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 |
|---|---|---|---|---|---|---|
Q32CG3 | CYSJ_SHIDS | Sulfite reductase [NADPH] flavoprotein alpha-component | Shigella | MTTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAEMPGITIISASQTGNARRVAEALRDDLLTAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENIAFAVFSLGDSSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQTAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSDLRYQPGDALGVWYQNDPALVTELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGEKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRTRAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY | 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. | Q32CG3 |
Q2IW74 | PXPA_RHOP2 | 5-oxoprolinase (ATP-hydrolyzing) subunit A | Rhodopseudomonas | MKIDLNCDLGEGFGAWSMGDDAAMMRIATSVNVACGFHAGDPDIMHKTVAMAKAHGVAIGAHPGFRDLHGFGRRPVPGITAAEIENLVAYQIGALQAVASLAGHKVTHVKAHGALSNVACQDDMTARAIAAAIKAVDPKLIFVVLANSKLVDAGEAAGLAMVHEVFADRAYEDDGNLVSRRKPGAVLHDPAVIAERVLRMAQDGAVVSMTGKVIKMRTDTVCIHGDTAGAVDIARGVRTALEANGITVAPFARS | Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. | Q2IW74 |
Q2YBP2 | LPTD_NITMU | LPS-assembly protein LptD | Nitrosospira | MKLRFIRSAGWLFLLFCLACNARADLPPLSSKPEQGRATPSGEGDDKPVVIDTERIRGHHEYESGTRSESELRSRSTISTDQIKKPNQKADPAAKDTPSAPQQNYTLSPAIKTDSRTGTSAQESEKAESMVLPGGVERLPGPAAEEGEPRLRTRTQSAPRTLSAQKRGEKPAKTPAPAEADQDRPGFAEGERIGGHREEAGDEKLRLAGETEPEAIEQKLAEAEAETDKQSPVFVVADRLQGHVEEEIEAIGKAELSAGPQFISAERMKYNQGTNDAEAQGNVRVEKEGDILEGSDLKFNLLSKTGQLSEPSYRLKDASSRGYAGMLLFEGENQYRLQKASYTTCPVGDDSWVLQVADLKLDNDKKVGTAKNVKLTFKDVPILYTPWMNFSYSGERKSGLLAPTYGTGSRTGLELAVPFYWNIAPNYDATFSARLMSKRGLAINNEFRFLGQNSSSNLLADIVPRDLDTQTTRWRTSFWHNHYLGAGFSARLDYNRVSDATYFRDFGNNLNLTSRTNLLQQGLLSYNRGLGDDGTFNVTSLVQSFQTIQDPLAAIVVPYKRLPQVGLNANKPDVFGTGVDVNLSGSWTNFSHPTLVNGSRTVLFPSMSYPLRNSFGFITPKVGMHYTRYSLGEGAGVSEENPTRTLPIFSLDSGLAFDRKMSLGGESFTQTLEPRVFYVYVPFRAQDQLPNFDSAKTDFSFAQMLAENRFSGSDRINDANQVTFALTTRLLESSTGRERLRLAVGHQLSFIDRRITLETPQTIDRRPDFIAAVSGFLTPTISTDTSFQFDQTRLLADVVRSGVSYRPEPGRVLNFGYRFTRDVLHQVDASSQWRWSERWQTVARLNYSLQDKRILEGLAGVEYNACCWSLRFVLQHLTLATQKSTTAAFLQLELNGLMQIGSNPLTVLQRSIPGYIRTGSQGSGLIEGP | Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. | Q2YBP2 |
Q0AQL8 | MURA_MARMM | UDP-N-acetylglucosamine enolpyruvyl transferase | Maricaulis | MDRIVIQGGARLEGRIEISGAKNSALKLMAAALLTDEPVILTRMPRLADSRFLGHLLEKLGVEVSDGQDAQLRLHAATIADTFAPYDLVRKMRASFNVLGPLLAREGHARVSLPGGCAIGARPVDLHLKALKALGAQIEISEGYVSAKAPAGGLVGGEIDLPFASVGATEHAMLAASLARGETVIENAAREPEIGDLADCLTAMGATIEGAGSSTIRIQGQSRLSGVTHKVVADRIETATYALAVAAAGGDAVLEGAVLAHNKALWSSMGEAGVTVEAVADGVRVARNGSRLDSVDIETQPFPGFPTDAQAQFMALMSLANGSSVIRETIFENRFMHAPELARLGADITVHGNEAVVRGVERLRGAPVMATDLRASVSLVIAGLAAEGETVVNRVYHLDRGFERLEAKLTGCGARIERLPDGA | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | Q0AQL8 |
B7HNP5 | OTC_BACC7 | Ornithine carbamoyltransferase | Bacillus cereus group | MSTVQVPKLNTKDLLTLEELTKEEIISLIEFAIYLKKNKQEPLLQGKILGLIFDKHSTRTRVSFEAGMVQLGGHGMFLSGKEMQMGRGETVSDTAKVLSQYIDGIMIRTFSHADVEELAKESSIPVINGLTDDHHPCQALADLMTIYEETNTFKGIKLAYVGDGNNVCHSLLLASAKVGMHMTVATPIGYEPNEEIVKKALAIAKETGAEIEILHNPELAVNEADFIYTDVWMSMGQEGEEEKYTLFQPYQINNELVKHAKQTYRFLHCLPAHREEEVTGEIIDGPKSIVFEQAGNRLHAQKALLVSLFKNVEELS | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | B7HNP5 |
Q7VGP6 | MIAB_HELHP | tRNA-i(6)A37 methylthiotransferase | Helicobacter | MKLFIQTLGCAMNERDSAHMIAELRDKKHYTLTNDIKQADLILINTCSVREKPEKKLFSEIGAFAKEKKAGAKIGVCGCTASHLGEEIIKKAPSVDFVLGARNVSKITQVLERPKAVEVDIDYDDSTYVFASSQGMGIKAHLNISIGCDKKCSYCIVPFTRGKEISVPKDLLISEAKKCVASGAKELLLLGQNVNNYGVRFSHSHPKTNFTQLLRALSEIDGLYRIRFTSPHPLHMDDEFLEEFASNPVIAKGIHIPLQSGSSQILKMMRRGYDKQWYLNRIAKLKSLVPNVGIGTDIIVGFPTESEQDFEDTMEVLSLVEFDTLYSFVYSPRPHTSAFEYDKSMLVSPEVAKERLARLQNLHKEILSKKAQLEIGRIHNVLIENHYNGEGQCWSEGRSSSNKLIKILDKKCEIGSIVKVEITHNEGGGLMGRFINELSLSEALASKEYFQNPIYIQEGALC | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q7VGP6 |
Q95168 | ZO2_CANLF | Zonula occludens protein 2 | Canis | MEELIWEQYTVTLQKDSKRGFGIAVSGGRDNPHFENGETSIVISDVLPGGPADGLLQENDRVVMVNGTPMEDVLHSFAVQQLRKSGKIAAIVVKRPRKVQLAPPQGSLPVDEDDRAFEVMDEFDGRSARSGYSERSRRSSHGGRSRSWEDSPERGRPHERAWSQERERSRGRSLERGLDHDDDYRRPRERSRGRSLERGLDHDDDYGRPGERSHGMSTDRGYDRGYDRGYDRGYDRTYSPEAEYGRRTQPDARHAGSRSRSREHLRSRSPSPELRGRPDHAGQPDSDRPIGVLLMKSKANEEYGLRLGSQIFIKQMTRTALATKDGNLHEGDIILKINGTVTENMSLTDARKLIEKSRGKLQLVVLRDSKQTLINIPSLNDSDSEIEDISEIESNRSFSPEERRQQYSDYDYHSSNEKLKERPNSREDMQNRWSRMGATPTPFKSMGDIASVVGTENSKEPRYQEEPPAPQPKAAPRTFLRPSPEDEAIYGPNTKMVRFKKGDSVGLRLAGGNDVGIFVAGIQEGTSAEQEGLQEGDQILKVNTQDFRGLVREDAVLYLLEIPKGEMVTILAQSRADVYRDILACGRGDSFFIRSHFECEKETPQSLAFSRGEVFRVVDTLYDGKLGHWLAVRIGNELEKGLIPNKSRAEQMASVQNAQRDNAGDRADFWRMRGQRSGMKKNLRKSREDLTAAVSVSTKFPAYERVLLREAGFKRPVVLFGPIADIALEKLANELPDLFQTAKTEPKDAGSEKSSGVVRLNTVRQIIEQDKHALLDVTPKAVDLLNYTQWFPIVIFFNPDSRQGVKTMRQRLNPTSNKSSRKLYDQANKLKKTCAHLFTATINLNSANDSWFGSLKDTIQHQQGEAVWVSEGKMEGMDDDPEDRMSYLTAMGADYLSCDSRLISDFEDTDGEGGAYTDNELDEPAEEPLVSSITRSSEPVQHEESIRKPSPEPRAQMRRAASRDQLRDSSPPPAFKPEPPKAKTQNREESFDISRSHDYKSNPSAVAGNEVSGASTRSCPPPIAAKPSFGRSILKPSTPVPSPESEEVGEGSEEQEGAPKSVLGKVKIFEKMDHKARLQRMQELQEAQNARIEIAQKHPDIYAVPIKTHKPDPGLSQHTSSRPPEPQKGPSRLYQDPRGSYGSDAEEEEYRQQLSEHSKRGYYSQPSRYRDTEL | Plays a role in tight junctions and adherens junctions. | Q95168 |
C3K2V2 | RS4_PSEFS | 30S ribosomal protein S4 | Pseudomonas | MARYIGPKCKLARREGTDLFLKSGVRAIESKCNIEAAPGIHGQRRGRQSDYGTQLREKQKVRRIYGVLERQFSGYYKEAAGKKGATGENLLQLLECRLDNVVYRMGFGSTRAESRQLVSHKSISVNGQTVNVPSYQVRAGDVVAVREKAKNQLRIVQALDLCAQRGRVEWVEVDTEKKSGVFKNVPARSDLSADINESLIVELYSK | With S5 and S12 plays an important role in translational accuracy. | C3K2V2 |
A6W5T0 | RPOB_KINRD | Transcriptase subunit beta | Kineococcus | MEGPLLAASLPASAPNSTYIGNQSPRTVSGRYSFGKIHEPLEVPDLLALQTDSFDWLLGNKRWQDRVEASTNGGLAVPTTSGLEEIFEEISPIEDFSGSMSLSFRDHRFEPPKYSLDDCKERDLTYSAPLFVTAEFINGNTGEIKSQTVFMGDFPLMTDRGTFVINGTERVVVSQLVRSPGIYFERVPDKTSDRDTWTAKIIPSRGAWLEFEIDKRDTVGVRVDRKRKQSVTVLMKALGWSESQIREEFADYESMISTLEKDHTSGVEDALLDIYRKLRPGEPPTQEAARNLLDNLYFNPKRYDLAKVGRYKVNKKLGTEEPLSDSVLSVDDIVRTIKYLVKLHAGEVTMPGVKNGQPVDVRVEVDDIDHFGNRRLRSVGELIQNQVRTGLSRMERVVRERMTTQDVEAITPQTLINIRPVVASIKEFFGTSQLSQFMDQTNPLAGLTHKRRLSALGPGGLSRERAGMEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSSYGRINPFGFIETPYRKIVDGVVSDEVEYLTADEEDAFVIAQANAPLDADSRFAEARVLVRAKGGETEFVPRDEVDYMDVAARQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVKSEAPLIGTGMEFRAAVDAGDVVVATKAGVATDVSADMITTSNDDGTSTTYKVAKFRRSNHGTAYNQQVVINEGDRVEVGTVLADGPSTDGGEMALGRNLMVAFMPWEGHNYEDAIILSQRLVQDDVLSSIHIEEHEVDARDTKLGPEEITRDIPNVAEEVLADLDERGIIRIGAEVRDGDLLVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGETGTVIGVKVFDRDEGDELPPGVNQLVRVYVANKRKITDGDKLAGRHGNKGVISKILPVEDMPFLEDGTPVDVILNPLGVPSRMNVGQVLELHLGWIASRGWKIEGQPDWAKLIPEEIREAPAGSRIATPVFDGAREEEITGLLSSTIPTRDGDRLVGGDGKARLFDGRSGEPFPDPVAVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWALEAYGAAYALQELLTIKSDDVLGRVKVYEAIVKGENIPEPGIPESFKVLIKEMQSLCLNVEVLSSDGMAIEMRDSDEDVFRAAEELGIDLARREPSSVEEV | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A6W5T0 |
