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2.75k
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5.51k
AlphaFoldDB
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A6TR38
EX7L_ALKMQ
Exodeoxyribonuclease VII large subunit
Alkaliphilus
MQIKALSVSEINHYIKRIMINDPILSNVYIKGEISNYKLHSSGHIYFTLKDEKSRVSSVMFKTNTEQLKFLPEEGMQVLCRGYISLYERGGLYQFYVDHMEAAGVGALYLAYQQLKEKLEKQGYFDGKFKKEIPLIPRKIAVVTSPTGAAVRDIISVIKRRFPHVEIYLFPVLVQGDRAAPSIARAVELLNLFGGIDVAIIGRGGGSIEELWPFNEETVAEAIFSSQVPIISAVGHETDFTIADFVADLRAPTPSVAAERVVPDVKEVVERLNTLKDRLNKTLVKSIDAKRNQLGIIKSNYYFKNPLNMIYDRQQHLDILMKDLTRNINVKNSLYSNNVHRLGERLNSVSPLSVFSRGYALAENKKGERIKTISNVKLKESITVQLIDGQLSCEVTNILKEDKLVGKNQI
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
A6TR38
P0CW58
RADA_METMI
DNA repair and recombination protein RadA
Methanococcus
MADVLTELPGVGPSTADKLIEGGYLDFMKIATATIGELTDIEGISEKAAAKMIMAARDLCDLGFKSGVELLKQRQSVWRLSTGSTELGTVLAGGIESQSVTEFAGMFGSGKTQIMHQTCVNLQMREKIFADLEGVVEEELEAPKAVYIDTEGTFRPERVVQMAEGAGIDGQTVLDNTFVARAYNSDMQMLFAEKIEDLIKGGNNIKLVIIDSLTSTFRNEFTGRGKLAERQQKLGRHMATLNKLADLYNCIVLVTNQVAAKPDAYFGVAEQAIGGHVVGHAATFRFFLRKSKGDKRVAKLYDSPHLPDSEAVFRITEKGIQD
Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
P0CW58
Q5LW06
RNPA_RUEPO
Protein C5
Ruegeria
MPPAVSVCASSGISVLRKRSDFLKAARARRQGAGSMMVQARKRDAGEAEGIRVGFTCSKKVGNAVARNRAKRRLREAARLVLPDMGRPGWDYVLIGRPSDTASRPFDGLLDDLRRALRKLHAPKP
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Q5LW06
O70453
HMOX3_RAT
Putative heme oxygenase 3
Rattus
MSSEVETAEAVDESEKNSMASEKENHSKIADFSDLLKEGTKEADDRAENTQFVKDFLKGNIKKELFKLATTALSYSAPEEEMDSLTKDMEYFFGENWEEKVKCSEAAQTYVDQIHYVGQNEPEHLVAHTYSTYMGGNLSGDQVLKKETQPVPFTREGTQFYLFEHVDNAKQFKLFYCARLNALDLNLKTKERIVEEATKAFEYNMQIFSELDQAGSIPVRETLKNGLSILDGKGGVCKCPFNAAQPDKGTLGGSNCPFQMSMALLRKPNLQLILVASMALVAGLLAWYYM
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase 3 could be implicated in some heme-dependent regulatory role in the cell.
O70453
A1B036
RS17_PARDP
30S ribosomal protein S17
Paracoccus
MPKRILQGKVVSDKNEQTVTVLVERRFKHPLLHKTVRSSKKYRAHDADNQFKVGDTVRIVECAPISKTKRWTVLTETAEVSA
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
A1B036
A6VQU4
MNTP_ACTSZ
Putative manganese efflux pump MntP
Actinobacillus
MSYYTLWVIAFGLSMDAFAVSVGKGLTLADFCWKFTLKIALCFGLFQACMPLLGYYVGSHFSDYISEFDHWIAFALLCVIGINMIKMSVTNENSDDDPSDFSLRHLTMLGVATSIDALAMGVSFAFLKVNIWTAAAIIGITTTILSLFGVKAGHWLGDRIHKQAELLGGIILIAMGVKVLIEHRVFG
Probably functions as a manganese efflux pump.
