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2.75k
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5.51k
AlphaFoldDB
stringlengths
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Q9Z6M1
AROK_CHLPN
Shikimate kinase
Chlamydia
MTIILCGLPTSGKSSLGKALAKFLNLPFYDLDDLIVSNYSSALYSSSAEIYKAYGDQKFSECEARILETLPPEDALISLGGGTLMYEASYRAIQTRGALVFLSVELPLIYERLEKRGLPERLKEAMKTKPLSEILTERIDRMKEIADYIFPVDHVDHSSKSSLEQASQDLITLLKS
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Q9Z6M1
Q8ZPK6
BIOD2_SALTY
Dethiobiotin synthase 2
Salmonella
MLKRFFITGTDTSVGKTVVSRALLQALASSGKSVAGYKPVAKGSKETAEGMRNKDALVLQSVSSLELPYEAINPIALSEEESSVAHSCPINYTLLSNGLASLSDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAVANDGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLSMLGSVLAVDRIMA
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Q8ZPK6
Q1GWJ6
HRCA_SPHAL
Heat-inducible transcription repressor HrcA
Sphingopyxis
MTTPPITELTTRARDVFRLVVDAYLETGQPVGSRTLSKLATLNLSPASIRNVMQDLEEYGLLASPHTSAGRMPTEQGLRLFVDGMMQVAEPSAEDRAQIEASLSEGGPIESALAQATAALSGLSACAGLVLVPKHERVLKQVAFVPMSERQALVVLVAGDGTVENRIIDVPAGLDPSALVEAGNFISATLSGLTLTEAMARVRREIEAERIAIDRAAQDLVSRGLAIWSSDGADRPVLIVRGQANLLDDSAVGDLDRVRQLLDELETKQDIAQLLDSAREGSATRIFIGSENKLFSLSGSSVIAAPYRGADGRVVGVVGVIGPTRLNYARIVPMVDFTAQSLSRLIR
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Q1GWJ6
A4SMW2
MINE_AERS4
Cell division topological specificity factor
Aeromonas
MSLLDYFRSNKKQNTAQLAKERLQIIVAHERSSRGGPDYLPQLKQDLLDVIRKYVQIDPDKITVQLDKKSDELSVLELNITFADDKKG
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.
A4SMW2
Q70RM6
NU4LM_PHOPH
NADH dehydrogenase subunit 4L
Phocoena
MSLIHINILMAFTMSLVGLLMYRSHLMSALLCLEGMVLSLFILMTLTILNSHFTLANMVPIILLVFAACEAAIGLALLVMVSNTYGTDYVQNLNLLQC
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Q70RM6
C4K7K9
GREA_HAMD5
Transcript cleavage factor GreA
Candidatus Hamiltonella
MTQIPMTLRGAEKLREELQHLKSVLRPQIIAAIAEAREHGDLKENAEYHAAREQQGFCEGRIQEIESKLSHAQIIDVTKIANKGIVIFGATVTVLNTHSEEKKIYQIVGDDEANFKKDLISVNSPIARGLIAKKISDVAVIHTPGGEVEYEILDVKYC
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
C4K7K9
Q8NR60
MOAA_CORGL
Molybdenum cofactor biosynthesis protein A
Corynebacterium
MTTRLYLSPTPPRNDREGASKSTSASIKHDAYLPPADGNRVLVDRFGRIARDLRVSLTDRCNLRCTYCMPAEGLEWLPTEQTLNDAEVLRLIRIAVVKLGIRQIRFTGGEPLLRKNLEDIIAGTAALRTDEGEKVHIALTTNGLGLDKRIAGLKEAGLDRVNISLDTIDAERYVSLTRRDRLSGVLASIDAAVAAGLHPVKINAVVMPGVNEVDIVPLAEYCISKGSQLRFIEQMPLGPREQWKRGDMVTAEEILARLEEKFTLSPAKEPRGAAPAALWNVVDKSNPDITGQIGIIASVTHPFCGDCDRSRLTTDGTIRNCLFSRTETPLRDALRDGASDDELAQLWAGAMWEKKPGHGIDDEGFLQPDRPMSAIGG
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Q8NR60
P38624
PSB1_YEAST
Proteinase YSCE subunit PRE3
Saccharomyces
MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity.
P38624
Q9MTM8
PSBM_OENEH
Photosystem II reaction center protein M
Oenothera
MEVNILAFIATALFILVPTAFLLIIYVKTVSQSD
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. This subunit is found at the monomer-monomer interface.
Q9MTM8
B6J4I8
SYE2_COXB1
Glutamyl-tRNA synthetase 2
Coxiella
MMKSRFCPSPTGLMHLGNARTALFNYLFAKSKDGIFLLRIEDTDVERSKETFDLGLQEDLRWLNLEWQEGPGADEGNGPYHQSKRQAIYDDYYQRLEEADQAYPCFCSEEQLRLSRKIQRSAGKPPRYAGTCRSLSAAEIEKKKAEGLQPALRFRVPDDEVVVFADLVRGEQRFQTNDIGDFIIRRANGTSPFMFCNAIDDALMGVSHVLRGEDHLTNTPRQLLILQALELPVPTYAHIALIVGPDGSPLSKRHGSRGIKELRDNGYLPLALTNYLARLGHYYASDELLSLAELAKGFNVESLSKSPVKFNAQQLDYWQKQTVNQLPNDDFWEWAGSELQSQIPTDKADLFLTTVKPNVSFPRDVAYWVNVCFGKTLNLETAQSELLRATGNRYFEEAFEAFKKFGKDLNSVVSHLKEKLNLKGKPLYQPLRIALTGAEHGPELAKLILIMDYETIQNRLQEACQ
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).
B6J4I8
Q3K3T3
GRPE_STRA1
HSP-70 cofactor
Streptococcus
MSEEIKKDDLQEEVEATETEETVEEVIEEIPEKSELELANERADEFENKYLRAHAEMQNIQRRSSEERQQLQRYRSQDLAKAILPSLDNLERALAVEGLTDDVKKGLEMTRDSLIQALKEEGVEEVEVDSFDHNFHMAVQTLPADDEHPADSIAEVFQKGYKLHERLLRPAMVVVYN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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.
Q3K3T3
B3QKH1
KTHY_RHOPT
dTMP kinase
Rhodopseudomonas
MVQKKPINRSLRGRFITFEGGEGAGKSTQIRLLAKRLEKARLRTLVTREPGGSPGAEAIRSALLAGIGKLIGGADAEALLFAAARDDHVRTLIEPALARGEWVLCDRFYDSTRAYQGKLGAVSLDLLNALQQVTIGDMKPDLTVILDIPVEIGLARAAVRRGSETPDRFESEAIDFHRGLREVFRQIAAQEPERCALIDANAEPEEVADRIWQAVRLRLLEPARAGAKSA
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
B3QKH1
A2BMC7
RNP1_HYPBU
Rpp29
Hyperthermus
MKRTAWNIVFHSLIGLRARVLATSDPGLRGLEGVVVEETRHSLVVETRDGRRVRVLKANSIFLFQLPGGSWVVVRGEEIAGSLAERVKRLGRLKGVGWLVRAGEKRRYTRG
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
A2BMC7
B2KAM4
DNAA_ELUMP
Chromosomal replication initiator protein DnaA
Elusimicrobium
MNNIINEDLKNRILKEMETVFGVEACETWLKPLSLSLKNDILTVTLPNKFWSKTIADKYVQEVKSSIEKEQGGDIQIKYDVLEDTTPYKRPEIPPQVMGANYNAKIPFPSRLNPNYTFEGFIEGPSNRFAYRAAEAVVKKLGERENNPLVIYSTPGLGKTHLLHAIGNRILKENPYAKILYMSGEEFVSEYIESLQNRNPEAFRKKHRSLDCFLMDDIQFVAGKESSVQEFFYTFNALFESKKQIVLTSDRTPQQLGIDPRLSSRLLSGIVSEIKRPDLETRIAILRQKRDTSNFDVGDDVIAFIAEGVQASIRELEGCLFRLTTYCNIHGVTPTIPIAREVLSDIISMEEKRLLINPNSIKKVVSKHFKIDIIDFNSKRKNHSIAWPRQIAMYLATELTDMSLPEIGREFERDHSTVVHAREKIKEEIENDPFFAAQINQIISDIKAVDKR
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
B2KAM4
B5QWW9
FDHE_SALEP
Protein FdhE
Salmonella
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLRMDLTARIKDANDQGKPPLDIHVLPRDKHWHTLLHSMIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE
Necessary for formate dehydrogenase activity.
