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
|
|---|---|---|---|---|---|---|
P01945
|
HBA_MESAU
|
Hemopressin
|
Mesocricetus
|
VLSAKDKTNISEAWGKIGGHAGEYGAEALERMFFVYPTTKTYFPHFDVSHGSAQVKGHGKKVADALTNAVGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLANHHPADFTPAVHASLDKFFASVSTVLTSKYR
|
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
|
P01945
|
B2IR74
|
CCA_STRPS
|
tRNA-NT
|
Streptococcus
|
MRLTQMPSEFQKALPVLEKIKEAGFEAYFVGGSVRDALLHSPIHDVDIATSSYPEETKQIFPRTADIGIEHGTVLVLDGDEEYEVTTFRTEDVYVDYRRPSAVSFVRSLEEDLKRRDFTVNAFALDETGEIVDLFHGLEDLEKQVLRAVGVASERFNEDALRIMRGFRFQASLGFALEPETFKAMKTLTPLLEKISVERTFVEFDKLLLAPFWRRGLASMIESQAYDYLPDMASSQDKLNRLFDLETDFTFESSEQAWAALLWALEIENAQSFLKSWKTSRQFAKQVQDLLIILALRENGELSKRDCYRFDIDLLLQAENLRQAQGKEVNPQAITEKYQSLTIHDKKDIQINGGILIKEYGYQPGPDLGEILTEIEFAIVDGELENNREAIHAYLREKK
|
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.
|
B2IR74
|
B0BUA6
|
RNC_ACTPJ
|
Ribonuclease III
|
Actinobacillus
|
MQLERLQKKLGYQFTNLDYLLQALTHRSAGAKNNERLEFLGDSILNFAIGKALFEKFPKANEGELSRMRATLVREQTLAILARKFGLGEYMKLGAGELKSGGYRRESILSDCVEAIIAAIYLDAGMDKAIAQVHLWYQDLLAEMKPGDAQKDPKTRLQEFLQGRKLPLPTYEVLNIKGEAHNQTFKVTCKIEMLEEIFIGIGTSRRKAEQNAAEQVLAKLTTK
|
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
|
B0BUA6
|
Q9CJW4
|
PYRE_PASMU
|
Orotate phosphoribosyltransferase
|
Pasteurella
|
MEAYKSEFIQFALSRQVLKFGEFTLKSGRISPYFFNAGLFNTGADLARLGEFYAKAIQASGVEYDVIFGPAYKGLPIATTVSVALFNHFQIDKPVCFNRKEAKDHGEGGQLIGYGLSGKILLVDDVITAGTAIRESMTLIAQNQAELSAVMIALNRQEKGKGELSAIQEVERDYQCQVLSIVNFDDLMTFIEQAPEYQQYLPAMRAYREQYGVK
|
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
|
Q9CJW4
|
Q8YEN0
|
ILVD_BRUME
|
Dihydroxy-acid dehydratase
|
Brucella
|
MPPYRSRTTTHGRNMAGARGLWRATGMKDEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIESAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMAALRLNIPVVFVSGGPMEAGKVVWEDSVKKLDLVDAMVAAADDHYTDEQVKAIERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSTLATHADRKRLFVEAGHLIVDLARRYYEQDDESVLPRSIATFSAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMADIDRLSRRVPVLCKVAPAVSSVHMEDVHHAGGIMGILGQLDNAGLLTTSIPTVHSETLAKALDHWDVTRTNSEMVHKFYSAAPGGVPTQVAFSQERRFDKVDTDREKGVIHSKEHAFSQDGGLAVLYGNLAEDGCIVKTAGVDDSILKFSGPARIFESQDSAVLGILNGKIKPGDIVLIRYEGPRGGPGMQEMLYPTSYLKSKGLGKACALITDGRFSGGSSGLSIGHVSPEAAEGGTIGLVREGDIIDIDIPNRKIHLAVDDATLAERRAEQDAAGWKPAEERKRKISTALKAYAAMATSAARGAVRKLPD
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
Q8YEN0
|
O34543
|
MHQE_BACSU
|
Putative ring-cleaving dioxygenase MhqE
|
Bacillus
|
MKTEGLHHVTAFARDPQENLRFYTEVLGLRLVKKTVNFDDPGTYHFYFGNQNGDPGTIMTFFPFQGSGQGTVGKGQAGRVYFSVPSGSLSFWKERLEKSGLSLEEKTLFGEKGLIFDDTEDLPLAIMEDAKSGKSEWTPDGITTNEAITGMKGVLLYSYDPQATIQLLTESFGYTKVAEEDQIVRLASSAAVGGVIDVHLHPEKRGVGGYGTVHHVAFRTKKKEQAKWLPIIAENHLPSSEILDREYFTSVYFREKGGILFEIATDEPGFMTDETFAELGTSLKLPEWLEKHRQQITDILPEL
|
Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds.
|
O34543
|
Q5U9D7
|
MRGRE_MACFA
|
Mas-related G-protein coupled receptor member E
|
Macaca
|
MEPREAGQHAGAADGAQEDVAFNLVILSLTEGLGLGGLLGNGAVLWLLSSNVYRNPFAIYLLDVACADLIFLGCHMVAIIPDLLQGRLDFPGFVQTSLATLRFFCYIVGLSLLVAVSVEQCLAALFPAWYSCRRPRHLTTCVCALTWACCLLLHLLLSGACTQFFGEPSRHLCRTLWLVAAVLLAVLCCTMCGASLMLLLQVERGPQRPPPRGFPTLILLAVLLFLFCGLPFGIYWLSRNLLWHIPHYFYHFSFLTAAVYCAAKPVVYFCLGSAQGRRLPLRLVLQRALGDEAELGAVRETSRRGLVDIAA
|
Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
|
Q5U9D7
|
A4XW05
|
MOAA_PSEMY
|
Molybdenum cofactor biosynthesis protein A
|
Pseudomonas
|
MHTNQLVDPFGRRITYLRLSVTDRCDFRCTYCMSEDMQFAPRQQILSLEELYAVADAFIGLGVRRIRITGGEPLVRKNLLSLLQRLGERDELDDLAITTNGSQLAEMAAPLRAAGVRRLNISLDSLQRERFAAFTRRDKLDQVLAGIDAARAAGFDRIKLNSVVQSGRNDDEVLDLVEFAVERGLDISFIEEMPLGSVVSHSREQTFCSSDEVRQRIEQRHALVRSSKVTGGPSRYWQVVGTQTQVGFISPHSHNFCGDCNRVRVTAEGKLVLCLGHDNALDLKRLLRAHPGDSERLRQALTEALRLKPERHHFATDEQVQVVRFMSMTGG
|
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
|
A4XW05
|
Q5E9F6
|
VPS72_BOVIN
|
Transcription factor-like 1
|
Bos
|
MSLAGGRAPRKTAGNRLSGLLEKEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSDFDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVSTPAGSSQKTREEKALLPLELQDDGTDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITEELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDVEGLDPAPMASALAARAGTGPVIPPARCSRTFITFSDDATFEEWFPQGRTPKIPVREVCPVTHRPALYRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQKIVIK
|
Deposition-and-exchange histone chaperone specific for H2AZ1, specifically chaperones H2AZ1 and deposits it into nucleosomes. As component of the SRCAP complex, mediates the ATP-dependent exchange of histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling.
|
Q5E9F6
|
Q729A4
|
PANC_DESVH
|
Pantoate-activating enzyme
|
Desulfovibrio
|
MQIITEPQTIQQACLRWRADGVHTALVPTMGYYHAGHESLMAHARAVSEKVIVSLFVNPAQFGPGEDFAAYPRDLERDAAMAEAQGVDVLFAPKAEDLYKKDHATWVEVPALSQTMCGLSRPTHFRGVCTVVTKLLMLTMPRIAVFGQKDWQQVAVIRRMVRDLNIPVDIVGRPIVREPDGLAMSSRNIYLTAEERLQAPHIHHGLALGRAITQSGERDAETIKTAIRRYWAQNLPGGEEDYLTIVDPVSLEPVDRLTGATLCATAVRVGQARLLDNMMLLGD
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
Q729A4
|
Q10ED2
|
KNOS8_ORYSJ
|
Homeobox protein OSH43
|
Oryza sativa
|
MESFASLAGGGSSSTTARLPELISPENPDHISPPPLLYQLLAGPESSARQHGHDGHHHGGGGGEAAAAAVQGQVSPAGAEAAVKAEIMSHPQYSALLAAYLGCKKVGAPPDVLTKLTAVPAAQQLDEADGHPRRRHEPQRDDDPDQLDQFMDAYCSMLTRYREELERPILEAAEFFSRVETQLDSLAESNCEGTGSSEEEQDPSDKQLKHQLLRKYGGSLGDLRQVFSKRTKKGKLPKEARQKLLHWWELHYKWPYPSEMEKMTLAQTTGLDQKQINNWFINQRKRHWKPTPVAGTAFPTMEAAGGGFRHSGHGGGLAAAAALPLYMGRPFVVDGMYRLGS
|
Probable transcription factor that may be involved in shoot formation during embryogenesis.
|
Q10ED2
|
Q46XB7
|
AROE_CUPPJ
|
Shikimate dehydrogenase (NADP(+))
|
Cupriavidus
|
MTSTESSQPADRYVVVGNPVAHSRSPFIHAAFARQTGEAVEYGRLEAPLDAFADTMRAFLAEGGYGFNVTVPFKLQAYDLADRLTPRAEAAGAVNTMWIEDGLIHGDNTDGIGLVRDIQDNLDTLLEDKRVLLLGAGGAAMGAMLPLIECRPSRIVVANRTASRASDMLEEFVEAADSFGVELWGGGLDALEQLSEDDVCDVVINASSSSLHGEVPPVPAFLLGDGVLAYDMMYGAEPTVFLQHAAQCGARTADGLGMLVEQAAEAFYIWRGVRPRTAPVLADLRAALQAERKG
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
Q46XB7
|
Q1LU72
|
PCKA_BAUCH
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Candidatus Baumannia
|
MLSNNIIRQQLIHYGITDCCELIYNPSFEQLVREETNHNLTNLERGTITNSGAIAVNTGIFTGRSPLDKYIVCDNDTHHQLWWSDQDKTSNNQPISQITWQYLKKLVSKQLSYKRLFIIDVYCGAKKNSRLRVRFVTEVAWQAHFVKNMFIQPDAIDLISFEPEFIVLNGAKCTNPNWREQNMHSENFIALNLTEGMQLIAGTWYGGEMKKGLFTVMNYHLPLKGIASMHCSANVGINKDVALFFGLSGTGKTTLSHDTNRALIGDDEHGWDNDGIFNLEGGCYAKTINLKPELEPEIFQAIRCNALLENVMVRADGSVNYHDNSKTDNARVSYPLNHIKNRVQPVSCASHASTIIFLTADAFGVLPPVATLTNEQAQYYFLSGFSAKLSGTERGIISPVPTFSACFGAAFLALHPTVYAALLAKRMNIAGTNAYLVNTGWNGNGSRIALKDTKAIINAILNKQIQDTPTIKLPIFNLSIPQILIGVDSNILDPRTSYINSSEWQNKARSLAQLFIKNFNKFTLPLTCKKLHNAGPQL
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
Q1LU72
|
C6E1S9
|
RUVA_GEOSM
|
Holliday junction ATP-dependent DNA helicase RuvA
|
unclassified Geobacter
|
MIALLTGKLAYKSPEFIILDVNGVGYQVHIPFSTYYTLPAEGGALSLQIHTSVKEDAINLYGFRTQQEKELFQLLIGVSGVGPKLATGILSNSEPSELADSLVNGNLARLSAIPGIGKKTAERLVLELKEKMKKLGLAQPQAGGATAPAKQEIRDDVLSALINLGYKEAVVQKALAELKVTEDATVELVLKQALKILMK
|
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.