P52327 | RPOD_PSEPU | Sigma-70 | Pseudomonas | MSGKAQQQSRIKELITRGREQGYLTYAEVNDHLPEDISDPEQVEDIIRMINDMGINVFESAPDADALLLAEADTDEAAAEEAAAALAAVETDIRRTTDPVRMYMREMGTVELLTREGEIEIAKRIEEGIREVMGAIAHFPGTVDYILGEYDRVNRGCRLSDVLSGYIDPDDNIAAPTEEVPIPGTKAAAAKEEADDDEEESEGGDDEEEPKAALTRSSQPSVSVRYPSSFSDHQGPEEKRSYPQGKRRALQALADLFMPIKLVPKQFEVLVERVRDALNRLRQQERAIMQLCVRDARMPRADFLRMFPSNETDQTWSGDLAKRNTKWAAALGEKDAAIVACQQKLIDLETETGLTVAEIKEINRRMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELGERMEMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDSTMQSPIYVATVESLKEATRDVLSGLTAREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKAWRKLRHPTRSEHLRSFLDE | Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. | P52327 |
Q9SBK9 | CAL_BRARP | Agamous-like MADS-box protein CAL | Brassica | MGRGRVEMKRIENKINRQVTFSKRRAGLLKKAHEISILCDAEVSLIVFSHKGKLFEYSSESCMEKVLERYERYSYAEKQLKAPDSHVNAQTNWSMEYSRLKAKIELLERNQRHYLGEDLESISIKELQNLEQQLDTSLKHIRSRKNQLMHESLNHLQRKEKEILEENSMLTKQIKERESILRTHQNQSEQQNRSHHVAPQPQPQLNPYMISHQASPFLSMGGMYQGEDPTAVRRNRLDLTLEPIYNCNLGYFAA | Probable transcription factor that promotes early floral meristem identity in synergy with APETALA1, FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1. | Q9SBK9 |
Q64WA9 | QUEF_BACFR | PreQ(0) reductase | Bacteroides | MTELKEQLSLLGRKTEYKQDYAPEVLEAFDNKHPENDYWVRFNCPEFTSLCPITGQPDFAEIRISYLPDVKMVESKSLKLYLFSFRNHGAFHEDCVNIIMKDLIRLMDPKYIEVTGIFTPRGGISIYPYANYGRPGTKYEEMATHRLMNHE | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | Q64WA9 |
A0KQ96 | EFG_AERHH | Elongation factor G | Aeromonas | MARTTPIERYRNIGISAHIDAGKTTTTERVLFYTGVSHKIGEVHDGAATMDWMEQEQERGITITSAATTAFWSGMGKQFQPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRTGANFLRCVEHIKTRLKGNPVPLQLNIGSEENFKGVIDLVKMKAINWSEADQGVSFDYEDVPAELLEKAQEMRMTLVEAAAEASEDLMEKYLGGEELTEEEIKKALRQRVLNNEIILVTCGSAFKNKGVQAMLDAVVDYLPAPTDVAAIDGLKLDGETKDERHASDDEPFAALAFKIATDPFVGNLTFFRVYSGVVNSGDSVLNSVKEKRERFGRIVQMHANKREEIKEVRAGDIAAAIGLKDVTTGDTLCDEKAPIILERMEFPEPVISIAVEPKTKADQEKMGLALGRLAQEDPSFRVWTDEESGQTIIAGMGELHLDIIVDRMRREFKVEANVGKPQVAYRETIRNTVKDIEGKHAKQSGGRGQYGHVVIDMYPLEEGKAYEFVNDIKGGVIPGEFIPGVDKGIREQLKSGPLAGYPVMDLGVRLHFGSYHDVDSSELAFKIAASMAFKAGFMKANPVLLEPIMKVEVETPEDYMGDVIGDLNRRRGLIEGMEDGPSGKIVRALVPLAEMFGYATALRSATQGRASYAMEFAKYHDAPTNVAQAVIEERKSK | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | A0KQ96 |
A8H0D4 | PANB_SHEPA | Ketopantoate hydroxymethyltransferase | Shewanella | MSKITSSTLRTFKQEGKKFTALTAYDASFAGAFDSEGIDVLLVGDSMGMVLQGHSDTLPVTVEEIAYHTRCVRRGIERALLIADMPFMSYATPEQTMINATTLMQAGANMVKVEGGKWLLESVAMLTERGIPVCAHLGLTPQSVHVFGGFKVQGRDADNAQRILDEAKALEAAGAQLLVVECIPAPLAKAITDALTIPVIGIGAGKDTDGQILVMHDVLGISSGYIPRFSKNYLKQTGEIRAAVRAYIDEVAQGIFPGSEHTFN | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | A8H0D4 |
A1S566 | KAD_SHEAM | Adenylate monophosphate kinase | Shewanella | MRIILLGAPGAGKGTQAQFIMEHYGIPQISTGDMLRAAVKAGTPLGLEAKKVMDAGQLVSDELIIGLVKERIAQDDCANGFLLDGFPRTIPQADAMAANGISIDHVIEIDVPDEEIVNRMSGRRVHPGSGRVYHVVFNPPKVEGKDDVTGEDLVIRPDDEESTVRKRLGIYHEQTKPLVDYYGKVAAEGNTKYTKFDGTQSVAEVSKLIQAALS | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | A1S566 |
Q6GGY2 | Y1438_STAAR | DegV domain-containing protein SAR1438 | Staphylococcus | MTKQIIVTDSTSDLSKEYLEANNIHVIPLSLTIEGASYVDQVDITSEEFINHIENDEDVKTSQPAIGEFISAYEELGKDGSEIISIHLSSGLSGTFNTAYQASQMVDANVTVIDSKSISFGLGYQIQHLVELVKEGVSTSEIVKKLNHLRENIKLFVVIGQLNQLIKGGRISKTKGLIGNLMKIKPIGTLDDGRLELVHNARTQNSSIQYLKKEIAEFIGDHEIKSVGVAHANVIEYVDKLKKVFNEAFHVDNYDINVTTPVISAHTGQGAIGLVVLKK | May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | Q6GGY2 |
Q338B0 | HFA2C_ORYSJ | Heat stress transcription factor 6 | Oryza sativa | MDPAAAGIVKEEMLESQQQQRQEDGGAAPRPMEGLHEVGPPPFLTKTYDLVEDPATDGVVSWSRAGNSFVVWDPHVFADLLLPRLFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQRHLLKTIKRRKPPSNAPPSQQQSLTSCLEVGEFGFEEEIDRLKRDKNILITEVVKLRQEQQATKDHVKAMEDRLRAAEQKQVQMMGFLARAMRNPEFFQQLAQQKEKRKELEDAISKKRRRPIDNVPFYDPGETSQTEQLDSPYLFDSGVLNELSEPGIPELENLAVNIQDLGKGKVDEERQNQTNGQAELGDDFWAELLVEDFTGKEEQSELDGKIDGIDELAQQLGYLSSTSPK | Transcriptional activator that specifically binds DNA of heat shock promoter elements (HSE). | Q338B0 |
Q1IHJ4 | DNLJ_KORVE | Polydeoxyribonucleotide synthase [NAD(+)] | Candidatus Koribacter | MSRTKDPAKQAEDLREKLRYHEHRYYVLDDPEISDADYDVMMNELKALEAKHPELLTPDSPTQRVGGKPREGFVKVAHSAPMLSLDNAYNEEELRDWARRVEELSGKAEIEYECELKLDGLSMALRYQDARFVLAVTRGDGSIGEDVTLNLRTVKSVPLGVSSATLKKTHMLGDFEVRGEVIFPTKSFEKMNEDREKQGLAKFANPRNAAAGAVRVLEPNITAQRRLDFYAYFLLVDGRVHIDRQSEALDTLEKLGFKVNSNRAVFKSIDDVLKFIHKKEEDREKLPYEIDGVVIKVNSTALWQRLGFTGKAPRWAIAYKYAARAAVTQVEDILVQVGRTGKLTPVAALKPVPIGGTTVSRATLHNMDEIDRLGLLIGDWVQVERGGDVIPKVVKVIDDKDHPRGKKKFKMPERCPECGGHVVRTEGEADHRCVNANCPAKLRESILHFASRGVMNIEGMGDSLVNQLVDRGLVKNVADIYELDEEKLLSLERMGKKSAQNILDEIKGTKKLPLERVIYGLGIRMVGERTAQFLAEHFGSLDGVMKATEEELLEVEEVGPRIAQSIHEFFAEPSNRELVKRLEAAGLQFKGVKKERGTALAGQTFVLTGSLPTYSRDEAKKLIEDAGGKVSGSVSKKTNYVVAGEEAGSKLDKARDLGVAVIDEDALKKLLGK | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Q1IHJ4 |
B7LVU3 | APAH_ESCF3 | Diadenosine tetraphosphatase | Escherichia | MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGTLTCLRWEDKQYFVQPSNRHKDLGEGEAVAS | Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. | B7LVU3 |
B2ATX1 | GATA_PODAN | Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial | Podospora anserina | MLSRSGLRGARLRVVSLTSQRRLLNHFITHPPEPIPPPPPPAPSSSPSPKQFTLAVKDNIATTIPGLPTTCASGILSKSYVSPIEATIITQLRARGAVITGKTNLDEFGMGSHSIYSHYGPVSQDTPPETSAGGSSGGSAVAVANGEVELALGTDTGGSVRLPAAYTGIIGYKPSYGMISRYGVIPYANSLDTVGFLSKQINPLKELIIGERGLWKEHDSNDPTSLTTAARKRCAAQRRGYRSRQGQTTELEGLKFGIPLEYNIAELDPEIRDAWAAAAKRLQDAGARIVPVSLPTTKHALAAYYVIAPAEASSNLAKYDGVRYGARDAEGASDASAGGVLYASTRGKGFGEEVKRRILLGSYTLSSEAMDNYFIKAQRVRRLVRRDFNRVFALENPLQERETFELSDLPEEVEMEDKWGPEEVDFLLCPTAPTLAPKLKGVMEQQPVDAYMNDVFTVPASLAGLPAISVPMKVATEGAAGLQLIGQYWDDARLLDVADAVAKEVRT | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | B2ATX1 |
Q9LS09 | ASF1B_ARATH | Silencing group A protein 1 | Arabidopsis | MSSINITNVTVLDNPAPFVNPFQFEISYECLTSLKDDLEWKLIYVGSAEDETYDQVLESVLVGPVNVGNYRFVLQADSPDPLKIREEDIIGVTVLLLTCSYMDQEFIRVGYYVNNDYDDEQLREEPPTKVLIDKVQRNILTDKPRVTKFPINFHPENEQTLGDGPAPTEPFADSVVNGEAPVFLEQPQKLQEIEQFDDSDVNGEAIALLDQPQNLQET | Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. | Q9LS09 |
B5F3C0 | RL9_SALA4 | 50S ribosomal protein L9 | Salmonella | MQVILLDKVANLGSLGDQVNVKAGYARNFLVPQGKAVPATKKNVEYFEARRAELEAKLADVLAAANARAEKINALETVTIASKAGDEGKLFGSIGTRDIADAVTAAGVDVAKSEVRLPNGVLRTTGEHEVNFQVHSEVFAKVIINVVAE | Binds to the 23S rRNA. | B5F3C0 |
