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2.75k
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AlphaFoldDB
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Q16T79
NUBP1_AEDAE
Cytosolic Fe-S cluster assembly factor NUBP1 homolog
Stegomyia
MSAPEVENKPADAPEHCPGTESENAGKASACAGCPNQQICATGPKGPDPSIALVKEKLKEVRNKILVLSGKGGVGKSTVTALLSRAMAQLNPERNYGVLDVDICGPSQPRVLGVLGEQVHQSGSGWSPVYVEDNLSLMSIGFLLGSPDDAIIWRGPKKNGMIRQFLTEVDWGQLDYLVLDTPPGTSDEHLSATTFLKETDGNWGAVLVTTPQEVALLDVRKEITFCKKMGIPVVGVVENMSVFVCPKCTTESDIFPAKTGGAEKMCEEMEVAYLGKLPLDPRLAKCCDEGKDFITEHSKSPTVIALHQIVAKVQDFFD
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Q16T79
Q8UAE8
SSUD_AGRFC
FMNH2-dependent aliphatic sulfonate monooxygenase
Agrobacterium tumefaciens complex
MSKHDKPLDFLWFIPTSGDGSYLGSDDLSRPADPGYFREIAQAADRLGYSGVLIPTGVACEESFILAANLAAYTEKLKFLVAIRPGVASPAYYARLASTLDRVSHGRLLLNIVVGGSAQELAGDGIFLPHDERYDHADEFFQVFNSLIETGKGDLDGKYIKAQGARLGLPPVQEPRPPLYFGGSSDAGIEFSAGITDKYLTWGEPPAQVAEKIVKVRAAAAKNGREVTFGIRLHFIVRETDEEAWADADRLISKLSDETIASAQEVFSKASDSVGQARMQALHNGRRDKLEVSPNLWAGIGLVRSGAGTALVGSPKTVAARLREYQALGIDTVIASGYPHLEEAYRLSELLFPEIGIDGPRNQIRSSFGAKQVFGGGGHGGNVKLVSGS
Catalyzes the desulfonation of aliphatic sulfonates.
Q8UAE8
Q8TYD5
HIS1_METKA
ATP phosphoribosyltransferase
Methanopyrus
MITVAVPNKGRLHEPALKLLERAGIGVEEPLGRRLKARTTDPDIEVMFVRAADIPRLVEEGVAQLGITGYDLIVEAGAEVKELLDLRFGRARLVLAVPEESDVKSPEDLDGGTVATEFPNIARQYFEDVGVDVEIIQVSGATEIMPRIGVADAIVDLCSTGTTLKVNRLRVVDELLETSARLIANPDATDGEVIRRVYLSLKGVLNADGKCLVMMNVPRERLEEFHELLPGVTGPTVSEIYGDEDMVEVYAVVNEEDVSEVVLRAKELGAEGIIVLPIERMIP
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q8TYD5
Q1CU78
ISPDF_HELPH
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Helicobacter
MSLIRVNGEAFKFSLESLEEDPFETKETLEILVKQTSVVLLAAGESRRFSQTIKKQWLRSNHTPLWLSVYESFKEALDFKEIVLVVSELDYIYIQRHYPEIKLIKGGASRQESVRNALKIIDSAYTLTSDVARGLANMETLKSLFLTLQQTSHYCIAPYLPCYDTAIYYNEALDREAIKLIQTPQLSHTKTLQSALNQGDFKDESSAILQAFPNSVSYIEGSKDLHKLTTSDDLKHFAFFFNPAKDTFIGMGFDTHAFIKDKPMVLGGVVLDCEFGLKAHSDGDALLHAVIDAVLGAIKGGDIGEWFPDNDPKYKNASSKELLKIVLDFSQSIGFELFEMGATIFSEIPKITPYKPAILENLSQLLGLEKSQISLKATTMEKMGFIGKQEGLLVQAHVSMRYKQKL
Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Q1CU78
B0U811
BIOB_METS4
Biotin synthase
Methylobacterium
MTTTERSDPAIRHDWTVAQVQAIHDMPLLDLVHRASLVHRAHHDPSDIQRASLLSIKTGGCPEDCGYCSQSAHHKETGVARQRLMPVEAVLREAAAAKAAGATRFCMGAAWRSPKDGPDFDAVLAMVRGVRGLGMEACVTLGMLTPSQAERLAEAGLTAYNHNLDTGPDYYDKIVSTRSYEDRLATLQAVRDAGIGVCCGGIIGMGEGVTDRVAMLQVLANHAPHPESVPINALAAVPGTPLGERPPVDPFEMVRMCATARIVMPRARVRLSAGRRALSREAQVLCFLAGANSIFYGERLLTTANTDADADAQLLRDIGVPVPAISALEAAE
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
B0U811
A1WVN6
IXTPA_HALHL
Nucleoside-triphosphate pyrophosphatase
Halorhodospira
MKIVLATGNAGKLAEMTRMLQGYDAEVVRQGHLGIDSPAETGLTFVENALIKARHCAERSGLPAVADDSGLAVPALGGEPGIYSARYAGSDAGDAANIERLLAELSERGQGDRRGTFHCVMVYLRHAADPAPVIAHGSWTGRIVETPRGHHGFGYDPVFEDPELGQTAAELDAPAKDARSHRGQALRALIQGIAAEVAG
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.
A1WVN6
Q3AUX8
MINE_SYNS9
Cell division topological specificity factor
unclassified Synechococcus
MTVKDFIDKLLGRQTSSASTAKQRLQLVLAHDRSDLNPELLAQMRREILEVVARYVEIDIEEGDVSLETEDRMTALVANLPIRRSIQQSPNGGTL
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Q3AUX8
Q3A3Z3
EX7L_SYNC1
Exodeoxyribonuclease VII large subunit
Syntrophotalea
MNISEGTVSVSRLVYLLKEVVEDNFVQVLVTGEIANFSAPSSGHYYFAVKDDQAQLRGVMFRSSNRLLKFTPENGMQVLCGGRVSLYPQRGELQLVVDRMEPLGVGSWQLAFEKLKTKLDAEGLFEVGRKRRLPSFPRTIGVVTSPTGAAIHDILNVLRRRGAGLHVLLSPVRVQGDGAADEIARAIADFNRHGQADVLIVGRGGGSPEDLWAFNEEVVARAVFASRIPVISAVGHEVDVTISDLVADLRAPTPSAAAELVVQGRQELERHVDHLVMRLSGQMQGRLSLLKERLDGLRRRLRSPVDDLRRQYRDLEQLRKRLFSAMEKTMQRAANRLGLAGSRLHALSPLATLDRGYAIVFSAKTSTIVRDARTLTPGDRVQIRFAKGSVEATVDEVDHGD
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q3A3Z3
A0A0H2ZH12
ODH_PSEAB
Pseudopaline dehydrogenase
Pseudomonas
MNAADESLGNVLLVGLGAVAIQVALDLRRHGAGRLGALNHPGRRSQRIAEALARGACLQLEGQGQHRWLSGNAALDVFHQDPAELRDDWQTLVLCVPADSYLDVVRGLPWERLGGVRTLLLVSAFIGANLLVRSALPAGCQATVLSLSSYYAATKVIDETQPLRALTKAVKRRVYLGSSRPDCPARETWRRVLAGSGVEVVPLATPEAAEGRNVTTYVHSPFFLGEFALARILSEQGPPGFMYKLYPEGPITPGAIGAMRRLWCELSELLRRMGAEPLNLLRFLNDDNYPVHETMLPRAAIDGFAEAGAERQEYLLFVRYAALLVDPFSPADEQGRHFDFSAVPFRRVSRDEDGLWRLPRVPLEDYRKLALIVALAAHFDLAMPQARSLLASYENAVSRFIDCQGASQCHPSLYPIDSRPAADAIYRQWCSTC
Catalyzes the NADH-dependent reductive condensation of alpha-ketoglutarate to the intermediate formed by the adjacently encoded enzyme CntL, namely (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate, leading to the production of pseudopaline. This is the last step in the biosynthesis of the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to Pseudomonas virulence. Can use neither pyruvate nor NADPH in place of alpha-ketoglutarate and NADH, respectively.
A0A0H2ZH12
C4KZ51
MTNX_EXISA
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
unclassified Exiguobacterium
MSTHVICDFDGTITEEDNIIALMRRFAPPEWVELKDSVLNQTLSIREGVGQMFSLLPSNQQERYREFLQSTITLRAGFVEFLQETQSHGFRFDVVSGGMDFFVHPILEGHVAPEHIFCNHVDFSGETARVTWPHACDVHCLNDCGCCKPTIARQIVSPTDTLIVIGDSVTDFEIAKRADVVYARGQLISLCEAEGIRHVPFETFYDISAYMKGVNV
Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
C4KZ51
Q3K0P4
RNZ_STRA1
tRNase Z
Streptococcus
MEIQFLGTGAGQPAKARNVSSLVLKLLDEINEVWMFDCGEGTQRQILETTIKPRKVKKIFITHMHGDHVFGLPGFLSSRAFQANEEQTDLDIYGPVGIKSFVMTGLRTSGSRLPYRIHFHEFDESSLGKIMETDKFTVYAEKLDHTIFCMGYRVVQKDLEGTLDAEALKLAGVPFGPLFGKVKNGENVTLEDGREIIAKDYISEPKKGKVITILGDTRKTDASIRLALGADVLVHESTYGKGDERIAKSHGHSTNMQAADIAKQANAKRLLLNHVSARFMGRDCWQMEEDAKTIFSNTHLVRDLEEVGI
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Q3K0P4
Q9A4C3
NADB_CAUVC
Quinolinate synthase B
Caulobacter
MTQYRITFEGPVILGAGLAGLTAALSATTGAAKTALVLSPTPLASGCSSAWAQGGMAAALSGDDSPALHAADTIAAGAGLCDPQAVDLLTREGPQAVRDLAALGAPFDRKADDGFVLSLEAAHSAARVARVGGDGAGAAIMAAVIAAVRATPGIEVRENARARRLLQDANGRVVGVLADVDGALVEIRSTAVILATGGVGGLYAVTTTPAQVRGEGLGLAALAGAMIADPEFVQFHPTAIDIGRDPAPLATEALRGEGAILRNADGKAFMADYHPAKELAPRDVVARALHAERAAGRGAFLDATAAVGAHFPHEFPAVFEACMSAGIDPRRQMIPVTPAVHYHMGGVATDLDGRASLPGLYAAGECASTGVQGANRLASNSLLEAAVFGARAGRAAAAEGATGGPPVSLEPLPDLPDAALQGLRKAMSRDAGVIRDADGLTRLLGEIETLEAGHGQGPILVAARLIVTAALAREESRGGHCRIDFPATDPVGVRTFVTLDGREPGLRYAAE
Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
Q9A4C3
A5W4E2
TODT_PSEP1
Response regulator protein TodT
Pseudomonas
MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to a 6-bp palindromic DNA structure in the tod promoter region.
