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
Q4R7X8	ZN322_MACFA	Zinc finger protein 322A	Macaca	MYTSEERCNQRTQKRKIYNVCPQKGKKIFIHVHAITQIDGHIYQCLECKQNFCENLALIMCERTHTGEKPYKCDMCEKTFVQSSDLISHQRIHNYEKPYKCSKCEKSFWHHLALSGHQRTHAGKKFYTCDICGKNFGQSSDLLVHQRSHTGEKPYLCSECDKCFSRSTNLIRHRRTHTGEKPFKCLECEKAFSGKSDLISHQRTHTGERPYKCNKCEKSYRHRSAFIVHKRVHTGEKPYKCGACEKCFGQKSDLIVHQRVHTGEKPYKCLECMRSFTRSANLIRHQATHTHTFKCLEYEKSFNCSSDLIVHQRIHMEEKPHQWSTCESGFLLGMDFVAQQKMRTQTEELHYKYTVCDKSFHQSSALLQHQTVHTGEKPFICNVSEKGLELSPPHASEASQMS	Transcriptional activator. Important for maintenance of pluripotency in embryonic stem cells. Binds directly to the POU5F1 distal enhancer and the NANOG proximal promoter, and enhances expression of both genes. Can also bind to numerous other gene promoters and regulates expression of many other pluripotency factors, either directly or indirectly. Promotes inhibition of MAPK signaling during embryonic stem cell differentiation.	Q4R7X8
P08098	MOBA1_ECOLX	Mobilization protein A	Escherichia	MGLSHKERREYGRSYKRDNNRTAPFSCWPRWIRPGGWSGHGGMSGTTRTGVTARLAFWGGWLSPCLSRAGEKPSCVRTSTRTQIITCCSRLTCSGLPGARAGWLSGLCWRGSGVLLLDGHFAAADEAVNRKLNRRAGAQPATGEMTDVRQPAFRGAGTVNALARFFHGRGPETAGVFLGKDEQGEPVLVPRDTWRKTNIQILGLPGSGKSVMATNALIRSVRDFGDAVVYFDQRGPVAALLPAHCPNFTLLDLRPGKPAQLNLFRDLDQYALKNLLVAGFNLSETGHVADHYRISEQKAAKLIAEQVSAGGKHSAGAGGGVRAAGGPEKGREGADHQAGERGRPERPADGQRHRRGGDNQRRRLLYVIGSMDDEAVIRVQKMLFARCAQIIIARDEFRRWPHASIMLDEIKYLLSKYVLNALGTVRSRDCNLRLAHHAGRLRAAGQDLPADFVKTTVLDNTPIRWFYRAASQESRSGAGQTGEIRVDVERRGPAGRRGTWSISAGTASSRRSRPLFDVNTLQHLLTGSR	This protein is essential to promote the specific transfer of the plasmid in the presence of conjugative plasmids.	P08098
Q6FWV2	ATP10_CANGA	Mitochondrial ATPase complex subunit ATP10	Nakaseomyces/Candida clade	MRVVFQQCTKFSTSCNRAFLARFLKPVMNASPKEHVVKQLLKPVGLNVPPRPNIKYSEGNSWLDLFDGAKTEERIKELEIEFAKSGMYEMATFRKTNGKLFLSPESYWKADKALYFPHLSGRTLSSEDHGNVEDVLRGKTSVIRVFSTQVGDKISREYIKNTELGIDNYENQSCQVIDINFLENKLKSWLFKLSLNNLKSTVPVQRHDNYWLCHREQIPFLMRERLLINNVYSGYIFVVDPNLKIRFMACGPASADEFNKLWKVVGQLSKEKK	Involved in assembly of the mitochondrial F1-F0 complex.	Q6FWV2
A5UGR9	MUTH_HAEIG	Methyl-directed mismatch repair protein	Haemophilus	MIPQTLEQLLSQAQSIAGLTFGELADELHIPVPPDLKRDKGWVGMLLERALGATAGSKAEQDFSHLGVELKTLPINAEGYPLETTFVSLAPLVQNSGVKWENSHVRHKLSCVLWMPIEGSRHIPLRERHIGAPILWKPTAEQERQLKQDWEELMDLIVLGKLDQITARIGEVMQLRPKGANSRAVTKGIGKNGEIIDTLPLGFYLRKEFTAQILNAFLDVKPL	Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.	A5UGR9
V5I2G9	E1172_IXORI	Evasin P1172	Ixodes	FLLKSQLCYCLFGIELIGAGIHALHEDEIFTVDYCGTNCTKQSNGSWTTCPGNCSCYHEDGKTDGFCLSTEYTDFTQFPNLTSEEMDAATPRPE	Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL5 and CXCL8.	V5I2G9
Q48D43	RL16_PSE14	50S ribosomal protein L16	Pseudomonas	MLQPKRTKFRKQMTGHNRGLALRGSKVSFGEFALKSVARGRLTARQIESARRALTRHVKRGGKIWIRVFPDKPVTKKPLEVRMGKGKGNVEYWVAQIQPGKVLYEIEGVTEELAREAFALAAAKLPLATSFVKRTVM	Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.	Q48D43
Q466D1	RL7A_METBF	Ribosomal protein L8e	Methanosarcina	MAQLAKFDVPEELTNKALEALELARDTGKIKKGTNEATKAIERGNAKLVLIAEDIEPAEIIAHIAPLSEEKKAPYIFIKNQKELGAASGLGVSCATVAIVDAGKAGEMVQDIAQKLEALK	Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.	Q466D1
A0A0D3MU35	ORGRE_CUCME	DnaJ-like cysteine-rich domain-containing protein Or	Cucumis	MDRVLVASYPINHLIRPHSFRIDYCWSTCFTSRLNSGKERQKLSSRWRWRSMASDSTDSSSSSSFAPSVESDPSDKTSASFCIIEGPETVQDFAKMELQEIQENIRSRRNKIFLHMEEVRRLRIQQRIKNAELGISKEERENELPNFPSFIPFLPPLSSENLKLYYVTCYSLIAGIILFGGLLAPTLELKLGLGGTSYEDFIRSVHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSNTGALVLIEPVSTLNGEHQPLSLPKTERCQNCSGSGKVMCPTCLCTGMAMASEHDPRIDPFD	Involved in chloroplast differentiation in fruit flesh.	A0A0D3MU35
Q32RL7	PSAI_ZYGCR	Photosystem I reaction center subunit VIII	Zygnema	MSASYLPSILVPLVGLVFPAITMVSLFLYIEQDEIV	May help in the organization of the PsaL subunit.	Q32RL7
Q0VSV6	HEMH_ALCBS	Protoheme ferro-lyase	Alcanivorax	MAYKGQENLEHLNPRKVGVLITNLGTPDAPETGALRRYLREFLSDPRVVEIPRFIWFFILNLVILVIRPRKSAEAYKSVWTEEGSPLLVYSLAQGEGIRQRLQSKYGDDVVVRVAMRYGNPSIASQLQAFEDEGIRKLVVLPLYPQYSGSTNGSTFDAVAQDFMGRRLLPDLRFISHYPDYPPYIQAMAEHIRAYREKNGSADKLVFSFHGVPKRFLLKGDPYFHECHQTSQLLAKALGLSDGQWMTTFQSRFGAEEWLQPYTDATMKSLPGEGVKSVQVFCPGFSADCLETVEEIDQENREYFEEAGGESFAYISALNAEPAHLDALAQLVEDNLQGFLP	Catalyzes the ferrous insertion into protoporphyrin IX.	Q0VSV6
Q8UH15	TAM_AGRFC	Trans-aconitate 2-methyltransferase	Agrobacterium tumefaciens complex	MAWSAQQYLKFEDERTRPARDLLAQVPLERVLNGYDLGCGPGNSTELLTDRYGVNVITGIDSDDDMLEKAADRLPNTNFGKADLATWKPAQKADLLYANAVFQWVPDHLAVLSQLMDQLESGGVLAVQMPDNLQEPTHIAMHETADGGPWKDAFSGGGLRRKPLPPPSDYFNALSPKSSRVDVWHTVYNHPMKDADSIVEWVKGTGLRPYLAAAGEENREAFLADYTRRIAAAYPPMADGRLLLRFPRLFVVAVKK	Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.	Q8UH15
Q9EUT5	GLGA_RHITR	Starch [bacterial glycogen] synthase	Rhizobium	MKVLSVSSEVFPLIKTGGLADVVGALPIALKPYGVETKTLIPGYPAVMKAIRDPVVRLELPDLLGEAATILEVEHAGISFLVLDAPAYYSRTGGPYVDATGKDYPDNWRRFAALSLAGAEIAAGLLPGWRPDLVHAHDWQSALVPVYMRYYPTPELPSVLTIHNIAFQGQFGADIFPGLRLPAHAFSVEGIEYYGDVGFLKGGLQTAHALTTVSPSYAEEILTPEFGMGLEGVIASKAYNLYGIVNGIDADIWNPATDPMIAQTYSAATLKERAINRHRVVEHFGLEEDDGPIFCVVSRLTWQKGMDILAEVASEVVHMGGKLAILGAGDAALEGALFAAAGRHRGRVGVVGRHNEPMSHLMQAGCDAIIIPSRFEPCGLTQLYGLRSGCLPIVARTGGLNDTIIDANHAALQAKVATGIQFSPVTAEGLLQAMRRAMHLFQDRKVWTQMQKQGMKSDVSWGRSAERYAALYSSLVSRGA	Synthesizes alpha-1,4-glucan chains using ADP-glucose.	Q9EUT5
A6TVS0	PYRDB_ALKMQ	Orotate reductase (NADH)	Alkaliphilus	MTKVNMKVNIAGVELKNPVMTASGTFGSGREYGEYVDLNQLGAVVVKGVANEPWKGNPSPRIAETYGGMLNSVGLQNPGVDEFIEKDIPFLRQYNTKIIVNIAGRTIEDYCEVVKKLGDADVDLLELNISCPNVKAGGVCFGTDPFMVEEVTKAVKKVAKQPLIVKLTPNVTDIVPIAKAAVAGGADGISLINTLLGMAIDIHKRKPILANVMGGFSGPAIKPVALRMVYQVANAVDVPIIGMGGIMTGEDAVEFILAGASGVAVGTANFINPRATIDVIEGIQGYMEQYSIKDLKEIRGSL	Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.	A6TVS0
Q8WKE7	MATK_FAGJA	Intron maturase	Fagus	MEEFQRYLELDRFRQHDFLYPLLFREYIYALAHDHGFNSYMLLENIGYDNKSSLLIVKRLITRMYQHNYLMISANDSNQNPFFGYNKNLHSQIISEGFAVIVEIPFSLRLISSFEGAEIVISYKLRSIHSIFPFLEDKLPHLNYTTDVRIPYPIHLEILIQTLRSRVKDASYLHLLRFFLHQYSNWNILIITTKSISIFSKSNPRFFLFLYNSHICQYESIFLFLGNQSSHLRLISSGVLFERLYLHKKIEHFAEVFANDFPVIPCFLKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHFYVWSHPGRIHINQLSKHSLDFWGYFSSVRLNPSVVRSQMLENSFLINNAPKKLDIIVPIIPLIGSLAKARFCNALGHPISKLTRADLSDFEILNRFLRICRNLSHYYSGSSKKKSMYRIKYILRLSCVKTLARKHKSTARAFLKKVGSEFVQEFFTEEEEFLSLIFPRTSFTLRRLYRGRVWYLDIIFINGLANHE	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.	Q8WKE7
Q8D3H1	FLHD_WIGBR	Flagellar transcriptional regulator FlhD	Wigglesworthia	MSNDNILKNIHEINLSYLLLAQELIKQDKKVASFRLGVCEDTLNKISKLSLSELIKLGAINQLICLLRLDDEKVINCLTRESRVDELQQVHTGIMLSTQLLRSHKSNSNHALKE	Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.	Q8D3H1
A7N5C4	GCSP_VIBC1	Glycine dehydrogenase (aminomethyl-transferring)	Vibrio	MTELLQSLSTQNEFVARHNGPNKSDQQKMLEAINAVSLDSLIDETVPAQIRLEQPMNLAEAKSEADMLAAMRKFADQNQIKRTFIGQGYYNTFTPNVILRNVMENPGWYTAYTPYQPEISQGRLESLLNYQQMVMDLTGMEIANASLLDEATAAAEAMTLCKRAGKSKSNVFFVADDVHPQTIEVVKTRAKFIGFEVLVGALDSLPEQDVFGALVQYPGTTGEVRDLTDLIAKAQANKTLVTVATDLLASALLKPAGEMGADVAIGSAQRFGVPMGYGGPHAAFMATRDKHKRTMPGRVIGVSIDTNGNQALRMAMQTREQHIRREKATSNICTAQALLANMASFYAVFHGAEGLRTIARRTHHMTAILAAGLTKGGFELAHNSFFDTITINTGAQTEDLYAKALAADINLRKLGTQLGVSFDETTTVADVEALFAVFGVKEEVAALSTEIAGNEFAAIPEALRRTTEYLTHPVFNTHHSETQMMRYLKQLENKDFSLTHGMIPLGSCTMKLNAAAEMIPVTWPEFGSIHPFAPADQAAGYAALAKDLKEKLCEITGYDAFSLQPNSGASGEYAGLIAIQRYHESRGEGHRNVCLIPSSAHGTNPATASMVSMKVVVVKCDEEGNIDVTDLAAKIKKHKDNLSSIMITYPSTHGVYEEQVKEVCEMVHAAGGQVYLDGANMNAQVGLTTPGFIGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKSHLAPFLPGHIENGADGENFAVSAADMGSASILPISWAYIAMMGEAGLTDATKVAILNANYVMEQLRPHYPVLYRGSNGRVAHECIIDIRPLKEETGISEEDIAKRLMDYGFHAPTMSFPVAGTLMVEPTESEDLEELDRFCDAMIAIREEMTKVKNGEWPLDNNPLVNAPHTQFDLAKEEWDRPYSRELGCFPSKATKSWKYWPTVNRVDNVYGDRNLICSCPSIDNYED	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.	A7N5C4
D4GVR1	HPRL1_HALVD	HGPRTase-like protein 1	Haloferax	MDQLRQSLLDAPIIEKGDYEYFVHPISDGVPMLEPGLLREIVIKIIRKANLENVDKIVTPAAMGIHISTAVSLMTDIPLVVIRKREYGLDGEVSLHQQTGYSEGDMFINDVNEGDRVLVLDDVLSTGGTMKAVLDALDHIGADVVDTVAIIKKAGPNELDDSDHHVKTLINVTVEDGEVVIVDEHGDD	May catalyze a purine salvage reaction, the substrate is unknown.	D4GVR1
P31105	CHER_BACSU	Chemotaxis protein methyltransferase	Bacillus	MDTYSVFTTKWKQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQALLNETLDRMTINVSEFYRNYKRWEVLETAILPLIKTSRPLKIWSAACSTGEEPYTLAMLLDQQKGLPGYQILATDIDEKALEKAKKGVYQERSLQEVPLSVKDRYFTQNANRSYEVKTEIKKNITFKKHNLLADRYEQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTEQIFNPEKFGLVPADTFFYQKR	Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents.	P31105
Q8DJ45	PTH_THEVB	Peptidyl-tRNA hydrolase	Thermosynechococcus	MALQPCVIVGLGNPGIEYATTRHNVGFRVLDTLAQRYRVQLTQQRRFLGEVAEVLIQGQKVRLLKPTTYMNSSGQSLHALLNFYKLPLERTLVVHDDADLPLGRLRLRLSGSTGGHNGIKSIIQHCHSQQFPRLKVGIAFGDRLQQQTGPRNAVPFVLGHFSATELAILPAVLDLAVDAIELSIQSGVEVAMNRYNGKSIPLPQA	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.	Q8DJ45
A5FMT0	GCSP_FLAJ1	Glycine dehydrogenase (aminomethyl-transferring)	Flavobacterium	MKTDAFALRHIGPRETDLQHMLQTIGVDSIEQLVYETLPDDIRLKAPLNLDPAMTEYEFANHIQELGKKNKVFKSYIGLGYHPTIVPAPIQRNIFENPGWYTAYTPYQAEIAQGRLEAILNFQTTVIELTGMEIANASLLDEGTAAAEAMALLFDVRTRDQKKNNTHKFFVSEEILPQTLSVLQTRSTPIGIELVVGNHETFDFSTEFFGAILQYPGKYGQVNDYGAFVAKAKENEIKVAFAADILSLAALTSPGEMGAAVVVGTTQRFGVPMGYGGPHAAYFATKDEYKRSMPGRIIGVSVDANGNRALRMALGTREQHIKREKATSNICTAQVLLAVMAGMYAVYHGPKGLKYIANKVHASAVTTAEALNKLGVFQTNTAFFDTILVKADAQKVKAIAEKNEVNFFYPDAESVSISLNETTSVSDINQIIAIFAEALGKEAVTVSELTTASQLPASLERTSSFLTHDVFNNHHSESQLMRYIKKLERKDLSLNHSMISLGSCTMKLNAASEMLPLSMPNWNSIHPFAPVEQAEGYITMLKKLEQQLNVITGFAGTTLQPNSGAQGEYAGLMAIRAYHLSRNEGHRNVCLIPSSAHGTNPASAAMAGMKIIVTKTTPEGNIDVEDLREKAIEHKDDLSCLMVTYPSTHGVFESSIIEITKLIHENGGLVYMDGANMNAQVGLTNPATIGADVCHLNLHKTFAIPHGGGGPGVGPICVNEKLVPFLPTNPILKVGGEQAITAISSAPYGSALVCLISYGYITMMGAEGLKSATEHAILNANYMKSRFEGHYPILYTGECGRAAHEMILDCRAFKENGIEVGDIAKRLMDYGFHAPTVSFPVAGTLMIEPTESEDLAELDRFCDALISIRKEIEAATADDKNNVLKNAPHTLAMLTSDSWDFPYSREKAAYPLEYIADNKFWPSVRRVDDAYGDRNLVCSCAPIEAYMEN	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.	A5FMT0
B0RZS0	RL24_FINM2	50S ribosomal protein L24	Finegoldia	MKIKNGDTVIVISGKDKGKTGNVIEVLAKKNKVVVEGVNIVTKHQKANGRGVESGLIKKEAPIDVSNVMYYDAKNKKGTRLGYKFEDGKKVRFMKSNNETIK	One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.	B0RZS0
Q87SG3	MURC_VIBPA	UDP-N-acetylmuramoyl-L-alanine synthetase	Vibrio	MTIQHTQDLAQIRAMVPEMRRVKCIHFIGIGGAGMSGIAEVLLNEGYEITGSDLSENPVTERLVSKGATVFIGHQASNVEKASVVVVSTAINEENPEVMAARELRIPIVRRAEMLAELMRFRHGIAVAGTHGKTTTTALVTQIYSEAGLDPTFVNGGLVKSAGTNARLGSSRILIAEADESDASFLHLQPMVSIVTNIEADHMDTYGGDFETLKQTFIDFLHNLPFYGQAIVCIDDPVIRELIPRISRQVITYGFSDDADVRIENYHQEGQQGKFTVVRKGRANLDITLNIPGRHNALNASAAIAVATEDDIEDDAILKAMAGTQGTGRRFDHLGEFDTGNGHAMLVDDYGHHPTEVDVTIKAARSGWQDKRLVMIFQPHRYSRTRDLYDDFANVLEQVDVLIMLDVYAAGEKPIAGADGRSLCRTIRSRGKVDPIFVPEIEQLPSVLANVIQDGDLILTQGAGDVGKVAKQLANLELNINKMLG	Cell wall formation.	Q87SG3
Q252U9	FABZ_CHLFF	Beta-hydroxyacyl-ACP dehydratase	Chlamydia	MKEAPVIKLRELLNLLPHRYPFLLVDKVLSYDLEKRSIVAQKNVTINEPFFVGHFPEAPIMPGVLILESLAQAAGVLLGLVLENDRNKRLALFLGIQKAKFRHAVRPGDILTLSAEFSLISSKGGKASARACVGSQVAAEGELSFALVDKESLD	Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.	Q252U9
Q8ZUR9	LIPA_PYRAE	Sulfur insertion protein LipA	Pyrobaculum	MIPSWVSLRAGDYEKIINVRRALSRHGIYTVCEGAKCPNIFHCWGEGTATFMILGEVCTRACRFCAVRTGNPRGYVDWGEVDRLVEAVRELGLKYVVVTSVARDDLPDGGASVFAAVVKKLREVGCVVEVLVPDFGGSPASVKTVVSSGPDVFAHNVETVRRLTPLVRDRRAGYERSLSVLKYAKEFGAPLTKSGLMLGLGETFEEVVETLEDLRRADVDIVTIGQYIKPSGSPRHLNPVRYATPEEFAKIKEVAVSLGFKAVASGPLVRSSYKAYSLYREALKNIVYLG	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.	Q8ZUR9
C4ZBS1	RL23_AGARV	50S ribosomal protein L23	Lachnospiraceae incertae sedis	MANVQYYDVILKPVVTEKSMNAMAEKKYTFLVHPDANKTMIKEAVERMFEGTKVAKVNTMNCEGKNKRRGMVTGKTAKTKKAIVQLTADSKDIEIFAGL	One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.	C4ZBS1
P49043	VPE_CITSI	Vacuolar-processing enzyme	Citrus	MTRLASGVLITLLVALAGIADGSRDIAGDILKLPSEAYRFFHNGGGGAKVNDDDDSVGTRWAVLLAGSNGFWNYRHQADICHAYQLLRKGGLKDENIIVFMYDDIAFNEENPRPGVIINHPHGDDVYKGVPKDYTGEDVTVEKFFAVVLGNKTALTGGSGKVVDSGPNDHIFIFYSDHGGPGVLGMPTSRYIYADELIDVLKKKHASGNYKSLVFYLEACESGSIFEGLLLEGLNIYATTASNAEESSWGTYCPGEIPGPPPEYSTCLGDLYSIAWMEDSDIHNLRTETLHQQYELVKTRTASYNSYGSHVMQYGDIGLSKNNLFTYLGTNPANDNYTFVDENSLRPASKAVNQRDADLLHFWDKYRKAPEGTPRKAEAQKQFFEAMSHRMHVDHSIKLIGKLLFGIEKGPEILNTVRPAGQPLVDDWGCLKSLVRTFESHCGALSQYGMKHMRSLANICNTGIGKEKMAEASAQACENIPSGPWSSLDKGFSA	Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles that accumulate during ethylene-regulated processes such as flower opening and flavedo degreening.	P49043
B5ZBG4	TRUB_UREU1	tRNA-uridine isomerase	Ureaplasma	MYTINKNIIVINKPINWTSNDVVQKVKRIIKAKKVGHAGTLDPNASGILVLGINEGTKLLTKLTLDSKTYVAEIQFGISTNTYDSTGEIISKINKFITLTEIESAIENLYKNEYWQKPPKFSALKINGKKAYELARNNISFEIEPRLVKIFEYNILDFNYEKQILKIIIKVSKGFYVRSFAVDLAARINNLAHLLSLVRTESGQFSINDAIEIEQVYDYWNNINKHSTN	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	B5ZBG4
P15329	GUNX_ACETH	Endo-1,4-beta-glucanase	Acetivibrio	IMKVTQDGSIPQIASNINNWLNTHNPDVVFLWIGGNDLLLSGNVNATGLSNLIDQIFTVKPNVTLFVADYYPWPEAVKQYNAVIPGIVQQKANAGKKVYFVKLSEIQFDRNTDISWDGLHLSEIGYTKIANIWYKYTIDILKALAGQTQPTPSPSPTPTDSPLVKKGDVNLDGQVNSTDFSLLKRYILKVVDINSINVTNADMNNDGNINSTDISILKRILLRN	This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.	P15329
Q0GY42	KBX2_TITCO	Potassium channel toxin TcoKIK	Tityus	KIKSGWERLTSESEYACPAIDKFCEDHCAAKKAVGKCDDFKCNCIKL	Blocks voltage-gated potassium channels.	Q0GY42
Q6LLW0	RL10_PHOPR	50S ribosomal protein L10	Photobacterium	MALNLQDKKAIVAEVNEAANGALSAVVADSRGVAVGAMTSLRKQARENGVYLKVVRNTLARRAVEGTDFECLKDVFVGPSLIGFSNEHPGAAARLFKDFAKENKDFEFKAAAFEGAVVDAEVLATLPTYDEAIARLMMCMKEASAGKLVRTIAAVRDQKEEAAA	Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.	Q6LLW0
Q02KH3	MTNB_PSEAB	Methylthioribulose-1-phosphate dehydratase	Pseudomonas	MNDNREQLTQQIIDAGRFLYGRGWSPATSSNYSARLDEQRALLTVSGKHKGQLGFDDVLATDLAGNSLEPGKKPSAETLLHTQLYAWNPAIGAVLHTHSVNATVLSRLVRGDRLVLQDYELQKAFAGVTTHEGQVEVPIFDNDQDIARLASRVQPWLEAHPYCPGYLIRGHGLYTWGARMSDALRQVEAFEFLFECELKVLSLSR	Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).	Q02KH3
O29460	COFH_ARCFU	FO synthase subunit 2	Archaeoglobus	MKSIRMLMVMLALDDLLKNPYETFRIADELRRELVGDTVTYVVNRNINFTDICINDCKFCSFRNRKKYLLSLDEIKQKVEEAVEFGCTELCIQGGLLPDADLDFYLSILQAVRDVDKKIHIHAFSPMEVVHAARNSGMTVEEVLKELKKEGLGSMPGTAAEILDDSIRALICPRKLKTAEWVEVIKTAHRVGIPTTATIMYGHIDTWEHRINHLLLIKKIQQETGGITELIPLPFMSKNNELGRYAKGSSGFDDLLMIAIARILLYPEIKNIQASWVKMGQKLAQAALHVGANDLGGTLMEENISKSAGATSGEFMHPEELRELIKIAGRVPKQRDTLYNILD	Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.	O29460
Q57RU6	CRCB_SALCH	Putative fluoride ion transporter CrcB	Salmonella	MLQLLLAVFIGGGTGSVARWMLSMRFNPLHQAIPIGTLTANLLGAFIIGMGFAWFNRMTHIDPMWKVLITTGFCGGLTTFSTFSAEVVFLLQEGRFGWALLNVLINLLGSFAMTALAFWLFSAAAAR	Important for reducing fluoride concentration in the cell, thus reducing its toxicity.	Q57RU6
A7MC64	RTN1_XENTR	Reticulon-1	Silurana	MAANPEVFSGRLEGNVAAARRPGSAQEEEGEAAGGALSCVDQGRTIKAEQAGHPTVAMEITSTDFTSTLHLHDAESKELPGDENGLSYTYLSSDKHSHTDSTYFTGISKKGTESPDIKEFSGVGPRSPKEIPTFDSRGLLSSDSGIEMTPAECSEVNKSLADPTEEEKQEAYKYIDISRSPDMKPQQVLDKDFGENKASTIGQAAPTEQQAYDSVTMSWQKDHYNGNISEYLPYVPYMEEPRKDFGLYNSPTSKEPKSAPVTISFTGMETTLQTEYPENQQGKSDKGLKLSPDMVPTVTVSEPEDNSPESITPPSTDADGYTEPSGLEEQRKYKISEDELISAIKAKEGTKGFSSETNEEKQSYSFNVEKQDFTVLPTRDAPAPLDMEGSSTESGDSEIELVSEDQVGAEEAMQSAYMTFSHIGGPPPSPASPSIQYSILREEREAELDSELIIESCDGSSASEESPKRDQDSPMMKPMIMDIIEEENLSRAESFDASDFESCSLKERKLNMENLAESACYLKGTYHTEIRADMPSTKKEELLPQKKSPEGSAYQSKVLGKTSTLPLKPLPFLSKRKAIELLYWRDIKQTGIVFGSVLLMLFSLTQFSVVSVIAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKSYLDMEISLSQEQIQKYTDCLQAYTNSIVKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLIMAVVSMFSLPVVYDKYQAQIDQYLGLVRTNMNTIVTKIQAKIPGTKQKE	Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity.	A7MC64