|
C6E1S9
|
Q494C5
|
ATPA_BLOPB
|
F-ATPase subunit alpha
|
Candidatus Blochmannia
|
MQLNSNEISKLIKRRIAQFDITCEIRNEGTITAVGDGVIHIHGLTNVMQGEMIALPSDQFAVALNLERDSVGAVVMGSYLNLSEGMVAKCTGNILRVPVGTALLGRVVNALGVPVDNKGVIQCSCYFPVEAVAPSVIDRKSIDEPIQTGYKSVDSMIPIGRGQRELIIGDRQTGKSALAIDAIINQRYSGVKCIYVAVGQKATTVANVVKKLEEHRALSNTIVVIASASESAVLQYLAPYSGCAMGEYFRDLGEDALIVYDDLSKQAIAYRQISLLLRRPPGREAYPGDIFYLHSRLLERASRVSSDYVERCTHGKITGRTGSLTAIPIVETQAGDVSSFIPTNVISITDGQIFLESHLFNSGIRPAVNPGISVSRVGGSAQTNIMKVLSGGIRTALAQYRELAAFSQFASELDDVTRKQLQHGQKVTELLKQKQYAPMAVSCQSIILFAAVHGYLEDVEVSKISDFESALILYMTYTEKELIKIIDHDGVYNIDIENKFKSILETFKSNQSW
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q494C5
|
P94336
|
FTSQ_CORGL
|
Cell division protein FtsQ
|
Corynebacterium
|
MNKKVIAIVVGVVVVLVAILGVVAWFVPILKVGNIEVTGATRTDPDQVLEVSGIVEGENLFRVDATAAGQNIVELPWVKSVTVNRALPSTITVELTEREPAVFIKRADGDHVIDTEGKEIIIGTPPVGTVEVSGADEGNSEVLPAVIAVINAIKAQDAQMTESIQVVEAPDQFDILLKMNDGREIYWGSSENNHDKAVAMSTVLKREGQRWNISSPSMVTVR
|
Essential cell division protein.
|
P94336
|
Q02CT4
|
NUOK1_SOLUE
|
NDH-1 subunit K 1
|
Candidatus Solibacter
|
MMNAVPISWFLTLSAILFALGVAGFLFRRNIITVFMSIELMLNAVNLSFVTFSYQHKEVAGHLFTFFVMVVAAAEAAVGLAIILTVFKNRSTLNIDDVNSMKN
|
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.
|
Q02CT4
|
A3CPT4
|
NRDR_STRSV
|
Transcriptional repressor NrdR
|
Streptococcus
|
MRCPKCGGNKSSVVDSRQAEDGNTIRRRRECEECQHRFTTYERVEERTLVVVKKDGTREQFSRDKIFNGIIRSAQKRPVSSDEIEEIVNRIEQKVRSQSDNEINSEYIGSLVMDELAELDEITYVRFASVYRSFKDVGELESLLKQITKGSKKKKDK
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
A3CPT4
|
Q3KLJ5
|
RUVC_CHLTA
|
Holliday junction resolvase RuvC
|
Chlamydia
|
MADLIMGIDPGTLVCGYALIKVENRYHIHPHSFGKVKLSQKLALAHRYKQLFTEISTILQQESPKAVVLETQYVHKNPQSTIKLGMARGVLLLAASLQDVPVFEYAPNTAKKAAVGKGNASKKQVQLMVSKLLRVPDLLAEDNEDIADAFALAMCHAHLALYQDLKKTLV
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
Q3KLJ5
|
Q8UDP9
|
PRMA_AGRFC
|
Ribosomal protein L11 methyltransferase
|
Agrobacterium tumefaciens complex
|
MSEIRLYVTTTEIKAGEILDLMSDYFGEEDVAIATTEVDEKRDIWEASVYLMAEQEEEFRERVSTLLAPAFPGLVIEKEIIPDVDWIAKSLEGLKPVRAGRFIVHGAHDRDKVQPHDLAIEIEAGQAFGTGHHGTTAGCLEMIEDVLRARKVRNALDLGTGSGVLAIAVRKMRPIPVLATDIDPIAVKVAKENVRLNGIVSGMALETAPGFHSDAFRKHGPFDLIIANILARPLIKMAPQLVTHLAPGGTVILSGILASQRWKVLSAYNGAKLSHIRTIWRNDWVTLHLRKD
|
Methylates ribosomal protein L11.
|
Q8UDP9
|
Q081U7
|
IHFB_SHEFN
|
Integration host factor subunit beta
|
Shewanella
|
MTKSELIEKLATRQSQLSAKEVESAIKEMLEQMATTLETGDRIEIRGFGSFSLHYRAPRTGRNPKTGTSVDLEGKYVPHFKPGKELRERVDAVNP
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
Q081U7
|
Q6BGU0
|
ISU1_DEBHA
|
Iron sulfur cluster scaffold protein 1
|
Debaryomyces
|
MISRSFLRLANPARRAMPAVKRVNMMPSMALPTKRLYHEKVLDHYSNPRNVGTLNKLDVDVGTGLVGAPACGDVMRLQIQVDDETGVIKDVKFKTFGCGSAIASSSYLTELVKGKTIEEAVKIKNTAIAKELSLPPVKLHCSMLAEDAIKSAVKDYRSKRSVKQPTLGPEAAQAETIAT
|
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISU1. In a second step, the cluster is released from ISU1, transferred to a glutaredoxin, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH.
|
Q6BGU0
|
A7ZY06
|
NADA_ECOHS
|
Quinolinate synthase
|
Escherichia
|
MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEETGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPVEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDKHLGRYVQKQTGGDILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVDMADAVGSTSQLIAAAKTLPHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWMAMNGLQAIAKALEQEGSNHEVHVEERLRERALVPLNRMLDFAATLRG
|
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
|
A7ZY06
|
Q7WY67
|
GERT_BACSU
|
Spore germination protein GerT
|
Bacillus
|
MFEWNKYFPFHNQFSKEALKKADPKEVETYVNRVMESVFGSDYAAQFPFRDPLPQKEHPAKPDAKPDVKPDIDIFETADHVFVKVPISEEWLEQVRIKHTSHELWLENLPRADHPKKVNLPCLVKRKGTKAVYKDGLLEVMFQKQQDYNMSEVEIIR
|
Involved in spore germination; probably required at the earliest stage of germination.
|
Q7WY67
|
Q92P48
|
COBB_RHIME
|
Hydrogenobyrinic acid a,c-diamide synthase
|
Sinorhizobium
|
MNGLMIAAPSSGSGKTTVTLGLMRALRRRGLSIAPGKAGPDYIDPAFHTAASGKPCFNYDPWAMRPELLLANAAAAAEDGSVLIMEAMMGLFDGAADGTGAPADLAAALGLAVILVVDCARLSHSVAALVGGYARHRDDVRVAGVILNRVGSDRHEGMLRDALAGIAMPVFGVLRQDAALKLPERHLGLVQAGEHGSLEAFIDHAAMRVASGCDLEAVLAAATPLTVGERAGTLKPLGQRTAVARDVAFAFCYEHLLSGWRGQGAEVTFFSPLADEAPDPRADAVYLPGGYPELHAEQLSNASNFRAAMHKAAGGGARVFGECGGYMVLGEGLVAADGGRYEMLGLLPLVTSFAERKRHLGYRRVTPVDDVFFRGPMTAHEFHYATIVSEGAAEPLFTVRDAAGLDLGRAGLRRRNVAGSFMHLIDFSE
|
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.
|
Q92P48
|
B1XK97
|
NDHN_SYNP2
|
NAD(P)H dehydrogenase I subunit N
|
unclassified Synechococcus
|
MALLTTGKSFIRTVEKSGAVAVYAPLEGGFEGRYVRRLRCSGYSVVNLTARGLGDVAAYLTQYHGIRPPHLGKKDIAGSGAAVGLRYYVPGIASYQLENLPQKSKGIILWIIEGFVLSRQEQEYLVSLTQDNPQIKVVVEMGGDRQFSFKPLADLLV
|
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.
|
B1XK97
|
Q72VI2
|
SERC_LEPIC
|
Phosphohydroxythreonine aminotransferase
|
Leptospira
|
MYLFQERIYNFGAGPAMLPNEVMEIAAAEFLNYKGSGMSVMEVSHREPLFEDVITEAEILLRKLLNLGEDYSIAFFSGGATLHFSALPLNLLKEGESFDVAHTGIWTKKAWEEGLKFNEVNVIYDSTNNHFTDVPVLTDSNLSGKGKYLHITSNNTIYGTQYPEIPKIKQIPLVADMTSELLSRKIDVKDFGVIFAGAQKNIGPSGLSLAIIRNDLLGISGRKIPILLDYSVMVKNRSLYNTPSTYSIYIAKLVFEWLLKLGGIEAIEKVNEQKAKLIYDFIDSSSLYVCPVQKRARSKMNVVFLLKDKNLDSKFLDEAEKNGLHGLGGHRLVGGFRASIYNSMPLTGVQKLVSFMKDFESKI
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
Q72VI2
|
O84810
|
ISPE_CHLTR
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Chlamydia
|
MHFLSPAKLNLFLQILGRREDDFHEIVTRYQAIAFGDQLSLSISSRDSLQVINACHLETPSNSIWKSVALFRRYTGITTPVSWRVVKQIPVGAGLAGGSSNAATALFALNQIFKTGLSDEEMRSLAEQLGVDTPFFFSTGAALGVARGEKIIALEESVSDRYVLYFSSEGVLTSRAFAAVQPSDCSSRKNLEYTQNDLEKPVFRLRLDLKEKKHWLENLWAELPVHIGLTGSGATLFVRYPEILEEDLSYAAQIQRAVTLSGGLLTSPIRRDPTAWYSIYSESALAAT
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
O84810
|
P23917
|
MAK_ECOLI
|
Manno(fructo)kinase
|
Escherichia
|
MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPLPWMDEDELRYREEVPCYCGKQGCIETFISGTGFAMDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNVDRLYQTVGQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWLWPQE
|
Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine.