A5W4E2
Q970V6
PURL_SULTO
Phosphoribosylformylglycinamidine synthase subunit II
Sulfurisphaera
MKITLSSYEMELVRKKLAREPNEAEWLTIDALWSEHCSYKSSKVFLRSFPSEGEKVLMGIEDWQDAGALDVGDGWAIVLKLESHNHPSAIDPFNGAATGVGGIIRDIISKGAKPIALLDMIRVGNLSNPRNKWLLKNIIAGIGFYGNSIGVPVVGGELDFDDSYNDNPLVDVAGVGIVRKDKIVPSVVKEPGLKIVIVGLTGLDGLGGASFASRKLSGEDEIGAVQIADPFAGKIVLDVTLEIADKVEAIKDLGGGGLVVGVTEMANGLGAIVNLDKVPLRVKDLKPEEILVSETQERMLFAVKEENVNEVCKAFEYYDYPCAVIGEFVKEPYIKFLYGGKEIVSLPSDLLLSPPRFIWEIKKPKLIKSDKKPEVGLEESIRAILSRIISKEWAYSQFDYEVGTSTVLKPGEADSALISLPNGKLLALKGDANPDLCAEDSYECGKSIVAEAYRNLASVGAIGIGVVDHLQFGDPKKPEVYYSFVEAIRGIAEASKFFSTPIVGGKVSFYNENKEGKAIKPTPLIVMAGLIKDKFLRNKVVEDSYITLIGFTRDEMRGSLFGKIFGNYGEVPKARLNEDYLASQLVVNLINDEKIFFAKDINKGGLIASLFSILVKGMGVEIETSSIPSDTDDWIPKLYSENGGRFIVLTNDPEYIIRKSKGIHISVIGKITKDQGIIKIDNKEINVNKEIDNYYNYLYEVMS
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Q970V6
Q6Q870
SIRN_LEPMC
Sirodesmin biosynthesis protein N
Leptosphaeria maculans species complex
MTVETKDLPESNYLLDYDDTEKRRLREQHDLIKAYTGKLILAPLDLTKPNLKILDSGTFDGHWLTEAAKPLTTPLLTGTDISPAAFPNPPPQNTSFHIQSITDPWPASWQNTFDLVHQRLVLAGTTPTGGLDAVRNLAGLAKPGGWVQLIEGKLLAESQRTRFPALHRFHSFIERMLPGFGWNIRAGLMVGGWLGEVGLEEVGEMEVEIPVGRANGDGRLGAMAEKNLRDVMGVWRQASSKLPADSPFKASELEEIFVDWDKEIETIGSLLRFAVVWGRRPALD
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL . 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone . Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide . This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL . The next steps of sirodesmin biosynthesis are not well understood yet but some predictions could be made from intermediate compounds identification . Phomamide is converted into phomalizarine via oxidation, probably by sirT . Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin . Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL .
Q6Q870
A3CQ50
ACCA_STRSV
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Streptococcus
MTKITRIIKEARDQARLTALDFAQGIFENFVELHGDRSFRDDGAVIGGIGTLNGQPVTVVGIQKGRNLQDNLRRNFGQPHPEGYRKTLRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSNLKVPIIAIIIGEGGSGGALALAVADKVWMLENSMYAVLSPEGFASILWKDGSRAMEAAELMKITSHELLQMEVVDKVIPERGFNNHELLAAVKEEIAAELDSLSQLPLEQLLENRYQRFRKY
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
A3CQ50
A8LR11
LEPA_DINSH
Ribosomal back-translocase LepA
Dinoroseobacter
MTELSRIRNFSIVAHIDHGKSTLADRLIQETNTVSARDMKEQLLDAMDIERERGITIKANTVRIDYTADDGQDYVLNLIDTPGHVDFAYEVSRSMRAVEGSLLVVDSTQGVEAQTLANVYQAIDADHEIVPVLNKIDLPASDCDRVAEQIEDVIGIDASGAIRVSAKTGQGIHETLEAIVHHLPAPKGTRDAPLKAMLVDSWYDAYLGVIVLVRIIDGTLRKGERIKMMSNGTVHHVDRIGVFRPAMQPVDELGPGEIGFLTASIKQVRDTRVGDTITHEKKGAETALPGFKPSQPVVFCGLFPVDSAEFEDLRDAIEKLALNDASFSYEMETSAALGFGFRCGFLGLLHLEVIRDRIEREYDIELITTAPSVIYHVYMRDGTMRELHNPADMPDLTHVDHLEEPRIKATILVPDDYLGDVLKLCQDRRGIQMDLTYAGSRAMVVYDLPLNEVVFDFYDRLKSVTKGYASFDYQMIGYRQDNLVKMQVLVNDEPVDALSTMVHRDRAEARGRAMCEKLKDLIPRHMFKIPIQAAIGGKVIARETLSALRKDVTAKCYGGDATRKRKLLDKQKAGKKKMRQFGKVDIPQEAFISALKMDG
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
A8LR11
Q73KE1
NPD_TREDE
Regulatory protein SIR2 homolog
Treponema
MDKEKNDYDKLFSEITKARHLVAFTGAGISTLAGIKDFRGKDGLYKQPNTEKMFDIDVFYRDPSVYYGMAKEFIYGLEEKQPAIVHTVLADLEKRGILKAVITQNIDLLHQKAGSKNVIEVHGSPSVHYCINCSYTETFEETAKTAKTGEVPRCPKCGSPIKPAITFFGEALPQKALMKAETEASKSDFMLVLGTSLLVYPAAALPAYTLRNGGKIAIVNNQPTQFDSYTDLLFEDLEETFEEIDKRLKKV
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Q73KE1
A7ZCN5
RL10_CAMC1
50S ribosomal protein L10
Campylobacter
MTRNEKTEVVAKLESEFKTAEAIVVCDYRGLSVKKLEVLRNSAKEQNVKVQVIKNTLANIALKNSDKVGMELKDTNIYLWSEDQLAVTKVAAKFEESNSDLFKIKTAYIDGEVASVDKVKALSKMPSRDELIAMLLQVWNAPIQNFTIGLNALKEKKEQSA
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
A7ZCN5
Q54RX1
TCTP2_DICDI
Translationally-controlled tumor protein homolog 2
Dictyostelium
MKLYKDLIGNSHDDLLTDRYEIKVGDVTFEVKTKMITKDLNVVVNNNSLGGSISTTVDNNNSITLSTNLEDEFENVEAAGTFQINNLVEQLRLVETSFDKKSYLAYMKLYIKDLINHIKQQPSNSDNEKIEHIQKGIQSFVKTMMDGENFKKYSFFTGSSMDANGLVALMYYKDDDPTTPTFVFIKYGLLQVDV
Involved in calcium binding and microtubule stabilization.
Q54RX1
B7VJ92
RLMM_VIBA3
23S rRNA 2'-O-ribose methyltransferase RlmM
Vibrio
MKHVLLYCRSGFEKECAGEIQDKATQLEVFGFPRLKNNTGFVLFECYQAGEADKLIKEIDFQSLIFARQMLAVAVEIKDLPTDDRISPILEALSEKEGFPRCGDIRIETPDTNEAKELLKFCRKFTVPMRQAMRGKGLMTAKDNAKKPVLHLCFIAPGHCFVGYSYPTNNSQFFMGIPRLKFPSDAPSRSTLKLEEAFHVFIPRDEWDERLAPGMWGVDLGACPGGWTYQLVKRSMFVHCVDNGMMADSLMETGQIKHHMVDGFKFEPDRKNVTWIICDMVEKPARVAHLMGEWIIKGWAKEALFNLKLPMKGRYDEVLQDIENLKQFLIDNKVKFKMQAKHLYHDREEITVHIQSLSNISPY
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
B7VJ92
Q2R114
CADH4_ORYSJ
Putative cinnamyl alcohol dehydrogenase 4
Oryza sativa
MAAECGSGNCDAWAARDPSGILSPYKFNRREVQSEDVSLRITHCGVCYADVIWTRNMFNDSIYPLVPGHEIAGVVTEVGADVKGFKVGDHVGVGVYVNSCQDCENCNSSLENHCSKCVVTYNSVDSDGTVTKGGYSSHILVHQRYCFKIPADYPLSKAAPLLCAGITVYTPMIRHNMNQPGKSLGVIGLGGLGHMAVKFGKAFGLKVTVFSTSESKREEAINLLGADNFVISSDENQMESLKSSLHFIIDTASGDHQFDPYLSLLKVGGVMVLLSFPSEIKVHPENLNLAARSLAGSVTGGTKDIQEMINFCAANNVYPDIEMIKIDYVNEALQRLINRDVRFRFVIDIENSFK
Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Q2R114
A0LIP0
ATP6_SYNFM
F-ATPase subunit 6
Syntrophobacter
MEHPILFLNLLFEKLGLHVVGPEQAKSFGDFLLQPHVTYTWVVMLVLLGLGSMAAKGLEMVPKGAQNFFEVVITGIEDFMISITGEEGRFVFPLIASLGMFILFSNYLGMIPGFFSPTANINTTAACALISVVFTHVIGIKFHGVKYIKHFMGPVWWLTPLIMPIEIIGHIARVLSLSIRLFGNVFGEELVLGILFFLAGFYLAPLPMMFLGLFTGFIQAFIFCLLSMMYFAGAIEHAH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
A0LIP0
Q8DH56
SYA_THEVB
Alanyl-tRNA synthetase
Thermosynechococcus
MTALTGDQIRQKFLDFYAAKGHTILPSASLIPDDPTVLLTIAGMLPFKPIFLGQEAPKVPRATTAQKCLRTNDIENVGRTARHHTFFEMLGNFSFGDYFKGEAIAWAWELMTTVYGLPPERLLVSVFENDDEAYDIWHRQVGLPKERIQRMGEESNFWTAGPTGPCGPCSEIYYDFYPEKGLANVDLDDDGRFIELYNLVFMELNQDDQGHRTPLKAKNIDTGMGLERMAQVLQGVPNNYETDLIFPIIEAAAQRAGIQYQKANASTQTSLKVIGDHTRAVVHLIADGVTASNVGRGYVLRRLIRRIVRHSRLLGINGLVTPDLAQVAIDLAANVYPNVRERQAVILSELQREEEQFLKTLDRGEKLLAEMLSPLKKAKGKKRSQPQLAGRDAFVLFDTYGFPLELTQEIAAEQGIGVDVAEFEACMAEQRQRSQAAHETIDVTVQEGIDSLGDQLHPTQFRGYEELSLTTTVTAILVAGHPATTATAGTEVQVILEATPFYAESGGQIGDRGYLASSDALVHIHDVQKQKELFVHYGKVERGSLKVGDRVSAQIDLSCRRRVQAHHTATHLLQAALKKLIDENISQAGSLVAFDRLRFDFNCPRPLTREELQQIEDQINAWISESHTTHTYIMALSEAKAKGAIAMFGEKYGEQVRVLDIPGVSMELCGGTHVHNTAEIGLFKIISESGVAAGIRRIEAIAGAAVRDYLQQRDSIVRELCDRFKAKPEEILDRISQLQADLKAQQKALEHLKAELALAKTQALLEQAKPVGNSHVLIASLAGVDPQGLKTAAEWLLNKLGSGAVVLATQPAADKVNLLVAASQDVVQRGVHAGQLVAALAQVCGGRGGGRPNFAQAGGSQPAKLAEALELAHSRLKEILES
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q8DH56
Q55749
SUMT_SYNY3
Uroporphyrinogen III methylase
unclassified Synechocystis
MVVRLQNGLMGKVYLVGAGPGDPGLITVKGKTLLENAEAVVYDALVSTAILAMVNPQAELIDAGKRRGRHTKLQSETTQLLAQLAEKHAVVVRLKGGDPFIFGRGGEEMEDLVKAGIEVEVVPGITAGIAAPAYAQIPLTHRAYSSSVTFVTGHESAGKYRPEVNWAAIAKGSETIVIYMGVYSLATILPQLMLAGLGEDTPIALIRWGTCPEQQKLVGTFATILAQIEVENFQAPAIVVIGAVVNYPANLRQQLAPILGGVN
Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of both cobalamin (vitamin B12) and siroheme.