Q8R3Y8 | I2BP1_MOUSE | Probable RING-type E3 ubiquitin transferase IRF2BP1 | Mus | MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPTSKDLASTGSQGSQLPPPQAQAQPSGTGGSVSGPDRYDRATSSSRLALPSPALEYTLGSRLANGLGREEAVAEGARRALLGSIPSLMPPGLLAAAVSGLGGRALTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYERRHGSGEWRQLGELLTDGVRSFREPAPAEALPQQYPEPAPAALCGPPPRAPSRNLAPTPRRRKASPEPEGETAGKMTTEEQQQRHWVAPGGPYSSETPGVPSPIAALKNVAEALGHSPKDPGGGGGSVRAGGASPAASSTTQPPAQHRLVARNGEAEVSPTAGAEAVSGGGSGTGATPGAPLCCTLCRERLEDTHFVQCPSVPGHKFCFPCSREFIKAQGPAGEVYCPSGDKCPLVGSSVPWAFMQGEIATILAGDIKVKKERDP | Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation. | Q8R3Y8 |
A7HP99 | PCKA_PARL1 | Phosphoenolpyruvate carboxykinase (ATP) | Parvibaculum | MKQTGPYISKNGADKSGFKNLAATHWNYRPAALYEEAIRRGEGHVAANGPFVVKTGVHTGRSAKDKFIVRDASTEKTVWWDNNKSMTPEAFDLLHADMLKHAEGKELFIQDLFGGADQTHRLATRIYTEYAWHSLFIQNLLIEPKPEELGSFDPQFTIIDLPSFEADPEKYGVRTGTVIACNFAKRIVLIAGTSYAGEIKKSVFSMLNYELPPKRVMPMHCSANVGEEGDTAIFFGLSGTGKTTLSAVATRTLIGDDEHGWSENGVFNFEGGCYAKMIKLSAEAEPEIYAVTRRFGTVLENVVMDENTRELDLDSAALAENSRGAYPLSFIPNASATGRAPHPKNIIMLTADAFSVLPPVARLTPSQAMYHFLSGYTAKVAGTEKGVTEPEATFSTCFGAPFMSRHPTEYGNLLRDLIAQHKVSCWLVNTGWTGGVYGTGNRMPIKATRALLAAALDGSLNNVEFRTDPNFGFEVPVDVPGVDNKILNPRETWADKAAYDAQAQKLVKMFIENFAKFEAHVDPDVRAAAPAAARAAE | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. | A7HP99 |
P32382 | NADO_THEBR | NADH oxidase | Thermoanaerobacter | MTHFPNLFSEGRIGNLVIRNRIVMPPMATNLANEDGSVSQRLIDYYVARARGGVGLIILENVQVDYPQGKNVACQLRLDDDKYMAGFFELAEAVHSYGAKIFMQIHHAGRQTTPGITEGLQPVAPSPVPCSFLGTQPRELTINEIEEIIQKFVDAAVRAKGAMFDGIELHGAHGYLIGQFMSPRTNRRVDKYGGSFERRMRFPLEIIRRIKEAVGEDYPISFRFSADEFVEGGNTLEEGKQIAKMLEEAGVHVLHVSAGIYESMPTLLEPSRFEQGWRVYLAEEIKKVVNIPVITVGVIREPEFAEKIIAEGRADFVAVGRGLIADPEWPKKAKEGRQNEIRKCISCNIGCIGGRVFQNLRLRCTVNPVAGREGVYSEIKQAPVKKKVVVVGGGPAGMQAAITAAKRGHQVILYEKKQHLGGQLEIASASPGKAKIKWFRDWLEAELSRAGVEVRSGVTADAETIAALSPDYVILATGSEPVTPRIKGAEKENTFVFQAWDVLAGKVSFDKDEEVVVIGGGLVGCETAHYLAEKGAKVTIVEMLSDIAIDMEPISRFDMMQQFTKLGISARTGKVVTEILPRGVAAVGKEGKQDFIRAHKVVLAIGQSPVGNELKKTLEDKGIDVRVIGDAYNVGKIIDAVSSGFQVAWQI | Reduces a range of alternative electron acceptors. | P32382 |
Q14HR4 | BIOB_FRAT1 | Biotin synthase | Francisella | MTLQQIKEIYSRPLTELILQALEIHNKNFGNDIELCSLKSIKTGTCPEDCKYCPQSGHYNTSIEKHKLLDKDSILAEAKNAKDAGSKRFCMGAAWKHIPKKDFDQVAEIITEVKNLGLETCVTLGSINADEATKLKQAGLDYYNHNLDTSREFYPEIITTRKFEERIETIRNVANADINVCCGGILGMGESLDDRFNLLLELLQLPAAPKSIPINTLIPIKGTPLGDKYTNAQIDSFELVRFIATTRILFPQARLRLSAGRENMSLETQTLCFLAGINSIFYGNKLLTENNATVNSDNFLLAKLGLKSNAELC | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | Q14HR4 |
Q9AKP0 | MURE_RICMO | UDP-N-acetylmuramyl-tripeptide synthetase | spotted fever group | MSHNLKQLFQQHKVKGLSINSKTVKDKDVFFAIKGRNTDGNAFIKDALSKGAVLVITDNKKNIVIDKVIYVKDVQAALHEAIEIFYPKKPKNLIAVTGTNGKSSVVSYIAQTHSLLGKKAASIGTIGVEIFGCDNLINDVPELTTLDYLSFRKIAHNLAENGIEYLVFEASSHGLDQARLREIKVNIACFTSFSQDHLDYHHTKENYLLAKLKLFINHLLPNGIAILNSDIEEIEFVKDYLHNHNIKFITVGKKGDLEITRINCSLKGQNINFTFNNREYNFNTPIIGSFQASNLLIAVLSMHYTGFAFDDVIDSLVEVKAVKGRMERIDNTNIFVDYAHTPDALEKALTELKNIKLHDSKLSVVFGCGGNRDKAKRSLMGQMAAKRADTIIITDDNPRNEDPKLIRAEIISGIEKADYTEIANREEAIKYGINNLKQDDILLVAGKGHENYQIIGDKKLPFDDAEVVRKCVKVCHPVA | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q9AKP0 |
B6JN44 | EFTU_HELP2 | Elongation factor Tu | Helicobacter | MAKEKFNRTKPHVNIGTIGHVDHGKTTLSAAISAVLSLKGLAEMKDYDNIDNAPEEKERGITIATSHIEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRQVGVPHIVVFLNKQDMVDDQELLELVEMEVRELLSAYEFPGDDTPIIAGSALRALKKAKAGNVGEWGEKVLKLMAEVDAYIPTPKRDTEKTFLMPVEDVFSIAGRGTVVTGRIERGVVKVGDEVEIVGIRATQKTTVTGVEMFRKELEKGEAGDNVGVLLRGTKKEEVERGMVLCKPGSITPHKKFEGEIYVLSKEEGGRHTPFFTNYRPQFYVRTTDVTGSITLPEGVEMVMPGDNVKITVELISPVALELGTKFAIREGGRTVGAGVVSNIIE | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | B6JN44 |
A1CAP4 | ARGJ_ASPCL | Arginine biosynthesis bifunctional protein ArgJ beta chain | Aspergillus subgen. Fumigati | MAAFARMVKGQVRNYSAPLDMAIPASKQKYIPSSGSYPKGFLVSGTHVGVKASNTRFPDLALISSETPCSAAAVFTTNKFQAAPVQVSKKTLQERQGQGIRSVVINSGCANAVTGKGGYEDAVNMGKKVDECEGLSKPSTLVMSTGVIGQRLPISKILDKIPTAYANLASTHEAWLTTARAICTTDTFPKLLSRTFTLPSSPGHTYSLAGMTKGAGMIHPNMATLLGVLCTDAPIAPSALQSLLKYAVSRSFNSISVDGDTSTNDTIAVLANGAAGGAPINSASSDDYAAMQEILTSFAQSLSQLVVRDGEGATKFVTVRVQNSPDYDSARLIASTIARSPLVKTALYGRDANWGRILCAIGYTQGVAPGTVVPERTSVSFKPVDGSAVLKLLVNGEPEQVDEERASAILQEEDLEIVVDLGGGEKGELGGEEAVYWFCDFSHEYVTINGDYRT | Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. | A1CAP4 |
Q0TA26 | MALK_ECOL5 | Maltose/maltodextrin import ATP-binding protein MalK | Escherichia | MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQQVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV | Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. | Q0TA26 |
Q57607 | Y142_METJA | UPF0332 protein MJ0142 | Methanocaldococcus | MRLKIMELRYKRELEKLIEKAEKSLEASENLYNSEFYDFAVSRIYYSMFYCVKALLLTKEINPKKHSGVLKMFAKEFIKTNELDVELFEYINEAYNYRQTADYDATIEIKKEEAEYLLHKGHIFLNKTKKYLISKNILKGENDNTKS | Putative toxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate antitoxin might be MJ0141. | Q57607 |
O35492 | CLK3_MOUSE | CDC-like kinase 3 | Mus | MPVLSARRKRLASTAGPRRGSGPSLAVRWVPPLGPEPSSDRGRAPMRPRGPTCSTTRRGAGRGPRLLPGPPGRDLHRCRPDPGGAGQSPRVCEFGARAVRPLGRVEPGPPTAASREGAVLPRAEARAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRIPYQRRYREHRDSDTYRCEERSPSFGEDCYGSSRSRHRRRSRERAPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHSSRNPSR | Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. | O35492 |
A6VA58 | RIMO_PSEA7 | Ribosome maturation factor RimO | Pseudomonas | MSTPTPKVGFVSLGCPKALVDSERILTQLRMEGYEVVPTYEDADVVVVNTCGFIDSAKAESLEVIGEAIAENGKVIVTGCMGVEEHAIRDVHPSVLAVTGPQQYEQVVTAVHEVVPPKTEHNPLIDLVPPQGIKLTPRHYAYLKISEGCNHSCSFCIIPSMRGKLVSRPVGDVLSEAERLVKAGVKELLVISQDTSAYGVDLKYKTDFWNGQPVKTRMKELCEALGGMGVWVRLHYVYPYPNVDDVIPLMAAGKLLPYLDIPFQHASPKVLKAMKRPAFEDKTLARFKHWREICPELTIRSTFIVGFPGETEEDFQYLLDWLTEAQLDRVGCFQYSPVEGAPANELGLEPVPDEVKQDRWERFMAHQQAISAARLQLKVGKEIEVLIDEVDEQGAVGRSWADAPEIDGNVFVDSDALKPGDKVRVRITDADEYDLWAEPV | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | A6VA58 |
Q9LVT4 | DRL37_ARATH | Probable disease resistance protein At5g47250 | Arabidopsis | MNCCWQVVEPCYKSALSYLCVKVGNICMLKENLVLLKSAFDELKAEKEDVVNRVNAGELKGGQRLAIVATWLSQVEIIEENTKQLMDVASARDASSQNASAVRRRLSTSGCWFSTCNLGEKVFKKLTEVKSLSGKDFQEVTEQPPPPVVEVRLCQQTVGLDTTLEKTWESLRKDENRMLGIFGMGGVGKTTLLTLINNKFVEVSDDYDVVIWVESSKDADVGKIQDAIGERLHICDNNWSTYSRGKKASEISRVLRDMKPRFVLLLDDLWEDVSLTAIGIPVLGKKYKVVFTTRSKDVCSVMRANEDIEVQCLSENDAWDLFDMKVHCDGLNEISDIAKKIVAKCCGLPLALEVIRKTMASKSTVIQWRRALDTLESYRSEMKGTEKGIFQVLKLSYDYLKTKNAKCFLYCALFPKAYYIKQDELVEYWIGEGFIDEKDGRERAKDRGYEIIDNLVGAGLLLESNKKVYMHDMIRDMALWIVSEFRDGERYVVKTDAGLSQLPDVTDWTTVTKMSLFNNEIKNIPDDPEFPDQTNLVTLFLQNNRLVDIVGKFFLVMSTLVVLDLSWNFQITELPKGISALVSLRLLNLSGTSIKHLPEGLGVLSKLIHLNLESTSNLRSVGLISELQKLQVLRFYGSAAALDCCLLKILEQLKGLQLLTVTVNNDSVLEEFLGSTRLAGMTQGIYLEGLKVSFAAIGTLSSLHKLEMVNCDITESGTEWEGKRRDQYSPSTSSSEITPSNPWFKDLSAVVINSCIHLKDLTWLMYAANLESLSVESSPKMTELINKEKAQGVGVDPFQELQVLRLHYLKELGSIYGSQVSFPKLKLNKVDIENCPNLHQRPL | Probable disease resistance protein. | Q9LVT4 |
