTPAKKRSVPEGLWEKCSNCGSALYGPELEENLEVCPKCDHHMAIRARARLAALFDLDSPTTEIAAQLGPVDVLKFKDQKKYGERIKASQKSSGEYDALIAMRGMLKGNPLVAAAFDFAFMGGSMGSVVGERFARAAEVALEVGCPFVCFSASGGARMQEGLFSLMQMAKTSAALGRLREAGLPYISVLTHPTTGGVSASFAMLGDINIAEPHALIGFAGPRVIEQTVRETLPEGFQRSEFLLDHGAIDQICDRRDMRDRIAELTTMMMRQPHPQDADAA	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.	Q4UWC9
Q8W032	CDC6B_ARATH	Cell division control protein 6 homolog B	Arabidopsis	MPTNAGTSLSSYKHIVAIGTTVKSESLESAAYEIPRKRKMRSDSAAVSGNSVSTPKKLKSHLPSSVPNPGMSEKEVVEDSNEILRYPVNLAVSDCLGTKSKWSPRDEEQMRAVKEALHVSKAPSTILCREDEQIRIFEFVKGCIDQQKAGSLYICGCPGTGKSLSMEKVVQQVGDWSTQAGLPPVDTLSVNCTSLSKTTDIFSKILGEIKPGKNANTNSSPLQHLQNLFSQKQESSSSRMMLIIADEMDYLITKDRGVLYDLFMLTTLPFSRCILIGVANAIDLADRFLPKLKSLNCKPMVITFRAYSKDQILRILQERLRVLSYVAFQPKALELCARKVAAASGDMRKALCVCRSALEILEIETRGSTGPESQGPTPDDSVVRMDHMAAALSKTFKSPVVETIQSLPQHQQIIICAAAKAFRGSKKDATVGELNKLYLEICKSWMISPAGITEFTNMCTVLNDQGILKVGQARRDKLKRVSLRVDESDITFALQEIRFFRNCLL	May be involved in the initiation of DNA replication.	Q8W032
Q47PU3	PAMO_THEFY	Baeyer-Villiger monooxygenase	Thermobifida	MAGQTTVDSRRQPPEEVDVLVVGAGFSGLYALYRLRELGRSVHVIETAGDVGGVWYWNRYPGARCDIESIEYCYSFSEEVLQEWNWTERYASQPEILRYINFVADKFDLRSGITFHTTVTAAAFDEATNTWTVDTNHGDRIRARYLIMASGQLSVPQLPNFPGLKDFAGNLYHTGNWPHEPVDFSGQRVGVIGTGSSGIQVSPQIAKQAAELFVFQRTPHFAVPARNAPLDPEFLADLKKRYAEFREESRNTPGGTHRYQGPKSALEVSDEELVETLERYWQEGGPDILAAYRDILRDRDANERVAEFIRNKIRNTVRDPEVAERLVPKGYPFGTKRLILEIDYYEMFNRDNVHLVDTLSAPIETITPRGVRTSEREYELDSLVLATGFDALTGALFKIDIRGVGNVALKEKWAAGPRTYLGLSTAGFPNLFFIAGPGSPSALSNMLVSIEQHVEWVTDHIAYMFKNGLTRSEAVLEKEDEWVEHVNEIADETLYPMTASWYTGANVPGKPRVFMLYVGGFHRYRQICDEVAAKGYEGFVLT	Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide).	Q47PU3
P67086	MIAB_MYCBO	tRNA-i(6)A37 methylthiotransferase	Mycobacterium tuberculosis complex	MVAHDAAAGVTGEGAGPPVRRAPARTYQVRTYGCQMNVHDSERLAGLLEAAGYRRATDGSEADVVVFNTCAVRENADNRLYGNLSHLAPRKRANPDMQIAVGGCLAQKDRDAVLRRAPWVDVVFGTHNIGSLPTLLERARHNKVAQVEIAEALQQFPSSLPSSRESAYAAWVSISVGCNNSCTFCIVPSLRGREVDRSPADILAEVRSLVNDGVLEVTLLGQNVNAYGVSFADPALPRNRGAFAELLRACGDIDGLERVRFTSPHPAEFTDDVIEAMAQTRNVCPALHMPLQSGSDRILRAMRRSYRAERYLGIIERVRAAIPHAAITTDLIVGFPGETEEDFAATLDVVRRARFAAAFTFQYSKRPGTPAAQLDGQLPKAVVQERYERLIALQEQISLEANRALVGQAVEVLVATGEGRKDTVTARMSGRARDGRLVHFTAGQPRVRPGDVITTKVTEAAPHHLIADAGVLTHRRTRAGDAHTAGQPGRAVGLGMPGVGLPVSAAKPGGCR	Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.	P67086
B2TZN1	HPCH_SHIB3	4-hydroxy-2-ketoheptane-1,7-dioate aldolase	Shigella	MENSFKAALKAGRPQIGLWLGLSSSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPNQPVVRPSWNDPVQIKQLLDVGTQTLLVPMVQNADEAREAVRATRYPPAGIRGVGSALARASRWNRIPDYLQKANDQMCVLVQIETREAMKNLPQILDVEGVDGVFIGPADLSADMGYAGNPQHPEVQAAIEQAIVQIRESGKAPGILIANEQLAKRYLELGALFVAVGVDTTLLARAAEALAARFGAQATAVKPGVY	Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.	B2TZN1
A1JNX2	FOLD_YERE8	Methenyltetrahydrofolate cyclohydrolase	Yersinia	MSAKIIDGKTIAQQVRNEVAALVQKRLAAGKRAPGLAVVLVGENPASQIYVASKRKACEEVGFVSRSYDLPMTTTEAELLALIDSLNNDSEIDGILVQLPLPAGIDNVKVLEHIHPDKDVDGFHPYNVGRLCQRAPKLRPCTPRGIVTLLERYDIPTYGLNAVVVGASNIVGRPMSLELLLAGCTTTVTHRFTKNLRQHVENADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLESGKVVGDVEFDVAVERAGWITPVPGGVGPMTVATLIQNTLQACEEYHDINENRVKGQ	Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.	A1JNX2
Q1QAQ4	MURB_PSYCK	UDP-N-acetylmuramate dehydrogenase	Psychrobacter	MTSALCSKPIAPHTLSDDLADLSYSNTMALACMADSVVTLTDEVQLDEFMAYYEQDTQHRKPLFVLSGGSNVLLPAKLNAIVLRPQMRGIQVTAQTDFHVDIEVMAGENWHDLVVHTVAQGWYGLENLALIPGLTGAAPIQNIGAYGVQLEDCLQYVRAYHLPSQTWHDLTAVDCEFGYRDSIFKRQPNTWLISRVGFRLHTDATKVLASYGDVQTVAQSYATQQGRTKPMPADVMHAIIEIRQQKLPDPKQLPNCGSFFQNPIVPQDQFATLQSSYPAIVGYPMPDAMTKVAAGWLIEQAGLKGGGIEPIFTHQQQALVLTNHAPYIATKQDVAAAQKYIIDTVYKKFAIQLSREPVWVNADGSIGYDEHVV	Cell wall formation.	Q1QAQ4
Q9URS0	ACTG_PENCH	Actin, gamma	Penicillium chrysogenum species complex	MEEEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPINPKFNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFSLPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPNVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIVMSGGTTMYPGISDRMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.	Q9URS0

F7ZLS5

HYEP_ROSLO

Hydrophobic dipeptide epimerase

Roseobacter

MKVEYHTVYLKKRFPLRISRGVFEGSDNLYISLTENGHTGWGEMAPGGTEGAETAAAGQAMLEQFCATGLSASIHDTWQNAHAAGVAPCALAALDMALWDLRAKQAGVPLYALLGLARRAVVSSVTVGINPPDVVRERVPLLLARGARALKIKLGSPEGIEADQAMFAAVFEAAQGSGAVLRVDANGGWSLKDARRMMGWLAEHDVEYIEQPLVRGAEDQLPDLFKDRAMPIFVDESCRMSGDIATFFQSVDGVNLKLMKCGGITEALRIVATARAFGLKTMIGCMGESSVSIAAGASIGALFDYIDLDSHLNLDPDPATGAPFENGITLPADQPGHGGVLSHA

Dipeptide epimerase with a preference for hydrophobic substrates. Catalyzes the epimerization of L-Ala-L-Thr, L-Ala-L-Met, L-Ala-L-His, L-Ala-L-Phe, L-Ala-L-Tyr, L-Ala-L-Trp, L-Ile-L-Ala, L-Ile-L-Ser, L-Ile-L-Met, L-Ile-L-His, L-Ile-L-Phe, L-Ile-L-Tyr, L-Ile-L-Trp, L-Phe-L-Met, L-Phe-L-His, L-Phe-L-Phe, L-Phe-L-Tyr, L-Phe-L-Trp, L-Phe-L-Ser, L-Phe-L-Thr and L-Phe-L-Lys (in vitro).

F7ZLS5

Q6CQP9

VMA21_KLULA

Vacuolar ATPase assembly integral membrane protein VMA21

Kluyveromyces

MPVDVPRSVIAKLMFFTVAMVVLPVLTFFWLQEHTDNTLVSGGLAAAMANLVLIAYVIMAFQEDSSSSEDDETKKEK

Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.

Q6CQP9

Q46WT0

HEM1_CUPPJ

Glutamyl-tRNA reductase

Cupriavidus

MQLLAIGINHTTAPVSLRERVAFPLEQIKPALGALRTHLAGRNGTEAAILSTCNRTEIYCATDILKPGAEGFEHTLRWLSQHHNVPASDLAPHLYSLPQSEAVRHAFRVASGLDSMVLGETQILGQLKDAVRTAGEAGSLGTYLNQLFQRTFAVAKEVRGQTEIGAHSVSMAAAAVRLAQRIFESVSTQRVLFIGAGEMIELCATHFAAQKPRQVVVANRTVERGEKLAEQLAEQGLTTQAIRLQELGERLHEFDIVVSCTASSLPIIGLGAVERAVKRRKHRPIMMVDLAVPRDVEPEVARLDDVFLYTVDDLGAVVREGNALRQAAVAQAEAIIESRVQNFMHWLETRSVVPVIRELQTAGESIRQAELERARRMLARGDDPEAVLEALSGALTRKFLHGPTHALNHMQGEDREALVRLVPGLFRQSSHSER

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).

Q46WT0

Q9HLV2

PCKG_THEAC

Phosphoenolpyruvate carboxykinase [GTP]

Thermoplasma

MLAIDESELNQHAMKWIEGIKKFTEAEDVVVCDGTPEEFKQISNELIKSGEFIKLNENRYPNSFLYRSDRTDVARSEERTFIAAPDASMAGSLNNHMTLQQVSEVWNKFFRGAYRGKTMFVIPYALGPLNSRFTDYGIEITDSRYVVLNLHYITRMGKQVIGSMPEKFVKGVHATGTLDPGNKFIIHIPWDKPEGVDADILSVNTNYGGNALLSKKCHALRIASVRARKEGWLAEHMLLLEVEDPHGRKVYITGAFPSASGKTNLAMINPPKQYAEAGWKTRLLSDDIAWMKMKDGMLYATNPENGFFAVVPGTNYRTNKNAMITLSRNTIFTNTGMTKTGEPWWEGLDPLQEELYDWKGVLRKPDGEPIAHPNSRFTSPLSNYPFLSDRSEDPEGVPVSAILFGGRRASLVPLVYEAFNWNHGVFMGATMGVEKTAASEGKVGELRRDPMAMRPFCGYNISDYFRHWIEMGRKLSRRPKIFYVNWFRRRQDGSFIWPGFSENFRVIEWILYRLDHNDNAIETPIGYIPENINTDGLNLTKQDMEELFRIDRDGWREEMKSIGDYFSQIGNIPEDLLIEFEMEKRRIS

Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.