A6VQU4
Q13EA7
GLGA_RHOPS
Starch [bacterial glycogen] synthase
Rhodopseudomonas
MTTLTALSVASEIFPLIKTGGLADVTGALPAAVKAHGVAMRTLVPGYPAVLGGIEDPQQVHSFTEFFGGSARLLAARCDELELLVLDAPHLYVRPGNPYVGPDAKDWPDNALRFAALAQAGAWIGQGLLPGYAPDILHAHDWQTGLLPAYLRYSGRPAPKCVFTIHNLAYQGQFPSELLARIGLPERAFSLDGVEYYGGIGYLKAGLQLADRITTVSPSYALEIQGSEAGMGLEGLLRLRAGQLSGILNGVDTKVWDPSADQLIPATYDVETIGARARNKQALQARFGLRAESGALLFGVISRLSWQKGLDMLLEVLPGMLADGAQLALLGAGDAPLEAGFRDAALKYPGQVGAVIGYDEALAHQIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVQFSPVTADMLTAALTKTRALYADHATWRNLQINGMTTDVSWKNPAQHYAKLYRELVDA
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Q13EA7
Q7MYG7
RL18_PHOLL
50S ribosomal protein L18
Photorhabdus
MDKKAARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSETLVAASTTEKAINEQLKYTGNKEAAAAVGKAIAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF
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.
Q7MYG7
Q8S8F2
FBL11_ARATH
BTB/POZ domain-containing protein FBL11
Arabidopsis
MALSSLVEFVILVVKNPCYQQDDASSSIQEISISASEIASWDMSEILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVEWNLESFLNLLMCLYGYDIEITSSSFLPLFESALYFGVEKLLSICKNWLSVLASSNDNALPKVELSDLIQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWLDAGGRLSDLPESSQDNTINLMEQVRFSLLPLWFIAGRSKSHGFSKFADQSIELVTKLMKMPSTCLVDSLTDGPPTDVRVRLTEYSEILDLSGCPQLNEASLLLSILPNSYFANLRWRKSLESFLKNPDDDERHQEQISHRTLPILSFESVKEIDISKCQRLDYKVVIKCFSKSFPSLRKLRAAYLLNIKVSTLLELLLNFRELTEVDLTVDVSPIIPVQASVFYSGQGHCLLSSITRLTLEGRSDICDMELRSISRVCESLCYLNIKGCALLSDACIASVIQRCKKLCSLIVCYTSFSENSILALCATISMTNEHMDINSVASNLQTLHMSKCEGISETSLLNLITHSQKMKSLCLRDTKVSDSVLCEFPGSTLEALDISNTTISWMALARVISRNPNLKTLKARGCKNLLQLEVDGRTDNFSPLVSGQEVFKCLSKGSGLEELEIGWGFSYFSFESLRPAASFLRVISVGLGASLGEDVLKLLPSTCPLLESIVLHFQEISDSALTSVLTSLKHLQELALSYCFGEISLQSFKFSMPNLRKLRLERVTRWMTNDDLLVLTQSCPNLTELSLVGCLHLTSDCQPIISAGWPGMISLHLEECGSITENGVASLYGCIALEDLFLRHNGSGIQKSFLLDATLKFPMLRLVSLDMCDAKEGGFDVPEEKEEGRSLSIVKISRCKSDRCSLGRRAAPMHRETLVMLWNGQTLTKTLLKQRL
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Q8S8F2
Q72CI5
RS12_DESVH
30S ribosomal protein S12
Desulfovibrio
MPTINQLIRKERKKVVKRKKTPALQACPQRRGVCTRVYTTTPKKPNSALRKVARVRLTNGLEVTAYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHIVRGTLDTSGVQDRRQGRSKYGAKRPK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q72CI5