|
P23917
|
A2SHS3
|
TRPA_METPP
|
Tryptophan synthase alpha chain
|
Methylibium
|
MSRIAATFERLRGQRRTALIPYITAGDPYADATVDIMLAMAGAGADVIELGVPFSDPMADGPVIQKASERALAKGIGMGQVLAMVRSFREHNDTTPVVLMGYANPVERYGIDRFVADAKSAGVDGVLVVDYPPEECEAFAAQLQGADLDPIFLLAPTSTEQRMKDVGRIARGYVYYVSLKGVTGAGHLDTDAVATMLPRIREHVKVPVGVGFGIRDAATAKALAAVADAVVIGSRIVQLLEAEPRESVAAVGGTFIASIREALDSSTEGVRA
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
A2SHS3
|
P0DO32
|
ILIC_NEOS2
|
Ilicicolin H biosynthesis cluster protein C
|
unclassified Neonectria
|
MITNDLIAQHSLTLTIASSVLLVFLLSRLLRKDATGKAQGCRPVAKRWQWDPILGLDIVLAQIGALKGNYYLPWLIELHSNMPKTFEINFFGKRQIYTSEPDNLKAMTATNFHDFGIEPMRRHTKGSMPFADKGISTVDGKEWEFSRFLLKPFFYREVYTSTDRIEPFADHMMALIPGDGESFNMQSLIQRWFLDLTTNFIFGKPMDALENPDRARITWAMLDVLKGGRLRAQFYMMMWAFNWTWWYKAVAEVHDFINVHIRETYKEIEEREQRIKDGKPVEPERTDLIWYMAWNLRDEELLRSQLCLVFVPNNDTTSIFISNCIWHLARHPEAWEKLRQEVLAHGDAPLTFEALRNMKYLQCVLNETHRLTPNNVTQIRVCLNDSVLPVGGGKNAKEPFFVRKGDVVSITKTVMYRDPEIWGNDAEEFKPERFDGRRVFWEFLPFGGGPRRCPAQMMVQTEAAYMLARLARVYRRIEARDPAPYTAVMRIGPSNKTGVQIAVYK
|
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IliC catalyzes the ring expansion of the tetramate intermediate to the acyclic 2-pyridone intermediate that contains the trans bis-diene chain . The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
|
P0DO32
|
Q6FM98
|
NST1_CANGA
|
Stress response protein NST1
|
Nakaseomyces/Candida clade
|
MPSGSKSKKKKSKSKGGVKKHAVEKVAPPIEAEIMDERDESDYPTSRVIKRGPNGDVIVESLPDKSTSGKKSKKKGKLSDLEVSESAKQMGITLDSHWESLSPDEKKNILRIEKEEVLEIIRNYQNDHNCSCSVCGRRHMAMNQEMERMYNLLYELEEQRDPDMNPVKFHLGIIKELQISKNKQILDQTEGPNDNTTHEEVVKNFLSSDIADKLKEEVHQFKQKQLSKQECNRPSSLANDNIEEEIPCAQIPQANEEAMTKDIQKTLEQLSVVEPVSKINVIQEDDLGEIKEENKEYLKFTESFISSQPKIAQKFIQKLDENPCMKAITDEVMQNSSYEFLDALKNLWAPNLLKIVESEDDDNLVNLNETLDPIEFTTMLHHGNPLSQQDYYDLQGAISRKVVNAFNFENRKLEHLSPLEVELFGRFMSSDQDNIFHNMLLEAYNERFKEEPFKMMSNIPQIIKAVATLTNLDGRMMDDVDENHFTSEEERYDDDITDYSDSEYEDYDSEYDDIDNGDIISDVDEPFSTLKSDQLRVNYDTNSGNINHSDNYESNSRLREVTDENEENLQYDTPQEKYNYSDHGKDHGTIADEDEDSIDEGYESSIDDMERLEEGRRLIQIAITKLLQGRIMESYHEKEADSNRLKLLKELEEEQMKKKEKEVKKIKKKEKEKEKRRLQQLAKEEEKRKKEEEERSAREEQERREMERREAQRKKVEEAKRKKDEERRRKLEEQRKREEQQEKQRKAKEEQKRKREEEKKKKEELERQLREEELMKKKEEEERLLREKERAEILKKETELAMSMKENHSSQSLSIQNQFFSNPQNSNIGMQNYFNNDLDNTNAGLGNGGPTNLGVRKNSHVLGLTQVYSDKANNSPGKNDDNNEINNEILNIINAATTAKSGSRTSMDMQALLQPPFTDNVNDQIRSSNLINDQASGMNSNGLSTNFHSPYGSNVFSGENQLSNNLQNDILTGLNADTSSTNLASWTSLPALNNLNANQHILSNNQTPLHQQKGTSPISNTMMDTKRDYLGDELSKLTTMLTTNSLNESPAFSSSNLQSSLWNDQNSSGKTPLGSNTTQIPLSQPAFLGTEPPVHRSSIWGDSSASMFNFSQRLSVPTNSNSVSSQTVPNQNIGMGSSFTNPSIWSTGSDFNVPSRDMNSGVAFTNSFSNTSPRNQFALNSGSMLQNQSQRQNIMDNIRLLSNSPQNNGYIPIDLLYQSINKQSTSDFPSFLNNVIDLERSHNYDLVKDQTGVINGVRVGSENRPVSTAFSNFHQNMDPTMKGPEHLSNSIPGTARNFEGNSYLAKEATMNIIPSSSLDR
|
May act as a negative regulator of salt tolerance.
|
Q6FM98
|
A8FSK8
|
TRMB_SHESH
|
tRNA(m7G46)-methyltransferase
|
Shewanella
|
MSDVTTAEFNEEGKYLRKVRSFVLREGRLTKGQAAAMEQHWPAMGLDYSPEPLDLKEVFGRDADTVLEIGFGMGASLVEMAKASPELNFIGIEVHKPGVGACLSVAGEAGVTNLRVFHHDAIEVLENSIVKGSLARVQLFFPDPWHKKRHHKRRIVQSEFAQLIRNTLKIGGVFHLATDWENYSEHMLEVMGAAEGYKNQSLTGDVVERPDHRPLTKFEARGHRLGHGVWDIMFERID
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
A8FSK8
|
Q30UA5
|
SYE1_SULDN
|
Glutamyl-tRNA synthetase 1
|
Sulfurimonas
|
MIVTRFAPSPTGYLHIGGLRTALFSYLWARKNGGKFLLRIEDTDKARNSQEAAEAIVKAFNWLGLEHDGEITYQSQRDDIYAIYVKQLLDEGKAYRCYMSREELDALRETQMANKERTKYDGKYRDFDGTPPDGVDSVIRIKAPLSGEIIVRDGVKGDVVFKAEDILDDFVIARADGSPTYNFVVAIDDHLMGVTEVIRGDDHLSNTPKQIVIYEALGFDVPKFYHVPMIHNSEGKKLSKRDGATDVMAYKEMGYTPAALLNFLVRLGWSNGDQEIFSMDEMRELFDPKNINRSASIYNTEKLDWLNSHYIKNTPNQELAKMLEEYNLTIASHDKKEILLDALKERAKTLKELALLVTEVINPPASYDEKALEKSLKGEAVEVLNNFIAKLSACKELHLPSEYHHVMQEVVDEMGIGFGKIGQPLRVALLGKMSGPGLDSVMAVIGIDETILRVKSALALVK
|
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).
|
Q30UA5
|
D3ERJ1
|
ECFT_STAA4
|
Energy-coupling factor transporter transmembrane protein EcfT
|
Staphylococcus
|
MKNKLIIGRYLPINSFVHHLDPRAKLMFVFLFIILIFFCHSPLTYLWVFALILFIMRLAKIQLWFLIKGLTPIFFFLIFTLMMHIFLTKGGYVLVEWHGITIETNGILEGLYISLRLIGIVMIATIMTLSTSPIDLTDAFERLLAPLKMFKLPVHQLSMIMSIALRFIPTLMDELDKIILAQKSRGSEISSGNIATRIKSFIPLLVPLFISAFQRAEELAVAMEVRGYDANVKRTSYRQLKWQLRDTISLTMIIPIAIILFVLKYSGV
|
Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
D3ERJ1
|
A7ZHN7
|
SFSA_ECO24
|
Sugar fermentation stimulation protein A
|
Escherichia
|
MEFSPPLQRATLIQRYKRFLADVITPDGRELTLHCPNTGAMTGCATPGDTVWYSTSDNTKRKYPHTWELTQSQSGAFICVNTLWANRLTKEAILNESISELSGYSSLKSEVKYGAERSRIDFMLQADSRPDCYIEVKSVTLAENEQGYFPDAVTERGQKHLRELMSVAAEGQRAVIFFAVLHSAITRFSPARHIDEKYAQLLSEAQQRGVEILAYKAEISAEGMALKKSLPVTL
|
Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism.
|
A7ZHN7
|
Q8DUI0
|
CLPX_STRMU
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Streptococcus
|
MAGNRTNDVTVHCSFCGKNQDEVKKIIAGNGVFICNECVELSQEIIREELAEEVLADLSEVPKPKELLAILDSYVIGQDRAKRALAVAVYNHYKRISFTESQDDQDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATALTEAGYVGEDVENILLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPQQEMIQIDTKNILFIVGGAFDGIEDIVKQRLGEKIIGFGQNNKKIDDQSSYMQEIISEDIQKFGLIPEFIGRLPVLAALEQLTVDDLVKILTEPKNALVKQYQTLLSYDGVELEFDQEALQAIAQKAIERKTGARGLRSIIEETMLDLMFEIPSQEDVTCVRITKKAVEGTDKPILETAS
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
Q8DUI0
|
B8DRC9
|
ATPD_DESVM
|
F-type ATPase subunit delta
|
Desulfovibrio
|
MTGNIVARRYARALFALGAKSGVGELDKLGSDLAALAGALDAAPELGRIFRNPIITAGEKRNVILKLVEKYGVSATVRNFCLLLADKGRLDCLSDIQAFYGVLLDAEKGVIRGELMTAVELAEAKRAQVKAALEQQAGRKLELTFSVNKDILGGVVLKVGDRVLDASLRAQLGILKDNIKRGE
|
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.
|
B8DRC9
|
Q99679
|
GPR21_HUMAN
|
Probable G-protein coupled receptor 21
|
Homo
|
MNSTLDGNQSSHPFCLLAFGYLETVNFCLLEVLIIVFLTVLIISGNIIVIFVFHCAPLLNHHTTSYFIQTMAYADLFVGVSCVVPSLSLLHHPLPVEESLTCQIFGFVVSVLKSVSMASLACISIDRYIAITKPLTYNTLVTPWRLRLCIFLIWLYSTLVFLPSFFHWGKPGYHGDVFQWCAESWHTDSYFTLFIVMMLYAPAALIVCFTYFNIFRICQQHTKDISERQARFSSQSGETGEVQACPDKRYAMVLFRITSVFYILWLPYIIYFLLESSTGHSNRFASFLTTWLAISNSFCNCVIYSLSNSVFQRGLKRLSGAMCTSCASQTTANDPYTVRSKGPLNGCHI
|
Orphan receptor.