Q55749
Q9DB42
ZN593_MOUSE
Zinc finger protein T86
Mus
MGRSRRTGAHRAHSLARQMKAKKRRPDLDEIHRELRPQGLPRPKPEPDAEPDPDLPGGGLHRCLACARYFIDSANLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVQPQRLGVPTEVSTDIPEMDTST
Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome. Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity.
Q9DB42
Q9ZV53
ATL49_ARATH
RING-type E3 ubiquitin transferase ATL49
Arabidopsis
MNKILPEMKSTQNLISSSPPPPLIPLKSNTSLSNLNSKITPNILLIIIILSIIFFISGLLHILVKFLLTPSRESREDYFDNVTALQGQLQQLFNLHDSGVDQSLIDTLPVFHYKSIVGLKISPFDCPVCLCEFETEDKLRLLPKCSHAFHVECIDTWLLSHSTCPLCRSNLLSGFSSHHNLSSSYLLVLESEQSSRDMVPVLESNSQLGYDVNNDSESTRIRSGRKSCDPDGDMDGLDEKVVPLEVKLGKFRNIDHVGEGSDQKKNSISGNSKNVDGRRCLSMGSYEYIMDQEATLKVHVSTKKLSGKDRVPSHRTVMSECGFDPTVKGIEKSVVERESFSLSKIWLRGKKEKQKGTSARDSDCSFVSSSSLRFPNHRIPPEESLKSENSESLETKTPSFARRTMHWLAGRQNKIVQPSTSNV
May be involved in female gametophyte development.
Q9ZV53
Q2G9E3
RNH_NOVAD
Ribonuclease H
Novosphingobium
MKHVEIFTDGACKGNPGKGGWGALLRMGEHEKEMAGSEKETTNNRMELMAAIRALEALKQPCRVTLHTDSKYVLDGITKWIFGWQKKGWKTADNKPVKNEDLWRALVDAVRPHKVEWVWVKGHDGHPENERVDKLASDAALAA
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q2G9E3
B3DR50
RL31_BIFLD
50S ribosomal protein L31
Bifidobacterium
MQQGIHPDYHPVEVTCSCGNTFVTRTAGKEDHMFVDVCSQCHPFYTGKQKILDTGGRVARFEKRYGKKSK
Binds the 23S rRNA.
B3DR50
P9WIB8
SCMU_MYCTO
*MtCM
Mycobacterium tuberculosis complex
MLTRPREIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYCQALPPA
Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
P9WIB8
Q9H426
RIMS4_HUMAN
Rab3-interacting molecule 4
Homo
MERSQSRLSLSASFEALAIYFPCMNSFDDEDAGDSRRLKGAIQRSTETGLAVEMPSRTLRQASHESIEDSMNSYGSEGNLNYGGVCLASDAQFSDFLGSMGPAQFVGRQTLATTPMGDVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGICIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVARVLLEELDLTTLAVGWYKLFPTSSMVDPATGPLLRQASQLSLESTVGPCGERS
Regulates synaptic membrane exocytosis.
Q9H426
Q5GS21
PLSX_WOLTR
Phosphate-acyl-ACP acyltransferase
unclassified Wolbachia
MLPTVNNNIVIALDAMGGDFAPLSVIQGAGFFLDNLVDPGIKVFFHIYGDQKEISPLLLKYRKVSDNSEFTHYSNNVLANDKPSFALRHRKDSSMKAAIEAVKKGKASGMVSSGNTGALMAISRFILGTLPNVYRPAIVSVCPTKAKSFALLDLGANVDCNVDSLFQFALMGSMFAKIALKVDNPEVALLNIGTEEVKGNDSVRGAFKLLKSAPNINFKGYIEASEFLEGNIDVIVADGFVGNVMLKTAEATASTFIDLIKQEMFNSWATKMLVGILLKSKLNKVLMRFNPKIRSGAMFLGLNGIVIKSHGNSDAVSFAHAIKFAVNSINENLNQKIISEVNQVE
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.
Q5GS21
P93841
ISPE_SOLLC
Ripening-associated protein pTOM41
Solanum subgen. Lycopersicon
LWLPVIFFVVSNPKLILLKRVVFFQSWSNRPHGSSYFNKNIQFRRNSFVIVKASGSRTSKKQVEITYNPEEKFNKLADEVDREAGLSRLTLFSPCKINVFLRITSKRDDGYHDLASLFHVISLGDKIKFSLSPSKSKDRLSTNVAGVPLDERNLIIKALNLYRKKTGTDNYFWIHLDKKVPTGAGLGGGSSNAATTLWAANQFSGCVATEKELQEWSGEIGSDIPFFFSHGAAYCTGRGEVVQDIPSPIPFDIPMVLIKPQQACSTAEVYKRFQLDLSSKVDPLSLLEKISTSGISQDVCVNDLEPPAFEVLPSLKRLKQRVIAAGRGQYDAVFMSGSGSTIVGVGSPDPPQFVYDDEEYKDVFLSEASFITRPANEWYVEPVSGSTIGDQPEFSTSFDMS
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
P93841
Q88VD4
RS20_LACPL
30S ribosomal protein S20
Lactiplantibacillus
MPIIKSAIERVKTNNKANVRNTAQMSAMRTAVKKFEAAKTAGADNVDDLYLAATSAVDKAASKGLIKRNKAARDKSRMAARYAK
Binds directly to 16S ribosomal RNA.
Q88VD4
B1XJJ0
RL15_SYNP2
50S ribosomal protein L15
unclassified Synechococcus
MKLSNLSPKAGSKKRRRRVGRGIAAGQGASCGFGMRGQKSRSGTGTKAGFEGGQMPLYRRVPKLKHFTIVNPKNFTIVNVGQLTDLPANTEVTLESLMAAGIVTTNDGPLKVLGDGELSVALKVTAAAFSNGAKAKIEAAGGSCEA
Binds to the 23S rRNA.
B1XJJ0
Q9SI09
XERIC_ARATH
RING-type E3 ubiquitin transferase XERICO
Arabidopsis
MGLSSLPGPSEGMLCVILVNTALSISIVKGIVRSFLGIVGISLSPSSSSPSSVTVSSENSSTSESFDFRVCQPESYLEEFRNRTPTLRFESLCRCKKQADNECSVCLSKFQGDSEINKLKCGHLFHKTCLEKWIDYWNITCPLCRTPLVVVPEDHQLSSNVW
Function on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation.
Q9SI09
Q9F4F2
CH10_BUCPP
Chaperonin-10
Buchnera
MNIRPLHDRVLVKRQEVELKSAGGIVLTGSAAGKSTRGTVVAVGKGRILDNGETKSLDVKIGDVVIFNEGYGAKTEKIDNEELLILTESDILAIVEE
Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Q9F4F2
A7FI10
PYRF_YERP3
OMP decarboxylase
Yersinia
MTSATKTNNSGSISSPIVVALDYANKDAALAFADQVSPQDCRLKVGKEMFTLYGPELIRDLHQRGFDVFLDLKFHDIPNTTARAVAAAAELGVWMVNVHASGGARMMSAAKEALLPYGAQAPLLIAVTVLTSMDSEDLRDIGITISPAEQAERLAKLTWDCGLDGVVCSAHEAVRLKQVCGEDFSLVTPGIRPQGSEAGDQRRIMTPEQAVAVGVDYMVIGRPITQSPDPEKTLREILASLTKVA
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
A7FI10
O96827
EF1B_DROME
Probable elongation factor 1-beta
Sophophora
MAFGDVTTPQGLKELNAFLADNSYISGYTPSKADLSVFDALGKAPSADNVNVARWYRHIASFEAAERAAWSGTPLPQLAGGKPTVAAAAKPAADDDDDVDLFGSDDEEDEEAERIKQERVAAYAAKKSKKPALIAKSSVLLDVKPWDDETDMKEMENNVRTIEMDGLLWGASKLVPVGYGINKLQIMCVIEDDKVSIDLLQEKIEEFEDFVQSVDIAAFNKI
EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
O96827
A8ESU7
RS19_ALIB4
30S ribosomal protein S19
Aliarcobacter
MARSIKKGPFVDAHLMKKVLSANSANDKKPIKTWSRRSTVLPEMIGITFNVHNGRNFVPVLITENHVGYKLGEFAPTRTFKGHKGSVQRKA
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
A8ESU7
Q87WV4
HIS1_PSESM
ATP phosphoribosyltransferase
Pseudomonas
MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQADVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYTGQGLYEPLDLQIAKCRLMTAGAIGAVEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQELIATISSRLVVNKASMKMQHARIQALIDTLRKAVESRHRC
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q87WV4
B8DDL2
RECU_LISMH
Recombination protein U homolog
Listeria
MAIGYPNGKKYAASQEELPQQKRKAPVTYGKRGMSLEDDLNDTIAYYLTHEIAVIHKKPTPVQIVSVDYPKRSSAKIKEAYFKTPSTTDYNGVYKGKYVDFEAKETQNTTSFPLSNFHDHQMTHMANVLKQDGIVFVIIAFQKLGETHFIPFEKFYPFWERMQSGGRKSVTIAEIQDVSDQIPYGLNPRLDFLQSIDKLYF
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
B8DDL2
Q8N6T0
TO6BL_HUMAN
Type 2 DNA topoisomerase VI subunit B-like
Homo
MEGTAVAVFEILRFLIIHWKCDIDVSKGALLEGQLVISIEGLNSKHQANALHCVTTVASAGSLFGGMVLKKFLKEIQSILPGISAKLTWTSEEGSYSQDMTGVTPFQMIFEVDEKPRTLMTDCLVIKHFLRKIIMVHPKVRFHFSVKVNGILSTEIFGVENEPTLNLGNGIALLVDSQHYVRPNFGTIESHCSRIHPVLGHPVMLFIPEDVAGMDLLGELILTPAAALCPSPKVSSNQLNRISSVSIFLYGPLGLPLILSTWEQPMTTFFKDTSSLVDWKKYHLCMIPNLDLNLDRDLVLPDVSYQVESSEEDQSQTMDPQGQTLLLFLFVDFHSAFPVQQMEIWGVYTLLTTHLNAILVESHSVVQGSIQFTVDKVLEQHHQAAKAQQKLQASLSVAVNSIMSILTGSTRSSFRKMCLQTLQAADTQEFRTKLHKVFREITQHQFLHHCSCEVKQQLTLEKKDSAQGTEDAPDNSSLELLADTSGQAENKRLKRGSPRIEEMRALRSARAPSPSEAAPRRPEATAAPLTPRGREHREAHGRALAPGRASLGSRLEDVLWLQEVSNLSEWLSPSPGP
Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.
