accession
stringlengths
6
10
name
stringlengths
6
11
Full Name
stringlengths
1
147
taxon
stringlengths
3
46
sequence
stringlengths
16
2.75k
function
stringlengths
6
5.51k
AlphaFoldDB
stringlengths
6
10
C0ZB86
RECO_BREBN
Recombination protein O
Brevibacillus
MLVKWEGIVIRSVDYGESSKVVTMFTRENGKLGVMARGAKKTKSRLAAVSQLFSHSYYLCKAGPGTGMPDLSQGDMLDSFRDMRQSLTATAYAAYIAELLDRLTQEREPNPYLFQLLLHTFRHLDEGRDAEILCRIFETKMLIVAGISPQLTACANCGEQREPYAISVGQGGLLCPVCLPSDPYAMAVTPSTWKLLRLFQVFDLERLGDIEVKPATRNQLKHVLRSFMDEYLDLRLKSRSFLEQLERMERMTQSDQD
Involved in DNA repair and RecF pathway recombination.
C0ZB86
Q96T53
MBOA4_HUMAN
Membrane-bound O-acyltransferase domain-containing protein 4
Homo
MEWLWLFFLHPISFYQGAAFPFALLFNYLCIMDSFSTRARYLFLLTGGGALAVAAMGSYAVLVFTPAVCAVALLCSLAPQQVHRWTFCFQMSWQTLCHLGLHYTEYYLHEPPSVRFCITLSSLMLLTQRVTSLSLDICEGKVKAASGGFRSRSSLSEHVCKALPYFSYLLFFPALLGGSLCSFQRFQARVQGSSALHPRHSFWALSWRGLQILGLECLNVAVSRVVDAGAGLTDCQQFECIYVVWTTAGLFKLTYYSHWILDDSLLHAAGFGPELGQSPGEEGYVPDADIWTLERTHRISVFSRKWNQSTARWLRRLVFQHSRAWPLLQTFAFSAWWHGLHPGQVFGFVCWAVMVEADYLIHSFANEFIRSWPMRLFYRTLTWAHTQLIIAYIMLAVEVRSLSSLWLLCNSYNSVFPMVYCILLLLLAKRKHKCN
Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity . In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient .
Q96T53
P84272
DAH56_RANDH
Dahlein-5.6
Ranoidea
GLLASLGKVFGGYLAEKLKPK
Has no antimicrobial activity. Strongly inhibits the formation of NO by neuronal nitric oxide synthase at micromolar concentrations.
P84272
B5RFJ0
THIC_SALG2
Thiamine biosynthesis protein ThiC
Salmonella
MSTTTLTRREQRAKAQHFIDTLEGTAFPNSKRIYVTGSQHDIRVPMREIQLSPTLIGGSKDNQQFEENEAVPVYDTSGPYGDPEVAINVQQGLAKLRQPWIDARNDSEELDDRSSAYTRERLADDGLDDLRFTGLLTPKRAKAGKRITQLHYARQGIVTPEMEFIAIRENMGRERICSEVLRHQHPGMSFGARLPENITPEFVRDEVAAGRAIIPANINHPESEPMIIGRNFPVKVNANIGNSAVTSSIEEEVEKLVWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLLEQAEQGVDYFTIHAGVLLRYVPMTAKRLTGIVSRGGSIMAKWCLSHHKENFLFEHFREICEICAAYDVSLSLGDGLRPGSIQDANDEAQFSELHTLGELTKIAWEYDVQVMIEGPGHVPMHMIQRNMTEELESCHEAPFYTLGPLTTDIAPGYDHFTSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKEDVKQGLITYKIAAHAADLAKGHPGAQIRDNAMSKARFEFRWEDQFNLALDPFTARAYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVRDYAAAQAIEVGMADMSESFRAKGGEIYLKREEA
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
B5RFJ0
A8MAJ5
RS8_CALMQ
30S ribosomal protein S8
Caldivirga
MVMLDVLSNALMSVKNAESRGDRQVIIWPSSKLIGNVLRVMQRYGYVGEFEYVYDGRGGKYVVQLLGRINDIGAIKPRFHVKVDELQKWEEKYLPARQVGILILTTSKGVVSHLEARENRVGGILVAYVY
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
A8MAJ5
Q9TR30
CX7A2_SHEEP
Cytochrome c oxidase subunit VIIa-liver/heart
Ovis
FENKVPEKQKLFQEDNGIPVHLKG
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Q9TR30
Q4WDA4
CD123_ASPFU
Cell division cycle protein 123
Aspergillus subgen. Fumigati
MPLLDPNTQTLAESSAAQPQRLPFPPVTYSHILHCSYHQWQPRYRTLTPKSRAIPLTPSFVSYLRANGIVLPPETTRPHGDDDIDTFSDDGADEESDPSVEWQEIHSQIKSTISEFGGKVTPKLNWSAPKDAVWMSATNDLQCRTPNDIYLLLKSSDFITHDLEHPFDGCVPDPDDSSEAPATQPDIPYYLVLRKYVNFNPSLEFRCFVRNRVLLCMCQRDQNHFDFLFSLRDTLRSRIQAFFDEKLKDTFPDPNFVFDVYIPEPHQRVWLIDINPWADRTDPLLFSWLEILQMKDPIGIKEEDTDAPEESFVRLSLNGATPTVVEVNRDEDSESEKDVGSADDGDDSPFLPEFRLVKRDDPEAYSFSTPQYSAHKLPKEVVDASLAGSGGMSEFLGKWQDILAKQTQEDTDSDDGR
Regulates the cell cycle in a nutrient dependent manner.
Q4WDA4
A6UP51
VATE_METVS
V-ATPase subunit E
Methanococcus
MGAEKITSKIMEDAKIQANVILAEAQKEKEALIKKAHEEAEKKKQAILKKGEKDAEMTRNRILAEARLSAKKNSLEERERTIAKAIQKLEEDLVKLPQKDEYKDILLKMIITGVYSVGGGELDLQLNKNDWKLIDDSTLWALEKEMEDRLKKVTVLKKGESLPIIGGCVVKTADKTKVSDNSLEATFERNLDIIRAKIAEMLF
Produces ATP from ADP in the presence of a proton gradient across the membrane.
A6UP51
Q2RSE3
RL13_RHORT
50S ribosomal protein L13
Rhodospirillum
MKTYSAKPSEVDRKWYVIDAEGVVLGRLAVIIADLLRGKNKTIYTPHIDTGDHVVVINAEKVHLTGNKAANERFFWHTGHPGGIKSRSLGQIRDGAHPERLIEKAVERMMPRGPLARAQFKKLRVYGGEAHPHDAQQPVVLDVAALNPKNKRSA
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Q2RSE3
P44707
DSBB_HAEIN
Disulfide oxidoreductase
Haemophilus
MLALLKQFSEKRFVWFLLAFSSLALESTALYFQYGMGLQPCVLCVYERLAMIGLFVAGTIALLQPRVFILRLIALALGLFSSIKGLLISFRHLDLQMNPAPWKQCEFIPNFPETLPFHQWFPFIFNPTGSCNESQWSLFGLTMVQWLVVIFSLYVVILTLLLIAQVIKTRKQRRLFN
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
P44707
Q9LVJ7
NFYA6_ARATH
Nuclear transcription factor Y subunit A-6
Arabidopsis
MQEFHSSKDSLPCPATSWDNSVFTNSNVQGSSSLTDNNTLSLTMEMKQTGFQMQHYDSSSTQSTGGESYSEVASLSEPTNRYGHNIVVTHLSGYKENPENPIGSHSISKVSQDSVVLPIEAASWPLHGNVTPHFNGFLSFPYASQHTVQHPQIRGLVPSRMPLPHNIPENEPIFVNAKQYQAILRRRERRAKLEAQNKLIKVRKPYLHESRHLHALKRVRGSGGRFLNTKKHQESNSSLSPPFLIPPHVFKNSPGKFRQMDISRGGVVSSVSTTSCSDITGNNNDMFQQNPQFRFSGYPSNHHVSVLM
Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Q9LVJ7
Q5XDK8
SYM_STRP6
Methionyl-tRNA synthetase
Streptococcus
MKKPFYITTPIYYPSGKLHIGSAYTTIACDVLARYKRLMGHEVFYLTGLDEHGQKIQTKAKEAGITPQTYVDNMAKDVKALWQLLDISYDTFIRTTDDYHEEVVAAVFEKLLAQDDIYLGEYSGWYSVSDEEFFTESQLKEVFRDEDGQVIGGIAPSGHEVEWVSEESYFLRLSKYADRLVAFFKERPDFIQPDGRMNEMVKNFIEPGLEDLAVSRTTFTWGVPVPSDPKHVVYVWIDALLNYATALGYGQANHANFDKFWNGTVFHMVGKDILRFHSIYWPILLMMLDLPMPDRLIAHGWFVMKDGKMSKSKGNVVYPEMLVERFGLDPLRYYLMRSLPVGSDGTFTPEDYVGRINYELANDLGNLLNRTVAMINKYFDGTVPAYVDNGTAFDADLSQLIDAQLADYHKHMEAVDYPRALEAVWTIIARTNKYIDETAPWVLAKEDGDKAQLASVMAHLAASLRVVAHVIQPFMMETSAAIMAQLGLAPVSDLSTLALADFPANTKVVAKGTPIFPRLDMEAEIDYIKAQMGDSSAISQEKEWVPEEVALKSEKDVITFETFDAVEIRVAEVKEVSKVEGSEKLLRFRVDAGDGQDRQILSGIAKCYPNEQELVGKKLQIVANLKPRKMMKQYISQGMILSAEHGDQLTVLTVDPSVPNGSIIG
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Q5XDK8
Q3MA19
RL11_TRIV2
50S ribosomal protein L11
Trichormus
MAKKVVAVIKLALNAGKANPAPPVGPALGQHGVNIMMFCKEYNAKTADQAGMVIPVEISVYEDRSFTFVLKTPPASVLIRKAAKIERGSNEPNKKKVGTITTAQLREIAQTKLPDLNANDIDAAMKIVAGTARNMGVTVTD
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q3MA19
Q9D1I5
MCEE_MOUSE
DL-methylmalonyl-CoA racemase
Mus
MRRVVKAAALAAGATGLFSRVQTSVAIGRSFSTPQSQFQESSPVWKLGRLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGFLQKNKAGGMHHVCIEVDNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIFLHPKDCGGVLVELEQA
Methylmalonyl-CoA epimerase involved in propionyl-CoA metabolism.