|
Q99679
|
O82626
|
ERG_ANTMA
|
GTP-binding protein ERG
|
Antirrhinum
|
MKAVRAALRLRPLTNSISTSVYLHRFYSAQPQHTDDEHHPKPEELLHQSDAVFDSSHFDLDLNNLAASGAETTTWDERYRDRVKSRVFDEDDTSSYSKILKRDEEKKYKSAALAKSLLEAALDDEEVEVGEVKEEDQKSLSVGIIGAPNAGKSALTNYIVGTKVSAVSRKTNTTTHEVLGVLTKRDTQICFFDTPGLMLKKSGIPYNDIKVRNESGWSSITLYDVLIVIFDVHRHLTRPDSRVVRLIERVGSVSSTSQKRVLCMNKVDLVTKKNDLVKVAKEFKDLPGYERHFMVSGLKGYGLKDLAQYLTEQAVKRPWDEDPFAMSEEVMKNISLEVVREKLLDYVHQEIPYGIEHRLMGWKELRDGSLRIEQHFITPKMSQRKILVGKKGSKIGTIGIEANEELRSIFKRNVHLILMVKVK
|
Has a crucial role in plant growth and development, possibly by influencing mitochondrial division.
|
O82626
|
Q9PH47
|
ILVD_XYLFA
|
Dihydroxy-acid dehydratase
|
Xylella
|
MPEYRSKTSTYGRNMAGARALWRATGMKDDDFQKPIIAIANSFTQFVPGHVHLKDLGQLVAREIERLGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMANAHCADALVCISNCDKITPGMLMASLRLNIPTVFVSGGPMEAGKTKLTDHKLDLVDAMVLAADPHASDEEVAAVERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTVVATHSDRKQLFLNAGRTVIELCHRWYGNEDATALPRGIATFAAFENAITLDIAMGGSTNTILHLLAAAQEAEVPFTMQDIDRLSRNVPQLCKVAPNTQKYHIEDVHRAGGIFGILAELARGNLLHTDVATVHSKTLGEAIATWDIIGTQDEAVHTFYKAGPAGISTQVAFSQSTRWPSLDTDRTEGCIRDMEHAFSKEGGLAVLYGNIAQDGCVVKTAGVDASIHVFEGSALVYESQEAAVKGILSDEVQPGMIVVIRYEGPKGGPGMQEMLYPTSYLKSKGLGKQCALFTDGRFSGGTSGLSIGHASPEAAAGGAIGLIRDGDRIRIDIPQRAINVLISEEELASRRLEQHAIGWKPAQSRTRKVSSALKAYALLATSADKGAVRNKTLL
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
Q9PH47
|
Q8GY31
|
CDC25_ARATH
|
Sulfurtransferase 5
|
Arabidopsis
|
MGRSIFSFFTKKKKMAMARSISYITSTQLLPLHRRPNIAIIDVRDEERNYDGHIAGSLHYASGSFDDKISHLVQNVKDKDTLVFHCALSQVRGPTCARRLVNYLDEKKEDTGIKNIMILERGFNGWEASGKPVCRCAEVPCKGDCA
|
Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots . Has an in vitro and in vivo arsenate reductase activity . Plays no role in arsenic metabolism .
|
Q8GY31
|
A8AIG6
|
LPXK_CITK8
|
Lipid A 4'-kinase
|
Citrobacter
|
MIARIWSGESPLWRLLLPLSWLYGLVSGGIRLCYRLGIKRAWRAPVPVVVVGNLTAGGNGKTPVVIWLVEQLQQRGIRVGVVSRGYGGKAASYPLLLTPQTSSAEAGDEPVLIYQRTGAPVAVSPVRSDAVKAILARHDVQIIVTDDGLQHYRLARDIEIVVIDGVRRFGNGWWLPAGPMRERASRLKSVDAVIVNGGVARPGEIPMQLAPGLAVNLCTGERRHVAELSNIVAMAGIGHPPRFFATLEACGASLQKCVPLADHQSLAFNDVKALVTDGQTLVMTEKDAVKCRGFAEDNWWYLPVDARLSGEQPDALLEQLISLAR
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
A8AIG6
|
Q9I340
|
MTNC_PSEAE
|
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
|
Pseudomonas
|
MTIKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERVIAILLQWIAEDRKATPLKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLDGHPTVASSPTSSWSERAGYPEGTLLLGSIAPWVPPSAG
|
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
|
Q9I340
|
Q9JVD2
|
ERA_NEIMA
|
GTPase Era
|
Neisseria
|
MDIETFLAGERAADGYRCGFVAIVGRPNVGKSTLMNHLIGQKISITSKKAQTTRNRVTGIYTDDTAQFVFVDTPGFQTDHRNALNDRLNQNVTEALGGVDVVVFVVEAMRFTDADRVVLKQLPKHTPVILVVNKIDKDKAKDRYALEAFVAQVRAEFEFAAAEAVSAKHGLRIANLLELIKPYLPESVPMYPEDMVTDKSARFLAMEIVREKLFRYLGEELPYAMNVEVEQFEEEDGLNRIYIAVLVDKESQKAILIGKGGERLKKISTEARLDMEKLFDTKVFLKVWVKVKSGWADDIRFLRELGL
|
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.
|
Q9JVD2
|
Q5HUG5
|
RSMG_CAMJR
|
16S rRNA 7-methylguanosine methyltransferase
|
Campylobacter
|
MIFKDYDFLQNYDLKNFEEKVKIYKELLSKFNRIHNLTHLKNIDENIFDSIKILDFYDFSKAKNIADIGSGAGFPAVFLAFLLQGNFHLFEPNPKKAAFLRTLKIECELSNLHIYKEKVQEYQNIFKADIITSRALMDVKPLLEICKNLKDENTVFILWKGSEIYQELENIKDYEIFENNLRKYCILK
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
Q5HUG5
|
A9IZV5
|
MDH_BART1
|
Malate dehydrogenase
|
Bartonella
|
MVRKKIALIGSGMIGGTLAHIIGLKELGDVVLFDISEGMPQGKALDIAESSPIDGFDVHLKGANAYEAIEGADVVIVTAGVARKPGMSRDDLLGINLKVMEQVGAGIKKYAPSAFVICITNPLDAMVWALQKFSGLPVHKVVGMAGILDSARFRYFLSEEFKVSVKDVTAFVLGGHGDSMVPLVRYSTVGGISLPDLVKMGWTTQERIDQIIQRTRDGGAEVISLLKTGSAYYAPAASAVSMAEAYLKGTKRVVPVAAYLSGEYGVNDTYVGVPVVLGSGGVERVIEIDLDKEERDAFDYSVNAVKKLCEACIALVPSLK
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
A9IZV5
|
C0HJP4
|
CO1A2_MYLDA
|
Alpha-2 type I collagen
|
Mylodon
|
SGGFDFSFLPQPPQEKAHDGGRYYLGPGPMGLMGPRGPPGASGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGSRGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNTGPSGPAGPRGEQGLPGVSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGASGATGARGLVGEPGPAGSKGESGGKGEPGSAGPQGPPGSSGEEGKRGPSGESGSTGPTGPPGLRGGPGSRGLPGADGRAGVIGPAGARGASGPAGVRGPSGDTGRPGEPGLMGARGLPGSPGNVGPAGKEGPAGLPGIDGRPGPIGPAGARGEAGNIGFPGPKGPAGDPGKAGEKGHAGLAGNRGAPGPDGNNGAQGPPGLQGVQGGKGEQGPAGPPGFQGLPGPAGTTGEAGKPGERGIPGEFGLPGPAGPRGERGSGAVGPSGAIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPAGSGGLPGERGAAGIPGGKGEKGETGLRGEVGTTGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGIVGPTGPVGSAGPAGPNGPAGPAGSRGDGGPPGVTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGLRGPRGDQGPVGRTGETGAGGPPGFTGEKGPSGEPGTAGPPGTAGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIGPPGARGPSGGVGPGVNGAPGEAGRDGNPGSDGPPGRDGLPGHKGERGYAGNGPVGAAGAPGPHGAVGPAGKHGNRGEPGPVGSAGPVGALGPRGPSGPQGIRGDKGEAGDKGPRGLPGLKGHNGLQGLPGLAGQHGDQGSPGPVGPAGPRGPAGPSGPPGKDGRTGHPGAVGPAGIRGSQGSQGPSGPPGPPGPPGPPGASGGGYDFGYEGDFYRA
|
Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
C0HJP4
|
O26666
|
AROD_METTH
|
Type I dehydroquinase
|
Methanothermobacter
|
MNTKICVPVFEKTAPEVTESAGRAIDAGADILEIRIDGLQNPGEVNIRELIEDIGFPVIATNRSPVEGGHFSGSEDERIKLLMAAAEVADFVDIELSSAREDIERVTGSARRSIVSYHNFRETPSLEALLRIVRMAKEMGDIAKVAVMPENLADTLVVLQLLTFEEDTVAISMGELGKYTRVAAALFGSPITFASMGRGTAPGQMDVDVTRKMIGELMPED
|
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
|
O26666
|
Q9LH79
|
SWET2_ARATH
|
Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 2
|
Arabidopsis
|
MDVFAFNASLSMCKDVAGIAGNIFAFGLFVSPMPTFRRIMRNKSTEQFSGLPYIYALLNCLICLWYGTPFISHSNAMLMTVNSVGATFQLCYIILFIMHTDKKNKMKMLGLLFVVFAVVGVIVAGSLQIPDQLTRWYFVGFLSCGSLVSMFASPLFVINLVIRTKSVEFMPFYLSLSTFLMSASFLLYGLFNSDAFVYTPNGIGTILGIVQLALYCYYHRNSIEEETKEPLIVSYV
|
Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
|
Q9LH79
|
P37397
|
CNN3_RAT
|
Calponin, non-muscle isoform
|
Rattus
|
MTHFNKGPSYGLSAEVKNKIASKYDQQAEEDLRNWIEEVTGMGIGTNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVALAGLAKTKGFHTTIDIGVKYAEKQTRRFDEGKLKAGQSVIGLQMGTNKCASQAGMTAYGTRRHLYDPKMQTDKPFDQTTISLQMGTNKGASQAGMSAPGTRRDIYDQKLTLQPVDNSTISLQMGTNKVASQKGMSVYGLGRQVYDPKYCAAPTEPVIHNGSQGTGTNGSEISDSDYQAEYPDEYHGEYPDEYPREYQYGDDQGIDY
|
Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
|
P37397
|
Q12326
|
PMG3_YEAST
|
Phosphoglyceromutase 3
|
Saccharomyces
|
MTVTDTFKLFILRHGQSELNSENIFCGWIDAQLTEKGKSQARHSAKLIKQFCDSNNISLPQIGYTSRLIRTQQTMDVILEELGLKHTNYVITTNTNIKEELQDTRFEGSMPVLQTWRLNERHYGAWQGQRKPDILKEYGKEKYMYIRRDYNGKPPKVNLNLEMVQEENDQGSSTGYDFKEPNRHLKYGPEEKANERLPESESLCEVVVRLKPFLNNVVLSTANKISQESCVIVGHGSSVRSLLKVLEGISDEDIKDVDIPNGIPLVIELDRDNYSFVRKFYLDPESAKVNAQMVRDEGFEKNP
|
Could be non-functional.
