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
|
|---|---|---|---|---|---|---|
Q5LZD1
|
RNZ_STRT1
|
tRNase Z
|
Streptococcus
|
MELQFLGTGAGQPSKARNVSSLVLKLLDEINEVWMFDCGEGTQRQILETTIKPRKVKKIFITHMHGDHIFGLPGFLASRSFQSSEEQTDLEVYGPVGIKQYVMTSIRTSGTRLSYHVHFKEIDENSLGLVMEDDKFAVYADKLDHTIFCVGYRVVQKDLEGTLDAEALKAAGVPFGPLFGQIKNGQDVVLEDGTKIIAKDFISAPKKGKVITILGDTRKTNASVRLGLGADVLVHESTYGKGDEKIAKSHGHSTNMQAAQVARDASAKRLLLNHVSARFLGRDIGKMAADAKTIFENTHIVRDLEEVEI
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
Q5LZD1
|
B4SP14
|
OBG_STRM5
|
GTP-binding protein Obg
|
Stenotrophomonas maltophilia group
|
MKLVDEAEIEVFAGNGGNGCIGFRREKFIPLGGPDGGDGGAGGSVYIRADENLNTLVDFRHDRIFKAQRGENGMGRQAYGKGGEDLTITVPVGTVIINVATDEIIGDLTQHGDRLLVAQGGRGGLGNMHFKSSTNRSPRQALPGEPGEERTLKLELKLLADVGLLGFPNAGKSTLIRAVSAATPKVADYPFTTLYPNLGVVKVENYRSFVIADIPGLIEGAADGAGLGAQFLRHLQRTRLLLHLVDISPMEGGVEGISPVEQVRAIERELEKHDPELLQKPRWLVLNKADLMFEDEAKAAAEQIVAELGWKEPWFLVSALGREGTFPIMSRIMAFFDRQKEDELEARNAL
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
B4SP14
|
A3DA26
|
ARGC_SHEB5
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Shewanella
|
MKNIAIIGASGYTGAQLTALIHAEAELTIQGLYVSENSLDKGKPLADLYPSYSHIALTLSPLSEDAKAKIVAEADAVVLATEHSVSLHLAAWFYSQGLAVFDLSGAYRFSDVAQYPKWYGFEHEYPEVLAKAVYGLAEWNAKEIAATKMIAVPGCYPTASLTALKPLASLLTSAYPVINAVSGVTGAGRKAQLHTSFCEVSLTPYGVLGHRHQPEIATQLGQEVIFTPHLGNFKRGILATITVQLKPGTTTADVAAAYSVYDQAPLVTVKHNQFPKVDDVVLTPNCHLGWKFDENSGYLVVASAIDNLMKGAASQALQCIKIHFNL
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
A3DA26
|
A6WNN5
|
SERC_SHEB8
|
Phosphohydroxythreonine aminotransferase
|
Shewanella
|
MSAIYNFCAGPAMLPAAVMKKAQQELLDWNGQGVSVMEISHRSKEFIALTQQAESDLRELMQIPTNYHVLFMHGGGRGQFSAVVNNFLGNHGRALYLVSGQWSSAALAEAQKLVGEAQIDSLNIVEKHNGLNAVVLPDLHKIDADYRYVHYCPNETVDGIEIFDELDSPWPIVADLSSTIMSREIDVSRYGLIYAGAQKNIGPSGLSIVIVRDDMLKLPSLPQSSIMDYRLAVEHDSMFNTPPTFAWYLAAEVFAWLKSTGGISSIAKINQQKAQMLYQCIDGNAFYRNGVVAANRSQMNVTFQLVNEALDGEFLKQAQIAGLVALKGHRIVGGMRASLYNAMPLDGIVALVKFMNEFAAKHS
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
A6WNN5
|
A5FNY2
|
AROK_FLAJ1
|
Shikimate kinase
|
Flavobacterium
|
MEKIVLLGYMGCGKSTIAQNLSKITQIPFLDLDICIEKRANLSIKEIFEQHGEIYFRKLEHEMFLELLQSSENAIIGLGGGTPCYANNHLLLQRDDIVSVYLKASIDTLYNRLVHNKSKRPLIANMDEEEMKEFIAKHLFDRSFYYNHAQHKVAVDNRTIDETVQDILDILA
|
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
|
A5FNY2
|
Q5PN21
|
TUSC_SALPA
|
tRNA 2-thiouridine synthesizing protein C
|
Salmonella
|
MKRIAFVFSTAPHGSASGREGLDALLATSALTEALGVFFISDGVFQLLPGQKPDAVLARDYIATFKLFDLYDIDQCWICAASLRERGLENVNFVVNATPLEPVALRRELGNYDVILRF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
|
Q5PN21
|
A8GV48
|
RRF_RICB8
|
Ribosome-releasing factor
|
belli group
|
MDKVTLKKNLQEKMDKALKVLDHELKGLRTGRASVNLLDSVTVEAYGDRMPLSQVASLTTPDARTINVQVWDKSMVSSVEKAITVANLGLTPSSDGQLIRLPIPALTEERRKELAKLAHKYGEDTKISLRNIRRDGNEELKKMEKDNIIAKDEHHSLAEQVQKLTDEYSSKVDSAIKQKEQEIMTV
|
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.
|
A8GV48
|
O31854
|
CDAS_BACSU
|
Diadenylate cyclase
|
Bacillus
|
MKAMRYEQISENAFKGKIQVYLEQILGDASLILKTLHEKDQCLLCELDDLGHVFQDMQGIASSFYLQSYIEEFTPAFIELAKAIKALSEHKHGALIVIERADPVERFIQKGTSLHAEISSSLIESIFFPGNPLHDGALLVRENKLVSAANVLPLTTKEVDIHLGTRHRAALGMSGYTDALVLVVSEETGKMSFAKDGVLYPLISPRT
|
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis . Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP . In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
|
O31854
|
P49518
|
RBCR_TRICV
|
Probable RuBisCO transcriptional regulator
|
Trieres
|
MTLPFTLQQLRILKAIATEKSFTRAAEVLFVSQPSLSKQIKTLESRLNISLLNRENNIVSLTQAGKLFLEYSERILALCEESCRVLNDLKTGDRGNLIVGASQTIGTYLMPRVLALFAQNHPQINIEVHVDSTRKIAKRVLEGDIDIAVVGGNIPEEIEKNLKVEDFVNDELILIIPKSHPFALKKKKKINKDDLYHLNFITLNSNSTIRKLIDNILIQIAFEPKQFNIIMQLNSIEAIKTAVSLGLGAAFVSSSAIEKEIELKTIEIVTIEDIKITRILSIISNPECYRSKAVDLFYNELWTLKNTSN
|
Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression.
|
P49518
|
P05107
|
ITB2_HUMAN
|
Complement receptor C3 subunit beta
|
Homo
|
MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES
|
Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL . Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity . Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils . Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation . Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages . In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils .
|
P05107
|
Q9XI37
|
PV42A_ARATH
|
CBS domain-containing protein CBSCBS4
|
Arabidopsis
|
MQEEKSKEDHSRLINVTAKDLTVRNRRLVEVPYTATLSHAMNTLVANSISALPVAAPPGHWIGAGGSMIMESDKQTGVVRKHYIGILTMLDILAHIAGEDSNLSDLDRKMSSQVSSIIGHCLEGLSLWTLNPNTSVLECMEVFSKGIHRALVPVESSIESNNTIAGVELIESASAYKMLTQMDLLRFLKDHHFDDLKTVLSRSISDLGAVNDSVYAITERTTVSNAINVMKGALLNAVPIVHAPDIAQEDHLQLVNGRHRKVIGTFSATDLKGCRLPELQTWLPLTALEFTEKTSGKEREVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSLRSTLS
|
Plays redundant role with PV42b in regulating male gametogenesis and pollen tube guidance.
|
Q9XI37
|
Q0ST16
|
HEM3_CLOPS
|
Pre-uroporphyrinogen synthase
|
Clostridium
|
MELIIATRKSKLAQVQTEKVMELLKKKENVDSKKLLVMTEGDRRLDVSLNKIGGKGLFVKEIELALLNKEAHGAVHSMKDVPFELPSEFELVAMPEREDIRDAFVSLNGSTLSNLRKGARIGTSSIRRAEQLKLFRDDLEIVPIRGNVQTRIKKITEENLDGIILAAAGLKRLGMEDVISDYFDPKVFLPAIGQGALGIECLKDGEFNDYFKALDSKEVRTTVEAERSFMKVLNGGCHSLIGAYSEVKDNDLYMIGTFTVNNRIVKKDILGNKEDNILLGKKLAEKILGEV
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q0ST16
|
A7HWJ3
|
SYT_PARL1
|
Threonyl-tRNA synthetase
|
Parvibaculum
|
MIKLKLPDGSVREHEVPLDGLAFAESIAKSLAKKAVAIKIDGQMKDLSTVIDRDAEVEIVTRETPDGVDLLRHDASHVMAEAVQELFPGTQVTIGPVIENGFYYDFARAEPFKAEDLEKIEQRMREIVDRDETITREVWDRDAAVEYFKKIGEIYKAEIIASIPAGEQVSVYRQGNWLDLCRGPHLPSTGKLGKAFKLTKLAGAYWRGDSRNEMLQRIYGTCWANENDLKAYLTMVEEAERRDHRKIGREMDLFHLQEEAQGSVFWHPKGWRIWQALEQYVRRRIDAAGYVEVRTPQLLDSKFWEQSGHWGKYRENMFVVPDEVPSTDEDAPVLSGKAKLMAIKPMNCPAHIQIFKQGVKSYRDLPLRMAEFGCCHRNEPHGALHGLMRVRQMTQDDAHIFCTEDQIKEETEAFVALLESVYEDMGFTGTKLRLATRPDVRAGTDETWDKAEKALEEALKALGKEFDFAPGEGAFYGPKLEFHLRDAIGRSWQLGTLQLDFVLPERLDASYIGEDGNKHRPVMLHRAILGSLERFIGILIENYEGRFPMWLAPVQAVVTTITSDADPYAEEMLQKLRDAGIRAELDLRNEKINYKVREHSVAKVPAIFVAGKREAEEGTVSIRRLGSQQQQTMKLDEAIKALAEEATPPDMR
|
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).
|
A7HWJ3
|
O09160
|
FUT1_MOUSE
|
Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1
|
Mus
|
MWTPSRRQLCLAFLLVCVLSAGSFFFHLNGGNFFRNGLTLSVLCSDYHLLKSPVAMVCLPHPLQTSNGSPSCPEQSSSLSGTWTITPGGRFGNQMGQYATLLALAQLNGRQAFIQPEMHAALAPVFRISLPVLDPEVDSLTPWQHLVLHDWMSEEYSHLEDPFLKLSGFPCSWTFFHHLREQIRREFTLHNHLREGAQYLLSGLRIGPAGIRPHTFVGVHVRRGDYLEVMPNRWKGVVGDRAYLQQAMDWFRARHKDPIFVVTSNGMKWCLENIDTSHGDVVFAGNGQEGTPGKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFRPEAAFLPEWVGINADLSPLQAQFDPWKPDSLFRLV
|
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens . H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis . Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a .