Q9HLV2

P47315

PTG3C_MYCGE

PTS system glucose-specific EIIA component

Mycoplasma

MQISLVKIRNKFKQRNRGSFRQWVGKLSNGLMIPIAVLPLAGIFLGIGDAISSNSSGIVGVKFFGEFIKQGGNVVFANLPILFAVAIAITFSQDAGVAGFSAFVFWATMNAFMSSLIIPVDANNTASGYNILYWKAVPQSAIASTLGLNSLSTSVFGGIIVGALTAYLYNKFYAIRLPDVIGFFSGTRFVPIICMTIAIPVALLLLMVWPGVSILLNLIGTGLGILGGRGYGANSLIFGYIERALIPFGVHHAFYAPLWYTSAGGSLQEIANQQVWIRAPGSDYVTRVIGWEDFNTPGKWVIPAALANGTSGMMNGATTTGQDSTSALSKYMSKESTNFLSWKELVDGLTRKGNFDELAKNGLLDGSNKIWIGLNQSGILGKKVLLSDGKDYTITFKTFANTTPTFWSHGAHALLPISGTPSAITNGVTVNGTANSKTYNVSQFTVAVPSLNPAQYSQGKFPFMLIGIPAAGLAMILAAPKGRRKEASSIIGSAAFTSFLTGITEPFEFTFLFLAPWLFYGIHAVLAAVSFWLMNLLSANVGQTFSGSFIDFILYGALPDGRGWLANSYLVPIIGIFLALIYFPTFYFLTIRFNLATPGRGGKLITKKEYLAAKAAQKTDQTTNTNFNQTQIEAGMLLRAYGGSENIAELGACITKLRVTVKNPELVNETIIKDLGAAGVMRTTPTFFVAVFGTRAAVYKSAMQDIIQGKVNWTELQKVLDKNDSTVEKPEIKPTPVLKVQDEIVILSPVNGTLKPLTQVPDDTFKNRLVGDGIAILPSDGHFKAPGDVGVKTELAFPTGHAFIFDVDGVKVMLHIGIDTVKINADKKPGEQLEVFDVKTKQGEYTKLKSESVVEVDLKKLKRKYDPITPFIVMQESLDNFKLVPIRQRGEIKVGQPLFKLIYKDKKS

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.

P47315

Q92209

KHSE_CANAL

Homoserine kinase

Candida

MSVISFKIKVPASSANIGPGFDVLGIGLQLYLTITVTIDPSIDTSSDPHHALLSYEGDGKVPFESNENLITQTALYVMRCNGIKDFPRGTHIHVNNPIPLGRGLGSSASAIVAGVYLGNEIGNLKLDKYRLLDYCLMIERHPDNIAAAMLGGFIGSYLNELSSEDSQLTTVPLDYILPKVKNGELITPQDKIVSQQPPNNIGQYVEYKWNKKIKCLTIIPNFELSTDLSRSVLPKNYQLPDIVYNLQRIAILTTALTQDPPNHKVIYQSMKDKLHQPYRFGLIPGLNTVLQKITPESYPGLCGICLSGAGPTILCLATDGFEKIANDVIEIFKQEGIECDSKLLDLAYDGATVEYGS

Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.

Q92209

P38623

RCK2_YEAST

CAM kinase-like protein kinase CLK1

Saccharomyces

MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWLNTFDCLPKEGESSQKKAGTSERRHPHKKQFQLFQRDSSLLFSPAAVAMRDAFDIGNAVKRTEEDRMGTRGGLGSLAEDEELEDSYSGAQGDEQLEQNMFQLTLDTSTILQRRKKVQENDVGPTIPISATIRE

Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.

P38623

Q5QYN5

IF3_IDILO

Translation initiation factor IF-3

Idiomarina

MKGGKRTQKAADKNRINEQITGVDEVRLIGTDGEQAGVVSINEALDAAAEAGVDLVEMSPNAEPPVCRLMDYGKFLFEKSKEQKEQKKKQKQIQVKEVKFRPGTDEGDYQVKLRNLRRFLEGGDKTKVTIRFRGREMAHQELGIELLNRVKNDLEEISIVESFPRRAEGRQMIMVLAPNKK

IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.

Q5QYN5

P50266

CYB5R_DROVI

Cytochrome b5-related protein

Drosophila

MVIETWKKSGIATKFPTYRNSAPVTVHSWQKGKRQDVEAEGLWRIKDGIYDFTEFIDKHPGGTFWIRETKGTDITEAFEAHHLTTAPEKMIAKYKVRDAYQRIYTLTLHEDGFYKTLKERVREKLKTIDKRPKRKSDVSDDL

May play a role in muscle cell metabolism.

P50266

Q8FB81

THIG_ECOL6

Thiazole synthase

Escherichia

MLHIADKTFDSHLFTGTGKFASSQLMVESIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIFAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGANAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQAGPGSRSHFAHATSPLTEFLEASA

Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.

Q8FB81

Q8L612

MACP1_ARATH

MACPF domain-containing protein At1g14780

Arabidopsis

MSRDGGDVIETAVKSLGKGFDLTADFRLKYCKDGDGSAGDDRLVVLDQTQNRELHIPGFGVFQNVSADINCDKGERTRFRSDILDFNKMSEYFNQRSSVTGKIPSGNFNATFGFQSGSWATDAANVKSLGLDASVVTLFNLHIHNPNRLRLTDRVRNAVPSSWDPQLLARFIERYGTHVITGVSVGGQDVVVVRQDKSSDLDNDLLRHHLYDLGDQLFTGSCLLSTRRLNKAYHHSHSQPKFPEAFNVFDDKQTVAFNNFSINSQNGITVICAKRGGDGRAKSHSEWLITVPDKPDAINFNFIPITSLLKDVPGSGLLSHAMSLYLRYKPPLMDLQYFLDFSGPRAWAPVHNDLPFGAAPNMASAYPALHINFMGPKLYVNTTPVTSEKNPVTGMRFFLEGKKCNRLAIHLQHLDNTRTTVGEKITDEHIWRGSDQITDNDRYFEPLNGKKFSHVCTVPVKYDPNWIKTTSNHKSQNDVAFIVTGAQLEVKKHGSKSVLHLRLRYTKVSDHYVVQNSWVHGPIGTSQKSGIFSSMSMPLTSGSVHHNMIQKDKNEVVLDSGVFPGGPPVPANNKIVKFVDLSQLCRGPQHSPGHWLVTGVRLYLDKGKLCLHVKFALLHRQRLLVSS

Negatively controls the salicylic acid (SA)-mediated pathway of programmed cell death in plant immunity.

Q8L612

P25576

POF1_YEAST

Promoter of filamentation protein 1

Saccharomyces

MKKTFEQFRKSNLLFQVLKGPQHLECQKLFVLDSSFNPPHLAHFQLLSQTIKNFKLKDTRSHVLLLLAVNNADKLPKPASFPTRLEMMCLFADYLQEKLPQSVVSVGLTVFSKFIDKDKILHEQFVKGCSADIGYLVGFDTIARIFDEKYYHPLKISDVMESFMSGSQLYCLARGDCHLSAESQLRYASDILEGKFEPVIPREWGARIHVMQNDYPALRNVSSSEIRNKLKNGQVESLKDELPLCIYDYLINNKTIFD

Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Involved in the salvage pathway for NAD(+) biosynthesis via NMN . Involved in the filamentation pathway. Suppresses the filamentation defect of a KSS1 deletion .

P25576

Q18BC9

RNH2_CLOD6

Ribonuclease HII

Clostridioides

MQDKSVREIKEIIETLEVEKYMEYIELLRVDERKSVQGLAIKLAKKLDNIRKEEERLETINIFENEGYDKGYLYIGGIDEAGRGPLAGPVVASVVVFKKDTKIEGVNDSKKLSEAKRDELFEVIKEEALDYGIGIVNNEEIDEFNILNATYMAMKKAINCLKKAPDYLLVDAATIPGIDISQNPIVKGDSKSISIAAASILAKVTRDSIMYQYDRVYPEYGFKSHKGYGTKEHYEAIEKYGITPIHRKSFLKNIL

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.

Q18BC9

Q972C1

GCSPA_SULTO

Glycine dehydrogenase (aminomethyl-transferring) subunit 1

Sulfurisphaera

MDMHPWLPNIKYIEEMLKSIGVNSIDDLFIDVPEEIKLKKELDLDYKKPLSEYEIILKLQELQNKNKRLKMPPFLGGGLCPHYVPEVVKFIIKRSEFYTAYTPYQPEISQGLLQALFEYQSLIAELFEMEVVNASLYDWGSALAEAIMMANRINKKKTVLVPKLMNPYHKEVVKTWTYGKGIKLVEIPPNERGTIDVSKLESMINEDDVSAIYIQQPNFYGIFEDEIEYIVDIAKKKKIITIMGVSPLALGLIKPPGEYEIDITVGDGQELGLSLNFGGPLLGILATRWDGQLVRQMPGRIVGLTKDSEGKRGFTLILQTREQFARREKATSNITTNEALMAIAAAVYLSLLGRNGIKELAKEIYIRSHYAKKRLEELGVNTVYNGDFFEEFAVDFRTDYDIIHSRLLEKNIHGGLKLGKTQALFCVTEVHTKSMIDELIESIREVFSG

The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.

Q972C1

Q4QLG0

MURD_HAEI8

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase

Haemophilus

MNAYQNKNITIIGLGKTGLSCVDYLLSQQANIRVIDTRKKPTGIDKLPQNIPLHTGSLNQEWLLESDMIVISPGLAVKTPEIQTALKAGVEVIGDIELFCRAATKPIVGITGSNGKSTVTTLVYEMAKAAGVKVGMGGNIGIPALSLLNEDCELYVLELSSFQLETTYSLKAAAATVLNVTEDHMDRYMDLEDYRQAKLRIYHNAEVGVLNNEDKLTFGEGENQARQTVSFAENSADYWLKTENGKQYLMVKDEVILPCEEVTLVGRHNYMNILAATALAQAVGINLDSIRTALRHFKGLDHRFQLVHQANGIRWINDSKATNVGSTVAALAGLYIEGKLHLLLGGDGKGADFSELAELINQPHIICYCFGRDGVQLAKFSSQSYLFETMEQAIEFLRPTLQSGDMVLLSPACASLDQFASFEKRGEEFTHLAQYSA

Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).

Q4QLG0

Q3AVC2

ILVC_SYNS9

Ketol-acid reductoisomerase type I

unclassified Synechococcus

MAQLFYDSDADLGLLNGKTVAIIGYGSQGHAHALNLKDSGVNVVVGLYEGSRSAEKAKADGLEVLTVAEASAKADWIMVLLPDEFQKDVYEKEIAPHLKSGKVLSFAHGFNIRFELIKPPADVDVVMIAPKGPGHTVRWEYQNGQGVPALFAIEQDASGNARGLTMAYAKGIGGTRAGILETNFKEETETDLFGEQAVLCGGLSELVKAGFETLVEAGYQPELAYFECMHEVKLIVDLMVKGGLTSMRDSISNTAEYGDYVSGPRLITADTKAEMKRVLADIQDGTFARNFVAECDAGKPEMKKIRDRDAQHPIEKVGKGLRSMFSWLKDA

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.