Q14FC5	RPOA_POPAL	Plastid-encoded RNA polymerase subunit alpha	Populus	MVREKVRISTRTLQWKCVESRADSKRLYYGRFILSPLMKGQADTIGIAMRRALLGEIEGTCITRAKSKKIPHEFSTITGIQESIHEILMNLKEIVLRSNLYGTHNASICVKGPGCVTAQDIILPPSVEIIDNTQHIASLREPIDLHIGLEIERNRGYCMKPPKNFQDGSYSIDAVFMPVRNANHSVHSYGNGNEKQEILFLEIWTNGSLTPKEALHEASRNLIDLFIPFLHAEEESFHLEKNQHKITLPLFAFHDRLAKLRKNQKEIALKSIFIDQLELAPKIYNCLKRSNIHTLWDLLKNSQEDLMKIEHFRIEDVKHIFGILKIEKHFTINLPKNKF	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	Q14FC5
B2FKN7	T23O_STRMK	Tryptophanase	Stenotrophomonas maltophilia group	MSVDNNQRDLEAGIHTDLQGRLTYGGYLRLDQLLSAQQPLSSPPHHDEMLFIIQHQTSELWLKLLGHELRAAIGFLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLGPSSGFQSLQYRYIEFLLGNKNAQMLQVFEHDPAGQAQLRTVLEAPSLYEEFLKYLARFGHAVPAVYEAHDWTQPHVADDALQPVFERIYQDTDRYWREYALCEDLVDLETAFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLAKALELTFFPELFQVRTSLQAAPPAEQA	Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.	B2FKN7
P0CH77	HN817_CYRHA	Peptide F8-17.06	Haplopelma	FECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKDI	Postsynaptic neurotoxin.	P0CH77
Q9UJA2	CRLS1_HUMAN	Protein GCD10 homolog	Homo	MLALRVARGSWGALRGAAWAPGTRPSKRRACWALLPPVPCCLGCLAERWRLRPAALGLRLPGIGQRNHCSGAGKAAPRPAAGAGAAAEAPGGQWGPASTPSLYENPWTIPNMLSMTRIGLAPVLGYLIIEEDFNIALGVFALAGLTDLLDGFIARNWANQRSALGSALDPLADKILISILYVSLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCFTAFTTAASAYSYYHYGRKTVQVIKD	Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.	Q9UJA2
Q73LG9	ERA_TREDE	GTPase Era	Treponema	MNSGVVTIIGRPSAGKSTFLNTASGEKVSIVSAIPQTTRNAIRGIVNTTKGQIVFIDTPGYHKSEKKLNLKLQEIAKTRLEEGDAVLYLIDLSREFGEEEKNICSLLIPLQNKTVIGLNKADLKSSKADLVKKELLSLLPDIPQERIFEISALKDEGINEILSLLIELLPEGEALYPEDIYTDQDVVFRITEIIREQAILHTREEIPHALYAGVEDAEMHKNGKELWVRAFLYVEKESQKAMLIGKGAAVIKSIRIKSMAELRKIFPYKVQLDLQVRVNKNWRQKDNIIKKISY	An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.	Q73LG9
Q5PEH7	CYSJ_SALPA	Sulfite reductase [NADPH] flavoprotein alpha-component	Salmonella	MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPAPEGKMPGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKALKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRAPVAAPSQSVATGAVNDIHTSPYTKDAPLTATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAQALIGLLRPLTPRLYSIASAQAEVESEVHITVGVVRYDIEGRARAGGASSFLAGRVEEEGEVRVFIEHNDNFRLPANPQTPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARCMAVDVEKALLEVIAEFGAMDIESADEYLSELRVERRYQRDVY	Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.	Q5PEH7
P52672	CYSH_THIRO	PAdoPS reductase	Thiocapsa	MSKPDLDAFLHGDDAALRETNRRLESMPAEDRVRWALEHLPPQHVLSSSFGTQSAVMLHLVSRQMPEIPVILVDTGYLFPETYRLVDALTDRFGLNLKVYRPALSPAWQEAGLGRLWEQGADGIERYNRLNKIDPMERALRDLDAGTWFAGLRRQQANSRAELPVLRRQDGRIKFHPIIDWHRPRRARYLRRHDLPDHPLRDQGYVSIGDVHTTVPLLPGMLEEETRFFGIKRECGLHR	Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.	P52672
Q330A4	NU2M_NYCAL	NADH dehydrogenase subunit 2	Nyctimene	MNPLIFTMILLTVMLGTAIVMTTSHWVMAWIGFEMNMLAVIPILMKKYNPRSMEASTKYFLTQATASMLLMLAIVINLVYSGQWSMTKPLTSTTSIIMTLALAMKLGLAPFHFWVPEVTQGVQLSSGLILLTWQKLAPMSILYQISPTINLDLLLLMSLLSILVGGWGGLNQTQLRKIMAYSSIAHMGWMTAIMVYNPTMALLNLVIYILLTTTTFMMLMMNSSTTTLSLSHMWNKTPLLTTAILTIMLSLGGLPPLSGFTPKWMIIQELTKNDNMIMPTIMAVMALLNLYFYMRLTYSTSLTMFPSTNNMKIKWQFSHKKPTANLSPLIILSTLILPLSPMLALLE	Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.	Q330A4
O74898	DPH5_SCHPO	Diphthamide biosynthesis methyltransferase	Schizosaccharomyces	MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHTLVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEHDIGPPLHSVVLVGRDVHDLELEFLRAYAVNLENFDRVAKTYLEK	S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.	O74898
Q8EDK6	BIOB_SHEON	Biotin synthase	Shewanella	MSQLQVRHDWKREEIEALFALPMNDLLFKAHSIHREEYDPNEVQISRLLSIKTGACPEDCKYCPQSARYDTGLEKERLLAMETVLTEARSAKAAGASRFCMGAAWRNPKDKDMPYLKQMVQEVKALGMETCMTLGMLSAEQANELAEAGLDYYNHNLDTSPEYYGDVITTRTYQNRLDTLSHVRASGMKVCSGGIVGMGEKATDRAGLLQQLANLPQHPDSVPINMLVKVAGTPFEKLDDLDPLEFVRTIAVARILMPLSRVRLSAGRENMSDELQAMCFFAGANSIFYGCKLLTTPNPEESDDMGLFRRLGLRPEQGAAASIDDEQAVLAKAAAYQDKASAQFYDAAAL	Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.	Q8EDK6
A4QG13	IDI_CORGB	Isopentenyl pyrophosphate isomerase	Corynebacterium	MTTEVELVVLADSEGNAIGTAPKATVHTKDTPLHFAFSTYILNPRGELLVTRRALSKKTWPGVWTNSMCGHPGPDETNADAIRRRGVDELGLEVDSFLDIQEVLPDYQYRAVDASGIVEWELCPVHLVRLAVGEFVEPLDDEVEEFEWAEPQKLFDAVDATPFVFSPWMVDQLSAPELRQAILEAFDAE	Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).	A4QG13
Q756E2	APT_ASHGO	Adenine phosphoribosyltransferase	Eremothecium	MSINEYAKELKAALAQYPNFPKEGVLFEDFLPIFRSPQLFQKLIDAFKMHLAEAFPETKIDYLVGLESRGFLFGPSLALAIGAGFVPVRKAGKLPGQVVKTTYVKEYEEDVFEMQVDSIPVGATVVVVDDILATGGSAGAAGDLIKQLGATILEFIFVMELDFLKGREKLQAPVFTLLQGQEEALGN	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Q756E2
Q9KA25	XERC_HALH5	Tyrosine recombinase XerC	Halalkalibacterium (ex Joshi et al. 2022)	MEIQNDQWVSAFLLYLKMEKNHSPHTIVNYELDLRHFRDFMEQQSIPSFAAVSYAFVRHYLTVLYEQEYARSTVSRKLSTLRSFYQFLVREKWVMENPFLLAHTPKGVKKLPSFLYEEEMEQLLDALNGDSPLQLRNRALFETIYASGLRVSECCGLKLQDVDLSIGTVFVFGKGRKERYVPIGSFACDAIQEYIENGREKLLKKSKSVDLPGDLFLNYRGGPLTERGVRKILHQALDQAALSTRVSPHSLRHSFATHLLNNGADLRVVQDLLGHENLSTTQVYTHVTKDRLRDVYRTHHPRA	Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.	Q9KA25
Q5GTK2	SSRP_WOLTR	Small protein B	unclassified Wolbachia	MEVIAENRKARFEYFILEEFEAGMVLLSSEVKSLRERKVNISDAYVTEKNGEIWLHNMHIAEYKAANKKKHKPKRERKLLLHKKEINKLISQIKTAGVTIVPLSIYFNDKGLVKTRIAIVKGKKLYDKRATIKQREWNRAKSRLSKNNL	Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.	Q5GTK2
P42508	REGA_RHOCA	Photosynthetic apparatus regulatory protein RegA	Rhodobacter	MAEEEFAELGSDRSLLLVDDDNAFLTRLARAMEKRGFQTEIAETVSAGKAIVQNRAPAYAVIDLRLEDGNGLEVVEALRERRPEARIVVLTGYGAIATAVAAVKMGATDYLSKPADANDITNALLAKGEALPPPPENPMSADRVRWEHIQRVYELCDRNVSETARRLNMHRRTLQRILAKRSPR	Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension.	P42508
B6YW71	SECG_THEON	Protein transport protein Sec61 subunit beta homolog	Thermococcus	MAKEKATLPPTGAGLMRFFDEDTKAVKISPRGVIALTLILVALEILLHAFGPQIFG	Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.	B6YW71
Q7VZG7	UBIG_BORPE	3-demethylubiquinone 3-O-methyltransferase	Bordetella	MTTATQSSAPGVNVDQAEVEKFSALAARWWDPESEFKPLHAINPLRLGWIQETAGSLSGKRVLDMGCGGGILSESMAVAGAQVTGIDLAEKSLKIARLHGLESGVKVDYRAVPVEELAAEQPGQYDVVTCMEMLEHVPDPASVVRACAALAKPGGWVFFSTLNRNPKSFLFAIVGAEYVLRLLPRGTHSYDSFIKPSELATSARQAGLEPTGMRGMEYNPITQVYSLSANTSVNYLMSTRK	O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.	Q7VZG7
B7KXI3	DEOB_METC4	Phosphodeoxyribomutase	Methylorubrum	MARALLIVLDSVGIGGAPDADRYGDAGSDTVGHIAEACAAGRGDRPGLRAGPLRMPNLTALGLGLACEGATGRVPPGLAPDGPVRALWGHAVETAAGKDTPSGHWEIAGVPVREAWGHFPDTQPAFPAELTAALIERAGLPGILGDCHASGTAIIEALGAEHVRTGKPICYTSADSVFQIAAHEEAFGLERLYETCRIAREVCDPYRVGRVIARPFLGSAAEGFRRTSHRKDFSVAPPAGTLLDGLEAAGRAVVSVGKIGDIFAHRATGREIKPAGNAACLDAALDAFAGLPEGGFVFLNLVDFDTEHGHRRDVPGYAAELEAFDARLPEIQAVLKPGDLCVITADHGNDPTWTGTEHTREQVPVLAFGPGLTPRALGRRESFADMGASVAAHLGLPPLGAGQAW	Phosphotransfer between the C1 and C5 carbon atoms of pentose.	B7KXI3
Q8DCM1	AROK_VIBVU	Shikimate kinase	Vibrio	MAEKRNIFLVGPMGAGKSTIGRYLAQQLHMEFLDSDTVIEERTGADISWVFDVEGEEGFRKREEAVINDLTLEQGIVLATGGGSVKSRENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPREVLESLAGERNPLYEEIADYTVRTDDQSAKVVANQIVKMLEES	Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.	Q8DCM1
Q8Z9H9	LPL_SALTI	leu operon attenuator peptide	Salmonella	MSYIVRFTGLLLLNAFIVRGRPVGGIQH	Involved in control of the biosynthesis of leucine.	Q8Z9H9
Q5HPU2	TOP1_STAEQ	Untwisting enzyme	Staphylococcus	MADNLVIVESPAKAKTIEKYLGKRYKVIASMGHVRDLPRSQMGVDTEDNYEPKYITIRGKGPVVKDLKKHAKKAKKIFLASDPDREGEAIAWHLSKILELEDSKENRVVFNEITKDAVKDSFKHPRGIEMDLVDAQQARRILDRLVGYNISPVLWKKVKKGLSAGRVQSVALRLVIDRENEIRNFKPEEYWSIEGEFRYKKSKFTAKFLHYKNKPYKLNNKDDVQRITEALNGDQFEITNVNRKEKTRYPAHPFTTSTLQQEAARKLNFKARKTMMLAQQLYEGIDLKRQGTVGLITYMRTDSTRISTSAKSEAQQYINDKYGEQYVSQRKSSGKQGDQDAHEAIRPTSTMRTPDDMKAFLTRDQHRLYKLIWERFVASQMAPAILDTVALDVTQNDIKFRANGQTIKFKGFMTLYVEAKDDKENDKENKLPQLDKGDKVTATKIEPAQHFTQPPPRYTEARLVKTLEELKIGRPSTYAPTIDTIQKRNYVKLESKRFIPTELGEIVYEQVKEYFPEIIDVEFTVNMETLLDKIAEGDMNWRKVIGDFYNSFKQDVERAESEMEKIEIKDEPAGEDCEVCGSPMVIKMGRYGKFMACSNFPDCRNTKAIVKTIGVTCPKCNEGDVVERKSKKNRIFYGCSRYPECDFISWDKPVGRDCPKCHHYLVNKKKGKSSQVVCSNCDYEEEVQK	Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.	Q5HPU2
C0M8R7	PYRDA_STRE4	Putative dihydroorotate dehydrogenase A (fumarate)	Streptococcus	MVSTATKIATFAFNNCLMNAAGVYCMTKEELLAIEASEAGSFVTKTGTLAPRQGNPEPRYADTALGSINSMGLPNHGYQYYLDIVTEMQKDQASKHHFLSVVGMSAEETETILKAIQASDYQGLVELNLSCPNVPGKPQLAYDFEATDQLLKKIFSYYTKPLGIKLPPYFDIVHFDQAAAIFNQYPLAFANCVNSIGNGLVIDDEQVVIKPKNGFGGIGGDYIKPTALANVHAFYQRLNSSIQIIGTGGVKTGRDAFEHILCGAAMVQIGTALHQEGPAIFKRITKELQDIMAEKGYQTLDDFRGQLQYKP	Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.	C0M8R7
Q718F4	NDB43_MESMA	Toxin peptide 6	Mesobuthus	MEIKYLLTVFLVLLIVSDHCQAFLFSLIPSAISGLISAFKGRRKRDLNGYIDHFKNFRKRDAELEELLSKLPIY	Has antibacterial activity against Gram-positive bacteria S.aureus, M.luteus, B.subtilis, and Gram-negative bacteria E.coli, and P.aeruginosa.	Q718F4
P76350	SHIA_ECOLI	Shikimate permease	Escherichia	MDSTLISTRPDEGTLSLSRARRAALGSFAGAVVDWYDFLLYGITAALVFNREFFPQVSPAMGTLAAFATFGVGFLFRPLGGVIFGHFGDRLGRKRMLMLTVWMMGIATALIGILPSFSTIGWWAPILLVTLRAIQGFAVGGEWGGAALLSVESAPKNKKAFYSSGVQVGYGVGLLLSTGLVSLISMMTTDEQFLSWGWRIPFLFSIVLVLGALWVRNGMEESAEFEQQQHYQAAAKKRIPVIEALLRHPGAFLKIIALRLCELLTMYIVTAFALNYSTQNMGLPRELFLNIGLLVGGLSCLTIPCFAWLADRFGRRRVYITGTLIGTLSAFPFFMALEAQSIFWIVFFSIMLANIAHDMVVCVQQPMFTEMFGASYRYSGAGVGYQVASVVGGGFTPFIAAALITYFAGNWHSVAIYLLAGCLISAMTALLMKDSQRA	Involved in the uptake of shikimate, an intermediate in the aromatic amino acid biosynthetic pathway.	P76350
P11229	ACM1_HUMAN	Muscarinic acetylcholine receptor M1	Homo	MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.	P11229
Q6MTV5	ENGB_MYCMS	Probable GTP-binding protein EngB	Mycoplasma	MIKQASFITSSANKSNWIDDDVSEICLIGRSNVGKSSFINSLTNNNKLAKISNTPGKTRLLNFFEINKGEYRLVDAPGYGYAKVDDNLKIQFAKMMEEYFINRRNLKGVFLLLDLRHKPSNDDIMMYQFLKHYNIPVVIIGTKLDKLKKSEYVKNEKMIKETISFYQEDDFVKISNLNKTNIIKCYELIDKLLGSK	Necessary for normal cell division and for the maintenance of normal septation.	Q6MTV5
A7GCD9	SYE_CLOBL	Glutamyl-tRNA synthetase	Clostridium	MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMEELIEAFNYRNINKAPAVFDTKKLKWMNGEYIRALSLDKFHEMALPYYEEALTRDLDTKKISELLHTRVEVLNEIPEQLDFFNNLLEYSPEMYIHKKMKTTYENSLKSLEEVLPKLEALENWTFENIKEVCMNLVKELEVKNGVVLWPIRTAVSGKQFTPGGAFEIADILGKEETLERIKIGIDKLKALQ	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).	A7GCD9
A0A355	PSAJ_COFAR	PSI-J	Coffea	MRDFKTYLSVAPVLSTLWFGALAGLLIEINRFFPDALTFPFFSF	May help in the organization of the PsaE and PsaF subunits.	A0A355
P26652	TIMP3_CHICK	Tissue inhibitor of metalloproteinases 3	Gallus	MTAWLGFLAVFLCSWSLRDLVAEACTCVPIHPQDAFCNSDIVIRAKVVGKKLMKDGPFGTMRYTVKQMKMYRGFQIMPHVQYIYTEASESLCGVKLEVNKYQYLITGRVYEGKVYTGLCNWYEKWDRLTLSQRKGLNHRYHLGCGCKIRPCYYLPCFATSKNECIWTDMLSNFGHSGHQAKHYACIQRVEGYCSWYRGWAPPDKTIINATDP	Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli.	P26652
Q6GNI4	EIF3K_XENLA	eIF-3 p25	Xenopus	MASFEQMRANVGKLLRGIDRYNPENLATLERYVETQAKENAYDLEANLAVLKLYQFNPAFFQTTVTAQVLLKALTNLPHTDFTLCKCMIDQAHQEDRPIRQILYLGDLLETCHFQSFWQALDENLDLIDGVTGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLSEPQLRVWMSKYGWIESENGKIFVCNQEENIKPKNIVEKIDFDSVSGIMASSQ	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.	Q6GNI4
B7GZN3	CCA_ACIB3	Phosphatase	Acinetobacter calcoaceticus/baumannii complex	MQVYLVGGAVRDYLLGHPYQEKDYVVVGATPEHMLAQGFQPVGKDFPVFLHPETKEEYALARTERKSGQGYHGFQFFTDTTVSLEDDLIRRDLTINAIAMDQDGKIYDPYGGQNDLENKILRHVSEAFAEDPLRVLRVARFAARYFPYGFQIAPETLQLMQTMADSGELDALTPERVWKETSRALMENHADIYFQTLRDCGALKHLFPEIDALFGVPQRPEYHPEVDCGIHTLMSLQQACKSNYSLDVRFAVLVHDLGKALTPAEELPRHIMHEERGIKPVTQLCERLRVPTQTKQLALSVCKEHLKCHQIMSLKPGTLWRLLQRLDVLRRPERVEAFVQACECDAKGRLGLEDRPYPQAQYMREAMQIVRSIKVQDLPENIKGAEIGEMLIQYRIEALAEFKNQHQSLSHS	Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.	B7GZN3
A0KJH4	CDD_AERHH	Cytidine aminohydrolase	Aeromonas	MHPRFAKPLDTLSAPLKAALLPMLGDDFQARFTPDQVATLKAATGLDDRALRLALLPLAAACSVAPISKFFVGAIACGLSGNWYFGANMEFAGQGLFHSVHAEQSAISNAWLGGETGISEITVNYTPCGHCRQFMNELSTAKILKVSLPDDLSALQSFLPHSFGPADLDITDALMSPQAHDELTLVSDDPLWQAALAAARQSYAPYSQGYAAVALQFADGRIFCGRYAENAAFNPSLPPMQMACAHAVLGGEDLATIRRAVLLESKDGQISQQDSARATLKALGSVELEYQAV	This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.	A0KJH4
Q4A7W5	RUVA_MESH7	Holliday junction ATP-dependent DNA helicase RuvA	Mesomycoplasma	MQIYQFGKIVSKNKNYLILENHGSGYLIYVPRIDRFSRDENRKIYIYEHENDYTKITYGFASFRERILFEDLISIQGVGPKTAISALNSGMQNLINLIAANDWKTLAKIPYLSEKNAKQIVFEFQKKYERFNENHKNQTEETNQDSQEKELEKNDDLADITIQKSNLEDKTAANLEDTLKMLGFKPRQIDYALTKVEPNENFENLIENAIKIISNAREFRN	The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.	Q4A7W5
B1V9R1	RSGA_PHYAS	Small ribosomal subunit biogenesis GTPase RsgA	16SrXII (Stolbur group)	MKKALVIRFLAGIYYIQDLDNQTILKAQKKGVLKKSNFIQDNQLKNNRDKMSIKVGDIVLYGMCYDKYLIYAILPRKNELKRPNIANIDQVLLVFSLVKPHFQTLLLDKFLLILQQHKLDVILVFSKIDLIEKEELEEIQQNMNYYFPFYTCYYVDSKQQIGIGVLKNIFEQKITVLAGQTGVGKSTLLKALIPDANLKTQEISESLGRGKHTTKNAQLYLFNNGFIADTPGFSKLDLGGFSYQNLKNFYPDFLKYVDNCYFGTNCLHLQETQCGVKEALTQGKIIPSRYSNYCYFMEEIKKEKKIYVKN	One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.	B1V9R1
A4W527	HLDD_ENT38	ADP-L-glycero-beta-D-manno-heptose-6-epimerase	Enterobacter	MIIVTGGAGFIGSNIIKALNDKGITDILVVDNLKDGTKFANLVDLNIADYMDKEDFLIQLMAGEEFGEIEAIFHEGACSSTTEWDGKYMMDNNYQYSKEVLHYCLEHEIPFLYASSAATYGGRTSDFIESREYEQPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGETPKLFEGSDGFKRDFVYVGDVAAVNLWFWENGVSGIFNLGTGRAESFQAVADAALAFHKKDSLEYIPFPEKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVAEYMAWLNRN	Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.	A4W527
Q94913	REG5_DROME	dReg-5	Sophophora	MTTAAKVILACCLLGAFHIQISSSSAIPIWEFLTRNEKMSHLYSTFAQLVSVHCKSTAAVGGLPVNQCKHNLLGYGSAKLQTLSDVQLEALDPYQRDANELIWSSIMGDHPSGASLVTTRQPLQQPLPTPPASSLIILTRQQLPHGASHAHPIQSSGSATNPIFESGEQKHKYAMDMDKAYGYGPQSSSELPMAAALTSEPSKRFLTGPLVIRVRPDGSPVEEDKMMPLPRDEDLPYFHLGLAAAQPNRHRKIATISSLKQQHFASILQSDLQPPHQTQRRLFRQQQA	Involved in the generation of biological rhythms (Potential). In the head, oscillates in abundance with a daily peak during early night, even under constant darkness. Oscillation is dependent on period (per) function.	Q94913
A7FHL4	SLYA_YERP3	Transcriptional regulator SlyA	Yersinia	MESTLGSDLARLVRVWRALIDHRLKPLELTQTHWVTLYNINRLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCANDRRAKRIKLTEQSSPIIEQVDGVICSTRKEILGGISSDEIAVLSGLIDKLEKNIIQLQTK	Transcription regulator that can specifically activate or repress expression of target genes.	A7FHL4