Q3V8A3
PDXA_METCA
4-(phosphohydroxy)-L-threonine dehydrogenase
Methylococcus
MPPRLLLTSGEPAGIGPDLCVLLSRRPFPCGITVLGDPDLLESRARLLGVPIELRRVVSGDVVPPHEPGVLHVLPTRRQPGTAPGKLDPANAAYVLETIADGARACLAGHYDALVTAPVQKSVINEAGIAFTGHTEFIAGITGGSPVMMLAAEGFRVALATTHLPLAEVSRAITVERLTGVLGVLHEDLVRRFGFSRPRILVCGLNPHAGEGGHLGGEEITVIEPVLARLRQDGMDLTGPLPADTLFLPHNLDRADAVLAMYHDQGLPVLKYAGFSRAVNITLGLPIIRTSVDHGTALDRAGTGQIDTGSLEEAVRVAMEMATGRPAESP
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Q3V8A3
D4D4Z2
MEP1_TRIVH
Fungalysin MEP1
Trichophyton
MHGLLLAAGLLSLPLHVLAHPQPSTSTSLAGRAGAVDLNEFRIAHRSSYTSHDEMKKLPSIASFRQGTYLEVATELVKQTIPNMEFRLVDDHYVGDSGIGHVRFRQTMHGIDIDNSDFNVNVGKDGKVLSHGNSFYTGPAPSSNPMVKRDFIDPMQALHGVRKALNLPIKADGAHVEDMSEHKVMFKGTSGALSDPTAKLCYMAKEDGSLALTWRVETDIGDNWLLSYMDAKESSKVHNVVDYVAHATFQVYKWGLADPTEGKREILTNPWNLKTSPLTWLSDGQNNFTATRGNNAIAQYNPDGGNDYENNYRPSPKNLKFEYPYSPDMNPPKTYIDASVTELFYTSNVCHDLYYMLGFNEKAGNFQVNNRGQGGKGNDFVILNAQDGSGTNNANFATPPDGQPGRMRAYIWTRANPPRDASFEAGTIIHEYTHGLSNRLCGGPANSRCLNAIESGGMGEGWGDFYATAVRLKPNDTRKTNYVKGGWVNNSPKGVRMYPYSTDMNVNPLVYTSNNKLNEVHAIGTVWCTMLYEVLWNLIDKHGKNDGPVPIFENGVPNDGKYLAMKIVMDGMAIQPCNPNFVQARDAILDADMNLTKGANKCEIWKGFAKRGLGVGAKFDPKNRTGSTQVPNECK
Secreted metalloproteinase probably acting as a virulence factor.
D4D4Z2
Q1D290
RS18_MYXXD
30S ribosomal protein S18
Myxococcus
MSNGTDSKTASAPPARSGGGFGGGGSRGGDRGDRGDRGGDRGDRGGGLGGDDDKRGGGRGFGRKKVCRFCAEKNASVDFKDQATLKYFVTERGKIIPRRISGNCAKHQREVAVAIKRARGIALLPYNAVVG
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q1D290
P04268
TPM1_CHICK
Tropomyosin-1
Gallus
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATDAESEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAQKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
P04268
Q9Y343
SNX24_HUMAN
Sorting nexin-24
Homo
MEVYIPSFRYEESDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKAESCGSFDETESEESSKLSHQPVLLFLRDPYVLPAASDFPNVVIEGVLHGIFYPHLQPR
May be involved in several stages of intracellular trafficking.
Q9Y343
P45751
HOFO_ECOLI
DNA utilization protein HofO
Escherichia
MNMFFDWWFATSPRLRQLCWAFWLLMLVTLIFLSSTHHEERDALIRLRASHHQQWAALYRLVDTAPFSEEKTLPFSPLDFQLSGAQLVSWHPSAQGGELALKTLWEAVPSAFTRLAERNVSVSRFSLSVEGDDLLFTLQLETPHEG
Required for the use of extracellular DNA as a nutrient.