Q9D1I5
Q01563
GSPB_DICD3
General secretion pathway protein B
Dickeya
MKNTPEVKASPQTGYRIPGYLLVVYALLLFTLGWFGHQRWADISPIPLSTSAAAIAAPPTKVGMVPASTAVTADENHPGSLHAAAENSATQTAASGSQTSASSQEATPDTKPAKLVTGWQTAKPGELPYIAFSAHVYTSAPDKRSVTLNGERYREGDSPYQGLVIEQIEQDMVIFSFNGEPFILDSLQDWPGGKPGDDAAQGNEQEPTSKPEQTVRTTKK
Out proteins are required for the translocation of pectate lyases and cellulases across the outer membrane.
Q01563
P16563
CRIS2_MOUSE
Testis-specific protein TPX-1
Mus
MAWFQVMLFVFALLLRSPLTEGKDPDFTSLLTNQLQVQREIVNKHNELRRSVNPTGSDILKMEWSIQATTNAQKWANKCILEHSSKDDRKINIRCGENLYMSTDPTLWSTVIQSWYNENEDFVYGVGAKPNSAVGHYTQLVWYSSFKIGCGIAYCPNQDNLKYFYVCHYCPMGNNVMKKSTPYQQGTPCASCPNNCENGLCTNSCDFEDLLSNCESLKTSAGCKHELLKTKCQATCLCEDKIH
May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation.
P16563
A1UD96
NUOI_MYCSK
NDH-1 subunit I
unclassified Mycobacterium
MPKLWDAVAGFAVTFGTLFKKPITEEYPEKPGPVAPRYHGRHQLNRYPDGLEKCIGCELCAWACPADAIYVEGDDNTADERYSPGERYGRVYQINYLRCIGCGLCIEACPTRALTMTNDYEMADDNRADLIWGKDKLLAPLQDGMLAPPHPMAPGATDDDYYLGRIGPATEDVR
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 menaquinone. 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.
A1UD96
Q6FW42
DRS1_CANGA
ATP-dependent RNA helicase DRS1
Nakaseomyces/Candida clade
MSLKMKGKKYTDLDFVPTISDSEEDVPDLDSDEEKPKPETKGKKKNKSVDEESADMNSGFRFNTDDGEINTNFDGWEFLGDEKDEEKKDVDLDKIIRKKGGLIGMAHVDEAEKSESEESESDDEDLAMDGFGMGAQEQPEGEEEDEDASNSEQESNDEEEDDDEETYDVGDAGDAEEKVEEDTAEEMQAFYAPESESENAKKEVHKTFNDLALSRPVMKGLSNLGYVKPSPIQSATIPIALLGKDIIAGAVTGSGKTAAFMIPIIERLLYKPAKVASTRVIVLTPTRELAIQVADVGKKIGQFVSNLTFGLAVGGLNLRQQEQMLKTRPDIVIATPGRFIDHIRNSASFNVDSVEVLVIDEADRMLEDGFQDELNEIMSLLPSKRQTLLFSATMNSRIKQLISLSLKRPVRIMIDPPKQAATKLTQEFVRIRKRDHLKPSLLFNLIRKLDPNGQKRIVVFVARKDMAHKLRIILGLLGMAVAELHGSLTQEQRLDSVNKFKSLQVPVLICTDLASRGLDIPKIEVVINYDMPKSYEIYLHRVGRTARAGREGRSITFVGEASAERSIVKDAIRGVNDSEIPGSKAVGRNVDWNQVEETNKIVENMDQTVQDILVEEKEEKEILRAEMELKKGENLLKHKDEIQSRPKRTWFQSEKEKKNSKIMGALSKTKKEVNSKKRKRNEAMEDGHKRSYKKTQSDRTADQERTMKKQAKANGKKKGKSKGKR
ATP-binding RNA helicase involved in ribosome assembly.
Q6FW42
A9MHF3
RL7_SALAR
50S ribosomal protein L7/L12
Salmonella
MSITKDQIIEAVAAMSVMDVVELITAMEEKFGVSAAAAVAVAGAGAAAEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKSLEEAGAEVEVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
A9MHF3
B7M0I6
RSXC_ECO8A
Rsx electron transport complex subunit C
Escherichia
MLKLFSAFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKMLPVHAPTSGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQSNAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQTNAEPEEQVDPRKAAVAAAIARAQAKKAAQQKVVNED
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
B7M0I6
Q9KWS6
DNAJ_PARTM
Chaperone protein DnaJ
Parageobacillus
MAKRDYYEILGVSKNATKEEIKKAYRKLSKKYHPDINKEPDAAEKFKEIKEAYEVLSDDQKRAHYDQFGHADPNQGFGGFRSDDFDFGGFSGFSGFDDIFSTFFGGGRRRDPNAPRAGADLQYTMTLTFEEAVFGKETDIEIPREETCNTCHGTGAKPGTKKETCSYCHGTGQISTEQSTPFGRIVNRRTCPYCGGTGQYIKERCTTCGGTGRVKRRKKIHVKIPAGIDDGQQLRVAGQGEPGINGGPPGDLYIVFHVEPHEFFERDGDDIYCEIPLTFAQAALGDEIEVPTLHGKVRLKIPAGTQTGTKFRLKGKGVPNVRGYGYGDQHVIVRVVTPTKLTEKQKQLLREFDQLGGSSMHQGPHGRFFEKVKKAFKGES
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.
Q9KWS6
Q9Z1P6
NDUA7_MOUSE
NADH-ubiquinone oxidoreductase subunit B14.5a
Mus
MASATRVIQKLRNWASGQDLQAKLQLRYQEIAKRTQPPPKLPVGPSHKLSNNYYCTRDGRREVVPPSIIMSSQKALVSGKAAESSAMAATEKKAVTPAPPMKRWELSKDQPYL
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q9Z1P6
B4S817
HSLV_PROA2
ATP-dependent protease subunit HslV
Prosthecochloris
MNRSEKPQLRATTVLGVIRNGKAALGSDGQMTLGNTVIKHSTKKIRRIQHANLITGFAGATADAVTLLDRFDEKLQAFGGQLERSAVELARDWRTDKYLRRLEAMLAVVSADKALIISGTGDVIEPEDGIVAIGSGSMYALSAARALIRYTDLSAREIVTESLKIAADICIYTNDHIVVEEV
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
B4S817
E9Q8Q8
SACA6_MOUSE
Sperm acrosome membrane-associated protein 6
Mus
MTSQRSLSSPQTRRPSVMGLISLVGSIVLLFLLIFRASTWACLFCFTTYEERLRVCQLFVGREETKINLCRNELEGAFEDLKDMKINYDERSYLHDEFTQMTVSLQEKAARRREPFWLAFKDAAAKLKRTIEHLKKAPACIPPCGLQEVARLFHCSGCFSKLCDLPLDCPVQDMLVNRGDQALFSCIVAFELPESEITYSWKFVGGVRTKDVTYFRDMPGAHGYLARIRPVQPKHGGTFSCVILHDQRPLARLYFYLNVTGPPPPEDTELQVTFREVMNRTPAEPEMIQPWSPSLGELLTNPQALTLGNLFLLAATAALGSASVTLLVWLFFRWYLSGN
Sperm protein required for fusion of sperm with the egg membrane during fertilization.
E9Q8Q8
P81377
KAP1_RAT
cAMP-dependent protein kinase type I-beta regulatory subunit
Rattus
MASPSCFHSEDEDSLKGCEMYVQKHGIQQVLKECIVHLCVAKPDRPLRFLREHFEKLEKEENRQILARQKSNSQCDSHDEEISPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFSHLDDNERSDIFDAMFPVTHIDGETVIQQGNEGDNFYVIDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRYNSFISLTV
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
P81377
C1D6I2
DNAA_LARHH
Chromosomal replication initiator protein DnaA
Laribacter
MTDLSAFWPQCLARFEAELSAQQFNTWIKPLVCVAGEDAIALYAANRFSLGFVKERFLSRIETFAEDILGRPVTIELRIGGAQAGASAPAAASPRSPGRPAPAPVAATPTTGSLADSIVSDVPLPNVKLTAPKPAIGGGHESTRLNPAFTFESLVTGKGNQLARAAALQIADNPGDSTYNPFFVYGGVGLGKTHLIQAIGNHVYQKNPQAKIRYIHAERYVADIMRAYQHKAFDEFKRYYHSLDLLLIDDIQFFAGKNRTMEEFFYAFNALLEGGKQVIMTCDSYPKQIEGMDERLISRFSWGLTVEIQPPELEMRVAILMKKAEADNLKLGNDVAFFIAQNVRSNVRELEGALKRVVAYSRFSNQPISLDLVKEALKDILAAGNRQISVDNIQKTVADYYKIKLSDMHSKKRSRDIARPRQVAMALAKELTSMSLPNIGDAFGGRDHTTVLHACKTIAEMRESDPDISRDYAALQQMLRN
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.
C1D6I2
Q8NX83
PT1_STAAW
Phosphotransferase system, enzyme I
Staphylococcus
MSKLIKGIAASDGVAIAKAYLLVEPDLTFDKNEKVTDVEGEVAKFNSAIEASKVELTKIRNNAEVQLGADKAAIFDAHLLVLDDPELIQPIQDKIKNENANAATALTDVTTQFVTIFESMDNEYMKERAADIRDVSKRVLSHILGVELPNPSMIDESVVIVGNDLTPSDTAQLNKEFVQGFATNIGGRTSHSAIMSRSLEIPAIVGTKSITQEVKQGDMIIVDGLNGDVIVNPTEDELIAYQDKRERYFADKKELQKLRDADTVTVDGVHAELAANIGTPNDLPGVIENGAQGIGLYRTEFLYMGRDQMPTEEEQFEAYKEVLEAMDGKRVVVRTLDIGGDKELSYLNLPEEMNPFLGYRAIRLCLAQQDIFRPQLRALLRASVYGKLNIMFPMVATINEFREAKAILLEEKENLKNEGHDISDDIELGIMVEIPATAALADVFAKEVDFFSIGTNDLIQYTLAADRMSERVSYLYQPYNPSILRLVKQVIEASHKEGKWTGMCGEMAGDETAIPLLLGLGLDEFSMSATSILKARRQINGLSKNEMTELANRAVDCATQEEVIELVNNYVK
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Q8NX83
P9WMA8
DATIN_MYCTO
Dormancy associated translation inhibitor
Mycobacterium tuberculosis complex
MEPKRSRLVVCAPEPSHAREFPDVAVFSGGRANASQAERLARAVGRVLADRGVTGGARVRLTMANCADGPTLVQINLQVGDTPLRAQAATAGIDDLRPALIRLDRQIVRASAQWCPRPWPDRPRRRLTTPAEALVTRRKPVVLRRATPLQAIAAMDAMDYDVHLFTDAETGEDAVVYRAGPSGLRLARQHHVFPPGWSRCRAPAGPPVPLIVNSRPTPVLTEAAAVDRAREHGLPFLFFTDQATGRGQLLYSRYDGNLGLITPTGDGVADGLA
Involved in translation regulation. Can also stimulate macrophages and peripheral blood mononuclear cells (PBMC) to secrete important cytokines that may be significant in granuloma formation and its maintenance. Increases secretion of IFN-gamma, TNF-alpha, IL-1 beta and IL-8 through human Toll-like receptor 2 (TLR2) signaling pathway.