B5QWW9
A7MYD3
NHAA_VIBC1
Sodium/proton antiporter NhaA
Vibrio
MNDVIRDFFKMESAGGILLVIAAAIAMTIANSPLGESYQAMLHTYVFGMSVSHWINDGLMAVFFLLIGLEVKRELLEGALKSKETAIFPAIAAVGGMLAPALIYVAFNAGDPEAISGWAIPAATDIAFALGIMALLGKRVPISLKVFLLALAIIDDLGVVVIIALFYTGDLSTMALLVGFAMTGVLFMLNAKEVTKLTPYMIVGAILWFAVLKSGVHATLAGVVIGFAIPLKGKKGEHSPLKHMEHALHPYVAFGILPLFAFANAGISLEGVSMSGLTSMLPLGIALGLLVGKPLGIFTFSWAAVKLGIAKLPQGVNFIHIFAVSVLCGIGFTMSIFISSLAFANVSPEFDTYARLGILMGSTTAAIIGYVLLHFSLPKKAVEEVASEKNA
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
A7MYD3
Q9U4X3
SODC_DROYA
Superoxide dismutase 1
Sophophora
MVVKAVCVINGDAKGTVFFEQESSETPVKVSGEVCGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVSITDSKITLFGADSIIGRTVVVHADADDLGKGGHELSKSTGNAGARIGCGVIGIAKV
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Q9U4X3
B7UN10
MUKB_ECO27
Structural maintenance of chromosome-related protein
Escherichia
MIERGKFRSLTLINWNGFFARTFDLDELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLHFRNTTEAGATSGSRDKGLHGKLKAGVCYSMLDTINSRHQRVVVGVRLQQVAGRDRKVDIKPFAIQGLPMSVQPTQLVTETLNERQARVLPLNELKDKLEAMEGVQFKQFNSITDYHSLMFDLGIIARRLRSASDRSKFYRLIEASLYGGISSAITRSLRDYLLPENSGVRKAFQDMEAALRENRMTLEAIRVTQSDRDLFKHLISEATNYVAADYMRHANERRVHLDKALEFRRELHTSRQQLAAEQYKHVDMARELAEHNGAEGDLEADYQAASDHLNLVQTALRQQEKIERYEADLDELQIRLEEQNEVVAEAIERQEENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYNQAIAALNRAKELCHLPDLTADSAAEWLETFQAKELEATEKMLSLEQKMSMAQTAHSQFEQAYQLVVAINGPLARNEAWDVARELLREGVDQRHLAEQVQPLRMRLSELEQRLREQQEAERLLADFCKRQGKNFDIDELEALHQELEARIASLSDSVSNAREERMALRQEQEQLQSRIQSLMQRAPVWLAAQNSLNQLSEQCGEEFTSSQDVTEFLQQLLEREREAIVERDEVGARKNAVDEEIERLSQPGGSEDQRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPSRHAIVVPDLSQVTEHLEGLTDCPEDLYLIEGDPQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPEVPLFGRAARESRIESLHAEREVLSERFATLSFDVQKIQRLHQAFSRFIGSHLAVAFESDPEAEIRQLNSRRVELERALSNHENDNQQQRIQFEQAKEGVTALNRILPRLNLLADDSLADRVDEIRERLDEAQEAARFVQQFGNQLAKLEPIVSVLQSDPEQFEQLKEDYAYSQQMQRDARQQAFALTEVVQRRAHFSYSDSAEMLSGNSDLNEKLRERLEQAEAERTRAREALRGHAAQLNQYNQVLASLKSSYDTKKELLNDLQRELQDIGVRADSGAEERARIRRDELHAQLSNNRSRRNQLEKALTFCEAEMDNLTRKLRKLERDYFEMREQVVTAKAGWCAVMRMVKDNGVERRLHRRELAYLSADDLRSMSDKALGALRLAVADNEHLRDVLRMSEDPKRPERKIQFFVAVYQHLRERIRQDIIRTDDPVEAIEQMEIELSRLTEELTSREQKLAISSRSVANIIRKTIQREQNRIRMLNQGLQNVSFGQVNSVRLNVNVRETHAMLLDVLSEQHEQHQDLFNSNRLTFSEALAKLYQRLNPQIDMGQRTPQTIGEELLDYRNYLEMEVEVNRGSDGWLRAESGALSTGEAIGTGMSILVMVVQSWEDESRRLRGKDISPCRLLFLDEAARLDARSIATLFELCERLQMQLIIAAPENISPEKGTTYKLVRKVFQNTEHVHVVGLRGFAPQLPETLPGSDEAPSQAS
Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organize and compact chromosomes. May achieve or facilitate chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division.
B7UN10
Q6D2S4
NUOI_PECAS
NDH-1 subunit I
Pectobacterium
MTLKELVVGFGTQIRSICMVGSNAFKKRETRMYPEEPVNPPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETKDGRWYPEFFRVNFSRCIFCGFCEEACPTTAIQLTPDFEMGEYKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKDKGEAENEAKPIDVKGLLP
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.
Q6D2S4
Q4R532
SYNG1_MACFA
Transmembrane protein 90B
Macaca
MDGIIEQKSMLVHSKISDAGKRNGLINTRNLMAESRDGLVSVYPAPQYQSHRVGASTVPASLDSSRSEPVQQLLDPNTLQQSVESRYRPNIILYSEGVLRSWGDGVTTDCCETTFIEDRSPTKDSLEYPDGKFIDLSADDIKIHTLSYDVEEEEEFQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDLHQASTSSRRALFLAVLSITIGTGVYVGVAVALIAYLSKNNHL
May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
Q4R532
Q4UXM5
SYD_XANC8
Aspartyl-tRNA synthetase
Xanthomonas
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPAEGDANSAEVFKVAASLGYEDVLQVEGVVRARHAVNDKIRTGKVEVIATRITILNKAAPLPFHAHENPGEDTRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVELAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKTSEFPVFAAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYSKLSETGEVSSPIAKFFGEEAFAALLAHVGAANGDIVFFGAGSYNKVSDFMGALRLKAGKDFGLVAAGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAAEQLAEVHVQVRPKQA
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Q4UXM5
Q6KID0
FOLD_MYCMO
Methenyltetrahydrofolate cyclohydrolase
Mesomycoplasma
MIILDGKKLSQKDTIFLKEKVNQFKIKPVFTIVQVGNLFSSNKYIKTKMDKALEIGVVSRLIKIPESISEKDLISIIEEESKISHGLIVQLPLPLQFDQSKILNSVPITKDIDGLSEKNSKNLYSGKSCIQPATARGIIDLIKEYNFTIKDKKVYVIGESNLVGKPIKELFKQAGAIVKSFNINTGIKGSEEADILIVAAGHPNLVKPENVKNNSIVIDVGINSIGENDKMIVTGDVDFSNVKTKVKAISPVPGGVGPMTVISLFKNLIEIFEKYLLDDN
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Q6KID0
Q8FW67
GATA_BRUSU
Glutamyl-tRNA(Gln) amidotransferase subunit A
Brucella
MSELTALTIAEARDKLKAKAITATELTDAYLSAIDAANDAINAYVAVTHDQARSMAKASDERIAKGEAGALEGIPLGVKDLFATKGVHTQACSHILDGFKPEYESTVTANLWADGAVMLGKLNMDEFAMGSSNETSYYGPVKNPWRAKGSNADLVPGGSSGGSAAAVAAHLCAGATATDTGGSIRQPAAFTGTVGIKPTYGRVSRWGTVAFASSLDQAGPIARDVRDAAILMKSMASLDLKDTTSVDLPVPDYEAALGRSVKGMKIGIPREYRVDGMPGEIEELWQKGIQYLKDAGAEIVDISLPHTKYALPAYYIVAPAEASSNLARYDGVRYGLRVPGKDIADMYEQTRAAGFGKEVKRRIMIGTYVLSAGYYDAYYLRAQKVRTLIKKDFEDVFAKGVDAILTPATPSAAFGLADEVLANDPVKMYLNDIFTVTVNMAGLPGIAVPGGLNGQGLPLGLQLIGRPFEEETLFQAAHVIEQAAGRFTPAKWW
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q8FW67
B2S6R2
RSMH_BRUA1
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Brucella
MASLGGDNSQAEGAEVRHVPVLIAEVIDALKPAPGAVIVDGTFGAGGYTRRILETGADVIAIDRDPTAIEAGRAMEKEFPGRLNLVESRFSALDEAVARMSGAGKKVDGVVLDIGVSSMQIDEAERGFSFQKDGPLDMRMSSRGPSAADAVNRLKTGDLARIFNFLGEERHAGRIARMIEKRRAAKPFTRTLDLANAIETLVGRNPKDRIHPATRVFQALRVYVNDELGELARALLAAERILKPGGRLVVVTFHSLEDRMVKRFFADRAGGSAGSRHMPETHMRLPSFTPAVKGAVGPTPEEEERNPRARSAKLRAGIRTENPPLEDDLSLFGLPKLPETNELARS
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
B2S6R2
A2C6G3
PSBX_PROM3
Photosystem II reaction center X protein
Prochlorococcus
MTASLANYLSSLVWAAVIVVIPAAVALVLISQNDQMYRK
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
A2C6G3
B2GC12
DAPB_LIMF3
4-hydroxy-tetrahydrodipicolinate reductase
Limosilactobacillus
MTKVLIAGFAGAMGQQAVTLVKSLPGFELSAVVGHHLTDLDPTSYGLENSTTVYADREQVETGAADIWLDFTVPAAVFENVSYALRHGMAPVVGTTGLSDEQVEELQQLAKQNGLGGLIAPNFGMSAVLLMKFAKEAAAYFPEVEIIEMHHEDKKDAPSGTALATAKLISENRPAHETAPDSTESLPGARGGDYQGIKLHAVRLPGYVAHEQVLFGGSGEALTIRQDSFDRSSFMSGVKVGLEKVGTLTELVVGLENVL
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
B2GC12
P19389
GIA2_GIAIN
Giardin subunit alpha-2
Giardia
MPKLSQIVADMKQAIDAKDEAQIAFIASEYSADARQRIAQGYRDQYGKELPDDIKKALKGGSEESLLMDLFSDRHEVRAQHIRDALSGKNDHMAFFDTVILCTPEDWHETVAAYTRMFKKPLVEDFMKDVGRKENWCLFMEKWMAHERTSREGSPDEEAEKLNKAFSESDHDYISSFMAGVPPEEYKSINTSFKSLTGKGIDQAFATIYTGTDYYSLYCAHFALLGMHKLAAYLVNCACNDKGDEKRMRRITGMMVDKCLAAKYAYKTYGSMKADVERCFDKRMAPILCTLWRLRE
Giardins are involved in parasite attachment to the intestinal mucosa and in the cytoskeletal disassembly and reassembly that marks the transition from infectious trophozoite to transmissible cyst. They may interact with other cytoskeletal proteins such as microtubules in the microribbons or crossbridges, to maintain the integrity of the ventral disk.
P19389
Q46GA5
RL14_METBF
50S ribosomal protein L14
Methanosarcina
MKGIRSNIPRALNAGAKVPCVDNTGAKVVEIISVKKYRGVKNRMPCAGIGDMCVVSVKKGTPEMRKQVLLAVVVRQKQEFRRPDGLRVSFEDNAMVITDEEGIPKGTDIKGPIAREVAERYPKIGTTASIIV
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Q46GA5
Q03974
LIC2A_HAEIN
Lipooligosaccharide biosynthesis protein lex-1
Haemophilus
MSAIENIVISMENATERRKHITKQFESKKLSFSFFNAYTYQSINQSINQSINQSINQSINQSINQSINQSNSILHNIEESRILTKGEKGCLISHFLLWNKCVNENFEYLKIFEDDVILGENAEVFLNQNEWLKTRFDFNDIFIIRLETFLQPVKLEKQTKIPPFNSRNFDILKSTHWGTAGYIISQGAAKYVIEYLKNIPSDEIVAVDELIFNKLVDVDNYIVYQLNPAICIQELQANQSKSVLTSGLEKERQKRSKIRKKKTLKQRLTRIKENIIRALNRKKWKEQQRIKEMQGKEIVRFM
Involved in extracellular lipooligosaccharide (LOS) biosynthesis and virulence expression. Involved in the synthesis of the oligosaccharide moiety of the LOS molecule by adding GalNAc.