|
O09160
|
P08281
|
GLNA2_PEA
|
Glutamate--ammonia ligase
|
Pisum
|
MAQILAPSTQWQMRITKTSPCATPITSKMWSSLVMKQTKKVAHSAKFRVMAVNSENGTINRVEDLLNLDITPFTDSIIAEYIWIGGTGIDVRSKSRTISKPVSHPSEVPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNILVVCDAYTPAGEPIPTNKRHRAAEIFSNPKVEAEIPWYGIEQEYTLLQTNVKWPLGWPVGGYPGPQGPYYCAAGADKSFGRDISDAHYKACIYAGINISGTNGEVMPGQWEYQVGPSVGIEAGDHIWASRYILERITEQAGVVLTLDPKPIEGDWNGAGCHTNYSTKSMREDGGFEVIKKAILNLSLRHKIHIEAYGEGNERRLTGKHETASINDFSWGVANRGCSIRVGRDTEKNGKGYLEDRRPASNMDPYVVTALLAESTLLWEPTLEAEALAAQKIALKV
|
The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.
|
P08281
|
Q57DX4
|
FABH_BRUAB
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
Brucella
|
MIRSVVRGIGSALPKRVMKNTDFEGIVETSDEWIVQRTGIRERHIAGEGETTVSLGAAAARAAIENAGLQPSDIDLVLLATSTPNNTFPASAVAIQRELGITRGFAFDLQAVCSGFIYAITTADLYIRGGMARRVLVIGAETFSRILDWTDRTTCVLFGDGAGAIVLEAAEGHGLTSDRGILAANLRSDGNHKEKLYVDGGPSTTQTVGHLRMEGREVFKHAVGMITDVIEASFEATGLTAEDIDWFVPHQANKRIIDASAKKLHIAEEKVVITVDRHGNTSAASVPLALATAVADGRIKKGDLVLLEAMGGGFTWGAVLVRW
|
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
|
Q57DX4
|
A8YTF2
|
RL7_LACH4
|
50S ribosomal protein L7/L12
|
Lactobacillus
|
MALDTDKIIEELKGASILELNDLVKAIEDEFDVTAAAPVAAAGAADAGAAKSEFDVELTEAGQEKVKVIKAVRDITGLGLKDSKDLVDGAPKNVKEGVSEDEANDIKAKLEEVGATVTLK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A8YTF2
|
Q822V6
|
GUAA_CHLCV
|
Glutamine amidotransferase
|
Chlamydia
|
MSNILILDFGSQYTNVLAKKIRLLSVFCEVLTWNTPLEKILQISPSGLIFSGGPHSVYQENSPKVDKEIYNSNIPILGVCYGMQLIARDFGSEVQGGKSEFGYTPIVFYPSELFKGLVDQDAFHTEIRMSHCDSVVIPPKDFFVIASSQHCPIAAIECPEKKLFGLQFHPEVSDSQAVGDKILSNFVKHICQASETWKIETIEKQLIQSIKEKVGETERVLLGLSGGVDSSVLAVLLHNALGDRLSCVFVDTGLLRKNEVEEVKQQFSSLGLEILVVDASEKFFHDLSGIEDPEQKRKVIGAAFIEVFDEVSRNLDVQWLAQGTIYSDVIESAKSCDATQVIKSHHNVGGLPEKLNLKLLEPLRFLFKDEVRALGKVLGLPDVLISRHPFPGPGLGVRVLGEVRREYVEIVKNADSIFIEELKKANLYHKVSQAFAVFLPCKSVAVKGDCRHYGYTIALRAIESTDFMTACWPSLSREFLNRCSSRIINEIPEVCRVVYDISDKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q822V6
|
Q7MQZ8
|
RS6_WOLSU
|
30S ribosomal protein S6
|
Wolinella
|
MRHYETMFIVKPTLTPEEIVEKINFYKEAIIKNGGEICATQDMGMRNLAYEINKNKRGYYFVVYFKSAPSLVIELERLYRINEDILRFIVIKYESKKEQNAWNTMVDKVNKKAEAPKSAPVAAPETAPVAPEATPEA
|
Binds together with S18 to 16S ribosomal RNA.
|
Q7MQZ8
|
A8MD44
|
METK_CALMQ
|
Methionine adenosyltransferase
|
Caldivirga
|
MARNIVVSGIRRPPTEDLPVELVERKGLGHPDYIADSISEYVSRELSKYYMENFGTILHHNVDKVLVIGGNAQVKFGGGEIIEPIRIIVSGRATTEVKSSTGVVKVPIGSIILSAARKFIIDNFRFLNPDQHLVIDYKVGQGSVDLVGVYELGVSSGGVPLANDTSIGVGFAPLTVTERLVYETERLLNSREFKARYPEVGEDVKVMGLRRGRKITLTVASALVSRLIKDKDHYISVKEDVVNAIYDNAVKLANGYEVEVHLNTADNPEHGIYYLTYTGTSAEHGDDGMTGRGNRANGLITPMRPMSMEATAGKNPVSHIGKIYYVLANMIAKRIHDEVKGTREVYVYLLSQIGKPIDNPLIANVEIITNEGEVTSEMKREAEAITDEEISRVTRLTSMFVKGEITPF
|
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
|
A8MD44
|
Q732C1
|
CTAA_BACC1
|
Cytochrome aa3-controlling protein
|
Bacillus cereus group
|
MQRFIKWLAVITSLDLLIVLLGGALVTKTGSGQGCGKSWPLCNGEFVPSNLSMETIIELSHRLTSGSAGILVTLLCILSWKYYKHVRETKTLAILSFVFLVAQALMGAAAVVWGQMPAVLAIHFGISLISFASVILLTCLIFEIDQKFDARSLIMDKKMKFHIYGVTIYSYIVVYTGALVRHERASLACPDFPLCSKNRPMPTQLHEWVQMGHRVAAMLIFAWILYAMILAIRHYKQQPVVYWGWIISFILVTLQAIVGILVVFTNASLSMALLHSLFISCLFAVLCYLVMLGTRSKVNAKEAASTSKQTK
|
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
|
Q732C1
|
P59415
|
TRPD_BUCBP
|
Anthranilate phosphoribosyltransferase
|
Buchnera
|
MKIILNKIYQGDTLNISETYTLFKSIMLKKINNIELSAILIALKIRGESQNEILGAVKACLEHMITFPKPTYMFSDIVGTGGDNSNSINISTTSALVGSACGFKIAKHCNGNISSKTGSADILKKFGINIQISPEKSKKMLDELNICFLFAPQYHINFKVVTQVRKILRIKTIFNIIAPLLNPAMPKLTVMGVCNFKLMLPIAQVLKTLNYHHAIIVCSDNIDEVTLHSFTKIIELKNNNITSYILHPDDFGVKYCHKNDILGGNTEENYNIIKKILQGKGPSAVTETIAVNVAILFKIFGYSNLKKNTEYALKVIRSGKVYEKIIQLSKF
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
P59415
|
A9M2I4
|
RSMH_NEIM0
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Neisseria
|
MSGAESYRHITVLLNEAVDALAVREDGVYVDGTFGRGGHSRLILSRLGDAGRLIVFDKDPQAIAVAEELARSDKRVGVVHGGFASFQTALDGLGIGKVDGALFDLGISSPQIDDGSRGFSFRFDAPLDMRMDTMRGMSAAEWIAVASEQDLHEVIKNYGEERFSRQIARAIVAQRAESPIDTTRKLAQIVAQNVRTRERGQDPATRTFQAIRIFINRELEEVGAVLPQVMCRLKEGGRLAVIAFHSLEDRIVKQFVKKYSQHAPLPRWAAVREADLPEPPLKIAGRALKPGEAEIAANPRARSAVLRVAERTAGPIPEQSQRKTSEWQ
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A9M2I4
|
B1KF47
|
AROA_SHEWM
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Shewanella
|
MKQLRLETINKVQGTVNIPGSKSISNRALLLATLAKGTTTLTNLLDSDDIRYMLASLKQLGVNYRLSEDKTVCELDGLGAPINSNVAQTLFLGNAGTAMRPLCAALTLGEGEFILTGEPRMEERPIGDLVDALRQLGAEVTYLKSEGFPPLTINATGLNAGDVEIAGDLSSQFLTALLMVSPLAKGDVNIKIKGELVSKPYIDITLALMAQFGVKVINHDYERFEIKSGQSYVSPGKVLVEGDASSASYFLAAGAIKGGEVKVTGVGRLSIQGDVKFADVLEKMGAEIEWGDDYIISRVAKLNAVDLDMNHIPDAAMTIATAALFATGTTHIRNIYNWRIKETDRLAAMATELRKVGAIVDEGHDYISVTPPTKPHTANIDTYNDHRMAMCFSMLAFADCGITINDPDCTSKTFPDYFEQFAALAC
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
B1KF47
|
Q9JJN1
|
FGF21_MOUSE
|
Fibroblast growth factor 21
|
Mus
|
MEWMRSRVGTLGLWVRLLLAVFLLGVYQAYPIPDSSPLLQFGGQVRQRYLYTDDDQDTEAHLEIREDGTVVGAAHRSPESLLELKALKPGVIQILGVKASRFLCQQPDGALYGSPHFDPEACSFRELLLEDGYNVYQSEAHGLPLRLPQKDSPNQDATSWGPVRFLPMPGLLHEPQDQAGFLPPEPPDVGSSDPLSMVEPLQGRSPSYAS
|
Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity probably requires the presence of KLB. Regulates systemic glucose homeostasis and insulin sensitivity.
|
Q9JJN1
|
Q1XDI6
|
RK5_NEOYE
|
50S ribosomal protein L5, chloroplastic
|
Neopyropia
|
MAIGLKEKYKTTVTQSLKDEFQYKNVHEVPRFTKITINRGLGEASQNAKALESSIQELTLITGQKPIVTKAKKSIAGFKIREEVPIGIVVHLRKDKMYSFLEKLINLTLPRIRDFRGISPRSFDGKGNYNLGLREQLIFPEIDYDNIDQIRGLDISIVTTAKTDQEGLALLKKLGMPFRES
|
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
|
Q1XDI6
|
Q8GT66
|
TIC40_PEA
|
Translocon at the inner envelope membrane of chloroplasts 40
|
Pisum
|
MENLNLALVSSPKPLLLGHSSSKNVFSGRKSFTFGTFRVSANSSSSHVTRAASKSHQNLKSVQGKVNAHDFASISSSNGQETTSVGVSPQLSPPPPSTVGSPLFWIGIGVGFSALFSVVASRVKKYAMQQAFKSMMGQMNTQNNPFDSGAFSSGPPFPFPMPSASGPATPAGFAGNQSQATSTRSASQSTVTVDIPATKVEAAAPAPDINVKEEVEVKNEPKKSAFVDVSPEETVQKNAFERFKDVDESSSFKEARAPAEASQNGTPFKQGFGDSPSSPSERKSALSVDALEKMMEDPTVQQMVYPYLPEEMRNPSTFKWMMQNPEYRQQLEAMLNNMGGGTEWDSRMMDTLKNFDLNSPDVKQQFDQIGLSPQEVISKIMANPDVAMAFQNPRVQAAIMDCSQNPMSIVKYQNDKEVMDVFNKISELFPGVSGPP
|
Involved in protein precursor import into chloroplasts. Part of the motor complex consisting of a co-chaperone (TIC40) and a chaperone (HSP93) associated with the import channel (TIC110). Causes the release of bound transit peptides from TIC110 and stimulates ATP hydrolysis by HSP93. Involved in reinsertion of proteins from the chloroplast stroma into the inner membrane.