P9WMA8
C7Z638
MTNA_FUSV7
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
Fusarium vanettenii
MSTLQAVKYIRGKLEVLDQLRLPHEFHYDEVSNRTEAFDSIYTMRVRGAPAIAIVAALGLAVELHNGSCTASSAEETIGQIEEALDYLKESRPTAVDLTNAINQLKARIREVGSTATKEAIISAFIEEAEKIFEKDLKTNLSIGDFGAEWLRAQVGASPEQQISVLTHCNTGSLATSGHGTALGIIRTLQAKKLLHHAFCTETRPYNQGSRLTAFELVFEGIPSTLITDSMAASLFRTRKQEKNIAAVIVGADRVVRNGDTANKIGTYQLAVLAKHHGVKFIVAAPTTSIDLETETGDGIKIEERKKEELTQVTGAVIKPDGTVDESSKVRVATADQRINVWNPAFDVTPAEFIDAVVTEKGAIEKGPDGKFDFSQILPERWAKITGA
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
C7Z638
Q32BC5
MTGA_SHIDS
Peptidoglycan glycosyltransferase MtgA
Shigella
MSKSRLTVFSFVRRFLLRLMVVLAVFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSAPSGYVRSRQAWILRQMYQLGGEPFMQQHQLD
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Q32BC5
A7IAU6
VATD_METB6
V-ATPase subunit D
Methanoregula
MALRDIKPTRSELINLKRKIQLSQRGYKILKMKRDGLIMEFFKILSEAKDSRGELLRRYKHAVEMMAVANTVEGALGVKAAAFSVKETPEITLKSKNIMGVVVPEIESSKVKKTLADRGYGVLGTSPVIDETASSFEDLVEAIIESAEIETTMKRLLDEIEKTKRRVNALEFKVIPELTEARDFIKMRLDEMEREELFRMKKIKARGSS
Produces ATP from ADP in the presence of a proton gradient across the membrane.
A7IAU6
Q8EBS1
SYA_SHEON
Alanyl-tRNA synthetase
Shewanella
MYQTTAALRSAFLEFFRSNGHQVVDSSSLVPGNDPTLLFTNAGMNQFKDVFLGMDKRSYTRATTAQRCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEDAIRFGWTFLTEVLMLPKERLCVTIYQTDDEAFEIWNKKIGVAAENIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGRPGSPEEDGDRFIEIWNIVFMQYNRQASGEMLPLPKPSVDTGMGIERIAAIMQGVHSNYEIDIFRALIAKAAEIIGVADLSNKSLRVIADHIRSCAFLVADGVMPSNEGRGYVLRRIIRRAVRHGNKLGATEAFFYKLVPTLIDVMGDAAKGLAETQVIVEKALKAEEEQFARTLERGLGILDSALNELQGDTLDGETVFKLYDTYGFPVDLTADVCRERNIIVDEAGFEAAMAEQRSRAQAAGNFGADYNAALKIDAETAFCGYSELTGNAKVTALYLNGESVPAINTGDDAVVVLDVTPFYAESGGQVGDKGVLMAQGIEFTVNDTQKFGQASGHKGTLTAGSLSVGQVLEAKVDKKLRHRTQLNHSVTHLLHAALRQVLGTHVTQKGSLVDPERLRFDFSHFEAVKPFELKQVEELVNTQIRRNHELKVAEMAIDEAKEKGAMALFGEKYDSQVRVVTMGDFSIELCGGTHVGRTGDIGLFKITSEGGIAAGVRRIEAVTGAAAMAYVAQQQAELEEAASLLKADAHSVVTKLKVQLDKMKQLEKEMQQLKDKLAAAASADLAGDAVVVNGVNVLIKKLEGVEAGALRGLQDELKQKLKSAIIVLGVAQEGKVNLIAGVSNDLIAKIKAGELVAMVATQVGGKGGGRPDMAQAGGSQPENLDAALSQVLPWITERLA
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.
Q8EBS1
Q8YHU3
CBID_BRUME
Cobalt-precorrin-6A synthase
Brucella
MNDETTPANKNPEKAELRCGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLAYEGLGEGYAMAGIVKDAGDDPDVTHGATIISTVYPAPPGTGIIFRAGEGVGTVTREGLAIPPPGEAAINPVPRRMMTEICEAICAEYGLPADLVITISVPGGEEIAQKTWNPRLGIIGGISILGTTGVVHPFSCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYNLPDFAILDMGDFAGGVLKYLREHPIDRLTIAGGFAKLTKLAQGALDLHSSRSQVDKGFLWQIAERAGAPADMKERILLANTAMEVLELTQSIGIDIAGPIALEARQTALKTLRGAPVEVEIIVTDRKGNILARV
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Q8YHU3
Q9V2N1
COBS_PYRAB
Cobalamin-5'-phosphate synthase
Pyrococcus
MRNILPFLTRIPVKGDFEKARNELWAFPLVSLVSSIIPIAILYLRIPLANVLALLSLYFVIGLLHLDGLADWADGIMVKGDRERKIKAMKDLNTGIAGVFAVVVVLFLQVYSLSMLPFYAIYIAELNSKFSMLLGLATKKPLGQGLGAYFMEGMNGRQLAIGVVLYVLLYLPVVIYDPSALFGVMGLVFAWYVIRLSLENFGGINGDCLGAMAEITRAGTLVILSFSLCFTT
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Q9V2N1
P02600
MYL1_RAT
Myosin light chain alkali 1/2
Rattus
MAPKKDVKKPAAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEEFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQGGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEAFVKHIMSV
Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function.
P02600
Q5P0Z8
OTC_AROAE
Ornithine carbamoyltransferase
Aromatoleum
MTKPRHYLQFKDFTRDDYRHVFDRTRWIKDKFKRYEPYHPLFDRTLVMIFEKASTRTRLSFEAGMQQLGGSAIYLNTRDSQLGRGEPVEDAAQVISRMSDVVMIRTFEQDIIERFAAHSRVPVINGLTNEYHPCQILADIYTFIEHRGSIQGRTVAWVGDSNNMCNTWLQAAELLDFNVHVSTPPGYEVEPERAGLYGTGHFEQFADPMEACKGADLVTTDVWTSMGFEAENDERMKDFADWCVDAEMMAAARADAVFMHCLPAHRGEEVTADVIDGAQSVVWDEAENRLHVQKALMEYLVLGKVED
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q5P0Z8
Q81D33
DDLA_BACCR
D-alanylalanine synthetase A
Bacillus cereus group
MLLWAGYASEKQVSIMTGNEMIAHLDKNKYEIVPITLNEKMDLIEKAKDIDFALLALHGKYGEDGTVQGTLESLGIPYSGSNMLSSSICMDKNISKKILRYEGVETPDWIELTKMEDLNLDELDKLGFPLVVKPNSGGSSVGVKIVYNKNELISMLETVFEWDSEVVIEKYIKGDEITCSILDGKQLPIVSIRHAAEFFDYNAKYDDTSTVEEVIELPAQIKERVNKASLTCYKALKCSVYARVDMMVKDGIPYVMEINTLPGMTQSSLLPKSAEAAGISYSKLLDMIIETSLKVRNEEGF
Cell wall formation.
Q81D33
O27129
RS12_METTH
30S ribosomal protein S12
Methanothermobacter
MPGLFAAKKLKSKRQKFKWKDTHYKRRSLRLDVKADPLEGAPQARGIVIEKVGIEAKQPNSAIRKCVRVQLIKNGKQITAFAPGDGAIGFIDEHDEVVVEGIGGPSGRSMGDIPGVRWKVTKVNNVSLQEMVKGKIEKPVR
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.
O27129
B3DWG1
HYPA_METI4
Hydrogenase maturation factor HypA
Methylacidiphilum
MHELSLCESLVSLLEEEMQKLGCGALKKVVLQVGPLALIEEGAMRFAFEVASKGTVVEGAELFIEWIAVRGYCLDCQKEALVYKIGESCPCCGGVMILSEEGKDLKVASIEVE
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
B3DWG1
A6L028
RIMP_PHOV8
Ribosome maturation factor RimP
Phocaeicola
MIDKNVVTRIVDEWLEGKDYFLVDVTVSPDDKIVVEIDHAEGVWIDDCVELSRYIESKLDREEEDYELEVGSAGIGQPFKVLQQYLIHIGKEVEILTKEGKKLEGVLKDANEENFTVTIEKKVKPEGAKRPKLVEEDITFAYDEIKYTKYLISFK
Required for maturation of 30S ribosomal subunits.