Q89AK6 | BIOF_BUCBP | 8-amino-7-ketopelargonate synthase | Buchnera | MNWNKRINHKLNMHIFNKKFRVKVAVQKNNNRIINVNGMQYINFSSNDYLGLRNNARIVQAWKTAATRYGIGSTGSSLITGYSTIHQSLEEKLAKWLDYPKAILFISGYTANTAIISTLIQKNDRIFMDKLSHSSILEPSYNSSGKCYRFIHNNPSSLMNKFYSSSGKNPLIITEGIFSMDGDIAPLSIISSFSKKIKGLLMVDDAHGIGVSGYNGKGSCEQHRVKPDILTITFGKAFGISGAAVLCSNNIAEYLWQFSKHLMFSTAMPIAQAYAIRQALYCIQHADKLRRKLQENINFFLKNSQCLSHLLKCSHTAIQPIIIGDNEETMILSDQLKSKGIWVNAIRPPTVPNKSSRLRITLNALHTKEDIEQLIESIYKLYDR | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | Q89AK6 |
Q68FQ2 | JAM3_RAT | Soluble form of JAM-C | Rattus | MALSRRLRLRLCARLPDFFLLLLFRGCVIEAVNLKSSNRNPVVHEFESVELSCIITDSQTNDPRIEWKKIQDGQTTYVYFDNKIQGDLAGRTDVFGKTSLRIWNVTRSDSAIYRCEVVALNDRKEVDELTIELIVQVKPVAPVCRVPKAVPVGKAATLQCQESEGYPRPYYSWYRNDVPLPTDSRANPRFQNSSFHVNSETGTLVFSAVHKEDSGQYYCIASNDAGAARCEGQDMEVYDLNIAGIIGGVLVVLIVLAVITMGICCAYRRGCFISSKQDGESYKSPGKHEGVNYIRTSEEGDFRHKSSFVI | Promotes chemotaxis of vascular endothelial cells and stimulates angiogenesis. | Q68FQ2 |
A0Q7L0 | DNLJ_FRATN | Polydeoxyribonucleotide synthase [NAD(+)] | Francisella | MTPNEFFSIKYHILAKAELKAYIDKLADYLSQQSYLYHTLDKPIISDSDYDKLFRLLQDLVNDNPQFKPINSVLDRVGGEVLAEFETIKHKKKMTSLANVFSLEELRDFYDKIEYDIELECEPKMDGLAISIFYKNGKFDYAVTRGDGIQGEKVSENVKTIRNVPLKLNTSNPPEELEVRGEIILDKQSFLSLNEYMQTHENKTFANPRNAAAGSIRMLDSKVVAKRPLKLYSYGIGYFSKDFVHPETQFELMQLLQSFGFTISDNMFLAKNFSEVEEYHHKMSHQRADLAYDIDGLVFKVNNIKLQDIIGYTARGPKWAVAYKFPAEEVESEVLNVEFQVGRTGAITPVARLKPVAVGGVIVSNATLHNINEIKRKDIRVGDRVIVRRAGDVIPEVVKSLPQYRKSDAQMVEMPTNCPVCDSAIENVNDQAIYRCTGGWHCQAQTTERLKHFVSRKAMDIDKLGAKLIEQLVAANLIKYPADIYKLNFDQLTGLERMGAKSSQNVLDSIKKSKTPSLARFIFAIGIKDIGEVSSDVLANHFGSLESFRDAKFEELIEINDIGEIMANNIVSFWHDSLNIKIVEELLAIGIKIQNPVKVEHAYNESFTGKTVVITGSFENYGRTELTQLLKSIGAKVTSSVSKKTDMVICGDNAGSKLTKAQELGVEVILEDNLKDLL | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | A0Q7L0 |
P04781 | CB23_PETSP | LHCII type I CAB-22R | unclassified Petunia | MAATTMALSSSSFAGKAVKLSSSSSEITGNGKVTMRKTVTKAKPASSSSPWYGPDRVKYLGPFSGEAPSYLTGEFPSDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELFARNGIKFGEAVWFKAGAQIFSEGGLDYLGNPSLVHAQSILAIWACQVVLMGAVEGYRVAGGPLGEVIDPLYPGGSFDPLGLAEDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWSYATNFVPGK | The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. | P04781 |
Q31NV7 | UCRI_SYNE7 | Rieske iron-sulfur protein | Synechococcus | MTQVSGASDVPSMGRRQFMNLLTFGSVTGVALGALYPVVNYFIPPSSGGSGGGVAAKDALGNDVVLSKFLADHNVGDRTLVQGLKGDPTYLVVESSEAIGDYGINAVCTHLGCVVPWNASENKFKCPCHGSQYDATGKVVRGPAPLSLALAHVSVTDDKVFLSPWTETDFRTGDNPWWA | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | Q31NV7 |
B8F4R6 | FDHE_GLAP5 | Protein FdhE homolog | Glaesserella | MSIRILPQEEIQQAASSFHNPPLLYANPKNLYARRAKRLRQLAEHNPFGDYLEFVANIVEVQLDLLENQPIANRVGELTAYLEAHQGVKPLDVKTFKRSDEWQKLLLAFIDKFKPYASDTVLATLEWLEKASNSELEMLADHLLNECYEEVGADKAVFLWAVLSLYWVQLTQQLPRNTKAEYGEERHTCPVCNSAPIASVVHFGETQGLRYLHCSLCESEWNMVRAKCSNCEQTGKLDYWSLDSMDAAVKAESCGDCESYLKVMYQDKDPHVEPIADDLGTLFLDAEMEQKGLARSAINPFLFQVE | Necessary for formate dehydrogenase activity. | B8F4R6 |
Q9I558 | ACSA1_PSEAE | Acyl-activating enzyme 1 | Pseudomonas | MSAASLYPVHPEAVARTFTDEATYKTMYQQSVVNPDGFWREQAQRIDWIKPFEKVKQTSFDDHHVDIKWFADGTLNVSHNCLDRHLAERGDQVAIIWEGDDPADHQEITYRQLHEQVCKFANALRGQDVHRGDVVTIYMPMIPEAVVAMLACTRIGAIHSVVFGGFSPEALAGRIIDCKSKVVITADEGVRGGKRTPLKANVDDALTNPETSSVQKIIVCKRTGAEIKWNQHRDVWYDDLMKVAGSTCAPKEMGAEDPLFILYTSGSTGKPKGVLHTTGGYLVYASLTHERVFDYRPGEVYWCTADIGWVTGHTYIVYGPLANGATTILFEGVPNYPDVTRVAKIIDKHKVNILYTAPTAIRAMMAEGKAAVAGADGSSLRLLGSVGEPINPEAWQWYYETVGQSRCPIVDTWWQTETGACLMTPLPGAHAMKPGSAAKPFFGVVPALVDNLGNLIEGAAEGNLVILDSWPGQARTLFGDHDRFVDTYFKTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEVESAMVAHPKVAEAAVVGMQHDIKGQGIYVYVTLNSGVEPSEALRQELKQWVRREIGPIATPDVIQWAPGLPKTRSGKIMRRILRKIAAAEYDTLGDISTLADPGVVQHLIETHRSMQAA | Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. | Q9I558 |
Q8UDA0 | RL25_AGRFC | General stress protein CTC | Agrobacterium tumefaciens complex | MSKESYELKAEARERVGKGSSRELRRNGLIPAVIYGDKQAPISIALSTNEVTKRIHAGGFMTTVGTIDVDGKKIKVLPKDYQLDPVRDFTMHVDFLRVSGNTLVNVEIPVHFENEEKSDIKIGGVLNIVRHTVEFHCPANDIPEAITVDLSGLKIGDSVHISNVKLPKNITPVIADRDFTIATIVAPAAGVEEETTEEASEE | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. | Q8UDA0 |
C4ZSG3 | MDTB_ECOBW | Multidrug transporter MdtB | Escherichia | MQVLPPSSTGGPSRLFIMRPVATTLLMVAILLAGIIGYRALPVSALPEVDYPTIQVVTLYPGASPDVMTSAVTAPLERQFGQMSGLKQMSSQSSGGASVITLQFQLTLPLDVAEQEVQAAINAATNLLPSDLPNPPVYSKVNPADPPIMTLAVTSTAMPMTQVEDMVETRVAQKISQISGVGLVTLSGGQRPAVRVKLNAQAIAALGLTSETVRTAITGANVNSAKGSLDGPSRAVTLSANDQMQSAEEYRQLIIAYQNGAPIRLGDVATVEQGAENSWLGAWANKEQAIVMNVQRQPGANIISTADSIRQMLPQLTESLPKSVKVTVLSDRTTNIRASVDDTQFELMMAIALVVMIIYLFLRNIPATIIPGVAVPLSLIGTFAVMVFLDFSINNLTLMALTIATGFVVDDAIVVIENISRYIEKGEKPLAAALKGAGEIGFTIISLTFSLIAVLIPLLFMGDIVGRLFREFAITLAVAILISAVVSLTLTPMMCARMLSQESLRKQNRFSRASEKMFDRIIAAYGRGLAKVLNHPWLTLSVALSTLLLSVLLWVFIPKGFFPVQDNGIIQGTLQAPQSSSFANMAQRQRQVADVILQDPAVQSLTSFVGVDGTNPSLNSARLQINLKPLDERDDRVQKVIARLQTAVDKVPGVDLFLQPTQDLTIDTQVSRTQYQFTLQATSLDALSTWVPQLMEKLQQLPQLSDVSSDWQDKGLVAYVNVDRDSASRLGISMADVDNALYNAFGQRLISTIYTQANQYRVVLEHNTENTPGLAALDTIRLTSSDGGVVPLSSIAKIEQRFAPLSINHLDQFPVTTISFNVPDNYSLGDAVQAIMDTEKTLNLPVDITTQFQGSTLAFQSALGSTVWLIVAAVVAMYIVLGILYESFIHPITILSTLPTAGVGALLALLIAGSELDVIAIIGIILLIGIVKKNAIMMIDFALAAEREQGMSPREAIYQACLLRFRPILMTTLAALLGALPLMLSTGVGAELRRPLGIGMVGGLIVSQVLTLFTTPVIYLLFDRLALWTKSRFARHEEEA | The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. | C4ZSG3 |
Q58EG3 | NECT3_DANRE | Poliovirus receptor-related protein 3-like | Danio | MALTMTAHFLRNNPIQLGLNLRVLLMLSFVSGLVYGSQVIVPPKVNAVLGKNVTLSCRVQVDTNLSLTQSSWERKLPNGWVTLAVYNPMFGISIPPDYERRLSFRSPSALDATIMLEDVGFADIGVYTCKVATFPLGNTQASTTVSVLVEPKVYVSAGSSALIDGGNETTVATCIAERARPPADVSWETNLYGMSEAHMQEDANGTTTTQVHYIWQPSRHAQGHTLTCVVKHPALQSDFRIPYIINVQFAPDILVLGYDGDWYVGRENVQLKCRAKANPPAQHFRWIRLDGEMPNGAERVNNTLVFTRPLQKNDSGVYRCEVANDIGLHSRDIRIRIQDPPSTTTMPPTTPVRLLTADISATAPGNKQRALITSPTLAPLHEGSLGTIVGGAVGGALFLLLLLILAGVYYQRQRRTFRGDYYTKQYHGPSDMQKAPQPHELQQVYSKGSPDTKLKSNQDNGTIYPDKDREEWGDFDRERSPNGRSRALREAGQLNHHNHQNHEHGFHSNHHTGHPQSYSPAHHIQRSSLQPQPRRYPAPQVMSNGSPYLPEDCYDNEYVSHTDGSMISRREWYV | May play a role in cell-cell adhesion. | Q58EG3 |
P0A521 | CH602_MYCBO | Heat shock protein 65 | Mycobacterium tuberculosis complex | MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGAGDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQIAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKEKASVPGGGDMGGMDF | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | P0A521 |
Q5FRW6 | ATPL_GLUOX | Lipid-binding protein | Gluconobacter | MDVQAAHEFGISIAQAARDLGAGIAVFALAGVGMGLGNIFSTLISSVARNPASRPHVFGIGMLGFALTEAVALFALLIAFLILFA | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | Q5FRW6 |