|
Q8GT66
|
O42493
|
NEUI_TAKRU
|
Neurophysin IT 1
|
Takifugu
|
MTGTAISVCLLFLLSVCSACYISNCPIGGKRSIMDAPQRKCMSCGPGDRGRCFGPGICCGESFGCLMGSPESARCAEENYLLTPCQAGGRPCGSEGGLCASSGLCCDAESCTMDQSCLSEEEGDERGSLFDGSDSGDVILKLLRLAGLTSPHQTH
|
Isotocin causes contraction of smooth muscles.
|
O42493
|
Q3Z967
|
RS8_DEHM1
|
30S ribosomal protein S8
|
Dehalococcoides
|
MISDPIADMLTRIRNGVMAKHEVVIMPASRMKQYLAKVMKQEGFIAGYEVIGAKPKRQLKIVLRYDEGGASFVSGLERISKPGLRVYVQRGEIPRVYGGLGIAIVSTSKGVMTGSQAWRQGLGGELLCKVW
|
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.
|
Q3Z967
|
P32606
|
PT127_YEAST
|
Putative mitochondrial translation system component PET127
|
Saccharomyces
|
MGFYNCRFLSRRLSVEPCRIGSAAKSYQQRSIYHFGAALTNAPSGRETPDKLRSDLHSALEMVDEIYDTNSTVEDIGNKEKGGRQKYTEEMDKAINLLKTNIKKEYRHDKYLERTKVGTYPGRRTYPGRRTYPARRTYPASRTYSDSNSYTFRINVQKIRHALVRYNQDGVQKHNQKPPRIGHGLTRVLYQPLSLQKLRDNRSRMYNFDPAVENINPEYLEKKSEKDVNTDSSGEGQSKPIFITPHKDESLLKVAKEHRKKYISSSSSMTSVLSQLHYLLSNFRRLNIIDSSISKNFPQKNCNYSESAYFPSAVILRKKRNGICSIDSDRSLDREIVLSVLGHYLEDFLTEKSLKNSSKSENYHYSSIDEFIVRSQLDAYDPNLPGTGVFDLKTRAVSAIRYDLSHVESNNNQTGYEIDKVYGEFESLEREYFELIRSALLKYSLQARIGKMDGIFVAYHNISKMFGFQYLPLDELDYIIHSSYNSKFDSLLKEKNDITKGIYGEEDYILHYDRDDRKIACLVANREFKMSMNLFSNILKHVEQLLNSSNTKWEKCKIMLKTEVEEKRSKSGRFFNEPVLNIVALPLSPEYEDKSLLVKDTSNEQLTEELLNLRSYNENLLEEHLNSLVGFKVNVKHFYHHHPNTTHLPDFALKKNDILDTESRKYISDMMKRDWYKDIPSTQTPNFFHASDVSTWEVNSTFTDINDKQILRKLYFKYLDVKLNALKNQVITRQEPDMSKKDEIMNRIKSLQARNDHRDNGSNKRYSNFGPTRLQTKLRAYAKKGALRRKLLERSNKFHI
|
Could be a component of the mitochondrial translation system with a role in promoting accuracy of translational initiation.
|
P32606
|
Q45410
|
EPSD_RALSL
|
NDP-N-acetyl-D-galactosaminuronic acid dehydrogenase
|
Ralstonia
|
MDRAIEIDFRTISVVGLGYIGLPTATVLASRQRELIGVDINQHAVDTINQARIHIVEPDLDMLVRAAVSQGYLRATTEPEPADAFLIAVPTPFLEDKQPDLTYIEAAAKAIAPVLKRGDLVVLESTSPVGATEQLSAWLSEQRSDLSFPHQLGEESDIRVAHCPERVLPGHVLRELVENDRIIGGMTPRCSQAAQRLYELFVRGRCIVTDARTAEMCKLTENAFRDVNIAFANELSMICDEIGVNVWELISVANRHPRVNILQPGPGVGGHCIAVDPWFIVDAAPESARLIRTAREVNDAKPHYVLDRVKQAARRFKEPVIACFGLSFKANIDDLRESPAIEIVRTMVQQQLGTVLVVEPHIKVLPASLEGVELLNAEPALSRADIVVLLVDHQKFRKLDTDRLQSRVVIDTRGMWSAKRLAA
|
Probably involved in synthesis of sugar components of EPS I, by converting NDP-N-acetyl-D-galactosamine into NDP-N-acetyl-D-galactosaminuronic acid.
|
Q45410
|
Q316L4
|
HIS6_OLEA2
|
ImGP synthase subunit HisF
|
Oleidesulfovibrio
|
MLSKRIIPCLDVRDGRLTKGIKFQGNVDIGDPVESARRYYEQGADEIVFYDITASHEGRGIFLDIVEKVASSIFIPFSVGGGINTVDDMRDALNAGAEKVSVNSGAVKDPDIISKGAARFGSQAIVLGMDVKRVAPTEAIPSGYEIVIHGGRKHMGMDALDWAKTAEVLGAGEICVNSIDADGTKDGYELTLTRMISDAVQIPVIASGGAGHPAHMYDALTKGGASAALIASIVHYGEYTIPDLKKQIQAMGCKMRLTW
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
Q316L4
|
Q478V2
|
THIE_DECAR
|
Thiamine-phosphate pyrophosphorylase
|
Dechloromonas
|
MATNKLRGLYAITPDRADGARLLADVEAALAGGCRVVQYRDKLSTMPEQVARAQALRELTRRFAATLLINDDLALAALVQADGVHLGKDDGNLVVARAILGPDKILGASCYADFAAAEAASRAGADYVAFGAVYPSPTKPQAANATTELFVRAKAELPAATCAIGGITLDNAPPLIVAGADLLAVITDLFSAPDIMARAAAYQRLFEEAHS
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q478V2
|
A4TEB1
|
XERC_MYCGI
|
Tyrosine recombinase XerC
|
Mycolicibacterium
|
MDTVLEEFDRYLELERGRSEHTRRAYLGDLRSLFAFLDERSPGTGLGGLTLPMLRSWLAAHAAAGTARSTLARRTSSVKTFTAWAVRRGLIGDDPASRLQVPKARRTLPSVLRQDQARDALEAAESGAQQGDPLAVRDRLVVEMLYATGIRVSELCGLDVDDVDTSRRLLRVLGKGNKQRTVPYGEPAHAALTAWLHEGRPALATADSGPALLLGARGKRLDPRQARTVVHQTVSAVGGAPDIGPHGLRHSAATHLLEGGADLRVVQELLGHSSLATTQLYTHVTVARLRAVHDQAHPRA
|
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
|
A4TEB1
|
A3D186
|
APAH_SHEB5
|
Diadenosine tetraphosphatase
|
Shewanella
|
MAHYFVGDIQGCFAELQKLLAKVDFNPSRDELWAVGDLVARGPDSLATLRFFRSLGDSAKTVLGNHDLHLMALHGKLKRAKPSDNLTEILESPDISASIDWLRQQPLMRELPEHQLIMSHAGVPPQWSLEVLREEAALVSCALNQDDYLEALISQMYSDSAEKWDPSAIGIERLRYCINALTRMRYLYVDGRLDFDCKQPPENCTNPQLKPWFEFASPLRQCHTLVFGHWAALMGNVGDTKLKALDTGCCWGEHLTLWHLEKDQKITQKKLKKS
|
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
|
A3D186
|
C5DGG6
|
ATP25_LACTC
|
ATPase synthesis protein 25, mitochondrial
|
Lachancea
|
MIERLILFNFQSDKNTKHTRVRNMLLRRAAAALPARKTPLHCYRRLGGSYRALSGSLLLRDEEKRLPHRVQDERDEAKADTDLAADGDSAATKPWYLNIVERPAQNMPLHQQEIVFPANSPKSLETIATFLRDKLGLSDVLIFDLRDSQDEQVTAASKISDFMVMATAKSGRHGHKSFIELNTLLKQEFKTVGQVEGNISANELRRRQKRLARHTNLSKSMGSRTATTRSGSNLESWYMIDCRLDNIFVNILTENKRQDLNLEELYAPPDQKHLYRREAPAEDVAPKEGDDNVLAGLKRLAARNQRRYFTTVPARVQIIDALSRQDFDLVLNVVSASKMDSLDILKAANQTLRSMPYGVKIEGESWITFLDEVWPLAPYSQDFWSTRLELFKLLNCAAPGQVNVDRVFTGYLKFKLASGESLTKSDLVEFLQLVETNLSENSHVDYEDLVAKNKCVLEALKLYKGLDPRLILDSEVMCLLLSTLSITQSGSTSTLRAFYEMVEFASREFSQEPPVPVTATVLRILADKQDYARILRFWEKSIASSPEKDHRPWPLFLDTVASTGDQEFAKKVIRDGHLLWIKRNGVKASPELREAIERLFAVADPAEVAFKDVKEFLTVE
|
Probable mitochondrial mRNA stabilization factor.
|
C5DGG6
|
A0M3J8
|
GUAA_GRAFK
|
Glutamine amidotransferase
|
Gramella
|
MQNNVLILDFGSQYTQLIARRVRELNIYCEIYPYHKIPEDLSGFKAVILSGSPFSVRAEDAPHPDLSQIRGKLPILAVCYGAQYFAHFHGGKVEPSDTREYGRANLTVIKDAEPLFENIKENSQVWMSHSDSIIRLPENGVRLASTSDVLNAAYRIEGEQTFAIQFHPEVYHSTDGKQLLENFLIKIAGTKATWTPGKFVDLTVSELKEKVGDDKVVLGLSGGVDSTVAAVLLHKAIGKNLYCIFVNNGLLRKNEFESVLDQYKDMGLNVKGVDASARFLDALKGLSDPEEKRKAIGNTFIEVFDDEAHEIKDVVYLAQGTIYPDVIESVSVNGPSVTIKSHHNVGGLPDFMKLKIVEPLRMLFKDEVRRVGKELGIDKELLGRHPFPGPGLAIRILGDITEEKVRILQEVDHIFIQGLRDWMLYDKVWQAGAILLPIQSVGVMGDERTYEQVVALRAVESTDGMTADWVNLPYEFLQKTSNTIINRVKGVNRVVYDISSKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
A0M3J8
|
Q04G50
|
POTA_OENOB
|
Spermidine/putrescine import ATP-binding protein PotA
|
Oenococcus
|
MTEETVQPLIEFKNVSLDYGETKVLKKVDLEIEEGKFYTLLGPSGSGKSTILSLISGRLQPTGGDILIEGKNVNSLPSNQRKVNTVFQNYALFPNMNVYDNVAFGPSIKGFSKKKIDQLVKSMLKLVKLDDFSDREISEISGGQQQRVAIARALANQPKVLLLDEPLSALDYKLRKEMQSELRELQQRLGITFIFVTHDQEEALAMSDWIFVINDGKVEQSGSPVDIYDEPINHFVANFIGEANIVPGVMKEDYLVSFAGKDFKNVDAGMRTNERVEVVIRPEDLDIVVPSRGKLQVTIEDQSFRGDSYEITAIDDAGNEWAVQATNPAKIGQRRGLKFDPEDIHIMRLNESEEDFDARLESYEGED
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
Q04G50
|
Q9KAG5
|
RGMG_HALH5
|
Putative ribose/galactose/methyl galactoside import ATP-binding protein
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MGEHFLLEMVDITKEFPGVKALDRVQLKVRKGSVHALMGENGAGKSTLMKILIGMYKPNEGKIIFDGEEVTFNSINDALDKGISMIHQELSPIPEMTVAENIFLGREPTFGKSGLVDNKKLIEMTRNLLESLEINIDPRKKMGELSIANTQMIEIAKAISFHSKLVIMDEPTSAITEKEVAQLFKMIESLKKKGVGIIYITHKMSELDEIADDISVFRDGKYIGTDTAKNLTRDDLIKMMVGRELNQIFDKPEPKLGEVILSVKSLTKQDYFEDVSFEVRKGEIVGFAGLMGSGRTEVLETIFGVKEAESGEIFVNGQKARIKSPQDAVKNNMGFLTEDRKLTGLFLPLSVRENMITVNIDKYINMGWLNGKRVKKDCEQQKQKLYIKTPSIEQIVENLSGGNQQKVLLARWLLKNPDILFLDEPTRGIDVGAKSEFYNLIFELASQGKAIVVVSSEMAEILGLCDRILVMHEGKVTGELTREEANQEKIMQYATGQAKMAKKLHVHNNFEQTVTANKIEIG
|
Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
|
Q9KAG5
|
C0QX60
|
GRPE_BRAHW
|
HSP-70 cofactor
|
Brachyspira
|
MEEEIKETSEDKEEENTEAEAVENNEKSEENAGNVEEDEITALKKRIEELENESADMKNKYMYAMAEAENIRKRTAKEKADSIKRANKGLLLSLLTFMDNFERALKAGEQDSNVQGSEYYKGIELIHKQFIDFMHDNGVSEIESLGEEFDPNVHEALTMIEVPDIDKEKVVEVYAKGYKLNDELLRTAKVVVGKPAAAKE
|
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.