Q3AVC2

Q3AJS6

HISZ_SYNSC

ATP phosphoribosyltransferase regulatory subunit

unclassified Synechococcus

MALQPAAGAKDLNPRQVETNRQLTERLASVYRLWGYDEVSPPRVERLATLMAGGAIDSSDIVRLVADDPLGLRPEMTASIARAACTRFADRQRPLRLWASGTVFRTRSADEGGQCIEENLQSGVELFGVSGSEAEMELLSLLMASVQTLGLQTSQKPRLLLGHTALMDLVLRPFNGAVRDQIRTALIDFDRLAIESFDLAYAEKTRLLSLMDCRGTPDQVLAQLSSLYGEQPVFDELRRLCTHLASAAQAQAVTIQLDPTFQPHFELYTGLVFQLVCDGRSSPVVFARGGRYDDLVRRCGATDDRAFGAGFSLAIDPIRELISDLDAAEQQQSDVLIAFSTASNLESAMERQRSWHEQGRTAVMALEPLSSMQEAELQAKAQGGLQLDWVDP

Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.

Q3AJS6

Q9D0C1

RN115_MOUSE

Zinc finger protein 364

Mus

MAEASAAGADAGSAVAAHRFFCHFCKGEVNPKLPEYICPRCDSGFIEEVTDDSSFLGGGGSRTDNSTATHFAELWDHLDHTMFLQDFRPFLSSNPLDQDNRANERGHQTHTDFWGPSRPPRLPMTRRYRSRGSTRPDRSPAIEGIIQQIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVNTGLECPVCKEDYTVEEKVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQTQSSEASASNRFSNDSQLHDRWTF

E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.

Q9D0C1

Q51520

PHZF_PSECL

Phenazine/pyocyanine biosynthesis protein PhzF

Pseudomonas

MHHYVIIDAFASAPLEGNPVTVFFDADDLSATQMQRIAREMNLSETTFVLKPRNCGDALIRIFTPVNELPFAGHPLLGTAIALGAHTDNHRLFLETQMGTIAFELERQNGSVVAASMDQPIPTWTALGRDVELLKALGISDSTFPIEIYHNGPRHVFVGLPSIAALSALHPDHRALSSFHDMAINCFAGAGRRWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHGQIEFGQQIEILQGVEIGRPSLMFARAEGRADQLTRVEVSGNGVTFGRGTIVL

Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.

Q51520

C0MFD9

XERS_STRS7

Tyrosine recombinase XerS

Streptococcus

MKRDLLLTKIEEYKNIMPWYVLDYYQSKLSVPYSFTTLYEYLKEYKRFFEWLIDSDLSKAARIADVDLTTLEHLSKKDMEAFILYLRERPSLNTYSTKKGVSQTTINRTLSALSSLYKYLTEEVENEHGEPYFYRNVMKKVATKKKRETLAARAENIKQKLFLGDETMAFLDYVDKEYEHKLSNRAKASFRKNKERDLAIIALLLASGIRLSEAVNLDLKDVNLNMMLVEVTRKGGKRDSVNVAAFAKPHLEAYLSVRKDRYQAEKQDVAFFLTAYRGLPNRIDASSIEKMVGKYSESFKIRVTPHKLRHTLATRLYDTTKSQVLVSHQLGHASTQVTDLYTHIVNDEQKNALDKL

Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division.

C0MFD9

Q57QP2

CBPA_SALCH

Curved DNA-binding protein

Salmonella

MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPNAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQQHEGQPYNAEDFDDIFSSIFGQHGRHSHHRHAARGHDIEIEVAVFLEETLEEHQRTISYSVPVYNAFGLVEREIPKTLNVKIPAGVSNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVNQDLEVVLPLAPWEAALGAKVSVPTLKERILLTIPPGSQAGQRLRIKGKGLASKKHTGDLYAIIKIVMPPKPDEKTAALWQQLADAQSSFDPRQQWGKA

DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.

Q57QP2

C5B704

UBIA_EDWI9

4-HB polyprenyltransferase

Edwardsiella

MEGCVAQSKWLAYCRLMRIDKPIGSLLLLWPTYWALWLAGGTAPGGKLLLVFTCGVFFMRAAGCVINDFADRHFDGHVKRTCQRPLPCGALSEREAKALFVLLVGLSFALVLTLNAMTIWLSVAALTLAWLYPFIKRFSHLPQVILGMAFGWSIPMAYAAVGESLPLSCWLLFAANICWTVAYDTQYAMVDRDDDLRIGIKSTAILFGRYDRLVIGLLQLATLLLLLWVGDLNQLQGAYYWGVLLAAVLFVYQQQLITRRARTSCFRAFMNNNYVGLILFLGILLAL

Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.

C5B704

Q96FG2

ELMD3_HUMAN

RNA-binding protein 29

Homo

MNEKSCSFHSKEELRDGQGERLSAGYSPSYDKDKSVLAFRGIPISELKNHGILQALTTEAYEWEPRVVSTEVVRAQEEWEAVDTIQPETGSQASSEQPGQLISFSEALQHFQTVDLSPFKKRIQPTIRRTGLAALRHYLFGPPKLHQRLREERDLVLTIAQCGLDSQDPVHGRVLQTIYKKLTGSKFDCALHGNHWEDLGFQGANPATDLRGAGFLALLHLLYLVMDSKTLPMAQEIFRLSRHHIQQFPFCLMSVNITHIAIQALREECLSRECNRQQKVIPVVNSFYAATFLHLAHVWRTQRKTISDSGFVLKELEVLAKKSPRRLLKTLELYLARVSKGQASLLGAQKCYGPEAPPFKDLTFTGESDLQSHSSEGVWLI

Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity.

Q96FG2

Q9KQH1

NTPPB_VIBCH

7-methyl-GTP pyrophosphatase

Vibrio

MQNYQLVLASTSPFRQQILAKLKLPFVTAKPDCDETPLIGETPEHLLMRLAENKARSCFLADPSLVIGSDQVCVIDDQIIGKPLTTEKAVEQLLRQSGQAITFYTGLALFNNQTQQTQVLCDTFTVHFRTLSESMARRYVEAEQPLHCAGSFKSEGLGIALFERLEGDDPNSLIGLPLIKLIQLLENEGLNVI

Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.

Q9KQH1

Q2J843

METK2_FRACC

Methionine adenosyltransferase 2

Frankia

MATRLFTSESVTEGHPDKIADQISDSILDAMIKDDPKSRVAVETLITTGQVHVAGEVTTKTYVDIASVVRERILEIGYDSSKKGFDGASCGVSVSIGAQSPDIAQGVDTAHETRVEGSADDEFDRQGAGDQGLMFGFACDETPELMPLPIALAHRLARRLSAVRKEGQIGYLRPDGKTQVTIEYVDGKPARLDTVVVSSQHAADIDLDTLLAPDIAEYVVEPELALLEIATEGRRLLVNPTGRFEIGGPMGDAGLTGRKIIVDTYGGYARHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLASRCEVQVAYAIGKAQPVGLFVETFGTGTVPDIQIQDAVTSVFDLRPAAIIRDLDLLRPVYAQTAAYGHFGRPELDFTWESTARAEALQRAVKG

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.

Q2J843

B0BTN9

RISB_ACTPJ

6,7-dimethyl-8-ribityllumazine synthase

Actinobacillus

MAKITGNLVATGLKFGIVTARFNDFINDKLLSGAIDTLVRHGADENNIDTAWVPGAFEIPLVAKKMATSGKYDAVICLGTVIRGSTTHYDYVCNEAAKGIGAVALETGVPVIFGVLTTENIEQAIERAGTKAGNKGSECALGAIEIVNVLKAI

Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.

B0BTN9

B0REV4

METK_CLAMS

Methionine adenosyltransferase

Clavibacter

MTDLRLFTSESVTEGHPDKICDQISDSILDALLTQDPSSRAAVETLVTTGLVHVAGEVTTSGYVDIPQIVRDRIRDIGYDSSEVGFDGSNCGVTVSIGAQSPDIAQGVDRSYESRSGSASTDAHDLQGAGDQGLMFGYASRDTPVFMPLPIYLAHRLAERLAAVRHSGELSYLRPDGKTQVTIGYEGLVPRTVDTVVLSTQHGPQVSQEDLRREVEEHVIRPVLAAAAEIGIELDSRDATLLINPTGKFEIGGPKGDAGLTGRKIIVDTYGGFSRHGGGAFSGKDPSKVDRSAAYAMRWVAKNAVAAGLADRLEVQVAYAIGKAAPVGLYVEAFGTAHVPEDRIVRAIRETFDLRPAAIVERLDLLRPIYAETAAYGHFGRELPDFTWEALDRVADLQSAAGL

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.

B0REV4

Q5LMK7

DAPA_RUEPO

4-hydroxy-tetrahydrodipicolinate synthase

Ruegeria

MFKGSMPALVTPFRNGELDLEALKRLVEWQIGEGSTGLVPVGTTGESPTLSHEEHETVVAEVVKAAAGRVPVIAGAGSNNTTEAIRFVQFAQRIGADAALVVTPYYNRPTQRGLIAHFTALHDCAEIPIVIYNIPGRSVVDMTPATMGALAKLPRIVGVKDATGDLARVSQQRASCGADFIQLSGEDATALGFNAHGGVGCISVTANVAPRLCAEFQQATLAGDYAKALDYQDRLMPLHEAIFIEPGLVGAKYALSKLGLCSEEVRSPLTGLEDSTKAAIDAAMKHAGLL

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).

Q5LMK7

B5FEA5

PCP_ALIFM

Pyroglutamyl-peptidase I

Aliivibrio

MKKILITGFEPFGNDKINPALEAVKLIAGRKLNGGEIVICQVPVVRYKSIETVKQAIEEQQPYAVITVGQASGRAAITPERIAINVDDFRIPDNEGIQVIDEPVVAGGPDAYFTTLPIKAMVSEIQAQGIPATVSNTAGTFVCNHLFYGIQHYLKDTNVRHGFVHIPLLPEQSVDGSQPTMKLEQIAEGLAIAAQAIIDNDSDIQQGAGTIC

Removes 5-oxoproline from various penultimate amino acid residues except L-proline.

B5FEA5

A9NNH7

LIAS_PICSI

Lipoic acid synthase

Picea

MSINPAFLRRITWGSKSLHHQFTRCQVRALSSSVEQTPESTTPALSALRERLANGGPTLSDFLTRNLGEEPYSVDVGTKKNPLPKPKWMKAAVPGGDKYTAIKAKLREMNLHTVCEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPNEPTNVAEAIVSWGLDYVVLTSVDRDDLPDQGSGHFAKTVQKLKQLKPKMLVEALVPDFQGNSECVQKVATSGLDVFAHNIETVEELQRVVRDHRANFNQSLEVLKMAKTYSPLGVLTKTSVMLGCGETPAQVIETMEKVREAGVDVITFGQYMRPTKRHMAVSEYVTPEAFEKYQKLGMEMGFRYVASGPMVRSSYKAGEFYIKSMIEDDRKKASSSSI

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.

A9NNH7

A3QEP5

RUVC_SHELP

Holliday junction resolvase RuvC

Shewanella

MPIILGVDPGSRITGYGVIQCQGRQQIYLGSGCIRTQSDDLPSRLKVIFDGISEIIRQYQPDEFAIERVFLAKNADSALKLGQARGAAIVAATNAQLPVAEYSATQIKNAVVGTGRAQKSQVQHMVQQILKLPAAPQADAADALGVALCHFHTYQSLIAMGGKASVRTYGRYR

Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.

A3QEP5

B8H0A0

FTSI_CAUVN

Penicillin-binding protein 3

Caulobacter

MSLSNLGPGGVHSPLWRWVVERVWRLEHAFERSRAAARPEDDTRIRIFLVMGFFGFCFVGVSLGAGWSALFSRAGQGGGYAQGVEGARGDVVDRNGKLLAVDLAHYALYVDPREVWDAKETRAALGRALPQVPAKRLDKAVFGDHRAFVLGGLTPDEKDAIFNLGLPGVTFEEQERRMYPLGPTAAHLIGFVDSGGKGLAGAERALDDPIRKAAGGEGGPAQLSIDVRVQAALEDELRKAAEEFTPKGAVGLVTNVHTGEILGMASWPDYDANKAGGATDDQRLNRAAASVYEMGSTFKAFTVAIGLDTGVATAASTFDAREPYKLGYRTIHDYHATKAVLNLVEVFQHSSNIGTAMLAERVGGQRLSQYFTNLGLTKPAKVELQESARPLTPRKWDQDTVASTSFGHGMNISPLALAQAMNALLNGGEMRPLTIRKLPPGVRPEGRRVLSEHTSAEMLKIMRANVVPGEGGSGGKADVPGLSVGGKTGTGEKYDPAIRRYNHQRQVSSFAATFPTDGPLEADRYFVLILLDEPKGNANSFGFSTGGWVAAPAAGRVIERIAPFLGVKRKTELVTIANSPKNAAPEAGL

Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.