Q03974
A1A3H8
RL9_BIFAA
50S ribosomal protein L9
Bifidobacterium
MAETKVILTKSVNHLGHPGDVVAVKSGYARNYLFPQGLAFAWSKGAAAQIEAMKRARLAKAVATREEAVAAKEIIEGSTVEIAAKVSESGKLFGGISAEKIAIALSSKVEVNPKNITVEPIKTTGDFPATVALHPEITANFFVKVVAE
Binds to the 23S rRNA.
A1A3H8
Q5ZL95
TET5C_CHICK
Terminal nucleotidyltransferase 5C
Gallus
MASKGSNTDCMSCSVLNWEQVSRLHEVLTEVVPIHGRGNFPTLKITLKDIVQTVRSRLNEAGIAVHDVRLNGSAAGHVLVKDNGLGCKDLDLIFQVSLPSEAEFQLVRDVVLRSLLNFLPEGVSKLKISPVTLKEAYIQKLVKVSTESDRWSLISLSNKHGRNVELKFVDCIRRQFEFSVDSFQIILDSLLFYYDYSENPMSEHFHPTVIGESMYGDFEAAFDHLQNKLIATKNPEEIRGGGLLKYSNLLVRDFRPMDKDEIKTLERYMCSRFFIDFPDILDQQRKLETYLQNHFSKEERSKYDYLMILRRVVNESTVCLMGHERRQTLNLISLLALKVLAEQNIIPNATTVTCYYQPAPYVSDVNFSNYYLANPPVPYSQSYPTWLPCN
Catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and enhances mRNA stability and gene expression.
Q5ZL95
P06634
DED1_YEAST
Defines essential domain protein 1
Saccharomyces
MAELSEQVQNLSINDNNENGYVPPHLRGKPRSARNNSSNYNNNNGGYNGGRGGGSFFSNNRRGGYGNGGFFGGNNGGSRSNGRSGGRWIDGKHVPAPRNEKAEIAIFGVPEDPNFQSSGINFDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLMACAQTGSGKTGGFLFPVLSESFKTGPSPQPESQGSFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLYVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEILTEANQEVPSFLKDAMMSAPGSRSNSRRGGFGRNNNRDYRKAGGASAGGWGSSRSRDNSFRGGSGWGSDSKSSGWGNSGGSNNSSWW
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing.
P06634
Q5F9J2
PYRF_NEIG1
OMP decarboxylase
Neisseria
MNPLITDFQTPQQRTPVIVALDFANEKDTLGFVRNLDPALCQIKIGKELFTATGRSLAESLIHQGFKLFLDLKYHDIPHTVAQACKVAADMGVWMVDMHASGGRRMMEAAAEAVAGYGTKPLLIGVTVLTSMEQSDLAEIGLNTAPEEQVIRLAKLAQSSGLDGVVCSAQEAAPLRRELGRDFVLVTPGIRLDVAGNNDDQRRIMTPAEALAAGSTYLVMGRPVTRAADPVAVLREVNRVANLEAN
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Q5F9J2
P70689
CXB6_MOUSE
Connexin-30
Mus
MDWGTLHTVIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETARKFIRGEKRNEFKDLEDIKRQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTVFMISASVICMLLNVAELCYLLLKLCFRRSKRTQAQRNHPNHALKESKQNEMNELISDSGQNAITSFPS
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
P70689
A0LDX4
ARGB_MAGMM
NAG kinase
Magnetococcus
MPMRNQVEKVKVLIEALPYMRRFEGKTFVIKYGGNAMVDEDLKSAFAQDVILMRQVGINPIIVHGGGPQIGLIMKRMGLEPKFIDGLRVTDEDTMSVVEMVLAGKVNKDIVNLINLNGGRAAGLSGKDGYTIQARKRTHVRKGPDVQVPEIIDLGWVGDVERIETNLLDRFRASDIIPVVAPVGVGANGETYNINADSVAGHIAIAMQAEKLILLTDVPGVQDKNGTLINQIDETDVDKLIRNGTVTGGMIPKLETCRTAHTGGVNASHIIDGRVEHALLLEIFTDSGIGTVLR
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
A0LDX4
Q6M0Z5
PURT_METMP
Phosphoribosylglycinamide formyltransferase 2
Methanococcus
MVGTPLFSNAKKILLLGSGELGKEVIIEAQRFGVECIAVDSYENAPAMQVAHKYHIIDMKDAGALRAVIEKEKPDLIVPEIEAINTDTLKEMESEGYHVVPTANATKLTMDREGIRRLAFEKLGLRTAKYEFAENLEELKEAVTRIGIPCIIKPIMSSSGKGQSTIKSESDIKTAWNYAKSAARGIGTKVIVEEFIKFDYEITLLTARTAEGTRFCEPIGHIQVDGDYHESWQPHPMCAPTKAKAQEMAKKITDELGGYGIFGVELFVLDDEVIFSEVSPRPHDTGMVTMVTQKMSEFEIHARAILGLPVNVDIVSPGASHVIKSEILKWAPEYEIHEASKVKDTKIRLFGKPIAKVGRRMGVALAVSDDVIKAREHAEKVAHLVKIK
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Q6M0Z5
A7X3N3
PCKA_STAA1
Phosphoenolpyruvate carboxykinase (ATP)
Staphylococcus
MSVDTYTETTKIDKLLKKPTSHFQLSTTQLYNKILDNNEGVLTELGAVNASTGKYTGRSPKDKFFVSEPSYRDNIDWGEINQPIDEETFLKLYHKVLDYLDKKDELYVFKGYAGSDKDTMLKLTVINELAWHNLFAKNMFIRPESKEEATKIKPNFTIVSAPHFKADPEVDGTKSETFVIISFKHKVILIGGTEYAGEMKKGIFSVMNYLLPMQDIMSMHCSANVGEKGDVALFFGLSGTGKTTLSADPHRKLIGDDEHGWNKNGVFNIEGGCYAKAINLSKEKEPQIFDAIKYGAILENTVVAEDGSVDFEDNRYTENTRAAYPINHIDNIVVPSKAAHPNTIIFLTADAFGVIPPISKLNKDQAMYHFLSGFTSKLAGTERGVTEPEPSFSTCFGAPFFPLHPTVYADLLGELIDLHDVDVYLVNTGWTGGKYGVGRRISLHYTRQMVNQAISGKLKNAEYTKDSTFGLSIPVEIEDVPKTILNPINAWSDKEKYKAQAEDLIQRFEKNFEKFGEKVEHIAEKGSFNK
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
A7X3N3
Q9I589
CBPD_PSEAE
Protease LasD
Pseudomonas
MKHYSATLALLPLTLALFLPQAAHAHGSMETPPSRVYGCFLEGPENPKSAACKAAVAAGGTQALYDWNGVNQGNANGNHQAVVPDGQLCGAGKALFKGLNLARSDWPSTAIAPDASGNFQFVYKASAPHATRYFDFYITKDGYNPEKPLAWSDLEPAPFCSITSVKLENGTYRMNCPLPQGKTGKHVIYNVWQRSDSPEAFYACIDVSFSGAVANPWQALGNLRAQQDLPAGATVTLRLFDAQGRDAQRHSLTLAQGANGAKQWPLALAQKVNQDSTLVNIGVLDAYGAVSPVASSQDNQVYVRQAGYRFQVDIELPVEGGGEQPGGDGKVDFDYPQGLQQYDAGTVVRGADGKRYQCKPYPNSGWCKGWDLYYAPGKGMAWQDAWTLL
Binds chitin but does not hydrolyze it, has no detectable protease or staphylolytic activity.
Q9I589
B4F6K2
GLO2_XENTR
Glyoxalase II
Silurana
MMLFGCRRSLWCALSFLGAAAGYRVGSAYLGTSVLQNQTPFELRNSKVVTQCTMKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNSTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGERDPISTMGAIRKEKDHFKVPKD
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
B4F6K2
Q54LU5
BZPN_DICDI
Probable basic-leucine zipper transcription factor N
Dictyostelium
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
Probable transcriptional regulator.
Q54LU5
Q35905
RMAR_SACPA
Ribosomal protein VAR1, mitochondrial
Saccharomyces
MKLRLLNMILSMMNKTNNNNNNNINNKKLLLKNMLLDMNNKRMNNMKTMLKNNNMNINNKLQHLNNMNNWNTQIYNYNKNMEIMNIMNDKLINKLLYKMMTLKLNNMNINKIIMSKTINQHSLNKLNIKFYYYYNNDINNMNNNNNNYYMNMMNKLMNIMNNNMNNSLCNILSYYYNKKVTIESIKLSYIYLNSDIFSKYISLNDMNKYNNGILTNYQRMLNNIMPKLNDHNISMNYINNINNINNNKYNNMINLLNNNNNNNNNNNNNNNNYIDNINNIYNNMTIDNIPMDILMYKYLVGWSIKFKGRLNNNNGRTSTTNLLNGTFNNKKYLWSNINNNYKLNYIPSNHNLYNNSNINKNGKYNIKVKLNFI
Essential for mitochondrial protein synthesis and required for the maturation of small ribosomal subunits.