P45751
Q7NC21
EFTS_MYCGA
Elongation factor Ts
Mycoplasma
MASITELIKQLRASTQAGFMDCKKALEATNNDIDQAIKWLRENGIAKAAKKVDNVASEGVIKLKLADQKATILEINSQTDFVTKNDQFVAFSNELVDLVHKHETTDVAKIEQLKLASGSTVAETQIHLTAIIGEKISLRRVAFVKEEANSSLATYLHSNSRIGVIVKTSKTDDKEFLKHLAMHIAASNPKFVSQKDVSADFIAKEREIAAAQAQSENKPKEFIDRIVDGRINKVLEEVCLVNQKFLVNQEQTVQQAAQAKKVEILSFIRYEVGEGIEKQVSNFADEVKAQMK
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Q7NC21
A1U5I2
FETP_MARN8
Probable Fe(2+)-trafficking protein
Marinobacter
MSRTVFCRKYQKELEGLAMPPMPGPKGQDIYENVSKLAWEEWQNQQTMLINEKHLNLMDVNNRKYLQAQMERFFNNEPFDQAEGYVPPEK
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
A1U5I2
P20459
IF2A_YEAST
Eukaryotic translation initiation factor 2 subunit alpha
Saccharomyces
MSTSHCRFYENKYPEIDDIVMVNVQQIAEMGAYVKLLEYDNIEGMILLSELSRRRIRSIQKLIRVGKNDVAVVLRVDKEKGYIDLSKRRVSSEDIIKCEEKYQKSKTVHSILRYCAEKFQIPLEELYKTIAWPLSRKFGHAYEAFKLSIIDETVWEGIEPPSKDVLDELKNYISKRLTPQAVKIRADVEVSCFSYEGIDAIKDALKSAEDMSTEQMQVKVKLVAAPLYVLTTQALDKQKGIEQLESAIEKITEVITKYGGVCNITMPPKAVTATEDAELQALLESKELDNRSDSEDDEDESDDE
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
P20459
Q5N749
MOR1_ORYSJ
Protein MICROTUBULE ORGANIZATION 1
Oryza sativa
MSTEDEKLLKEAKKLPWDERLQHKNWKVRNDANIDLAALCDSITDPKDARLREFGPLFKKTVADSNAPVQEKALDALLAFQRAADADASRYAKEVCDAIVAKCLTGRPKTVEKAQAAFLLWVELEAAEVFLESMEKAVKNKVAKAVVPAIDVMFQALSEFGAKVVPPKKILKMLPELFDHPDQNVRASSKGLTLELCRWIGKEPVKAILFEKMRDTMKKELEAELANVSGIAKPTRKIRSEQEKELEEEVVPEAAGTNNSEEAVPEAPMEIDEYDLVDPVDILTPLEKSGFWDGVKATKWSERRDAVAELTKLASTKKIAPGDFHEICRTLKKLITDVNLAVSVEATQAIGNLAKGLRTHFSGNSRVLLPVLLEKLKEKKPTMTEALSQTLQAMHKSGCITLLDVIEDVRVAVKNKVPLVRSLTLNWVAFCIETSNKATVLKLHKEYVPICMECLNDGTPEVRDASFSVLTAIAKMVGMKPLERSLEKLDDVRKKKLSDMIGSASDTTSGTVAASNTGVGTSAREVMDSSSMRRSAASMLSGKKPVQAVPATKKSGPAKSATAKKTDGGPQSKASAAPVIEDVEPSEMSLEEIEEKLSSVVKSETISQLKSTVWKERLEAISMLKQEVESLTELDKSAELLVRLLCAVPGWSEKNVQVQQQVIEVSTYIASTVNRFPKRCVVLCLLGISERVADIKTRGHAMKCLTAFCEAVGPGFVFERLYKIMKEHKNPKVLSEGILWMVSAVEDFGISNLKLKDTIDFCKDIGLQSSAAATRNATIKLIGVLHKFVGPDIKGFLSDVKPALLSTLDAEYEKNPFEGTASAPKRTVRAADAVSSASSGTSDGLPREDISAKITPTLLKNLGSPDWKLRLESIDAVSKIVEEAHKRIQPTGTVELFTALRARLYDSNKNLVMATLSTIGGLASAMGPAVEKSSKGILADVLKCLGDNKKHMRECTLTALDLWVAAAQLDKMVPYITVTLGDQKTGSEGRKDLFDWLSKHASNMSDPSEALPLLKPSASSLMDKSSEVRKAAESFMNEILKICGQDVVAKNLKDLPSPTLAIVAERLKLSTVHEGFSDSVKMVTTSMSLPSKAGSKNNKHGPNDRGSNVSKAVSQRGIPARSSVTMISSQDSIQSQALFNIKDSNKEERERRVLVRKFKFEEPRREQIDELKIELFRHFREDVSLRLWNSDFKRQIDGIELLQKALPSSRKEVIELLDILLRWFVLRFCESNTTCLLKVLDFLPELFDVLKDQSYMLTEAEAAIFLPCLMEKSGHNIEKVREKMGELIKQMVNIYSLPKLLPYILEGLRSKNNRTRIECVDIIGYFMDHHGTEVSGLLKNLPSVAALTAERDGEIRKAALNTLATAYKNLGDDVWRYVGKLSDAQRSMLDDRFKWKAREMDKRREGRPGDARAALRRSVRENGSDIAEQSGEAVSRSMAGSMISRENFGYSDAHMVPRQMATATPGPADWREALDIVALGLPEQSVEGMKVICHELTQAVDPESSVLDDLIKEADRLVSCLAVMVPKTFNFSLSGASSRSCKYVLNTLMQTFQIKRLAHAVKEGTLDNLITELLLWLLDERVPLMDDGSQLLKALNVLMLKILDNAERTSSFVVLINLLRPLDPSRWPSPTPPESLAVKNQKFSDLVVKCLIKLTKVLQSTIYEVDLDRILQSIHIYLQELGMEEIRRRAGADDKPLRMVKTVLHELVKLRGTAIKGHLSMVPIDAEPQPIILAYIDLNLQTLAAARMLTPSGTMGQTHWGDAGSNNPNPSTHSTDAQLKQELAAVFKKIGDKQTCTIGLYELYRITQLYPKVDIFAQLQNASEAFRTYIRDGLAQVEKNAAAGRTPSSLPLSTPPPIAPIPSPKFAPSPVHTKSINNKTDCNEDDAGGDTHPFRGQGEIDNRLQTTNLQTDRYQSSGTLDALRERMKSIQAAAVGANFDGVQARPLPSMNGNTLHGGTRLDADPQTQNIIPPMDERALSGLQARMERLKSGSMEPL
Microtubule-associated protein that is essential for cortical microtubules organization and function.
Q5N749
A9B415
RL2_HERA2
50S ribosomal protein L2
Herpetosiphon
MGIKRYKPTSPGRRGMTVSDFAEITKFEPEKSLTEPLKKHAGRNNHGHITTRHRGGGHKRRYRLIDFKRKKFDIPAKVAGIEYDPNRSANIALLHYTDGEKRYIIAPLGLKVGDTLMAGPNAEIRVGNALPLANIPIGSQIHNIELTPGRGGQLVRSAGNTAQLMAREGNYATVRLPSGEMRMVHIKCMATLGQVGNVDHQNIMIGKAGRSRWLGRRPVVRGSAMNPVDHPHGGGEGRAPTGMNPKTKWGKPAMGKKTRHNPRTQRFIVRTRKQK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
A9B415
Q8D2Z3
MRAY_WIGBR
UDP-MurNAc-pentapeptide phosphotransferase
Wigglesworthia
MLVWLCEKLVYLYSGFNVFSYLTIRSIISLLTSFFLSLFFGPRVILFLKKFQIKQIIRLDGPKSHLYKCNTPTMGGVMILVSVIFSVLSWSHLSNSYIWYVLYVLTGYGIIGFFDDYKKIINKNSQGLKAKWKYIWQSIIAISISVFIFLKYQNTNATKLVIPFFKDIMPQLGLWYILLSYFVIVGSSNAVNLTDGLDGLAIMPTVFISAGLAIIAWVTGNINFSSYLNIPYIKFSGELVIICTSIIGSGLGFLWFNTYPAKIFMGDVGSLSLGGALGIISVLTRQEILLFIMGGVFVLETISVILQVIFFKISGQRIFKMAPIHHHYELRGCPEPRLIVRFWIISFILVLLGISTLKVR
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.