O70157	TOP3A_MOUSE	DNA topoisomerase III alpha	Mus	MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPKDLNLVALVEQQTVDPHWGAFAQTILERGGPTPRNGSKSDQAHPPIHPTKYTSGLQGDDRRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLIILARNYLDVYPYDHWSDKLLPVYEQGSHFQPSTVEMVDGETSPPQLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTSDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICEGKKDKFQVLRQQVQKYKQVFIEAVAKAKKLDEALSQYLGERTEMAQQEEIYPAMPEPVRKCPQCNKDMVLKTKKSGGFYLSCMGFPECRSAVWFPDSVLEASRDNSVCSVCQPPPVYRLKLKFKRGSLPPAMPLEFVGCIGGCDETLKEIFGLRFPRALPRASQPSGHLQASQALNRMDSSQHNLSQPLVNRHTRPSKTVAQALLPPTTAGESNSVTCNCGREAVLLTVRKQGPNQGRHFYKCSNGDCNFFLWADSSHSTGGGTPTSASGPPGSSVGCPSSVGSHMDGFGSLGSDSDGGTPCLCGQPAVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENVAPGSFAAPAWPGGRGKAQRPEAASKRPRAGSSDAGSTVKKPRKCSLCHQPGHTRTFCPQNR	Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2.	O70157
Q92GY3	RS5_RICCN	30S ribosomal protein S5	spotted fever group	MSKVKKNDETLSEVLVDVNRVTKVVKGGRSFAFSAYVVVGDKAGRVGAGHGKAKEVNEARGKAKQAAKKRMMKVPLYQNRTIHHDVVGKSGAAKVILRRAKAGTGIIAGGSMRAIFDSLGVHDIVAKSIGSTNVYAMISATFDALNKLASPKSIAMRRDKKVNEISVKSAEIQVNE	Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.	Q92GY3
P42848	ENO_THEMA	2-phosphoglycerate dehydratase	Thermotoga	MYVEIVDVRAREVLDSRGNPTVEAEVVLEDGTMGRAIVPSGASTGKFEALEIRDKDKKRYLGKGVLKAVENVNETIAPALIGMNAFDQPLVDKTLIELDGTENKSKLGANAILAVSMAVARAAANYLGLPLYKYLGGVNAKVLPVPLMNVINGGQHADNNLDLQEFMIVPAGFDSFREALRAGAEIFHTLKKILHEAGHVTAVGDEGGFAPNLSSNEEAIKVLIEAIEKAGYKPGEEVFIALDCAASSFYDEEKGVYYVDGEEKSSEVLMGYYEELVAKYPIISIEDPFAEEDWDAFVEFTKRVGNKVQIVGDDLYVTNVKRLSKGIELKATNSILIKLNQIGTVTETLDAVEMAQKNNMTAIISHRSGESEDTFIADLAVATNAGFIKTGSLSRSERIAKYNQLLRIEEELGKVAEFRGLKSFYSIKR	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.	P42848
Q2HW56	NOOT1_MEDTR	Protein NODULE ROOT 1	Medicago	MSLEDSLRSLSLDYLNLLINGQAFSDVVFSVEGRLVHAHRCILAARSLFFRKFFCGPDPPSGLDPSGNRVNPSGSARSGVIPVNSVGYEVFLLMLQFLYSGQVSIVPQKHEPRPNCGDRGCWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMHQLWTTCSHLVAKSGLPPEVLAKHLPIDIIAKIEELRIKTSLSRRSLMPHHHHPHHHDHLTAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALPYAVENCSREVVKALLELGAADVNFPAGPTGKTPLHIAAEMVSPDMVAVLLDHHADPNVRTVDGVTPLDILRTLTSDFLFKGAVPGLTHIEPNKLRLCLELVQSAALVMSREEGNNNNSNNNNNATASSATNMYPHHNMNEDHHHSHNNNNMDSRLVYLNLGANTQMSTSRMDSGDDDNTHREAINNSMYHHHSHGHDY	Involved in the promotion of leaf and floral meristem fate and determinacy . Promotes normal stipule growth and development . Involved in the coordination of the symbiotic nodule developmental program . Necessary for the robust maintenance of nodule identity throughout the nodule developmental program . Involved in the regulation of indeterminate nodule identity in association with NOOT2 .	Q2HW56
B7N1J7	RTCA_ECO81	RNA 3'-terminal phosphate cyclase	Escherichia	MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITGIRAGRAKPGLLRQHLTAVKAAAEICRATVEGAELGSQRLVFRPGTVRGGDYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGVHQQTTLLRHGFYPAGGGVVATEVSPVASFNSLQLGERGNIVQMRGEVLLAGVPRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASPAAVGEYLADQLVLPMALAGAGEFTVAHPSCHLQTNIAVVERFLPVRFSLIETDGVTRVSIE	Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.	B7N1J7
C0QKY2	TGT_DESAH	tRNA-guanine transglycosylase	Desulforapulum	MLTFDIINQSLESRARTGRITTAHGVIETPIFMPVGTLGTVKAVSVEELKACQAQIILGNTYHLYLRPGCEVMAHMGGLHPFMNWDRPILTDSGGFQFFSLAKLAKFKDEGVSFQSHIDGSRHLFTPERAVEIQSILGSDIMMSLDWCMGYPATRKEAMGALEKTTQWAERGRNFWIEQGRVNNLFGIVQGGMFADLRSISARQLADLDFPGYAIGGLSVGEPTELMYEMADHTVPQLPLEKPKYVMGVGTPENLVELAGMGVDMFDCVMPSRNARNGQLFTSTGTMNISNAAFRLDESPLDAECSCYTCQNYSRAYLRHLYKSRELLAYRLNTIHNLHYYLDLMHQMRNAINQGRFMAFKQEFYRKRER	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).	C0QKY2
Q8G0G3	ENO_BRUSU	2-phosphoglycerate dehydratase	Brucella	MTAIIDIVGREILDSRGNPTVEVDVVLEDGSFGRAAVPSGASTGAHEAVELRDGGSRYLGKGVEKAVEVVNGKIFDAIAGMDAESQLLIDQTLIDLDGSANKGNLGANAILGVSLAVAKAAAQASGLPLYRYVGGTNAHVLPVPMMNIINGGAHADNPIDFQEFMILPVGATSIREAVRYGSEVFHTLKKRLKDAGHNTNVGDEGGFAPNLKNAQAALDFIMESIEKAGFKPGEDIALGLDCAATEFFKDGNYVYEGERKTRDPKAQAKYLAKLASDYPIVTIEDGMAEDDWEGWKYLTDLIGNKCQLVGDDLFVTNSARLRDGIRLGVANSILVKVNQIGSLSETLDAVETAHKAGYTAVMSHRSGETEDSTIADLAVATNCGQIKTGSLARSDRTAKYNQLIRIEEELGKQARYAGRSALKLL	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.	Q8G0G3
Q65G81	ACCA_BACLD	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha	Bacillus	MAGELEFEKPVVELREKISELKKFTQDSDMDLSSEITKLEARLERLEEDIYTNLKAWDRVQIARHPNRPTTLDYIEHLFTDFFECHGDRYFGDDEAIVGGIAKFRGLPVTVIGQQRGKDTKENIRRNFGMPHPEGYRKALRLMKQADKFNRPIICFIDTKGAYPGKAAEERGQSEAIAKNLFEMAGLSVPVISIVIGEGGSGGALALGVANRLLMLENSTYSVISPEGAAAILWKDSGLAKKAAETMKITAPDLKELDIIDHVIKEVRGGAHRDVEQQAAYIDEALKGELKSLLKLDKNELIQQRYNKYKSIGKISTENQYVGIK	Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.	Q65G81
Q89K81	NUSB_BRADU	Antitermination factor NusB	Bradyrhizobium	MADNNKKPAGLTEKKANRRGAARLAAVQALYQMDIAGAGINDIFAEFESHWLGNEVEGDTYLPAEAAFFRDVVSGVVRDQKKLDPLIDEALSKGWPLKRIEAILRAVLRAGAYELQHRKDVPGRVVVSEYVDVANAFVDREETGMVNAVLDQIGRQFRGDEFGRG	Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.	Q89K81
B1IVX4	SULA_ECOLC	Cell division inhibitor SulA	Escherichia	MYTSGYAHRSSSFSSAASKIARVSTENTTAGLISEVVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSREWVQASGLPLTKVMQISQLSPCHTVESMVRALRTGNYSVVIGWLADDLTEEEHAELVDAANEGNAMGFIMRPVSASSHATRQLSGLKIHSNLYH	Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division.	B1IVX4
Q5NF12	RPOA2_FRATT	Transcriptase subunit alpha 2	Francisella	MALENLLHPTNIKIDEYAKNATKFSFEALERGVGYTLGFALKQTMLYSIAGACVTSIKINDGKVTSLEDVIPCDETVADIILNVKSLPVTLAEGVETGTITFELSGSEEEIFSEEAKLSEGLAITEEVFICSYNGGKKLKIEAKVEKGVGFRPAQDNFKDGEFLLDATFSPVVFCDFEIKDARVGRRTDLDKLELNIKTNGNVNCEEALRLAATKIQNQLRNILDIEEINKGIFVEDPTKDINPILLKHVEELNLTARSSNCLKAVNIRLIGELVQKTENELLKAPNFGKKSLTEIKDKLSELGLSLGTLIENWPQDL	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	Q5NF12
Q1GTK9	NUOK_SPHAL	NDH-1 subunit K	Sphingopyxis	MISVGHYLAVSAVLFTLGVLGIFINRKNIIVILMAIELILLAVNINLVAFSAALGDLVGQVFSMFVLTVAAGEAAIGLAILVIYFRGRGTIAVDDANRMKG	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	Q1GTK9
Q88VG4	OBG_LACPL	GTP-binding protein Obg	Lactiplantibacillus	MFVDQVKVDVKAGNGGNGMVAFRREKFVPNGGPAGGDGGRGGSVVLQADEGLRTLMDFRYTRKFKAAAGGNGMIKQMTGRSAKDTIIKVPLGTTVTDAETGELIGDIVNKDQRLVVAKGGRGGRGNIHFASAKNPAPEIAENGEPGDELTIRMELKVLADVGLVGFPSVGKSTLLSVVTSAKPKIAAYHFTTLVPNLGMVRLDDGRDFVMADLPGLIEGAANGVGLGIQFLRHIERTRVILHLIDMSGVEENDPFEDYHKINHELTSYDPDLLKRPQIVVATKMDMPDAEANLEDFKAKLATDDTLPNTPAVYPVSSITQQGLKALLAKTADLLDTTPQFPIKGVDDLKHRDYTTEADADFSIDNPEPGLFVLSGDKLERLFKMTNLDHEESLMRFARQLRGMGVDDALRAAGAKNDDTIQILDYSFQFMD	An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.	Q88VG4
D1BHT8	PSA_SANKS	Proteasome core protein PrcA	Sanguibacter	MSMPFYVSPEQLMKDRADYARKGIARGRSVVVAAYDGGIAFATENPSRALHKISEIYDRIAFAAVGKYNEFENLRVAGVRYADLRGYSYDRSDVDARGLANAYAQTLGTVFTTESKPLEVEIVVAQVGATAHDDQIYRLSYDGSVADEHGFVVMGGEAEQLGTAMTERWRPGLTLSEVLRLVREVLAGPPVDGSPREIPATHLEVAVLDRTRPRRAFRRVAGPVLDDLLASPAGTSGPTGEPGPAGTAATDGGDL	Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.	D1BHT8
A1KWB6	TRUA_NEIMF	tRNA-uridine isomerase I	Neisseria	MDTAQKQRWAITLSYDGSRFYGWQKQADGVPTVQAALETALAQIAGEAVSTTVAGRTDTGVHATAQVVHFDTTAARPQQAWVRGVNAHLPEGIAVLHARQVAPEFHARFDAYGRHYRYLLESVPVRSPLLKNRAGWTHLKLDIGPMRRAAALLIGEQDFSSFRAAECQAKSPVKTIYRADLTQSSGLVRLDLHGNAFLHHMVRNIMGALVYVGSGRLSVEGFAALIQERSRLKAPPTFMPDGLYLTGVDYPEAYGIIRPQIPEWL	Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.	A1KWB6
Q6R653	UN5CL_MOUSE	ZU5 and death domain-containing protein	Mus	MSPQESSVQPSQFLLLVGIPVASALLLAQCLRWHCCQWLPGTCRKPDDPEEPVSPSTPLPEYELPRQCPAPTLPEVAAFYQELHMPTQGQTVTRQMMHKLLVFSAREVDHRGGCLILQDTGISLLIPPGAVTVGRQERVSLVLVWDLTDAPSLSHRQGLVSPVVACGPHGASFLKPCTLTFKHCAQQPSQACAYSSNTSLLDAKDWKPLGQPGTHISRDECRILLSHFSLYTCVLEAPLGQTARKWLQLAMFCSPLVPGQTHLQLRVYFLNNTPCALQWAITNEQPHGGRMRGPCQLFDFTGARADQCLKLKYISEGWENVDDSSSQLVPHLHIWHGKCPFRSFCFRRKAANGNEECSALTNEIIVTMHTFQDGLETKYVEILRFQASEEETWAVPPPVSQPPLCNRLPPELFEQLQMLLEPNSVTGNDWRRLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTSMERLDCASAIQNYLNRSPRGSPDRLHGGTWENHGLELDEKL	Inhibits NF-kappa-B-dependent transcription by impairing NF-kappa-B binding to its targets.	Q6R653
Q0TC48	RTCA_ECOL5	RNA 3'-terminal phosphate cyclase	Escherichia	MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITGIRAGRAKPGLLRQHLTAVKAAAEICRATVEGAELGSQRLVFRPGTVRGGDYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGVHQQTTLLRHGFYPAGGGVVATEVSPVASFNSLQLGERGNIVQMRGEVLLAGVPRHVAEREIATLAASFSLHEQAVHSLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASPAAVGEYLADQLVLPMALAGTGEFTVAHPSCHLLTNIAVVERFLPVRFGLIETDGVTRVSIE	Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.	Q0TC48
Q5QY15	SYV_IDILO	Valyl-tRNA synthetase	Idiomarina	MDKTYSPAAIEQDLYQQWEDKGYFKPSGKGDPYSIMIPPPNVTGSLHMGHAFQHTIMDTLTRYQRMDGLNTLWQVGSDHAGIATQMVVERQLAAQGQTRQELGRDAFIDKIWEWKEQSGGTITQQMRRLGDSVDWDRERFTMDEGLSDAVREVFVKLHEDNLIYRGKRLVNWDPALQTAISDLEVENKEQQGYIWYLRYPLADGEKTEDGKDHLVVATTRPETMLGDVCVAVHPDDERFAHLVGKFLELPIVNRRIPIVADHHVDSEFGTGCVKVTPAHDFNDYEIGKRHQTGMISIFDDTAHVMAKAGLYTSTGETLEELNGFNGILPEQYAGKERFEARKQLVAEFDELGLLEKIEKHTNKIPYGDRGGVPIEPHLTDQWYVRVEPMAKQATAAVEDGRIEFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDEQGNVYVGRTEEEVREKHNLGDTPLQQDEDVLDTWFSSALWTFSTLGWPKNTEDLKTFHPTDVLVTGFDIIFFWVARMIMMTMHFMKDEEGQPQVPFKKVYVTGLIRDEEGQKMSKSKGNVLDPLDMIDGISADELVAKRTANLMQPKMREKIEKRTRKEFPEGITAHGTDALRFTLTALASTGRDINWDMKRLEGYRNFCNKLWNASRYVLMSTEEHDCGLENDDMTLSLADEWIIARFNSTVKDFRQALDTYRFDQAAAIAYEFTWNQFCDWYLELTKPVLQNGTESQQRGTRHTLVNVLEQLLRLLHPVMPYITETIWQRVKPLVGNTDDTIMLQPFPRVEDNVSHQAMQDMEWLKRVILAIRNIRGEMDLSPNKPLPLLLSNADAMAKGRIQNNESFLSSLAKLESIEFIESDDDAPASMTALVDTLKLHIPMAGLIDKEAELQRLQKSIEKANKEWQRLNGKLSNDNFVSKAPEAVIAKEREKLSEAETTLKQLQEQQDKIKAL	Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.	Q5QY15
A1USC8	RPOB_BARBK	Transcriptase subunit beta	Bartonella	MAQTLAMMSQFNGRKRVRKFFGKIPEVAEMPNLIEVQKASYDQFLMIKEPKGGRPDEGLQAVFKSVFPISDFSGTAMLEFVRYEFDAPKFDVEECRQRDLTYAAPLKVILRLIVFDIDEDTGSKDIKDIKEQGVYMGDMPLMTSNGTFIINGTERVIVSQMHRSPGVFFDHDKGKSHSSGKVLFAARVIPYRGSWLDIEFDAKDIVYARIDRRRKIPVTSFLMALGMDASDILSTFYNKVTYERVESGWRIPYSVDRFKGVKLVSDLVDAESGEVVAEAGKKLTARTAKLLVEKGLKAIRVSEDELLGSYLADDIVNYETGEIYLEAGDEIDEKVLKVLFDVGANQINILDIDHMSVGAYIRNTLKVDKNESRQDALFDIYRVMRPGEPPTIDTAEAMFHSLFFDSERYDLSAVGRVKMNLRMGLDCPDTVRVLRQEDIIGVVKMLVELRDGRGEIDDIDNLGNRRVRSVGELMENQYRVGLLRMERAIKERMSSVEIDTVMPQDLINAKPAAAAVREFFGSSQLSQFMDQTNPLSEITHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRICPIETPEGPNIGLINSLATFARVNKYGFIESPYRKITDGKVTTEVVYLSAMEEAKHYVAQANSSLDSEGRFTEEFVVCRHAGEVLMVPRDHIDLMDVSPKQLVSVAASLIPFLENDDANRALMGSNMQRQAVPLIRSEAPFVGTGMEAIVARDSGAAISAKRGGIVDQVDATRIVIRATEDLDPSKSGVDIYRLQKFQRSNQSTCINQRPLVHVGDRIEKGDIIADGPSTDLGDLALGRNVLVAFMPWNGYNYEDSILLSERIVADDVFTSIHIEEFEVAARDMKLGPEEITRDIPNVAEEALRNLDEAGIVYIGAEVQPGDILVGKITPKGESPMTPEEKLLRAIFGEKASDVRDTSMRMPPGTFGTVVEVRVFNRHGVEKDERAMEIEREEIERLAKDRDDEQSILDRNVYARLAGMLKDKSAIRGPKGFEKGQKIDSTVLNNYPRSQWWQFAVDDEKVQNKIEALCNQYDESKEALQRRFMDKVEKVQRGDEMPPGVMKMVKVFVAVKRKIQPGDKMAGRHGNKGVVSRILPVEDMPFLEDGTHADIVLNPLGVPSRMNVGQILETHLGWACAGMGKKIGDLVDFYQETGDILPLRQRIENLIPDNDRNEPVRQYDDESLVKLAHQMRKGVSIATPVFDGAHEADINAMLEDAGLDSSGQVTLYDGRTGEPFDRQVTVGYIYMLKLHHLVDDKIHARSIGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVAGRTKVYEAIVRGDDTFEASIPESFNVLIKEMRSLGLNVKLGDAREFMAQQALPEVVEN	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	A1USC8
B2KAX0	DNAK_ELUMP	Heat shock protein 70	Elusimicrobium	MARIIGIDLGTSNTAAAAMEGGRATIIPSAEGSSIGGKAFPSYVAFTKDGQRLVGEPARRQAIANPEGTVTAFKRRMGEDYKFTLRGQEFTPQQLSAFVLQKVKKDAEAFLGEPVEKAVITVPAYFNDNQRQATKDAGRIAGLEVVRLVNEPTAAALAYGIDKAGKEQKIMVFDLGGGTLDVTIMEMGKEGTFDVLSTSGDTKLGGTDMDNAIIEWMVSEFKKSTGIDLSADKQAAQRLKDAAEKAKIELSTTMETDINLPFISAGADGPKHLELKLSRAKLESLVDSIVKRCGASIDQALNDSSLKSTEIDKIILVGGPTRMPIVQKYVEDHAGKKIERGIDPMECVATGAAVQAGILTGDVKDVLLLDVTPLSLGLETLGGVTTRLIERNTTIPVRKTQVFSTASDNQPAVTINVLQGERPMAKDNVPLGKFDLDGIPPAPRGVPQIEVTFDIDANGILNVSAKDLGTNKQQHITITSKTKLSDDEVQKFVKEAEKFADEDKKTKERVDAKNEADSVLFQTEKALKEHGDKVPQEDRLNIDRALGDLKEALKGDDVERIKKAKDDALAASQKLGEIIYKESQAKAQGAAGPQPGAQAQGQPNDGGKEDVVEAEVVDK	Acts as a chaperone.	B2KAX0
Q9SHL8	PILS5_ARATH	Auxin efflux carrier-like protein 5	Arabidopsis	MGFWSLLEVASMPVIQVLFMSLVGAFMASDRCKLFPVEARNSMNKVVFVLFAPALMFANLAQTVTLEDIISWWFMPVNMGLTFLIGGLLGWLVVKILKPPPYLEGLIVATCSAGNMGNLPIILVPAICDEDKSPFGNRSVCRTVGLSYASFSMALGGFYIWTYTFRLIKGSAMKVQAIEESEKIAIKSSNSDLEADHKTHLLGAPEDKENKVVKEKTGFWRKGVDFLHEILEELLAPPTLGAIIGFIFGAVRWLRNLIIGDDAPLRIVQSTAKLLGDGTIPCMTIILGGNLIQGLRSSAVKPMVVLGIVCVRYIAMPIIGIGIVLTAANLGFLPADPLFQYVLMLQFTLPPAMNIGTMTQLYNVAQDECSVLMLWTYLVAILALTVWSTIFLHLLV	Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.	Q9SHL8
B2JKH5	BIOD_PARP8	Dethiobiotin synthase	Paraburkholderia	MSPALSLFVTGTDTEIGKTLVSAALLRGFVRDGLRAAAMKPIAAGATLVNGVLHNEDADQLDAAANVLLPPDIRTPFMLKEPAAPHIAAAHESVTLDMARIVDAHEAALQMADVVVVEGVGGFRVPLTDSHDTADLAFALNLPVVLVVGMRLGCISHALLTAEAIAARGLRVVGWVANRVDPAMLFPDENIDTLRDRLARQYDAPLLGSVPHLSPASPDVAATHLDTTRLLHALRTAPR	Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.	B2JKH5
Q03EL1	ATPD_PEDPA	F-type ATPase subunit delta	Pediococcus	MSLDKTTIAKRYSKALFEIVSEKGQRDETRAELNQIQQVFNDNEGLGKILTDKGLEQNQKLEILNILTKDASNYVGNLIKMTFDYGRMDYLTAIIDEFNNLCDADEKIVRAKVVSAIPLSDQQLDKMAEQFAKRLKVSEVVLDSEVDDSIIGGAIIKTDSLIYDGSIQTQINQIRQRLIG	This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.	Q03EL1
Q5P6P9	APAH_AROAE	Diadenosine tetraphosphatase	Aromatoleum	MAIYAIGDIQGCFREFRELVDQCGFDPSSDRLWLVGDLVNRGPASLETLRFVRSLGDAAVSVLGNHDLYLLKIAYAGASGRKRHDTLQQVLEAPDRDELIAWLRTLPLMHLEGGYAMVHAGLLPGWTAEPARALAREVEAVLSGDSCEAFLQHMWGNSPKAWRDDLAGWERLRVIVNAMTRMRFCTPDGRMEFDAKGPPDSAPPNHLPWFAHPNRASSDTTIVCGHWSALGLRMEPNLLALDSGCVWGEKLTAVRLEDRRVFQVHAGKQLGSF	Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.	Q5P6P9
B8HRT5	DNAA_CYAP4	Chromosomal replication initiator protein DnaA	unclassified Cyanothece	MDISLESLWNQILERLQLQLSRPTFETWIKTATAEAFTEDRLTIRTPNPFARNWIQKYYLKTIADVAHDILGHPVDVQLVIAEGEETPSSEETDLGFAFPPLFRNPSPAPAPQRERMSDLNPKYVFSRYVVGPNNRMAHAACLAVAESPGREFNPLFLCGGVGLGKTHLMQAIGHYRLEICPDSKIFYVSTEQFTNDLIAAIRKDSMQSFREHYRAVDVMLVDDIQFIEGKEYTQEEFFHTFNTLHEAGKQVVLASDRPPSQIPRLQERLCSRFSMGLIADIQPPDLETRMAILQKKAEYENIRLPREVIEYIASSYTSNIRELEGALIRAVAYISISGLPMTVENIAPVLTPTTAKLEASPQTILLAVSDTFGIPIEDLKGNSRRREISVARQVGMYLMRQHTGLSLPKIGEEFGGKDHTTVLYSCEKVADLQRTDPEIAQTLRQLSDRINLASRQTEN	Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.	B8HRT5
D2Q187	MSHD_KRIFD	Mycothiol synthase	Kribbella	MTLEAVPSPLPPATAVAVTELARLAAQSDGVNPLSEQTLLHVDSEHHGDLHVLAYDGEPGTLDVSGLQTAENLIGYAALGPDGSAELVVTPAARRQGTGTALLRMLLDHGKDRLRLWAHGRLPGADELAAHFDLTVARELYFLRRPSAPLPEPGWPEGIDVRAFVPGQDDDAWLEVNARAFATHPEQGAWTTEDLGDRLHQPWFDPEGFFLAVDSKTGALAGFHWTKVEGDEGEVYVVGVDPSYQGTGLGKALTLHGLHHLQEVRGLPAVTLYVDGTNTAARALYEKLGFTTAALDVQYAPATV	Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.	D2Q187
Q9CEU1	AROK_LACLA	Shikimate kinase	Lactococcus	MSIILIGFMGAGKSTVAKLLTENFTDLDQLIEEEIEMTIAEFFELFGEADFRKIENEVFELALQKNIIIATGGGIIENPKNLEALDREAGVVFLTADFETLWERISMDLQNVRPLAQDKKAAQLLFEKRKNDYAKVADLTIDVTDKSPEQIVEEIREKWGIN	Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.	Q9CEU1
Q07UU4	RL19_RHOP5	50S ribosomal protein L19	Rhodopseudomonas	MNLIQTLEKEQFDKLSAGRVIPEFGPGDTVIVNVKVVEGERSRVQAYEGVCIGRSGGGINESFTVRKISYGEGVERVFPLLSPMIDSIKVVRRGKVRRAKLYYLRNLRGKSARITEKKQDRPAKVVAGAAE	This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.	Q07UU4
P95980	DNAG_SACS2	DNA primase DnaG	Saccharolobus	MSFQMKYDIRLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEVKTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETLINLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPIGREVEELTGKEIAKALSNMMPLTQYLKKVQEAEQAIAKNVIAKEEKPIQSETTQQVVQITLPQNILEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIIFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS	RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Can use NTPs but not dNTPs. Binds DNA. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.	P95980