B8H0A0

A1R6G6

Y2084_PAEAT

Nucleotide-binding protein AAur_2084

Paenarthrobacter

MDEATAKSGTEQDGLTPVKPPEAELLVVTGMSGAGRSTASDALEDHGWYVVDNLPPQMLGTLAEIVSHAPKSIPKLAVVVDVRSKDLFTDIQTALGALSASGITFRVLFLDANDDVLVRRFEQGRRPHPLQGGGRILDGIGIEREVLRELREHADVVLDTSEFNVHGLATAITELFSDTGPVTLRLNVMSFGFKYGLPVDANFVADARFIPNPHWVPQLRPHTGLDEDVSDYVLGAEGVQEFVDRYVRALEPVLDGYRQENKHYATLAVGCTGGKHRSVAVAMELSKRLAQYPRVTVTTTHRDLGRE

Displays ATPase and GTPase activities.

A1R6G6

Q4KM33

PLEK_RAT

Pleckstrin

Rattus

MEPKRIREGYLVKKGSVFNTWKPMWVVLLEDGIEFYKKKSDNNPKGMIPLKGSTLTSPCQDFGKRMFVLKITTTKQQDHFFQAAYLEERDAWVRDIKKAIKCIEGGQKFARKSTRRSIRLPETIDLGALYLSMKDPEKGIKELNLEKDKKVFNHCFTGSGVIDWLVSNKLVRNRQEGLMISASLLSEGYLQPASDLSKNAADGIAENPFLDNPDAFYYFPDSGFFCEENSSDDDIILKEEFRGIIIKQGCLLKQGHRRKNWKVRKFILREDPAYLHYYDPAGGEDPLGAIHLRGCVVTSVESNPDGKKSDEENLFEIITADEVHYYMQAATAKERTEWIKAIQVASRTGK

Major protein kinase C substrate of platelets.

Q4KM33

Q5ACK7

DRS1_CANAL

ATP-dependent RNA helicase DRS1

Candida

MPDFILTIDSDEEVDVSDSEQLQDINPDFKFQIDGETTNTLEEFDFQENKVKEVDLDEIIKKKGGLKEESDDEELALDGFGMGASKQEEEEEEEEEEVEVPEVKEVVEPEDSAEAIADFYEESSPQQTHTSFQTLQLSRPVLKGIAELKFTKPTPIQSASIPIALLGKDIVAGAQTGSGKTGAYMIPIIERLLYKPSTSTKVIILTPTRELALQVYEFGKKLSHHVNNLNIGLAVGGLNLRQQEEQLKTRPDIVIATPGRLIDHIRNSPSFSVQDIQVLVIDEADRMLEEGFQDELTEILSLIPKHKRQTLLFSATMNTRIQDLIQLSLQKPVRIMIDPPKSVASKLLQQFVRIRKRDQLKPALLYQLLKGVSSRVVVFVARKETAHRLRIVLGLLGLKVSELHGALTQEQRLQNVKNFKSLEVPVLICTDLAARGLDIPKIELVINYDMPKTFEIYLHRVGRTARAGRDGTSITFVGESSQERAIVKSAIVNGKGVAKTVDWKQAEETNKLLESKESVIDEVLEEEKEAKELLRAEMELTKASNLIKHEQEIHSRPKRTWFKGEVMEQLTKHGKKVNSKKRKANEVRKDEGRSYKKTKTDRMKISNKKKSKK

ATP-binding RNA helicase involved in ribosome assembly.

Q5ACK7

Q8ZTY5

IF2A_PYRAE

eIF-2-alpha

Pyrobaculum

MRLVKKEFPDVGELVIGTVKKIAEHGAYVYLDEYDLEAFAPTQEIVQSWFHSIRDYVKEGNKTVFKVISVNPKMRVVEVSLKRVRVDEKEKKLLLYRHRVRVLKLLEIAMKKLNRPAEEALKVMWYLEEQFGDPFKVFEEVVKTGPHVLDDLQLDAKLKEIIIELARQQVELPPTKISGIIKIVSVEGDGVEKIKAALIELEKTLREKFPQISTKIYVVGPPRYRIDLTGQQPKQVEAAFSEAANILQALQKKYKVIGNIQRIEQ

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.

Q8ZTY5

Q9Y0B7

PP4C_DICDI

Serine/threonine-protein phosphatase 4 catalytic subunit

Dictyostelium

MSSDLDRQIEQLKRCEIIKESEVRALCSKAREILLEEGNVQRVDSPVTICGDIHGQFYDLKELFKVGGDCPQTNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYEECVRKYGSVTVWKYCTEIFDYLSLSALVDGKIFCVHGGLSPSINTLDQIRAIDRKQEVPHEGPMCDLMWSDPEDIPGWNGSPRGAGFLFGEDVVQKFNHDNNLEFICRAHQLVMEGFKYMFNETLVTVWSAPNYCYRCGNVAAILQLDENLKKNFAIFEAAPQESRGAPAKKPAPEYFL

Required for development, chemotaxis and the expression of numerous genes.

Q9Y0B7

A2XSX6

TIF9_ORYSI

Protein TIFY 9

Oryza sativa

MSTRAPVELDFLGLRAAAADADDRHAKSGGSSASSSSSIRGMETSAIARIGPHLLRRVIAAARPPPPPSTAPVPEEMPGAAAAAAPMTLFYNGSVAVFDVSHDKAEAIMRMATEATKAKGLARGNAIVGNFAKEPLTRTKSLQRFLSKRKERLTSLGPYQVGGPAAVGATTSTTTKSFLAKEEEHTAS

Repressor of jasmonate responses.

A2XSX6

Q5F8N2

DPO4_NEIG1

DNA polymerase IV

Neisseria

MSLRKIIHIDMDAFYASVELREQPHLKGRPVVVAWEGARSVICAASYEARQFGLHSAMSVATVKRLCPQAVYVPPHFDLYRQVSAQIHAVFRRYTDLIEPLSLDEAYLDVTRNFKNIPYAGEVAKEIRAAIFAETGLTASAGIAPNKFLAKIASDWRKPNGQFVLPPHKVMAFLETLPLGKIPGAGKVTLKKMQSLGMRTAGDLRRFERGELLNHFGRYGYRLYDLARGTDEHPVKAERERLQISTEITLPEDLPLGQAAGHLPHLAEDLWRQITRKNVEAQSVTLKLKTYDFRIITRTLTYSSVLPDCAALLQAAQMLMARVPPQTEDAFRLIGIGVGRLVPKNQQQDLWA

Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.

Q5F8N2

Q31N85

PLSX_SYNE7

Phosphate-acyl-ACP acyltransferase

Synechococcus

MTRARIAVDAMGGDFAPEEIVKGALRAQEELQADVILVGDPDRLRAICQDHAPHLQVRIEAAEEAIAMEDAAVSVRSRPRASINVAMDLVKAGEADAVISAGHSGAVMASALLRLGRIRGIDRPAIGALLPTVIPGKPVLVLDVGANVDCKPRFLEQFAVMGSIYSRDVLGQANPRVGLVNIGEEDSKGNELALASHQLLRNNPRICFVGNAEGRDVLSGQFDVVVCDGFVGNVLLKFAEAVGSVFLEIIRDELPRGMRGKVGSTLLRRNLRRIKQRLDHAEHGGALLLGVNGICIISHGSSKAPSIYSAIRLAVEAAENRVIDHLHQIQEPPSPAADLVTEPVVS

Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.

Q31N85

Q0BYA1

RL1_HYPNA

50S ribosomal protein L1

Hyphomonas

MATKGKRARAIEQTVDKTKAYSVSEAVKLVKSNAKAKFDESIEIAINLGVDPKYADQQVRSVVNLPAGTGKTIRVAVFAKDKKAEEALAAGADIVGADDLFEKVNGGFMDFDRVIATPDMMGLVGRLGKVLGPRGLMPNPKVGTVTPNVAQAVKDAKGGAVEFKVEKAGIVHAGVGKASFSDADIEKNVQAFISAVVKARPSGAKGTFVRKVTLSSTMGTGVAIDLAEAKS

Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.

Q0BYA1

O94886

CSCL1_HUMAN

Transmembrane protein 63A

Homo

MMDSPFLELWQSKAVSIREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSESRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKEKKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVLGCEWEDAISYYTRMKDRLLERITEEERHVQDQPLGMAFVTFQEKSMATYILKDFNACKCQSLQCKGEPQPSSHSRELYTSKWTVTFAADPEDICWKNLSIQGLRWWLQWLGINFTLFLGLFFLTTPSIILSTMDKFNVTKPIHALNNPIISQFFPTLLLWSFSALLPSIVYYSTLLESHWTKSGENQIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFQYEFGAMYAWMLCVFTVIVAYSITCPIIAPFGLIYILLKHMVDRHNLYFVYLPAKLEKGIHFAAVNQALAAPILCLFWLYFFSFLRLGMKAPATLFTFLVLLLTILVCLAHTCFGCFKHLSPLNYKTEEPASDKGSEAEAHMPPPFTPYVPRILNGLASERTALSPQQQQQQTYGAIHNISGTIPGQCLAQSATGSVAAAPQEA

Acts as an osmosensitive calcium-permeable cation channel . Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion .

O94886

B6J1Y7

RNH_COXB2

Ribonuclease H

Coxiella

MAKQEQNIVYLYCDGACRGNPGPGGWGVLLRYNQHERQLHGGVANTTNNQMELTAAIEGLKSLKKPCQVVVTTDSQYLRRGITEWLPVWKRRGWRTSNKKPVKNQPLWETLEREVERHTIVWHWVKGHSGHAENEIADELANRGIDEVLKRGAQ

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.

B6J1Y7

Q6GBS6

SDRC_STAAS

Serine-aspartate repeat-containing protein C

Staphylococcus

MNNKKTVTNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSENKTTEKVDSRQLKDNTQTATADQPKVTMSDSATVKETSSNMQSPQNATASQSTTQTSNVTTNDKSSTTYSNETDKSNLTQAKDVSATPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHLNKDTGKTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTTTYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEVSLGNDTYSEEIIVDYGNKKAQPLISSTNYINNEDLSRNMTAYVNQPKNTYTKQTFVTNLTGYKFNPNAKNFKIYEVTDQNQFVDSFTPDTSKLKDVTNQFNITYSNDNKTATVDLMNGQTSSNKQYIIQQVAYPDNTSTDNGKIDYTLDTDKTKYSWSNSYSNVNGSSTANGDQKKYNLGDYVWEDTNKDGKQDANEKGIKGVYVILKDSNGKELDRTTTDENGKYQFTGLSNGTYSVEFSTPAGYTPTTANAGTDDAVDSDGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKGVKVTLQNEKGEVIGTTETDENGKYRFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDTDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDADSDTDSDSDAGKHTPAKPMSTVKDQHKTAKALPETGSENNNSNNGTLFGGLFAALGSLLLFGRRKKQNK

Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion.

Q6GBS6

B6I7J7

ARNC_ECOSE

Undecaprenyl-phosphate Ara4FN transferase

Escherichia

MFEIHPVKKVSVVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSIIAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKENE

Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.