Q35905
P21651
RE107_YEAST
Meiotic recombination protein 2
Saccharomyces
MVARGRTDEISTDVSEANSEHSLMITETSSPFRSIFSHSGKVANAGALEESDKQILEWAGKLELESMELRENSDKLIKVLNENSKTLCKSLNKFNQLLEQDAATNGNVKTLIKDLASQIENQLDKVSTAMLSKGDEKKTKSDSSYRQVLVEEISRYNSKITRHVTNKQHETEKSMRCTQEMLFNVGSQLEDVHKVLLSLSKDMHSLQTRQTALEMAFREKADHAYDRPDVSLNGTTLLHDMDEAHDKQRKKSVPPPRMMVTRSMKRRRSSSPTLSTSQNHNSEDNDDASHRLKRAARTIIPWEELRPDTLESEL
Essential for meiotic chromosome segregation. MER1 and MER2 proteins must interact directly or indirectly. MER1 might be responsible for regulating the MER2 gene and/or gene product. MER2 is not required for mitosis and mitotic DNA repair mechanisms. Component of the MER2-MEI4-REC114 complex which seems to be required for meiotic double-strand break (DSB) formation.
P21651
Q9VWR8
DPY19_DROME
C-mannosyltransferase dpy-19 homolog
Sophophora
MREPNLYVILSHALIGCGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYVLPELVTAYFFHVVRSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCICIGRIIHRQRHTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTALVNAFVLDYSLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRQLRHVRSRRLGHAQDLLNGDLFSLKFLMLTLLLASSVQTTLIELFNRAGVVSVTEGDQQHFFDICAHWALQVNVGFVAHLSACNPQYARVAWSELWQLVKTMIVKPYCMYGVVMLAMFFRRWRKSGAPVSALTEEQRERARKYVLEDFIEEHFVSMSDMSSKETEKQLYKCFRLLKSCDYDYERYKRAQASLRKEQPPARDDFMQDIKRLRAQINRNSVKQRKERAQETKEAATDGASTPTEEEDKDPEAESESKKKNQEPGSGETETESAADPTETPPSRSADNEEEEEEHSATAAGCGSNSSGHRQRKRSSSRRSSVVPTANAQILNMHYVYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAPTVCSKLWYHRQRNIFWSVSLAVFLLSMFDPGMVNIREEYFPTRYSKSGDDLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDIYNQCAQLKIQYLIISLDECTNEVRDDCDLLAIWDDKQPAYQKYPQFCHELLHKNVPSFLKVFANDHYGIIKMFSQSVQINLKHNKMPEMSI
Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.
Q9VWR8
Q48AT5
PEPQ_COLP3
Proline dipeptidase
Colwellia
MTTLNAKLASQYPAHIAQLQQMTKSVLSRENLEGLVIHSGQEVKAFLDDNCYPFKVNPHFKYWLPLIDIPNSWLVVNGEDKPTLIYYQPVDFWHKVTPLAESYWGEFFNIKILTKASEVDKLLPYDKKGFAYIGSHIEVATALGFEAINPEPLLNYVHYHRGYKSKYEHECLRQSNALAVKAHQAARNAFLQGDSEYDIQQAYLKSIGYGTNDTPYGNIVALNKNCSILHYMSLDKMTPQVHQSFLIDAGANFNGYSADITRTYSYKNDKFAELIARMDQLMLNAVAGLKPGVSYVDLHIETHRAIGQVLRDFNFINVDADTAVESGIISTFFPHGLGHHLGLQVHDVGGFMADERGTHVNTPAEHPFLRTSRVIETNQVFTIEPGLYFIDSLLADLKASANADQVNWQNVDEMRCFGGIRIEDNIIVHQSHNENMTRDLGLS
Splits dipeptides with a prolyl residue in the C-terminal position.
Q48AT5
B2A383
RRF_NATTJ
Ribosome-releasing factor
Natranaerobius
MDSIFKDAEQKMKKALSSLKSELASLRAGRANPSILEGINVDYYGMATPLNQLANISAPEPRLLVVQPYDKSAIEDIEKAILKSDVGLTPNNDGQVIRLAVPQLTEERRNELVKIVRQKGEDTKVVVRNVRRDANDELKKLEKEKEISEDESIRGQDEIQKITDKYIKKIDEVMNAKEEEITSF
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
B2A383
A7GVZ2
SYT_CAMC5
Threonyl-tRNA synthetase
Campylobacter
MSEIIAYKLNGELIDTQSINGREAVAQPVYFDNSPDALHVIRHSCAHLMAQAIKSLYPNAKFFVGPNVEDGFYYDFRVDEAGTKLGESDLEAIEKKMKELAEAKFEITKICSTKAAMSEKFKNDDLKQEVLKRIPEGEVSSYAQGDFEDLCRGPHVPNTKFLRFFKLTRVAGAYLGGDETREMLNRIYGTAYADKASLAEHIRIIEEAKKRDHRKLGVEMKLFGFDEEVGGGLPIWLPNGGRLRSKLEQILYKAHRDRGYEPVRGPELLKADVWKRSGHYANYKENMYFTTIDDAEYGIKPMNCVGHIKVYQTEIRSYRDLPLKFFEYGVVHRHEKSGVLHGLFRVREFAQDDSHIFCMPSQIKQNILEILSFAGKIMQNFGFEYEMEISTKPAKAIGSDEIWDIATNALKEALDENGFKYGIDEGGGAFYGPKIDIKITDALKRKWQCGTIQVDFNLPERFDLGYIDANNERQRPVMLHRALLGSFERFIGILIEHTAGELPFFIAPTQVVIVPISDAHLDYAKEIARELRKFNIDSEVASKNESLNKRIRTAEKQRVPMIIVLGDNEVANRSVALRDRQARTQSDMSLAEFLNLTKEKLSEVHF
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
A7GVZ2
Q17WC3
RL19_HELAH
50S ribosomal protein L19
Helicobacter
MKNRYIQQFEDAQLKDKVMPQFKAGDTLRLGITIKEGEKTRTQYFEGVCIAIRGNGVDKTFRVRKMGANNIGVEKIFPFYSESLASVEVLRVGRVRRAKLYYLRDRRGKAARIKEIRH
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Q17WC3
Q03XY9
RISB_LEUMM
6,7-dimethyl-8-ribityllumazine synthase
Leuconostoc
MIYKAKLIDQTNKKIAIVASKFNDLIVKQLISGAQESLEMHGIDESNIDIIWVPGALEIPMVAKRIAQVQKYDGIVTLGAVIKGDTDHYDLVINGVANGISQISLSTDVPIVFGVLTTDTLEQAQQRSGAKSGNKGAEVALSLLELINIFEQIKSI
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Q03XY9
Q9S9Z8
14311_ARATH
General regulatory factor 11
Arabidopsis
MENERAKQVYLAKLNEQAERYDEMVEAMKKVAALDVELTIEERNLLSVGYKNVIGARRASWRILSSIEQKEESKGNEQNAKRIKDYRTKVEEELSKICYDILAVIDKHLVPFATSGESTVFYYKMKGDYFRYLAEFKSGADREEAADLSLKAYEAATSSASTELSTTHPIRLGLALNFSVFYYEILNSPERACHLAKRAFDEAIAELDSLNEDSYKDSTLIMQLLRDNLTLWTSDLEEGGEQSKGHNQQDEN
Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Q9S9Z8
Q9KQS9
DBHB_VIBCH
DNA-binding protein HU-beta
Vibrio
MNKTQLVEQIAANADISKASAGRALDAFIEAVSGTLQSGDQVALVGFGTFSVRTRAARTGRNPKTGEEIKIAEAKVPSFKAGKALKDACN
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Q9KQS9
Q8R778
DDL_CALS4
D-alanylalanine synthetase
Caldanaerobacter
MLKVAVMFGGKSVEHEVSIITGLQVIENMNKEKYEPIPVYVGRDGRWYTGKGLLDISNYKDIPSLLKKCEQVVLPPVPGLNKLYYYPFRKKFMSKEYDYIDVDVIFPAFHGTHGEDGTMQGLFQLANIPYVGSGVVGSATGMDKVIMKDIFKANNLPIVNYLWFLRKEYEKNKEAMLDLIESKLKYPMFVKPANLGSSIGISKAKNRDELFDAIEIAIYYDRKIIVEEAVKDPMEVNCSVMGIDRDLEISLCEMPVPWEEFLSYQDKYMRKEKGGKGSTTRQIPAPIPEEKTKEIQELAKKVFQILDCSGLARIDFLLEKETMKVYVNEINTIPGSFAFYLWKPLGISFEKLIDRLIEYAVERHKEYARNMYTFETTLLLKAADRGTKM
Cell wall formation.