|
C0QX60
|
Q48ED3
|
CYSD_PSE14
|
Sulfate adenylate transferase
|
Pseudomonas
|
MVDKLTHLKQLEAESIHIIREVAAEFDNPVMLYSIGKDSAVMLHLARKAFFPGKLPFPVMHVDTRWKFQEMYRFRDKMVEEMGLDLITHINPDGVAQGINPFTHGSAKHTDIMKTEGLKQALDKHGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELWNVYNGNVNKGESIRVFPLSNWTELDIWQYIYLEGIPIVPLYFAAERDVIEKNGTLIMIDDERILEHLTDEEKSRIVKKKVRFRTLGCYPLTGAVESEATSLTDIIQEMLLTRTSERQGRVIDHDGAGSMEEKKRQGYF
|
With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
|
Q48ED3
|
P42342
|
RR7_SPIMX
|
30S ribosomal protein S7, chloroplastic
|
Spirogyra
|
MSRRSNTVSRPTKPDPIYRNRLVNMLVNRILKNGKKSLGYRILYTALKTIKQKTKKNPLSVLRQAVRRATPNVVVKARRRGGSTYQVPIEVKPSQGRALAIRWLLSAARKRSGRSMGLKLSYELMDAARQTGNAIRKREETHRMAEANRAFAHFR
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
|
P42342
|
A7ZSL0
|
RS10_ECO24
|
30S ribosomal protein S10
|
Escherichia
|
MQNQRIRIRLKAFDHRLIDQATAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHLRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG
|
Involved in the binding of tRNA to the ribosomes.
|
A7ZSL0
|
B7V1F5
|
RBFA_PSEA8
|
Ribosome-binding factor A
|
Pseudomonas
|
MAKDYSRTQRIGDQMQRELAQLIQREIKDPRLGLVTITGVEVSRDVAHAKVFITVMGQDDAGKIALNMEILNDAAGYLRMLLGKSMKLRSVPQLHFHYDESIRRGAELSALIERAVAEDGRRHGDDETED
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
B7V1F5
|
Q5RAX9
|
PRD10_PONAB
|
PR domain-containing protein 10
|
Pongo
|
MDSKDESSHVWPTSAEHEQNAAQVHFVPDTGTVAQIVYTDDQVRPPQQVVYTADGASYTSVDGPEHTLVYIHPVEAAQTLFTDPGQVAYVQQDATAQQTPLGGLEAKEEEDEDEDEDTEEDEEEDGEDADLDDWEPDPPRPFDPHDLWCEECNNAHSSVCPKHGPLHPIPNRPVLTRARASLPLVLYIDRFLGGVFSKRRIPKRTQLGPVEGPLVRGSELKDCYIHLKVSLDKGDRKDRDLHEDLWFELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVNQKIHDISEEERKVLREQEKNWPCYECNRRFISSEQLQQHLNSHDEKLDVFSRTRGRGRGRGKRRFGPGRRPGRPPKFIRLEITSENGEKSDDGTQDLLHFPTKEQFDEAEPATLNGLDQPEQTTIPIPQLPQETQSSLEHEPETHTLHLQPQHEESVVPTQSTLTADDMRRAKRIRNAALQHLFIRKSFRPFKCLQCGKAFREKDKLDQHLRFHGREGNCPLTCDLCNKGFISSASLESHMKLHSDQKTYSCIFCPESFDRLDLLKDHVAIHINDGYFTCPTCKKRFPDFIQVKKHVRSFHSEKIYQCTECDKAFCRPDKLRLHMLRHSDRKDFLCSTCGKQFKRKDKLREHMQRMHNPEREAKKADRISRSKTFKPRITSTDYDSFTFKCRLCMMGFRRRGMLVNHLSKRHPDMKIEEVPELTLPIIKPNRDYFCQYCDKVYKSASKRKAHILKNHPGAELPPSIRKLRPAGPGEPDPMLSTHTQLTGTIATPPVCCPHCSKQYSSKTKMVQHIRKKHPEFAQLSSTIHTPLTTAVISATPAVLTTDSATGETVVTTDLLTQAMTELSQTLTTDYRTPQGDYQRIQYIPVSQSASGLQQPQHIQLQVVQVAPATSPHQSQQSTVDVGQLHDPQPYPQHAIQVQHIQVSGQPLSPSAQQAQQGLSPSHIQGSSSTQGQALQQQQQQQQNSSVQHTYLPSAWNSFRGYSSEIQMMTLPPGQFVITDSGVATPVTTGQVKAVTSGHYVLSESQSDLEEKQTSALSGGVQVQPPAHSDSLDPQTTSQQQTTQYIITTTTNGNGSSEVHITKP
|
May be involved in transcriptional regulation.
|
Q5RAX9
|
B8E1E6
|
RS14Z_DICTD
|
30S ribosomal protein S14 type Z
|
Dictyoglomus
|
MAKKSQIVKWLKPKKYKVREYNRCRICGRPRGYIRKFGLCRLCFRELALKGEIPGVRKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
B8E1E6
|
Q4URH2
|
MDH_XANC8
|
Malate dehydrogenase
|
Xanthomonas
|
MKAPVRVAVTGAAGQIGYALLFRIASGEMLGKDQPVILQLLELSNEKAQAALKGVMMELEDCAFPLLAGMVGTDDAEVAFKDIDVALLVGARPRGPGMERKDLLLENAKIFTAQGAALNKVAKRDVKVLVVGNPANTNAYIAMKSAPDLNPKNFTAMLRLDHNRALSQLSLKLGKPVGGIEKLVVWGNHSPTMYPDYRFATSDGASIGDAINDQEWNAGTFIPTVGKRGAAIIEARGLSSAASAANAAIDHVRDWVLGSNGKWVTMGVPSDGSYGIPEGVIFGFPVTTENGQYTLVKDLPIDDFSQKYIDKTLAELEEERSGVSHLLG
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
Q4URH2
|
Q0CPB0
|
KYNU1_ASPTN
|
L-kynurenine hydrolase 1
|
Aspergillus subgen. Circumdati
|
MGSRLHLRDIKHGPPLPYHDDIRAFTKEYAESLDAQDPLRKFRDEFIIPSKKDLKRTVLAADENTDDSTDPRCIYLCGNSLGLQPRSTRKYIDRYLRTWAIKGVTGHFTPHDDQLLPPFVDVDVAGAKLMAPVVGALESEVAVMDTLTTNLHLLMASFYRPTQERYKIIIEGKAFPSDHYAVESQIRHHNREPSEAMVLIEPEDPKHPILTTDQILRVIDENASSAALILLSAIQFYTGQYFDIKTITAHAQSKGIIVGWDCAHAAGNVDLQLHDWNVDFAAWCNYKYLNSGPGGMAGLFVHERHGHVESKNGAQNEGFRPRLSGWWGGDKETRFLMDNNFRPQVGAAGFQLSNPSVLDMNAVVASLEIFSRASMEKIRQKSLHLTGYLEHLLVTYPLDAPPEEKPFTIITPSNPAERGAQLSLRLGPGLLEKVLEVLEEQGVIIDERKPDVIRVAPAPLYNTYAELSSSGIHIAYSSYNQYS
|
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.
|
Q0CPB0
|
Q96H86
|
ZN764_HUMAN
|
Zinc finger protein 764
|
Homo
|
MAPPLAPLPPRDPNGAGPEWREPGAVSFADVAVYFCREEWGCLRPAQRALYRDVMRETYGHLSALGIGGNKPALISWVEEEAELWGPAAQDPEVAKCQTQTDPADSRNKKKERQREGTGALEKPDPVAAGSPGLKSPQAPSAGPPYGWEQLSKAPHRGRPSLCAHPPVPRADQRHGCYVCGKSFAWRSTLVEHVYSHTGEKPFHCTDCGKGFGHASSLSKHRAIHRGERPHRCLECGRAFTQRSALTSHLRVHTGEKPYGCADCGRRFSQSSALYQHRRVHSGETPFPCPDCGRAFAYPSDLRRHVRTHTGEKPYPCPDCGRCFRQSSEMAAHRRTHSGEKPYPCPQCGRRFGQKSAVAKHQWVHRPGAGGHRGRVAGRLSVTLTPGHGDLDPPVGFQLYPEIFQECG
|
May be involved in transcriptional regulation.
|
Q96H86
|
Q57HA8
|
KATG_SALCH
|
Peroxidase/catalase
|
Salmonella
|
MSTTDDTHNTLSTGKCPFHQGGHDRSAGAGTASRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYVGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTHRHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAAAASHVGADPEAAPIEAQGLGWASSYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAVDAPDIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPQPLYQPTQEDIINLKAAIAASGLSISEMVSVAWASASTFRGGDKRGGANGARLALAPQRDWEVNAVAARVLPVLEALQKTTNKASLADIIVLAGVVGIEQAAAAAGVSISVPFAPGRVDARQDQTDIEMFSLLEPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTVLVGGMRVLGTNFDGSQNGVFTDRPGVLSTDFFANLLDMRYEWKPTDESNELFEGRDRLTGEVKYTATRADLVFGSNSVLRALAEVYACSDAHEKFVKDFVAAWVKVMNLDRFDLQ
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
Q57HA8
|
A1JNR2
|
THII_YERE8
|
tRNA 4-thiouridine synthase
|
Yersinia
|
MKFIIKLFPEITIKSQSVRLRFIKILTTNIRNVLKNLEDDTLAVVRHWDHIEIRTKDDNLGPQICDALTRVPGIHHILEVEDRSYTDMHNIFEQTLEAYRETLIGKTFCVRVKRRGKHEFSSGDVERYVGGGLNQHIESAKVKLTHPQVTVHLEIDQDKLTLIKARHEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGSAHEIGVKQVAHYLWNRFGSSHRVRFVAIDFEPVVGEILEKVEDGQMGVVLKRMMVRAASQVAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLAREIGTEDFAKTMPEYCGVISKSPTVKAVKAKIEEEESHFDFSILDRVVNEAKNVDIREIAAQSREQVVEVETVAELADTDVLLDIRAPDEQDEKPLKLDGIEVRTLPFYKLSTQFADLDQSKSYLLYCDRGVMSRLQALYLREQGYTNVKVYRP
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
A1JNR2
|
P31656
|
CADH_MEDSA
|
Probable cinnamyl alcohol dehydrogenase
|
Medicago
|
MGSIEAAERTTVGLAAKDPSGILTPYTYTLRNTGPDDVYIKIHYCGVCHSDLHQIKNDLGMSNYPMVPGHEVVGEVLEVGSNVTRFKVGEIVGVGLLVGCCKSCRACDSEIEQYCNKKIWSYNDVYTDGKITQGGFAESTVVEQKFVVKIPEGLAPEQVAPLLCAGVTVYSPLSHFGLKTPGLRGGILGLGGVGHMGVKVAKALGHHVTVISSSDKKKKEALEDLGADNYLVSSDTVGMQEAADSLDYIIDTVPVGHPLEPYLSLLKIDGKLILMGVINTPLQFVTPMVMLGRKSITGSFVGSVKETEEMLEFWKEKGLTSMIEIVTMDYINKAFERLEKNDVRYRFVVDVKGSKFEE
|
This protein catalyzes the final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers. It acts on coniferyl-, sinapyl-, 4-coumaryl- and cinnamyl-alcohol.