B6I7J7

Q9ZKB1

6PGL_HELPJ

6-phosphogluconolactonase

Helicobacter

MGYQLFEFENLEDCHKALIERFKEFFNAALKKHHQVSVAFSGGRSPISLLQKLSVLDLKWHECLISLVDERIIEASHEDSNAKLLHDYLLQNNALKASFTPLLPEKISGDTNELLDFANQHFKQPHLAILGMGTDGHTASLFPETSAFLNEEKENIVLTKPTNAPYERLSMSINALENCEKLFLSISGVEKRGVLEKALKENAPYSLPIARILHSKKVTTEVFYAKN

Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.

Q9ZKB1

Q8P243

PCP_STRP8

Pyroglutamyl-peptidase I

Streptococcus

MKILITGFDPFGGEAINPALEAIKKLPATIHGAEIKCIEVPTVFQKSADVLQQHIESFQPDAVLCIGQAGGRTGLTPERVAINQDDARIPDNEGNQPIDTPIRADGKAAYFSTLPIKAMVAAIHQAGLPASVSNTAGTFVCNHLMYQALYLVDKYCPNAKAGFMHIPFMMEQVVDKPNTAAMNLDDITRGIEAAIFAIVDFKDRSDLKRVGGATH

Removes 5-oxoproline from various penultimate amino acid residues except L-proline.

Q8P243

P60209

KAX94_HOTTA

BTK-2

Mesobuthus

VGCAECPMHCKGKMAKPTCENEVCKCNIGKKD

Blocker of human voltage-gated potassium channel Kv1.1/KCNA1 .

P60209

C6L862

AHLL_MICTS

N-acyl homoserine lactonase

Microbacterium

MILAHDVSGSGPLLVLLHGITEDRRSWDPVDFTDGFTVVRVDLRGHGASAAEEPYDIPTLATDVHDTLAQLAENDVIPGELPVIVGHSMGGIVATAYGALFPARAIVNVDQPLQLAGMQGQVQQAEGMLRGADFPLFIHGMFAQMAGGLDAEELARVNGIRSPRQDVVLGMWRPLLEDSPEELAALVSGLTRIPEDVPYLVITGLDAGPEYAAWLQREIPQAVQEVWQPPTHYPHLVDPARFVERVEAFVR

Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3. Has slight activity towards L-homoserine lactone, and no activity towards gamma-butyrolactone.

C6L862

Q6YPI8

ACP_ONYPE

Acyl carrier protein

Candidatus Phytoplasma asteris

MVFEKIKALIATQLSLDASTITLDTRFKEDLGLDSLDALELVMEVEKTFQINISDATLQNFKTVQDIVFYITKNTP

Carrier of the growing fatty acid chain in fatty acid biosynthesis.

Q6YPI8

Q07532

IWR1_YEAST

Interacting with RNA polymerase II protein 1

Saccharomyces

MSTISTTTAPEFIRVKRRRDEDSVQALLIDEGKRVKKQKFIFKLSKTVSSESYQSEQESSTPLLKLAHEDHRHFVLEQRKKSRRDSDDEKSQQRLAAEGSTVDDDGLPPEINQMVNDYLKLNKGVEKTERKKPSRKYFTGDSAKIASLPSLDYVFDIYHLEKIHDDEVARYNNEKNIGFVKIIEHIDLALDEESDPNEARSDDEDSNDENYYQNDYPEDEDDDRSILFGSEGEDIAALGEEIVIGVNKSRFSSWNDDKIQGSNGYHDVEEEYGDLFNRLGGKSDVLKSINSSNFIDLDGQEGEIEISDNEDDSDEGDDIEYPRNEFFPTDVDDPLAHHRDRIFHQLQKKINRS

Directs RNA polymerase II nuclear import. Binds RNA polymerase II in the active center cleft between the two largest subunits in the cytoplasm. Then uses an N-terminal bipartite nuclear localization signal that may be recognized by karyopherin alpha to direct the polymerase II complex nuclear import. In the nucleus, is displaced from polymerase II complex by transcription initiation factors and nucleic acids, enabling its export and recycling.

Q07532

P56833

MRAY_STRCO

UDP-MurNAc-pentapeptide phosphotransferase

Streptomyces albidoflavus group

MKQILFAGVIGLFLTLVGTPLLIKLLARKGYGQYIRDDGPREHASKRGTPTMGGIAFILATVAAYFLAKGITSYLDPDIDAGPTFSGLLVLGLMVGMGLVGFLDDYIKIVKRRSLGLRARAKMIGQLTVGIAFAVLSLQFADNRGNTPASTKLSFITDFGWTIGPVLFVVWALFMILAMSNGVNLTDGLDGLATGASVLVFGAYTFIGVWQFQESCANALTLTNPGACYEVRDPLDLAVVASALMGSCLGFLWWNTSPAKIFMGDTGSLALGGVLAGLAICSRTELLMAILGGLFVLITMSVVIQVGSFRLTGKRVFRMAPLQHHFELKGWSEVLVVVRFWIIQGICVIVGLGLFYAGWATDK

Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.

P56833

A0A0R4I987

CDII_YERPY

Immunity protein CdiI-YPIII

Yersinia

MNDIVKSAWASVKMNTDFICVDTYSGYRSNQLDPLGVQHLSSPDVSDLDLGEMVKDALSHSRFVLPAPRTDIWIHPEVTFDLDLYDSRRTVERYDEWVKKLMVHYGYKTKRALFKDMKSCDICCNHDAITISPTRHEKLEVWGGTGLKGSDNVILSVDSSPTEIGAGLRLALSRCKG

Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Neutralizes the toxic activity of cognate toxin CdiA-YPIII (residues 954-1077). Does not inhibit toxic activity of CdiA from other toxin-immunity modules.

A0A0R4I987

O55208

FIGLA_MOUSE

Transcription factor FIGa

Mus

MDTAPASPEPFLVTPQAEVLEELIQAQMGPLPRLAAICRLKRLPSGGYSTTDDLHLVLERRRVANAKERERIKNLNRGFAKLKALVPFLPQSRKPSKVDILKGATEYIQILGCVLEEAKVSEKQSPEEQTHSGRPSDPHVSSTRELLGNATQPTSCASGLKKEEEGPWAYAGHSEPLYSYHQSTVPETRSYFTH

Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters.

O55208

Q6AAU3

GLYA_CUTAK

Serine hydroxymethyltransferase

Cutibacterium

MSDPRAVDPTARDIAEKLAPAYRTMLDAIAQVEPRIAEATRAELTDQRHSLKLIASENYASLPVLATMGTWFSDKYAEGTAGHRFYAGCQNVDTVETIAAEHACALFGAEHAYVQPHSGIDANLTAYWTILAHHIETPALSEFGARTVNDLTQVDWDTLRHRFNDQRAIGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPQTGLLDYDKVAELAREFKPLVIVAGYSAYPRRVNFAKMREIADEVGAVLMVDMAHFAGLVAGKVFTGDENPIPHAQVVTTTTHKSLRGPRGGMVLTTKDYADDVDRGCPMVLGGPLSHVMAAKAVALAEARTQTFRDYAQRVANNAKALAEGLMKRGVKLVTDGTDNHINLLDVTTSFGLTGRQAEAALLDAGVVTNRNSIPTDPNGAWYTSGIRIGTPALTSRGFGPDEFDQVAELIVTTLEATTPMTASTGKPGKAKYQIADGVAQKVHDAADELLGNFPLYPGLDLA

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.

Q6AAU3

Q0HEW2

MDH_SHESM

Malate dehydrogenase

Shewanella

MKVAVLGAAGGIGQALALLLKTQLPAGSQLSLYDIAPVTPGVAVDLSHIPTAVEIKGFAGEDPTPALVGADVVLISAGVARKPGMDRSDLFNINAGIVRNLIEKVAVTCPKALVGIITNPVNTTVAIAAEVLKKAGVYDKNRLFGVTTLDVIRSETFIAELKGLNVADVKVNVIGGHSGVTILPLLSQVEGVTFSDEEVASLTKRIQNAGTEVVEAKAGGGSATLSMGQAACRFGMSLVRGLQGEANIVECAYVDGGSEHAEFFAQPVLLGKNGIEKVLPYGEVSAFEANARDSMLDTLKGDIKLGVDFVK

Catalyzes the reversible oxidation of malate to oxaloacetate.

Q0HEW2

C6DGY3

CLSA_PECCP

Cardiolipin synthase A

Pectobacterium

MSTFYTVISWLLVFGYWLLIAGVTLRILMKRRAVPSAMAWLLVIYILPLVGIVAYLSFGELHLGKRRAERASKMWPSTAKWLRELKEYRRIFATENSEVASALFQLCERRQGVGGVKGNQLQLMTTFDDTIKALLRDIELARSNIEMVFYIWQPGGLVEQVSSSLIAAARRGVHCRILLDSAGSVQFFRQHHPELMRTAGIEVVEALKVNLFRAFLRRMDLRQHRKIILIDNRIAYTGSMNMVDPRFFKQDAGVGQWIDLMARIEGPVATTLGIIYCCDWEMETGKRLLPPPPDVNVMPFEQESGHTIQVIASGPGYPEEMIHQALLTSVYSARKQLIMTTPYFVPSDDLLHAICTAAQRGVDVSIIVPHKNDSVLVGWASRAFFTELLAAGVKIYQFKDGLLHTKSVLVDGQLSLVGTVNLDMRSLWLNFEITLVIDDAGFGSDLACVQEDYIARSRLLNATQWQNRPYWQRIVERLFYFFSPLL

Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.

C6DGY3

B2A4D5

RS7_NATTJ

30S ribosomal protein S7

Natranaerobius

MSRKGPAPKRDVNPDPIYNSKMVTKFINKLMLDGKKGLSQRIFYKALELVGERTNEEPLEVFETAVKNVMPVLEVKARRVGGATYQVPVEVEPNRKQVLAIRWIVNYARERGERAMSERLAGELIDAYNNTGGAIKKKEDTHKMAEANKAFAHYRW

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.

B2A4D5

A0PJR5

ECHD3_DANRE

Enoyl-CoA hydratase domain-containing protein 3, mitochondrial

Danio

MLLRGFSELLKCRGVMMKMRMKMSGDSSSLTLTEQQGGIRRIILNNPRKRNALSLQMLESLRENILTDADNPELHVIIISAVGPVFSSGHDLQELSSAEGSDLPRRVFHSCSELMMLIQDLPVPVIAMVNGVATAAGCQLVASCDVAVASEKSTFATPGVNVGLFCSTPAVAIGRTVPRKIAMQMLLTGRPLSAQQALQHGLLSAVFSEERLEDETLAIARRVCESSRPVVSLGKQIFNTQMSQSRDAAYSTAGAAMLDNLRLRDGQEGIRAFLEKRKPVWSNTDDCIH

May play a role in fatty acid biosynthesis and insulin sensitivity.

A0PJR5

A7N2Q0

BETB_VIBC1

Betaine aldehyde dehydrogenase

Vibrio

MDMKAHYIDGAMHLGCSEEHFTTYNPANGEPLANVKQANQQDMQAAIESAKRGFAIWSAMTATERSRILLKAVALLRERNDELAALEVADTGKPIQEANCVDIATGADVIEYYAGLAPSMHGEQQPLNESQFFYTRREPLGICAGIGAWNYPIQIAMWKSAPALAAGNAMIFKPSEETPLTALKLAEIYSEAGLPDGVFNVIQGDYRVGQMLTAHPDIAKVSFTGESGTGKVVMGDSAATLKQVTMELGGKSPMIIFDDAKLDDAVSAAMVANFYTQGEVCTHGTRVFVHEGIYDEFVVQLKKRTELLVVGDPLDEQTQIGALISKEHESKVLSAIEQAKASKATLLTGGYKVTENGLASGNFVVPTVFIDCEDDMPHVQQEIFGPVMSVLKFSDEDEVIARANNTDYGLAAGVFTQNLSRAHRVIHQIQAGICWINTWGDSPAEMPVGGYKLSGIGRENGVETLTHYTQTKSVLVHLGDFDSPYA

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.