Q8N6T0
P60600
HIS5_MYCPA
ImGP synthase subunit HisH
Mycobacterium avium complex (MAC)
MTSKSVVVLDYGSGNLRSAQRALERVGASVQVTADADAAAAADGLVVPGVGAYEACMTGLRKIGGDRIIAERVAAGRPVLGVCVGMQILFARGVEFSVETSGCGQWPGSVTRLQAPVIPHMGWNVVESGPDSVLFRGLDADTRFYFVHSYAAQQWEGSPEAVLTWSRHEGPFLAAVEDGPLSATQFHPEKSGDAGAAVLRNWIERL
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
P60600
P21812
MCPT4_MOUSE
Serosal mast cell protease
Mus
MQALLFLMALLLPSGAGAEEIIGGVESRPHSRPYMAHLEITTERGFTATCGGFLITRQFVMTAAHCSGREITVTLGAHDVSKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLLCAGVAHGIVSYGRGDAKPPAVFTRISSYVPWINRVIKGE
Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing.
P21812
O24822
SYDND_HALVO
Non-discriminating aspartyl-tRNA synthetase
Haloferax
MRNRTYTADAEPGDTVTVAGWVHEVRDLGGIAFLILRDTSGKIQVKFEKDEMDDDLVETGLGVHRESVISVTGEVDEEPRAPTGVEVTPESLDVIAEAEAQLPLDPSGKVDAELSTRLDNRTLDLRKDEVKAIFEIRAEVQRAVRDKFRDLRATEINTPKIVATGTEGGTELFPITYFGQEAFMNQSPQLFKQLMVGSGLERVFEVGPIFRAEEHNTPRHLNEATSIDFESAFIDHTEAMDVCEAVVTAAYEAVEENCQDELEALGLEEEFERRPRVPAAHLRGGHRAHQRTGELDEQLVWGDDLPTEGEKALGEDVGEHYFITDWPSEIKPFYIKDHDDDETLSTGFDMMHPNMELVSGGQREHRFDHLVAGFEQQGLDPDAFEYYTKMFKYGMPPHAGFGLGGERLIMTMLGLENIREAVLFPRDRQRLSP
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
O24822
Q9WYY4
SYP_THEMA
Prolyl-tRNA synthetase
Thermotoga
MRMKDLYAPTLKETPSDVETVSHEYLLRGGFIRKVAAGIYTYLPLGRRVLLKIENIVREEMNRIGAQEILMPILQPAELWKQSGRWDDYGPEMMKLKDRHERDFTLGPTHEEIVTDLVKNELRSYKQLPLTLYQIANKYRDEIRPRFGLLRAREFIMKDAYSFHASWESLDETYEQFKKAYSRIMERLGVRYMIIEAETGAIGGNASHEFVVPAKIGETNVLFCEKCGYQASDEKAEYKGEYTQEQEEEKPLKKVPTPGVKTIEEVSEFLGVPPSKIVKSLLYKGREGYVMVLIRGDLELNEAKLKAHLKDQSLRMATPEEILKDFGVPVGFIGPIGVDVKKVADHSVRGLKNFVVGGMEEDTHYVNANHPRDFKVDEWYDLRTVVEGDPCPVCGEPLKATKGIELGHIFKLGTKYSEAMKAYFMDENGEMKPFIMGCYGWGVSRTMAAVVEHFHDENGMIWPLSIAPYTVVVDILNMNDAEQKQVGEKIYQVLSEKGEEVVLDDREVSPGFKFKDADLIGFPIRINVGRSLKEGVVELKKRYSKELVKVNIKNGFGALLETLEKMKREYDPKEAVR
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Q9WYY4
Q899J1
MURC_CLOTE
UDP-N-acetylmuramoyl-L-alanine synthetase
Clostridium
MSFDFLKYIKKVHFIGIGGISMSGMAEILLKKGYKVSGSDSTKSPIIDKLINLGAEIYIGHKAENIKNVDLIVYTAAVSEDNPELTKALTNNIKIMNRAEFLGYLMDGHKYNIAVSGTHGKTTTTSMMSHITVNANLDPTILVGGELNIINGNVRTGKSEYFLTEACEYKESFLKFFPYIGVILNIDADHLDYYKDINHIKNAFSKFANLIPKDGYLIACAEDENINDIIKNIDCTIITYGLNKGDIQAKNITFDNKGCASFDVIKNSSVLFSVKLNVPGSYNVLNALASICVSFALNIDKESIIKGLESFHGTHRRFELKGVRNDVTVIEDYAHHPTEIKATLSAAKNYPSNRILCVFQPHTYTRTYSLFEDFTESFYNTDTLILADIYPAREKDTGIVSSDMLGNKLRKKNINCINLHSFEDISDYLKKETKPGDLVLIMGAGDIYKAGDLFLK
Cell wall formation.
Q899J1
Q2FGF7
RECO_STAA3
Recombination protein O
Staphylococcus
MLMRQKGIIIKAVDYGESDKIITILNEHGAKVPLMARRAKKVKTGLQAQTQLFVYGLFIYNQWRGMGTLNSVDVISQHYKLQMDLYVSSYAALAAETIERSMDEGDIAPYNYQLLQFVLEKIESGTSAQLMSVVVMLKCMKRFGFTASFNRCAVSGNDTQADLIGYSFKFDGAISRQEASKDVHAVILSNKTLYLLDVLQKLPIDKMNSLNIHQEIIDEMSDIILMLYREYAGMFFKSQKLINQLKRLEQ
Involved in DNA repair and RecF pathway recombination.
Q2FGF7
Q5AUW7
ORSD_EMENI
Orsellinic acid/F9775 biosynthesis cluster protein D
Aspergillus subgen. Nidulantes
MPPVRFGPRKILEYDGRYGVLICHECRYAIQKSALQSHLLRHKIYRADRQQLVAMINELDLLEPDDVLLPPPESPPIDGLPVIAGYRCTAPGCANLCASLKRMKGHWRESHGIADASLARPAKLQTFFRGTKIRYFEVTPTTEDEDDEENESENDEEEGDVDLEEQEDDNGGRQSTTVTTSPGPSAPSVNVDLETLSYFHHFMSATSLTLPCPQDMQSGAQYWKEKAVPQALQQRWLMCGLLALAACHLAAFPDNAAAGQQHRKRAAEFSLEFRTGWRELADTSGEGLREVATEIECLLRCAHWALAESPCDQRIMPEPGVPEHLQSIISTIQSTVPAAAPHEAETSAYATRILRWNTSEAGNSVLAEIRNRLHDLPARMADTFGRPENIQDVLVLLSALAAMGECCDTSFASEEVGPAWWGMATWWTRVPLRFKELVARHYPASLVVVAHWAALMVNRTERCGCWLVKGLAMTILLRIAERLPEDDDGNVQRLVALTIAA
Part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B . The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units . Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B . The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B .
Q5AUW7
C5CT25
RS15_VARPS
30S ribosomal protein S15
Variovorax
MIAASIKAEVVKDNARAANDTGSPEVQVALLTARINELTPHFKTHAKDHHGRRGLLRMVSRRRKLLDYLKSKDADRYTALIAKLGLRK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
C5CT25
Q65W50
TRMN6_MANSM
tRNA m6A37 methyltransferase
Basfia
MTTFMNNKTKSAGFTFKQFHVSHDKCAMKVGTDGILLGAWASLQGNRYLDLGTGSGLIALMLAQRTQTDCHITGVEIDPSAYRQATENVRQSPWADKIQLEQQNIVDFTRTCTKKFDTVLSNPPYFEQGVDCRDKQRDTARYTQTLSHSDWLNLAADCLTNTGRIHLILPYAAGKNLQKQTALFCARCCEVITKSGKIPQRLLLTFSKQPCTTEQSRLVVYNEQNQYTEQFIALTRDFYLNF
Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Q65W50
P57091
C18BA_PAEPP
Parasporal delta-endotoxin CryXVIIIB(a)
Paenibacillus
MNNNGNALSRTALTPTNNKVISGDLVTNGLPPIDNNIICSNGFMPINVTRKNPFRKRTTQEFIREWTEWKENSPSLFTAPIVGVVTSTLLEALKKQVQSRLLLLMTNLLFPNNSTSTMEEILRATEQYVQEQLDTVTWNRVSQELEGLKNNLRTFNDQIDDFLQNRVEISPTAMIDSINTMQQVFVNRLPQFQLSDYQLLLLPLFAQGATLHLTFIRDIIINAGEWNIPEAQLNTCKRYLKQYVAQYSNYALSTYEGAFRARFYPRATLENMLQFKTFMTLNVLDLVSIWSLLKYMNLYISTSANLYNIGDNKVNEGEYSISYWPFFNSYIQTKSNYVLSGVSGYAIRWYYLNTFFGEYIQDNLYNIIASYVGGVNGPKIGVQLSTTELDKQIKQQARAGMPTGLDDLSFNCTLRNPTTVPYFACNFQELTSSGTAGTGGFIRSDVFRSEDNICGLGTGYASAWTSYPDYYITNISATVQVDGINIDITPLCFGEDRAITSTHGVNKVIAVYNRKANIAGTNQNGTMIHQAPNDGTGFTVSPLHLASFTHPSEAHIQENYGNSGDSLRLTGPTTAITYMLSGDGRTIYKLVLRVSGVITRITAKVRGNSIGYLEYINTVDNNQGITDNGSKFQDFEFRPTITIDAQTPIVLEFSATSNFDLMNLIFIPYYDTPIY
Binds to the brush border membrane vesicles of scarab larvae and damages the gut wall somehow to allow the vegetative cells of P.popilliae to enter the hemolymph.