Q3UFY0 | RRP36_MOUSE | Ribosomal RNA processing protein 36 homolog | Mus | MRKAGSRARAEAEGPHRAMEGGEVTGDRLKADTPDVSFEELLRLQGQGRPKAHKQLVAGNSTRTRSPQQPVCVADKHRPLEMSAKVRVPFLRQVVPISKKVARDPRFDDLSGDYNPEVFDKTYQFLNDIRAKEKQLVKKQLKRHRSGEERDKLQQLLQRMEQQEMAQQERKQQQELRLALKQERRAQAQQGHRPYFLKKSEQRQLALAEKFKELRRSKKLESFLSRKRRRNAGKDRRHLPLSKE | Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA. | Q3UFY0 |
P00756 | K1KB3_MOUSE | Nerve growth factor gamma chain 2 | Mus | MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP | 7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic activity for chick embryo fibroblasts. | P00756 |
C3PMH5 | RL10_RICAE | 50S ribosomal protein L10 | spotted fever group | MLRSEKPVAVEDIVNIYKESPSIIITHYHGLTVSQVSSLRESLKSKEAGFKVVKNTLAKIAANQTGLNSIVNLFAGPTAIVYSKEPVEMAKLVVNFAKANDNLKIIGGIVDNHVLDEHSIKELSKLPTLNELRGKIVGLLQAPATKVVGVLQAPSSSMARVIQAHASKN | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | C3PMH5 |
Q057A2 | EFTU_BUCCC | Elongation factor Tu | Buchnera | MSKEKFNRSKPHINVGTIGHVDHGKTTLTSAITTVLSKRFGGKACAFEQIDNAPEEKARGITINTSHVEYDTELRHYAHVDCPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPHIIVFLNKCDMVDDEELLELVEMEVRDLLTQYDFPGDNIPIIRGSALKALEGEKIWEDKIIELANSLDKYIPIPVRAVDEPFLLPIEDVFSISGRGTVVTGRIERGILKVGEEVEIVGIKSTTKTICTGVEMFRKLLDEGRAGENVGILLRGTKREDIERGQVLAKPGTINPHVKFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGSIELPENIEMVMPGDNINMVVTLIHPIAMAEGLRFAIREGGRTVGAGVVTKVIA | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q057A2 |
A4PBQ1 | CRJ38_CRYJA | Pathogenesis-related thaumatin-like protein 3.8 | Cryptomeria | MAKVSDLALLLVAGMAISLYIQETGAVKFDIKNQCGYTVWAAGLPGGGQQLTQGQTWTVNLAAGTQSARFWGRTGCSFDASGKGTCQTGDCGGQLSCTVSGAVPATLAEYTQSDQDYYDVSLVDGFNIPLSINPTNAQCTAPACKADVNAVCPAELKVDGGCKSACAAFQTDQYCCTGTYANSCPATNYSMIFKNQCPQAYSYPKDDTATFACPSGTDYSIVFCP | May be involved in disease resistance. | A4PBQ1 |
Q1GK13 | RL18_RUEST | 50S ribosomal protein L18 | unclassified Ruegeria | MANSKRTLFLKRRLRVRNKLRKVNAGRLRLSVHRSNKNISVQLIDDVKGVTLAAASTLEKDLGFVGKNNIEAATKVGSVIAERAKAAGVTEAYFDRGGFLYHGKVKALADAAREGGLKI | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | Q1GK13 |
Q47TA8 | PLSX_THEFY | Phosphate-acyl-ACP acyltransferase | Thermobifida | MSSPVTAQRPPAAPPLIAVDAMGGDHAPREIVAGAVRAVREHGLRLALVGRSSELAPLVAAEQAARELPIVHAEEALAMHEGALAAWRRARSSVAVGCKLVRQGTAAALVSAGSTGGVVSTATVRLRTLPGVLRPALALVLPTTPTPTILLDAGANADAKPEMLVQFAHLGAAYARVGHGIAEPRVGILTIGSEPGKGNKLARRAAELLSANATEDRLDFRGNIEGHDLLAGLVDVVVTDGFTGNVALKSVEGAVRFAFDEIRAALTSSPLARFGTLFQRRALRELRTRFDSETYGGAVLLGLNGTVVIAHGASRAEGIAHACLLAHNLVVGRITDQIRRGIAGVSRTPSWLHRLSAPEE | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q47TA8 |
Q5FFT9 | RS10_EHRRG | 30S ribosomal protein S10 | Ehrlichia | MVMVTQKIYIELKAFDSYLLDRSARSIILTAKRSGARVNGPIFFPRRVAKFIVNRSTHVDKKSREQFEIRTHKRLISLPKANSTIIQALMSLQLPAGVDVKVKVIGGSNG | Involved in the binding of tRNA to the ribosomes. | Q5FFT9 |
Q31FZ5 | TGT_HYDCU | tRNA-guanine transglycosylase | Hydrogenovibrio | MKFELDKQDGRARRGRLIFKRGVVETPAFMPVGTYGSVKGMMPEEVADTGAQIILGNTFHLSIRPGTDIIEQHGDLHDFMNWKGPILTDSGGFQVFSLGKMRKITEEGVHFRNPVNGSKIFMGPEESMDVQRKLGSDIVMIFDECTPYPATHDVAADSMRLSLRWAERSKQAHGDNPSALFGIVQGGMYEDLRQESIKGLTDIGFDGYAIGGLSVGEPKEEMMGTLDFTEPHMPKDKPRYMMGVGKPEDIVEAVRRGIDMFDCVIPTRNARNGFLFTHSGVVKIRNAVNKTSLEPLDAKCDCYTCQNYTRAYLHHLDKCGEIQGARLNTIHNLHYYQLLMKGLREAIASETLDTFVSEFYQARGEDVPAL | 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). | Q31FZ5 |
Q32RS5 | RR14_STAPU | 30S ribosomal protein S14, chloroplastic | Staurastrum | MAKKSMIERDKKRKFLSAKYSIQRQQLKEQINQSLSLDEKAHLYRKLQSLPRNSAPTRITRRCFVTGRPKAVYRDFGLSRHVLREMAHACLLPGVIKASW | Binds 16S rRNA, required for the assembly of 30S particles. | Q32RS5 |
Q96JN2 | CC136_HUMAN | Nasopharyngeal carcinoma-associated gene 6 protein | Homo | MQAMEGEVLLPALYEEEEEEEEEEEEVEEEEEQVQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSPSIKMSLESYGKSYGSMVPSNENCRKTYDTTVDDNESYYKSYTSTQTSSKSFLKSYDSSTSASEAYGKSYCTTSNSSITYKKSYGSTSSSDTCQKSFVSSCTDEEPAEPEDMERFEEMVVKVLIKLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQNDKNEIKELQTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREKRPSVVKEARGKNANKNMNKNANGVKMKKVTKPCSDTSESDLETRKSLEVVLYYKASQRKLDGLAKEEEKKEEMEEEKKQVKEEAKEQCGDELVAEPADPEEAKSTEDQEENEEDKEEEEKEEDSEEEEDDADSSLESPEENNPLRLSESKKSSPTPNPPIFSLPLVGLVVISALLWCWWAETSS | May play a role in acrosome formation in spermatogenesis and in fertilization. | Q96JN2 |
P66366 | RS11_TROW8 | 30S ribosomal protein S11 | Tropheryma | MSKQAQSRSRKKARKNIPAGLAHIKSTFNNTIVTITDLSGNVIGWSSSGAVGFKGSRKSTPYAAQMAADAAARSAQEHGVKKVDVFVKGPGSGRETAIRSLQTAGLEIGSISDTTPLAFNGCRPPKKRLV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | P66366 |
B1XP88 | PYRR_SYNP2 | Uracil phosphoribosyltransferase | unclassified Synechococcus | MTKSVIEILSAEEMRRTITRLASQIVEKAGDLTDLALLGIHTRGVPLAENIAKQIETLEGIAVPVGALDITFYRDDLDQIRVRTPSKTDIPFDLNGKNLVLIDDVIYKGRTIRAALNAVNDYGRPEVIRLAVLVDRGHRQLPIQPDFTGKKLPTAKEEKVKVYLQDLDGRDAVELIK | Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. | B1XP88 |
Q9Z6T7 | FTSY_CHLPN | Signal recognition particle receptor FtsY | Chlamydia | MFKFFRNKLQSLFKKNISLDLIEDAESLFYEADFGTELTEELCARLRRTKKADASTIKDLITVLLRESLEGLPSQASQSSQTRPIVSLLLGTNGSGKTTTAAKLAHYYKERSESVMLVATDTFRAAGMDQARLWANELGCGFVSGQPGGDAAAIAFDGIQSAIARGYSRVIIDTSGRLHVHGNLMKELSKIVSVCGKALEGAPHEIFMTVDSTLGNNAIEQVRVFHDVVPLSGLIFTKVDGSAKGGTLFQIAKRLKIPTKFIGYGESLKDLNEFDLDLFLNKLFPEVEKI | Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). | Q9Z6T7 |
A8GVB8 | RS19_RICB8 | 30S ribosomal protein S19 | belli group | MARSVWKGPFVDGYLIKKVQKLMESGKSEMIKTWSRRSTILPIFVGFTFSVHNGNKFIPVSVNEEMVGRKLGEFSPTRTFHGHGADKKVKRK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | A8GVB8 |
Q2GCU4 | MIAB_NEOSM | tRNA-i(6)A37 methylthiotransferase | Neorickettsia | MLLYLADVVIFSHAKVYMEKIEKKNNSLKKFHIKTYGCQMNVYDSEMIEKIVSGLGFTLSERAEDADLIILNTCNIREKAAEKLYSELGQIRLLQKKKQERILIVVAGCVAQAEGEEIMRRAENVDVVVGPQSIHSLPELIAKVNRQSGKAIKMEFDPIEKFDYLAEETRKRRVPQSSAFLSIQEGCDKFCAFCVVPYTRGAEYSRSTEEVYREALSLTTKGVKEITLLGQNVNGYHGTLDSGNKVLNLGQLISRLGKIPSLKRIRYTTSHPVDMHKELYDAHANESKLMPFVHLPVQSGSDKILKQMNRKYTTADYLKIINEFQNARSDIAFSSDFIVGFPGESDDDFQQTLALIEQVNYAQCYSFKYSPRPGTPGATYPQISEETKNTRLQKLQQLLKEKQLEFNKKMIGKTVTVLFDKKHPDKISGRTEYMQQVFSDDSNLLDKIVTMRVEDASTFTLKCTAEDIIST | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q2GCU4 |
A7FIA5 | MINC_YERP3 | Probable septum site-determining protein MinC | Yersinia | MSQSPIELKGSSFTLSVVHLHDSRPEVIRQALQEKVDQAPAFLKNAPVVINVATLPNGANWKDLQQAVTSAGLRIVGISGCQDERQKRAIARAGLPLLSEGKGQKLAPEPVISPPENVPTQTRIINTPVRSGQQIYARNCDLIVISSVSAGAELIADGNIHIYGMMRGRALAGASGDAKCQIFCTHLGAELVSIAGQYWLSDQIPLEYFGQAARLYLQDNTLTIQPLN | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | A7FIA5 |