Q8R778
Q7UKU7
CLPX_RHOBA
ATP-dependent Clp protease ATP-binding subunit ClpX
Rhodopirellula
MNAEYGVGARLPAKTSLIVIRRRRGTSPQCWTHKSKESCMPTKETSNSRRGSAATKKNAFCSFCRKSYRDVGPLVEGPGDVYICAECIDLCQSILDQEQRRRGPSKSLFSDIPSPRSIVEHLDNYVIGQGSAKRVLAVAVHNHYKRLSNGADGSNGEVEIEKSNILLAGPTGSGKTLLARSLARMLNVPFAIGDATTLTEAGYVGEDVENLLLKLLHAADFDVEAAQRGILYIDEVDKIGSTNGNVSITRDVSGEGVQQSLLKMLEGTVANVPPQGGRKHPEQQYIQLDTSNILFICGGTFVGIEEIIRRRLGHRTLGFGEGANVRNEQTPGELVAQVQTEDILKFGLIPELVGRMPVISYLQPLDLEGLIQVLTEPKNSLVKQYQALFAMENCELEFTEEALHAIAKKAVDKGVGARGLRGIMEDVMLDIMYDLPEQEAGKVYTIDEAIVTGKQDLFKMPTTKSA
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Q7UKU7
Q3JVV1
MIAB_BURP1
tRNA-i(6)A37 methylthiotransferase
pseudomallei group
MTKKVYVKTFGCQMNEYDSDKMVDVLNAAEGLEKTDTPEDADIILFNTCSVREKAQEKVFSDLGRVRELKEAKPDLLIGVGGCVASQEGASIVARAPYVDLVFGPQTLHRLPQMIDARRESGRAQVDITFPEIEKFDHLPPARVEGPSAFVSIMEGCSKYCSYCVVPYTRGDEVSRPLDDVLTEVAGLADQGVREVTLLGQNVNAYRGAIAAGSAEIADFATLIEYVADIPGIERIRYTTSHPKEFTQRLLDVYAKVPKLVDHLHLPVQHGSDRILMAMKRGYTVLEYKSVIRKLRAIRPNLSLSTNIIVGFPGETDADFDKTMALVHEMSYDTSFSFIYSPRPGTPAANLADDTPRELKLKRLQHLQATIEENVARISQSMLGKVERILVEGPSRKDPNELAGRTENNRVVNFPAPSAAHPRLIGQMIDVKINHAYPHSLRGELVLAHGDASAATH
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Q3JVV1
Q3A9Z9
DTD_CARHZ
Gly-tRNA(Ala) deacylase
Carboxydothermus
MRAVVQRVKRGKVTVDGQVVSEIGPGLVALVGIRQGDGERECRYLAEKLVNLRIFEDGKGKFNYSVKDVGGEILVVSNFTVYGDTRKGRRPSFTEAAPPEVAREVFERFLDILKEQEVSVKSGIFQATMEVEIINDGPVTVIVEI
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Q3A9Z9
B2KB59
RIMO_ELUMP
Ribosome maturation factor RimO
Elusimicrobium
MAKIFTISLGCSKNLTDTEEMLGILNHKKHYLVADESEADTILINTCAFIKPAREEADREIKRASKLKAQGKIEKLIVAGCLTQKEGKSLPSKYPLVDAFIGLKGIEKIDNVIKRPKHSFCPAPDYIKAPDFKLQLTAPHSAYLKVADGCNNRCAYCTIPAIRGPFRSKSMEDIVAEAKAMEKNGVKEISLIAQDTTAYGQDIFGKPSLVKLLKKLVKIKGIEWFRIMYAYPETVTKDLLDFIACEPKICRYLDMPLQHISAPVLKAMNRRSTEDEVRAKIKLIRQIVPGMSLRTNFIAGFPGETAEDFEKLKKFIAEAKFNNVGVFAYSKEDGTPAAVMKRQVAEKIKKQRVEELVSAQSRVIDSINRKLKGKTVKVLLDNLFCGRSESDSPDIDGRVEVKGNKKYKAGDFVKVKITSAKGYNRTGKII
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
B2KB59
A1RHF4
FTSB_SHESW
Cell division protein FtsB
Shewanella
MKFFVIALIVLLGLLQYRLWSGSNSLPEYFVLQKHIAVQQEGNDKLNERNQVLKEEIIDLKSGTEAIEERARNELGMVKEGETFYRVVGGERSVSSPSQ
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
A1RHF4
P75221
MNMG_MYCPN
Glucose-inhibited division protein A
Mycoplasma
MSFTLTVIGGGHAGLEAAFIASKLGLKVNLLVLDPNHVGSCPCNPAIGGPAKGIVTREIDVLGGMQGKAADATALQYKLLNSSKGPAVQAIRAQIDKIAYQKWFRQQIDQTPNIELIAGEAVDILESNGKVKGVVLADGSELASDAVIVTTGTYLKAKTYCGSLSKEEGPDRAKRSEYLSTNLIKRGFKTLRLKTGTPPRILRESLDFSQMAVEANTTPHLAFSFTTKNYLPLEQQVICHLIHTNPQIHQLILANLKQSAVFNGSIKANGPLYCPSIEDKVFRFQDKERHQIFVEPESLSLETVYLAGFSTSFPPEVQEHIVRLLPGFKNARFQKYGYAIEYDAFSSIQLKSTLETKLIQNLYFAGQINGTSGYEEAAGQGLIAGINAALKLQRKPEFVLQRNEAYLGVMINDLVTKEISDPYRLLTSRAEHRLWLRNDNLQERLIEKSRALGLVEADVYANYLEQQQKKKQLIDYLQTTTVGQIAALKLNFKNTAQTLFDFTKRAEIKLVDLVQLLPKRFDLDVQSLNQIDIDIKYAGYIKKSEKYFKSLNNLSSVKIPLKLNYHKVPNLASEAIVKLSKIRPTDLSVASQVAGINFNDILAIKHFLDNHE
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
P75221
Q9CDM8
RS6_LACLA
30S ribosomal protein S6
Lactococcus
MTKYEILYIIRPNIDEEAKAALVERFDGILTDNGAANLESKDWEKRKLAYEINDFREGIYHIATFEAETTSEALSEFDRLAKINLDILRHMIVKVEA
Binds together with S18 to 16S ribosomal RNA.
Q9CDM8
P52391
NSHR_STRAS
Nosiheptide-resistance methyltransferase
Streptomyces
MTEPAIITNASDPAVQRIIDVTKHSRASIKTTLIEDTEPLMECIRAGVQFIEVYGSSGTPLDPALLDLCRQREIPVRLIDVSIVNQLFKAERKAKVFGIARVPRPARLADIAERGGDVVVLDGVKIVGNIGAIVRTSLALGAAGIVLVDSDLATIADRRLLRASRGYVFSLPVVLADREEAVSFLRDNDIALMVLDTDGDLGVKDLGDRADRMALVFGSEKGGPSGLFQEASAGTVSIPMLSSTESLNVSVSVGIALHERSARNFAVRRAAAQA
Specifically methylates the adenosine-1067 in 23S ribosomal RNA. Confers resistance to antibiotic nosiheptide.
P52391
Q5SKC1
HISX_THET8
Histidinol dehydrogenase
Thermus
MIYAAEEVRARFARRGLSFDPTVEEIVRGILEAVREEGDEALDRFSRDLDGYPVEEVPKRAWREAYEDLDEDLRDALETARERIEAFYREEARGGFLRAEGGGVLAQLVRPLERVGVYVPGGSAPLLSTLLMTVVPAKVAGVREVIVASPPKVHPGVLAAAWVAGADRLFAMGGAQAIAALAYGTGRVPRVDKIVGPGNRYVVAAKRLVYGTVGIDGLAGPTETMIIADGSASPRLLAADLLAQAEHGPDSEPWLLSPDRALLERVEAELSWQLQDLPRAEVARQALEKGGLVLTKDLEEAFALANLYAPEHLSLALSDPLPWLEKVQNAGGVFLGEGSPEALGDYIAGPSHVMPTSGTARFQGGLAVRDFLKVIPVVGLSEGAARELAKKGALLARAEGLEGHARSLDLRR
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Q5SKC1
Q4A044
HISX_STAS1
Histidinol dehydrogenase
Staphylococcus
MIIDKTLFLKKYLNQSSLNEDLYPIVKDICENVRLHGDDALRNYNQQFDQVETCNLEVAYQTLENAYNRLDSDLREALQQSHARIQSYQESIKWTKQQGTSDCYELYHPLERVGVYVPGGKASYPSTVLMTVTLAKVAGVKNISVVTPPQLNGIPDIVLAACYIAGVDNVYQVGGAQSIAALAYGTETLPKVDKIVGPGNQFVAYAKKYLFGQVGIDQIAGPSEIALIIDDSADLDAIAYDVFAQAEHDELARTFVISEDEALLKQLEQKIQHILPQIERQSIVQASLNDNHFLIHVNNFSEACDLMNQIAPEHASIQTVSPHDYLNHVRYVGALFLGYYSPEVIGDYVAGPSHVLPTNQTARFTNGLSVNDFLTRHSVIDLSKDTFDTVELTARKLAHVEQLYNHEQSIEIRTSKEFNDDKN
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Q4A044
A1SYT9
PROA_PSYIN
Glutamyl-gamma-semialdehyde dehydrogenase
Psychromonas
MDLQSLGKLAKEASYELAITGSEKKNAALEAIALALEANQDKIVSANKEDIQAGKEAGLTEALLDRLLLDETRLAGVVSDVRSVIKLDDPVGEEFDGKLLENGLKLSKRRVPIGVIGVIYEARPNVTIDIAVLSLKTGNACILRGGKETIRSNIVLVEVIQAALKSVGLPETSVQYIKSTDRALVGELLKMDDYVDMIIPRGNAGLQKFCKENSNIPVIVGGIGVCHLFADKSVDQEKALAIVANAKVQRPTVCNALETLLVHQDIAEEFLPKLHAHLAPMGVTLIAEEKAKAILGDKATLAEAGDFDREWLCLNLGVKVVADFHEAIMHIRTHSSGHSDGILTNDFTIANKFINVVNSAAVYINASTRFTDGSQFGLGAEVAVSTQKLHARGPMGLQELTTYKWIGIGENLIRP
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
A1SYT9
Q9ZSK5
ZOG_PHALU
Trans-zeatin O-beta-D-glucosyltransferase
Phaseolus
MALNDKSIPHETKVVVLLIPFPAQGHLNQFLHLSRLIVAQNIPVHYVGTVTHIRQATLRYNNPTSNIHFHAFQVPPFVSPPPNPEDDFPSHLIPSFEASAHLREPVGKLLQSLSSQAKRVVVINDSLMASVAQDAANISNVENYTFHSFSAFNTSGDFWEEMGKPPVGDFHFPEFPSLEGCIAAQFKGFRTAQYEFRKFNNGDIYNTSRVIEGPYVELLELFNGGKKVWALGPFNPLAVEKKDSIGFRHPCMEWLDKQEPSSVIYISFGTTTALRDEQIQQIATGLEQSKQKFIWVLREADKGDIFAGSEAKRYELPKGFEERVEGMGLVVRDWAPQLEILSHSSTGGFMSHCGWNSCLESITMGVPIATWPMHSDQPRNAVLVTEVLKVGLVVKDWAQRNSLVSASVVENGVRRLMETKEGDEMRQRAVRLKNAIHRSMDEGGVSHMEMGSFIAHISK
May regulate active versus storage forms of cytokinins, and could have an impact on seed growth. Can also use UDP-xylose to catalyze the formation of O-xylosylzeatin but at much lower affinity.