P57091
Q5PEN3
RPPH_SALPA
(Di)nucleoside polyphosphate hydrolase
Salmonella
MIDDDGYRPNVGIVICNRQGQVMWARRFGQHSWQFPQGGINPGESAEQAMYRELFEEVGLSRKDVRILASTRNWLRYKLPKRLVRWDTKPVCIGQKQKWFLLQLMSADAEINMQTSSTPEFDGWRWVSYWYPVRQVVSFKRDVYRRVMKEFASVVMALQDNPPKLQSAPAYRRKRG
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Q5PEN3
O24755
FUR_VIBPA
Ferric uptake regulation protein
Vibrio
MSDNNQALKDAGLKVTLPRLKILEVLQQPDCQHISAEDLYKKLIDLGEEIGLATVYRVLNQFDDAGIVTRHHFEGGKSVFELSTQHHHDHLVCLDCGEVIEFSDDIIEERQREIAAKYNVTLTNHSLYLYGKCSDGGCKENPDAHKPAK
Fur acts as a repressor, employing Fe(2+) as a cofactor to bind the operator of the iron transport operon.
O24755
B1HTF6
END4_LYSSC
Endonuclease IV
Lysinibacillus
MLLGSHVSMSGKEMLLGSSKEALSYGANTFMIYTGAPQNTRRKAIADLNIMNGRLHMKEHGMTNIVVHAPYIINIGNTEKPETFRLGVDFLQSEIERTAALEATQIVLHPGAHVGAGADAGIAKIIEGLNEVLSQDYPVQIALETMAGKGTECGRSFEELAKIIDGVTHNERLSVCFDTCHTHDAGYNIVEDFDGVLNEFDKLIGVDRIKVLHINDSKNVRGAAKDRHENIGFGHIGFDALNYVVHHPQLMAIPKILETPFVPLASDAKSKSAPYKAEIEMLRSSTFKPELIEALKG
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
B1HTF6
B1YVD7
LPXK_BURA4
Lipid A 4'-kinase
Burkholderia cepacia complex
MSAPGGPLARLEARVTREWQRRGALAWALTPFACVFGLCAALRRTAYAQGWKQPVDVGVPVVVVGNVTVGGTGKTPTVIALVDALRAAGFTPGVVSRGYGANVKTPTAVTPASRASAAGDEPLLIARRTDAPVWVCPDRVAAAQALRAAHPDVDVIVSDDGLQHYRLARTVELVVFDHRLGGNGFLLPAGPLREPLSRHRDATLVNDPYSGALPPWPDTYALALTPGAAWHLDQPALRRPLSQFAHERVLAAAGIGAPERFFATLRAAGLAPATRALPDHYAFADNPFVDDAVDAILITEKDAVKLGASWRDARLWVVPVEAALDPRLIALVVEKLRGRSPA
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).
B1YVD7
C3KU98
GATC_CLOB6
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Clostridium
MSVSKKDVEYVAELARLEFKEEEKDNFVNDLNKILNYMEKLDELNTDDVDIVVNPYYIENKYREDNVEKSMELKEVIDNAPESLEEYVIVPKVID
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).
C3KU98
A9BUK3
MRAY_DELAS
UDP-MurNAc-pentapeptide phosphotransferase
Delftia
MLLMLSQWLQGLSPEFGFLRVFQYLTMRAVMAALTALVIGLLAGPRLIRMLTSLKIGQPVRGYGMETHLAKSGTPTMGGALILLSIAVSTLLWFDLSNRFVWIVLLVTLGFGTIGWVDDWRKVVNKDPEGMRSGEKYFWQSVIGLLAALYLVFCISENSNAQVFELFVTWVQSGFALDLPPKAGLLVPFFKEVSYPLGVLGFVIMTYLVIVGASNAVNLTDGLDGLAIMPVIMVGSALGIFAYVTGNAGYAKYLLFPHIPGSGELLVYCAAMAGAGLAFLWFNAHPAQVFMGDVGALALGASLGTIAVIVRQEIVLAIMGGIFVVEALSVMLQVTWFKFTKKRYGQGRRLLKMAPLHHHFEKSGWKETQVVIRFWIITMLLCLLGLSTLKLR
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
A9BUK3
B1VDE8
NRDR_CORU7
Transcriptional repressor NrdR
Corynebacterium
MLCPSCRCEDSRVVDSRVVEGGIAIRRRRECLQCLTRFTTMERSVLLVTKRNGVTEEFSREKVIKGVKQACQGRDVSDDDLKLLAHEVEQSVRADYGSQVNAHDIGLAILPPLRRLDEVAYLRFASVYKSFSSSEDFEAEIALLRRQHQGNAPSSGS
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
B1VDE8
A4J683
RNC_DESRM
Ribonuclease III
Desulforamulus
MSKQDEQANRLKTRLGFKWHNPTLLIQALTHSSCVHENRGHGLCHNQRLEFLGDAVLELIISEHLYKMFPDRTEGELTKMRASSVCEPSLAKVARGLDLGRCLRMGRGEERSGGRERPSILADAFEALLGAIYLDQGLEISRHFVLNCLSSIIDDVVAGRLDRDYKTELQEILQQSSPDPLTYTIMDESGPDHDKTFTAGVIYKGKVIGKGSGHSKKEAEQQAAKDAFQHLEGMGKSGHKSAGPIR
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.
A4J683
B2S682
EFG_BRUA1
Elongation factor G
Brucella
MAREYKIEDYRNFGIMAHIDAGKTTMTERILFYTGKNHKIGETHDGASTMDWMEQEQERGITITSAATTTFWQGRDGKKRRFNIIDTPGHVDFTIEVERSLRVLDGAIALLDANAGVEPQTETVWRQAEKYHVPRMVFVNKMDKIGADFYRSVEMVGSRLGAVALPVQLPIGAENDFVGVVDLIEMKALTWDGTIGAPATVGEIPADMADKAEEYREKLIELAVEIDEAAMEAYLEGTMPTNDELRALIRKGTIEVKFHPILCGTAFKNRGVQPLLDAVVEFLPAPTDVPAIKGIDVKTETETTRESSDEAPLSMLAFKIMNDPFVGSLTFARIYSGKLTKGVSLENTVKGKRERIGRMLQMHSNSREDIDEAFAGDIVALAGLKETTTGDTLCDPLKPVILERMEFPDPVIEIAIEPKTKADQEKMGIALNRLAAEDPSFRVKSDEESGQTIIAGMGELHLDILVDRMKREFKVEANVGAPQVAYRESITRAAEIDYTHKKQSGGSGQFARVKIIFEPHDGDDFIFESKIVGGSVPKEYIPGVQKGIESVMGAGPLAGFPMLGVKATLIDGAYHDVDSSVLAFEIASRAAFREGAQKAGAQLLEPIMKVEVVTPEDYVGDVIGDLNSRRGQISGTEARGIAAVVNAMVPLANMFGYVNSLRSMSQGRAQYTMQFDHYEPVPTAVAQEIQKKFA
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.
B2S682
B8G1X2
RS3_DESHD
30S ribosomal protein S3
Desulfitobacterium
MGQKVNPKGLRVGIIRDWEGRWFADKNYLELLHEDLKVRKFVKTKLQQAGVPKVEIERAANRVKVSIYAAKPGIVIGRGGTEVENLRKQLEAMTGKQVAVNIVEVKKPELDAQLVAESVAQQLEKRVSFRRAMKQTVQRTMRQGGQGIKISCSGRLGGAEIARTEWYSEGKVPLHTLRADIDYGFAEANTTYGKIGVKVWIYKGEVLPAKKVAQVEGGK
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
B8G1X2
A8GCI3
KDSB_SERP5
CMP-2-keto-3-deoxyoctulosonic acid synthase
Serratia
MSFIAIIPARYASTRLPGKPLADIHGKPMVVHVMERARESGASRVIVATDHPAVAEAVKAAGGEVCMTRADHNSGTERLAEVIEHYGFADDEIIVNVQGDEPLIPPVIVRQVAENLAGSQAGMATLAVPIESAEEAFNPNAVKVVMDAQGYALYFSRATIPWDRERFAQSKESIGDSLLRHIGIYAYRAGFVRRYVTWAPSQLEQIELLEQLRVLWYGEKIHVAVAKAMPTVGVDTQEDLQRVRDSIKG
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
A8GCI3
P20613
SSP2_BOMMO
Arylphorin
Bombyx
MKSVLILAGLVAVALSSAVPKPSTIKSKNVDAVFVEKQKKILSFFQDVSQLNTDDEYYKIGKDYDIEMNMDNYTNKKAVEEFLKMYRTGFMPKNLEFSVFYDKMRDEAIALLDLFYYAKDFETFYKSACFARVHLNQGQFLYAFYIAVIQRPDCHGFVVPAPYEVYPKMFMNMEVLQKIYVTKMQHGLINPEAAAKYGIHKENDYFVYKANYSNAVLYNNEEQRLTYFTEDIGMNAYYYYFHSHLPFWWTSEKYGALKERRGEVYFYFYQQLLARYYFERLTNGLGKIPEFSWYSPIKTGYYPLMLTKFTPFAQRPDYYNLHTEENYERVRFLDTYEKTFVQFLQKDHFEAFGQKIDFHDPKAINFVGNYWQDNADLYGEEVTKDYQRSYEVFARRVLGAAPMPFDKYTFMPSAMDFYQTSLRDPAFYQLYNRIVEYIVEFKQYLKPYTQDKLYFDGVKITDVKVDKLTTFFENFEFDASNSVYFSKEEIKNNHVHELRCATRLNHSPFNVNIEVDSNVASDAVVKMLLAPKYDDNGIPLTLEDNWMKFFELDWFTTKLTAGQNKIIRNSNEFVIFKEDSVPMTEIMKMLDEGKVPFDMSEEFCYMPKRLMLPRGTEGGFPFQLFVFVYPFDNKGKDLAPFESFVLDNNLLASLWIAPLLMHYSRFLTCISRIFSFTTRVNGSLTNSIFLRMTHMIMLFQKIKF
Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.