Q4R7X8

ZN322_MACFA

Zinc finger protein 322A

Macaca

MYTSEERCNQRTQKRKIYNVCPQKGKKIFIHVHAITQIDGHIYQCLECKQNFCENLALIMCERTHTGEKPYKCDMCEKTFVQSSDLISHQRIHNYEKPYKCSKCEKSFWHHLALSGHQRTHAGKKFYTCDICGKNFGQSSDLLVHQRSHTGEKPYLCSECDKCFSRSTNLIRHRRTHTGEKPFKCLECEKAFSGKSDLISHQRTHTGERPYKCNKCEKSYRHRSAFIVHKRVHTGEKPYKCGACEKCFGQKSDLIVHQRVHTGEKPYKCLECMRSFTRSANLIRHQATHTHTFKCLEYEKSFNCSSDLIVHQRIHMEEKPHQWSTCESGFLLGMDFVAQQKMRTQTEELHYKYTVCDKSFHQSSALLQHQTVHTGEKPFICNVSEKGLELSPPHASEASQMS

Transcriptional activator. Important for maintenance of pluripotency in embryonic stem cells. Binds directly to the POU5F1 distal enhancer and the NANOG proximal promoter, and enhances expression of both genes. Can also bind to numerous other gene promoters and regulates expression of many other pluripotency factors, either directly or indirectly. Promotes inhibition of MAPK signaling during embryonic stem cell differentiation.