Q9ZSK5
Q54NM6
MOCS1_DICDI
Molybdenum cofactor biosynthesis protein C
Dictyostelium
MTNIIKSFITRNTYLNKLSPSPYQFNKYYSNSISTPPTHSYEKKQQPIQNVDDKKYILTDRFNRHHTYLRISLTERCNLRCKYCMPEEGVMLSQADKILTTDEIIRLSKLFVSAGVNKIRFTGGEPLVRKDVEPLIEEVGKIKGLQKIGITTNGILLSRKLDRLHKAGVNLLNISLDTLNSDKFTLITRRLGWDRVFQSIDNALKLDNIKVKVNCVIMKGLNDMEICDFVEMTRDKSVEIRFIEYMPFDGNLWSDKKFLSYTDMIKIIHEKYPTFKKYTIEEEEPNNTSKTYHVPGFKGKVGFITSMSEHFCSSCNRLRITADGNLKVCLFGNTEVNLRDRIRDGASDQQLLEIINAAVLKKKASHAGMYEIAQNKNRPMILIGEKSKIQINFKNKSIKQKKEVKNYLLKLINSSFINSNNNNNNNNNNNNNSKLQYIQQRNYSTNKNNQNLENNEFSHITKDGKLPTMVDISDKIITKRTAHAQSILEFPSNVLSQLLNLEKNNDIDNDNNISKNKEIVSKKGPVFATSIVAGTMAVKNTSNLIPFCHPIPIESCKIEITIIDSTSVKVDCIVSMSGKTGVEMEALTGATITSLTIYDMCKALSKDIVIKETKLISKFGGKSSSPQITK
Isoform mocs1a and isoform mocs1b probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). mocs1a catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and mocs1b catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP.
Q54NM6
Q5FTY3
RL3_GLUOX
50S ribosomal protein L3
Gluconobacter
MRTGLIAKKLGMTRLFKEDGTHVPVTVLHLDNVEVVDARTNERDGYTAIQLGLGNAKVKNVTKANRGHFARTKVEPKRHLAEFRVSEDALLEAGTKLSAAHFVVGQKVDVTGQSKGKGFAGVMKRHNFAGLEASHGVSISHRSHGSTGQRQDPGKVFKGKKMAGHMGDERVTTLNLEIAAVDEERNLIMVRGAIPGAKNGLVLIRDAIKKARHADAPYPAATVAAAG
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Q5FTY3
Q02454
3SA0_NAJSP
Cardiotoxin
Naja
MKTLLLTTVVVTIVCLDLEYTLKCNKLVPLFYKTCPAGKNLCYKMFMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN
Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Q02454
O08739
AMPD3_MOUSE
Heart-type AMPD
Mus
MPRQFPKLNMSDLDEHVRLLAEKVFAKVLREEDSKDVMSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPTQQDWKGPPTASPAMSPATPLVPGATSKPGPAPYAMPEYQRVTISGDYCAGITVEDYEQAAKSLAKALMIREKYARLAYHRFPRTTAQYLAHQGESVPLEEGLPDFHPPPLPQEDPYCLDDAPPNLGYLVRMHGGVLFVYDNQTMLERQEPHSLPYPDLETYIVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKLGRKITLRQVFDSLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEDSKYQYSEPRLSIYGRSPKEWSSLARWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPSPDLWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTK
AMP deaminase plays a critical role in energy metabolism.
O08739
Q6CKU1
YTH1_KLULA
mRNA 3'-end-processing protein YTH1
Kluyveromyces
MSIVHPDTSKYEFNFEPFLRKEYSFSLDPDRPVCQYYNSREGIKSCPNGARCPNKHVLPIFQNKIVCKHWLRGLCKKNDQCEYLHEYNLRKMPECVFFTKNGYCTQSPECQYLHVDHKSQLEECEDYNMGFCPSGPACTKKHVKKVLCPRYLVGFCPLGKDCDWSHPKFKVPSEHSKLRIKKDEHINTRKMDEERERRLNAIINGDILVT
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Q6CKU1
C0ZYA2
RIMP_RHOE4
Ribosome maturation factor RimP
Rhodococcus erythropolis group
MPVPSRERVIELISELVHAQGYDVEDVVVTSAGKHSAVRIMVDSDAGIELDAAAEISRLVSELFDSLEEIGETPYTLEVTSPGIDRPLTLERHWRRARGRKARIDLAGETVVGRIGTLNDDSVAVVIGGRGGLTVREIALGDVQKAVVQVEFSKPSEAELELAGGIPEGRAVPSDAVDLTDDSGVDSVEDDEAELEDVENEEGFDK
Required for maturation of 30S ribosomal subunits.
C0ZYA2
Q319V1
RNPA_PROM9
Protein C5
Prochlorococcus
MALPKDMRLKGHRTFNYIHKNSIKYHGKLMTFKVARSNPEILLSHNHTNASNNFRAAIAISKKVSKKAVDRNKIRRILQEWLITNIPKINSHKPYWLLVNLKFGDFCNDKNKLLEEFQNLMFKSRLIK
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Q319V1
A1SNK3
RL6_NOCSJ
50S ribosomal protein L6
Nocardioides
MSRIGKLPVAVPSGVDVAIDGARVTVKGPKGTLSHTVAAPITVEKGDGVLDVKRPDDERESKALHGLTRTLVNNMVVGVTEGYEKKLEIVGVGYRVLSKGPTQLEFQLGYSHPITFNAPEGITFAVEGPTRLGVQGIDKQLVGEVAANIRKLRKPEPYKGKGVRYAGEHIRRKVGKAGK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
A1SNK3
P20865
CB2_DUNSA
Chlorophyll a-b binding protein of LHCII type I, chloroplastic
Dunaliella
MQLSTPPEVPDMKNTYSNNECPAAEQELCSEQGGRAGKSTKKGAKAVSKSSSSANQFYGPDATSGWDLQHQHPRLPTGEFPGDYGWDTAGLSADPETFKRYRELELIHARCGLLGALGMVTPELLADEDGIKFGDAAIWFKAGAAIFQDGGLNYLGNPSLIHAQNIVATLAVQVVLMGLVEGYRVNGGPAGEGLDPLYPGEAFDPLGLADDPDTFAELKVKEIKNGRLAMFACLGFFVQAIVTGKGPIENLTDHLANPAENNAFAYATKFTPQ
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
P20865
Q73F89
RL16_BACC1
50S ribosomal protein L16
Bacillus cereus group
MLMPKRVKYRREHRGKMRGRAKGGTEVAFGEFGLQAQAASWITNRQIEAARRAMTRYMKRGGKVWIKIFPSKPYTAKPLEVRMGSGKGAPEGWVAVVKPGKIMFEIAGVSEEVAREALRLAAHKLPVKCKFVKREENGGESNEN
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Q73F89
B2HD59
AHPD_MYCMM
Alkylhydroperoxidase AhpD
Mycobacterium
MSIENLKAALPEYAKDLKLNLGSISRTTVLDEEQLWGTLLASAAATRNAQVLAEIGAEAADNLSAQAYQAALGAVSIMGMNNVFYRGRGFLEGQYDDLRAGLRMNIIANPGVDKANFELWSFAVSSVNGCSHCVVAHEHTLREAGVGREAVLEALKAAAIVCGVAQALTAAQTLAAVG
Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
B2HD59
B8F3E4
NDK_GLAP5
Nucleoside-2-P kinase
Glaesserella
MIQQTLAIIKPDATKRHLIGEILSYMEKNGLAIKALKMLHLTKEQTEGFYAEHQGKDFFDPLVAFMISEPIVVAVLEGENAVENYRLLMGATKPEERKLGTIRKMFGLGYRENAVHGSDSETSAKREIAYFFTPSEIV
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
B8F3E4
P99029
PRDX5_MOUSE
Thioredoxin-dependent peroxiredoxin 5
Mus
MLQLGLRVLGCKASSVLRASTCLAGRAGRKEAGWECGGARSFSSSAVTMAPIKVGDAIPSVEVFEGEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIEEWGRAHQAEGKVRLLADPTGAFGKATDLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILSQL
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
P99029
U4PAZ9
PTRN1_CAEEL
Patronin (microtubule-binding protein) homolog
Caenorhabditis
MDFPLPALLAIEDYDENEGKLAASIRWLISRVYEEKRDMPDKLRDGVQRDENGHFQIDEAVVGALCNGSLYAQAAAKIFKESALVTKGHGAVLAVLTDYGIDVLHDGNELVEEAQLVASAPFNMSAHLAIIDALMMAHLRDVIPVSRVVEAVSRHTAVEPSEKPIDSVDALLFWINKICLLVRDDVEREDSNTNIPEMEDLYEDISDGQCLCALLHWYRPHEMPVADISFNDSATTRDCQYNLMLLQLFCRHHLAVDPFHFEIEDLLYLRDSLQMNVNAFLADLFVQFEPPVTPEPVETPRIGPSPRRFVPASAIPDLRAANAAARSSMHNRNRPRMYNPPPAVSHSQGPSRSVSRMSQDSLFYSRPASIALQRRSMDQDSVTDFQTIRQGFENQAGTAQLNRYDGSVTASVRLAMEEKRRKHDQQMAQMSFSSANETERLEKSKAAFFALRKNDNDQTSKGKEEWYDHFEAKLRALELRVGLEEGEDGTQSARLNRASSQPSVVQAGQTYPANYMTLPMNAAAQMTQSYIQHPQTPHDYYMQQQMQQQQQQQAQAQSNYASPSQLRNSLSNGMINHAGYIVQSMYPGDYQQQQQQMQMQQGQMPVQPVGAYTPEGYFIPHHMQPIPVQQGYQQMPQPGMGFNGMPATSQPGFNMEGSPAQMGYIQTANKPLDMEMPMQQQPPQQPPQQMLPPNQNAFHLHSKSDDATQVQADPPLEINRNLTNWGMTYKQEMPARSIPSRRTWQNETFIKNELDLVNSKESVPHITDETTTQPEEAARRFPDLMLDNHSENLAPGRGFSRQNDRDDLSTGRKSDDSPTDTPGRTFDDDEGSGENMEKIANERRIAKKAALIAKTMKRKEEIETKVDLAEQRNAERRQVENEKKELALRKKVEKEQQRQKILDEYKRKKLEKELGAELSARSTGRGHSQPPFIRTKSQMSEVTESSRQNTPRMRGQSSVEQRVSVSSLAEPTHKLYAKTVTKSNRGLINNALQFSVFPGAVNNATRQATITQMASSSSKHFLILFRDQKCQYRGLYTWDEISDTAVKISGQGPPKCTEAMMNSMFKYDSGAKNFTNIATKHLSATIDGFAILDQYWQKARIPHSGTPAHKNN
Required for microtubule stability and anchorage by binding to the minus ends of microtubules . Acts redundantly with noca-1 to control circumferential microtubule assembly along the body which is necessary for larval development, viability, morphology and integrity of the epidermis . Promotes microtubule stability and polymerization in neurons . Involved in the maintenance of neurite morphology in ALM and PLM neurons . May play a role in synaptic protein localization in the PLM neuron . May act upstream of dlk-1 in neuronal regeneration . Plays a role in postembryonic epidermal tissue integrity and wound healing .