P20613
P27807
H2B1_WHEAT
Histone H2B.1
Triticum
MAPKAEKKPAAKKPAEEEPAAEKAEKTPAGKKPKAEKRLPAGKSAAKEGGDKKGKKKAKKSVETYKIYIFKVLKQVHPDIGISSKAMSIMNSFINDIFEKLAGEAAKLARYNKKPTITSREIQTSVRLVLPGELAKHAVSEGTKAVTKFTSS
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P27807
A4QJL3
PSBJ_AETGR
Photosystem II reaction center protein J
Aethionema
MADTTGRIPLWIIGTGAGILVIGLIGIFFYGSYSGLGSSL
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
A4QJL3
Q9DCT6
BAP18_MOUSE
BPTF-associated protein of 18 kDa
Mus
MTSASTKVGEIFSAAGAAFTKLGELTMQLHPVSDSSPAGAKWTETEIEMLRAAVKRFGDDLNHISCVIKERTVAQIKTTVKRKVYEDSGIPLPAESPKKGPKKMTSGVLSPPNAPPPSSSSVPEAGVPPIKKQKADVTLSALNDSDANSDLVDVEGLGETPPAKKLNFDQA
Component of chromatin complexes such as the MLL1/MLL and NURF complexes.
Q9DCT6
Q94WW5
CYB_OCTGL
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Octodontomys
MTNIRKSHPLIKIINHSFIDLPAPSNISAWWNFGSLLGVCLMLQIITGLFLAMHYTADTTTAFSSVTHICRDVNYGWLIRYLHANGASMFFIFLYLHIGRGIYYGSFTFMETWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGPNLVEWIWGGFSVDKATLTRFFAFHFILPFIITAMVMIHLLFLHETGSNNPSGLNSDSDKIPFHPYYTIKDILGLLFMVLTLMTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVFSILILMLFPLLQMSKQRSMSFRPLSQCLLWVLVANLIILTWIGGQPVEHPFIMIGQLASVIYFSIILIFMPIISLMENKLLKW
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.
Q94WW5
Q82MF1
ANMK_STRAW
AnhMurNAc kinase
Streptomyces
MRVIGLMSGTSYDAIDAAAADLGLAGDRLVLKPLGLMSEAYDSGLREELAAALPPAATSLAGVCRLDTRIGQAFAAAAVRADRELCGGRAELVASHGQTVYHWAEAGRVYGTLQLGQPAWIAEATGLPVVADFRPRDIAAGGQGAPLVSLVDLLWLRGRAGTSVALNLGGIANLTAPDGTAFDTGPACALIDAAAHGLSGGRLDHDVDGALAARGTVHEPMLRRLLAEPYYALPAPKTTGKELFHLGYLRDALAGFGTLTAEDVIATLTRLTALTVADAVRAVRATEVVASGGGTRNPVLMEMLARELGAVALRTSDELGLPSAAKEAYAFAVLGFLTVHGLAGTDPVSTGARHPSVLGSVTPGRDGLRLPPRADWSPVRLVLE
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Q82MF1
Q0WNP3
PP319_ARATH
Protein SEEDLING LETHAL 1
Arabidopsis
MFSLSLIQPRLRISEIPVTQSYKSPTICYSSDSRTKREEQRHVRLPGFRLVSGKRASFDSGFSGFKGENVNQDDSSSFDSERVDYALLAEWLQSSNGMRLIKRIHAMALKCFDDQVIYFGNNLISSCVRLGDLVYARKVFDSMPEKNTVTWTAMIDGYLKYGLEDEAFALFEDYVKHGIRFTNERMFVCLLNLCSRRAEFELGRQVHGNMVKVGVGNLIVESSLVYFYAQCGELTSALRAFDMMEEKDVISWTAVISACSRKGHGIKAIGMFIGMLNHWFLPNEFTVCSILKACSEEKALRFGRQVHSLVVKRMIKTDVFVGTSLMDMYAKCGEISDCRKVFDGMSNRNTVTWTSIIAAHAREGFGEEAISLFRIMKRRHLIANNLTVVSILRACGSVGALLLGKELHAQIIKNSIEKNVYIGSTLVWLYCKCGESRDAFNVLQQLPSRDVVSWTAMISGCSSLGHESEALDFLKEMIQEGVEPNPFTYSSALKACANSESLLIGRSIHSIAKKNHALSNVFVGSALIHMYAKCGFVSEAFRVFDSMPEKNLVSWKAMIMGYARNGFCREALKLMYRMEAEGFEVDDYIFATILSTCGDIELDEAVESSATCYLETS
Required for proper chloroplast development (Ref.7, PubMed:24144791). Involved in the regulation of plastid gene expression probably through regulation of plastid-encoded polymerase (PEP) dependent chloroplast transcription . Required for RNA editing of several chloroplastic transcripts, especially accD transcripts . Required for processing of the chloroplastic rpoA pre-mRNA (Ref.6, Ref.7). Required for the monocistronic rpoA transcript processing from the rpl23-rpl2-rps19-rpl22-rps3-rpl16-rpl14-rps8-rpl36-rps11-rpoA polycistron. Binds the intergenic sequence of rps11-rpoA for rpoA monocistronic RNA cleavage (Ref.7).
Q0WNP3
Q5PDJ4
DNAJ_SALPA
Chaperone protein DnaJ
Salmonella
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q5PDJ4
P42497
PHYD_ARATH
Phytochrome D
Arabidopsis
MVSGGGSKTSGGEAASSGHRRSRHTSAAEQAQSSANKALRSQNQQPQNHGGGTESTNKAIQQYTVDARLHAVFEQSGESGKSFDYSQSLKTAPYDSSVPEQQITAYLSRIQRGGYTQPFGCLIAVEESTFTIIGYSENAREMLGLMSQSVPSIEDKSEVLTIGTDLRSLFKSSSYLLLERAFVAREITLLNPIWIHSNNTGKPFYAILHRVDVGILIDLEPARTEDPALSIAGAVQSQKLAVRAISHLQSLPSGDIKLLCDTVVESVRDLTGYDRVMVYKFHEDEHGEVVAESKRNDLEPYIGLHYPATDIPQASRFLFKQNRVRMIVDCYASPVRVVQDDRLTQFICLVGSTLRAPHGCHAQYMTNMGSIASLAMAVIINGNEEDGNGVNTGGRNSMRLWGLVVCHHTSARCIPFPLRYACEFLMQAFGLQLNMELQLALQVSEKRVLRMQTLLCDMLLRDSPAGIVTQRPSIMDLVKCNGAAFLYQGKYYPLGVTPTDSQINDIVEWLVANHSDSTGLSTDSLGDAGYPRAAALGDAVCGMAVACITKRDFLFWFRSHTEKEIKWGGAKHHPEDKDDGQRMNPRSSFQTFLEVVKSRCQPWETAEMDAIHSLQLILRDSFKESEAMDSKAAAAGAVQPHGDDMVQQGMQEIGAVAREMVRLIETATVPIFAVDIDGCINGWNAKIAELTGLSVEDAMGKSLVRELIYKEYKETVDRLLSCALKGDEGKNVEVKLKTFGSELQGKAMFVVVNACSSKDYLNNIVGVCFVGQDVTGHKIVMDKFINIQGDYKAIIHSPNPLIPPIFAADENTCCLEWNTAMEKLTGWPRSEVIGKLLVREVFGSYCRLKGPDALTKFMIVLHNAIGGQDTDKFPFPFFDRKGEFIQALLTLNKRVSIDGKIIGAFCFLQIPSPELQQALEVQRRQESEYFSRRKELAYIFQVIKNPLSGLRFTNSLLEDMDLNEDQKQLLETSVSCEKQISKIVGDMDVKSIDDGSFLLERTEFFIGNVTNAVVSQVMLVVRERNLQLIRNIPTEVKSMAVYGDQIRLQQVLAEFLLSIVRYAPMEGSVELHLCPTLNQMADGFSAVRLEFRMACAGEGVPPEKVQDMFHSSRWTSPEGLGLSVCRKILKLMNGGVQYIREFERSYFLIVIELPVPLMMMMPSS
Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
P42497
Q82VQ6
COXX_NITEU
Heme O synthase
Nitrosomonas
MTTSSLAWQQATARVQQFYRLTKPRVVSLIVFTAVIGMFLSVPGAVPLDKLIFGTVGISLVAGAAAALNCLVEYKFDAIMARTKGRPLPQGKVSVPETLFFLVLIGGFGLFMLHQWVNPLTMWLTLGTFVGYAIIYTVILKPLTPQNIVIGGASGAMPPVLGWAAVTGEISADALLLFLIIFAWTPPHFWALALYRKTDYAKIGMPMLPVTHGDEFTRLHVLLYTIILCVVTVLPYLTQMSGLIYLGSVLILDAIFFYYAIRIYLHYTDQIAREAFRYSIAYLALLFTALLVDHYFYF
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.
Q82VQ6
Q93113
GST1D_ANOGA
GST class-theta
Anopheles
MDFYYLPGSAPCRAVQMTAAAVGVELNLKLTDLMKGEHMKPEFLKLNPQHCIPTLVDNGFALWESRAIQIYLAEKYGKDDKLYPKDPQKRAVVNQRLYFDMGTLYQRFADYHYPQIFAKQPANPENEKKMKDAVGFLNTFLEGQEYAAGNDLTIADLSLAATIATYEVAGFDFAPYPNVAAWFARCKANAPGYALNQAGADEFKAKFLS
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.
Q93113
Q7TX14
NUDC_MYCBO
NADH pyrophosphatase
Mycobacterium tuberculosis complex
MTNVSGVDFQLRSVPLLSRVGADRADRLRTDMEAAAAGWPGAALLRVDSRNRVLVANGRVLLGAAIELADKPPPEAVFLGRVEGGRHVWAVRAALQPIADPDIPAEAVDLRGLGRIMDDTSSQLVSSASALLNWHDNARFSALDGAPTKPARAGWSRVNPITGHEEFPRIDPAVICLVHDGADRAVLARQAAWPERMFSLLAGFVEAGESFEVCVAREIREEIGLTVRDVRYLGSQPWPFPRSLMVGFHALGDPDEEFSFSDGEIAEAAWFTRDEVRAALAAGDWSSASESKLLLPGSISIARVIIESWAACE
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Q7TX14
Q96GD0
PLPP_HUMAN
Pyridoxal phosphate phosphatase
Homo
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED
Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism . Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine .
Q96GD0
B4TRN5
RLMC_SALSV
23S rRNA(m5U747)-methyltransferase
Salmonella
MQCALYDAGRCRSCQWITQSVNEQLSAKTADLHRLLTGLPVEQWCASIGGPEQHFRNKAKMVVSGSVEKPLFGMLHRDGTPVDLCGCPLYPASFAPVFSALKPFIARAGLTPYNVARKRGELKYLLLTESQFDGGMMLRFVLRSETKLTQLRAALPWLRAQLPQLRVITANIQPVHMAIMEGETEIYLTDQQALAERFNDVPLWIRPQSFFQTNPTVASRLYATARDWVGQLPVRHMWDLFCGVGGFGLHCATPQMQLTGIEIAPEAIACAKQSAAELGLTRLHFQALDSTQFATAQGETPDLVLVNPPRRGIGKPLCDYLAQMAPRFIIYSSCNAQTMAQDIRHLPNYRIQSVQLFDMFPHTAHYEVLTLLCRL
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
B4TRN5
Q4R3R9
MIER3_MACFA
Mesoderm induction early response protein 3
Macaca
MAEASFGSSSPVGSLSSEDHDFDPTAEMLVHDYDDERTLEEEEMMDEGKNFSSEIEDLEKEGTMPLEDLLAFYGYEPTIPAVANSSANSSPSELADELPDMTLDKEEIAKDLLSGDDEETQSSADDLTPSVTSHETSDFFPRPLRSNTTCDGDKESEVEDVETDSGNSPEDLRKEIMIGLQYQAEIPPYLGEYAGNEKVYENEDQLLWCPDVVLESKVKEYLVETSLRTGNEKIMDRISAGTHTRDNEQALYELLKCNHNIKEAIERYCCNGKASQEGMTAWTEEECRSFEHALMLFGKDFHLIQKNKVRTRTVAECVAFYYMWKKSERYDYFAQQTRFGKKRYNHHPGVTDYMDRLVDETEALGGTVNASALTSNRPEPIPDQQLNILNSFTASDLTALTNSVATVCDPTDVNCLDDSFPPLGSTPRGQVNHVPVVTEELLTLPSNGESDCFNLFETGFYHSELNPMNMCSEESERPAKRLKMGIAVPESFMNEVSVNNLGVDFENHTHHITSAKMAVSVADFGSLSASETNGFISAHALHQHAALHSE
Transcriptional repressor.
Q4R3R9
B5L5P4
WAPD_AUSSU
Supwaprin-d
Austrelaps
MSSGGLLLLLGLLTLWAEVTPISGQDRPKKPGLCPPRPQKPCVKECKNDWSCPGQQKCCNYGCIDECRDPIFVN
Damages membranes of susceptible bacteria. Has no hemolytic activity. Not toxic to mice. Does not inhibit the proteinases elastase and cathepsin G.
B5L5P4
A2RP20
DNAJ_LACLM
Chaperone protein DnaJ
Lactococcus cremoris subsp. cremoris
MNNTEYYERLGVDKNASQDEIKKAYRKMSKKYHPDLNKEEGAEDKYKEVQEAYETLSDEQKRAAYDQYGEAGANGGFGGGGFGGASGFSGFGGASGGFGGFEDIFSSFFGGGGAQVNPNAPRQGDDLQYRINLKFEEAIFGVEKQVKYNREELCHTCGGSGAKAGTHPETCHKCGGRGQINVVRDTPLGRMQTQTTCDVCHGTGKEIKEKCTTCHGSGHEKVAHTVKVTVPAGVETGQKMRLQGQGDAGVNGGPYGDLYVVFQVEASDKFERDGAEIYYKMPMDFVQAALGDEVEVPTVHGNVKLKIPAGTQTGANFRLKGKGAPKLRGSGNGDQYVIINIVTPKNMNQAQKEALQAFAKASGIEVSGSGKKGFFDKFK
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A2RP20
Q6NXH8
MET25_MOUSE
Probable methyltransferase-like protein 25
Mus
MAAACPLPRTPDLPTLHDKLQGLLSFLRGALAISSAHTVDFYTKSVWQELVDLPPESVLAALRESAVEAEPREAETGSGFTELPKIFCETSQKLLSVEAFARTAKHYSVQNLGLCTPSEQLLTALQGNKRQRVDENVKAIEFMNTKKSHEVQAMSELICSIADYCGLKQIIDVGSGKGYLSSFLSLKYGLNVYGIDSSNTNTHGAKERNRKLKKHWSLYHPHSRADANGWASERPRELKVPKGVECKGDAESVQRSRLGNPDLSATDGLPDFSGSAISVIRKQQKNVLAQPAEEENLYFEDAFSLIDFLPVDAIEPTSSQVQNTEKSGLRKERRNTASKARDSSIYSPLTSFITADSQLHDIIEDLEDCLMVGLHTCGDLAPSTLRIFTSKAEVKAVCSVGCCYHLLSEEFENQHKDRCANENWGFPMCHYLKEERWCCGRNARMSACLALQRVAVGQGLPTESLFYRAVLQNIIKDYYGISKCEQHVGKIYSKCSSFLEYVRMSLKKLGLDESKVSEEIIMDYYENYKPRMNELEAFNMLKVVLAPCIETLILLDRLCYLKEQDGVAWSALVKLFDPVQSPRCYAVIALKKQCDLG
Probable methyltransferase.
Q6NXH8
Q9M8S7
ARS1_ARATH
Protein ABA AND ROS SENSITIVE 1
Arabidopsis
MDAQAKKKAMFRSKLNAKKKDTRIDSPLVRYNESDQPVCRVCNVVLKSESLWDVHQASRKHHEAIDSLKASAAGVQRGSKPAETRPTKIEALAKSSNSQTSSGLPPNFFENREPARAEVEPAKSKNLEQSKHTIGSETNKSKGPLPAGFFDNQKTDSSNTKTTSEPKQSQTQTTGPETKPMVNGNLPTGFFDNKEADLLAHGIKLVKPDIKDEYKEFEKLIQDDLQVVDSRMEEEEVDAAETIEEEEQREQRSYKEKVEILKRKKMELKAARLAKRSKTSEGSVKKPKKTEEESPSDEEDDEDSAVDWRAQHL
Essential for breaking seed dormancy before seed germination . Prevents reactive oxygen species (ROS) accumulation in response to abscisic acid (ABA) and oxidative stress, probably by repressing the accumulation of ABA-induced ROS-scavenging enzymes (e.g. CSD3) .
Q9M8S7
Q4V1F5
IOLD2_BACCZ
3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase 2
Bacillus cereus group
MQTVRMTTAQALVKFLNQQYIEFDGEQQKFIKGIFTIFGHGNVVGLGQALEEDAGELEVYQGRNEQGMANAAMAFAKQKHRKQIMACTSSVGPGSANMITSAATASANNIPVLLLPGDVFATRQPDPVLQQIEQTHDLSISTNDAFRAVSKYWDRINRPEQLMTAMIQAMRVLTNPADTGAVTICLPQDVQGEAWDFPSYFFQKCVHRIERRLPTRASLADAVEMIKRKKKPVMICGGGVRYAEAAEELKQFAEAFRIPFGETQAGKSAIESSHPYNLGGIGVTGNLAANTIAKEADLVIGIGTRFTDFTTASKQLFQNEEVEFVNINISEFHANKLDALKVIADAKEALLALINELQAIEYRSSYTVEIAAAKEFWETELARLHNIRFTGQDFKPEVEGHFDDNLNEYVDALGTQLTQTAVIGEMNTLLDEDAIIVGAAGSLPGDLQRMWTSRKPNTYHMEYGYSCMGYEVAGALGAKLAEPSKEVYAMVGDGSYQMLHSELVTSLQENKKINVLLFDNSGFGCINNLQMGNGMGSFGTEFRYRNEETRKLNGAIMKIDFAASAAGYGVKTYRVTSVEQLQEALKDAKKQTVSTLIDIKVLPKTMTNGYESWWHVGVAEVSNSQSVQAAYESKVSNLQKARSY
Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG).
Q4V1F5
Q10492
PNN1_SCHPO
Pinin homolog 1
Schizosaccharomyces
MKILAMDERREELSAKSTVQNVKISEAPILDGKVNNEDSHMEIDQPEGSMEEDDHRQVKEKNTSENSVEQKRGRRMFGALLGTLGKFQQESEREQKSARKVKRAELEEKLAKRREQELQELEKQEKIEAEILESRLQEQRKVALDELELDRNDLKKVLDNKKSYYLRTKTQPSLFYRPYYLLPSQRTQLEQMKSEAP
Transcriptional activator that may participate in the regulation of mRNA splicing.
Q10492
B2XWM5
PSAJ_FAGEA
PSI-J
Fagopyrum
MRNLKTYLSVAPVLSTLWFGSLAGLLIEINRFFPDALTFPFFSF
May help in the organization of the PsaE and PsaF subunits.
B2XWM5
Q6BLM3
RAD18_DEBHA
RING-type E3 ubiquitin transferase RAD18
Debaryomyces
MNSNPFTKNLQNVTDPSDWEPTKLPNLKELDSLQRCYICKEFLKAPVITSCNHTFCSHCIREYLIVNSHCPLCKAEQFESNLKRVILLEEIVLCFSKFRPILLELLKKEESNEAYDKNRSPFSEIPSKDEDSRKRSSPDQEVIEISSDESNSLELSEASNDVPKKKIKAEINSNSRNAIPTRNEMVECPICAEVMSADLLQTQHIDYCLSGKSQPSSSRSAGNSSSRYQSMKRRQPNKTNNGISSFFKPADNKPIMAGAGKLDLSKTDNQNFYFDEVSKHHHNDIKKLPKLDFSSLTTPKLKEKLSHLKLPVQGTRIQLELRYNQYYILFNSNLDSNHPLSEKVLKQKLNQWELSHSAFTNQGSTSTLFNNGSPAVKSITDKNFSVKEWLDANRNEYKSLVKAARASIKKASTKNVTSSISIDTEAINTHSVGGQHLNERSEYRSEANLIEPIDDGASEEIQQNEISNLNFKKDIANSPLFVKDTLNESHS
E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Q6BLM3
Q48K99
LEUC_PSE14
Isopropylmalate isomerase
Pseudomonas
MAGKTLYDKLWDSHLVKQRDDGSALIYIDRHIIHEVTSPQAFEGLRLAKRKPWRIDSIIATPDHNVPTTSERKGGIDAIEDQVSRLQVQTLDDNCDEYGITEFKMNDPRQGIVHVIGPEQGATLPGMSVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVSVEGQLPFGVTAKDIVLAVIGKIGTAGGNGYAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGMVATDEKTVEYVKGRPFAPKGAEWDLAVEAWKDLVSDADAVFDTVVRLDAAQIKPQVSWGTSPEMVLAVDQNVPDPAQEPDLVKRGSIERALKYMGLKANQPITDIQLDRVFIGSCTNSRIEDLRAAADVAKGRKVAATIKQAIVVPGSGLIKEQAEKEGLDKVFIEAGFEWREPGCSMCLAMNPDRLGSGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVRDLIQL
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q48K99
Q3SZ76
COMD3_BOVIN
COMM domain-containing protein 3
Bos
MELSEYVQKGFQMLADPGSFDSNTFTLLLRAAFQSLLDAQADEAVLDHPDLKHIDPVVLKHRHAAAATYILEAGKQRADRSTLSTYLEDCKFDSERIELFWTEYQNNRNSLEILLGSIGRSLPHITDVSWRLEYQIKTNQLDKMYRPAYLVTLNVENTDSRSHPEISFSCNMEQLQDLVGKLKDASKSLERATQL
May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits.