Q4R7X8

P08098

MOBA1_ECOLX

Mobilization protein A

Escherichia

MGLSHKERREYGRSYKRDNNRTAPFSCWPRWIRPGGWSGHGGMSGTTRTGVTARLAFWGGWLSPCLSRAGEKPSCVRTSTRTQIITCCSRLTCSGLPGARAGWLSGLCWRGSGVLLLDGHFAAADEAVNRKLNRRAGAQPATGEMTDVRQPAFRGAGTVNALARFFHGRGPETAGVFLGKDEQGEPVLVPRDTWRKTNIQILGLPGSGKSVMATNALIRSVRDFGDAVVYFDQRGPVAALLPAHCPNFTLLDLRPGKPAQLNLFRDLDQYALKNLLVAGFNLSETGHVADHYRISEQKAAKLIAEQVSAGGKHSAGAGGGVRAAGGPEKGREGADHQAGERGRPERPADGQRHRRGGDNQRRRLLYVIGSMDDEAVIRVQKMLFARCAQIIIARDEFRRWPHASIMLDEIKYLLSKYVLNALGTVRSRDCNLRLAHHAGRLRAAGQDLPADFVKTTVLDNTPIRWFYRAASQESRSGAGQTGEIRVDVERRGPAGRRGTWSISAGTASSRRSRPLFDVNTLQHLLTGSR

This protein is essential to promote the specific transfer of the plasmid in the presence of conjugative plasmids.

P08098

Q6FWV2

ATP10_CANGA

Mitochondrial ATPase complex subunit ATP10

Nakaseomyces/Candida clade

MRVVFQQCTKFSTSCNRAFLARFLKPVMNASPKEHVVKQLLKPVGLNVPPRPNIKYSEGNSWLDLFDGAKTEERIKELEIEFAKSGMYEMATFRKTNGKLFLSPESYWKADKALYFPHLSGRTLSSEDHGNVEDVLRGKTSVIRVFSTQVGDKISREYIKNTELGIDNYENQSCQVIDINFLENKLKSWLFKLSLNNLKSTVPVQRHDNYWLCHREQIPFLMRERLLINNVYSGYIFVVDPNLKIRFMACGPASADEFNKLWKVVGQLSKEKK

Involved in assembly of the mitochondrial F1-F0 complex.

Q6FWV2

A5UGR9

MUTH_HAEIG

Methyl-directed mismatch repair protein

Haemophilus

MIPQTLEQLLSQAQSIAGLTFGELADELHIPVPPDLKRDKGWVGMLLERALGATAGSKAEQDFSHLGVELKTLPINAEGYPLETTFVSLAPLVQNSGVKWENSHVRHKLSCVLWMPIEGSRHIPLRERHIGAPILWKPTAEQERQLKQDWEELMDLIVLGKLDQITARIGEVMQLRPKGANSRAVTKGIGKNGEIIDTLPLGFYLRKEFTAQILNAFLDVKPL

Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.

A5UGR9

V5I2G9

E1172_IXORI

Evasin P1172

Ixodes

FLLKSQLCYCLFGIELIGAGIHALHEDEIFTVDYCGTNCTKQSNGSWTTCPGNCSCYHEDGKTDGFCLSTEYTDFTQFPNLTSEEMDAATPRPE

Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL5 and CXCL8.

V5I2G9

Q48D43

RL16_PSE14

50S ribosomal protein L16

Pseudomonas

MLQPKRTKFRKQMTGHNRGLALRGSKVSFGEFALKSVARGRLTARQIESARRALTRHVKRGGKIWIRVFPDKPVTKKPLEVRMGKGKGNVEYWVAQIQPGKVLYEIEGVTEELAREAFALAAAKLPLATSFVKRTVM

Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.

Q48D43

Q466D1

RL7A_METBF

Ribosomal protein L8e

Methanosarcina

MAQLAKFDVPEELTNKALEALELARDTGKIKKGTNEATKAIERGNAKLVLIAEDIEPAEIIAHIAPLSEEKKAPYIFIKNQKELGAASGLGVSCATVAIVDAGKAGEMVQDIAQKLEALK

Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.

Q466D1

A0A0D3MU35

ORGRE_CUCME

DnaJ-like cysteine-rich domain-containing protein Or

Cucumis

MDRVLVASYPINHLIRPHSFRIDYCWSTCFTSRLNSGKERQKLSSRWRWRSMASDSTDSSSSSSFAPSVESDPSDKTSASFCIIEGPETVQDFAKMELQEIQENIRSRRNKIFLHMEEVRRLRIQQRIKNAELGISKEERENELPNFPSFIPFLPPLSSENLKLYYVTCYSLIAGIILFGGLLAPTLELKLGLGGTSYEDFIRSVHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSNTGALVLIEPVSTLNGEHQPLSLPKTERCQNCSGSGKVMCPTCLCTGMAMASEHDPRIDPFD

Involved in chloroplast differentiation in fruit flesh.

A0A0D3MU35

Q32RL7

PSAI_ZYGCR

Photosystem I reaction center subunit VIII

Zygnema

MSASYLPSILVPLVGLVFPAITMVSLFLYIEQDEIV

May help in the organization of the PsaL subunit.

Q32RL7

Q0VSV6

HEMH_ALCBS

Protoheme ferro-lyase

Alcanivorax

MAYKGQENLEHLNPRKVGVLITNLGTPDAPETGALRRYLREFLSDPRVVEIPRFIWFFILNLVILVIRPRKSAEAYKSVWTEEGSPLLVYSLAQGEGIRQRLQSKYGDDVVVRVAMRYGNPSIASQLQAFEDEGIRKLVVLPLYPQYSGSTNGSTFDAVAQDFMGRRLLPDLRFISHYPDYPPYIQAMAEHIRAYREKNGSADKLVFSFHGVPKRFLLKGDPYFHECHQTSQLLAKALGLSDGQWMTTFQSRFGAEEWLQPYTDATMKSLPGEGVKSVQVFCPGFSADCLETVEEIDQENREYFEEAGGESFAYISALNAEPAHLDALAQLVEDNLQGFLP

Catalyzes the ferrous insertion into protoporphyrin IX.

Q0VSV6

Q8UH15

TAM_AGRFC

Trans-aconitate 2-methyltransferase

Agrobacterium tumefaciens complex

MAWSAQQYLKFEDERTRPARDLLAQVPLERVLNGYDLGCGPGNSTELLTDRYGVNVITGIDSDDDMLEKAADRLPNTNFGKADLATWKPAQKADLLYANAVFQWVPDHLAVLSQLMDQLESGGVLAVQMPDNLQEPTHIAMHETADGGPWKDAFSGGGLRRKPLPPPSDYFNALSPKSSRVDVWHTVYNHPMKDADSIVEWVKGTGLRPYLAAAGEENREAFLADYTRRIAAAYPPMADGRLLLRFPRLFVVAVKK

Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.

Q8UH15

Q9EUT5

GLGA_RHITR

Starch [bacterial glycogen] synthase

Rhizobium

MKVLSVSSEVFPLIKTGGLADVVGALPIALKPYGVETKTLIPGYPAVMKAIRDPVVRLELPDLLGEAATILEVEHAGISFLVLDAPAYYSRTGGPYVDATGKDYPDNWRRFAALSLAGAEIAAGLLPGWRPDLVHAHDWQSALVPVYMRYYPTPELPSVLTIHNIAFQGQFGADIFPGLRLPAHAFSVEGIEYYGDVGFLKGGLQTAHALTTVSPSYAEEILTPEFGMGLEGVIASKAYNLYGIVNGIDADIWNPATDPMIAQTYSAATLKERAINRHRVVEHFGLEEDDGPIFCVVSRLTWQKGMDILAEVASEVVHMGGKLAILGAGDAALEGALFAAAGRHRGRVGVVGRHNEPMSHLMQAGCDAIIIPSRFEPCGLTQLYGLRSGCLPIVARTGGLNDTIIDANHAALQAKVATGIQFSPVTAEGLLQAMRRAMHLFQDRKVWTQMQKQGMKSDVSWGRSAERYAALYSSLVSRGA

Synthesizes alpha-1,4-glucan chains using ADP-glucose.

Q9EUT5

A6TVS0

PYRDB_ALKMQ

Orotate reductase (NADH)

Alkaliphilus

MTKVNMKVNIAGVELKNPVMTASGTFGSGREYGEYVDLNQLGAVVVKGVANEPWKGNPSPRIAETYGGMLNSVGLQNPGVDEFIEKDIPFLRQYNTKIIVNIAGRTIEDYCEVVKKLGDADVDLLELNISCPNVKAGGVCFGTDPFMVEEVTKAVKKVAKQPLIVKLTPNVTDIVPIAKAAVAGGADGISLINTLLGMAIDIHKRKPILANVMGGFSGPAIKPVALRMVYQVANAVDVPIIGMGGIMTGEDAVEFILAGASGVAVGTANFINPRATIDVIEGIQGYMEQYSIKDLKEIRGSL

Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.

A6TVS0

Q8WKE7

MATK_FAGJA

Intron maturase

Fagus

MEEFQRYLELDRFRQHDFLYPLLFREYIYALAHDHGFNSYMLLENIGYDNKSSLLIVKRLITRMYQHNYLMISANDSNQNPFFGYNKNLHSQIISEGFAVIVEIPFSLRLISSFEGAEIVISYKLRSIHSIFPFLEDKLPHLNYTTDVRIPYPIHLEILIQTLRSRVKDASYLHLLRFFLHQYSNWNILIITTKSISIFSKSNPRFFLFLYNSHICQYESIFLFLGNQSSHLRLISSGVLFERLYLHKKIEHFAEVFANDFPVIPCFLKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHFYVWSHPGRIHINQLSKHSLDFWGYFSSVRLNPSVVRSQMLENSFLINNAPKKLDIIVPIIPLIGSLAKARFCNALGHPISKLTRADLSDFEILNRFLRICRNLSHYYSGSSKKKSMYRIKYILRLSCVKTLARKHKSTARAFLKKVGSEFVQEFFTEEEEFLSLIFPRTSFTLRRLYRGRVWYLDIIFINGLANHE

Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.

Q8WKE7

Q8D3H1

FLHD_WIGBR

Flagellar transcriptional regulator FlhD

Wigglesworthia

MSNDNILKNIHEINLSYLLLAQELIKQDKKVASFRLGVCEDTLNKISKLSLSELIKLGAINQLICLLRLDDEKVINCLTRESRVDELQQVHTGIMLSTQLLRSHKSNSNHALKE

Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.

Q8D3H1

A7N5C4

GCSP_VIBC1

Glycine dehydrogenase (aminomethyl-transferring)

Vibrio

MTELLQSLSTQNEFVARHNGPNKSDQQKMLEAINAVSLDSLIDETVPAQIRLEQPMNLAEAKSEADMLAAMRKFADQNQIKRTFIGQGYYNTFTPNVILRNVMENPGWYTAYTPYQPEISQGRLESLLNYQQMVMDLTGMEIANASLLDEATAAAEAMTLCKRAGKSKSNVFFVADDVHPQTIEVVKTRAKFIGFEVLVGALDSLPEQDVFGALVQYPGTTGEVRDLTDLIAKAQANKTLVTVATDLLASALLKPAGEMGADVAIGSAQRFGVPMGYGGPHAAFMATRDKHKRTMPGRVIGVSIDTNGNQALRMAMQTREQHIRREKATSNICTAQALLANMASFYAVFHGAEGLRTIARRTHHMTAILAAGLTKGGFELAHNSFFDTITINTGAQTEDLYAKALAADINLRKLGTQLGVSFDETTTVADVEALFAVFGVKEEVAALSTEIAGNEFAAIPEALRRTTEYLTHPVFNTHHSETQMMRYLKQLENKDFSLTHGMIPLGSCTMKLNAAAEMIPVTWPEFGSIHPFAPADQAAGYAALAKDLKEKLCEITGYDAFSLQPNSGASGEYAGLIAIQRYHESRGEGHRNVCLIPSSAHGTNPATASMVSMKVVVVKCDEEGNIDVTDLAAKIKKHKDNLSSIMITYPSTHGVYEEQVKEVCEMVHAAGGQVYLDGANMNAQVGLTTPGFIGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKSHLAPFLPGHIENGADGENFAVSAADMGSASILPISWAYIAMMGEAGLTDATKVAILNANYVMEQLRPHYPVLYRGSNGRVAHECIIDIRPLKEETGISEEDIAKRLMDYGFHAPTMSFPVAGTLMVEPTESEDLEELDRFCDAMIAIREEMTKVKNGEWPLDNNPLVNAPHTQFDLAKEEWDRPYSRELGCFPSKATKSWKYWPTVNRVDNVYGDRNLICSCPSIDNYED

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.

A7N5C4

D4GVR1

HPRL1_HALVD

HGPRTase-like protein 1

Haloferax

MDQLRQSLLDAPIIEKGDYEYFVHPISDGVPMLEPGLLREIVIKIIRKANLENVDKIVTPAAMGIHISTAVSLMTDIPLVVIRKREYGLDGEVSLHQQTGYSEGDMFINDVNEGDRVLVLDDVLSTGGTMKAVLDALDHIGADVVDTVAIIKKAGPNELDDSDHHVKTLINVTVEDGEVVIVDEHGDD

May catalyze a purine salvage reaction, the substrate is unknown.

D4GVR1

P31105

CHER_BACSU

Chemotaxis protein methyltransferase

Bacillus

MDTYSVFTTKWKQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQALLNETLDRMTINVSEFYRNYKRWEVLETAILPLIKTSRPLKIWSAACSTGEEPYTLAMLLDQQKGLPGYQILATDIDEKALEKAKKGVYQERSLQEVPLSVKDRYFTQNANRSYEVKTEIKKNITFKKHNLLADRYEQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTEQIFNPEKFGLVPADTFFYQKR

Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents.

P31105

Q8DJ45

PTH_THEVB

Peptidyl-tRNA hydrolase

Thermosynechococcus

MALQPCVIVGLGNPGIEYATTRHNVGFRVLDTLAQRYRVQLTQQRRFLGEVAEVLIQGQKVRLLKPTTYMNSSGQSLHALLNFYKLPLERTLVVHDDADLPLGRLRLRLSGSTGGHNGIKSIIQHCHSQQFPRLKVGIAFGDRLQQQTGPRNAVPFVLGHFSATELAILPAVLDLAVDAIELSIQSGVEVAMNRYNGKSIPLPQA

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

Q8DJ45

A5FMT0

GCSP_FLAJ1

Glycine dehydrogenase (aminomethyl-transferring)

Flavobacterium

MKTDAFALRHIGPRETDLQHMLQTIGVDSIEQLVYETLPDDIRLKAPLNLDPAMTEYEFANHIQELGKKNKVFKSYIGLGYHPTIVPAPIQRNIFENPGWYTAYTPYQAEIAQGRLEAILNFQTTVIELTGMEIANASLLDEGTAAAEAMALLFDVRTRDQKKNNTHKFFVSEEILPQTLSVLQTRSTPIGIELVVGNHETFDFSTEFFGAILQYPGKYGQVNDYGAFVAKAKENEIKVAFAADILSLAALTSPGEMGAAVVVGTTQRFGVPMGYGGPHAAYFATKDEYKRSMPGRIIGVSVDANGNRALRMALGTREQHIKREKATSNICTAQVLLAVMAGMYAVYHGPKGLKYIANKVHASAVTTAEALNKLGVFQTNTAFFDTILVKADAQKVKAIAEKNEVNFFYPDAESVSISLNETTSVSDINQIIAIFAEALGKEAVTVSELTTASQLPASLERTSSFLTHDVFNNHHSESQLMRYIKKLERKDLSLNHSMISLGSCTMKLNAASEMLPLSMPNWNSIHPFAPVEQAEGYITMLKKLEQQLNVITGFAGTTLQPNSGAQGEYAGLMAIRAYHLSRNEGHRNVCLIPSSAHGTNPASAAMAGMKIIVTKTTPEGNIDVEDLREKAIEHKDDLSCLMVTYPSTHGVFESSIIEITKLIHENGGLVYMDGANMNAQVGLTNPATIGADVCHLNLHKTFAIPHGGGGPGVGPICVNEKLVPFLPTNPILKVGGEQAITAISSAPYGSALVCLISYGYITMMGAEGLKSATEHAILNANYMKSRFEGHYPILYTGECGRAAHEMILDCRAFKENGIEVGDIAKRLMDYGFHAPTVSFPVAGTLMIEPTESEDLAELDRFCDALISIRKEIEAATADDKNNVLKNAPHTLAMLTSDSWDFPYSREKAAYPLEYIADNKFWPSVRRVDDAYGDRNLVCSCAPIEAYMEN

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.

A5FMT0

B0RZS0

RL24_FINM2

50S ribosomal protein L24

Finegoldia

MKIKNGDTVIVISGKDKGKTGNVIEVLAKKNKVVVEGVNIVTKHQKANGRGVESGLIKKEAPIDVSNVMYYDAKNKKGTRLGYKFEDGKKVRFMKSNNETIK

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.

B0RZS0

Q87SG3

MURC_VIBPA

UDP-N-acetylmuramoyl-L-alanine synthetase

Vibrio

MTIQHTQDLAQIRAMVPEMRRVKCIHFIGIGGAGMSGIAEVLLNEGYEITGSDLSENPVTERLVSKGATVFIGHQASNVEKASVVVVSTAINEENPEVMAARELRIPIVRRAEMLAELMRFRHGIAVAGTHGKTTTTALVTQIYSEAGLDPTFVNGGLVKSAGTNARLGSSRILIAEADESDASFLHLQPMVSIVTNIEADHMDTYGGDFETLKQTFIDFLHNLPFYGQAIVCIDDPVIRELIPRISRQVITYGFSDDADVRIENYHQEGQQGKFTVVRKGRANLDITLNIPGRHNALNASAAIAVATEDDIEDDAILKAMAGTQGTGRRFDHLGEFDTGNGHAMLVDDYGHHPTEVDVTIKAARSGWQDKRLVMIFQPHRYSRTRDLYDDFANVLEQVDVLIMLDVYAAGEKPIAGADGRSLCRTIRSRGKVDPIFVPEIEQLPSVLANVIQDGDLILTQGAGDVGKVAKQLANLELNINKMLG

Cell wall formation.