A7N2Q0

P08228

SODC_MOUSE

Superoxide dismutase [Cu-Zn]

Mus

MAMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

P08228

P33711

SOMA_CANLF

Growth hormone

Canis

MAASPRNSVLLAFALLCLPWPQEVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF

Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

P33711

B5YKP5

MTIP_THEYD

5'-methylthioinosine phosphorylase

Thermodesulfovibrio

MHNKQQVKIGIIGGSGLSESEAKKEIITIKTPYGEPSCPYEIEKIDDIEVLFLRRHGQKHSIPPHKVNYRANIYGFKNFGIERIFGVFATGSLTENIPPGSIVIPNQIIDFTQGMRANTFYEEKKVVHIDFTEPFCSEIRHYLLETARKIGINVISHATYICVNGPRLETAAEIKFFKNIGADIIGMTIMPEASLAREVEICYAAVAVVANYAAGISKFPLTVKEVIETMEDSLDAVGFLIKETIKKLPEERKCLCKHALKNASF

Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.

B5YKP5

A5WGS6

TGT_PSYWF

tRNA-guanine transglycosylase

Psychrobacter

MQFTLHKTAAGESRARRGTVTVNHGEIRTPAFMPVGTYGTVKGMLPRDIEDIGADIILGNTFHLWLRPGTEVIDKFGGLHQFMNWNKPILTDSGGFQVFSLGAMRKITEEGVAFKSPIDGAKVFLSPEKSMQIQYSLNSDIVMQFDECTPYPATYSEAQKSLELSLRWGQRCVDEHKKLGNTNALFGIVQGSMYEDLRRQSMDGLLEIGFDGYAIGGLSVGEPKEEMISVLNYMPELMPADKPRYLMGVGKPEDILEAVRRGVDMFDCVMPTRNARNGHYFVTGNEDNQGIVRIRNSQYREDQGPLDPECDCYCCQNFSRAYLYHLNKCKEMLGAQLATIHNLRYYQRLMQGIRDAIDEDRFDEFVADFYHRRGQDVPPLELK

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

A5WGS6

O78516

FTSH_GUITH

ATP-dependent zinc metalloprotease FtsH

Guillardia

MKISWKNILLTLIPLGLISFLVWQGFNNTTNPQFTKNIASSRMTYGRFLEYLDLGWVKKVDLYDEGHTAIVEAIGPELGNRIQRIRVELPATAPELITKLRKANVDLDAHATNDSTPAWSLIGNLIFPILLIAGLAFLFRRSSNLPGGPGQAMNFGKSKARFQMEAKTGVTFNDVAGVDEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENSPCIVFIDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGIIIIAATNRVDVLDAALLRPGRFDRQVTVDVPDVKGRLEILNVHARNKKLDLSISLELIAKRTPGFSGADLANLLNEAAILTARRRKKQITISEIDASIDRVIAGMEGKALVDSKTKRLIAYHEVGHAIIGTLLKHHDPVQKVTLVPRGQAKGLTWFTPSEDQSLISRSQILARIMGALGGRAAEEVVFGLPEVTTGAGNDLQQVTSMARQMVTRFGMSNIGPLSLESQNSDPFLGRTMGSSSQYSEDIASRIDMQVRAIIQHCHTETVQIIKDNRVVIDKLVDLLIEKETIDGDEFRQIVGDFTSLPEKIDYKSQLKST

Acts as a processive, ATP-dependent zinc metallopeptidase.

O78516

O62327

GPX2_CAEEL

Glutathione peroxidase 2

Caenorhabditis

MASVHGITVKNAQGEDTPLSNYQGKVLIIVNVASQCGLTNSNYNQFKELLDVYKKDGLEVLAFPCNQFGGQEPSCEIDIAAFVADKFKFEPTLFQKIDVNGDNTAPLYKFLKQEKGGFLVDAIKWNFTKFLVGRDGHVIKRFSPTTEPKDMKKDIEAALQAKL

May constitute a glutathione peroxidase-like protective system against oxidative stresses.

O62327

Q6S5L9

SHC4_MOUSE

Src homology 2 domain-containing-transforming protein C4

Mus

MRERSQDSQAGLTLYVGLFGHLGMLHRTKYSRFRNESITSLDEGSPGGSVGNKGSSPPPYPALAPHLPTEDATVSSQESPTALCTLIPRMASMKLANPITFLGLKTFCLGTKQVSRLKLQENQDQTPSRPASPESNLNRTGPAPAPDPDQVGRRPTSLRPDTCPLPGPGEPSPRSKQDGPPLQHLLGNGLNYCVRYMGCIEVLQSMRSLDFGMRTQVTREAISRLCEAVPGAHGAIKKRKAPVKFLTTVLGKSNLQFSGMNIKLTVSTSSLTLMNLDNQQIIANHQMQSISFASGGDPDTTDYVAYVAKDPVNQRACHILECRSGMAQDVISTIGQAFELRFKQYLKNPSLNTWEREEVLVDGAPEDRDHDYYNSIPGKQPPEGGISDVRIQAQATDQMAYCPIRCEKLCYLPGNSTCSGVYKNCMGRSRPIGIPHERAGQGDTPSLRHFWRVDLFDDPCYVNTQALQSMHSYAGNQSSALPQGSPWHLGKAPETVQPGATAKPGSALALPHIRQQLWDEECFHGKLSRGAAEKLLVKDGDFLVRESVTSPGQFVLSGLQGGQAKHLLLVDPEGKVRTKDHVFDNVGHLIKYHMDNNLPIISSGSEVRLKQPIRKYDNTGLLPPKK

Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1.

Q6S5L9

B0SA31

RL18_LEPBA

50S ribosomal protein L18

Leptospira

MINKTAKNTKRLRRAERVRYKLRQTSERPRLVFNKTNRYLTAQIIDDAKGVTLVYATTLEKDFPKHENSKKSKSAATELGKVVADKAKKAGVSQVVLDRSGMVYHGRIAAFADSAREGGLEF

This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.

B0SA31

Q9UJ71

CLC4K_HUMAN

Langerin

Homo

MTVEKEAPDAHFTVDKQNISLWPREPPPKSGPSLVPGKTPTVRAALICLTLVLVASVLLQAVLYPRFMGTISDVKTNVQLLKGRVDNISTLDSEIKKNSDGMEAAGVQIQMVNESLGYVRSQFLKLKTSVEKANAQIQILTRSWEEVSTLNAQIPELKSDLEKASALNTKIRALQGSLENMSKLLKRQNDILQVVSQGWKYFKGNFYYFSLIPKTWYSAEQFCVSRNSHLTSVTSESEQEFLYKTAGGLIYWIGLTKAGMEGDWSWVDDTPFNKVQSVRFWIPGEPNNAGNNEHCGNIKAPSLQAWNDAPCDKTFLFICKRPYVPSEP

Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.

Q9UJ71

Q9W5B6

MTU1_DROME

Mitochondrial tRNA-specific 2-thiouridylase 1

Sophophora

MIRNVVVGVSGGVDSAVSAHLLAEQGFKVLGVFMRNWDEADEVGRCSGEADLKDAEWACRQLGVELRQVNYVREYWTAVFSQFLDDYQMGLTPNPDILCNRHIKFDLFHKHALENLGYDAVATGHYARNSLGNYLEGIASNNDARLLIPADTFKDQTFFLAGISRKALQRTMFPLGDFQKSQVKDLAKKIGFQRLAKKKESTGICFVGKRNFKDFIQEYITSKRGPFLDIDSGAVVGHHEGIHQWTVGQRCRLSSFLQPYFVARKEAASNTIYVASGHNHPALLSTHIAVDPPNWLCSKSQQILSDTGSLRCRFRFQHTKPLVDCQLSISPSNTFLVELDAPLRAITPGQYAVFYDDTACLGSARILSANPLKKKNAQTQQAQAANLVS

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.

Q9W5B6

A5IN99

PANC_THEP1

Pantoate-activating enzyme

Thermotoga

MKIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARDENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRKLLEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKVKIDYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTILG

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.

A5IN99

Q10133

RHO2_SCHPO

GTP-binding protein rho2

Schizosaccharomyces

MLQSQPIRRKLVVVGDGACGKTSLLSVFTLGYFPTEYVPTVFENYVSDCRVDGKSVQLALWDTAGQEEYERLRPMSYAKAHIILVGFAIDSPDSLENVSTKWIEEINTLCPNVPFILVGMKADLRSDPVAIEEMRRRNQNFVKSQQAELVAQRIGARKYMECSSLTGDGVDDVFEAATRAALTVRDSENDKSSTKCCIIS

Involved in cell morphogenesis, the maintenance of growth direction, control of polarity and of cell wall integrity. Regulates the synthesis of alpha-D-glucan through activation of pck2.

Q10133

Q8R6T8

PURA_CALS4

IMP--aspartate ligase

Caldanaerobacter

MSVTVIVGAQWGDEGKGKITDYLAERSEVVVRYQGGNNAGHTVEKDGVQYKLHLIPSGILYPDKICVIGNGVVVDPSALLKEIEDLKAKGVEVKEDNLKISDRAHVVFPYHIKEDELEEKGKGDEDLGTTKKGIGPCYRDKTERIGIRMCDLMNAEVFREKLKKNLERKNKIFKDIYGEDGFDFEQIFETYREYAERLRPYVTDTSVLLYNLAKEGKKILFEGAQGTLLDLDFGTYPYVTASHPVAGGATIGAGIGPTMIDNVIGVVKAYTTRVGKGPFPTELKDEIGDFLREKGYEYGTTTGRPRRCGWIDIVMLRYAVRVSGITSLALTKLDTLTGLEKIKICTGYKINGKIIEDFPASLEELKMCEPIYEEMEGWSENIQDVRSFEDLPLNAKKYVKRLEELVGVEFSIISVGPEREETIVLRNF

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Q8R6T8

Q67PR8

RPOZ_SYMTH

Transcriptase subunit omega

Symbiobacterium

MIKPSLDQLMHLVDSKYTLVILAARRARDLQDGKHQMVESKSNKPVTIALEELAAGKLFFERGKPTPLG

Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.

Q67PR8

P02163

MYG_ROUAE

Myoglobin

Rousettus

MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGQHEAQLKPLAQSHATKHKIPVKYLEFISEVIIQVLQSKHPGDFGADAQGAMGKALELFRNDIAAKYKELGFQG

Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

P02163

Q6LU31

GUAA_PHOPR

Glutamine amidotransferase

Photobacterium

MTTSTNIHDQRILILDFGSQYTQLIARRIREIGVYCELWSWDVDEADIRDFNPNGIILSGGPESVTGDESPRAPQYVFEAGVPVFGVCYGMQTMAEQLGGKVAGSSMREFGYAQVEIVEPTSFFKNIEDAVAEDGNGLLDVWMSHGDKVVEIPSDFVKVAQTDTCPFAAIANEEKHFYGVQFHPEVTHTRQGMRIIENFVLNICGCENLWTSANIIEDAIANIKEQVGDDEVILGLSGGVDSSVVAMLLHRAIGDKLTCVFVDNGLLRLNEGEQVMDMFGDHFGLNIVHVKAEDRFLNALAGENDPEAKRKIIGHAFIDVFDEESKKLKNAKWLAQGTIYPDVIESAASKNGKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHSADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVDGISRVVYDISGKPPATIEWE

Catalyzes the synthesis of GMP from XMP.