Q3SZ76
P00341
LDHA_SQUAC
LDH-M
Squalus
MATLKDKLIGHLATSQEPRSYNKITVVGVGAVGMACAISILMKDLADEVALVDVMEDKLKGEMMDLQHGSLFLHTAKIVSGKDYSVSAGSKLVVITAGARQQEGESRLNLVQRNVNIFKFIIPDIVKHSPDCIILVVSNPVDVLTYVAWKLSGLPMHRIIGSGCNLDSARFRYLMGERLGVHSSSCHGWVIGEHGDSSVPVWSGMNVAGVSLKELHPELGTDKDKENWKKLHKDVVDSAYEVIKLKGYTSWAIGLSVADLAETIMKNLCRVHPVSTMVKDFYGIKNDVFLSLPCVLDNHGISNIVKMKLKPDEEQQLQKSATTLWDIQKDLKF
Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+).
P00341
B4R8Q8
PTH_PHEZH
Peptidyl-tRNA hydrolase
Phenylobacterium
MLLIAGLGNPGPTYAKNRHNIGFMAVDEIARRWGFPAARSRFRSLAAEGAIDTPQGPVRTLILKPQTYYNESGRAVGEAMKFFKLQPSDVVVFYDEIDLAPGRFRMKTGGGAAGNNGIRSVASQIGPDFRRARLGTGHPGQKELVHGHVLSDFHKAEMKWVEPLLEACADAAPLLALGDDEKYQAEVMRLAPAEKADPRKLAQGKPRGE
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
B4R8Q8
Q8PR13
GLGB1_XANAC
Glycogen branching enzyme 1
Xanthomonas
MSNRWDSGVVRALAEARHGDAFAVLGAHPSDKGRLLRTYLPGADRVGAVLDDGQVVALDAGPEPGLFAGELPAHGGYRLRIGWPGGEQETADPYAFGPQLSDFDLHLISEGHHLQLADALGANVVEVEGVRGTRFAVWAPNASRVAVVGDFNSWDARRHPMRLRHQSGVWELFVPDVGPGAHYKYQLRGPHGHELPAKADPVARRAELAPGTASIVADPTPHQWSDDGWMATRARRQAHDAPMSIYEIHAGSWLREAGVDLDWDGLADRLIPYVADMGFTHVELMPVSEHPFGGSWGYQPLGLFAPTARFGTPDGFARFVDRCHREGIGVIVDWVPAHFPTDAHGLAHFDGTALYEHADPREGFHRDWNTLIYNHGRREVSGFLIASAMEFLQRYHVDGLRVDAVASMLYRDYSRNAGEWIPNIHGGRENYETIAFLRRLNEVVREHTPGAVMIAEESTAFPGVTAEVAHGGLGFHYKWNMGWMHDTLHYAGLDPIYRRYHHGELTFSMVYAYSERFVLPISHDEVVHGKGSLLGRMPGDDWQRFANLRAYLGFMFTHPGRKLLFMGCEFGQPTEWNHDAGLPWHLLDDPRHRGVQTLVRDLNRLYVQYPALHAHDDDPSGFAWVVGDDAGNSVVAFLRKGKRGDAPVLVVINFTPVVQHAYRIGVPQGGQWREVFNSDAGIYGGSNLGNGGSVTAEQQSMHGHAQSLPLLLPPLGAIVLTPYG
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Q8PR13
Q85FG3
MNME_CYAM1
Probable tRNA modification GTPase MnmE
Cyanidioschyzon
MTLANVFIQDTIVAIATYLAPSSVAIIRLSGNEAIRLAKSICVKKNHWHSHRIIHTYVQDDQNQLIDEVLVLPMLAPRSYTRQDVVEIHAHGGVVVAQTILQLLINRGARLAKPGEFTLRAFINGRLTLTQAESVLELIHAPSVAMAKKALSNLRGALSTQLHQVRSELIQLLAQIEAHLDFDLDNTFVFNSFINSLTNIINQIQNLLNTPSKFYRYGIQVALLGPANAGKSTLFNALIGEERSIVTPIAGTTTDVVEATLQWQQICFRFFDTAGLKEASSEIETKAMAKAQQIAKQCDLILWIIDATSPNLPIPPYLLNSKPLLVVYNKIDVDSSDVLDHVLDHTSYPTVKVSALYATNLSQLKQLIWQQATQLFQLDGIYINERQSQLLQQAKQHLCNLQSALDEGYPLEIISWHLKNAIQCLDENDVNASTLNAIFSQFCIGK
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.
Q85FG3
B7V7J4
RDGC_PSEA8
Recombination-associated protein RdgC
Pseudomonas
MWFRNLLVYRLTQDLQLDADSLEKALGEKPARPCASQELTTYGFTAPFGKGPDAPLVHVSQDFFLISARKEERILPGSVVRDALKEKVDEIEAQQMRKVYKKERDQLKDEIVQTLLPRAFIRRSSTFAAIAPSLGLILVDSASAKKAEDLLSTLREALGSLPVRPLSVKVAPTATLTDWVKTQEAAGDFHVLDECELRDTHEDGGVVRCKRQDLTSEEIQLHLTAGKLVTQLSLAWSDKLSFVLDDKLAVKRLRFEDLLQEQAEKDGGEDALGQLDASFTLMMLTFAEFLPALFEALGGEEIPQGV
May be involved in recombination.
B7V7J4
O61443
MK38B_DROME
Mitogen-activated protein kinase p38b
Sophophora
MSRKMAKFYKLDINRTEWEIPETYQNLQPVGQGAYGQVCKAVVRGTSTKVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDVFHPGQPADSLDQFQQVYMVTHLMDADLNNIIRTQKLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPAESEMTGYVATRWYRAPEIMLNWMHYNQTADIWSVGCIMAELLTGRTLFPGTDHIHQLNLIMEVLGTPADEFMSRISSESARNYIRSLPVMPRRNFRDIFRGANPLAIDLLEKMLELDADKRITAEQALAHPYMEKYHDPTDEQTAALYDQSFEENELPVEKWREMVFSEVTAFKPTAAFAELLPKEQ
Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. May down-regulate insect immunity gene expression after prolonged infection.
O61443
Q029T9
ISPG_SOLUE
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Candidatus Solibacter
MAVKPRRNAVVVDVGGVKVGGTHPIVVQSMTNTDTADVASTVNQVMALARAGSELVRVTVNTEAAAAAVPKIVDACAAFGVRVPIIGDFHYNGHLLLKKYPECARALAKYRINPGNSDIGRKTDDNFRTMIEVAIENRKPVRIGVNWGSLDSALLTRMMDENSLLPEPKDAREVTLDAMVASAVQSARAAERHGLAHDQIILSAKVSGVQDLIDVYRALAAVCDYPLHLGLTEAGLGSKGIVATTAALAPVLQDGIGDTIRTSLTPMPNGDRTEEVIVSQQILQSLGIRSFTPQVTACPGCGRTTSTFFQEMADEIQTYLRVQMPSWKATHPGVETMKVAVMGCVVNGPGESKHSNIGISLPGTFEEPKAPVYVDGRLMTTLKGDRIVAEFLEILNEYVDTHYAIAGEPELVSGD
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q029T9
Q1MSG7
RF1_LAWIP
Peptide chain release factor 1
Lawsonia
MFAKLENLEQKFIEIECSLAQPNIFNDQEQYRKLTKTHSDLKPIVTTFQQFKKLQQQLSENKELISDIDPDIQEMALEEIKKLELELTHLEYELKILLLPKDPLDEKNILLEIRAGTGGEEAALFAADLFRMYCRYAEKMHWKVEIMSQSDSDTGGFKEIIALIQGDNVYSRLKFESGTHRVQRVPTTESQGRIHTSAATVAVLPEAEDVDIEIRPEELRFDVFRSSGPGGQSVNTTDSAVRVTHIPTGIVVTCQDEKSQHKNKAKALKVLSSRLLQIKQEQQEIEQADARRALVGSGDRSERIRTYNFPQGRVTDHRINLTLYSLIKVMEGEIQEFIDALSTHAQTEALKMQATQIAS
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q1MSG7
Q47RN4
YBEY_THEFY
Endoribonuclease YbeY
Thermobifida
MSIDVANESGVPADEERLARLARYILDALRVHPLAELSVLLVDEEPMADLHVRWMNEPGPTDVLSFPMDELRPGAPGRTSEPGILGDVVICPQVAARQAERAGHSMQDEIDLLCTHGILHLLGYDHAEPDEHREMFSLQNELLAGWRRSLEEEER
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q47RN4
Q05840
CLCR_PSEPU
ClcABD operon transcriptional activator
Pseudomonas
MEFRQLRYFIAVAEEGNIGAAARRLHISQPPITRQIQALEQDLGVVLFERTHRGVELTAAGTTFLEDARRLLHVTEISRVRSRAASRGEIGELRVAYFGTVVLHTLPLLLRQLLSVAPSATVSLTQMSKNRQIEALDAGTIDIGFGRFYPYQEGVVVRNVTNERLFLGAQKSRARSFGEQVHCSALRNEPFILFPREGRPSFADEVIGVFKNARVEPKVVAIVEDVNAAMALALAGVGVTIVPETVAMISWPDFGFTELVGSKATVPVSCIYRHDHIAPILKTFLNLLPIRESQ
Involved in regulation of chlorinated catechol metabolism. Transcriptional activator of the clcABD chlorocatechol oxidative operon.
Q05840
Q6G0M4
KDSB_BARQU
CMP-2-keto-3-deoxyoctulosonic acid synthase
Bartonella
MALKPIIVIPARIGSTRLPQKALAEIAGKPMIVHVAEQAKKAAFGRTIVATDHHDIAKAVIAYGHECIMTSSHHESGSDRIYEALNHIDPERCYNTILNVQGDLPTITPHEIISALRPLKNSLTDIATLGAKIVEKDEKTDPNVVKIIGTPLSQNRLRALYFTRATAPYGDGPLYHHIGIYAYRREALEKFVALKPSTLEQREKLEQLRALEHNMRIDVEIIDTIPLGVDTQYDLERVRKILA
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Q6G0M4