U4PAZ9
C9K1X6
COTB3_STRMJ
Cyclooctat-9-en-7-ol 5-monooxygenase
Streptomyces violaceusniger group
MRERGPVTPAKSSAPPERPWTTGTAPGSVPLLGHTMALWRRPLQFLASLPAHGDLVEVRLGPSRAYLACHPELVRQVLLNPRVFDKGGVFDKARQLLGNSLSVSRGEDHRYQRRMIQPAFHTPKIAAYTAAVADDTRAAIGSWEPGRTLDISDTMHALLMRVAARTLFSTGIDEATIDEARHCLRIVSDGIYKRTMAPLGIMEKLPTPGNRRYDRANARLRQIVDEMIRERRRSGADHGDLLSTLLRAEHPETGKGLDDGEVLDQVVTFLVAGSETTASTLAFVFHLLGAHPEVEKRVHAEIDEILEGRSPTFEDLPSLEYTRGVITESLRLYPPSWMAMRVTAAETELGGRTVPAGTMILYSAQALHHNPELFPDPERFDPERWLGDRAKEVERGALLPFGAGSHKCIGDVLALTETALIVATIASRWRLRPVPGTTLRPEPKATLEPGPLPMVCEPR
Involved in the biosynthesis of cyclooctatin, a potent inhibitor of lysophospholipase. Catalyzes the stereospecific hydroxylation of cyclooctat-9-en-7-ol to form cyclooctat-9-ene-5,7-diol.
C9K1X6
Q8FG03
MDTC_ECOL6
Multidrug transporter MdtC
Escherichia
MKFFALFIYRPVATILLSVAITLCGILGFRMLPVAPLPQVDFPVIMVSASLPGASPETMASSVATPLERSLGRIAGVSEMTSSSSLGSTRIILQFDFDRDINGAARDVQAAINAAQSLLPSGMPSRPTYRKANPSDAPIMILTLTSDTYSQGELYDFASTQLAPTISQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDDVRTAISNANVRKPQGALEDGTHRWQIQTNDELKTAAEYQPLIIHYNNGGAVRLGDVATVTDSVQDVRNAGMTNAKPAILLMIRKLPEANIIQTVDSIRARLPELQSTIPAAIDLQIAQDRSPTIRASLEEVEQTLIISVALVILVVFLFLRSGRATIIPAVAVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENIARHLEAGMKPLQAALQGTREVGFTVLSMSLSLVAVFLPLLLMGGLPGRLLREFAVTLSVAIGISLLVSLTLTPMMCGWMLKASKPREQKRLRGFGRMLVALQQGYGKSLKWVLNHTRLVGAVLLGTIALNIWLYISIPKTFFPEQDTGVLMGGIQADQSISFQAMRGKLQDFMKIIRDDPAVDNVTGFTGGSRVNSGMMFITLKPRGERSETAQQIIDRLRKKLAKEPGANLFLMAVQDIRVGGRQANASYQYTLLSDDLAALREWEPKIRKKLATLPELADVNSDQEDNGAEMNLIYDRDTMARLGIDVQAANSLLNNAFGQRQISTIYQPMNQYKVVMEVDPRYTQDISALEKMFVINNEGKAIPLSYFAKWQPANAPLSVNHQGLSAASTISFNLPTGKSLSDASAAIDRAMTQLGVPSTVRGSFAGTAQVFQETMNSQVILIIAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALELFNAPFSLIALIGIMLLIGIVKKNAIMMVDFALEAQRHGNLTPQEAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGSELRQPLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKPKQAVTE
The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate.
Q8FG03
Q9ZHQ1
TYLH1_STRFR
Cytochrome P-450 monooxygenase TylH1
Streptomyces
MSSSGDARPSQKGILLPAARANDTDEAAGRRSIAWPVARTCPFSPPEQYAALRAEEPIARAELWDGAPVWLISRQDHVRALLADPRVSIHPAKLPRLSPSDGEAEASRSLLTLDPPDHGALRGHFIPEFGLRRVRELRPSVEQIVTGLLDDLTARGDEADLLADFALPMATQVICRLLDIPYEDRDYFQERTEQATRPAAGEEALEALLELRDYLDRLISGKTGRESGDGMLGSMVAQARGGGLSHADVLDNAVLLLAAGHETTASMVTMSVLVLLQHPTAWRELTVNPGLLPGAVDELLRYLSIADGLRRSATADIEIDGHTIRAGDGLVFLLAAANRDEAVFSEPEAFDIHRSARRHVAFGYGPHQCLGQNLARMELEVALGAVLERLPALRPTTDVAGLRLKSDSAVFGVYELPVAW
Involved in the biosynthesis of the complex macrolide antibiotic tylosin. Catalyzes the hydroxylation of 20-oxo-5-O-beta-mycaminosyltylactone at the C-23 position to yield 5-O-beta-mycaminosyltylonolide.
Q9ZHQ1
Q7MK21
LIFO_VIBVY
Lipase modulator
Vibrio
MKKTALTIITIASGSLGAVYFLPSEPAVQKDIRATSQHDTSVDNTSPKAFLDYSLSTLGEKPWQTITQDVVSEERALGELQLDEQLFALYLRYKQALADLDIEITGSDITSLETLHQAILDLQREYFSAQQIDLIFGEENQLRALALEKARLSEQGYSAEEQKQLWRDHLALQPEYVQESDANRRLMSELAQGEDAQTTYLKRVELVGEAGAQRLEVLDQNRAEFDRVFQHYLVQRSAILDDLGLSDEQKRQQIKMLRETSFDAKQWRRIEALERIADGG
May be involved in the folding of the extracellular lipase during its passage through the periplasm.
Q7MK21
E1WFA0
PHOQ_SALTS
Sensor histidine protein kinase/phosphatase PhoQ
Salmonella
MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE
Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance (Probable).
E1WFA0
Q92P98
COBT_RHIME
N(1)-alpha-phosphoribosyltransferase
Sinorhizobium
MSASGLPFDDFRELLRNLPGPDTAALVAARERDGQLTKPPGALGRLEEIAFWLAAWTGRPPAVNRPLVAIFAGNHGVTRQGVTPFPASVTAQMVENFAAGGAAINQICVAHDLGLKVFDLALDYPTGDITEEPALSERDCAATMAFGMEAIAGGTDLLCIGEMGIGNTTIAAAINLGLYGGTAEEWVGPGTGSEGEVLMRKIAAVEKAVALHRDHLSDPLEVMRRLGGREIAAMAGAILAARMQKVPVIIDGYVATAAAAILKAANPAALDHCLIGHVSSEPGHMRAIEKLGKTPLLALGMRLGEGTGAALAAGIVKAAAACHSGMATFAQAGVSNKE
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Q92P98
Q65UK9
LEXA_MANSM
LexA repressor
Basfia
MKPIKALTARQQEVFNFLKHHIETTGMPPTRAEISRELGFRSPNAAEEYLKALARKGVVEILSGTSRGIRLLVDTEESANDEDAGLPLIGRVAAGEPILAEQHIEGTYKVDADMFKPQADFLLKVYGQSMKDIGILDGDLLAVHSTKDVRNGQVIVARIEDEVTVKRLERKGDVVYLHAENEEFKPIVVNLKEQPNFEIEGIAVGIIRNNAWM
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Q65UK9
Q6A8I4
AROC_CUTAK
5-enolpyruvylshikimate-3-phosphate phospholyase
Cutibacterium
MLRYLTAGESHGPALVATMEGIPAHVQVGAVEISEELRRRRLGAGRGARMSFEADELELLAGFRHGETLGDPLAIRIGNSEWEKWRTVMAPGPVAPEDLAGHARAAALTRPRPGHADLAGMQKYDFDEARPILERASARETAARVALGAIAKAFLKQSLGIEVLSHVVSLGPVSAPNGPRPDPSDLTRIDADPVRCADSVTSKRMVAEIEACRKEGDTLGGVVEVLAYGLPAGLGSHSQGDRRLDARLAGALMGIQAIKGVEFGDGFDLTRRRGSQAHDWMEPTEGGIHRVSDRAGGTEGGMSTGQILRVRAAMKPIATVPRALPTVDVTTGEAANAHHQRSDVCAVPAAGVVAEAMAALVLAECALEKFGGDSVTETRRNAQAYLDRLAARGLAVAP
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Q6A8I4
A5U4P1
AMPA_MYCTA
Leucyl aminopeptidase
Mycobacterium tuberculosis complex
MTTEPGYLSPSVAVATSMPKRGVGAAVLIVPVVSTGEEDRPGAVVASAEPFLRADTVAEIEAGLRALDATGASDQVHRLAVPSLPVGSVLTVGLGKPRREWPADTIRCAAGVAARALNSSEAVITTLAELPGDGICSATVEGLILGSYRFSAFRSDKTAPKDAGLRKITVLCCAKDAKKRALHGAAVATAVATARDLVNTPPSHLFPAEFAKRAKTLSESVGLDVEVIDEKALKKAGYGGVIGVGQGSSRPPRLVRLIHRGSRLAKNPQKAKKVALVGKGITFDTGGISIKPAASMHHMTSDMGGAAAVIATVTLAARLRLPIDVIATVPMAENMPSATAQRPGDVLTQYGGTTVEVLNTDAEGRLILADAIVRACEDKPDYLIETSTLTGAQTVALGTRIPGVMGSDEFRDRVAAISQRVGENGWPMPLPDDLKDDLKSTVADLANVSGQRFAGMLVAGVFLREFVAESVDWAHIDVAGPAYNTGSAWGYTPKGATGVPTRTMFAVLEDIAKNG
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
A5U4P1
A3CV22
TPIS_METMJ
Triose-phosphate isomerase
Methanoculleus
MDSPFVLVNLKTYQEGMGSNAHRIAAAAETVAKESGAVIGIAPAFTELHPMSHHYAIPVYAQHIDAITPGAHTGHILPEAVRSAGARGTLINHSERRLTLADIGACVESARRLHLETVVCTNNDATSAAAAALRPDYVAIEPPELIGSGVSVSKADPGIIERSVNAVRAVNPDVNVLTGAGIQSGECVKIAVDLGTCGVLLASSVVKADDPEAVLRDLVSLL
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
A3CV22
A3KMZ6
COX11_BOVIN
Cytochrome c oxidase assembly protein COX11, mitochondrial
Bos
MGGLWRPAWRRVVFCGWSWSHLGRPTRAAERAEPCLRPGRSGPAGTEQGLRRLGTWRRPSPAEQPARRPKSTNPYTRSQEEDWRRRNKTVLTYMAAAAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHASDQIENMVPVKDRIIKITFNADVHASLQWNFRPQQTEIYVVPGETALAFYKAKNPTDKPVIGISTYNVVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMVNVDLITLSYTFFEAKEGHTLPVPGYNSNQQLSPASNL
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
A3KMZ6
C5B780
SYP_EDWI9
Prolyl-tRNA synthetase
Edwardsiella
MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGLRVLNKVENIVREEMNYAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGDRPFVLGPTHEEVITDLVRNEISSYKQLPLNFYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTTQESLQETYEAMYAAYSRIFSRMGLDFRAVQADTGSIGGNASHEFQVLAQSGEDDIVFSTASDYAANIELAEALAPATGRAAANQPMQLVNTPDARTIAELVEQHGLPIEKTVKTLLVHASEESGHALVALLVRGDHELNEVKAEKLALVASPLTFANEAEIRALVNAGPGSLGPVNLPLPIVADRAVAAMSDFGAGANIDGKHYFGINWERDAALPQIADIRNVIEGDPSPDGKGTLLIKRGIEVGHIFQLGTKYTEALNATVQGEDGRNQLMTMGCYGIGVTRVVAAAIEQNHDERGIIWPDAIAPFQVAILPMNMHKSFRVKEVAERLYDGLRAKGIEVLLDDRKERPGVMFADMELIGIPHTIVIGDRNLDNNEIEYKYRRSGDKLMISVDEIEAFLQAQIAR
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.