A6L028
Q5E7A2
SYDP_ALIF1
Protein Syd
Aliivibrio
MPLSVEQALANFSQRYVEAWKAQHDCLPINEELVGLASPCIEETRDLEISWQPIVRDEAIRLHNIEQGIELDLHDDFHAFYGTQYSADMTAKFEDMNIELLQVWSDEDLERLQGNMLGHLVMQRRLKLVPTLFVAVTDDEMEVVSICNQSGEVILDRVGTKNRTVLAANMAEFLNKLEPVIAA
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
Q5E7A2
A9WIN9
COBQ_CHLAA
Cobyric acid synthase
Chloroflexus
MQAPVLMVVGTASSVGKSTLVTALCRLAYRRGLRVAPFKAQNMSNNAAVTADGKEIARSTAVQAAAAGIAPTVAMNPILIKPEGQRRSQIIVEGRPWQSLTATDFWQRKAQLWSVVTRNLDHLRATYDLVIAEGAGSPVELNLKPGDIVNMRVARYAQAQTILVGDIDRGGIFAQLLGTLMLLEPEERQLITGCIVNRFRGDPSLFADGVTILEERSGLPVLGVIPWLDDLGLPEEDAVALEQPPVAPAHGLIIAVIRLPTIANFDDFDPLAREPGVVVRYIDHPLELTGAAAVILPGVKHTLAARHWLHERGFDNALREFTGAIVGICGGYQLLGERISDPLAVEGSGGEAAGLGLLPIETIFTTAKQTTQTIACAQVPWAGNEPLQGYEIHMGQSYRRGEAPAFLRIIQRGNTPTSADDGCISSDGRVWGCYLHGIFANDTFRRGWLRRLGWQPPTTPVARADPFDRLADHVAAALGPAVLDRLMRR
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
A9WIN9
A3CV35
PAN_METMJ
Proteasome regulatory particle
Methanoculleus
MGDIARQAPDKDTGEDIYQYLLERITNLENRNLELREQFRQMESEKRYVETQKIRYERELRKLKSEIEQLRSPPLVIGTVTDVIDNSRVIVRSSAGPRFLVRTSQLIDPDLLKPGVRCTLNQQSLAIVDVLPTSYDAQIYGMELVESPEETYENIGGLEPQIEEIREAVELPLTKPQLFEKVGISPPKGVLLYGPPGTGKTLLARAVAHQTNAHFLRVVGSELVQKYIGEGARLVRELFDLAKQRAPSIIFIDEIDAIGAHRNDSTTSGDREVQRTLMQLLAEMDGFDNRGDVKIVAATNRIDILDRALLRPGRFDRMIEIPLPDHQGRLAILKIHTQYMNIGEDVNLSEVSRLTEGKNGADLRAICMEAGMFAIRMERDAVNSEDFMKAIDKLALDFDRHHFHTTFGEMFA
ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
A3CV35
A1AV04
UPPP_PELPD
Undecaprenyl pyrophosphate phosphatase
Pelobacter
MNLLHALILGALQGVTEVLPISSSAHLILVPWLLGWPESGLTFDVALHLGTFLALVVYFRRDIVDMAVSTIDAVKHRSLDTPARRLPFLVIASAVPAALVGKLFETQIEELFRSRPLLIGLFLILFGVGLGLADLFGRKRRFMAQVTVSHALVIGLFQCLALIPGVSRSGITITAGLMLGFNRVGAARFSFLMSLPIVAGAALFKMLHLLDQGIPAGEGLPLAAGIVSSAVTGYISVAFLLRFVQKRSIAPFVWYRLIAGGAVVSVILTGISG
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
A1AV04
Q68XI5
RECN_RICTY
Recombination protein N
typhus group
MFYSLSVKNFILIDELEIEFNKGLCVITGETGAGKSILLDAILFCLGYKTSNNVIKHGKDYTVVNIIFSLNDEIKKFLIQNFIEPEELLLVKCLQKVEGRKNFFINNQIVTKTLMKQLANYLFELHGQNNNITLLEASTQRDILDSYGNLLEFRVQLAKCYQIWQNTRKEIEEITVKQNEIEQEIDYLSFVTEELTKLNIQIGEEETLTNIRKDLQNKGKNLQLIRDIIAEINNPEINISINRACKLLARQDYNDRFNAVVTSLEEAYNNLEVARQELSNILGSFTYEEYNLEETEERLFLIKAISRKYNVPANELGIFLDKSLEQLGILKNKIANSNKLQAQEVLLQEQYYKLASDLSAKRLIAAKHLEESLNQELKQLKMENANFKIEVKTRIDPTASGNDDIVFKASTNPGMKIEAINKIASGGELSRFMLALKTSLFDKMIKPSIIFDEIDVGIAGEAADKIGDRLKKLSSVTQVIVITHQPQVAGKADLHIKIEKTQLEQETKVKVKALNLAERQTELARMISGKTITAASLKVAKELLHPVAFSHDQK
May be involved in recombinational repair of damaged DNA.
Q68XI5
B3DQN2
MURC_BIFLD
UDP-N-acetylmuramoyl-L-alanine synthetase
Bifidobacterium
MSQDQPIVLDPTYASFDAAARPADLGATHFIGIGGAGMSVLAEMLHAEGVAVDGSDRAHSAKTDRLETLGITVEFGQRAENVAQAETVVYSSAIKPDNPEIVAAHAAGKRIVHRSDILALLMNGKRAVTVAGAHGKTTTSSMLSHILVNAGADPSYAIGGFIQGPDGTTLDGGHAGKGDILVAEADESDGSFAKYHPTIAIITNCEADHLDHYGDEAHYRAAFVAHAGRATGHVIISIDDPDGLAVLEALPADVKSHTVAYGTTARESLPDLGGAAYVWIASESETAGSGVEQLTLHLPAAVTAGEPVSQSVALKVPGVHNARNAAAAISAAVLLGVSPADAANAAGTFLGAARRFQVRGTVKQVTVVDDYAHHPTEIAALLDAARRRYPDSTIRVIFQPHLFSRTKFFAHQFAKSLAKADDVIITGIFPAREKQADFPDISPSTIVDAAAGLKDASAGTWIQPVEDMCLAAKMMAMRAHHGDVIFTVGAGDITDMDQVLLTALEAHRESCE
Cell wall formation.
B3DQN2
Q12MQ7
SEQA_SHEDO
Negative modulator of initiation of replication
Shewanella
MKYIEVDEELYRFIASKTERIGESASDILRRLLTLPVDTVTPFEPNAIDEPSLDVAHHQASNFAASNQEQQTGHGHAGEPSAVQTPESNDYAKAQPHSSGYQPGQLEGHKSEPQTLAQLNSQPLAVGQSSQSATSQVDFNALVNEHLLSQQKGAVGRFMWLLEGLAALAPSQFNKVLLVQGKGRLYFARSKDELLASSASANPKEIGTTGYWVTTNNNTAKKQAILVEVLTKLHCDETLASAIADRICDKVAG
Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated.
Q12MQ7
Q07ZQ7
AROC_SHEFN
5-enolpyruvylshikimate-3-phosphate phospholyase
Shewanella
MSGNSIGQNFVVTTFGESHGVALGCIIDGCPPGLELTVEDMQHDLDRRRPGTSRYTTARREADEVRILSGVFEGKTTGTSIGLLIENTDQRSQDYSDIKDTFRPGHADYTYQQKYGMRDYRGGGRSSARETAMRVAAGAVAKKYLKQVHGIEIHGYLAQLGPISADTIDLTQIEQNAFFFPDASKLEALDEYMRGLRKSGDSIGAKITVAATGVPVGLGEPVFDRLDADIAHALMGINAVKGVEIGDGFGVVTQKGSQGRDLMSPQGFASNHAGGVLGGISSGQPVVAHIALKPTSSISVPGQSMTVQGETIDMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRHRAQNQDVTSQTPVIGMR
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.
Q07ZQ7
A0A2H5AIY2
TYDC2_NARPS
Tyrosine decarboxylase 2
Narcissus
MEESLKPMDAEQLRENAHKMVDFIADYYKSIESFPVLSQVKPGYLRDLLPDSAPDHPESLEDVLEDIRQKIVPGVTHWQSPNYFAYYPSNSSVAGFLGEMISAGFNIVGFNWIASPAATELEVIVLDWLAKMLNLPNQFLSSGQGGGVIQGTASEANLVVLLAARDKFLNRFGKRSLEKLVVYASDQTHAAMKKACQIAGIYPENFRVLNADHTSNYALVPEALSDAISNDLSAGLIPFFLCATVGTTSSAAVDPLSELGKISKVNDMWFHVDAAYAGSACICPEYRHYIDGIEEAASFNMNAHKWFLTNFDCSLLWIKDRSALIQSLSTYPEYLKNKASQENSVVDFKDWQIPLGRRFRSLKLWMVLRLYGLENLQSYIRNHIKLAGQFEQLVCSDSRFEVVVPRTFSLVCFRLLPPPNHQDNGYKLNHSLLDAVNSSGKIFVSHTVLSGKYVIRFAVGAPLTEEEHIKQAWKVFQDQATILLAGSDGSDFGASNGDII
Catalyzes the decarboxylation of L-tyrosine to tyramine, which is converted to norbelladine, a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine-type alkaloids, promising anticancer agents.
A0A2H5AIY2
B9JZ26
LGT_AGRVS
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Agrobacterium
MNTVASLFAILPYPQIDPIALSIGPVAIRWYGLAYVTGILIGWWLARRMIANLSLWPGNTTPITEKHLDDFLVWAAIGIVLGGRIGYILFYDLQPVLDNPLVALEIWRGGMSFHGGLTGATLAMIVFARRNGLPVWMLFDLVACVAPIGLFFGRIANFINGELWGRVSDVAWAMQFPTGGPFTRHPSQLYEAALEGLVLFVLLQVLARQFHALKTSGVISGVFICGYALARIFVEFFREPDEQLGYLVGGWLTMGMLLSLPMLALGLWAIWRARRAGRSQEPSGLKG
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
B9JZ26
Q9LY41
ATL4_ARATH
RING-type E3 ubiquitin transferase ATL4
Arabidopsis
MESLINPSHGGGNYDSHSSSLDSLKPSVLVIILILLMTLLISVSICFLLRCLNRCSHRSVLPLSSSSSVATVTSDSRRFSGHRVSPETERSSVLDSLPIFKFSSVTRRSSSMNSGDCAVCLSKFEPEDQLRLLPLCCHAFHADCIDIWLVSNQTCPLCRSPLFASESDLMKSLAVVGSNNGGGENSFRLEIGSISRRRQTPIPESVEQHRTYSIGSFDYIVDDVDSEISESNFNRGKQEDATTTTATATAVTTNPTSFEASLAADIGNDGSRSWLKDYVDRLSRGISSRAMSFRSSGRFFTGSSRRSEELTVMDLEANHAGEEISELFRWLSGV
E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
Q9LY41
P68250
1433B_BOVIN
14-3-3 protein beta/alpha, N-terminally processed
Bos
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLQLLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13.