Q6LU31

Q88PD5

SODF_PSEPK

Superoxide dismutase [Fe]

Pseudomonas

MAFELPPLPYAHDALQPHISKETLEYHHDKHHNTYVVNLNNLVPGTEFEGKTLEEIVKSSSGGIFNNAAQVWNHTFYWNCLSPNGGGQPTGALADAINAAFGSFDKFKEEFTKTSVGTFGSGWGWLVKKADGSLALASTIGAGCPLTSGDTPLLTCDVWEHAYYIDYRNLRPKYVEAFWNLVNWAFVAEQFEGKTFKA

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Q88PD5

P42111

YXAL_BACSU

Uncharacterized protein YxaL

Bacillus

MVKSFRMKALIAGAAVAAAVSAGAVSDVPAAKVLQPTAAYAAETVFSQNNGASGFLPGRYDVQAMAPAMFNWSRESRFAGNTDGTLKWQNDIRTTPQNGAGAVIDGDGTVYLHSRDGEMKAFNPDGSVKWVTGNLGKTYTQSPVLGTNGVIYLASYDKKIYFIDKETGEILTTVPLSGGPSSETVIGSDGTLYFSTLDNYVHAIKPTSKSTWTERWKLKTNGVVSSVPVLAKNGTVYVGTYNYVFYAINSGTGQVKWSRTTSNAFKGYPVIDKDGNIYAGNQDGQLYAYTSTGSLKWTFPLNGFSSSSPAIDHNGNIYIGSGSGELFSISKNGDMNWSFYTDGPVRTAPLIDAKGTVYFGSDDMKVYAADANGNELWSYQTDSNVVSSPQLAEDGTLYIGSYTKLMAFGK

Increases the processivity of the PcrA helicase, but does not bind to DNA.

P42111

A4W7Z0

MTNK_ENT38

Methylthioribose kinase

Enterobacter

MSQYRTFTAQDAVEYAKQFGGLDNPSSLVEAQEIGDGNLNLVFKIFDAQGVSRIIVKQALPYVRCVGESWPLTLDRARLEAQTLVEHYQHSPQHTVKIHHYDPELAVMVMEDLSSHKIWRGELISGVYYPQASRQLGEYLAHTLFHTSDFYLHPHAKKAQVAKYINPEMCEITEDLFFNDPYQIHERNNYPAELEADVAALRSDDQLKIAVASLKHRFFSQAEALLHGDIHSGSIFVAEDSLKAIDAEFGYYGPIGFDIGTAIGNLLLNFCGLPGHLGIRDAAAAREQRLTDIQELWNTFSERFQALATEKTRDAALSVPGYASQFLKKVWTDAIGFCGTELIRRSVGLSHVADIDTIKDDAMRHECLRHAITLGKALIVIADRIDSAEALVARVRQYS

Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.

A4W7Z0

Q8U1R2

PANB_PYRFU

Ketopantoate hydroxymethyltransferase

Pyrococcus

MREITPKRIMEMKGKEKITMITAYDYPSALLADKAGFDIVFVGDSLGMVVYGEQNTLNVTMDQMIFHTRAVAKAVKRALVLADMPFGSYEVSVEEGVKNAIKLIQAGADAVKIEGGYDHRKLVKKLVRMGIPVMGHTGLTPQRYLRLGGYRIMGENEEEVEEILRDAKALEKAGAFAVVLEFVLADVAKLVTEEVSIPTIGIGSGPYVDGQVLVWHDVLGLYESSPPFAKRYANLREEILRAISEFRKEVKEGKFPGKEHYWEYQDKETFNRIKENVMRKLRL

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.

Q8U1R2

Q5L3Z4

RL2_GEOKA

50S ribosomal protein L2

Geobacillus thermoleovorans group

MAIKKYKPTSNGRRGMTVLDFSEITTDQPEKSLLAPLKKKAGRNNQGKITVRHQGGGHKRQYRIIDFKRDKDGIPGRVATIEYDPNRSANIALINYADGEKRYIIAPKNLKVGMEIMSGPDADIKIGNALPLENIPVGTLVHNIELKPGRGGQLVRAAGTSAQVLGKEGKYVIVRLASGEVRMILGKCRATVGEVGNEQHELVNIGKAGRARWLGIRPTVRGSVMNPVDHPHGGGEGKAPIGRKSPMTPWGKPTLGYKTRKKKNKSDKFIIRRRKK

One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.

Q5L3Z4

Q5YXQ1

MAIA_NOCFA

Maleate cis-trans isomerase

Nocardia

MGIRRIGLVVPSSNVTVETEMPALLSRHPGAEFSFHSTRMRMHTVSPEGLAAMNAQRERCVLEIADAAPEVILYACLVAVMVGGPGEHHRVESAVAEQLATGGSQALVRSSAGALVEGLRALDAQRVALVTPYMRPLAEKVVAYLEAEGFTISDWRALEVADNTEVGCIPGEQVMAAARSLDLSEVDALVISCCVQMPSLPLVETAEREFGIPVLSAATAGAYSILRSLDLPVAVPGAGRLLRQDSAVTAS

Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Shows a strict specificity for maleate, with no activity detected toward structurally related substrates including citraconate, mesaconate, dimethylmaleate, and maleamide.

Q5YXQ1

Q9C8H0

AB12C_ARATH

Multidrug resistance-associated protein 13

Arabidopsis

MGFEALNWYCKPVADGFWEKAVDGAFGAYTPCAIDSLVMLVSHFVLLGLCFYRIWIIFHNTKAQIYVLRKKYYNCVLGLLACYCVVEPVLRLVMGISLFDMDEETDFPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEFRWYVRFGVLYVLVADAVLLDLVLPLKNSINRTALYLFISSRCSQALFGILLLIYIPELDPYPGYHIVNNEPLDNVEYDALRGGEHICPERHASIFSRIYFGWITPLMQLGYRKPITEKDVWQLDKWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGGRFWLAGIFKIGNDLSQFVGPVILSHLLRSMQEGDPAWVGYVYAFIIFVGVTLGVLCEAQYFQNVWRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQISQQLHGLWSAPFRIIVSMILLYQQLGVASLFGSLILFLLIPLQTLIISKMRKLTKEGLQWTDKRVGITNEILSSMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTVVSFGVFVLLGGDLTPARAFTSLSLFAVLRFPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGTPAISIKNGYFSWDSKTTKPTLSDINLEIPVGTLVAIVGGTGEGKTSLISAMLGELSHAETTSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDATALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVAHQVFDSCMKDELRGKTRVLVTNQLHFLPLMDKIILVSEGMIKEEGTFVELSKSGILFKKLMENAGKMDATQEVNTNDENILKLGPTVTVDVSERNLGSTKQGKRRRSVLIKQEERETGIISWNVLMRYKEAVGGLWVVMILLACYLATEVLRVSSSTWLSIWTDQSTSKNYSPGFYIVVYALLGFGQVAVTFTNSFWLITSSLHAARRLHDAMLSSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLQNGNTNNQAGFASTMGLLLSYTLNITSLLSGVLRQASRAENSLNSVERVGNYIDLPSEATDIIENNRPVCGWPSGGSIKFEDVHLRYRPGLPPVLHGLTFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEVEKGRIMIDDCDVAKFGLTDVRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAGLWEALHRAHIKDVISRNPFGLDAEVCEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLSNLVFERRENGMSVGG

Pump for glutathione S-conjugates.

Q9C8H0

B0KDB8

ADDB_THEP3

ATP-dependent helicase/nuclease AddB

Thermoanaerobacter

MGIRFIYGRAGTGKTYFCLREIKEKINDGNSHPLILLVPEQFTFEAEKYLLETVEKDRKMRAQVLSFKTLANRVFTEVGGLTRQHVNSCGRSMVIYKIMEDLKENLKVYYKASRQQGFIKKISEVITEFKRFEVTPEKLMDTAESIQKEGLREKLRELSLIYGKFDELLHQKYIDEEDALTLLAEKLEYSEQFKGAEFWIDGFTGFTPKQYKVLEKLLKKAARVSVTLTMDTSKDSIDNTDLFYTTKKTEDKLLKICYENNISYEKPVDLNEGVPKRFEKNEEMAFLEKHLFSYPYKIYSKDTKNISLFKAVNVYSEVEETAREIIRLVRDENLRYSDIVVTARDLKRYHKLIKTIFSHYGIPHFIDLKLDIKNNPIIVYITSLFEIYLKNWSYESVFRHLKTGFTNLNKEDISFLENYVLANGIKGGKWKEEWKYSFRNRLDKLFDDQDEKEALEKVNTIKNGISEPLNKFYKDFSNANTVREACEILYNFLVERDIPQRIENLIREFKENKEFEIANQYSQIWDIVVDVLDQMVEVMGEEKINIDLFSKILDIGFEAYQIGSIPPALDEVLVTSVDRMKSHNAKALFVIGANDGIFPASSFEEGILTDEDRQILTSYEVELDRDTKAKVFEEQFLVYTALTSTSKFLRISYPIADHEGRSLRPSIIISRFKRIFPQITQFSNVIEMDTDEENLHRVSSPDPTFNEMIKSFKEWDIKDKINSLWLDVYNWYSNKEVWRKRIEKVLEGFNYSNQVRVIPSAKIKRLYKDEINFSVSRLEKYAACPFAYFVQYGLKAKERKIYSFDPPDLGIFMHNVLNEVSKALEKEDKTWEDLDREYCDEVVNIVVDNMLKGVSEHILKSSPRYEYLSKRLTRVLSNAVWVISEHIKRSSFIPSGHEVAFGENQMYPPIKIILSNGEEINLIGRIDRVDVFEKGEESYIRIIDYKSGNKELKLEDVFYGLELQLLIYLDAILESADKENTDIKPAGIFYFRIDDPIVKADKDITDEELQKEILKKLRLDGLVLKDAEIIKEMDKSINGTSYIIPASINKDGTIGKKTKGATKEQFELLRKHVKNMIKDLAEQMINGNISITPYRKGKETACKYCPYSSVCKFETNFEGNKYMFIKEQKEEEIWNMLQKEVNKDGDKVD

The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.

B0KDB8

Q26972

SEM1A_TRICF

Semaphorin-I

Tribolium

MVVKILVWSICLIALCHAWMPDSSSKLINHFKSVESKSFTGNATFPDHFIVLNQDETSILVGGRNRVYNLSIFDLSERKGGRIDWPSSDAHGQLCILKGKTDDDCQNYIRILYSSEPGKLVICGTNSYKPLCRTYAFKEGKYLVEKEVEGIGLCPYNPEHNSTSVSYNGQLFSATVADFSGGDPLIYREPQRTELSDLKQLNAPNFVNSVAYGDYIFFFYRETAVEYMNCGKVIYSRVARVCKDDKGGPHQSRDRWTSFLKARLNCSIPGEYPFYFDEIQSTSDIVEGRYNSDDSKKIIYGILTTPVNAIGGSAICAYQMADILRVFEGSFKHQETINSNWLPVPQNLVPEPRPGQCVRDSRILPDKNVNFIKTHSLMEDVPALFGKPVLVRVSLQYRFTAITVDPQVKTINNQYLDVLYIGTDDGKVLKAVNIPKRHAKALLYRKYRTSVHPHGAPVKQLKIAPGYGKVVVVGKDEIRLANLNHCASKTRCKDCVELQDPHCAWDAKQNLCVSIDTVTSYRFLIQDVVRGDDNKCWSPQTDKKTVIKNKPSEVENEITNSIDEKDLDSSDPLIKTGLDDDSDCDPVSENSIGGCAVRQQLVIYTAGTLHIVVVVVSIVGLFSWLYSGLSVFAKFHSDSQYPEAPFIEQHNHLERLSANQTGYLTPRANKAVNLVVKVSSSTPRPKKDNLDVSKDLNIASDGTLQKIKKTYI

Plays a role in growth cones guidance.