Q9C7D2 | SCP15_ARATH | Serine carboxypeptidase-like 15 | Arabidopsis | MASWIFKLLLLLQCVLVLIQHADSSSIIRYLPGFEGPLPFELETGYIGVGQKEEDQLFYYFIKSENNPEEDPLLVWLTGGPGCSSFSGLVYENGPLAFKVETYNGSVPTLVSTTYSWTKVANIIYLDQPVGTGFSYSRNPFADIPSDTGSVKRVNEFVRKWLAKHPEYFSNPFYVTGNSYSGKVIPAIVQEISNGNYICCKPQINLQGYVIGNPVAYYDHDKDFRIPFAHGVALISDELFESLKASCGGSYSVVDPLNTECLKLIEDYDKCVSGIYEELILKSKCEHTSPDCYTYRYLLSEYWADNETVRRALKVVKGSKGTWERCDYRVLSNQDIKSSIPFHINNSIRGYRSLVISGDHDMTIPFLGTQAWIRSLNYSITEKWRPWMILDQVAGYTKTYANKMTLATVKGGGHTLEYKPEENSVLFKRWISGQPL | Probable carboxypeptidase. | Q9C7D2 |
A9AHS8 | DAPE_BURM1 | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Burkholderia cepacia complex | MSATLALTEQLIARASVTPDDQHCQQIMTERLAALGFDCETVASHGVTNLWAVKRGTDGRDGKLLAFAGHTDVVPTGPLEQWTSPPFVPAHRDGKLYGRGAADMKTSLAAFVVAAEEFVAAHPDHRGAIAFLITSDEEGPATDGTVKVVELLESRGERLDYCIVGEPTSTAELGDVVKNGRRGSMSGELIVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHQLDYTLKWTVSGLPFLTPRGELSNALEHAIRAETGLTTELSTTGGTSDGRFIARICPQVIEFGPPNGSIHKIDEHIEVRFVEPLKNVYRRVLEQLIA | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | A9AHS8 |
Q3BZD0 | KDUI_XANC5 | DKI isomerase | Xanthomonas | MSLYCKTHYATHPDAIKGASNDALRELYLLDGLFVDDAVTLKYTHYERFVLGGAAPLGKTLELPRQTEPASAAGHPFLERRELGVLNVGAGTGTVTVDGTAYTLGPKDGLYVAMGSTDVSFASADAANPAKFYLASTPAHARFETKQLSIKDAVALERGALETSNERTIYQYIVPATCQSSQLLLGLTVLKPGSVWNTMPPHLHDRRSEVYFYFDLGANDRVYHFMGEPDAQRHIVIQNNEAVVSPPWSIHMGAGTSNYAFIWAMGGENLDYTDMHVLDICQLK | Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. | Q3BZD0 |
P80725 | DPS_LISIN | Non-heme iron-containing ferritin | Listeria | MKTINSVDTKEFLNHQVANLNVFTVKIHQIHWYMRGHNFFTLHEKMDDLYSEFGEQMDEVAERLLAIGGSPFSTLKEFLENASVEEAPYTKPKTMDQLMEDLVGTLELLRDEYKQGIELTDKEGDDVTNDMLIAFKASIDKHIWMFKAFLGKAPLE | Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Does not bind DNA. | P80725 |
A6VQ42 | RNFC_ACTSZ | Rnf electron transport complex subunit C | Actinobacillus | MTDVLTRYNSGKLWDFDGGIHPPEMKSQSNSTPISTALLAEDYYVPVKQHAGNAGNLLVKEGDYVLKGQPLTLGDGLRVLPVHAPTSGTVVAIEPHIAAHPSGLSELAVHIHADGKDQWRPQNPTEDYFTHTPERLIEKIYRAGVAGLGGAVFPTGAKVDAALGKVKLLIINGAECEPYITCDDRLMRDYAAEIIEGVRILRYILRPEKVVIAIEDNKPEAVNALRTSLQGANDMDIRVIPTKYPSGAAKQLIYVLTGMEVPHGQRSSSIGVLMQNVGTAFAVKRAVINDEPLIERVVTLTGDKIPHKGNQWVRLGTPIDFILKHVGYQPDNRFPVFVGGPMMGLIVPDLRAPITKTANCLLAPDHFEYDPQATEQACIRCSACSDACPVHLMPQQMYWYARAEDHEKSNQYQLMDCIECGLCAYVCPSHIPLIQYFRQEKAKIWDIEAKARKSEEAKIRFEARQARLEREEQARKARSQRAAAARREELAANKGEDPVQAALARLKAKKAGEAPETGGSAQGAPHIKTIRTEKGQSVPDNSEITALRRARRLARQQTNGNSPVSSASNSDSATISADNTHSTPKTAQNQTAPDPKKAAVAVAIARAKAKKAAQTTTGETVTENVTEKTAQNPTAPDPKKAAVAAAIARAKAKKAAQATTGETATEKTAQNPTAPDPKKAAVAAAIARAKAKKAAMLAESEKK | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | A6VQ42 |
Q2FTN5 | RL13_METHJ | 50S ribosomal protein L13 | Methanospirillum | MVVVIDGDGLLLGRLASNVAKRALAGEEIAVVNAEKAVISGNRARVLGNYKQKRQRGSREGGPFFPRRPDHILKRTIRGMIPYKRERGIEAMKRIRIYVGVPDELSGQPFETIEDASKKRLGNPSHVTLGAVSTFLGAKY | This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | Q2FTN5 |
A3NT04 | PURT_BURP0 | Phosphoribosylglycinamide formyltransferase 2 | pseudomallei group | MQIGQRLGTPLSPSATRVMLLGAGELGKEVIIALQRLGVEVIAVDRYPNAPGHQVAHRAHVIDMTDPDALRALVDAERPHLVVPEIEAIATDALAAIEAAGVCEVIPTARATQLTMNREGIRRLAAEELGLPTSPYAFAQSFDEFAAAVARIGFPCVVKPVMSSSGKGQSVVRSEADIEPAWRYAMAGGRVNHGRVIVEGFIRFDYEITQLTVRAIDPASGQTRTSFCAPIGHLQVAGDYVESWQPQPMSAKALERSRDIAHRVTSALGGRGIFGVELFVRGDDVWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPVEPALATPAASAVIYGGLDEAGIAFEGVRDALAVPGADLRLFGKPESFAKRRMGVALATGANVDEARERAKRAAAAVRPVSAR | Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. | A3NT04 |
A1S3I3 | HLDE_SHEAM | D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase | Shewanella | MKVTLPAFEKARVLVVGDVMLDRYWVGPTGRISPEAPVPVVRINQIEDRPGGAANVALNIAALGGKVQLSGLVGQDDTADALTRGVQALGVEPHWLVVEDKPTITKLRVLSRNQQLIRLDFEEAFDKHSSDALLNQAQARLDDVDVVILSDYAKGAVGEPADFIASARAKGVKVLVDPKGSDFARYRGATLLTPNMSEFEAVVGTVTSEADLVDKAQKLLQDLALDALLVTRSEKGMTLITPNAPELHIPTVAREVYDVTGAGDTVISALATALGAGAELPQACAIANTAAGVVVGKLGTSTVSRIELIEALKSHQGESGIGVVSEDQLVYALEQAKLRGERVVMTNGCFDILHAGHVSYLAQAKALGDRLIVAVNDDDSVRRLKGDGRPVNSVDRRMAVLAGLASVDWVVPFSEDTPQRVIARLLPDLLVKGGDYKVEDIAGGAEVIANGGQVKVLGFEDGVSTTAIIQNIMSRH | Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. | A1S3I3 |
Q96QP1 | ALPK1_HUMAN | Lymphocyte alpha-protein kinase | Homo | MNNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRALLPSELRTLIQEAKEMKWPFVPEKWQYKQAVGPEDKTNLKDVIGAGLQQLLASLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKGLHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKNDYEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTPLFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFEIGLLTKRDDEPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHAASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKEHLQVQSFSNVDDRSYVPESFECRLDKLILHGQGDFQKILDTYSQHHTSVCEVFESDCGNNKNEQKDAKTGVCITALKTEIKNIDTVSTTQEKPHCQRDTGISSSLMGKNVQRELRRGGRRNWTHSDAFRVSLDQDVETETEPSDYSNGEGAVFNKSLSGSQTSSAWSNLSGFSSSASWEEVNYHVDDRSARKEPGKEHLVDTQCSTALSEELENDREGRAMHSLHSQLHDLSLQEPNNDNLEPSQNQPQQQMPLTPFSPHNTPGIFLAPGAGLLEGAPEGIQEVRNMGPRNTSAHSRPSYRSASWSSDSGRPKNMGTHPSVQKEEAFEIIVEFPETNCDVKDRQGKEQGEEISERGAGPTFKASPSWVDPEGETAESTEDAPLDFHRVLHNSLGNISMLPCSSFTPNWPVQNPDSRKSGGPVAEQGIDPDASTVDEEGQLLDSMDVPCTNGHGSHRLCILRQPPGQRAETPNSSVSGNILFPVLSEDCTTTEEGNQPGNMLNCSQNSSSSSVWWLKSPAFSSGSSEGDSPWSYLNSSGSSWVSLPGKMRKEILEARTLQPDDFEKLLAGVRHDWLFQRLENTGVFKPSQLHRAHSALLLKYSKKSELWTAQETIVYLGDYLTVKKKGRQRNAFWVHHLHQEEILGRYVGKDYKEQKGLWHHFTDVERQMTAQHYVTEFNKRLYEQNIPTQIFYIPSTILLILEDKTIKGCISVEPYILGEFVKLSNNTKVVKTEYKATEYGLAYGHFSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKVFTTNFGKRGIFYFFNNQHVECNEICHRLSLTRPSMEKPCT | Serine/threonine-protein kinase that detects bacterial pathogen-associated molecular pattern metabolites (PAMPs) and initiates an innate immune response, a critical step for pathogen elimination and engagement of adaptive immunity . Specifically recognizes and binds ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria . ADP-Heptose-binding stimulates its kinase activity to phosphorylate and activate TIFA, triggering pro-inflammatory NF-kappa-B signaling . May be involved in monosodium urate monohydrate (MSU)-induced inflammation by mediating phosphorylation of unconventional myosin MYO9A . May also play a role in apical protein transport by mediating phosphorylation of unconventional myosin MYO1A . May play a role in ciliogenesis . | Q96QP1 |
A0LJL8 | NUON2_SYNFM | NDH-1 subunit N 2 | Syntrophobacter | MNWMSFAPELITLTSALWFLLLSMTARSDPKREHVAALVLSALGLAACLASVGAEGYCFAGAYKVDLFSQVFKVLLAAGLFLIVTLCGELSDIEERNRREFYVLLFVCTLAMMLLVGANHFLVVFISLELSSYSLYVLVALRRDRGLGLEAGIKYFLVGIFASGVMIFGLALLYGASGIAALDGMARVLPGIIHQPAVVIGLLLTLSGFFFKLAVFPFHFWAPDAYQGAANQVSAYIATASKVAAIGVLVRVIASAGDGGTYLVHVLAVLSVVSMTVGNLAAIAQQDLKRLLAYSTVAHAGYVLIGVLSMNPAGYSAAVFYAFALLVMKFTAFLVLVEVASDGGNLRVEELAGLHRRSPILALALMVSLFSLAGIPPTVGFTGKFLVFVAAMGEGHFTLVLIAMINVVISLYYYLLVIKAAYLLEPRQELPALRVSPPLKLLSGVLVIAMVAAGFFPNQIIRVAESAAKALL | 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. | A0LJL8 |