|
P31656
|
A2CC34
|
RL16_PROM3
|
50S ribosomal protein L16
|
Prochlorococcus
|
MLSPKRVKFRKQQRGRMRGVATRGNTIAFGEFALQAQECGWITSRQIEASRRAMTRYVKRGGKIWIRIFPDKPVTMRPAETRMGSGKGNPEFWVAVIKPGRILFEMGGEEITEEIAREAMRLAQYKLPIKTKFIGLDDQEKVAGSDKPASVPAITAES
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A2CC34
|
P12112
|
ATPA_WHEAT
|
F-ATPase subunit alpha
|
Triticum
|
MATLRVDEIHKILRERIEQYNRKVGIENIGRVVQVGDGIARIIGLGEIMSGELVEFAEGTRGIALNLESKNVGIVLMGDGLMIQEGSFVKATGRIAQIPVSEAYLGRVVNALAKPIDGKGEIIASESRLIESPAPSIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQGVICVYVAIGQRASSVAQVVTTFHEEGAMEYTIVVAEMADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELQAFAQFASALDKTSQNQLARGRRLRELLKQSQANPLPVEEQIATIYTGTRGYLDSLEIEQVNKFLDELRKHLKDTKPQFQEIISSSKTFTEQAEILLKEAIQEQLERFSLQ
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
P12112
|
Q8NH74
|
O10A6_HUMAN
|
Olfactory receptor OR11-96
|
Homo
|
MERQNQSCVVEFILLGFSNYPELQGQLFVAFLVIYLVTLIGNAIIIVIVSLDQSLHVPMYLFLLNLSVVDLSFSAVIMPEMLVVLSTEKTTISFGGCFAQMYFILLFGGAECFLLGAMAYDRFAAICHPLNYQMIMNKGVFMKLIIFSWALGFMLGTVQTSWVSSFPFCGLNEINHISCETPAVLELACADTFLFEIYAFTGTFLIILVPFLLILLSYIRVLFAILKMPSTTGRQKAFSTCAAHLTSVTLFYGTASMTYLQPKSGYSPETKKVMSLSYSLLTPLLNLLIYSLRNSEMKRALMKLWRRRVVLHTI
|
Odorant receptor.
|
Q8NH74
|
A3NQX6
|
LIPA_BURP0
|
Sulfur insertion protein LipA
|
pseudomallei group
|
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
A3NQX6
|
P53621
|
COPA_HUMAN
|
Proxenin
|
Homo
|
MLTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPTEDLVVSASLDQTVRVWDISGLRKKNLSPGAVESDVRGITGVDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKAWEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMIVFKLERERPAYAVHGNMLHYVKDRFLRQLDFNSSKDVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRASNLENSTYDLYTIPKDADSQNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKVQVPNCDEIFYAGTGNLLLRDADSITLFDVQQKRTLASVKISKVKYVIWSADMSHVALLAKHAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHIKYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLTAATHGLDEEAESLKETFDPEKETIPDIDPNAKLLQPPAPIMPLDTNWPLLTVSKGFFEGTIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEDGFVEATEGLGDDALGKGQEEGGGWDVEEDLELPPELDISPGAAGGAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQALPCLPSMYGYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQQLITICREYIVGLSVETERKKLPKETLEQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLELGPKPEVAQQTRKILSACEKNPTDAYQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGKDVIGLRISPLQFR
|
Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.
|
P53621
|
B8JEH9
|
TTCA_ANAD2
|
tRNA 2-thiocytidine biosynthesis protein TtcA
|
Anaeromyxobacter
|
MQQIHRLERKLLRATAEAIRDFDLVSQGDRIMVAVSGGKDSYTLLHLLMRLRERAPIDFDLVAVNLDQGQPGFPAQVVEDHLRSVGVPYRMLQRDTYSVVRRLVPEGKTTCPVCSRLRRGVLYNAAVEMGCTKIALGHHRDDLVETLLLSALYSGALKSMPPKLRSRDGRNVVVRPLCYAAEEDVAAFAEAMRFPIVPCDLCGSQPNLRRKRVKRLLAELSAEHPAVKGNLLHALAHVVPSHLLDRDLHRQLADATGRDPWLDAEDEEAEDCGEPPAGDGVVSLGGARGGR
|
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
|
B8JEH9
|
B5RL25
|
DDL_BORDL
|
D-alanylalanine synthetase
|
Borrelia
|
MKKNLMLIFGGVSFEHEISLRSAYGIYSSLLKLDKYNVFSVFVDKVTGIWYLLDSVPSSAELIKRHTTSIVNFIPGCGIFVNNKSLEIDVIFPIIHGRTGEDGAIQGFVKMMDIPCVGAGILGSAISINKYFCKVLLKSFNIPVVSFIGFKKDDYILNKEGIKEDINNKLNYPVIVKPSVLGSSIGINVAYNVSQIEKYIEEAFEYDLTVVVEKFIKAREIECAVIGNDQIKIFTPGEIVVQDFIFYDYDAKYSTVPGDSIVFNIPAHLDMKHLLDIKEYAFLTYKYLELRGMARIDFLISKDTNLLYVNEVNTIPGFTDISMFAKMCEHDGLSYESLVDKLITLAFESYKKRKDKIDFTRLES
|
Cell wall formation.
|
B5RL25
|
Q5QWR3
|
KAD_IDILO
|
Adenylate monophosphate kinase
|
Idiomarina
|
MRIILLGAPGAGKGTQAQFLMNTFGIPQISTGDMLRSAIKSGSELGKKAKQVMDAGQLVSDDIIIELVKERIAEPDCQNGFLLDGFPRTIPQADAMRDNGIEIDYVLEFDVPDEIIVDRMSGRRVHPGSGRVYHVEHNPPKVEGKDDETGEDLVVRPDDQEQTVRKRLSVYHEQTEPLVEYYQKLSEEGKTEYHKIDGTQPVERVSEQLGDLLRK
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
Q5QWR3
|
Q32PD0
|
FCF1_BOVIN
|
rRNA-processing protein FCF1 homolog
|
Bos
|
MGKQKKTRKYATMKRMLSLRDQRLKEKDRLKPKKKEKKDPSALKEREVPQHPSCLFFQYNTQLGPPYHILVDTNFINFSIKAKLDLVQSMMDCLYAKCIPCITDCVMAEIEKLGQKYRVALRIAKDPRFERLPCTHKGTYADDCLVQRVTQHKCYIVATVDRDLKRRIRKIPGVPIMYISNHRYNIERMPDDYGAPRF
|
Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly.
|
Q32PD0
|
Q886Q4
|
DAPE_PSESM
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Pseudomonas
|
MTAPADLSPTLQLACDLIRRPSVTPVDADCQTVMMQRLGDAGFKLEPMRIEDVDNFWATHGTREGPVLCFAGHTDVVPTGPVQDWQNDPFDALIDEHGMLCGRGAADMKGSLAAMLVAAERFVADHPDHKGSVAFLITSDEEGPAHHGTKAVVERLAARNERLDWCIVGEPSSTTLVGDVVKNGRRGSLGAKLTVRGKQGHVAYPHLAKNPIHLATPALAELAAEHWDNGNDFFPPTSFQISNLNSGTGATNVIPGDLVAVFNFRFSTESTVEGLQQRVAAILDKHELDWHVDWALSGLPFLTEPGALLDAVSSSIKSVTGRDTKASTSGGTSDGRFIATLGTQVVELGPVNATIHQVNERILASDLDVLTEIYYQTLVKLLA
|
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.