P68250
A9L543
AC4CH_SHEB9
N(4)-acetylcytidine amidohydrolase
Shewanella
MLLNKITFFERFEHDILSGAKTITLRDEAESHVIVGQILPVSTFETERWFCDIQIIDVTPVKLTELTEVHAKQENMTLPQLRDVIAEIYPGLEQLFMIRFRILSQ
Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
A9L543
Q67N85
TDH_SYMTH
L-threonine 3-dehydrogenase
Symbiobacterium
MAETMRALRKLEAGPGATLQEVPIPTIGPRDVLVKVRAASICGTDYHIYTWDPWSAGRVKPPLTIGHELAGEVVAVGREVTACKVGDYVSAETHIVCNRCPRCHMGEYHLCENTKILGVDTDGAFAEYVAVPEQNIWVNDKDIPFELQSIQEPLGNAVHTALNGDLTARSVLITGCGPIGIMSVPVAKMAGAEIVMAMDINEYRLQLAGQLGADVLINPTKQDPVEVVRSYTRGYGADVVLEMSGNPTAIRQGLKAARNGARISLLGLPGRPLELDLAADVIMRGLVLQGITGRRMWQTWYQVRSLYRAGLAERLRPLVTHRMPLEQIDAAMELMGSGQSGKIVLVPDLKA
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Q67N85
Q09715
TUP11_SCHPO
Transcriptional repressor tup11
Schizosaccharomyces
MASVEDATKVQEMLDALKAEYNALAHHSFASKARGNDYESSMIQSQIQEIEAFRKTVDDMYEKQKSIRETYEKDINKLKRELEELGVEANTASYRNRGERSELAASNNQVTHIDQEHPSQTKSTSQPPSNHLPAFQQIPPIHQSAYPQNNVAEVLMPPIPPSVEASSGQNFNQGIASQNPAISTSNLPSTTPLYIPPVNYGANQVSQQPNPQLPGVSNYYNPSATSKPAVNVQPPRIPTKATPSAEPSMTASANAGSISQAGPDGEYQGREQIAPVSDTEAARKTTSQSWYVTYNPACKRVFNINLVHTLEHPSVVCCVKFSNNGKYLATGCNQAANVFDVQTGKKLFTLHEESPDPSRDLYVRTIAFSPDGKYLVTGTEDRQIKLWDLSTQKVRYVFSGHEQDIYSLDFSHNGRFIVSGSGDRTARLWDVETGQCILKLEIENGVTAIAISPNDQFIAVGSLDQIIRVWSVSGTLVERLEGHKESVYSIAFSPDSSILLSGSLDKTIKVWELQATRSVGLSAIKPEGICKATYTGHTDFVLSVAVSPDSRWGLSGSKDRSMQFWDLQTGQSYLTCQGHKNSVISVCFSPDGRQFASGSGDLRARIWSIDPASP
Transcriptional repressor.
Q09715
A4WUM8
ATPG_CERS5
F-ATPase gamma subunit
Cereibacter
MPSLKDLKNRIGSVKNTRKITKAMQMVAAAKLRRAQEAAEAARPFAERMTAVMTGLAGSVGSSESAPRLLAGTGSDKVQLLVVMTAERGLCGGFNSSIVRLARAHAAKLLAEGKTVKILTVGKKGREQLRRDLGQHFIGHVDLSEVKRMGYPVAQGIARDVLDRFDKGEFDVATIFFARFQSVISQIPTAQQVIPAVFEGEGEVNSLYDYEPSEEGVLADLLPRGVATQIFTALLENGASEQGARMSAMDNATRNAGDMINRLTIQYNRSRQAAITKELIEIISGAEAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
A4WUM8
Q94FA5
METK4_BRAJU
Methionine adenosyltransferase 4
Brassica
METFLFTSESVNEGHPDKLCDQVSDAILDACLEQDPESKVACETCTKTNMVMVFGEITTSAKVDYEKIVRSTCREIGFISADVGLDADKCNVLVNIEQQSPDIAQGVHGHLTKKPEDIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYKNEGGAMIPIRVHTVLISTQHDETVTNDEIAVDLKEHVIKPVIPAKYLDENTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVATGLARRCIVQVSYAIGVPEPLSVFVDTYKTGTIPDKDILVLIKEAFDFRPGMMAINLDLKRGGNFRFQKTAAYGHFGRDDPDFTWEVIKPLKPKA
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Q94FA5
Q39F31
DAPE_BURL3
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Burkholderia cepacia complex
MSATLALTEQLIARASVTPDDQHCQQIMTERLTALGFECETIASHGVTNLWAVKRGTDGRDGKLLAFAGHTDVVPTGPLEQWSSPPFIPAHRDGKLYGRGAADMKTSLAAFVVASEEFVAAHPGHRGTIAFLITSDEEGPATDGTVKVVELLEARGERMDYCIVGEPTSTTELGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLHAGTGASNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHGLEYTLKWSVSGLPFLTPRGELSGALENAIRTETGITTELSTTGGTSDGRFIARICPQVIEFGPPNGSIHKIDEHIEVRFVDPLKNVYRRVLEQLIA
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Q39F31
Q60764
MKRN3_MOUSE
Zinc finger protein 127
Mus
MEESTAPIEAHAAAGAEAGAEGGEGVSVPPPPQFEAAGASAGVSSAPLQQASGLAPLLVTPGPAIRRAASLRPAPAEGGGARSGPERNSGSWTKQILCRYYLHGQCKEGDNCRYSHDLSGRRRSRGGQDAQPRASADRGPKMATRWEPPTQEVAEAPPAASSSSLPLIGSAAERGFTEAEIDNAGIRSAAERGFSEAEIDNASLAAGAAAGAGAEGWEGAIEFVPGQPYRGRMVPPHGPEAPLQSPAIEREHMAMGMGMPMPVPMPMPVPMPVPMPLPLCRYAARGQCLRGDRCAYPHGEICDMCGQQALHPWDAAQQEAHRRACVEAHERDMELSFAVQRSMDKVCGICMEVVYEKADPSDRRFGILFSCNHTYCLRCIRRWRSATQFENRISKSCPQCRVSSGFVIPSEFWVEEEEEKEKLVQQYKEGMSQKACRYFAGGLGHCPFGEFCFYKHEYPEGWRDQPPRPDGGGSSSAYWHQVLEPVQLREGNVLFKSRKKEHSVLRLANQLLKKLLCLRGSSSFSDDRWLLLQYQLEEYFSLNL
E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Q60764
Q14L37
DNLJ_SPICI
Polydeoxyribonucleotide synthase [NAD(+)]
Spiroplasma
MTFEQAKKRSLVLKEQLEKWNYEYYVNDNPSVSDQEYDRALQELIAIEQQYSELITIDSPTQRVSGQISEKFNKYVHTSPMLSLGNAFNYDDLIHFDEQIKEFTALPEIEYTCELKIDGLSISLVYDNHVLVMGATRGDGLTGEDVTINIKQIKSIPLRIDQPTLIVRGEVYLSVEEFNKINEERVKNGEFKFANPRNAAAGTLRQLDSTIVAKRKLNAFLYYYVNALQDGIQSQYEALQRLEQLKFKINPEYRYCSNIAAVWAYIQEYEPKRNQLGYEIDGIVIKVNNLNLYNRIGYTAKNPKWAIAYKFPAEVVVTKLLNIFPSVGRTGRITYNAVLEPIRIVGTIVRAATLHNADFITERDIRIGDNVQVKKAGDIIPEVINYVAARRQKNAQKWQEATHCPECNSLLERVEGEVDQYCINSVCPKKITRGLEHYCSRNAMNIEGISEKIIERLFKLEYLKSFSDLYQLEQYRAEIIELENFGEKSFENMITSINNSKNNSLERLLFALGIRHVGQKTAKLLARQFKTIDNLAAMNIEQLSIINDIGPIVAASVVDYFAIPANQQELALLRQNGVKMEYFATNQHLAQKFENYRFVITGVLSKSREYFKELIESYGGQVSESVSAKTTYLLAGTDAGNKLVKAQKLNVKIINEEEFQQLLSKED
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Q14L37
Q06J19
RPOC2_BIGNA
Plastid-encoded RNA polymerase subunit beta''
Bigelowiella
MEKIFFNYPFNKGKLKTLLIWSILNTGQYNMINLVENLKKVGFQYATTAGISLGIDDLKTISTKYDLIEKTNDNIKDITNHLNLAVLNEVEHSQKLINSWQKISEILKININKKFKTVNKLNPIYMMAFSGARGNISQVRQLIGMRGLMADPNGQIIHLPIKSNFREGLTVTEYLISCYGARKGVVDTALRTATAGYLTRRLVDTAQHVIISQLDCGTKQGIFLSNLYQGTDILLALKDQLYGRVLGKDIKINSLMYLKNQQIDDSLSILLANHLKRVFIRSPLTCKASNSTLCQLCYGWNLSHSKLISLGEIVGVIAAQSIGEPGTQLTMRTFHTGGVFSGNVKSQLYSPFDGIVEYSSSLYGDIVNLYNGNFAFLVKRKGLIIINPIIKKIKPKKFEAILYTLVFVKNNEKVKKNQLIAQQSNKISNTQQIEGKYTVNSKLEGEILFDENHLSTNKKKIWILHGKIYKSVFPLQLFPKKNDFLSYKFPLAQAKLLNLSASFLKVCVVRKKRHFIKDNISQSNEILLFTEYPLYKFLIKNIKNYHQFQFFYPIQNKIKEVEKSLRINNKVIKDNRIKIPFNSIAKSKLLNLLNKRLEQNTFFSKNTFSNYYENTDERTTWFTQNSILKYNAIYFYKSSKSVEAKTSRKIPITFNSKNFLIKEKLFFIKNNSVLLPIFSSDFFTKFTLKNEYFKPKHNIQRKLGFLSPTSYFKYISNNYFLKYLNFYQKHISVEMNDIIKVKLYYKQEFEEKTNFKKQNLHKIDSKINLFMNKLILVIEHLILTKLFSTKINNINYLLFYFNYLKYLKESNKFTIFYCNKKKETIFDLLFLLKTLNTTSNLIILAENKISTKLLSEFIYQTIYLIKNNITINSTNSVLENFNYFQQRKEDLFQHRNIFEKVPNFSGKRFSNLSLNINNENYSISKAENKMLIQDLLTLTILNNNIKYFNSHKSFLDKRFFYNESLPIPKILKDFTSILNRINFWSFSSSQFYKKHFLFALKTDNLINIKNKNFIFISRIPQIQAVNFALKKSLKSSFDLKSYEILQYNLKFPLGFYSLIKMIIEERSLFDIDYFQKFIIQYKNFSFHLINKKLKNIFTNNSYGSFTDESTLLESKYFNKRRPTKTTFSKLMNQIKFKFFIKVPLLLSTFSKKDTVLFNIFITNKKENFRNYKIVNMLTNDFYKNLNLQTHSSEKNSQLKLSSKNLEIFNLFYTSSIINVIMKKSITNFNKNFFIDNLFQFSKTHFNWLPKWDTIVRIQFLSPYQGEIIAQNIVKYSGYKTLYNHLMILTKNEKLQVSIFRNKNQETIIKKDTKNYFITKPHCCKIYPKFGSLIYSTSQVSPGKKINQSGQIIEKSNSFLVLRKGTPLLSPITGIFYVWNGDFVSQGSPIMTLLYNKLKTGDIVQGIPKIEHFFEARKGNVDLIQTNLYIKLLAFFKKYNKTLSEYRAVKRSILKIQKIIIDGVCRVYCSQGILVSRKHFEVIVKQMTSKVKIVNGGETGLLEGEFINFQKLEKINTNLYHRRVVYEPLVLGITKVSLRTESFISSASFQETTKVLSQAALEKRIDFLNGLKENVILGKLIPGGTGLIVKIITNKI