Q487Z3 | RL3_COLP3 | 50S ribosomal protein L3 | Colwellia | MTIGLVGRKVGMTRVFTEDGVSTPVTVIEVEANRVAQVKTVDNDGYSALQVTTGKRKASRVTKPAAGHFAKAGIEAGRGLWEFRLNENEGSDIEAGSEITVEVFNDTKLVDVTGTSKGKGFQGGIKRWNFTMQHATHGVSLSHRSNGSLGQCQTPGRVFKGKKMSGHMGAVRCTTQNLELVRVDAERNLLLIKGAVPGAINGNVIIKPAVKA | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q487Z3 |
A9ADK7 | RS8_BURM1 | 30S ribosomal protein S8 | Burkholderia cepacia complex | MSMSDPIADMLTRIRNAQMVEKVSVAMPSSKVKVAIAQVLKDEGYIDDFAVKTEGAKAELNIALKYYAGRPVIERLERVSKPGLRVYRGRNEIPQVMNGLGVAIVSTPKGVMTDRKARATGVGGEVICYVA | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | A9ADK7 |
C0HLD7 | PLS21_PHYTB | Phylloseptin-2.2TR | Phyllomedusa | FLSLIPHIATGIAALAKHL | Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 25922 (MIC=50 uM), Gram-positive bacterium S.epidermidis ATCC 12228 (MIC=12.5 uM) and against fungus C.albicans ATCC 24433 (MIC=100 uM) . Has an anti-inflammatory effect, since it inhibits the production of the pro-inflammatory cytokines TNF-alpha, and induces the production of the anti-inflammatory cytokine IL-10 . Is cytotoxic to cancer line cells . Shows moderate hemolysis on mouse erythrocytes (LC(50)=41 uM) . | C0HLD7 |
Q8IIJ6 | UCH37_PLAF7 | PfUCH54 | Plasmodium (Laverania) | MARDNENILEEWCLIESNPCIFYDMLKRMGATEISVEDVYSLSYFDDYINNKEIINMNHILGVDTYLGENNKTLDKENNVVDVIELYKNNICMEDKYNKLLKHHSYIYGIIFLFNIGKHYKNNKYIEHNVPDNLFFAKQVIPNACATQAILSIVLNKDIELNDEIKNIKTFSLNFDSSMKGLTLSNCTFLRNIHNSYKPPIYLDKEDVHHDKKKSEDSFHFVSYISFQDKVYLLDGLQSGPVLINADEQNKPNPNNNNNNKDNDNDNNNNNNNNNNNNNNNNNNNNNNNNNNIGMNGKDWIEISREHIKKEIDEICNSQTNNDVRFNIIAVMKDKEYIIQEYINIHRIVKQRVNIKLINLGENIELSDEINEDEFPLLNDIPSIENLPNNVDTLYNIVNKSTLEINYLQSLLHEQKEIKKLWNKELTFKFFNFYPFIMSSLNLMAKHKLLKDAYQKEKLKNATKS | Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. | Q8IIJ6 |
A8GPC4 | RS20_RICAH | 30S ribosomal protein S20 | spotted fever group | MANHSSAKKAARQTVKRTLINKARSSAIKTFIKKVVHEISLGNKENANLALSVAQSKIMQGVKKNIIKLNTASRKISRLSKQIKSLNESK | Binds directly to 16S ribosomal RNA. | A8GPC4 |
O36028 | ATCZ_SCHPO | Putative phospholipid-transporting ATPase C4F10.16c | Schizosaccharomyces | MPSLINFDAISSLKSSLHGLSICAFNHLHHVPQHNGSLAHEGPTNQTDYSSRHHESQFSQEAHAEQRSRDDEEANSFEGSCNNSDQSWTSRVTSKKNEAGTESGDASVRRIYVTSIPEEHRHLPSQWFPSNKIRTTKYTPVSFIPKNLWNQFKNIANAFFLFVTLLQCIPLFCPEHLGLSFIPLSVILLTTAIKDGIEDYRRCVLDKKFNNTLTWKLVGFNNANALGEHIGLWRKLKKFISHTVADMSYCLKNSGISSGLATLTVDNISHRHSLESDSAFTLSSVSQDSLEIHEIGNSGPSNSFSVIQEQSTGSSNAKFERVCRKSLLVGDIVKVLADEAIPADLLILSTENSNGVCYVETKNLDGETNLKDKYALCSTKCCKSEYRCSAASFWVECEQPHADLYSLNGVVKAPGAVQSPSESTNGRKIHEEPFSISNVLLCGCTLRNSKWVIGLVLYTGSETRIQKNRGLTPSKRSRITRDLNWTIILNFLLLFAMCLFSGVLRSIYSAQNNSARVFELSKNSNTAPAHGIISIFTSLILFQNLVPISLYITMDIVRSIQSYFIFSDREMYDEKLDCPCSPKSWNISDDLGQIEYIFSDKTGTLTQNIMSFKKCSINGIRYGKSHNEDTCIKKRRNLNYNENLSCKVDLDKKKMLETLSLSDSPNPESITFISSKFVDHLQSNENYIQTEACFEFFKALALCHSVVTDVQDETLIYNAQSPDEEALVKVARDFGFTLLNTKNRRYTIRIRGENKNFRVLDIIPFTSTRKRMSVIIRDEDGIIHLICKGADTVIFPRLSSGQNNIIEKTKKHLASFSSEGFRTLCIARRTIDKQDYLEWKVNFNEANSAIHERNEKVSKVSEMIEQELELLGGTAIEDKLQENVPETIALLAIAGIKLWVLTGDKVETAINIGYSCNLLDPNMTIFRIDANSFGALEEVEAFIRNTLCFNFGYMGTDEEFRFLLKDHSPPSPKHAIVIDGDALNFVLSEQVSFLFLMLCKQCKTVLCCRVSPSQKAAVVALVKKSLNVVTLAIGDGANDVSMIQEADVGVGIKGVEGQAASMSADYAIGQFSFLGRLLLVHGRWDYKRMSQMISFFFYKNVIWTFILFWYQFYNEFDGNYIFDYTYVMLFNLLFTSLPVIIAGCFDQDVDASVSMKNPSLYQRGILGLEWNGKRFWSYMLDGIYQSLVCFGVALFVFKFGDFVSWTGRNIECIEDIGLFISSPTIFVINIFILMNQERLNLISLITWMFSIGVFWIWTFIYSEVGPSYAFHKSASRTCQTFGFWCVTVLTIALCLLPRFSYICLQKLFYPRDIDLLRRRLCAKSDDETSSSSSFATDIEMCEQCNDPLSSKKNSGIVTSVSFDDSNK | Catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. | O36028 |
Q98QJ9 | NAGB_MYCPU | Glucosamine-6-phosphate isomerase | Mycoplasmopsis | MREIYIFKDLQDLHKFSAKQIIDQIKIKKDSTLGFATGKTPLKTYQLLVKDHQENKTSWKDITSFNLDEFVDIDPSHPESFIKQMKSNLFDHLDINEQKINIPKSNSSNPDQEALNYENKIRKNNGIDLQFISIGVNGHIAYNEPGTPKDSLTHVSNLTKETILDLIAKNKFSSIDEVPKKAITMGVKTILNQCKKIMMVSFGKEKAQVTKQMLEDKPNENVTASFLQEHPNCIYILDKEAASLLNEETLKKAKWI | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | Q98QJ9 |
P52726 | MT_OREMO | null | Oreochromis | MDPCECAKTGTCNCGGSCSCTKCSCKSCKKSCCDCCPSGCSKCASGCVCKGKTCDTSCCQ | Metallothioneins have a high content of cysteine residues that bind various heavy metals. | P52726 |
Q3AAQ2 | DEOB_CARHZ | Phosphodeoxyribomutase | Carboxydothermus | MKRVVLIVLDSVGIGELPDAHLYGDEGSNTLANTAKKVGGFELPNLEKLGLGKIHPILGLKGDIKALGAYGKMGEKSPGKDTTTGHWEICGLILEKPFPVYPNGFPEDLIKRFEEAIGRKTLGNKPASGTAIIEELGEEHMRTGYPIVYTSADSVFQIAAHEEVIPLEELYKMCKIARGLLTGEHAVGRVIARPFTGTPGNFKRTANRHDYSLEPTGKTVLDKLVEQGYEVLGVGKIYDIFAGRGLTWHESTKNNEDGLVKTVNLLYKDFTGLLFTNLVDFDMVYGHRNNAEGYYEALKQFDSYLPKIMEKLREDDLLIITADHGCDPTTPSTDHSREYVPLLVYGHSIKEDVNLGTRETFADVAATLEEIFGLEPGIGQSFWGEIRK | Phosphotransfer between the C1 and C5 carbon atoms of pentose. | Q3AAQ2 |
P61490 | CH60_THET2 | Heat shock protein 60 | Thermus | MAKILVFDEAARRALERGVNAVANAVKVTLGPRGRNVVLEKKFGSPTITKDGVTVAKEVELEDHLENIGAQLLKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPLALKRGIEKAVEAAVEKIKALAIPVEDRKAIEEVATISANDPEVGKLIADAMEKVGKEGIITVEESKSLETELKFVEGYQFDKGYISPYFVTNPETMEAVLEDAFILIVEKKVSNVRELLPILEQVAQTGKPLLIIAEDVEGEALATLVVNKLRGTLSVAAVKAPGFGDRRKEMLKDIAAVTGGTVISEELGFKLENATLSMLGRAERVRITKDETTIVGGKGKKEDIEARINGIKKELETTDSEYAREKLQERLAKLAGGVAVIRVGAATETELKEKKHRFEDALNATRAAVEEGIVPGGGVTLLRAISAVEELIKKLEGDEATGAKIVRRALEEPARQIAENAGYEGSVIVQQILAETKNPRYGFNAATGEFVDMVEAGIVDPAKVTRSALQNAASIGALILTTEAVVAEKPEKKESTPASAGAGDMDF | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | P61490 |
Q9CIV9 | DHAS_LACLA | HTH-type dhaKLM operon transcriptional activator DhaS | Lactococcus | MSAFFLNMKKSIITQKIIAKAFKDLMQSNAYHQISVSDIMQTAKIRRQTFYNYFQNQEELLSWIFENDFAELINDNSDYYGWQNELLLLLRYLDENQIFYQKIFVIDKNFEHFFLIQWENLLDKVIFDQEKKSDYHWSDLEKSFICRYNAAAICAITRESIIRGNSLEKLYSQIVNLLLAQIKIFES | In complex with DhaQ, upon activation by dihydroxyacetone, activates transcription of the dhaKLM operon. Binds the inverted repeat sequence 5'-GGACACATN(6)ATTTGTCC-3' located upstream of and partially overlapping with the -35 promoter sequence of the dhaKLM operon promoter. | Q9CIV9 |
Q0SNY5 | MNME_BORAP | tRNA modification GTPase MnmE | Borreliella | MSKLFERDDDIVALATPFLSSALCVIRSSGASSISKFSKIFSNHSALNSAAGNTIHYGYILDNENNCKVDEVVVCLYRAPKSFTGQDAVEVIAHGSVIGIKKIIDLFLKSGFRMAEPGEFTFRSFLAKKIDLTKAEAINEIIFAKTNKAYSLAVNKLSGALFVKIDTIKKCILNFLSAVSVYLDYEVDDREIDIPFDLILNSKVELKKLIDSYKVYEKIDHGITLVLAGSVNAGKSSLFNLFLKKDRSIVSSYPGTTRDYIEASFELDGILFNLFDTAGLRDADNFVERLGIEKSNSLIKEASLVIYVIDISSNLTRDDLLFIDSNKSNSKILFVLNKIDLKINKSTEEFVRSSVLNSSNLIMISIKNLEGIDILYDKIRTLISYERVEIGLDDIIISSSRQIQLLEKAYALILDLLSKIDRQVSYDMLAFDAYEIINCLGEITGEVSSEDVLDNMFKNFCLGK | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q0SNY5 |