|
Q886Q4
|
A4WLW1
|
G1PDH_PYRAR
|
sn-glycerol-1-phosphate dehydrogenase
|
Pyrobaculum
|
MKQLESFEIPRTVIFGPGAISKTPQVVAKHKAERILIISGKSVTANYANEVAHLLSGYSVDVVRYDEVDTSYSKYDLVLGVGGGRPIDVAKVYSYLHRAPLIVIPTSASHDGIASPYVSYALSQKMASHGKIVASPIAIIADTTVILNAPSRLLKAGIGDLLGKIVAVRDWQLAHRLKGEEYSEYAAHLALTSYRIVVSNAFRIKNFTKEEDVRVLVKALIGCGVAMGIAGSSRPCSGSEHLFAHAVELLLGEKNNEAIHGELVALGTVVMAYLHGMNWRRIKRVAKEVGLPTTLKQIGIDADVAIEALTTAHTLRPDRYTILGSGLGKEAARRALETTELI
|
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
|
A4WLW1
|
Q6D3J9
|
RL25_PECAS
|
50S ribosomal protein L25
|
Pectobacterium
|
MITIKAEARQGQGKGASRRLRSAGKFPAIVYGGSEAPVSIELDHDSVKNQEVKEGFYGETLILSIDGKEVQVKVQAVQRHVYKPKLTHIDFVRV
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
Q6D3J9
|
B4EY51
|
NCPP_PROMH
|
Nucleoside-triphosphate phosphatase
|
Proteus
|
MYHVIAATTNPAKINAIKLAFEQVFGKDTFDIEDINVDSRVPQQPIGNTETRTGARQRVMAARQVRPEADFWVGVEAGIEDDMTFAWIVIEHEQIRGESRSASLMLPEQILKGVREGRELGDEMAFLTKIDNIKQKGGAIGYFTDGLLSRTSVYQQAIVLALVPVTHDIYKQLNKKDDE
|
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
B4EY51
|
B2FPB2
|
SECA_STRMK
|
Protein translocase subunit SecA
|
Stenotrophomonas maltophilia group
|
MINSLLTRVFGSRNERQLRQLNRIVAKINALEPEIEKLSDEQLQAKTPEFKQRIADGEALDKVLPEAFAVCREAGRRVLGMRHYDVQLIGGMVLHLGKIAEMRTGEGKTLVATLPVYLNALEGKGVHVVTVNDYLARRDAAQMGKLYNWLGLSVGVVYPGMPHSDKREAYAADITYGTNNEFGFDYLRDNMALSKADRYQRGLHYAIVDEVDSILIDEARTPLIISGPADDSPELYIRVNRVVPHLVKQEAEDGEGDFWVDEKGKQVHLSEAGMEHAEQLLVEAGILNGETEGLYAAQNLTVVHHLNAALRAHAIYQRDVDYIVRDGEVVIVDEFTGRTLAGRRWSDGLHQAVEAKEGVPVQRENQTLASITFQNLFRMYKKLSGMTGTADTEAFEFQSIYGLEVVVIPTNRPTIRKDSPDQVFLNRKGKFNAVLADIEECAKRGQPVLVGTTSIETSEMLSEHLSKAGVKHEVLNAKQHDREATIVANAGRPGAVTIATNMAGRGTDIVLGGSLEAELHALGEDATDEQKAAVKADWQKRHEAVKAAGGLHIVGTERHESRRIDNQLRGRSGRQGDPGSSRFYLALEDNLLRVFGGERVQKMMRMMGMKEEDVIEDRLVTRMIEKSQRKVEAHNFDIRKNLLDFDDVNNDQRKVIYAQRDELLDAESVKDNVDGIRDDVIFDVVARFVPPNSIDEQWDLRGLEATLESDFGLQMSLTDLVKEHEELDAEAIAAKVQERVNQHFAEKEASVGEETMRALEKHVMLTVLDQSWKEHLARMDYLRQGIYLRGYAQKQPKQEYKKEAFELFSDMLENVKREVVTLLSRVRIRSDEEVQALEAAERQQAEARLSQSQFQHQDVGGYSADEEAAQVQAAQQGVAQMQRDEPKIGRNDPCPCGSGKKYKHCHGQLS
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
B2FPB2
|
Q6DAV4
|
FPG_PECAS
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Pectobacterium
|
MPELPEVETSRRGISPYLVGHTILYAEVRNARLRWPVSAEILSLSDEPVLSVRRRAKYLLIELTHGWIIVHLGMSGSLRILPEYSEPEKHDHVDLVMDSGKVLRYTDPRRFGAWLWTDSLETSSVLAHLGPEPLEAEFFADYLYQASRGKKTAIKQWIMDNKVVVGVGNIYASESLFAAGIHPDRAAGSLNENDADVLVRVIKQVLQLSIEQGGTTLRDFLQSDGKPGYFAQELRVYGRNGEPCRTCGTPIETAKHGQRSTFFCRRCQV
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
|
Q6DAV4
|
Q98F84
|
TOLB_RHILO
|
Tol-Pal system protein TolB
|
Mesorhizobium
|
MRSFLKPLLTIAAMALGMTAVIPMPAWALVELNVNKGNVEPLPIAITDFQGGDALGAQISQIVTADLKRSGLFAPIDKSAFIEKISNPDAAPRFDDWKVINAQALVTGSVSKEADGRIRAQYRLWDTFAGQQMSGEQFFANDANQRRVAHIIADAIYERLTGEKGYFDTRVVFIDESGAKNARKKRLAIMDQDGANVRYLSDGRSIVLTPRFSPNRQEITYMSYESGQPRVYLLQIETGQRELVGNFPGMTFAPRFSPDGQKVIMSLLRDDGNSNIFAMDLRSRSTTRLTNSTAIDTSPSYSPDGSKVVFTSDRGGRAQIYVMGADGSGQTRISFGDGVYSTPVWSPRGDLIAFTKQTGGEFQIGVMKTDGSGERILSSGFQQEGPTWAPNGRVLMFFRDSNGGPKLVSVDLTGRNEQPIPTANFASDPAWSPLLE
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
Q98F84
|
B8G1Y1
|
RL6_DESHD
|
50S ribosomal protein L6
|
Desulfitobacterium
|
MSRIGKRPISIPGGVDVNIEGNVVTVKGPKGTLTKEMHSLINIAVEEQQIVVTRPDDQPLSRSLHGLTRTLVANMVEGVTKGFSKSLDMVGVGYRAAKQGNKLVLSVGKSHPVELIPFEGIEVEVPAQNKIIVKGMDKELVGDFAAEIRKERPPEPYKGKGIKYENEVVRRKAGKTGAKKGGKK
|
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.
|
B8G1Y1
|
Q5F4Z1
|
ATPG_NEIG1
|
F-ATPase gamma subunit
|
Neisseria
|
MAVGKEILTKIRSVQNTQKITKAMQMVSTSKMRKTQERMSLARPYAEKVRMVMSHLAQTNTDHGIPLLESHREIRRVGFILITSDKGLCGGLNANVLKKFLAQVQEYRNQGIEEEIVCLGSKGLMACQSIGLNVVASAVNLGDTPKMEMLLGPLTELFQRYEKHEIDRIHLVYSGFVNTMRQEPRMEVLLPIGENVIGDSAPKSPFSWEYRYEPTALAVLEYLVRRYLESVVYQALSDNMASEQAARMVAMKAATDNAGNAIKELRLVYNKSRQAAITTELSEIVAGAAAV
|
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.
|
Q5F4Z1
|
Q3J7B4
|
RL13_NITOC
|
50S ribosomal protein L13
|
Nitrosococcus
|
MKTFSAKPKEVRRDWYLVDANGVTLGRLASEIARRLRGKHKAIYTPHIDTGDYIVVVNAEKIRATGKKMAQKHYYRHSGYPGGIKSLTLEKLLERAPERAIELAVKGMLPKNPLGRAMFRKLNVYGGSNHPHIAQQPQPLKI
|
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.
|
Q3J7B4
|
Q31L16
|
RS17_SYNE7
|
30S ribosomal protein S17
|
Synechococcus
|
MAVKERVGVVVSDKMDKTVVVAIEDRTAHPKYGKIVVRTKRYKAHDEDNRAKTGDRVRIQETRPLSRTKRWTVAEILESVGA
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q31L16
|
A5FUK7
|
MRAY_ACICJ
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Acidiphilium
|
MLYALLLPHVAAFHAFNLIRYITFRAGGACLTALVVSFLLGPRLIRWLKSLQKQGQPIRADGPERHLIEKKGTPTMGGFLILIALTVSTLLWADLRNGYVWAVLMITIGYGALGFADDFLKLTKRNTKGVPGRIKLVVQAVLGLGAAVWITQLMPGSIADSLAVPVFKHLMIPFGPLFPLVAMFVMMGASNAVNLTDGLDGLAIVPTIIAAGVFTLIAYLVGNRIFSHYLEINFVPGTGELAVFCSALIGAGMGFLWFNAPPAAVFMGDTGSLALGGALGSVAVATKNEIVLAITGGLFVVETVSVIVQVFWYKRTGRRVFLMAPLHHHFEKKGWAEPTVVIRFWIVAMILALLGLATLKIR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
A5FUK7
|
A1TC25
|
NDK_MYCVP
|
Nucleoside-2-P kinase
|
Mycolicibacterium
|
MTERTLVLIKPDGVQRRLIGEIISRIEAKGLTVAALELKNVDDALARAHYAEHEGKPFFASLLEFITSGPVVAAILEGPRAIAAFRQLAGGTDPVEKATPGTIRGDLGLETQFNLVHGSDSPDSAAREIELWFPGR
|
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.
|
A1TC25
|
A4WGA0
|
RHAM_ENT38
|
Type-3 mutarotase
|
Enterobacter
|
MIRKAFVMQVNPDSHDEYERRHTPIWPELESVLKDHGAHHYAIYLDKARNLLFATVEIESEERWNAVAHTDVCQRWWKHMRDVMPSNPDNSPVSAELKEVFYLD
|
Involved in the anomeric conversion of L-rhamnose.
|
A4WGA0
|
P0AAH9
|
SAPF_ECOL6
|
Peptide transport system ATP-binding protein SapF
|
Escherichia
|
MIETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFGEALTADAWRKDR
|
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
|
P0AAH9
|
Q94F30
|
ESD4_ARATH
|
Protein EARLY IN SHORT DAYS 4
|
Arabidopsis
|
MGAVAINRKRSDESFNFINQQSTNPLRNSPYFQASKKRRFSFAMSEDSGKPASSNPTISRISRYPDAKAPLRREIHAPSRGILRYGKAKSNDYCEKDANFFVRKYDDAKRSALEALRFVNKGKDFVDLGDEVEKEEVVSDDSSVQAIEVIDCDDDEEKKNLQPSFSSGVTDVKKGENFRVEDTSMMLDSLSLDRDVDNDASSLEAYRKLMQSAEKRNSKLEALGFEIVLNEKKLSLLRQSRPKTVEKRVEVPREPFIPLTEDEEAEVYRAFSGRNRRKVLATHENSNIDITGEVLQCLTPSAWLNDEVINVYLELLKERETREPKKYLKCHYFNTFFYKKLVSDSGYNFKAVRRWTTQRKLGYALIDCDMIFVPIHRGVHWTLAVINNRESKLLYLDSLNGVDPMILNALAKYMGDEANEKSGKKIDANSWDMEFVEDLPQQKNGYDCGMFMLKYIDFFSRGLGLCFSQEHMPYFRLRTAKEILRLRAD
|
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Acts predominantly as an isopeptidase, cleaving SUMO-conjugated proteins better than SUMO peptides. Plays an important role in the control of flowering time.