Q26972

P39683

NPT1_YEAST

Nicotinate phosphoribosyltransferase

Saccharomyces

MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKFSKIICYSDSLNVEKAITYSHAAKENGMLATFGIGTNFTNDFRKKSEPQVKSEPLNIVIKLLEVNGNHAIKISDNLGKNMGDPATVKRVKEELGYTERSWSGDNEAHRWT

Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate . Essential for growth under anaerobic conditions .

P39683

P0AD98

LIVJ_ECO57

Leu/Ile/Val-binding protein

Escherichia

MNIKGKALLAGCIALAFSNMALAEDIKVAVVGAMSGPVAQYGDQEFTGAEQAVADINAKGGIKGNKLQIVKYDDACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLILRTTGLDSDQGPTAAKYILEKVKPQRIAIVHDKQQYGEGLARAVQDGLKKGNANVVFFDGITAGEKDFSTLVARLKKENIDFVYYGGYHPEMGQILRQARAAGLKTQFMGPEGVANVSLSNIAGESAEGLLVTKPKNYDQVPANKPIVDAIKAKKQDPSGAFVWTTYAALQSLQAGLNQSDDPAEIAKYLKANSVDTVMGPLTWDEKGDLKGFEFGVFDWHANGTATDAK

This protein is a component of the leucine, isoleucine, valine, (threonine) transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids.

P0AD98

Q8L765

BPM1_ARATH

Protein BTB-POZ AND MATH DOMAIN 1

Arabidopsis

MGTTRVCSEVSSGSSKSLSQSLTVSTSTTETVNGFHEFKICGYSLAKGVGVGKYVASDTFMVGGYSWAIYFYPDGKSPEDNSSYVSLFIALASEGADVRALFELTLVDQSGNGKHKVHSHFGRALDSGPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRVGVVKSVTEGPRYYNIPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLCEGVAINTVATTLALAEQHHCLQLKAVCLKFVALPENLKAVMQTDGFDYLKESCPSLLTELLQYVARLSEHSVIVSGHRKEIFADGCDASGRRVKPRLH

May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.

Q8L765

Q145X4

PTH_PARXL

Peptidyl-tRNA hydrolase

Paraburkholderia

MIKLIVGLGNPGAEYTATRHNAGFWLVDQLAREAGTTLRDERRFHGFYAKARLHGEEVHLLEPQTYMNRSGQSVVALAQFFKILPDEILVAHDELDMPPGSVKLKLGGGSGGHNGLKDITAHLSSQQYWRLRIGIGHPRDLIPESARAGARPDVANYVLKPPRREEQDVIDASIERALAVMPQVIKGELERAMMQLHRNP

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.

Q145X4

A0A023GPI8

LECA_CANBL

Lectin gamma chain

Canavalia

ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGRDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSSDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN

D-mannose/D-glucose-binding lectin . Has anti-inflammatory activity in animal models when applied intravenously . Has antinociceptive activity in mice when applied intravenously .

A0A023GPI8

A6X0C8

RL14_BRUA4

50S ribosomal protein L14

Brucella

MIQMQTNLDVADNSGARRVMCIKVLGGSKRRYASVGDIIVVSIKEAIPRGRVKKGDVMKAVVVRTAKDIRRPDGSVIRFDNNAAVLIDNKKEPIGTRIFGPVPRELRAKNHMKIISLAPEVL

Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.

A6X0C8

Q5SK67

PYRC_THET8

Dihydroorotase

Thermus

MILIRNVRLVDARGERGPADVLIGEGRILSLEGGEAKQVVDGTGCFLAPGFLDLHAHLREPGEEVKEDLFSGLLAAVRGGYTDLVSMPNTKPPVDTPEAVRALKEKAKALGLARLHPAAALTEKQEGKTLTPAGLLREAGAVLLTDDGRTNEDAGVLAAGLLMAAPLGLPVAVHAEDAGLRRNGVMNDGPLADLLGLPGNPPEAEAARIARDLEVLRYALRRSPATPRLHVQHLSTKRGLELVREAKRAGLPVTAEATPHHLTLTEEALRTFDPLFKVAPPLRGEEDREALLEGLLDGTLDAIATDHAPHTLAEKEKDLLRAPFGIPSLEVAFPLLYTELHLKRGFPLQRLVELFTDGPRRVLGLPPLHLEEGAEASLVLLSPKERPVDPSAFASKARYSPWAGWVLGGWPVLTLVAGRIVHEALK

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.

Q5SK67

Q4UWC9

ACCD_XANC8

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Xanthomonas

MSWLSKLMPSGIRTENTPAKKRSVPEGLWEKCSNCGSALYGPELEENLEVCPKCDHHMAIRARARLAALFDLDSPTTEIAAQLGPVDVLKFKDQKKYGERIKASQKSSGEYDALIAMRGMLKGNPLVAAAFDFAFMGGSMGSVVGERFARAAEVALEVGCPFVCFSASGGARMQEGLFSLMQMAKTSAALGRLREAGLPYISVLTHPTTGGVSASFAMLGDINIAEPHALIGFAGPRVIEQTVRETLPEGFQRSEFLLDHGAIDQICDRRDMRDRIAELTTMMMRQPHPQDADAA

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.

Q4UWC9

Q8W032

CDC6B_ARATH

Cell division control protein 6 homolog B

Arabidopsis

MPTNAGTSLSSYKHIVAIGTTVKSESLESAAYEIPRKRKMRSDSAAVSGNSVSTPKKLKSHLPSSVPNPGMSEKEVVEDSNEILRYPVNLAVSDCLGTKSKWSPRDEEQMRAVKEALHVSKAPSTILCREDEQIRIFEFVKGCIDQQKAGSLYICGCPGTGKSLSMEKVVQQVGDWSTQAGLPPVDTLSVNCTSLSKTTDIFSKILGEIKPGKNANTNSSPLQHLQNLFSQKQESSSSRMMLIIADEMDYLITKDRGVLYDLFMLTTLPFSRCILIGVANAIDLADRFLPKLKSLNCKPMVITFRAYSKDQILRILQERLRVLSYVAFQPKALELCARKVAAASGDMRKALCVCRSALEILEIETRGSTGPESQGPTPDDSVVRMDHMAAALSKTFKSPVVETIQSLPQHQQIIICAAAKAFRGSKKDATVGELNKLYLEICKSWMISPAGITEFTNMCTVLNDQGILKVGQARRDKLKRVSLRVDESDITFALQEIRFFRNCLL

May be involved in the initiation of DNA replication.

Q8W032

Q47PU3

PAMO_THEFY

Baeyer-Villiger monooxygenase

Thermobifida

MAGQTTVDSRRQPPEEVDVLVVGAGFSGLYALYRLRELGRSVHVIETAGDVGGVWYWNRYPGARCDIESIEYCYSFSEEVLQEWNWTERYASQPEILRYINFVADKFDLRSGITFHTTVTAAAFDEATNTWTVDTNHGDRIRARYLIMASGQLSVPQLPNFPGLKDFAGNLYHTGNWPHEPVDFSGQRVGVIGTGSSGIQVSPQIAKQAAELFVFQRTPHFAVPARNAPLDPEFLADLKKRYAEFREESRNTPGGTHRYQGPKSALEVSDEELVETLERYWQEGGPDILAAYRDILRDRDANERVAEFIRNKIRNTVRDPEVAERLVPKGYPFGTKRLILEIDYYEMFNRDNVHLVDTLSAPIETITPRGVRTSEREYELDSLVLATGFDALTGALFKIDIRGVGNVALKEKWAAGPRTYLGLSTAGFPNLFFIAGPGSPSALSNMLVSIEQHVEWVTDHIAYMFKNGLTRSEAVLEKEDEWVEHVNEIADETLYPMTASWYTGANVPGKPRVFMLYVGGFHRYRQICDEVAAKGYEGFVLT

Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide).

Q47PU3

P67086

MIAB_MYCBO

tRNA-i(6)A37 methylthiotransferase

Mycobacterium tuberculosis complex

MVAHDAAAGVTGEGAGPPVRRAPARTYQVRTYGCQMNVHDSERLAGLLEAAGYRRATDGSEADVVVFNTCAVRENADNRLYGNLSHLAPRKRANPDMQIAVGGCLAQKDRDAVLRRAPWVDVVFGTHNIGSLPTLLERARHNKVAQVEIAEALQQFPSSLPSSRESAYAAWVSISVGCNNSCTFCIVPSLRGREVDRSPADILAEVRSLVNDGVLEVTLLGQNVNAYGVSFADPALPRNRGAFAELLRACGDIDGLERVRFTSPHPAEFTDDVIEAMAQTRNVCPALHMPLQSGSDRILRAMRRSYRAERYLGIIERVRAAIPHAAITTDLIVGFPGETEEDFAATLDVVRRARFAAAFTFQYSKRPGTPAAQLDGQLPKAVVQERYERLIALQEQISLEANRALVGQAVEVLVATGEGRKDTVTARMSGRARDGRLVHFTAGQPRVRPGDVITTKVTEAAPHHLIADAGVLTHRRTRAGDAHTAGQPGRAVGLGMPGVGLPVSAAKPGGCR

Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.

P67086

B2TZN1

HPCH_SHIB3

4-hydroxy-2-ketoheptane-1,7-dioate aldolase

Shigella

MENSFKAALKAGRPQIGLWLGLSSSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPNQPVVRPSWNDPVQIKQLLDVGTQTLLVPMVQNADEAREAVRATRYPPAGIRGVGSALARASRWNRIPDYLQKANDQMCVLVQIETREAMKNLPQILDVEGVDGVFIGPADLSADMGYAGNPQHPEVQAAIEQAIVQIRESGKAPGILIANEQLAKRYLELGALFVAVGVDTTLLARAAEALAARFGAQATAVKPGVY

Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.

B2TZN1

A1JNX2

FOLD_YERE8

Methenyltetrahydrofolate cyclohydrolase

Yersinia

MSAKIIDGKTIAQQVRNEVAALVQKRLAAGKRAPGLAVVLVGENPASQIYVASKRKACEEVGFVSRSYDLPMTTTEAELLALIDSLNNDSEIDGILVQLPLPAGIDNVKVLEHIHPDKDVDGFHPYNVGRLCQRAPKLRPCTPRGIVTLLERYDIPTYGLNAVVVGASNIVGRPMSLELLLAGCTTTVTHRFTKNLRQHVENADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLESGKVVGDVEFDVAVERAGWITPVPGGVGPMTVATLIQNTLQACEEYHDINENRVKGQ

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.

A1JNX2

Q1QAQ4

MURB_PSYCK

UDP-N-acetylmuramate dehydrogenase

Psychrobacter

MTSALCSKPIAPHTLSDDLADLSYSNTMALACMADSVVTLTDEVQLDEFMAYYEQDTQHRKPLFVLSGGSNVLLPAKLNAIVLRPQMRGIQVTAQTDFHVDIEVMAGENWHDLVVHTVAQGWYGLENLALIPGLTGAAPIQNIGAYGVQLEDCLQYVRAYHLPSQTWHDLTAVDCEFGYRDSIFKRQPNTWLISRVGFRLHTDATKVLASYGDVQTVAQSYATQQGRTKPMPADVMHAIIEIRQQKLPDPKQLPNCGSFFQNPIVPQDQFATLQSSYPAIVGYPMPDAMTKVAAGWLIEQAGLKGGGIEPIFTHQQQALVLTNHAPYIATKQDVAAAQKYIIDTVYKKFAIQLSREPVWVNADGSIGYDEHVV

Cell wall formation.

Q1QAQ4

Q9URS0

ACTG_PENCH

Actin, gamma

Penicillium chrysogenum species complex

MEEEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPINPKFNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFSLPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPNVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIVMSGGTTMYPGISDRMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Q9URS0