Q1IIT5 | RBFA_KORVE | Ribosome-binding factor A | Candidatus Koribacter | MEQRALKHHRERLGEAIREEIGAILEGELGDPRIGLVTVSEVMIASNGKSAIVLVAVAGEEQEAVDTLEGLAAATGYIRHEVAARLGLRVAPELLFRLDQTERYGGRVEELLKRVNKRKKSSR | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. | Q1IIT5 |
P57298 | MUTT_BUCAI | dGTP pyrophosphohydrolase | Buchnera | MELLSKKKVYITRGKYKKNIWEFPGGKVKKHENIVHALKRELLEEVGIIVLKINFFQYIEYIYPEKKIKLYFFLKKKWKGRPYSIEGYTYLWKRLCHLRALDFPLANHSVINALKKNNILIKFR | Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. | P57298 |
A0JTZ0 | FOLD_ARTS2 | Methenyltetrahydrofolate cyclohydrolase | Arthrobacter | MAQAAKILDGKAAAAAIKSELAERVAKLKARGVTPGIATVLVGADPASQLYVSMKHKQSVEIGMNSIQRELPADATQAQVEALIDELNADPACHGYIVQLPLPKHLDTDAILERIDPAKDADGLHPTNLGRLVLNVSGEITSPLPCTPRGVIELLERNGYSLSGKHVVVVGRGVTIGRTIGLLLTRRSVNATVTLTHTGTENLSQLLRQADVIVGAAGAKHIVKAADVKPGAALLDVGVTRETDPETGKSKVHGDIDPAAAEVAGWISPNPGGVGPMTVALLMTNVVEAAERKLAAESAGTA | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | A0JTZ0 |
O43896 | KIF1C_HUMAN | Kinesin-like protein KIF1C | Homo | MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINEDPNARLIRELQEEVARLRELLMAQGLSASALEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNTESQIGPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERERGVPPPPGPPSEPVDWNFAQKELLEQQGIDIKLEMEKRLQDLENQYRKEKEEADLLLEQQRLYADSDSGDDSDKRSCEESWRLISSLREQLPPTTVQTIVKRCGLPSSGKRRAPRRVYQIPQRRRLQGKDPRWATMADLKMQAVKEICYEVALADFRHGRAEIEALAALKMRELCRTYGKPDGPGDAWRAVARDVWDTVGEEEGGGAGSGGGSEEGARGAEVEDLRAHIDKLTGILQEVKLQNSSKDRELQALRDRMLRMERVIPLAQDHEDENEEGGEVPWAPPEGSEAAEEAAPSDRMPSARPPSPPLSSWERVSRLMEEDPAFRRGRLRWLKQEQLRLQGLQGSGGRGGGLRRPPARFVPPHDCKLRFPFKSNPQHRESWPGMGSGEAPTPLQPPEEVTPHPATPARRPPSPRRSHHPRRNSLDGGGRSRGAGSAQPEPQHFQPKKHNSYPQPPQPYPAQRPPGPRYPPYTTPPRMRRQRSAPDLKESGAAV | Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. | O43896 |
Q2W2L1 | KAD_MAGSA | Adenylate monophosphate kinase | Magnetospirillum | MNLVLLGPPGGGKGTQAKRLQDKYGLVQLSTGDMLRAAVASGSEVGKKAKAVMDAGQLVSDEIVIAIIDERLDQADVAKGAIFDGFPRTVAQAEALDAMMAKKGKKLDFAIEIRVPDAYIVERITGRYTCAKCGAGYHDKFQLPQVAGKCDSCGGTEFARRPDDNVDTVTKRLDAYHAQTAPLLPYYDKKGSLKLVDGTMDIADVTKALEGILDASK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | Q2W2L1 |
O58665 | PANB_PYRHO | Ketopantoate hydroxymethyltransferase | Pyrococcus | MREITPKRIREMKGKEKITMITAYDYPSALLADKAGFDIVFIGDSLGMVVYGEPSTLNVTMEQMIFHTRAVAKAVKRALVLADMPFGSYEVSVEEGIKNAIKLVQAGADAVKIEGGYDHRKLVKKLVRIGIPVMGHTGLTPQRYLRLGGYRIMGGTEEEVEEILRDAKALEKAGAFAIVLEFVLADVAKLVTEEVSIPTIGIGSGPYVDGQVLVWHDVLGLYESSPPFAKRYANLKEEILRAISTFREEVKEGKFPGREHYWEFQDKEEFKRIKDNVMKKLNL | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | O58665 |
B0K532 | CLPX_THEPX | ATP-dependent Clp protease ATP-binding subunit ClpX | unclassified Thermoanaerobacter | MVKYDNQKQLKCSFCGKTQDQVKRLVAGPGVYICDECIELCQEIINEEFEEDIDMGIGELPKPKEIKEFLDQYVIGQEKAKKALAVAVYNHYKRINSRIKPDDVELQKSNILLLGPTGSGKTLLAQTLAKLLNVPFAIADATSLTEAGYVGEDVENILLKLIQAADYDIEKAEKGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTIANVPPQGGRKHPHQEFIQIDTTNILFICGGAFEGIEKIIESRIGKKSLGFGAEVQSRKEKDLSEILSHIMPQDLLKFGMIPEFIGRVPIVVTLDPLSKDDLVRILTEPKNALTKQYEKLFELDGVKLEFDKKALGLIADMALERKTGARGLRAILEEIMLDVMYEIPSSDNIEKCIITEETVLKKAPPTLVYSDAQKAKKKIKKTESVS | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | B0K532 |
O35796 | C1QBP_RAT | Glycoprotein gC1qBP | Rattus | MLPLLRCVPRALGAAATGLRASIPAPPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPELTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQTTGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ | Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense. | O35796 |
A5CT01 | ISPG_CLAM3 | 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase | Clavibacter | MPAVNLGMPKVPEVLAPRRKTRQISVGKVKVGGNAQVSVQSMTTTQTTNINATLQQIAELTATGCDIVRVAVPHQDDADVLHILAKKSQIPIIADIHFQPRYVFTAIDAGVGAVRVNPGNIRKFDDQVGAIAKAAKAAGVSIRIGVNAGSLHPSLLQKYGKATPEALVESAVWEASLFEEHDFHDFKISVKHNDPVIMVKAYRLLAERGDWPLHLGVTEAGPAFQGTIKSATAFGILLSEGIGDTIRVSLSAPPAEEVKVGLQILQSLNLRERKLEIVSCPSCGRAQVDVYSLAEQVTEGLKHVNVPLRVAVMGCVVNGPGEAREAELGVASGNGRGQIFVKGEVIKTVPEAEIVQTLIEEANRLAAEMPAGSIGSPEILV | Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. | A5CT01 |
Q9CDX5 | RS14Z_LACLA | 30S ribosomal protein S14 type Z | Lactococcus | MAKKSMVVKNQRPAKFSTQAYTRCERCGRPHSVYRKFKLCRICLRELAYKGQLPGVKKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | Q9CDX5 |
Q9LLC1 | BCCP2_ARATH | Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic | Arabidopsis | MASLSVPCVKICALNRRVGSLPGISTQRWQPQPNGISFPSDVSQNHSAFWRLRATTNEVVSNSTPMTNGGYMNGKAKTNVPEPAELSEFMAKVSGLLKLVDSKDIVELELKQLDCEIVIRKKEALQQAVPPAPVYHSMPPVMADFSMPPAQPVALPPSPTPTSTPATAKPTSAPSSSHPPLKSPMAGTFYRSPGPGEPPFVKVGDKVQKGQIVCIIEAMKLMNEIEAEKSGTIMELLAEDGKPVSVDTPLFVIAP | This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | Q9LLC1 |
P72588 | DNLJ_SYNY3 | Polydeoxyribonucleotide synthase [NAD(+)] | unclassified Synechocystis | MTTPDRLLQLRQQLQKASYAYYVLDAPVMEDSVYDQLYRELQRLEAENPELITPDSPTQRVGEQPASQFRSVAHNIPLYSLENAFNVQELQQWQERWQRIAPTIEKAEYVCELKIDGSAIALTYENGLLVRGVTRGDGTTGEEISQNIKTIRSIPVKLNLDNPPPTVEVRGEAFLPLEEFNRINHEREAQGESLFANPRNAAAGTLRQLDPKIVHQRRLQFFAYTLHLPGQEDKIQSQWQALEYLKKAGFMVNPHCQLCKGLDEVVAYFEDWEGARQRLPYMTDGVVVKINQYPLQRELGFTQKFPRWAIALKYPAEETPTVVKAIEVNVGRTGAVTPLAVMEPVQLAGTTVQRATLHNQDRIQELDIRVGDTVIIRKAGEIIPEVVRVMTELRPENTTPYIFPSHCPACGSPLVRPLEEAVIRCVNSSCSAILQGSLIHWASRNALDIQGLGEKVVITLLENRLVNSVADLYGLQVEQLLGLERFAQKSAEKLIAAIEVSKSQPWSRILFGLGIRHVGQVNAKLLSQQFPTVEKLSQASIPDLEGVYGIGPEIAEAVVNWFRNPGNQQLIQDLEELGLVLANQGIDQTKTDSGKLKGKTFVLTGTLPNLSRLEAQELIEQSGGKVTSSVSTKTDYVLLGDKPGSKAAKAESLGIKLLSEAEFLQLLEP | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | P72588 |
Q7V303 | NDHK_PROMP | NDH-1 subunit K | Prochlorococcus | MNNSLSPKAIRELREETCNPLGAPQVTTDLSENIIMTSLDDLHNWARLSSLWPLLYGTACCFIEFAALIGSRFDFDRFGLVPRSSPRQADLLIVAGTVTMKMAPALVRLYEQMPEPKYVIAMGACTITGGMFSADSTTAVRGVDKLIPVDLYLPGCPPRPEAIFDAVIKLRKKVANESILERNKSEQTHRYLTVDHEMNLVFSENTGEYLNKKSEKSIESSKLNPVEESSENIYETNSIDEVIK | NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | Q7V303 |
P47620 | RSMG_MYCGE | 16S rRNA 7-methylguanosine methyltransferase | Mycoplasma | MNNANFEKYVDLVFEANKNFNLTGFKTKEAIYQNLVIEILTLFKGYEKFFIDKTVADLGSGNGSPGIILKLLFQKIKKLVLIDSKHKKISFLNKLTKQLNLEKTVAICERIEVHKNHYDVICSRGLSTIIKVNDLAFSLLNSKGIIFHIKQSLDQYIEFEKSNQKNQFNLLFIKHFTSQNKKLILIALQKND | Specifically methylates the N7 position of a guanine in 16S rRNA. | P47620 |
P0AA37 | RLUA_ECOLI | tRNA pseudouridine(32) synthase | Escherichia | MGMENYNPPQEPWLVILYQDDHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETGKPAQTEYEVVEYAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAPRLLLHAEMLTITHPAYGNSMTFKAPADF | Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. | P0AA37 |
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