|
Q94F30
|
O26542
|
UVRB_METTH
|
Excinuclease ABC subunit B
|
Methanothermobacter
|
MMKFKLVSDYRPLGDQPKAIRSLVNGIKAGMREQTLLGVTGSGKTFTVANVIAEVQKPTLVISHNKTLAAQLYEEFREFFPENAVEYFVSYYDFYQPEAYIPQTDTYIDKEASINDEIDRMRHSATQSLLSRDDVIVVSSVSCIYGIGAPTDYGEFTLHLEVGSGPGREEVLEGLINMQYERNDVEFDRGQFRVRGDTVEINPIHGTPPIRIEFFGDEIDSISTVHRVTGRRIQKLDRVTIFPAKHFVIPEDRLQRAIESIEAELEERLTELRSQNKLLEAQRLEQRTRFDMEMLREMGYCQGIENYSMHLSGRKWGEKPNTLLDYFPEDFLTVIDESHVTVPQIRGMYNGDRARKDTLVEYGFRLPSARENRPLRFDEFQESVNQVIYVSATPGRYELSRSQNIVEQIIRPTGLVDPEVRIRPVKGQVDDLLSEIRRRVERGERVLVTTLTKRMAEDLTDYYSRVGVKVRYLHSEIDTLERVEIIDDLRRGEFDCLVGVNLLREGLDLPEVALVAILDADKEGFLRSETSLIQTIGRAARNVNGEVLIYAGRFTDSVMAAVETTNRRRKLQMEYNRRHGIKPRSTRRTLREEEGPLRNLKVDEIPDHELELIIKDLEAEMRDAARNLEFERAARIRDRIMSLKSN
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
O26542
|
A8H5M1
|
MNMA_SHEPA
|
tRNA-specific 2-thiouridylase MnmA
|
Shewanella
|
MTSIEPTHLGKKVIVGMSGGVDSSVSAYLLMKQGYQVEGLFMKNWEEDDTDEYCAAADDLKDAQAVCDKLGIKLHTVNFASEYWDNVFEYFLAEYKAGRTPNPDIMCNKEIKFKAFLEFADEILDADYIAMGHYVRRRDIDGTSQMLRGVDGNKDQSYFLYTLGYEQVARSLFPVGELDKSEVREIAKEMGLITHDKKDSTGICFIGERKFTDFLQTFLPAQPGNIETSEGEVIGTHQGLMYHTLGQRKGLGIGGLKNSNDDPWYVVEKDLVRNVLIVGQGGNHPRLMSNGLVANQLHWVDRKGPANGSKITVKTRYRQQDVPCSVTYDSDDVLRVIFDEPVAAVTPGQSAVFYDGEICLGGGIIDALIRD
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
A8H5M1
|
Q19V65
|
ATPB_CHLAT
|
F-ATPase subunit beta
|
Chlorokybus
|
MTTTNAVKTKNIGYITQIIGPVMDVKFSPGKMPNIYNALIVNGKNEAGDEISVTCEVQQLLGDNKVRAISMSGTDGLMRGMEVLDTGAPLSVPVGEATLGRIFNVLGEPVDNLGPVANKSTLPIHRDPPAFTELDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYQEMKESKVINEENLSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNNQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSREMGTLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYDTAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLADTIKGFLMILSGELDSLPEQAFYLVGDIGEAIAKAEKLKDK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q19V65
|
Q52953
|
MURD_RHIME
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Sinorhizobium
|
MIPVTSFKGRKVALFGLGGSGLATAQALVSGGADVVAWDDNPDSVAKAAAAGIATADLRGADWHAFAAFVLSPGVPLTHPKPHWSVDLAHQAGVEIIGDVELFVRERRKHAPDCPFIAITGTNGKSTTTALIAHILRTSGRDTQLGGNIGTAVLTLDPPKAGRFYVVECSSYQIDLAPTLDPTAGILLNLTPDHLDRHGTMQHYADIKERLVAGSGTAVVGVDDSLSSLIADRVERAGTKVVRISRRHPLAEGIYAEGSALMRAQDGASSLFTDLAGIQTLRGGHNAQNAAAAIAACLAVGISGKDIVDGLRSFPGLKHRMQPVAKKGEVVFVNDSKATNAEAAAPALSSYDRIYWIAGGLPKEGGITSLAPFFPKIVKAYLIGEAAPSFAATLGEAVPYEISGTLEKAVAHAAADAARDSQGPAAVMLSPACASFDQYKNFEVRGDAFVGHVAALEGVSMLI
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q52953
|
Q02U08
|
YQGF_PSEAB
|
Putative pre-16S rRNA nuclease
|
Pseudomonas
|
MASDKPLRLLLGFDYGTRQIGVAVGQAVTGQARELCVLKAQNGVPDWNRVEALIKEWQPDAIVVGLPLNMDGSPSEMSERAEKFGRRLNGRFNLPVFTHDERLTTYAAKGERLAQGQRDGYRERPVDALAAALLLEGWLAEHPD
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q02U08
|
P39962
|
KC13_YEAST
|
Casein kinase I homolog 3
|
Saccharomyces
|
MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRILNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQYQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLGHVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALRLNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKSRISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTNLANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC
|
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
|
P39962
|
A7MLT4
|
ASR_CROS8
|
Acid shock protein
|
Cronobacter
|
MKKVLALVVAATMGLSAAAFAADNTAAPAPAAAATTTTTAAPAKAPAAKTHHKKSHKKAVEQKAQAAKKHHKKAAEQKPAAEQKAQAAKKHHKKAAAQKPAVEQKAQAAKKHHKKAVKHDAAKPAAQPAA
|
Required for growth and/or survival at acidic conditions.
|
A7MLT4
|
Q9QYM2
|
PARG_RAT
|
Poly(ADP-ribose) glycohydrolase
|
Rattus
|
MSAGPGCEPCTKRPRWGAAGTSAPTASDSRSFPGRQKRVLDPKDAPVQFRVPPSSSACVSGRAGPHRGSVTSFVFKQKPITTWMDTKGPKTAESESKENNNTRTDPMMSSVQKDNFYPHKVEKLGNVPQLNLDKSPTEKSTPYLNQQQTAGVCKWHSAGERAEQLSASEPSAVTQAPKQLSNANIDQSPPTDGHSDTDHEEDRDNQQFLTPVKLANAKQTVGDGQARSNCKCSASCQCGQDCAGCQREEADVIPESPLSDVGAEDIGTGSKNDNKLTGQESGLGDSPPFEKESEPESPMDVDNSKTSCQDSEADEEASPVFDEQDDQDDRSSQTANKLSSRQAREVDGDLRKRYLTKGSEIRLHFQFEGGSNAGTSDLNAKPSGNSSSLNVDGRSSKQHGKRDSKITDHFVRIPKSEDKRKEQCEVRHQRAERKIPKYVPPNLPPDKKWLGTPIEEMRKMPRCGVRLPLLRPSASHTVTVRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALVDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCDKPLTRLHVTYEGTIEGNGRGMLQVDFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQRCCTEIVAIDALHFRRYLDQFVPEKVRRELNKAYCGFLRPGVPPENLSAVATGNWGCGAFGGDARLKALIQLLAAAAAERDVVYFTFGDSELMRDIYSMHTFLTERKLNVGKVYRLLLRYYREECRDCSSPGPDTKLYPFIYHAAESSAETSDQPGQRTGT
|
Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
|
Q9QYM2
|
Q8I5V4
|
PDEA_PLAF7
|
cGMP-specific 3',5'-cyclic phosphodiesterase alpha
|
Plasmodium (Laverania)
|
MMDTKVDQTIQPKFYVDKKLSKSFDNKLDEDIFNYPFKKESFLKSEKFSFEHTKDSLWKCIKEKAKKKSDMEYFNCVNNLCCKFICTIRKYVKYFLYLKDSSYEIYNINLYNNNNMNIINNKNITNNKNITNNINNSFSNDYINYNHNYNHLNNSSSSKHNNYNVNNIDEKNIKNDYNTYHNIYEQIFFKYNPSFYEYLMFTLMKKLIHYKNYIFNKTKKINNSYNNNDIKNIDGFLIFQNINFEEIFLNTFYSSFPFKLFLHSLYMIFICFIYFVVLYFMLLKKIYTHPFIFHLSVLKFLFDIIFFLSFILYPLFLRLKRIDKIIYSSYISSYIFVCVTFLYSFIIFKCSSYSVKMNSNTYQNNFVFQNMLFLLINIIYICIFCFLKNYMILYSFLYNCRFSIFCILFIFLYYYLFFSLDFYRIIHLPLDNFFFPFLCFLFFSFLFIFKIIMSLYYEYVYEKKYRILFVKKNNLIEKRITKRKNTNINNAYFTKYFSIDNTIPTSPIEDILNNFKHILETINIIEENPNHNLTTNIMKIKEKIKNCDNILRTKNINQVQIGKYRKFEKVYNIWCLDKMYLNYPLNQEETKSFLSNSLNRISFNSFSNMHSLLSSKFQEHYNDIYDWNGNIENIYKANTFISIGYKLLYPLGVLEANFDKEKLKKFLFRICSYYNDIPYHTSLHAAQVAHFSKSMLFMLDMNHKISAIDEFCLHISSLCHDTGHPGLNNYFLINSENNLALTYNDNSVLENYHCSLLFKTLKNPNYNIFEHYPYHIFISCKKNIIKAILSTDMKNHFEYISDFRTSKEFIDYDNLSNDQIWQIFCLILKASDIGHSTLEWNKHLEWTLKINEEFYLQGLLEKSLNIQNSFLCDINTMNKLALSQIDFLKHLCIPLFNELNYICKNNDVYTHCIQPIENNIERWESHKNDNQNLGLHEKYKEENLLSKLELIKFE
|
Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes.
|
Q8I5V4
|
B4EVE1
|
MGSA_PROMH
|
Methylglyoxal synthase
|
Proteus
|
MEQIDRTLATEKNIALVAHDHCKSSLLEWVKNNSEQLSHHKLFATGTTGNLVNHHTGLEVTQMLSGPMGGDQQIGAMIAEKKIDILIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNRATANFLISSPLFSQESKIKIPDYEGYLKERLK
|
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
|
B4EVE1
|
P26697
|
GSTA3_CHICK
|
GST-CL3
|
Gallus
|
MAAKPVLYYFNGRGKMESIRWLLAAAGVEFEEVFLETREQYEKLLQSGILMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLYGKDLKERALIDMYVGGTDDLMGFLLSFPFLSAEDKVKQCAFVVEKATSRYFPAYEKVLKDHGQDFLVGNRLSWADIHLLEAILMVEEKKSDALSGFPLLQAFKKRISSIPTIKKFLAPGSKRKPISDDKYVETVRRVLRMYYDVKPH
|
Catalyzes the conjugation of GSH to a wide variety of electrophilic alkylating agents. Also involved in the metabolism of lipid hydroperoxides, prostaglandins and leukotriene A4 and in binding of non-substrate hydrophobic ligands such as bile acids, a number of drugs and thyroid hormones. This GST does not exhibit peroxidase activity.
|
P26697
|
A6LLK6
|
GATB_THEM4
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Thermosipho
|
MRFKPVIGLEIHVQLNTKTKAFCSCPADVFELEPNNAICPVCTGQPGALPVPSKQMYEFGILLAAALNCKIHEFTRFDRKNYFYPDLPKGYQITQYFYPLATNGYLKLNGKKIRINRIHLEEDAGKLLHSSETITQAESTLVDMNRCGVPLAEIVTEPDIESPEEARKFLEKLRQILRYLGVSTGDMEKGALRCDANISVIDLENNVQSNKVEVKNMNSFKFVEKALEYEFNRIKKHLKKGENVVKETRGWDLASKKTISMRSKEEANDYRYFPEPDIPPVVIPKEEINKIIEKIPELPDEKINRFKIQYGLTDYEAGILTTSINLANYFEECVKETKNPKETSNWFLTELLKYISPEEVFENLKIKPKHFKELFDLISSGKITRNIAKEIFKEIFETGKNPEEIVKEKGIEVIGDESLIEDMLKKIMAENEDKVNAYKNGKKGLLGFFVGQIMKQTKGKADAKKANEIAKRLLGD
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A6LLK6
|
C4K3W7
|
METK_HAMD5
|
Methionine adenosyltransferase
|
Candidatus Hamiltonella
|
MPHQLFTSESVSEGHPDKIADQISDAVLDAILIQDPKARVACETYVKTGMVIVGGEITTSAWVDIEEITRCTLAEIGYVHSDMGFDAHSCAVLSAIGKQSPDINQGVDRIDPLDQGAGDQGMMFGYATNETDVLMPAPITYSHRLVKRQSEMRKIGQLPWLRPDAKSQITFKYDKGYAVAIDTIVFSTQHEEDVTQKQLEEAVMEEIIKPVIPTQWLSSSTKYFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQISYAIGVANPTSIMLETFGTEKITIQKIMSLIHQHFDLRPYGLIKMLDLLKPIYRATAAYGHFGRDVFPWEATDKAELLREQAGLNQ
|
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.