Q87SG3

Q252U9

FABZ_CHLFF

Beta-hydroxyacyl-ACP dehydratase

Chlamydia

MKEAPVIKLRELLNLLPHRYPFLLVDKVLSYDLEKRSIVAQKNVTINEPFFVGHFPEAPIMPGVLILESLAQAAGVLLGLVLENDRNKRLALFLGIQKAKFRHAVRPGDILTLSAEFSLISSKGGKASARACVGSQVAAEGELSFALVDKESLD

Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.

Q252U9

Q8ZUR9

LIPA_PYRAE

Sulfur insertion protein LipA

Pyrobaculum

MIPSWVSLRAGDYEKIINVRRALSRHGIYTVCEGAKCPNIFHCWGEGTATFMILGEVCTRACRFCAVRTGNPRGYVDWGEVDRLVEAVRELGLKYVVVTSVARDDLPDGGASVFAAVVKKLREVGCVVEVLVPDFGGSPASVKTVVSSGPDVFAHNVETVRRLTPLVRDRRAGYERSLSVLKYAKEFGAPLTKSGLMLGLGETFEEVVETLEDLRRADVDIVTIGQYIKPSGSPRHLNPVRYATPEEFAKIKEVAVSLGFKAVASGPLVRSSYKAYSLYREALKNIVYLG

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.

Q8ZUR9

C4ZBS1

RL23_AGARV

50S ribosomal protein L23

Lachnospiraceae incertae sedis

MANVQYYDVILKPVVTEKSMNAMAEKKYTFLVHPDANKTMIKEAVERMFEGTKVAKVNTMNCEGKNKRRGMVTGKTAKTKKAIVQLTADSKDIEIFAGL

One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.

C4ZBS1

P49043

VPE_CITSI

Vacuolar-processing enzyme

Citrus

MTRLASGVLITLLVALAGIADGSRDIAGDILKLPSEAYRFFHNGGGGAKVNDDDDSVGTRWAVLLAGSNGFWNYRHQADICHAYQLLRKGGLKDENIIVFMYDDIAFNEENPRPGVIINHPHGDDVYKGVPKDYTGEDVTVEKFFAVVLGNKTALTGGSGKVVDSGPNDHIFIFYSDHGGPGVLGMPTSRYIYADELIDVLKKKHASGNYKSLVFYLEACESGSIFEGLLLEGLNIYATTASNAEESSWGTYCPGEIPGPPPEYSTCLGDLYSIAWMEDSDIHNLRTETLHQQYELVKTRTASYNSYGSHVMQYGDIGLSKNNLFTYLGTNPANDNYTFVDENSLRPASKAVNQRDADLLHFWDKYRKAPEGTPRKAEAQKQFFEAMSHRMHVDHSIKLIGKLLFGIEKGPEILNTVRPAGQPLVDDWGCLKSLVRTFESHCGALSQYGMKHMRSLANICNTGIGKEKMAEASAQACENIPSGPWSSLDKGFSA

Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles that accumulate during ethylene-regulated processes such as flower opening and flavedo degreening.

P49043

B5ZBG4

TRUB_UREU1

tRNA-uridine isomerase

Ureaplasma

MYTINKNIIVINKPINWTSNDVVQKVKRIIKAKKVGHAGTLDPNASGILVLGINEGTKLLTKLTLDSKTYVAEIQFGISTNTYDSTGEIISKINKFITLTEIESAIENLYKNEYWQKPPKFSALKINGKKAYELARNNISFEIEPRLVKIFEYNILDFNYEKQILKIIIKVSKGFYVRSFAVDLAARINNLAHLLSLVRTESGQFSINDAIEIEQVYDYWNNINKHSTN

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

B5ZBG4

P15329

GUNX_ACETH

Endo-1,4-beta-glucanase

Acetivibrio

IMKVTQDGSIPQIASNINNWLNTHNPDVVFLWIGGNDLLLSGNVNATGLSNLIDQIFTVKPNVTLFVADYYPWPEAVKQYNAVIPGIVQQKANAGKKVYFVKLSEIQFDRNTDISWDGLHLSEIGYTKIANIWYKYTIDILKALAGQTQPTPSPSPTPTDSPLVKKGDVNLDGQVNSTDFSLLKRYILKVVDINSINVTNADMNNDGNINSTDISILKRILLRN

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

P15329

Q0GY42

KBX2_TITCO

Potassium channel toxin TcoKIK

Tityus

KIKSGWERLTSESEYACPAIDKFCEDHCAAKKAVGKCDDFKCNCIKL

Blocks voltage-gated potassium channels.

Q0GY42

Q6LLW0

RL10_PHOPR

50S ribosomal protein L10

Photobacterium

MALNLQDKKAIVAEVNEAANGALSAVVADSRGVAVGAMTSLRKQARENGVYLKVVRNTLARRAVEGTDFECLKDVFVGPSLIGFSNEHPGAAARLFKDFAKENKDFEFKAAAFEGAVVDAEVLATLPTYDEAIARLMMCMKEASAGKLVRTIAAVRDQKEEAAA

Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.

Q6LLW0

Q02KH3

MTNB_PSEAB

Methylthioribulose-1-phosphate dehydratase

Pseudomonas

MNDNREQLTQQIIDAGRFLYGRGWSPATSSNYSARLDEQRALLTVSGKHKGQLGFDDVLATDLAGNSLEPGKKPSAETLLHTQLYAWNPAIGAVLHTHSVNATVLSRLVRGDRLVLQDYELQKAFAGVTTHEGQVEVPIFDNDQDIARLASRVQPWLEAHPYCPGYLIRGHGLYTWGARMSDALRQVEAFEFLFECELKVLSLSR

Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).

Q02KH3

O29460

COFH_ARCFU

FO synthase subunit 2

Archaeoglobus

MKSIRMLMVMLALDDLLKNPYETFRIADELRRELVGDTVTYVVNRNINFTDICINDCKFCSFRNRKKYLLSLDEIKQKVEEAVEFGCTELCIQGGLLPDADLDFYLSILQAVRDVDKKIHIHAFSPMEVVHAARNSGMTVEEVLKELKKEGLGSMPGTAAEILDDSIRALICPRKLKTAEWVEVIKTAHRVGIPTTATIMYGHIDTWEHRINHLLLIKKIQQETGGITELIPLPFMSKNNELGRYAKGSSGFDDLLMIAIARILLYPEIKNIQASWVKMGQKLAQAALHVGANDLGGTLMEENISKSAGATSGEFMHPEELRELIKIAGRVPKQRDTLYNILD

Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.

O29460

Q57RU6

CRCB_SALCH

Putative fluoride ion transporter CrcB

Salmonella

MLQLLLAVFIGGGTGSVARWMLSMRFNPLHQAIPIGTLTANLLGAFIIGMGFAWFNRMTHIDPMWKVLITTGFCGGLTTFSTFSAEVVFLLQEGRFGWALLNVLINLLGSFAMTALAFWLFSAAAAR

Important for reducing fluoride concentration in the cell, thus reducing its toxicity.

Q57RU6

A7MC64

RTN1_XENTR

Reticulon-1

Silurana

MAANPEVFSGRLEGNVAAARRPGSAQEEEGEAAGGALSCVDQGRTIKAEQAGHPTVAMEITSTDFTSTLHLHDAESKELPGDENGLSYTYLSSDKHSHTDSTYFTGISKKGTESPDIKEFSGVGPRSPKEIPTFDSRGLLSSDSGIEMTPAECSEVNKSLADPTEEEKQEAYKYIDISRSPDMKPQQVLDKDFGENKASTIGQAAPTEQQAYDSVTMSWQKDHYNGNISEYLPYVPYMEEPRKDFGLYNSPTSKEPKSAPVTISFTGMETTLQTEYPENQQGKSDKGLKLSPDMVPTVTVSEPEDNSPESITPPSTDADGYTEPSGLEEQRKYKISEDELISAIKAKEGTKGFSSETNEEKQSYSFNVEKQDFTVLPTRDAPAPLDMEGSSTESGDSEIELVSEDQVGAEEAMQSAYMTFSHIGGPPPSPASPSIQYSILREEREAELDSELIIESCDGSSASEESPKRDQDSPMMKPMIMDIIEEENLSRAESFDASDFESCSLKERKLNMENLAESACYLKGTYHTEIRADMPSTKKEELLPQKKSPEGSAYQSKVLGKTSTLPLKPLPFLSKRKAIELLYWRDIKQTGIVFGSVLLMLFSLTQFSVVSVIAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKSYLDMEISLSQEQIQKYTDCLQAYTNSIVKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLIMAVVSMFSLPVVYDKYQAQIDQYLGLVRTNMNTIVTKIQAKIPGTKQKE

Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity.

A7MC64

Q14FC5

RPOA_POPAL

Plastid-encoded RNA polymerase subunit alpha

Populus

MVREKVRISTRTLQWKCVESRADSKRLYYGRFILSPLMKGQADTIGIAMRRALLGEIEGTCITRAKSKKIPHEFSTITGIQESIHEILMNLKEIVLRSNLYGTHNASICVKGPGCVTAQDIILPPSVEIIDNTQHIASLREPIDLHIGLEIERNRGYCMKPPKNFQDGSYSIDAVFMPVRNANHSVHSYGNGNEKQEILFLEIWTNGSLTPKEALHEASRNLIDLFIPFLHAEEESFHLEKNQHKITLPLFAFHDRLAKLRKNQKEIALKSIFIDQLELAPKIYNCLKRSNIHTLWDLLKNSQEDLMKIEHFRIEDVKHIFGILKIEKHFTINLPKNKF

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Q14FC5

B2FKN7

T23O_STRMK

Tryptophanase

Stenotrophomonas maltophilia group

MSVDNNQRDLEAGIHTDLQGRLTYGGYLRLDQLLSAQQPLSSPPHHDEMLFIIQHQTSELWLKLLGHELRAAIGFLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLGPSSGFQSLQYRYIEFLLGNKNAQMLQVFEHDPAGQAQLRTVLEAPSLYEEFLKYLARFGHAVPAVYEAHDWTQPHVADDALQPVFERIYQDTDRYWREYALCEDLVDLETAFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLAKALELTFFPELFQVRTSLQAAPPAEQA

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

B2FKN7

P0CH77

HN817_CYRHA

Peptide F8-17.06

Haplopelma

FECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKDI

Postsynaptic neurotoxin.

P0CH77

Q9UJA2

CRLS1_HUMAN

Protein GCD10 homolog

Homo

MLALRVARGSWGALRGAAWAPGTRPSKRRACWALLPPVPCCLGCLAERWRLRPAALGLRLPGIGQRNHCSGAGKAAPRPAAGAGAAAEAPGGQWGPASTPSLYENPWTIPNMLSMTRIGLAPVLGYLIIEEDFNIALGVFALAGLTDLLDGFIARNWANQRSALGSALDPLADKILISILYVSLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCFTAFTTAASAYSYYHYGRKTVQVIKD

Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.

Q9UJA2

Q73LG9

ERA_TREDE

GTPase Era

Treponema

MNSGVVTIIGRPSAGKSTFLNTASGEKVSIVSAIPQTTRNAIRGIVNTTKGQIVFIDTPGYHKSEKKLNLKLQEIAKTRLEEGDAVLYLIDLSREFGEEEKNICSLLIPLQNKTVIGLNKADLKSSKADLVKKELLSLLPDIPQERIFEISALKDEGINEILSLLIELLPEGEALYPEDIYTDQDVVFRITEIIREQAILHTREEIPHALYAGVEDAEMHKNGKELWVRAFLYVEKESQKAMLIGKGAAVIKSIRIKSMAELRKIFPYKVQLDLQVRVNKNWRQKDNIIKKISY

An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.

Q73LG9

Q5PEH7

CYSJ_SALPA

Sulfite reductase [NADPH] flavoprotein alpha-component

Salmonella

MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPAPEGKMPGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKALKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRAPVAAPSQSVATGAVNDIHTSPYTKDAPLTATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAQALIGLLRPLTPRLYSIASAQAEVESEVHITVGVVRYDIEGRARAGGASSFLAGRVEEEGEVRVFIEHNDNFRLPANPQTPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARCMAVDVEKALLEVIAEFGAMDIESADEYLSELRVERRYQRDVY

Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.

Q5PEH7

P52672

CYSH_THIRO

PAdoPS reductase

Thiocapsa

MSKPDLDAFLHGDDAALRETNRRLESMPAEDRVRWALEHLPPQHVLSSSFGTQSAVMLHLVSRQMPEIPVILVDTGYLFPETYRLVDALTDRFGLNLKVYRPALSPAWQEAGLGRLWEQGADGIERYNRLNKIDPMERALRDLDAGTWFAGLRRQQANSRAELPVLRRQDGRIKFHPIIDWHRPRRARYLRRHDLPDHPLRDQGYVSIGDVHTTVPLLPGMLEEETRFFGIKRECGLHR

Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.

P52672

Q330A4

NU2M_NYCAL

NADH dehydrogenase subunit 2

Nyctimene

MNPLIFTMILLTVMLGTAIVMTTSHWVMAWIGFEMNMLAVIPILMKKYNPRSMEASTKYFLTQATASMLLMLAIVINLVYSGQWSMTKPLTSTTSIIMTLALAMKLGLAPFHFWVPEVTQGVQLSSGLILLTWQKLAPMSILYQISPTINLDLLLLMSLLSILVGGWGGLNQTQLRKIMAYSSIAHMGWMTAIMVYNPTMALLNLVIYILLTTTTFMMLMMNSSTTTLSLSHMWNKTPLLTTAILTIMLSLGGLPPLSGFTPKWMIIQELTKNDNMIMPTIMAVMALLNLYFYMRLTYSTSLTMFPSTNNMKIKWQFSHKKPTANLSPLIILSTLILPLSPMLALLE

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.

Q330A4

O74898

DPH5_SCHPO

Diphthamide biosynthesis methyltransferase

Schizosaccharomyces

MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHTLVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEHDIGPPLHSVVLVGRDVHDLELEFLRAYAVNLENFDRVAKTYLEK

S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.

O74898

Q8EDK6

BIOB_SHEON

Biotin synthase

Shewanella

MSQLQVRHDWKREEIEALFALPMNDLLFKAHSIHREEYDPNEVQISRLLSIKTGACPEDCKYCPQSARYDTGLEKERLLAMETVLTEARSAKAAGASRFCMGAAWRNPKDKDMPYLKQMVQEVKALGMETCMTLGMLSAEQANELAEAGLDYYNHNLDTSPEYYGDVITTRTYQNRLDTLSHVRASGMKVCSGGIVGMGEKATDRAGLLQQLANLPQHPDSVPINMLVKVAGTPFEKLDDLDPLEFVRTIAVARILMPLSRVRLSAGRENMSDELQAMCFFAGANSIFYGCKLLTTPNPEESDDMGLFRRLGLRPEQGAAASIDDEQAVLAKAAAYQDKASAQFYDAAAL

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.

Q8EDK6

A4QG13

IDI_CORGB

Isopentenyl pyrophosphate isomerase

Corynebacterium

MTTEVELVVLADSEGNAIGTAPKATVHTKDTPLHFAFSTYILNPRGELLVTRRALSKKTWPGVWTNSMCGHPGPDETNADAIRRRGVDELGLEVDSFLDIQEVLPDYQYRAVDASGIVEWELCPVHLVRLAVGEFVEPLDDEVEEFEWAEPQKLFDAVDATPFVFSPWMVDQLSAPELRQAILEAFDAE

Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).

A4QG13

Q756E2

APT_ASHGO

Adenine phosphoribosyltransferase

Eremothecium

MSINEYAKELKAALAQYPNFPKEGVLFEDFLPIFRSPQLFQKLIDAFKMHLAEAFPETKIDYLVGLESRGFLFGPSLALAIGAGFVPVRKAGKLPGQVVKTTYVKEYEEDVFEMQVDSIPVGATVVVVDDILATGGSAGAAGDLIKQLGATILEFIFVMELDFLKGREKLQAPVFTLLQGQEEALGN

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.

Q756E2

Q9KA25

XERC_HALH5

Tyrosine recombinase XerC

Halalkalibacterium (ex Joshi et al. 2022)

MEIQNDQWVSAFLLYLKMEKNHSPHTIVNYELDLRHFRDFMEQQSIPSFAAVSYAFVRHYLTVLYEQEYARSTVSRKLSTLRSFYQFLVREKWVMENPFLLAHTPKGVKKLPSFLYEEEMEQLLDALNGDSPLQLRNRALFETIYASGLRVSECCGLKLQDVDLSIGTVFVFGKGRKERYVPIGSFACDAIQEYIENGREKLLKKSKSVDLPGDLFLNYRGGPLTERGVRKILHQALDQAALSTRVSPHSLRHSFATHLLNNGADLRVVQDLLGHENLSTTQVYTHVTKDRLRDVYRTHHPRA

Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.

Q9KA25

Q5GTK2

SSRP_WOLTR

Small protein B

unclassified Wolbachia

MEVIAENRKARFEYFILEEFEAGMVLLSSEVKSLRERKVNISDAYVTEKNGEIWLHNMHIAEYKAANKKKHKPKRERKLLLHKKEINKLISQIKTAGVTIVPLSIYFNDKGLVKTRIAIVKGKKLYDKRATIKQREWNRAKSRLSKNNL

Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.

Q5GTK2

P42508

REGA_RHOCA

Photosynthetic apparatus regulatory protein RegA

Rhodobacter

MAEEEFAELGSDRSLLLVDDDNAFLTRLARAMEKRGFQTEIAETVSAGKAIVQNRAPAYAVIDLRLEDGNGLEVVEALRERRPEARIVVLTGYGAIATAVAAVKMGATDYLSKPADANDITNALLAKGEALPPPPENPMSADRVRWEHIQRVYELCDRNVSETARRLNMHRRTLQRILAKRSPR

Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension.

P42508

B6YW71

SECG_THEON

Protein transport protein Sec61 subunit beta homolog

Thermococcus

MAKEKATLPPTGAGLMRFFDEDTKAVKISPRGVIALTLILVALEILLHAFGPQIFG

Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.

B6YW71

Q7VZG7

UBIG_BORPE

3-demethylubiquinone 3-O-methyltransferase

Bordetella

MTTATQSSAPGVNVDQAEVEKFSALAARWWDPESEFKPLHAINPLRLGWIQETAGSLSGKRVLDMGCGGGILSESMAVAGAQVTGIDLAEKSLKIARLHGLESGVKVDYRAVPVEELAAEQPGQYDVVTCMEMLEHVPDPASVVRACAALAKPGGWVFFSTLNRNPKSFLFAIVGAEYVLRLLPRGTHSYDSFIKPSELATSARQAGLEPTGMRGMEYNPITQVYSLSANTSVNYLMSTRK

O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.

Q7VZG7

B7KXI3

DEOB_METC4

Phosphodeoxyribomutase

Methylorubrum

MARALLIVLDSVGIGGAPDADRYGDAGSDTVGHIAEACAAGRGDRPGLRAGPLRMPNLTALGLGLACEGATGRVPPGLAPDGPVRALWGHAVETAAGKDTPSGHWEIAGVPVREAWGHFPDTQPAFPAELTAALIERAGLPGILGDCHASGTAIIEALGAEHVRTGKPICYTSADSVFQIAAHEEAFGLERLYETCRIAREVCDPYRVGRVIARPFLGSAAEGFRRTSHRKDFSVAPPAGTLLDGLEAAGRAVVSVGKIGDIFAHRATGREIKPAGNAACLDAALDAFAGLPEGGFVFLNLVDFDTEHGHRRDVPGYAAELEAFDARLPEIQAVLKPGDLCVITADHGNDPTWTGTEHTREQVPVLAFGPGLTPRALGRRESFADMGASVAAHLGLPPLGAGQAW

Phosphotransfer between the C1 and C5 carbon atoms of pentose.

B7KXI3

Q8DCM1

AROK_VIBVU

Shikimate kinase

Vibrio

MAEKRNIFLVGPMGAGKSTIGRYLAQQLHMEFLDSDTVIEERTGADISWVFDVEGEEGFRKREEAVINDLTLEQGIVLATGGGSVKSRENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPREVLESLAGERNPLYEEIADYTVRTDDQSAKVVANQIVKMLEES

Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.