Q8D2Z3
A0A0A2IJP3
CNSP_PENEN
Communesin biosynthesis cluster protein P
Penicillium
MSTTTVITPGTITREKNENGAPLYPDYMPFYDPLEKVEDIGAFEHFDPGHRADPKLPNLLKNATKVWELSPHVGTEIHGVQLSQLDSAGLDELALLAAQRGALVFRDQDFVNIGFDAQKKLVSHFGPLHIHGWAPHPAAGSEEHMIIYDHKDDLRVRQSWAGRSPVQWHTDQSPEQQPPGTTFIAMLESPTTAGGDTLVSSSVRAYSSLSPRFRKRLEGLTAIHTNNDGVSQELKHGQQAVMRRGVLQAEHPVVLVHPVTKQKALYVNPVYTKKIVGFDQEESDCILKFLFDHIAKRQDFSCRIRYEAGTVLVWDQRVTNHSQTLDYPIGDRRHGFRLTPLANKPIPAKIEEDDEEFSTDDARHLVGNAS
Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of communesins, a prominent class of indole alkaloids with great potential as pharmaceuticals . Communesins are biosynthesized by the coupling of tryptamine and aurantioclavine, two building blocks derived from L-tryptophan . The L-tryptophan decarboxylase cnsB converts L-tryptophan to tryptamine, whereas the tryptophan dimethylallyltransferase cnsF converts L-tryptophan to 4-dimethylallyl tryptophan which is further transformed to aurantioclavine by the aurantioclavine synthase cnsA, probably aided by the catalase cnsD . The cytochrome P450 monooxygenase cnsC catalyzes the heterodimeric coupling between the two different indole moieties, tryptamine and aurantioclavine, to construct vicinal quaternary stereocenters and yield the heptacyclic communesin scaffold . The O-methyltransferase cnsE then methylates the communesin scaffold to produce communesin K, the simplest characterized communesin that contains the heptacyclic core . The dioxygenase cnsJ converts communesin K into communesin I . Acylation to introduce the hexadienyl group at position N16 of communesin I by the acyltransferase cnsK leads to the production of communesin B. The hexadienyl group is produced by the highly reducing polyketide synthase cnsI, before being hydrolytically removed from cnsI by the serine hydrolase cnsH, converted into hexadienyl-CoA by the CoA ligase cnsG, and then transferred to communesin I by cnsK . Surprisingly, cnsK may also be a promiscuous acyltransferase that can tolerate a range of acyl groups, including acetyl-, propionyl-, and butyryl-CoA, which lead to communesins A, G and H respectively . The roles of the alpha-ketoglutarate-dependent dioxygenases cnsM and cnsP have still to be determined .