|
Q12326
|
Q1GMQ8
|
PSD_RUEST
|
Phosphatidylserine decarboxylase beta chain
|
unclassified Ruegeria
|
MNMIGTFIKPMHPEGRKFVAIFAAVTFGLFLLTPILGWIGVGLTVWCYYFFRDPERVTPARPGLVISPADGVVSLIEPAVPPAELGLPDVPLTRVSVFMSVFNCHVNRAPVAGEVTAVAYRPGKFFNASLDKASADNERNSLAIRMEDGRDLAVVQIAGLVARRIVCFVKPGAQLGRGERFGLIRFGSRLDVYLPEGVSPQVEIGQTMIAGETVIAELGTGVHTDQNKGELHG
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
Q1GMQ8
|
Q1MIH8
|
PLSY1_RHIL3
|
Lysophosphatidic acid synthase 1
|
Rhizobium
|
MLSNLMSWQITLPIALAAAIIGYLFGSIPFGLILTRAAGLGDVRSIGSGNIGATNVLRTGNRTLAAATLLLDALKASAAAWVVSYFLGEEAAIIAGFFAFIGHLFPVWIGFKGGKGVATYIGTLLGVAPIMVVLFAAVWLAVAFTTRYSSLSALVAMLVIPVALWILGNEKVAAVMAIMTLISYWKHKANISRLMGGTESKIGAKG
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
Q1MIH8
|
A9ML30
|
ENTH_SALAR
|
Enterobactin synthase component H
|
Salmonella
|
MMIWKRDLTLDELNATSQNTLVAHLGIVYTRLGDEVLEAEMPVDIRTHQPFGLLHGGASAALAETLGSMAGYLMTRDGQCVVGTELNATHHRAVSQGKVRGVCQPLHLGRQNQSWEITLFDEQGRRCCTCRLGTAVMG
|
Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules.
|
A9ML30
|
Q3ZWC1
|
TGT_DEHMC
|
tRNA-guanine transglycosylase
|
Dehalococcoides
|
MDKSFILNKTSSRSLARRGQLFTAHGKVETPVFCPVGSQAAVKTLTPEDLKSVNINMILSNTYHLYLRPGIPIIKEMGGLHKFMNWDEVILTDSGGYQIFSLANLRKLDEGGVSFRSHIDGSTRYITPEDAVSFQQDLGSDIAMVLDECPHSEASENEVLAAMERTHQWAKRCLAAHTLKIQHLFAIVQGGLSPELRRQSAEYLASLDFPGYALGGLSLGEPKDITFETVRHTLRFLPENKPRYLMGVGAPEDLLEGVSCGVDIFDCVLPTRVARNGAFFSRLGRLNIRNAAFATQKGPIDPECNCYTCRNYSAAYLHHLFRCEEILAYRLATIHNIAFLSNLMQEIRTSIEKDCFEEFKADFLSRYQPTNEAIRIEQKQKWLFGRNGEPPS
|
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).
|
Q3ZWC1
|
P30608
|
CP52F_CANTR
|
CYPLIIA6
|
Candida
|
MATQEIIDSALPYLTKWYTVITLAALVFLISSNIKNYVKAKKLKCRDPPYFKGAGWTGISPLIEIIKVKGNGRLARFWPIKTFDDYPNHTFYMSIIGALKIVLTVIQENIKAVLATQFTDFSLGTRHAHFYPLLGDGIFTLDGEGWKHSRAMLRPQFARDQIGHVKALEPHIQILAKQIKLNKGKTFDIQELFFRFTVDTATEFLFGESVHSLYDEKLGIPTPNEIPGRDNFATAFNTSQHYLATRTYSQTFYFLTNPKEFRDCNAKVHYLAKYFVNKALNFTPEEIEEKSKSGYVFLYELVKQTRDPKVLQDQLLNIMVAGRDTTAGLLSFAMFELARHPEIWSKLREEIEVNFGVGEESRVEEITFESLKRCEYLKAILNETLRMYPSVPVNSRTATRDTTLPRGGGPNGTDPIFIPKGSTVAYIVYKTHRLEEYYGKDADDFRPERWFEPSTKKLGWAYVPFNGGPRICLGQQFALTEASYVITRLVQMFETVSSPPDVEYPPPKCIHLTMSHDDGVFVKM
|
Together with an NADPH cytochrome P450 the enzyme system catalyzes the terminal hydroxylation as the first step in the assimilation of alkanes and fatty acids. Preferentially hydroxylates hexadecane.
|
P30608
|
Q87T31
|
TPIS_VIBPA
|
Triose-phosphate isomerase
|
Vibrio
|
MRRPVVMGNWKLNGSKAMVTELLTGLNAELEGVEGVDVAVAPPALYIDLAERLIAEGGNKIILGAQNTDLNNSGAFTGDMSPEMLKDFGATHIIIGHSERREYHNESDEFIAKKFNFLKENGLTPVFCIGESEAQNEAGETEAVCARQINAVIDTYGVEALNGAIIAYEPIWAIGTGKAATAEDAQRIHASIRALIAAKDEAVAAQVIIQYGGSVKPENAEAYFSQPDIDGALVGGASLDAKSFAAIAKAAAAAKA
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q87T31
|
Q88SB0
|
MURQ2_LACPL
|
N-acetylmuramic acid 6-phosphate lyase 2
|
Lactiplantibacillus
|
MNLEKLTTETRNQKTMALDMLSVKEMLELMNQEDQRVPVAVSKELPQIECAVDKIVANFKAGGRLIYMGAGTSGRLGVLDAAECVPTFGTSPEMVQGLIAGGMSAMTVAVEGAEDSIELGQQDLVDLHLTSHDTVVGVAASGRTPYVIGGLDYACEVGATTVSIACNADASISQHAQIPIEVEVGPEILTGSTRLKSGTAQKLVLNMLSTASMVGIGKVYKNLMVDVKPTNEKLVERAKRIIVQATDCSDETAVKVFMTADQNVKLAIVMVLTNMSKAEASVRLDHANGFVRQAVN
|
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
|
Q88SB0
|
B8HVS0
|
RS12_CYAP4
|
30S ribosomal protein S12
|
unclassified Cyanothece
|
MPTIQQLIRSERQELKKKTKSPALKSCPQRRGVCTRVYTTTPKKPNSALRKVARVRLTSGFEVTAYIPGIGHNLQEHSVVMIRGGRVKDLPGVRYHIIRGTLDTAGVKDRKQGRSKYGAKRPKPGAASTASTGKKR
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
B8HVS0
|
Q7VJ79
|
RL1_HELHP
|
50S ribosomal protein L1
|
Helicobacter
|
MGKKIAKRLQTLQAKVEPQKVYSIQSGVSAVKSLASAKFDETVEVALRLGVDPRHADQMIRGAVVLPHGTGKKVRVAVFAKGIKADEAKNAGADVVGADDLAEEIKNGNINFDMVIATPDMMALVGKVGRILGPKGLMPNPKTGTVTIDVAKAVANAKSGQVNFRVDKKGIIHAPIGKASFNEEKILDNMLELVRAINRLKPTSAKGKYIRSSSLSLTMSPAIKLDSQELMDMK
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q7VJ79
|
O83452
|
IXTPA_TREPA
|
Nucleoside-triphosphate pyrophosphatase
|
Treponema
|
MRAVDFLRRATVCWYMRIYLASNNAHKHAEFSSLFPMHTILLPKDEGIDFFSPEDGSTFFANARQKADALYDVVHAPVLADDSGLCVDALDGDPGVHSARFGAQHGVHTDTARMQLLLERMHGRQDRACSFVCVAVLKLGSVPLCVGRGVCRGVLTTEMSGVEGFGYDPIFLLPHLGRTFAQLSIEEKNRVSHRALAALRLAQVLAMMQLPRALRYELKLLRGARRMTRGGVLRPGAPCAQRKGQTAQTARRHKFYARARRCARRIHRA
|
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
O83452
|
O70240
|
AXIN2_RAT
|
Conductin
|
Rattus
|
MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGIPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHQQCHALLPTGGKLPPEAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHSKPPEPLPGEQFCGSRGGTLPKRNTKGTEPGLALPAREGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSTQSIRKSYPLESARAPPGERVSRHHLLGASGHPRSAARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHPATGQAGPTSFSNPSLASEDHKEPKRLASVHALQASELIVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
|
Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
|
O70240
|
Q8XHQ7
|
THYX_CLOPE
|
Thymidylate synthase ThyX
|
Clostridium
|
MLKVKLLQYTPEPEKTIAAAAKLCYSPVGVDDILENLTDEGAEKFLNMLMSYGHMSPIEHVSFTFAVEGVSRSLTHQLVRHRIASYSQQSQRYVKLDQFEYIVPPAIENDEVAKKLFIDQMQGAQKAYDEIVERLKDKYISEGIGEKPAEKKAIEDARYVFPNACETKIVFTMNARSLMNFFHHRCCDRAQWEIRTMAEKMVNEVKKVAPILFKNAGPSCVAGPCPEGKMCCGKLKEMRTLYLGK
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
|
Q8XHQ7
|
Q62JC2
|
GLND_BURMA
|
[Protein-PII]-UMP uridylyl-removing enzyme
|
pseudomallei group
|
MSASVAEPPPALSRKAEFKAAKAELLARFKSANHVTPLMHALSRATDDALRSLWQECGLPATLALVAVGGFGRGELSPHSDVDILVLLPDAHASELDERIERFIGMAWDLGLEIGSSVRTVDQCIEEASHDVTVQTSLLEARRIVGSTALFERFMLRYREALDARAFFQAKVLEMRQRHAKFQNTPYSLEPNVKESPGGLRDLQTILWIARAAGFGSSWRELDTRGLITDREARELRRNEGFLKTLRARLHVIAGRRQDILVFDLQTQAAESFGYQPTSAKRASEQLMRRYYWAAKAVTQLATILIQNIEAQLFPATSGVTRVLSPGRFVEKQGMLEIAADDVFERHPDAILEAFLLYEATRGVKGLSARTLRALYNSRDVMNNAWRRDPRNRHTFMQILQQPEGITHAFRLMNQTSVLGRYLLNFRRIVGQMQHDLYHVYTVDQHILMVLRNIRRFAVAEHAHEYPFCSQLIVNFERPWVLYVAALFHDIAKGRGGDHSALGMADARRFCREHGIEGDDAALVVWLVQHHLTMSQVAQKQDTSDPVVIKRFAELVGSERRLTALYLLTVADIRGTSPKVWNTWKGKLLEDLYRATLAVLGGAQPDAHSELKTRQEEALALLRLETVPPDAHRALWDQLDVGYFLRHDAADIAWQTRVLYRHVAADTAIVRARPSPVGDALQVLVYVKDRSDLFAGICAYFDRNGLSVLDARVNTTRHGYALDNFIVTQTEHDVQYRDIANLVEQQLAARLAESAPLPEPSKGRLSRLSRTFPITPRVDLRADERGQYYILSVSANDRPGLLYSIARVLAEHRVGVHAARINTLGERVEDVFMLDGTGLSDNRLQIQVETELLRAIAV
|
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
|
Q62JC2
|
Q7YJV3
|
RK20_CALFG
|
50S ribosomal protein L20, chloroplastic
|
Calycanthus
|
MTRIRRGYIARRRRTKIRLFASTFRGAHSRLTRTITQQKMRALVSTQRDRGRRKRDFRRLWITRINAVTRENRVSYSYSRLIHDLYKKRLLLNRKILAQIAISNRNCLDTISNEILK
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
Q7YJV3
|
A1VN50
|
LPXD_POLNA
|
UDP-3-O-acylglucosamine N-acyltransferase
|
Polaromonas
|
MTLRLADMTELLADKVQAELLGNSELLIERLSTLEAAGPNDLAFLSHPKYLGQLAQSAAGCVIVAPSAREAALKRGPCIVVDDPYYYFALVTQLWKRQHFPGAAPAIHASACIDPAAIISPHVSIGAFACIAAGAVIGEGARIAEHCVIGANAIVGANSRLSARVTVADDCRIGERCIIHPGAVIGADGFGFAPHDGQWVKIEQLGAVRIGNDVEIGANTCIDRGALQDTVIEDGVKLDNLVQIAHNVRVGRHSAMAGCAGVAGSATIGAHCTVGGGAIVLGHLRLADGVHVSAASIVTRSLLKPGHYTGLFPIDDNAAWEKNAATLKQLHALRERLKQTEKSLLQLQGSLEEKP
|
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
A1VN50
|
P19802
|
FMRF_LYMST
|
EFLRI-amide
|
Lymnaea
|
MKTWSHVALLACLSIKWLTCVMADSIYCDDPDMCSMTKRFLRFGRALDTTDPFIRLRRQFYRIGRGGYQPYQDKRFLRFGRSEQPDVDDYLRDVVLQSEEPLYRKRRSTEAGGQSEEMTHRTARSAPEPAAENREIMKRETGAEDLDEEKRFMRFGRGDEEAEKRFMRFGKSFMRFGRDMSDVDKRFMRFGKRFMRFGREPGTDKRFMRFGREPGADKRFMRFGKSFDGEEENDDDLYYNESDADSNDDVDKRFMRFGKSAEEKRFMRFGKSEDASRDKKEFLRIGKRESRSAEVENNIQIAAKQS
|
FMRFamide induces contractions in visceral and somatic musculature as well as in the heart. May play a role as cotransmitters or modulators in a number of significant neuronal systems.