C5B780
Q3BTX1
CRCB_XANC5
Putative fluoride ion transporter CrcB
Xanthomonas
MNAPVWWQQLLLAMTGGALGSGLRFAIGASLIQRFGTGFPWGTLTVNLLGSFVAGVLLVWLDARGPSSWPLRALLIVGVIGGLTTFSSLMMECLVFARTDRSTMIGIYLAVTLLAGLALVVAGARTGQWLVAR
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q3BTX1
B5ZY95
QUEF_RHILW
PreQ(0) reductase
Rhizobium
MPNTDVSSLSMLGQQTETAQSPEQAVLEKVPSNHAGTDYVVRFTAPEFTSLCPMTGQPDFAHIVIDYIPGEWLVESKSLKLFLHSFRNHGAFHEDCSIYIAKRIVELLDPKWLRIGAYWYPRGGIPIDVFWQTGKPPEGVWLPEQGVATYRGRG
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
B5ZY95
A1KCL2
RPOZ_AZOSB
Transcriptase subunit omega
Azoarcus
MARITVEDCLKRIPNRFQLTLAATYRARQLTAGGTPQIELDPHDKDKPTVIALREVAAGKVGLEMLNRGQA
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
A1KCL2
Q38UT9
ECFA1_LATSS
Energy-coupling factor transporter ATP-binding protein EcfA1
Latilactobacillus
MDENKIIEVAHLKYEYPQASRLALNDLSVSINAGEWVAIIGHNGSGKSTFAKSLNGLLDLQSGDITIDGLPLSIETVWDIRRKIGMVFQNPDNQFVGATVEDDVAFGLENQGIERTEMQRRVQDAVDRVGMTQFMTREPSRLSGGQKQRVALAGIIAQQPEILILDEATSMLDPKGRQEVLETIHTLKQETNMTVLSITHDIDEAASADRIVMLDKGQVIDQGTPAEIFAYGQRLLDLGLDVPYPEKLKAALTKLGVPMPVDYLTTERMVDHLWTLHSKM
ATP-binding (A) component of a common 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.
Q38UT9
Q6AYQ8
FAHD1_RAT
Oxaloacetate decarboxylase
Rattus
MASTKPLSRFWEWGKNIVCVGRNYADHVKEMRSTVLSEPVLFLKPSTAYAPEGSPVLMPAYCRNLHHEVELGVLLGRRGEAVPEAAAMDYVAGYALCLDMTARDVQDECKKKGLPWTLAKSFTSSCPVSAFVPKEKIPDPHALRLWLKVNGELRQEGKTSSMIFSIPYIISYVSKIITLEEGDLILTGTPKGVGAVKENDEIEAGIDGVVSMRFKVERSKY
Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro. Also has oxaloacetate decarboxylase activity.
Q6AYQ8
A4QL32
CYF_DRANE
Cytochrome f
Draba
MQTRNTFSWIREEITRSISVSLIIYIITRASISSAYPIFAQQNYENPREATGRIVCANCHLASKPVDIEVPQAVLPDTVFEAVVKIPYDMQLKQVLANGKKGALNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQNYRPNKKNILVIGPVPGQKYSEITFPILAPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAGGIISKIVRKEKGGYEITIVDPSNERQVIDIIPRGLELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLASVVLAQIFLVLKKKQFEKVQLSEMNF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
A4QL32
A3NS56
KYNU_BURP0
L-kynurenine hydrolase
pseudomallei group
MKTREEALALDRDDPLAPLREQFALPAGVIYLDGNSLGAQPRAAAARAQQVIGAEWGEGLIRSWNTAGWFALPRRLGDRLAPLIGAADGEVAITDTISINLFKLLAAMLRHQARHAPKRRVIVSERSNFPTDLYIAQGLIAQLDRDYELRLIDDPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYKYLNGGPGSPAFVWVPKRHQRAFEQPLSGWWGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQTDMHAIRRKSLALTDAFVALVESRCAGQPLKLVTPRAHHQRGSQASFEHPHGYEVMQALIARGVIGDYREPRILRFGFTPLYTRFVDVWDAVETLRDILDTEAWRAPEFATRAAVT
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
A3NS56
Q39239
TRXH4_ARATH
Thioredoxin 4
Arabidopsis
MAAEEGQVIGCHTNDVWTVQLDKAKESNKLIVIDFTASWCPPCRMIAPIFNDLAKKFMSSAIFFKVDVDELQSVAKEFGVEAMPTFVFIKAGEVVDKLVGANKEDLQAKIVKHTGVTTA
Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity.
Q39239
B7LP19
CBPA_ESCF3
Curved DNA-binding protein
Escherichia
MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQMWQHRNDPQFNRQFHHGDGQSFNAEDFDDIFSSIFGQHARQARQRPATRGHDIEIEVPVFLEETLSEHKRTISYNLPVYNAFGMVEQEIPKTLNVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLIIHIAPHPLFDVVGQDLEIVVPVAPWEAALGGKVTVPTLKESILLTIPAGSQAGQRLRVKGKGLVSKKHTGDLYAVLKIVMPPKPDENATALWQQLADAQSSFDPRKDWGKA
DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
B7LP19
P9WGY8
RPOB_MYCTO
Transcriptase subunit beta
Mycobacterium tuberculosis complex
MLEGCILADSRQSKTAASPSPSRPQSSSNNSVPGAPNRVSFAKLREPLEVPGLLDVQTDSFEWLIGSPRWRESAAERGDVNPVGGLEEVLYELSPIEDFSGSMSLSFSDPRFDDVKAPVDECKDKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTEKGTFIINGTERVVVSQLVRSPGVYFDETIDKSTDKTLHSVKVIPSRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTSEQIVERFGFSEIMRSTLEKDNTVGTDEALLDIYRKLRPGEPPTKESAQTLLENLFFKEKRYDLARVGRYKVNKKLGLHVGEPITSSTLTEEDVVATIEYLVRLHEGQTTMTVPGGVEVPVETDDIDHFGNRRLRTVGELIQNQIRVGMSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRKVVDGVVSDEIVYLTADEEDRHVVAQANSPIDADGRFVEPRVLVRRKAGEVEYVPSSEVDYMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVRSEAPLVGTGMELRAAIDAGDVVVAEESGVIEEVSADYITVMHDNGTRRTYRMRKFARSNHGTCANQCPIVDAGDRVEAGQVIADGPCTDDGEMALGKNLLVAIMPWEGHNYEDAIILSNRLVEEDVLTSIHIEEHEIDARDTKLGAEEITRDIPNISDEVLADLDERGIVRIGAEVRDGDILVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGESGKVIGIRVFSREDEDELPAGVNELVRVYVAQKRKISDGDKLAGRHGNKGVIGKILPVEDMPFLADGTPVDIILNTHGVPRRMNIGQILETHLGWCAHSGWKVDAAKGVPDWAARLPDELLEAQPNAIVSTPVFDGAQEAELQGLLSCTLPNRDGDVLVDADGKAMLFDGRSGEPFPYPVTVGYMYIMKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDTVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAIELREGEDEDLERAAANLGINLSRNESASVEDLA
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
P9WGY8
Q06GP9
YCF4_PIPCE
Photosystem I assembly protein Ycf4
Piper
MNRRSERIWIEFIMGSRKTSNFCWACILLLGSLGFLLVGISSYLGRNLISLFPSQQINFFPQGIVMSFYGIAGLFISSYLWSTILWNIGSGYDRFDRKEGIVCIFRWGFPGINRRIFLRVFMGDIQSIRIEVKGGVYPRRVLYMDIRGQGSVPLTRTDENFTPREIEQKAAESAYFLRVPIEVF
Seems to be required for the assembly of the photosystem I complex.
Q06GP9