Q8DCM1

Q8Z9H9

LPL_SALTI

leu operon attenuator peptide

Salmonella

MSYIVRFTGLLLLNAFIVRGRPVGGIQH

Involved in control of the biosynthesis of leucine.

Q8Z9H9

Q5HPU2

TOP1_STAEQ

Untwisting enzyme

Staphylococcus

MADNLVIVESPAKAKTIEKYLGKRYKVIASMGHVRDLPRSQMGVDTEDNYEPKYITIRGKGPVVKDLKKHAKKAKKIFLASDPDREGEAIAWHLSKILELEDSKENRVVFNEITKDAVKDSFKHPRGIEMDLVDAQQARRILDRLVGYNISPVLWKKVKKGLSAGRVQSVALRLVIDRENEIRNFKPEEYWSIEGEFRYKKSKFTAKFLHYKNKPYKLNNKDDVQRITEALNGDQFEITNVNRKEKTRYPAHPFTTSTLQQEAARKLNFKARKTMMLAQQLYEGIDLKRQGTVGLITYMRTDSTRISTSAKSEAQQYINDKYGEQYVSQRKSSGKQGDQDAHEAIRPTSTMRTPDDMKAFLTRDQHRLYKLIWERFVASQMAPAILDTVALDVTQNDIKFRANGQTIKFKGFMTLYVEAKDDKENDKENKLPQLDKGDKVTATKIEPAQHFTQPPPRYTEARLVKTLEELKIGRPSTYAPTIDTIQKRNYVKLESKRFIPTELGEIVYEQVKEYFPEIIDVEFTVNMETLLDKIAEGDMNWRKVIGDFYNSFKQDVERAESEMEKIEIKDEPAGEDCEVCGSPMVIKMGRYGKFMACSNFPDCRNTKAIVKTIGVTCPKCNEGDVVERKSKKNRIFYGCSRYPECDFISWDKPVGRDCPKCHHYLVNKKKGKSSQVVCSNCDYEEEVQK

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.

Q5HPU2

C0M8R7

PYRDA_STRE4

Putative dihydroorotate dehydrogenase A (fumarate)

Streptococcus

MVSTATKIATFAFNNCLMNAAGVYCMTKEELLAIEASEAGSFVTKTGTLAPRQGNPEPRYADTALGSINSMGLPNHGYQYYLDIVTEMQKDQASKHHFLSVVGMSAEETETILKAIQASDYQGLVELNLSCPNVPGKPQLAYDFEATDQLLKKIFSYYTKPLGIKLPPYFDIVHFDQAAAIFNQYPLAFANCVNSIGNGLVIDDEQVVIKPKNGFGGIGGDYIKPTALANVHAFYQRLNSSIQIIGTGGVKTGRDAFEHILCGAAMVQIGTALHQEGPAIFKRITKELQDIMAEKGYQTLDDFRGQLQYKP

Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.

C0M8R7

Q718F4

NDB43_MESMA

Toxin peptide 6

Mesobuthus

MEIKYLLTVFLVLLIVSDHCQAFLFSLIPSAISGLISAFKGRRKRDLNGYIDHFKNFRKRDAELEELLSKLPIY

Has antibacterial activity against Gram-positive bacteria S.aureus, M.luteus, B.subtilis, and Gram-negative bacteria E.coli, and P.aeruginosa.

Q718F4

P76350

SHIA_ECOLI

Shikimate permease

Escherichia

MDSTLISTRPDEGTLSLSRARRAALGSFAGAVVDWYDFLLYGITAALVFNREFFPQVSPAMGTLAAFATFGVGFLFRPLGGVIFGHFGDRLGRKRMLMLTVWMMGIATALIGILPSFSTIGWWAPILLVTLRAIQGFAVGGEWGGAALLSVESAPKNKKAFYSSGVQVGYGVGLLLSTGLVSLISMMTTDEQFLSWGWRIPFLFSIVLVLGALWVRNGMEESAEFEQQQHYQAAAKKRIPVIEALLRHPGAFLKIIALRLCELLTMYIVTAFALNYSTQNMGLPRELFLNIGLLVGGLSCLTIPCFAWLADRFGRRRVYITGTLIGTLSAFPFFMALEAQSIFWIVFFSIMLANIAHDMVVCVQQPMFTEMFGASYRYSGAGVGYQVASVVGGGFTPFIAAALITYFAGNWHSVAIYLLAGCLISAMTALLMKDSQRA

Involved in the uptake of shikimate, an intermediate in the aromatic amino acid biosynthetic pathway.

P76350

P11229

ACM1_HUMAN

Muscarinic acetylcholine receptor M1

Homo

MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC

The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.

P11229

Q6MTV5

ENGB_MYCMS

Probable GTP-binding protein EngB

Mycoplasma

MIKQASFITSSANKSNWIDDDVSEICLIGRSNVGKSSFINSLTNNNKLAKISNTPGKTRLLNFFEINKGEYRLVDAPGYGYAKVDDNLKIQFAKMMEEYFINRRNLKGVFLLLDLRHKPSNDDIMMYQFLKHYNIPVVIIGTKLDKLKKSEYVKNEKMIKETISFYQEDDFVKISNLNKTNIIKCYELIDKLLGSK

Necessary for normal cell division and for the maintenance of normal septation.

Q6MTV5

A7GCD9

SYE_CLOBL

Glutamyl-tRNA synthetase

Clostridium

MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMEELIEAFNYRNINKAPAVFDTKKLKWMNGEYIRALSLDKFHEMALPYYEEALTRDLDTKKISELLHTRVEVLNEIPEQLDFFNNLLEYSPEMYIHKKMKTTYENSLKSLEEVLPKLEALENWTFENIKEVCMNLVKELEVKNGVVLWPIRTAVSGKQFTPGGAFEIADILGKEETLERIKIGIDKLKALQ

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).

A7GCD9

A0A355

PSAJ_COFAR

PSI-J

Coffea

MRDFKTYLSVAPVLSTLWFGALAGLLIEINRFFPDALTFPFFSF

May help in the organization of the PsaE and PsaF subunits.

A0A355

P26652

TIMP3_CHICK

Tissue inhibitor of metalloproteinases 3

Gallus

MTAWLGFLAVFLCSWSLRDLVAEACTCVPIHPQDAFCNSDIVIRAKVVGKKLMKDGPFGTMRYTVKQMKMYRGFQIMPHVQYIYTEASESLCGVKLEVNKYQYLITGRVYEGKVYTGLCNWYEKWDRLTLSQRKGLNHRYHLGCGCKIRPCYYLPCFATSKNECIWTDMLSNFGHSGHQAKHYACIQRVEGYCSWYRGWAPPDKTIINATDP

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli.

P26652

Q6GNI4

EIF3K_XENLA

eIF-3 p25

Xenopus

MASFEQMRANVGKLLRGIDRYNPENLATLERYVETQAKENAYDLEANLAVLKLYQFNPAFFQTTVTAQVLLKALTNLPHTDFTLCKCMIDQAHQEDRPIRQILYLGDLLETCHFQSFWQALDENLDLIDGVTGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLSEPQLRVWMSKYGWIESENGKIFVCNQEENIKPKNIVEKIDFDSVSGIMASSQ

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.

Q6GNI4

B7GZN3

CCA_ACIB3

Phosphatase

Acinetobacter calcoaceticus/baumannii complex

MQVYLVGGAVRDYLLGHPYQEKDYVVVGATPEHMLAQGFQPVGKDFPVFLHPETKEEYALARTERKSGQGYHGFQFFTDTTVSLEDDLIRRDLTINAIAMDQDGKIYDPYGGQNDLENKILRHVSEAFAEDPLRVLRVARFAARYFPYGFQIAPETLQLMQTMADSGELDALTPERVWKETSRALMENHADIYFQTLRDCGALKHLFPEIDALFGVPQRPEYHPEVDCGIHTLMSLQQACKSNYSLDVRFAVLVHDLGKALTPAEELPRHIMHEERGIKPVTQLCERLRVPTQTKQLALSVCKEHLKCHQIMSLKPGTLWRLLQRLDVLRRPERVEAFVQACECDAKGRLGLEDRPYPQAQYMREAMQIVRSIKVQDLPENIKGAEIGEMLIQYRIEALAEFKNQHQSLSHS

Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.

B7GZN3

A0KJH4

CDD_AERHH

Cytidine aminohydrolase

Aeromonas

MHPRFAKPLDTLSAPLKAALLPMLGDDFQARFTPDQVATLKAATGLDDRALRLALLPLAAACSVAPISKFFVGAIACGLSGNWYFGANMEFAGQGLFHSVHAEQSAISNAWLGGETGISEITVNYTPCGHCRQFMNELSTAKILKVSLPDDLSALQSFLPHSFGPADLDITDALMSPQAHDELTLVSDDPLWQAALAAARQSYAPYSQGYAAVALQFADGRIFCGRYAENAAFNPSLPPMQMACAHAVLGGEDLATIRRAVLLESKDGQISQQDSARATLKALGSVELEYQAV

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.

A0KJH4

Q4A7W5

RUVA_MESH7

Holliday junction ATP-dependent DNA helicase RuvA

Mesomycoplasma

MQIYQFGKIVSKNKNYLILENHGSGYLIYVPRIDRFSRDENRKIYIYEHENDYTKITYGFASFRERILFEDLISIQGVGPKTAISALNSGMQNLINLIAANDWKTLAKIPYLSEKNAKQIVFEFQKKYERFNENHKNQTEETNQDSQEKELEKNDDLADITIQKSNLEDKTAANLEDTLKMLGFKPRQIDYALTKVEPNENFENLIENAIKIISNAREFRN

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.

Q4A7W5

B1V9R1

RSGA_PHYAS

Small ribosomal subunit biogenesis GTPase RsgA

16SrXII (Stolbur group)

MKKALVIRFLAGIYYIQDLDNQTILKAQKKGVLKKSNFIQDNQLKNNRDKMSIKVGDIVLYGMCYDKYLIYAILPRKNELKRPNIANIDQVLLVFSLVKPHFQTLLLDKFLLILQQHKLDVILVFSKIDLIEKEELEEIQQNMNYYFPFYTCYYVDSKQQIGIGVLKNIFEQKITVLAGQTGVGKSTLLKALIPDANLKTQEISESLGRGKHTTKNAQLYLFNNGFIADTPGFSKLDLGGFSYQNLKNFYPDFLKYVDNCYFGTNCLHLQETQCGVKEALTQGKIIPSRYSNYCYFMEEIKKEKKIYVKN

One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.

B1V9R1

A4W527

HLDD_ENT38

ADP-L-glycero-beta-D-manno-heptose-6-epimerase

Enterobacter

MIIVTGGAGFIGSNIIKALNDKGITDILVVDNLKDGTKFANLVDLNIADYMDKEDFLIQLMAGEEFGEIEAIFHEGACSSTTEWDGKYMMDNNYQYSKEVLHYCLEHEIPFLYASSAATYGGRTSDFIESREYEQPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGETPKLFEGSDGFKRDFVYVGDVAAVNLWFWENGVSGIFNLGTGRAESFQAVADAALAFHKKDSLEYIPFPEKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVAEYMAWLNRN

Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.

A4W527

Q94913

REG5_DROME

dReg-5

Sophophora

MTTAAKVILACCLLGAFHIQISSSSAIPIWEFLTRNEKMSHLYSTFAQLVSVHCKSTAAVGGLPVNQCKHNLLGYGSAKLQTLSDVQLEALDPYQRDANELIWSSIMGDHPSGASLVTTRQPLQQPLPTPPASSLIILTRQQLPHGASHAHPIQSSGSATNPIFESGEQKHKYAMDMDKAYGYGPQSSSELPMAAALTSEPSKRFLTGPLVIRVRPDGSPVEEDKMMPLPRDEDLPYFHLGLAAAQPNRHRKIATISSLKQQHFASILQSDLQPPHQTQRRLFRQQQA

Involved in the generation of biological rhythms (Potential). In the head, oscillates in abundance with a daily peak during early night, even under constant darkness. Oscillation is dependent on period (per) function.

Q94913

A7FHL4

SLYA_YERP3

Transcriptional regulator SlyA

Yersinia

MESTLGSDLARLVRVWRALIDHRLKPLELTQTHWVTLYNINRLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCANDRRAKRIKLTEQSSPIIEQVDGVICSTRKEILGGISSDEIAVLSGLIDKLEKNIIQLQTK

Transcription regulator that can specifically activate or repress expression of target genes.

A7FHL4

O70157

TOP3A_MOUSE

DNA topoisomerase III alpha

Mus

MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPKDLNLVALVEQQTVDPHWGAFAQTILERGGPTPRNGSKSDQAHPPIHPTKYTSGLQGDDRRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLIILARNYLDVYPYDHWSDKLLPVYEQGSHFQPSTVEMVDGETSPPQLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTSDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICEGKKDKFQVLRQQVQKYKQVFIEAVAKAKKLDEALSQYLGERTEMAQQEEIYPAMPEPVRKCPQCNKDMVLKTKKSGGFYLSCMGFPECRSAVWFPDSVLEASRDNSVCSVCQPPPVYRLKLKFKRGSLPPAMPLEFVGCIGGCDETLKEIFGLRFPRALPRASQPSGHLQASQALNRMDSSQHNLSQPLVNRHTRPSKTVAQALLPPTTAGESNSVTCNCGREAVLLTVRKQGPNQGRHFYKCSNGDCNFFLWADSSHSTGGGTPTSASGPPGSSVGCPSSVGSHMDGFGSLGSDSDGGTPCLCGQPAVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENVAPGSFAAPAWPGGRGKAQRPEAASKRPRAGSSDAGSTVKKPRKCSLCHQPGHTRTFCPQNR

Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2.

O70157

Q92GY3

RS5_RICCN

30S ribosomal protein S5

spotted fever group

MSKVKKNDETLSEVLVDVNRVTKVVKGGRSFAFSAYVVVGDKAGRVGAGHGKAKEVNEARGKAKQAAKKRMMKVPLYQNRTIHHDVVGKSGAAKVILRRAKAGTGIIAGGSMRAIFDSLGVHDIVAKSIGSTNVYAMISATFDALNKLASPKSIAMRRDKKVNEISVKSAEIQVNE

Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.

Q92GY3

P42848

ENO_THEMA

2-phosphoglycerate dehydratase

Thermotoga

MYVEIVDVRAREVLDSRGNPTVEAEVVLEDGTMGRAIVPSGASTGKFEALEIRDKDKKRYLGKGVLKAVENVNETIAPALIGMNAFDQPLVDKTLIELDGTENKSKLGANAILAVSMAVARAAANYLGLPLYKYLGGVNAKVLPVPLMNVINGGQHADNNLDLQEFMIVPAGFDSFREALRAGAEIFHTLKKILHEAGHVTAVGDEGGFAPNLSSNEEAIKVLIEAIEKAGYKPGEEVFIALDCAASSFYDEEKGVYYVDGEEKSSEVLMGYYEELVAKYPIISIEDPFAEEDWDAFVEFTKRVGNKVQIVGDDLYVTNVKRLSKGIELKATNSILIKLNQIGTVTETLDAVEMAQKNNMTAIISHRSGESEDTFIADLAVATNAGFIKTGSLSRSERIAKYNQLLRIEEELGKVAEFRGLKSFYSIKR

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.

P42848

Q2HW56

NOOT1_MEDTR

Protein NODULE ROOT 1

Medicago

MSLEDSLRSLSLDYLNLLINGQAFSDVVFSVEGRLVHAHRCILAARSLFFRKFFCGPDPPSGLDPSGNRVNPSGSARSGVIPVNSVGYEVFLLMLQFLYSGQVSIVPQKHEPRPNCGDRGCWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMHQLWTTCSHLVAKSGLPPEVLAKHLPIDIIAKIEELRIKTSLSRRSLMPHHHHPHHHDHLTAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALPYAVENCSREVVKALLELGAADVNFPAGPTGKTPLHIAAEMVSPDMVAVLLDHHADPNVRTVDGVTPLDILRTLTSDFLFKGAVPGLTHIEPNKLRLCLELVQSAALVMSREEGNNNNSNNNNNATASSATNMYPHHNMNEDHHHSHNNNNMDSRLVYLNLGANTQMSTSRMDSGDDDNTHREAINNSMYHHHSHGHDY

Involved in the promotion of leaf and floral meristem fate and determinacy . Promotes normal stipule growth and development . Involved in the coordination of the symbiotic nodule developmental program . Necessary for the robust maintenance of nodule identity throughout the nodule developmental program . Involved in the regulation of indeterminate nodule identity in association with NOOT2 .

Q2HW56

B7N1J7

RTCA_ECO81

RNA 3'-terminal phosphate cyclase

Escherichia

MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITGIRAGRAKPGLLRQHLTAVKAAAEICRATVEGAELGSQRLVFRPGTVRGGDYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGVHQQTTLLRHGFYPAGGGVVATEVSPVASFNSLQLGERGNIVQMRGEVLLAGVPRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASPAAVGEYLADQLVLPMALAGAGEFTVAHPSCHLQTNIAVVERFLPVRFSLIETDGVTRVSIE

Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.

B7N1J7

C0QKY2

TGT_DESAH

tRNA-guanine transglycosylase

Desulforapulum

MLTFDIINQSLESRARTGRITTAHGVIETPIFMPVGTLGTVKAVSVEELKACQAQIILGNTYHLYLRPGCEVMAHMGGLHPFMNWDRPILTDSGGFQFFSLAKLAKFKDEGVSFQSHIDGSRHLFTPERAVEIQSILGSDIMMSLDWCMGYPATRKEAMGALEKTTQWAERGRNFWIEQGRVNNLFGIVQGGMFADLRSISARQLADLDFPGYAIGGLSVGEPTELMYEMADHTVPQLPLEKPKYVMGVGTPENLVELAGMGVDMFDCVMPSRNARNGQLFTSTGTMNISNAAFRLDESPLDAECSCYTCQNYSRAYLRHLYKSRELLAYRLNTIHNLHYYLDLMHQMRNAINQGRFMAFKQEFYRKRER

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).

C0QKY2

Q8G0G3

ENO_BRUSU

2-phosphoglycerate dehydratase

Brucella

MTAIIDIVGREILDSRGNPTVEVDVVLEDGSFGRAAVPSGASTGAHEAVELRDGGSRYLGKGVEKAVEVVNGKIFDAIAGMDAESQLLIDQTLIDLDGSANKGNLGANAILGVSLAVAKAAAQASGLPLYRYVGGTNAHVLPVPMMNIINGGAHADNPIDFQEFMILPVGATSIREAVRYGSEVFHTLKKRLKDAGHNTNVGDEGGFAPNLKNAQAALDFIMESIEKAGFKPGEDIALGLDCAATEFFKDGNYVYEGERKTRDPKAQAKYLAKLASDYPIVTIEDGMAEDDWEGWKYLTDLIGNKCQLVGDDLFVTNSARLRDGIRLGVANSILVKVNQIGSLSETLDAVETAHKAGYTAVMSHRSGETEDSTIADLAVATNCGQIKTGSLARSDRTAKYNQLIRIEEELGKQARYAGRSALKLL

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.