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q06J19
Q9V2W8
FLAB4_THEKO
Flagellin B4
Thermococcus
MRRRGAIGIGTLIVFIAMVLVAAVAAGVIIGTAGYLEQKAQAAGRQTTQEVASGIKVLNVYGYTNATPPSNGTIERMAIFITPNAGSEGIDLSNVKIVLSDGRRLVVYNYSGSFQNAESVKDLFNMTYVGVWNSTNGTASFGIAVINDIGSEMQGTHPTLEFGDMVALCVWTTMFEYEDKDGIGPSTRITGKVIPERGAAGVLDFTTPATFSYNVMVLQ
Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
Q9V2W8
Q9KMU6
PRTV_VIBCH
18 kDa metalloprotease PrtV
Vibrio
MKTIKKTLLAAAIASFFSSGLYAQTPIDLGVVNEDKLIEMLVRTGQIPADASDVDKRIALERYLEEKIRSGFKGDAQFGKKALEQRAKILKVIDKQKGPHKARVFALDVGQKRTDKVLALLIDFPDLPWDDNRLTKEHTEMLYDRYEPSHYQDLLFSDKGYTGPNGENFISMRQYYESESGNSYSVSGQAAGWYRASKNAAYYGGNSPGTNNDMNARELVREALDQLARDPNINLADYDIEDRYDYNGNGNFREPDGVIDHLMIFHASVGEEAGGGVLGADAIWSHRFNLGRYHVLEGTKSNVPGRFNGQFAAFDYTIQPIDAAAGVCAHEYGHDLGLPDEYDTQYTGTGEPVSYWSIMSSGSWAGKIGGTQPTAFSSWAKQFLQNSIGGRWINHEQLSINELEAKPRVVTLFQTTDNSRPNMVKVTLPMKRVEGIKPAEGEFSFYSNRGDDLKNRMSRPLTIPAGSQATLRFKAWFQIEKDYDYARVLINGKPIAGNITTMDDPFKSGLVPAISGQSDGWVDAQFDLSAWAGQTVELAFDYLTDGGLAMEGLYVDDLRLEVDGNQTLIDNAEGTSSFAFQGFTKNGGFHEANHYYLLQWRSHNDVDQGLANLKRFGQLMSFEPGLLVWYVDESYADNWVGKHPGEGWLGVVDADQNALVWSKTGEVAQTRFQVRDATFSLFDQAPLKLVTADGNTLEDMNLTANASFSDDQDYSSPQAPDSGRKVMPFGLKIDLLSQSKENEYGVVRLSKVTTENIAPVARFELKVEGLSVMSQNTSSDSDGNIVSYLWDFGNGQTSTEAAPTWSYTKAGSYSVTLTVTDDKGDSDTHQQTIKVDTPNALPQASANYIHLGRWVTMWSTSTDSDGRIVDTEWTLPNGKIKRGRMFTAIFPSYGHHDVQLKVMDDRGAVTTITIKVKL
Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen.
Q9KMU6
A0QKV0
IF1_MYCA1
Translation initiation factor IF-1
Mycobacterium avium complex (MAC)
MAKKDGAIEVEGRVVEPLPNAMFRIELENGHKVLAHISGKMRQHYIRILPEDRVVVELSPYDLSRGRIVYRYK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
A0QKV0
Q56A73
SPIN4_HUMAN
Spindlin-4
Homo
MSPPTVPPMGVDGVSAYLMKKRHTHRKQRRKPTFLTRRNIVGCRIQHGWKEGNEPVEQWKGTVLEQVSVKPTLYIIKYDGKDSVYGLELHRDKRVLALEILPERVPTPRIDSRLADSLIGKAVEHVFEGEHGTKDEWKGMVLARAPVMDTWFYITYEKDPVLYMYTLLDDYKDGDLRIIPDSNYYFPTAEQEPGEVVDSLVGKQVEHAKDDGSKRTGIFIHQVVAKPSVYFIKFDDDIHIYVYGLVKTP
Exhibits H3K4me3-binding activity.
Q56A73
B1W0N3
HIS3_STRGG
Phosphoribosyl-AMP cyclohydrolase
Streptomyces
MTSTPGATPPASSLDPAVAARLKRGADGLVPAIAQQYDTGEVLMLGWMDDEALHRTLTTGRCTYWSRSRQEYWVKGDTSGHVQHVKSVALDCDADTVLVKVDQTGAACHTGDRTCFDADALPLGK
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
B1W0N3
Q7V1D9
RLMH_PROMP
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Prochlorococcus
MLQTNRLSINAIGKIKKNWIREGINQYKKRMPDLIINESKSFNIDNIRVNNIIICLTEEGQSFNSIELTSLLLNFKNKKINFLIGDADGIPSDIKDKSNLLLSLSPLTFPHELARLILIEQIYRAISISNNSPYHRA
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Q7V1D9
Q252Y9
COAE_CHLFF
Dephosphocoenzyme A kinase
Chlamydia
MLDLLKVSITGDLSSGKTEACRVFQDLGAYVISADKVSHSFLVPHSHIGHRVIDLLGSDVVVDNAFDRKVIAEKVFDNLVLLQALEAILHPEVCRIIEEQYCLVAKENKYPLFIAEVPLLYEIQYANKFDRVILITADENTRRERFTRKTNCSDLNFYQRCARFSSNEEKMMHADIIIENNGTKEELRHKVEEYFYALKGAL
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Q252Y9
B7IHG0
CBID_THEAB
Cobalt-precorrin-6A synthase
Thermosipho
MKKELRYGYTTGSCATAAAKAATYMLFNDEILKSIKIDLPIGKEIELDIFYIERKEGEVICGVRKDAGDDPDVTHNMIIYAKAEKSKEFLITGGEGIGVVTKKGLPLQVGDYAINPVPRKMIESEVKKVLPEGKNVKITIFAPEGKYIAKRTLNPKLGIIGGISILGTTGIVEPLSDEAYKKTIDLEISMASSESNEICLVFGNYGKNFTTLSSKMPLVTMGNYVGFALESACKHRIKKVYLVGQIGKMIKVAGGIFNTYSYIADARNEIFTAYLSLYGLDRGILEKVMSANTTEEILDLIEGKVGKDFFENLALRIKEKCTQYVKGCLEVEVEIFSLKKGHLAKTWSDFK
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
B7IHG0
Q5E3F1
LPXA_ALIF1
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Aliivibrio
MIHETAKIHPSAVIEGNVTIEANVSVGPFTYISGNVTIGEGTEVMSHVVIKGDTTIGKDNRIFAFAIIGEESQDKKYGGEATTVVIGDRNVIRESVQIHRGTVQDRGVTTVGSDNLLCVNVHIAHDCVVGDNIIMGNNATLAGHVTVEDFAIVSALSPVHQFCTVGAHSFIGGASVVVQDVPPFVMAQGNHCKPFGINIEGLKRRGFEKAEIHAIRRAYKALYRNGNTLEEAKVEINKEIEAFPVLQGFLDLFEKSTRGIIR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q5E3F1
Q9BQ70
TCF25_HUMAN
Nuclear localized protein 1
Homo
MSRRALRRLRGEQRGQEPLGPGALHFDLRDDDDAEEEGPKRELGVRRPGGAGKEGVRVNNRFELINIDDLEDDPVVNGERSGCALTDAVAPGNKGRGQRGNTESKTDGDDTETVPSEQSHASGKLRKKKKKQKNKKSSTGEASENGLEDIDRILERIEDSTGLNRPGPAPLSSRKHVLYVEHRHLNPDTELKRYFGARAILGEQRPRQRQRVYPKCTWLTTPKSTWPRYSKPGLSMRLLESKKGLSFFAFEHSEEYQQAQHKFLVAVESMEPNNIVVLLQTSPYHVDSLLQLSDACRFQEDQEMARDLVERALYSMECAFHPLFSLTSGACRLDYRRPENRSFYLALYKQMSFLEKRGCPRTALEYCKLILSLEPDEDPLCMLLLIDHLALRARNYEYLIRLFQEWEAHRNLSQLPNFAFSVPLAYFLLSQQTDLPECEQSSARQKASLLIQQALTMFPGVLLPLLESCSVRPDASVSSHRFFGPNAEISQPPALSQLVNLYLGRSHFLWKEPATMSWLEENVHEVLQAVDAGDPAVEACENRRKVLYQRAPRNIHRHVILSEIKEAVAALPPDVTTQSVMGFDPLPPSDTIYSYVRPERLSPISHGNTIALFFRSLLPNYTMEGERPEEGVAGGLNRNQGLNRLMLAVRDMMANFHLNDLEAPHEDDAEGEGEWD
May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development.
Q9BQ70
Q9Y6Z9
SOU1_SCHPO
Sorbitol utilization protein sou1
Schizosaccharomyces
MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR
Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol.