|
P19802
|
A5UFG0
|
PXPA_HAEIG
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Haemophilus
|
MKKIDLNADIAEGFPFDESLLQLLSSANIACGLHAGGAKEMQSAVKFAKENKVRIGAHPSFPDRENFGRTAMALSSQELIAHLRYQLGALKAICDGEGAVISYVKPHGALYNQAAKDEKIARVIAQTVYQFDPHLKLMGLAGSLMLCIAEEEKLQTISEVFADRHYMPDGSLVPRSQPNAMVESDKEAIQQVLQMVTKGQVNAIDGSLVPVKAESICLHGDNQHSLQFAKRIVEELEKNHIKITA
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
A5UFG0
|
A4SI48
|
RSMH_AERS4
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Aeromonas
|
MTQAAEHITVLLHEAVEGLAIKPDGIYVDGTFGRGGHSRLILQHLGPNGRLIAIDRDPQAIAEAAKIQDPRFEIVHGPFSGIVSYLDERGLLGKVDGFLLDLGVSSPQLDDAERGFSFMKDGPLDMRMDPTSGQSAAQWLARADVDDIAWVLKTFGEERFAKKIARAIVHDRVTEPYVRTRQLAEMIARVNPSKEKGKHAATRSFQAIRIYINSELDEIETALNGALQALAPEGRLSVISFHSLEDRLVKHFIRKHEKGPEVPRGIPLTEAQLAGGRKLKSVGKALKPSEHEVTENSRSRSSVLRVAQRLAE
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A4SI48
|
A8ZUN0
|
PDXA_DESOH
|
4-(phosphohydroxy)-L-threonine dehydrogenase
|
Desulfosudis
|
MNPRPLIGITMGDPVGIGPEIILTALAGTSVYEKCRPLVIGDPGVLGQAMAVAGYAPVIHMTDTPETGVYRPGTISMFSPAPPLSPVTWGEPTPETGGAMEAWITTAVDMAMAGAISAMVTCPINKEALKMAGSAFAGHTEMLAMRTGTNRYAMMLAGNRLRVVLVTIHTALQNVPGLLSVDAIADTILLTVESLKQRFGMNAPRVAVAGLNPHAGEGGLFGDEEARLITPAIEAARRKTEAAITGPWPPDTVFVKAAAGDFDAVVCMYHDQGLIPFKLLHFEDGVNTTLGLPIIRTSVDHGTAYDIAGTGRADCRSLTAAIDMAIDQAACLGKRPAA
|
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
|
A8ZUN0
|
P20855
|
HBB_CTEGU
|
Hemoglobin beta chain
|
Ctenodactylus
|
VHLSAEEKAAVTGLWGKVNVEEVGGEALGRLLVVYPWTQRFFESFGDLSSAAAVMGNPKVKAHGKKVLTSFSEGLSHLDNLKGTFAKLSELHCDKLHVDPENFRLLGNMIVITLAHHYGPEFGPQTQAAFQKVVAGVANALAHKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P20855
|
Q9NFS4
|
ANXE1_GIAIN
|
Annexin XXI
|
Giardia
|
MANKNYQMSTGVTAVVQKVVEACQDESKRLDLIEIARSYPPNQLRNMQRTFQAITGTFLDAFLKKHLSKDFESLVLMLYKPRAQLLCELIRGATKGAGTDEKCLVDVLLTIETHEVREIRQLYYQLYNDSLGDVVRKDCGDKYMWAKLINAVATGDRIPRDTHELEEDLVLVRKAIETKGVKKDEVSTWIRIFATYTRADFRQLHKMYSAKYNGDSLRAGVEDEFQGLDEYAFKLAHDFLYDPCCAAAFSMNVAFAGSGSDSNRLNRITAMHFRECKGCKYYYKKVYGQAFDERCATELKGVYGDAIKLLWEPVTVPLLSMDDYQGSEQHRPMTLEL
|
May function as a calcium-regulated structural element linking phospholipid bilayer and underlying axoneme.
|
Q9NFS4
|
P49572
|
TRPC_ARATH
|
Indole-3-glycerol phosphate synthase, chloroplastic
|
Arabidopsis
|
MEGLVPVQRLPIKVASPSLYRCNNSVSIRRSISGFAMDRKINFRAPSQFSIRAQQSDLKESLAVSSSSVEDKGNVLRIKEWEVEMYQEELAISQGIRIRRKPPSKAPLGYSGPFELRLHNNDADSPRNILEEITWYKDVEVSRMKELNPLDVLKKAVEDAPPTRDFVGALRMAHKRTGFPGLIAEVKKASPSRGILKENFDPVEIAQAYEKGGAACLSVLTDQKYFQGGFENLEAIRSAGVKCPLLCKEFVVDPWQIYYARTKGADAVLLIAAVLADLEITFLLKICKKLSLAALVEVHDEREMGRVLGIEGIELVGINNRSLETFEVDISNTKKLLEGEHGRQIRERDMIVVGESGLFTPDDIAYVQAAGVKAVLVGESIVKQNDPEKGIAGLFGRNISHT
|
Indole-3-glycerol phosphate synthase required for tryptophan biosynthesis.
|
P49572
|
P22525
|
YCBB_ECOLI
|
Probable L,D-transpeptidase YcbB
|
Escherichia
|
MLLNMMCGRQLSAISLCLAVTFAPLFNAQADEPEVIPGDSPVAVSEQGEALPQAQATAIMAGIQPLPEGAAEKARTQIESQLPAGYKPVYLNQLQLLYAARDMQPMWENRDAVKAFQQQLAEVAIAGFQPQFNKWVELLTDPGVNGMARDVVLSDAMMGYLHFIANIPVKGTRWLYSSKPYALATPPLSVINQWQLALDKGQLPTFVAGLAPQHPQYAAMHESLLALLCDTKPWPQLTGKATLRPGQWSNDVPALREILQRTGMLDGGPKITLPGDDTPTDAVVSPSAVTVETAETKPMDKQTTSRSKPAPAVRAAYDNELVEAVKRFQAWQGLGADGAIGPATRDWLNVTPAQRAGVLALNIQRLRLLPTELSTGIMVNIPAYSLVYYQNGNQVLDSRVIVGRPDRKTPMMSSALNNVVVNPPWNVPPTLARKDILPKVRNDPGYLESHGYTVMRGWNSREAIDPWQVDWSTITASNLPFRFQQAPGPRNSLGRYKFNMPSSEAIYLHDTPNHNLFKRDTRALSSGCVRVNKASDLANMLLQDAGWNDKRISDALKQGDTRYVNIRQSIPVNLYYLTAFVGADGRTQYRTDIYNYDLPARSSSQIVSKAEQLIR
|
Responsible, at least in part, for generating a meso-diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link.
|
P22525
|
A0A0F6B506
|
SARA_SALT1
|
Salmonella translocated effector E
|
Salmonella
|
MMRFVYIYILVIYGSYLWFSLGGNMFTINSTNRVASTIAPYACVSDVNLEDKATFLDEHTSIHANDSSLQCFVLNDQHVPQNTLATDVEGYNRGLQERISLEYQPLESIVFLLGTPAVLETKESLSLPVSPDALTQKLLSISSNDECKLSGSTSCTTPASHNPPSGYIAQYRHSAEVFPDE
|
A Salmonella strain-specific effector that induces a host STAT3-dependent anti-inflammatory pathway. In bacteria-infected host cells (human) leads to phosphorylation of host STAT3, at least on 'Tyr-705' and interleukin-10 (IL-10, IL10) production; expressing the gene alone in host cells induces STAT3 phosphorylation and IL-10 production. IL-10 production requires STAT3 in infected cells. Contributes to virulence in mouse infection models . Encoded in only a few S.typhimurium serovars, it may be a specific effector for adaptation to bovine hosts (Probable).