A0A0A2IJP3
Q7VRE2
DXR_BLOFL
2-C-methyl-D-erythritol 4-phosphate synthase
Candidatus Blochmannia
MISGAQQYRDKFAVRALVAHNDVAVMIEQCFLVSPQYVCMICEEVARNLKYKLVLMDKNNIQVLSGMKDACVLSALDAVDMVVSTMAGIARLQPIFSAIRVGKKILLANKETLVLSGQLFMTEVYKYNASVLPLDSEYNAIFQNLSVIYQKKLGQVSLSQYGICCIVLTDSGGVLYKITRTKLFKITPVQVYIHPNWSMGLKISVNSATVMNRVLEYIEAHHLFNVSSNEIEILLHTQTIIYATIRYSDGSVLAHFSTPDMKIFIAYAMAYLNKIKLNNISTYSKQYEIYNTYCGNNTLNLDILDTKNYPCLQTAIDASNHSQDSVIVLNADNEVTVEAFLCEMIAFIKIPNFIYRIMNTLNHFQEPSTIDDIIYIDHCIKETEIRYAIGN
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q7VRE2
A8G3M2
PURA_PROM2
IMP--aspartate ligase
Prochlorococcus
MANVVVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVDDKVLKLHLIPSGILYKNTSCLIGSGTVVDPKILLKEIDMLIDNGIDISGLKISSTSHVTMPYHRILDEAMEADRGSNKIGTTGRGIGPTYADKSQRNGIRIRDLLNNERLKDVIEIPLREKNGLLEKIYGIKPLKLEDILEEYLDYGERLSKHVVDCTRTIHAASKNKKNILFEGAQGTLLDLDHGTYPFVTSSNPISGGACIGAGVGPTLIDRVIGVAKAYTTRVGEGPFPTELQGSINDQLCDRGSEFGTTTGRRRRCGWFDGVIGKYAVSVNGLDCLAVTKLDVLDELDEIQVCIAYDLDGEEIDYFPTNSDDLKKCKPIFKKLKGWQCSTADCRKLSDLPQNAMNYLRFLAELMEVPIAIVSLGANRDQTIVIEDPIHGPKRALLR
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
A8G3M2
Q2S9R9
RISB_HAHCH
6,7-dimethyl-8-ribityllumazine synthase
Hahella
MTVKVVEGDFLQGASAKYAIVVGRFNSFVVESLLEGALDALRRHGVAESQITVYRAPGAFEIPLLAQQVAVRTKPDAVIALGAVIRGGTPHFEYVAGECAKGLGQVSLQSGIPVAFGVLTVDSIEQAIERSGTKAGNKGAEAALSALEMVGLLQQVGE
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Q2S9R9
P28056
CYB6_SYNP2
Cytochrome b6
unclassified Synechococcus
MFTKEVTDSKLYKWFNERLEIQAISDDISSKYVPPHVNIFYCLGGITLTCFIIQFATGFAMTFYYKPTVAEAFTSVQYIMNEVNFGWLIRSIHRWSASMMVLMMILHIFRVYLTGGFKRPRELTWITGVIMATITVSFGVTGYSLPWDQVGYWAVKIVSGVPAAIPVVGDQMVELLRGGASVGQATLTRFYSLHTFVLPWLIAVFMLAHFLMIRKQGISGPL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
P28056
A7FSG8
HEM3_CLOB1
Pre-uroporphyrinogen synthase
Clostridium
MNFVIATRRSKLAQVQTEIIIDLLNKKHDIECEKLLIETVGDKILEVSLDKIGGKGLFVKDIEVAMLEQRADAAVHSMKDVPYEMPKGFEIIAIPEREDVRDAFISLDNIKFKDLRKGAKIGTSSRRRAAQLKLLRPDLDIVPIRGNVQTRIEKIKKENLDGVILAVAGLKRVNLDHLITDYFDTKEMVPAIGQGALGIEVMEEHPKKELFKDLDHYNSKICVLAERAFMRELDGDCHSTIGAYASIKDNIMHIIGIFERKNKIIKKEITGTKDQYEKLGISLAEHILKD
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
A7FSG8
Q3T1J8
RTF2_RAT
Replication termination factor 2 domain-containing protein 1
Rattus
MGCDGGTIPKRHELVKGPKKVEKVDKDAELVAQWNYCTLSQEVLRRPIVACELGRLYNKDAVIEFLLDKSAEKALGKATSHIRSIKNVTELKLSDNPAWEGDKGNTKGDKHDDLQRARFICPVVGLEMNGRHRFCFLRCCGCVFSERALKEIKAEVCHTCGAAFQEEDIIVLNGTKEDVEMLKRRMEERRLRAKLEKKTKKPKTAESASKLGISQDSAGPSKAKAGKSEEADPDPREKKSSLAPRGTASNGSASGKVGKPPCGALKRSIADSEESETYKSIFTSHSSAKRSKEESAHWVTHTSYCF
Replication termination factor which is a component of the elongating replisome. Required for ATR pathway signaling upon DNA damage and has a positive activity during DNA replication. Might function to facilitate fork pausing at replication fork barriers like the rDNA. May be globally required to stimulate ATR signaling after the fork stalls or encounters a lesion. Interacts with nascent DNA.