Q9Y6Z9
D5CE33
RUTB_ENTCC
Ureidoacrylate amidohydrolase RutB
Enterobacter cloacae complex
MTTLNARPEAITFSAPQSALIVVDMQNAYASPGGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFHKSNALKTMRKRPELQGKLLAKGGWDYQLVDELVPEAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSNVADFCDALNPPLARIA
Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
D5CE33
P62877
RBX1_HUMAN
E3 ubiquitin-protein transferase RBX1, N-terminally processed
Homo
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair . CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets . The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.
P62877
Q46HD3
TRMB_PROMT
tRNA(m7G46)-methyltransferase
Prochlorococcus
MRQHVNPLSQFFQLPLSLPSKNILFEKSHYPIHLDIGSAKGEFLIELATKCPDWNFVGLEIREPLVSLCEKKRRKLELTNLKFLFCNVNVSLDEWLSDLDFGQLKRVSIQFPDPWFKRKHFKRRVLKTNILNSIAKAMSKNGEIFIQSDIFELIEYMTNTIDENRYFTRKNVGDLRSINKNPYNVMTDREILSLKKNLLIYRVMYIRNSLLFTN
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Q46HD3
P27615
SCRB2_RAT
Scavenger receptor class B member 2
Rattus
MARCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFDSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANVQFGENGTTISAVTNKAYIFERNQSVGDPTVDLIRTINIPLLTVVEMAQQPFLREIIEAMLKAYQQTLFVTHTVHELLWGYKDEVLSLVHIFRPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFTKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDETLYIFPSDFCRSVYITFSSFENVEGLPAFRYKVPAEILANSSENAGFCIPEGNCMDAGVLNVSICKNGAPIIMSFPHFYQADEKFVSAIKGMRPNKEEHESFVDINPLTGIILRGAKRFQINTYVKKLDDFVETGNIRTMVFPVMYLNESVLIDKETASQLKSVINTTLIVTNIPYIIMALGVFFGLIFTWLACRGQGSTDEGTADERAPLIRT
Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting.
P27615
Q30TI8
FLIW_SULDN
Flagellar assembly factor FliW
Sulfurimonas
MKFDVCVPILGFENVKEVTLEKIDDAFMRMESSNDEHISFTLINPFALREYDFEIPDATQKLLEIDEKSNILILNIAIIQTPVEDTVVNFIGPMIFNTDNNKAAQLVLSESTKYGVAEKISLYLKK
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Q30TI8
Q67KC5
ARGJ_SYMTH
Arginine biosynthesis bifunctional protein ArgJ beta chain
Symbiobacterium
MEWLAGGVTAPAGFVAAGACADIKGNGAGKKDVALLASRVPCAAAGVYTTNLVKAAPVVLTRGRTETGELQAVVANSGNANACTGEQGMRDAAEMARLAAEALGIRPELMGVASTGVIGVPLPMDRVSAGIRAAAAALSPEGGADAAEAIMTTDTFPKQAAARLEIGGATVTIGAMAKGSGMIHPNMATMLGFVTTDAAVDAAALREALREATDRSFNMITVDGDTSTNDMVLVLANGLAGNPRIMPGSAHYRAFADALAAVLIHLAKEIARDGEGATKLIEVRVKGAATLSDARKAARAVCGSNLVKAAVFGEDANWGRVLAALGYSGAQFDPGRVDLWLGDLQMMRAGEPVAFDEAAAARVLREKEVVFTADLHAGECEATAWGCDLTYDYVKINGSYRT
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Q67KC5
Q8TKX4
PTH_METAC
Peptidyl-tRNA hydrolase
Methanosarcina
MSEYKQCIVTRDDLKLSKGKFAVQVAHAALSAAEWASKSDLEKWKEGGQKKIVLRVPTIKDLYELKEKARREGLPTALIQDAGLTEIPAGTVTVLGIGPAKEEVIDKVTRDLKLV
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q8TKX4
Q9CKC8
ZIPA_PASMU
Cell division protein ZipA
Pasteurella
MDLNTILIILGIIALIILVVHGLWANRREKSQYFKSANTFTRDSRLREPPAHIQSASEEKKDANTSTPTAEVSPAQRTFAFEAEKQFAHEQQAVEQAIENIKITLPKEEQPYQAKIEPDTPPTSPALTTIAEVENYANQEEGIDTHSEQLRQQLADLAQQSPSVTLAALQEEQALMESQAQQQASEDVRQDTDATFIMMYVVAPENYQFQGARLAKILDELGFLFGEHNIYHRHSDLSVNSPVLFSVANIEQPGTFDYNMHDFSTVGIALFMQLPSEGNDLMNLRMMIRAAKSIAEDLGGFVLTDQQAIFDDQAEKAYLDKVR
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Q9CKC8
Q6AR67
TAL_DESPS
Probable transaldolase
Desulfotalea
MKFFIDTANLDEIREGVELGLVDGVTTNPSLIARENLPFEELIAEICKIVDGPVSAEVISLDAPGMVAEAKKLASIDEKVVIKVPMTAEGLKAVRQLSAAGIKTNVTLIFSANQALLAAKAGASYVSPFVGRLDDIGVNSADLISDILTIFDNYGYASEVIVASVRGPQHVLDSALLGADIATIPLKTIKQLTKHPLTDKGMEQFLADWEKRTQ
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q6AR67
Q749B2
RS4_GEOSL
30S ribosomal protein S4
Geobacter
MARYTGPSCRLCRRENMELFLKGERCYTDKCAIKRRNYPPGQHGQGRPKVSNYGVQLREKQKVRRIYGILEKQFRSYFQEADRLKGVTGENLLSLLERRLDNVVYRLGFAASRTEARILVRHNHFTLNGKKANIPSIQLRAGDVVELKEKSRKIACINESLDAVVRRGIPQWLELEKDAYKGVVKTLPVREDITMPIQEQLIVELYSK
With S5 and S12 plays an important role in translational accuracy.
Q749B2
Q5H0A7
G6PI_XANOR
Phosphohexose isomerase
Xanthomonas
MTQTNGFDALHAHAQRLRGAAIPALLAAEPERPTQYAWQVGPLYFNFARQKYDRAALDALFAIARERDLAGAFQRLFRGEQVNVTEQRAALHTALRGDLTDAPVASEAYATAAEVRQRMGALIQQLEATDVTDIVSVGIGGSDLGPRLVADALRPVSGARLRVHFVSNVDGAAMQRTLATLDPARTAGILISKTFGTQETLLNGSILHAWLGGSERLYAVSANPERAAKAFDIAPGRVLPMWDWVGGRYSLWSAVGFPIALAIGFERFEQLLEGAAQFDAHALNTPLEENVAVLHGLTAVWNRNLLGSATHAVMTYDQRLALLPAYLQQLVMESLGKRVKLDGSAVDSDTVSVWWGGAGTDVQHSFFQALHQGTSVVPADFIGTVHNDDPYAENHVALMANVLAQTEALANGQDSSDPHRSYPGGRPSTVILLDALTPQALGALISMYEHSVYVQSVMWGINAFDQFGVELGKQLASQLLPALKGESADVADPVTRELLSKLRG
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q5H0A7
A5EVK4
COAX_DICNV
Pantothenic acid kinase
Dichelobacter
MYLLIDVGNSRIKWLYGNKVPSTIEAVSYKQDWQMKLIRAWHLLPEPEAIALSSVNKAEITTTIEEIVRQLWHKTVKIFVSQKQTNHTLTVVYQKPEKLGSDRYLAMLGARSLCHDPLCVVGCGTAITLDAVDGDGRHLGGFILPGMRLAENALLQNTQKLVPMRWTPHLLGNDTASCISAGIHHALPAGVDHIIDELEGQCGYYFKRFAFGGDAQILFGNRPTYRIEPDLIFGGMFAHLSPPKQV
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
A5EVK4
A3DEU4
NADD_ACET2
Nicotinate mononucleotide adenylyltransferase
Acetivibrio
MEVNVKRIGILGGTFDPIHNGHLIMAEIIRGAFELDRVLFIPSGNPPHKKNQTVTDAEHRYNMVCEALKGNPYFEKSRIEVDREGYTYTIDTLGILNEQYRGIADLYYIIGADVLYDLLTWKDYEKVFGICKFIAALRPGTGKEGFRERIKYLEDRFSASILEAEIPLIEISSTMIRNRVKEGKSIKYLVPETVENYIKKEGLYLK
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
A3DEU4
Q3AU08
RECA_CHLCH
Recombinase A
Chlorobium
MTMDNPKVEQAGHAVDSAKLKQLNLAVDALEKQFGKGTIMRMGDGSAGLTVQAISTGSMALDFALGVGGLPRGRVTEIYGPESSGKTTLALHVIAEAQKEGGITAIVDAEHAFDPSYARKLGVDINALLISQPESGEQALSIVETLVRSGAVDVVVVDSVAALVPQAELEGEMGDSSMGLQARLMSQALRKLTGAISKSSTVCIFINQLRDKIGVMYGSPETTTGGKALKFYSSVRLDIRKIAQLKDGDELTGSRTRVKVVKNKVAPPFKMAEFDILYGEGISALGELIDLGVEFGVIKKAGSWFSYGTEKLGQGRESVKKILREDPVLYQKIHMQVKELMTGHTEIISSPTE
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Q3AU08
A1QZM2
DNAA_BORT9
Chromosomal replication initiator protein DnaA
Borrelia
MQEGKNIWSLILAAIRKELSEEEFYIWFENLYFIDATDESIKISAPNSFHKNQVEKRFSKRIKEILTEKGHNTINVEFINPPKEPKTHSMELKNTSLKDISIQQDSPEKRTILNTHTKNIIEHTKHYVIKEDIHTKYRNPFLKKKYTFENFIIGPNNKLAYNASLSIAKNPGKKYNPCLIYGGVGLGKTHLLQSIGNKTEELHKEFKILYVTAENFLNEFVESIKTNETKRFKKKYRHLDMLLIDDIHDLQKKEGIQEELFHTFNALYEDNKQMVFTCDRQPSELINFTDRLKSRFTRGLNVDISKPNFELRVAIIEKKAEEDGIKVPKNILNLVAKKVTTNIRDLEAAVTKLKAHIDLEDIEIDTSIVDKIIKEIIAYENDKTNTNNTINIESIKKVILRELKLTNKDIEGNSKKPEITKARHIYAYLLRNFTELSTIEIGKIIGGKTHSTVLYSINKIDKERNNDLEINNLIIELMNKINKN
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.