|
A0A0F6B506
|
Q46RX3
|
NAPA_CUPPJ
|
Periplasmic nitrate reductase
|
Cupriavidus
|
MKVSRRDFIKQTAIAATASVAGIPLGTEAANFVTDSEVTKLKWSKAPCRFCGTGCGVTVAVRDNKVVATQGDPQCEVNKGLNCVKGYFLSKIMYGQDRLTKPLLRMKNGKYDKNGEFAPVTWDQAFDEMERQFKRVLKEKGPTAVGMFGSGQWTVWEGYAASKLYKAGFRSNNIDPNARHCMASAVQGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRITDRRLSHPKTRVAVLSTFTHRSFDLADIPIIFTPQTDLAMLNYIANYIIQNNKVNKDFVNKHTVFKEGVTEIGYGLRPDHPLQKAAKNAANPGDSKPITFDDFAKFVSKYDADYVSKLSGVPKDKLRQLAELYADPNVKVMSLWTMGFNQHTRGSWVNNMVYNVHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFSHRLPADMVVTNPKHREEAERIWKLPPGTIVEKPGYHAVLQNRMLRDGKLNAYWVQVNNNMQAAANIMEEALPGYRNPANFIVVSDAYPTVTALSADLILPSAMWVEKEGAYGNAERRTQFWHQLVDAPGDARSDLWQLMEFSKRFKVEEVWPAELVAKKPEYKGKTLFDVLYRNGQVDKFPIKEVSTEYHNAEAQAFGFYVQKGLFEEYASFGRGHGHDLAPFDRYHEERGLRWPVVNGKETRWRYREGSDPYVKAGTGFQFYGNPDGKAVIFALPYEPPPESPDKEYPFWLATGRVLEHWHSGSMTRRVPELYRAFPNAVVFMHPEDAKAMGLRRGVEVEVVSRRGRMRSRVETRGRDAPPRGLVFVPWFDASQLINKVTLDATCPISLQTDYKKCAVKIVKV
|
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
|
Q46RX3
|
Q751L8
|
SODC_ASHGO
|
Superoxide dismutase [Cu-Zn]
|
Eremothecium
|
MVKAIAVLKGDAGVSGVVHFEQEADAAVTTISWNITGFEPNTEHGFHIHEFGDVTNGCTSSGSHFNPFKKTHGSPEDENRHVGDMGNVLADANGVAVGSAKDPLIKIFGPTSILGRTVVVHAGKDDLGRGGNEESLKTGNAGPRPACGVIGIAN
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Q751L8
|
Q01383
|
ELYS_HALSO
|
Sperm-lysin
|
Haliotis
|
MKLLVLCIFAMMATLAMSRRWHYVPPKFLNKAFEVALKVQIIAGFDRTLVKWLRTHGGTLSHVQKKALYFVNRRYMQTHWANYMLWINKKTDALGRTPVVGDYTRLGAEIGRRIDMDYFYNFLKGRNMIPKYLPYMEEINRMRSADIPVKYMGK
|
Dissolves the egg vitelline layer nonenzymatically during fertilization. It creates a hole of about 3 mu-m in diameter through which the sperm pass.
|
Q01383
|
A4XYL4
|
RL21_PSEMY
|
50S ribosomal protein L21
|
Pseudomonas
|
MYAVIVTGGKQYKVTEGEFLKIEKLELATGEAVTFDRVLLIGNGDDVKIGAPVVDGAKVVAEVVSQGRHDKVRIIKFRRRKHHMKRQGHRQWFTEIKITGIQA
|
This protein binds to 23S rRNA in the presence of protein L20.
|
A4XYL4
|
Q1PG55
|
CYB_EPOWA
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Epomophorus
|
MTNIRKSHPLLKIINDSLIDLPAPSNISSWWNFGSLLGICLGIQILTGLFLAMHYTSDTATAFQSVTHICRDVNYGWILRYLHANGASMFFICLFLHVGRGLYYGSYIFMETWNVGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTSLVEWIWGGFSVDKATLTRFFAFHFLLPFIIAALVMVHLLFLHETGSNNPTGIPSDMDMIPFHPYYTIKDMLGALAMILALLALVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILILMPLLHTSKQRSMMFRPLSQCLFWLLVADLLTLTWIGGQPVEHPFIIIGQLASILYFSLILILMPFVSIMENHLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q1PG55
|
A2CI34
|
DUSTY_PIMPR
|
Receptor-interacting serine/threonine-protein kinase 5
|
Pimephales
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MENPQKAGPLLRDLTRAFSHYNKHNLLLKKNLKETIAFFREIRQNHSNTCSTSGPELDSGQLRCISFPRHDEDHLQKVVGCAPYILILGQDCSARYQLLNCMLGERLLPLGSDAGGACGVEGGACRRRKLCFTHGRQTRLSLALPGQYELVHQLAAHCGRWDTVPREDLEIQECEDPAQRLAELEITLHHALLQEAKIMVLPCRNVQPVEEALEDCRRGILPIILYAVSKATLSADQLSELQKVRETLPYPVCFVRIPTEPAPDPPGQRSALFAQLVSQELIGGAAGNCACGAPAQTPGKMQGILGEDLERLHRVLVPFARQVLQSQQVEATTLLNAVHCRCLDLFINQAFDMQRDLQITPRRLEYTREKEGELYSSLMAIANRKQEEMKEMIVETLESMKEQLLEDAANLEFTDIIMTSNSEPMSSKDIKVCISQIQDLIVIRLNQAVANKLTSSVDYLRESFVGTLERCLCSLEKSTGEPCAHNVTSNHLKQILNAAYHVEVTFHSGSSVTRLFWEQIKQIIHRISWVNPPSVTSEWKRKVAQDAIESLSAAKLAKSICSQFRTRLNSSHEAFASSLRQLEEGHTGRLERTEDLWLRVRKDHAPRLARLSLESRSLRDILLHGKPKLGRELGRGQYGVVYLCDNWAGRHPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERLVNLHGSVIDHSYGGGSSIAVLLIMERLHRDLYTGLKAGLVLKERLQIALDVVEGIRFLHGQGLLHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYLCTGSVKLPEAFERCSSKDQLWTNVKKGSRPERLASFDEECWQLMEACWNGDPSQRPLLGIVQPSLQSIMDRLCNDSDQKSGNLEDSN
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May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development.
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A2CI34
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Q8Y789
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MUTS_LISMO
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DNA mismatch repair protein MutS
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Listeria
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MTEYTPMIKQYLEIKDKYQDAFLFFRLGDFYEMFFEDALNASQILEITLTGREGGTKEKIPMCGVPYHSASGYIDTLIEKGYKVAICEQVEDPKTTKGMVKREVVQLISPGTVMDERGLKAKENNYIASLYCYEGKEYGFAYSDLSTGELKSTVIEASEDRLINELTTLSTRELIVSSSEKEVLSDVMKEQLGLTFSVHEEDTIPAENEKLVTRHMSLSEKRAIGKLLHYLKETQKRDLGHLQQAVHYETSNYMKMDYYSKRNLELAESIRGKGRQGTLLWLLDNTQTAMGGRMLKQWIDRPLIDRKKIIERQNDVSELMAHFFERLELVENLKNVYDLERLAGRVAYGNVNARDLIQLRNSLYQIPRIRATLLSMSSESLTELAEQLDPCEELTEKLEEAIMDSAPISIREGGIIKDGYNSQLDTYRDASRNGKTWIAELERKERELTGIKTLKVGFNRVFGYYIEVTRANTHLLPEGRYERKQTLTNAERYITPELKEKEKLILDAEEKSMELEYQLFSEVREMVKDYIERLQKLAKSVSEIDCLQSFADISEKNHFIRPTLSEDGSLHVKQGRHPVVEKVMGAQSYVANDCDLDENREILLITGPNMSGKSTYMRQVALTAICAQVGCFVPAEEAILPIFDQIFTRIGAADDLIAGQSTFMVEMLEARNAIVHATKDSLILFDEIGRGTATYDGMALAQAIIEYIHENVHAKTLFSTHYHELTDLEKELRGLQNIHVSAVEENGKVVFLHKIKEGPADKSYGIHVAELAELPKSLIERASRILEQLENDDKKIIIASVKQPEEVHEEVQLSMFPLEPEKKASSKETKLLKEIASMNIMQMTPMDAMNKLYELQSKIH
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This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
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Q8Y789
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B0RD39
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ACPS_CLAMS
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4'-phosphopantetheinyl transferase AcpS
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Clavibacter
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MIRGIGVDVVDVARFARSAERTPGLVPRLFAPAERSLPTRSLAARFAAKEALIKALGGPGGISWQDMEVVRDAHGDPSFQVGGAVARVAAARGVTRIHLSMSHDAGLATAFVVTEGEGA
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Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
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B0RD39
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Q92BI2
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RUVB_LISIN
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Holliday junction ATP-dependent DNA helicase RuvB
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Listeria
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MDERIISSETVDAEEVSFETSLRPQTLSQYIGQDKVKNNLTVFIEAATLRNEALDHVLLYGPPGLGKTTLAMVIASEMGSEIKTTSGPAIERPGDLATILTSLEPGDVLFIDEIHRLSRAIEEILYPAMEDYCLDIVIGTGPTARSVRLDLPPFTLIGATTRAGLLSAPLRDRFGVIDHLEFYTEEQLTEIVLRTSGILDTKIDDLGAREIARRSRGTPRIANRLLKRVRDFAQVRGNGTVTEKLAKEALTLLQVDPRGLDTIDQKLLHTIIQSFRGGPVGLDTIAASIGEERETIEDMQEPYLLQIGFLQRTPRGRIATETAYNHLGISYEKEV
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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.
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Q92BI2
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Q83FY2
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RNC_TROWT
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Ribonuclease III
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Tropheryma
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MDGVDELLLRKFNLTLPPGLLRTAFVHKSFSFENGACQNNERLEFLGDAVLGLVVSHYLFETCPEYTEGQLSAARSYIVSGTSIAQIAKELNLGQFMLLGKGEKLAGGMDKTSLLADLLESLIGAVMVDQGFESARDFVLALVGEKLRQVGEFSVDDPKTKLQKLTRTQLVYEVVTEGPPHSRTFKASVIVNEKRFFGQGSSKKQAQVAAAMSALASLENKSS
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Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
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Q83FY2
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Q21XT4
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COXX_ALBFT
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Heme O synthase
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Rhodoferax
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MSVHVLSVEVSVIKQFYALTKPRVIQLIVFCALIGMVLAVPGLPTWAELQLALLACLGIWLVAGAAAAFNCVVEKSIDAKMKRTAWRPTARGELADWQTLLFSAVLCAAGSILLYFWVNPLTMWLTFATFIGYAVVYTVILKPLTPQNIVIGGASGAMPPVLGWAAMAGDVGPEALILFLIIFLWTPPHFWALALYRVEDYRKSGLPMLPVTHGNEFTRLMVLLYTFILFAACLMPYVYGMSSWLYLIAAVVLNLGFCLYAFYLWRDYSDLLARKTFRFSLIHLSLLFAALLLDHYLL
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Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
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Q21XT4
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Q8GXM7
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ATHBX_ARATH
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Homeodomain transcription factor ATHB-X
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Arabidopsis
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MALSPNSSSLDLTISIPSFSPSPSLGDHHGMRDFDINQTPKTEEDREWMIGATPHVNEDDSNSGGRRRKKLRLTKEQSHLLEESFIQNHTLTPKQKKDLATFLKLSQRQVEVWFQNRRARSKLKHTEMECEYLKRWFGSLKEQNRRLQIEVEELRALKPSSTSALTMCPRCERVTDAVDNDSNAVQEGAVLSSRSRMTISSSSSLC
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Probable transcription factor.