|
C4K3W7
|
P06845
|
TYRO_STRGA
|
Monophenol monooxygenase
|
Streptomyces
|
MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVTTHNAFIIGDTDAGERTGHRSPSFLPWHRRYLLEFERALQSVDASVALPYWDWSADRTARASLWAPDFLGGTGRSLDGRVMDGPFAASAGNWPINVRVDGRAYLRRSLGTAVRELPTRAEVESVLGMATYDTAPWNSASDGFRNHLEGWRGVNLHNRVHVWVGGQMATGMSPNDPVFWLHHAYVDKLWAEWQRRHPGSGYLPAAGTPDVVDLNDRMKPWNDTSPADLLDHTAHYTFDTD
|
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
|
P06845
|
O05102
|
C17AA_PARBF
|
Insecticidal toxin CryXVIIA(a)
|
Paraclostridium
|
MNNKKIEQNKIVEYNSNLDIQPRELNTLNGLVFTGATVSIILPLIGTTAVVPVVGGVIGIIAALLPVIWPAGTSSNDNLFDAVMKDTEMIMDEKISEYVVNDAMTRLESLYNILDYYRLSKDFWEKNKDDPLAIAELKERFSKLHSQFIESMAYFKRANYEVLLLPAYANAANLHLLLLREGLLLNKVIDNFITEGLHYEEFKTKRSTYIAHCSTWYNKGLENIKNKTRDFNKINKYDAYMNLSVLDIISLFLSYDPYQYDKATKLQTLTRTVFSDPLQRAPRDLYISPKEETLFKNLKGLRAFFAEGDLVLTGFRNYFRNTYINDQIIEGDLFGYTTNNERYKLFTDSKIYKVTVFIDNVALAIVKLIFHDTDNKEWDFSKTDITDINKYRKEEVYLNLLSNNEIQKEPSHYLYKMHHYGDNYNDSYLFQWIHQSISPENYLFDKDKDDNYIITQIPAIKASELSNLGELSLQAIKGPRFTGGNVILSSVSKIDNNDPLYGGTIKIPLLTAFNNTSKFKIRIYYAANHNYNHDYIGALLTINSQHVANFKFKQTFSGEDYSNLSYNNYQFDYLVQTVAFPQNTSDVTLNLQFFYDPKFLNDYKQIVIIDKIEFIPEN
|
Not significantly toxic to mosquito larvae. May increase the toxicity of the Pesticidal crystal-like protein cry16Aa (Cbm71).
|
O05102
|
Q492P4
|
FABA_BLOPB
|
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
|
Candidatus Blochmannia
|
MLNKREYYTKEDLLASSRGELFGKNGPTLPAPNMLMMDRVIKMTKNGGNYNKGFIEAELDIQSDMWFFNCHFIKDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVKEVKFTGQILPTSKKVTYFIHFRRIINRKLIMGMADGEVSCDGKIIYTATDLKVGLFKNSTVF
|
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
|
Q492P4
|
Q944K3
|
HDA2_ARATH
|
Histone deacetylase 2
|
Arabidopsis
|
MTHTRVISTWTELTRDLAIYLLFTFFAIKVFKFLFSCNRTSEISSFSMATHPEALRRERILNSKLYFDVPLSKVSIIYSSSYDISFMGIEKLHPFDSSKWGRVCKFLVSDGFLEEKAIVEPLEASKIDLLVVHSENYLNSLKSSATVARITEVAPVAFFPNFLVQQKVLYPFRKQVGGTILAAKLATERGWAINIGGGFHHCTAERGGGFCAFADISLCIHFAFLRLRISRVMIIDLDAHQGNGHETDLGDDNRVYILDMYNPEIYPFDYRARRFIDQKVEVMSGTTTDEYLRKLDEALEVASRNFQPELVIYNAGTDILDGDPLGLLKISPDGITSRDEKVFRFAREKNIPLVMLTSGGYMKSSARVIADSIENLSRQGLIQTRPE
|
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
|
Q944K3
|
P24847
|
DAPA2_WHEAT
|
4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic
|
Triticum
|
MMAAQPTANPGVRLGWKAPGALASPPRLALSRSAAAPLASHRVGRGKFSAAAITTDDYLPMRSTEVKNRTSVDGIKSLRLITAVKTPYLPDGRFDLEAYDSLINTQINGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGTNIKVIGNTGSNSTREAIHASEQGFAVGMHAALHVNPYYGKTSTAGLISHFDEVLPMGPTIIYNVPSRTGQDIPPAVIEALSTYPNMAGVKECVGHERVKCYTDKGITIWSGNDDECHDSRWKYGATGVISVTSNLVPGLMRSLMFEGENAALNEKLLPLMKWLFSEPNPIGLNTALAQLGVVRPVFRRPYAPLSLEKRTEFVRIVEAIGRENFVGQKEVRVLDDDDFVLISRY
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
P24847
|
Q9M020
|
LRK63_ARATH
|
Lectin receptor kinase A4.2
|
Arabidopsis
|
MLVLFLLLTIPTRAQRTTTETPKTEFIFRGFSGNQSNIVTTGAATIKLDGLLRLTDRNSNVTGTSFYHKPVRLLETNTSSTNSTIRSFSTSFVFVIIPTSSSNGGFGFTFTLSPTPDRTGAESAQYLGLLNKANDGNSTNHVFAVEFDTVQGFKDGADRTGNHIGLNFNSLTSDVQEPVVYYDNEDPNRKEDFPLQSGDPIRAILDYDGPTQTLNLTVYPANLKSRPVRPLISRPVPKLSQIVQEEMYVGFTAATGRDQSSAHYVMGWSFSSGGDLLTEDTLDLLELPRPPPNTAKKRGYNSQVLALIVALSGVTVILLALLFFFVMYKKRLQQGEVLEDWEINHPHRLRYKDLYAATDGFKENRIVGTGGFGTVFRGNLSSPSSDQIAVKKITPNSMQGVREFIAEIESLGRLRHKNLVNLQGWCKQKNDLLLIYDYIPNGSLDSLLYSRPRQSGVVLSWNARFKIAKGIASGLLYLHEEWEKVVIHRDIKPSNVLIEDDMNPRLGDFGLARLYERGSQSNTTVVVGTIGYMAPELARNGKSSSASDVFAFGVLLLEIVSGRRPTDSGTFFLADWVMELHARGEILHAVDPRLGFGYDGVEARLALVVGLLCCHQRPTSRPSMRTVLRYLNGDDDVPEIDNDWGYSDSSRSDLGSNFEGYVSSDRASSSVPSFSVTRVSSSSVISGR
|
Involved in negative regulation of abscisic acid response in seed germination.
|
Q9M020
|
A1SEK1
|
RPOB_NOCSJ
|
Transcriptase subunit beta
|
Nocardioides
|
MQIEERIVEGHLLAARTTPGNTRRISFAKITEPLEVPQLLSLQTDSFDWLVGNDKWNAAVERRRSEGEDVSSKSGLQEIFEEISPIEDFSETMSLSFENPVFYDPKYTVDECKEKDFTYSAPLYVSAEFTNNDTGEIKGQTVFMGDFPLMTDKGTFIINGTERVVVSQLVRSPGVYFERTADKTSDKDIYTAKLIPSRGAWLEFEIDKRDMVGVRLDRKRKQNVTVLLKALGWTNEQIREEFGEYESMMLTLEKDHTQGQDDALLDIYRKLRPGEPPTREAAQTLLNNYYFNPKRYDLAKVGRYKINKKLGLLEAFDQQTLTIDDVVAAIKYIVALHDGREQIEAPQGTLDISADDIDHFGNRRMRTVGELIQNQLRTGLARMERVVRERMTTQDVEAITPQSLINIRPVVAALKEFFGTSQLSQFMDQTNPIAGLTHKRRLSALGPGGLSRDRAGMEVRDVHPSHYGRMCPIETPEGPNIGLIGSLASYGRINPFGFVETPYRKVTKGKVTDQIDYLTADDEDRYVIAQANAALDDKSRFVEERVLVRQRDGEVSEVLADEVDYMDVSPRQMVSVATALIPFLEHDDANRALMGANMQRQAVPLIKSDSPLVGTGIEYRAAVDAGDVVVATAAGVVKEVSADVIETMNDDGTYSTYRLAKFKRSNQGTCINQRPLVSEGDRLEIGTPIADGPCTDEAEMALGTNLLVAFMPWQGHNYEDAIILSQRLVQEDILTSIHIEEHEVDARDTKLGPEEITRDIPNVSEEMLADLDERGIIRIGAEVTTGDVLVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSMKVPHGESGTVIGVRVFDREDGDELPPGVNQLVRVYVAQKRKISVGDKLAGRHGNKGVIAKILPIEDMPFMEDGTPVDVVLNPLGVPRRMNIGQILELHLGWLAKQGWDLNLNDDKSGADWKQRLIKIHADKAEPGTKVATPVFDGAREDEITGLLGSTIPNRDGVRMIDNTGKASLFDGRSGEPFPEPVAVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWAMEAYGAAYALQELLTIKSDDVPGRVKVYEAIVKGENIPDSGIPESFKVLVKEMQSLCLNVEVLSQDGTAIEMRDAEEDVFRAAEELGIDLSRREPSSVEEV
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A1SEK1
|
C4K3I6
|
DNAK_HAMD5
|
Heat shock protein 70
|
Candidatus Hamiltonella
|
MTKIIGIDLGTTNSCVAIMDGSKPRVLENSEGDRTTPSIIAYTDDGETLVGQPAKRQAVTNAKNTFFAIKRLVGRKFSDQETQRDKDIMPFDILESDNGDAWLSVKGQKTAPPQISAEVLKKMKKTAEDYLGETVTEAVVTVPAYFNDAQRQATKDAGRISGLEIKRIINEPTAAAIAYGLDKGKGNSTIAVYDLGGGTFDISIIEIDDVDGEKTFEVLATNGDTHLGGEDFDNRLINYLVDEFKKEQGFDLRKDPLAMQRLKEAAEKAKVELSSAQQTDVNLPYITADATGPKHMNMKVTRAKLESLVEDLVSRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVADFFGKEPRKDVNPDEAVAIGAAVQGGVLSGEVKDLLLLDVTPLSLGIETMGGVMTSLISKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAIDNKSLGQFNLDGIQPAPRGTSQIEVTFDIDADGILHVSAKDKNTGREQKITIKASSGLSEAEIEKMVRDAESNSETDRKFEELIQVRNQADHLIHATNKKLKEAGDKVSPEEKTSIEQALKALETAIKGEDKTDIESKANALTMVSAKLEEASQQNSSSNNAEKNDSSDVKADAVDAEFEEVKDKK
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Acts as a chaperone.
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C4K3I6
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B0T410
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PYRF_CAUSK
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OMP decarboxylase
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unclassified Caulobacter
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MSADPRLILPLDLSSVSEARAMVETLGDAVSFYKIGLELLATDGMALARQLKGEGKQIFLDWKLHDIGATVERSARVLAGAGCDLLTVHAEPQVMAAAVKAKGGSDLKILAVTVLTSLTDADLIELGYAFSARDLVARRIRQAIEAGVDGVVSSPQEAALAREIAGPDFLVVTPGVRPFWSAKNDQARAATPADALKAGASHLVCGRPITAANDPREAALKVVGEMAGL
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Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
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B0T410
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A8FUX0
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RUVB_SHESH
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Holliday junction ATP-dependent DNA helicase RuvB
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Shewanella
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MIEADRLIHAEPQGPEERDEQIDRAMRPKLLDEYTGQDDTRAQLKIFIKAAQNRGEALDHMLIYGPPGLGKTTLAMIVANEMGVNIKSTSGPVLEKAGDLAALLTNLEPGDVLFIDEIHRLSSVVEEILYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLIGATTRAGALTSPLRARFGIPLRLEFYNTKDLSSIVSRSANVLELPIDDEGAIELAKRSRGTPRIANRLLRRVRDFAEVKHDGEINKAVADLALDMLDIDSEGFDYMDRKLLLAIIDKFMGGPVGLDNLAAAIGEERETIEDVLEPFLIQQGFIQRTPRGRIATDRAYRHFDIIQPEK
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The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
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A8FUX0
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