Q8G0G3

Q65G81

ACCA_BACLD

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Bacillus

MAGELEFEKPVVELREKISELKKFTQDSDMDLSSEITKLEARLERLEEDIYTNLKAWDRVQIARHPNRPTTLDYIEHLFTDFFECHGDRYFGDDEAIVGGIAKFRGLPVTVIGQQRGKDTKENIRRNFGMPHPEGYRKALRLMKQADKFNRPIICFIDTKGAYPGKAAEERGQSEAIAKNLFEMAGLSVPVISIVIGEGGSGGALALGVANRLLMLENSTYSVISPEGAAAILWKDSGLAKKAAETMKITAPDLKELDIIDHVIKEVRGGAHRDVEQQAAYIDEALKGELKSLLKLDKNELIQQRYNKYKSIGKISTENQYVGIK

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

Q65G81

Q89K81

NUSB_BRADU

Antitermination factor NusB

Bradyrhizobium

MADNNKKPAGLTEKKANRRGAARLAAVQALYQMDIAGAGINDIFAEFESHWLGNEVEGDTYLPAEAAFFRDVVSGVVRDQKKLDPLIDEALSKGWPLKRIEAILRAVLRAGAYELQHRKDVPGRVVVSEYVDVANAFVDREETGMVNAVLDQIGRQFRGDEFGRG

Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.

Q89K81

B1IVX4

SULA_ECOLC

Cell division inhibitor SulA

Escherichia

MYTSGYAHRSSSFSSAASKIARVSTENTTAGLISEVVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSREWVQASGLPLTKVMQISQLSPCHTVESMVRALRTGNYSVVIGWLADDLTEEEHAELVDAANEGNAMGFIMRPVSASSHATRQLSGLKIHSNLYH

Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division.

B1IVX4

Q5NF12

RPOA2_FRATT

Transcriptase subunit alpha 2

Francisella

MALENLLHPTNIKIDEYAKNATKFSFEALERGVGYTLGFALKQTMLYSIAGACVTSIKINDGKVTSLEDVIPCDETVADIILNVKSLPVTLAEGVETGTITFELSGSEEEIFSEEAKLSEGLAITEEVFICSYNGGKKLKIEAKVEKGVGFRPAQDNFKDGEFLLDATFSPVVFCDFEIKDARVGRRTDLDKLELNIKTNGNVNCEEALRLAATKIQNQLRNILDIEEINKGIFVEDPTKDINPILLKHVEELNLTARSSNCLKAVNIRLIGELVQKTENELLKAPNFGKKSLTEIKDKLSELGLSLGTLIENWPQDL

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Q5NF12

Q1GTK9

NUOK_SPHAL

NDH-1 subunit K

Sphingopyxis

MISVGHYLAVSAVLFTLGVLGIFINRKNIIVILMAIELILLAVNINLVAFSAALGDLVGQVFSMFVLTVAAGEAAIGLAILVIYFRGRGTIAVDDANRMKG

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Q1GTK9

Q88VG4

OBG_LACPL

GTP-binding protein Obg

Lactiplantibacillus

MFVDQVKVDVKAGNGGNGMVAFRREKFVPNGGPAGGDGGRGGSVVLQADEGLRTLMDFRYTRKFKAAAGGNGMIKQMTGRSAKDTIIKVPLGTTVTDAETGELIGDIVNKDQRLVVAKGGRGGRGNIHFASAKNPAPEIAENGEPGDELTIRMELKVLADVGLVGFPSVGKSTLLSVVTSAKPKIAAYHFTTLVPNLGMVRLDDGRDFVMADLPGLIEGAANGVGLGIQFLRHIERTRVILHLIDMSGVEENDPFEDYHKINHELTSYDPDLLKRPQIVVATKMDMPDAEANLEDFKAKLATDDTLPNTPAVYPVSSITQQGLKALLAKTADLLDTTPQFPIKGVDDLKHRDYTTEADADFSIDNPEPGLFVLSGDKLERLFKMTNLDHEESLMRFARQLRGMGVDDALRAAGAKNDDTIQILDYSFQFMD

An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.

Q88VG4

D1BHT8

PSA_SANKS

Proteasome core protein PrcA

Sanguibacter

MSMPFYVSPEQLMKDRADYARKGIARGRSVVVAAYDGGIAFATENPSRALHKISEIYDRIAFAAVGKYNEFENLRVAGVRYADLRGYSYDRSDVDARGLANAYAQTLGTVFTTESKPLEVEIVVAQVGATAHDDQIYRLSYDGSVADEHGFVVMGGEAEQLGTAMTERWRPGLTLSEVLRLVREVLAGPPVDGSPREIPATHLEVAVLDRTRPRRAFRRVAGPVLDDLLASPAGTSGPTGEPGPAGTAATDGGDL

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.

D1BHT8

A1KWB6

TRUA_NEIMF

tRNA-uridine isomerase I

Neisseria

MDTAQKQRWAITLSYDGSRFYGWQKQADGVPTVQAALETALAQIAGEAVSTTVAGRTDTGVHATAQVVHFDTTAARPQQAWVRGVNAHLPEGIAVLHARQVAPEFHARFDAYGRHYRYLLESVPVRSPLLKNRAGWTHLKLDIGPMRRAAALLIGEQDFSSFRAAECQAKSPVKTIYRADLTQSSGLVRLDLHGNAFLHHMVRNIMGALVYVGSGRLSVEGFAALIQERSRLKAPPTFMPDGLYLTGVDYPEAYGIIRPQIPEWL

Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.

A1KWB6

Q6R653

UN5CL_MOUSE

ZU5 and death domain-containing protein

Mus

MSPQESSVQPSQFLLLVGIPVASALLLAQCLRWHCCQWLPGTCRKPDDPEEPVSPSTPLPEYELPRQCPAPTLPEVAAFYQELHMPTQGQTVTRQMMHKLLVFSAREVDHRGGCLILQDTGISLLIPPGAVTVGRQERVSLVLVWDLTDAPSLSHRQGLVSPVVACGPHGASFLKPCTLTFKHCAQQPSQACAYSSNTSLLDAKDWKPLGQPGTHISRDECRILLSHFSLYTCVLEAPLGQTARKWLQLAMFCSPLVPGQTHLQLRVYFLNNTPCALQWAITNEQPHGGRMRGPCQLFDFTGARADQCLKLKYISEGWENVDDSSSQLVPHLHIWHGKCPFRSFCFRRKAANGNEECSALTNEIIVTMHTFQDGLETKYVEILRFQASEEETWAVPPPVSQPPLCNRLPPELFEQLQMLLEPNSVTGNDWRRLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTSMERLDCASAIQNYLNRSPRGSPDRLHGGTWENHGLELDEKL

Inhibits NF-kappa-B-dependent transcription by impairing NF-kappa-B binding to its targets.

Q6R653

Q0TC48

RTCA_ECOL5

RNA 3'-terminal phosphate cyclase

Escherichia

MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITGIRAGRAKPGLLRQHLTAVKAAAEICRATVEGAELGSQRLVFRPGTVRGGDYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGVHQQTTLLRHGFYPAGGGVVATEVSPVASFNSLQLGERGNIVQMRGEVLLAGVPRHVAEREIATLAASFSLHEQAVHSLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASPAAVGEYLADQLVLPMALAGTGEFTVAHPSCHLLTNIAVVERFLPVRFGLIETDGVTRVSIE

Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.

Q0TC48

Q5QY15

SYV_IDILO

Valyl-tRNA synthetase

Idiomarina

MDKTYSPAAIEQDLYQQWEDKGYFKPSGKGDPYSIMIPPPNVTGSLHMGHAFQHTIMDTLTRYQRMDGLNTLWQVGSDHAGIATQMVVERQLAAQGQTRQELGRDAFIDKIWEWKEQSGGTITQQMRRLGDSVDWDRERFTMDEGLSDAVREVFVKLHEDNLIYRGKRLVNWDPALQTAISDLEVENKEQQGYIWYLRYPLADGEKTEDGKDHLVVATTRPETMLGDVCVAVHPDDERFAHLVGKFLELPIVNRRIPIVADHHVDSEFGTGCVKVTPAHDFNDYEIGKRHQTGMISIFDDTAHVMAKAGLYTSTGETLEELNGFNGILPEQYAGKERFEARKQLVAEFDELGLLEKIEKHTNKIPYGDRGGVPIEPHLTDQWYVRVEPMAKQATAAVEDGRIEFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDEQGNVYVGRTEEEVREKHNLGDTPLQQDEDVLDTWFSSALWTFSTLGWPKNTEDLKTFHPTDVLVTGFDIIFFWVARMIMMTMHFMKDEEGQPQVPFKKVYVTGLIRDEEGQKMSKSKGNVLDPLDMIDGISADELVAKRTANLMQPKMREKIEKRTRKEFPEGITAHGTDALRFTLTALASTGRDINWDMKRLEGYRNFCNKLWNASRYVLMSTEEHDCGLENDDMTLSLADEWIIARFNSTVKDFRQALDTYRFDQAAAIAYEFTWNQFCDWYLELTKPVLQNGTESQQRGTRHTLVNVLEQLLRLLHPVMPYITETIWQRVKPLVGNTDDTIMLQPFPRVEDNVSHQAMQDMEWLKRVILAIRNIRGEMDLSPNKPLPLLLSNADAMAKGRIQNNESFLSSLAKLESIEFIESDDDAPASMTALVDTLKLHIPMAGLIDKEAELQRLQKSIEKANKEWQRLNGKLSNDNFVSKAPEAVIAKEREKLSEAETTLKQLQEQQDKIKAL

Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.

Q5QY15

A1USC8

RPOB_BARBK

Transcriptase subunit beta

Bartonella

MAQTLAMMSQFNGRKRVRKFFGKIPEVAEMPNLIEVQKASYDQFLMIKEPKGGRPDEGLQAVFKSVFPISDFSGTAMLEFVRYEFDAPKFDVEECRQRDLTYAAPLKVILRLIVFDIDEDTGSKDIKDIKEQGVYMGDMPLMTSNGTFIINGTERVIVSQMHRSPGVFFDHDKGKSHSSGKVLFAARVIPYRGSWLDIEFDAKDIVYARIDRRRKIPVTSFLMALGMDASDILSTFYNKVTYERVESGWRIPYSVDRFKGVKLVSDLVDAESGEVVAEAGKKLTARTAKLLVEKGLKAIRVSEDELLGSYLADDIVNYETGEIYLEAGDEIDEKVLKVLFDVGANQINILDIDHMSVGAYIRNTLKVDKNESRQDALFDIYRVMRPGEPPTIDTAEAMFHSLFFDSERYDLSAVGRVKMNLRMGLDCPDTVRVLRQEDIIGVVKMLVELRDGRGEIDDIDNLGNRRVRSVGELMENQYRVGLLRMERAIKERMSSVEIDTVMPQDLINAKPAAAAVREFFGSSQLSQFMDQTNPLSEITHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRICPIETPEGPNIGLINSLATFARVNKYGFIESPYRKITDGKVTTEVVYLSAMEEAKHYVAQANSSLDSEGRFTEEFVVCRHAGEVLMVPRDHIDLMDVSPKQLVSVAASLIPFLENDDANRALMGSNMQRQAVPLIRSEAPFVGTGMEAIVARDSGAAISAKRGGIVDQVDATRIVIRATEDLDPSKSGVDIYRLQKFQRSNQSTCINQRPLVHVGDRIEKGDIIADGPSTDLGDLALGRNVLVAFMPWNGYNYEDSILLSERIVADDVFTSIHIEEFEVAARDMKLGPEEITRDIPNVAEEALRNLDEAGIVYIGAEVQPGDILVGKITPKGESPMTPEEKLLRAIFGEKASDVRDTSMRMPPGTFGTVVEVRVFNRHGVEKDERAMEIEREEIERLAKDRDDEQSILDRNVYARLAGMLKDKSAIRGPKGFEKGQKIDSTVLNNYPRSQWWQFAVDDEKVQNKIEALCNQYDESKEALQRRFMDKVEKVQRGDEMPPGVMKMVKVFVAVKRKIQPGDKMAGRHGNKGVVSRILPVEDMPFLEDGTHADIVLNPLGVPSRMNVGQILETHLGWACAGMGKKIGDLVDFYQETGDILPLRQRIENLIPDNDRNEPVRQYDDESLVKLAHQMRKGVSIATPVFDGAHEADINAMLEDAGLDSSGQVTLYDGRTGEPFDRQVTVGYIYMLKLHHLVDDKIHARSIGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVAGRTKVYEAIVRGDDTFEASIPESFNVLIKEMRSLGLNVKLGDAREFMAQQALPEVVEN

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

A1USC8

B2KAX0

DNAK_ELUMP

Heat shock protein 70

Elusimicrobium

MARIIGIDLGTSNTAAAAMEGGRATIIPSAEGSSIGGKAFPSYVAFTKDGQRLVGEPARRQAIANPEGTVTAFKRRMGEDYKFTLRGQEFTPQQLSAFVLQKVKKDAEAFLGEPVEKAVITVPAYFNDNQRQATKDAGRIAGLEVVRLVNEPTAAALAYGIDKAGKEQKIMVFDLGGGTLDVTIMEMGKEGTFDVLSTSGDTKLGGTDMDNAIIEWMVSEFKKSTGIDLSADKQAAQRLKDAAEKAKIELSTTMETDINLPFISAGADGPKHLELKLSRAKLESLVDSIVKRCGASIDQALNDSSLKSTEIDKIILVGGPTRMPIVQKYVEDHAGKKIERGIDPMECVATGAAVQAGILTGDVKDVLLLDVTPLSLGLETLGGVTTRLIERNTTIPVRKTQVFSTASDNQPAVTINVLQGERPMAKDNVPLGKFDLDGIPPAPRGVPQIEVTFDIDANGILNVSAKDLGTNKQQHITITSKTKLSDDEVQKFVKEAEKFADEDKKTKERVDAKNEADSVLFQTEKALKEHGDKVPQEDRLNIDRALGDLKEALKGDDVERIKKAKDDALAASQKLGEIIYKESQAKAQGAAGPQPGAQAQGQPNDGGKEDVVEAEVVDK

Acts as a chaperone.

B2KAX0

Q9SHL8

PILS5_ARATH

Auxin efflux carrier-like protein 5

Arabidopsis

MGFWSLLEVASMPVIQVLFMSLVGAFMASDRCKLFPVEARNSMNKVVFVLFAPALMFANLAQTVTLEDIISWWFMPVNMGLTFLIGGLLGWLVVKILKPPPYLEGLIVATCSAGNMGNLPIILVPAICDEDKSPFGNRSVCRTVGLSYASFSMALGGFYIWTYTFRLIKGSAMKVQAIEESEKIAIKSSNSDLEADHKTHLLGAPEDKENKVVKEKTGFWRKGVDFLHEILEELLAPPTLGAIIGFIFGAVRWLRNLIIGDDAPLRIVQSTAKLLGDGTIPCMTIILGGNLIQGLRSSAVKPMVVLGIVCVRYIAMPIIGIGIVLTAANLGFLPADPLFQYVLMLQFTLPPAMNIGTMTQLYNVAQDECSVLMLWTYLVAILALTVWSTIFLHLLV

Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.

Q9SHL8

B2JKH5

BIOD_PARP8

Dethiobiotin synthase

Paraburkholderia

MSPALSLFVTGTDTEIGKTLVSAALLRGFVRDGLRAAAMKPIAAGATLVNGVLHNEDADQLDAAANVLLPPDIRTPFMLKEPAAPHIAAAHESVTLDMARIVDAHEAALQMADVVVVEGVGGFRVPLTDSHDTADLAFALNLPVVLVVGMRLGCISHALLTAEAIAARGLRVVGWVANRVDPAMLFPDENIDTLRDRLARQYDAPLLGSVPHLSPASPDVAATHLDTTRLLHALRTAPR

Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.

B2JKH5

Q03EL1

ATPD_PEDPA

F-type ATPase subunit delta

Pediococcus

MSLDKTTIAKRYSKALFEIVSEKGQRDETRAELNQIQQVFNDNEGLGKILTDKGLEQNQKLEILNILTKDASNYVGNLIKMTFDYGRMDYLTAIIDEFNNLCDADEKIVRAKVVSAIPLSDQQLDKMAEQFAKRLKVSEVVLDSEVDDSIIGGAIIKTDSLIYDGSIQTQINQIRQRLIG

This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.

Q03EL1

Q5P6P9

APAH_AROAE

Diadenosine tetraphosphatase

Aromatoleum

MAIYAIGDIQGCFREFRELVDQCGFDPSSDRLWLVGDLVNRGPASLETLRFVRSLGDAAVSVLGNHDLYLLKIAYAGASGRKRHDTLQQVLEAPDRDELIAWLRTLPLMHLEGGYAMVHAGLLPGWTAEPARALAREVEAVLSGDSCEAFLQHMWGNSPKAWRDDLAGWERLRVIVNAMTRMRFCTPDGRMEFDAKGPPDSAPPNHLPWFAHPNRASSDTTIVCGHWSALGLRMEPNLLALDSGCVWGEKLTAVRLEDRRVFQVHAGKQLGSF

Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.

Q5P6P9

B8HRT5

DNAA_CYAP4

Chromosomal replication initiator protein DnaA

unclassified Cyanothece

MDISLESLWNQILERLQLQLSRPTFETWIKTATAEAFTEDRLTIRTPNPFARNWIQKYYLKTIADVAHDILGHPVDVQLVIAEGEETPSSEETDLGFAFPPLFRNPSPAPAPQRERMSDLNPKYVFSRYVVGPNNRMAHAACLAVAESPGREFNPLFLCGGVGLGKTHLMQAIGHYRLEICPDSKIFYVSTEQFTNDLIAAIRKDSMQSFREHYRAVDVMLVDDIQFIEGKEYTQEEFFHTFNTLHEAGKQVVLASDRPPSQIPRLQERLCSRFSMGLIADIQPPDLETRMAILQKKAEYENIRLPREVIEYIASSYTSNIRELEGALIRAVAYISISGLPMTVENIAPVLTPTTAKLEASPQTILLAVSDTFGIPIEDLKGNSRRREISVARQVGMYLMRQHTGLSLPKIGEEFGGKDHTTVLYSCEKVADLQRTDPEIAQTLRQLSDRINLASRQTEN

Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.

B8HRT5

D2Q187

MSHD_KRIFD

Mycothiol synthase

Kribbella

MTLEAVPSPLPPATAVAVTELARLAAQSDGVNPLSEQTLLHVDSEHHGDLHVLAYDGEPGTLDVSGLQTAENLIGYAALGPDGSAELVVTPAARRQGTGTALLRMLLDHGKDRLRLWAHGRLPGADELAAHFDLTVARELYFLRRPSAPLPEPGWPEGIDVRAFVPGQDDDAWLEVNARAFATHPEQGAWTTEDLGDRLHQPWFDPEGFFLAVDSKTGALAGFHWTKVEGDEGEVYVVGVDPSYQGTGLGKALTLHGLHHLQEVRGLPAVTLYVDGTNTAARALYEKLGFTTAALDVQYAPATV

Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.

D2Q187

Q9CEU1

AROK_LACLA

Shikimate kinase

Lactococcus

MSIILIGFMGAGKSTVAKLLTENFTDLDQLIEEEIEMTIAEFFELFGEADFRKIENEVFELALQKNIIIATGGGIIENPKNLEALDREAGVVFLTADFETLWERISMDLQNVRPLAQDKKAAQLLFEKRKNDYAKVADLTIDVTDKSPEQIVEEIREKWGIN

Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.

Q9CEU1

Q07UU4

RL19_RHOP5

50S ribosomal protein L19

Rhodopseudomonas

MNLIQTLEKEQFDKLSAGRVIPEFGPGDTVIVNVKVVEGERSRVQAYEGVCIGRSGGGINESFTVRKISYGEGVERVFPLLSPMIDSIKVVRRGKVRRAKLYYLRNLRGKSARITEKKQDRPAKVVAGAAE

This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.

Q07UU4

P95980

DNAG_SACS2

DNA primase DnaG

Saccharolobus

MSFQMKYDIRLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEVKTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETLINLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPIGREVEELTGKEIAKALSNMMPLTQYLKKVQEAEQAIAKNVIAKEEKPIQSETTQQVVQITLPQNILEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIIFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS

RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Can use NTPs but not dNTPs. Binds DNA. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.

P95980