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Q8GXM7
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Q089S6
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MURI_SHEFN
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Glutamate racemase
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Shewanella
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MSGPILVFDSGIGGLSVMNEIRKQLPLHDYCYLFDNARLPYGNLSEQELITGCVALITHHARRLNASIVVVACNTASTLVLPLLRQQLTIPIVGVVPAIKPAAMLSKKKHIGLLATPGTVKRDYTQALINQFAGNCKVELFGTSDLVLLAEQYVAQQQIDMDKLNEILAPIAASNIDVLVLGCTHFPMIATEISHYLGEGVTLLDSGEAVAKRVRFLLSKESNSNKQLQACYTKDIGQGLKAALVDYGFSDFSLVTITD
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Provides the (R)-glutamate required for cell wall biosynthesis.
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Q089S6
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P05682
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REPA_AGRRH
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Putative replication protein A
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Agrobacterium
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MAKSVLKAAPVVVGLTALMERHADALSSQLQAHHLKVFPPHSEKGIRTFGPSEASKLLGVGESYLRQTASEMPELNVSMSPGGRRMFSIEDIHVIRKYMDQVGRGNRRYLPHRRGGEQLQVISVMNFKGGSGKTTTAAHLAQYLAMRGYRVLAIDLDPQASLSALFGSQPETDVGPNETLYGAIRYDDEQVAIERVVRGTYIPDLHLIPGNLELMEFEHDTPRALMNRKEGDTLFYGRISQVIEDIADNYDVVVIDCPPQLGYLTLSALTAATSILVTVHPQMLDVMSMNQFLAMTSNLLREIENAGAKFKFNWMRYLITRFEPSDGPQNQMVGYLRSIFGENVLNFPMLKTTAVSDAGLTNQTLFEVERGLFTRSTYDRALEAMNAVNDEIETLIKKAWGRPT
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This protein is coded by a hairy root Ri plasmid. It is possibly involved in regulating the plasmid copy-number.
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P05682
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C4LJJ2
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GATC_CORK4
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Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
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Corynebacterium
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MSSISRDEVAHLARLSRLSLTDDELDEFADQIDGIIEHVQKVSNVDTEGVEPMSHPSDLAGVMREDEVHPTLTAEQALDQAPASQRDRFEVPRILGE
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Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
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C4LJJ2
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G5EFM9
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NEKL3_CAEEL
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Never in mitosis A kinase-like 3
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Caenorhabditis
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MDKISNIYNFDDPPPDKLSLELFIIEKKIGKGQFSEVFRAQCTWVDLHVALKKIQVFEMVDQKARQDCLKEIDLLKQLNHVNVIRYYASFIDNNQLNIVLELAEAGDMSRMIKHFKKGGRLIPEKTIWKYFVQLARALAHMHSKRIMHRDIKPANVFITGNGIVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIQESGYNFKSDLWSTGCLLYEMAALQSPFYGDKMNLYSLCKKIENCEYPPLPADIYSTQLRDLVSRCILPEASKRPETSEVLQVAEHMNNYFSPSGDQSTTPSTQF
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Probable serine/threonine-protein kinase required for the completion of molting.
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G5EFM9
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B7KWJ1
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GLMM_METC4
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Phosphoglucosamine mutase
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Methylorubrum
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MRKHFGTDGIRGRANVVITPELALKVGQAAGVIFQRGDHRHRVVIGKDTRLSGYMIETALVAGFTSVGMDVLLLGPMPTPAVAMLTRSMRADIGVMISASHNPYEDNGIKLFGPDGFKLNDDLELEIESLIDGDMRNRLSASRDLGRAKRIESVHARYIEFAKRTLPRHVTLDGLRVVVDCANGAAYRVAPETLWELGAEVISIGVEPDGFNINHDVGSTAPETLVQKVRELRADVGIALDGDADRVLIVDEKGQKVDGDQLMAAVARSWQEDERLTQPGLVATIMSNLGLERYINSIGLTLARTAVGDRYVLEHMRQHGYNLGGEQSGHIIMSDYATTGDGLVAALQLLSVVKRRNLPVSEVCHCFEPLPQILKNVRFRSGEPLRADSVVTAIAHAKDRLGQSGRLVIRPSGTEPVIRVMAEGDDRDLVAEVVDEVVDAVTRAAA
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Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
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B7KWJ1
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B1JET1
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PCKA_PSEPW
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Phosphoenolpyruvate carboxykinase (ATP)
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Pseudomonas
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MTQANNTVYTDLSVDELVKEALQRGEGVLADTGALVVETGHRTGRSPADRFIVEEPSTQDAIAWGPINRKFPADKFDALWDRVEAFNNAQDHFVSYVHVGAAAEHYLPVKMTTQTAWQNLFGRCLFINPEQFNPAGRDQWQVLNVANFECVPERDGTNSDGCVIINFAAKKVLIAGMRYAGEMKKAMFSVQNFLLPAADVLPMHCAANIGEEGDVTLFFGLSGTGKTTLSADESRYLIGDDEHGWGEGVVFNMEGGCYAKCIDLSEKNEPVIWKAIKHGAVLENVVLDGNKHADYADVSLTQNSRAAYPLEHVAKRAEANLGGEPNAVIFLTCDLTGVLPPVSILNNEQAAYHFLSGYTALVGSTEMGSGGGIKSTFSTCFGAPFFPRPAGEYAELLIKRINAFGSKVYLVNTGWTGGGYGVGKRFSIPTTRGVIAAIQSGALVGTETEHLDIINLDVPKAVPGVETELLNPRNTWADKAAYDEAAKGLAKLFTENFKKFEVSDAIKAAGPQL
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Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
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B1JET1
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P47914
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RL29_HUMAN
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Large ribosomal subunit protein eL29
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Homo
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MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAMSARAEAIKALVKPKEVKPKIPKGVSRKLDRLAYIAHPKLGKRARARIAKGLRLCRPKAKAKAKAKDQTKAQAAAPASVPAQAPKRTQAPTKASE
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Component of the large ribosomal subunit . The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell .
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P47914
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B3H5J1
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GLV10_ARATH
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GLV10p
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Arabidopsis
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MSSIHVASMILLLFLFLHHSDSRHLDNVHITASRFSLVKDQNVVSSSTSKEPVKVSRFVPGPLKHHHRRPPLLFADYPKPSTRPPRHN
|
Signaling peptide (root growth factor) that maintains the postembryonic root stem cell niche . Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells .
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B3H5J1
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B7VIX1
|
HLDE_VIBA3
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D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
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Vibrio
|
MKPILPDYSQSGVLVVGDVMLDRYWYGPTGRISPEAPVPVVKVENNEERPGGAANVAMNIASLGGHAHIVGLTGKDEPAEVLKNTLGALKVKCDFVELDDYPTITKLRVMSRGQQLIRLDFEDKFENTDPELVLSRMEQALPNVRSVILSDYAKGALEHVQSFIQKARAANVPVFIDPKGADFERYRGATLLTPNMAEFELVAGKVKSEDEMIEKGLALIEEFDFEALLVTRSEHGMTLLRKGVEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKPLDEACALANAAAGVVVGKLGTSTLSTIELAEAIHGSQDTDYGVISEAALVEAVKRARAKGEKVVMTNGCFDILHAGHVSYMNHAAELGDRLIVAVNTDESVKRLKGPGRPVNPTDRRMAVLAGLGAVDWVVPFSEDTPQRLISEVLPSILVKGGDYKPEEIAGGAEVIAAGGEVKVLNFEDGCSTTEIIKAIKGGRG
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Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
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B7VIX1
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P46983
|
ATG36_YEAST
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Autophagy-related protein 36
|
Saccharomyces
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MASVNNYQVDCGSRSARIQPRINNGIHDEESLFEVLELSEEEFELDFHRLKSFNDVRVINNPDLSPECTNTAISRDETLESASSAFEVPSDEIAILSISSDSNKNSPPSEQPAPALRNIRSSSNSDRIDEWCLGSHLFNELHQNVPQSSDGVNHGFPVYSFKERELYTSAKLKKLTNAQRIAVQKLSRDLYPILRTCYREKTRRQLLTYHHERIFDDIPSFFPQRDFIFNYYSMPLEFDRLSDVDIDSSSRSRFTDESTGETLNRSPSAASSSLENTSWFGWTLLSRFLDREW
|
Required for autophagic breakdown of peroxisomes, called pexophagy, through linking peroxisomes to the autophagy apparatus. Involved in regulation of the glyoxylate cycle.
|
P46983
|
Q6ZPU9
|
KBP_MOUSE
|
KIF1-binding protein
|
Mus
|
MANAPGPEIREKFQAALALSRVELHKNPEKEPYKSKYGARALLEEVRALLGPAPEDEDEPAADDGPGDQALGAGEPREAEGPGAQRALRLAVVEFHLGVNHIDTEELSAGEEHLVRCLSLLRPYRLSLGCVSLYIQAQNNLGILWSEREEIETARTYLESSEALYSQYMKEIGSPPLDPTEHFLPEEEKLTEQERSKRFEKVYTHNLYYLAQVYQHMEMFEKAAHYCHSTLKRQLEHNAYHPMEWAINAATLSQFYINKLCFMEARHCLSAANVIFGQTGKIPATEDTPEVEGDVPELYHQRKGEIARCWIKYCLTLMQNAQLSMQDNIGELDLDKQSELRALRKKELDEEESVRKRAVQFGTGELCDAISAVEEKVRYLRPLDFEEARELFLLGQHYVCEAKEFFQIDGYVTDHIEVVQDHSALFKVLSFFEADMERRCKMHKRRIAMLEPLTVDLNPQYYLLVSRQIQFEIAHAYYDMMDLKVAIADKLRDPDSHIVKKINSLNKSALKYYQLFLDSLRDPNKVFPEHIGEDVLRPAMLAKFRVARLYGKIITADPKKELENLATSLEHYKFIVDYCETHPEAAQEIEVELELSKEMVSLLPTKMERFRAKMALT
|
Required for neuronal development and differentiation. Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development.
|
Q6ZPU9
|
C3MPR5
|
TRM1_SULIL
|
tRNA(m(2,2)G26)dimethyltransferase
|
Sulfolobus
|
MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSVNATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR
|
Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
|
C3MPR5
|
Subsets and Splits
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