A1QZM2
O13297
CET1_YEAST
mRNA 5'-triphosphate monophosphatase
Saccharomyces
MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
O13297
Q8DK88
METK_THEVB
Methionine adenosyltransferase
Thermosynechococcus
MRYLFSSESVTEGHPDKICDQIADAILDALLTQDPQSRVAAEVVVNTGLVLITGEITTKAQVNYVNLARQKIHEIGYTDANNGFAANSCAVLVALDEQSPDIARGVDTAQEAREQLSDAELDRIGAGDQGIMFGYACNETPEYMPLPISLAHRMARRLAAVRKTGQLPYLRPDGKTQVTVIYEDGKPVGIDTILISTQHTATIDDISEESAVQAKIKADLWEAVVKPVFADLTLQPDGNTRFLVNPTGKFVIGGPQGDSGLTGRKLVVDTYGGYARHGGGAFSGKDPTKVDRSAAYMARYIAKNIVAAGLADKCELQISYAIGVARPMSLFVDTFGTGKLSPEQLLELIKTHFDLRPAAIIQTLNLRHLPQERGGRFYQDVAAYGHFGRHDLDLPWEKLDKVADLQAAAAQFLSAV
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Q8DK88
B5BIA8
CLSA_SALPK
Cardiolipin synthase A
Salmonella
MTTFYTVVSWLVILGYWVLIAGVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLSVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAQENSSVASSLFKLCERRQGIAGVKGNQLQLLTDSDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRDIHCRLMLDSAGSVAFFRSPWAAMMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMVMIDNYIAYTGSMNMVDPRFFKQDAGVGQWVDLMARMEGPVATAMGIVYSCDWEIETGKRILPPPPDVNIMPFEQASGHTIHTIASGPGFPEDLIHQALLTATYAAREYLIMTTPYFVPSDDLLHAICTAAQRGVDVSIILPRKNDSLLVGWASRAFFSELLAAGVKIYQFEGGLLHTKSVLVDGELSLVGTVNLDMRSLWLNFEITLVIDDTGFGADLAAVQDDYISRSRLLDARLWVKRPLWQRITERLFYFFSPLL
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
B5BIA8
Q7SXE8
CDK9_DANRE
Cell division protein kinase 9
Danio
MSKYYDGVEFPFCDEFSKYEKLAKIGQGTFGEVFKAKHRQTGKKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKGEATQFNRYKGSIYLVFDFCEHDLAGLLSNANVKFTLAEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQGNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPGVDKKYELYQKMELPKGQKRKVKDRLKAYVKDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKNMLSTHNTSMFEYLAPPRRRGHMPQQPANQNRNPATTSQSEFDRVF
Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) polr2a, supt5h and rdbp. This complex is inactive when in the 7SK snRNP complex form. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export.
Q7SXE8
C0MFA6
DEF_STRS7
Polypeptide deformylase
Streptococcus
MSAQDKLIKAQHLIDMNDIIREGNPTLRAVAKEVEFPLSDDDIILGEKMMQFLKHSQDPVMGEKLGLRAGVGLAAPQIDVSKRIIAVLVPNPEDSEGNPPKEAYSMEEVLYNPKIVSHSVQDAALADGEGCLSVDRVVEGYVVRHARVTVEYYDKHNEKHRIKLKGYNAIVVQHEIDHINGVLFYDRINAKKPFEAKEGMLILE
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
C0MFA6
Q1GZA1
CYNS_METFK
Cyanate lyase
Methylobacillus
MSRLDVTEKIITAKVMKGLKWADVAAKLNLSKEWVTAACLGQMTLNAEQAKIIAEIFDLSDEDQKWLMVTPCKGSLPTAVPTDPLIYRFYEMINVYGTTIKQLIHEEFGDGIMSAIDFKMDLQRVADPMGDRVNIVLNGKFLPYKQF
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Q1GZA1
A4YSK8
RL18_BRASO
50S ribosomal protein L18
unclassified Bradyrhizobium
MSRAKVTNARRKQRVRLSLRRSAGGRPRLSVFRSSKHIYAQVIDDQKGETIASASSMEKEMRSAGNTGADIDAAKAVGKLLAERAVKAGIKEVVFDRGGYLYHGRVKALADAARESGLSF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
A4YSK8
B8EFD7
TAL_SHEB2
Transaldolase
Shewanella
MANTLEQLKLYTTIVADTGDIEAIKRYQPEDATTNPSLILKAAQIPEYESLIDNAIDWAKSQSDDLAQQLDDASDKLAVNIGVEILKLVPGRISTEVDARLSFDKEQSIAKAHKLVRLYKEAGVDKSRILIKLASTWEGICAAKELEKEGINCNLTLLFSFAQARACAEAGAYLISPFVGRILDWYKKDTGKDYDAVNDPGVVSVTEIYNYYKQHGFNTVVMGASFRNIGEIIELAGCDRLTIGPSLLEELANSQIDITPKLVAATSTVAAEAPLTEAQFRWDFNQDPMAVDKLAEGIRNFAIDQGKLEVMLTAKLAN
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
B8EFD7
Q3IYX7
PGSA_CERS4
Phosphatidylglycerophosphate synthase
Cereibacter
MNWSIPNILTVLRLLAAPGVAVMFLYFHRPWADWFALTLFILAAVTDFFDGYLARLWKQESKFGAMLDPIADKAMVVIALVIITGYSGMNPWLILPVTLILFREVFVSGLREFLGAKASLLKVTKLAKWKTTAQMVAIAILFLGTGLEHLEGIARQGMTWEQYARAVSAGEADPIRSCGMHGCSSYATWLGLALIWIAAALTFITGWDYFRKALPYLKDEK
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Q3IYX7
Q2GIJ7
YBEY_ANAPZ
Endoribonuclease YbeY
phagocytophilum group
MPVEVSTIDRKWYRIIRKPKATSQEIVLFALRELKVDRYNPIVSVVLAHDALLLELNHKYRNINKPTNVLSFNYEALSHNCCLGEIFLSIDRLTYESKTLGVEVHAHFTHMLIHGVLHILGYDHEVPEDAQEMQALEIDLLSKRSIENPYLIQE
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q2GIJ7
Q9KA72
DPO3_HALH5
DNA polymerase III PolC-type
Halalkalibacterium (ex Joshi et al. 2022)
MNEEQRVRQERFKLLMEQLLIPEDVTANHLKDGKIEKLTIKKDERRWHFQLSIPTVLPASIYELLADRLVQTFSHIAKVSFQIQYGQPDLSEQVWQSYWPLIVAKLTNISQPLKEMLEKQTPRFDGKRLVIQVGNETEAIALKRKLTEPLQQAVQSFGFPAVQLDAEVKESKQAFEKFVEQRKQEDHSKVVEAILEKKKLEQQVEKKMKEEKLTIGYPIKDEPVPLETIVEEERRITVQGYIFAAETKELRSGRTLLTFKITDYTDSILVKMFSRDKEDIPLLQAVKKGMWVKVRGGVQNDTFVRDLVMIANDVNEVSGKETKDEAPDDEKRVELHLHTAMSQMDGISSAGAYVTQASKWGHKAIAITDHGVVQAFPEAYGASQKHGIKVIYGVEANLVDDGVPIAYNEAHIPLLDSEFVVFDVETTGLSAVYNKIIELAAVKVKNGEIIDRFERFADPHEPLTNTIIELTGITDDMLKGQPEVEQVLNEFHAFIGDAVLVAHNASFDMGFLNTGFQKMGLGEAKNPVIDTLELGRFLYPTLKNHRLNTLCKKFDIELVSHHRAIYDAEATGHLLWRMVKDATERDILYHDQLNDNMGEGNFHRQRPSHCILLAQTQEGLKNLYKLVSMAHVEYFYRTPRIPRSQLQKHREGILVGSGCDKGEVFEGMMQKTPQEVEEIAKFYDYIEVQPLANYEHLIEKELVKSREALQEIVANIVKLGEQLGKPVVATGNAHYLKEEDYIYRKILIASQGGANPLNKQTLPQVHFRTTSEMLEAFAFLGEEKAKEIVVTNTNHIADQIEEIHPIPDKLYTPKIEGADEEIRQMSYNRARKIYGDPLPEIVEARLEKELKSIIGHGFAVIYLISHKLVKKSLDDGYLVGSRGSVGSSFVATMTEITEVNPLPPHYVCPNCHHSHFFNDGSVGSGYDLPDENCPKCGTPYVKDGQDIPFETFLGFKGDKVPDIDLNFSGEYQPRAHNYTKELFGESYVYRAGTIGTVAEKTAYGYVKGYQSDHDLHFRGAEIDRLVTGCTGVKRTTGQHPGGIIVVPDYMDIHDFCPIQFPADDRGAEWKTTHFDFHSIHDNLLKLDILGHDDPTVIRMLQDLSGIDPKTIPTDDPEVMKIFSGPDVLGVTEEQILCKTGTLGIPEFGTRFVRQMLEETKPSTFSELVQISGLSHGTDVWLNNANELIYNGTCELKDVIGCRDDIMVYLIYKGLEPSLAFKIMEFVRKGKGLQPEWIEEMKKHDVPDWYIGSCLKIKYMFPKAHAAAYVLMAVRIAYFKVHYPILYYASYFTVRADDFDLDTMVKGSAAIRAKIEEINGKGLDASPKEKSLLTVLELALEMVERGFSFQKVDLYRSEATEFLVEGNTLIPPFNALTGVGTNAAINIVKARDEREFLSKEDLQQRSKITKTVLENLDAHGCLEGLPESNQLSLF
Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Q9KA72
Q057C6
RS13_BUCCC
30S ribosomal protein S13
Buchnera
MTRIAGINISDKKHILVALTSIYGIGISLSKKICFSIGIRCDVKINSLTKEKIESLRSIISKFLVEGDLRREKTINIKRLMDIGCYRGLRHRKHLPVRGQRTKTNARTRKGPRKLIKSR
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Q057C6
Q1LI61
RS11_CUPMC
30S ribosomal protein S11
Cupriavidus
MAKGPNNAAQRARKKVKKNVADGIAHVHASFNNTIITITDRQGNALSWATAGGQGFKGSRKSTPFAAQVAAENAGRVAQDQGIKNLEVRIKGPGPGRESAVRALNALGIKIAVIEDVTPVPHNGCRPPKRRRI
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Q1LI61