Q3T1J8
A4TP60
FOLD_YERPP
Methenyltetrahydrofolate cyclohydrolase
Yersinia
MSAKIIDGKTIAQQVRNEVAAVVQQRLAAGKRAPGLAVVLVGENPASQIYVASKRKACEEVGFVSRSYDLPMATSEAELLALIDSLNEDTEIDGILIQLPLPNGIDNVKVLERIHPDKDVDGFHPYNVGRLCQRAPKLRACTPRGIMTLLERYDIPTYGLNAVVVGASNIVGRPMSLELLLAGCTTTVTHRFTKNLRHHIENADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLESGKVVGDVAFDVAAERAGWITPVPGGVGPMTVATLIQNTLQACEEYHDISQN
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
A4TP60
Q84J75
PG2B1_ARATH
Rab geranylgeranyl transferase beta subunit 1
Arabidopsis
MSSTSSSQMVQLVADKHVRYILMAEKKKESFESVVMDHLRMNGAYWGLTTLDLLDKLGCVSEEEVISWLMTCQHESGGFAGNTGHDPHILYTLSAVQILALFDKINILDIGKVSSYVAKLQNEDGSFSGDMWGEIDTRFSYIAICCLSILKCLDKINVEKAVKYIVSCKNLDGGFGCTPGAESHAGQIFCCVGALAITGSLHHVDKDSLGWWLCERQLKAGGLNGRPEKLADVCYSWWVLSSLIMIDRVHWIDKAKLVKFILDCQDLDNGGISDRPEDAVDIFHTYFGVAGLSLLEYPGVKVIDPAYALPVDVVNRIIFTK
Required for male fertility and root tip growth.
Q84J75
Q54BN0
TMEDB_DICDI
Transmembrane emp24 domain-containing protein B
Dictyostelium
MNKTNQLINICILVTLFLIGSSSALTLQVEPKSQECFYNFIESGKTSLLLYQVIRGGLLDINVKLTDPKGNTIFERLHFDTQMKGKQSFTAGESGAYKVCFNNEMSRFTAKVVTFTWASEEEGVKEVAKGDSITPMDQSVQKIERVLQSVIHEQKKLRYREQANRDTSESTNARVVWWTIAEVIVLVVMGVGQIWYLRKWFDNKSTGRV
Could have a role in the budding of coatomer-coated and other species of coated vesicles.
Q54BN0
Q5QY61
TRMB_IDILO
tRNA(m7G46)-methyltransferase
Idiomarina
MSHFKSAEEAAAAGKYVRTVRSFVKREGRLTKGQAAAIERLWPTVGLTLENGRLDLAMVFGREAPVTLEIGFGMGHSLVEMAANAPERDFIGIEVHEPGVGACLMAAEEAGVENFRVFHEDAVEVLKQCIPDNSLNCVQIFFPDPWHKKRHHKRRIVQPEFVKLLIQKIETGGVIHLATDWENYAEHMLEVLNDEPRLTNLSSSGDYVPRPENRPKTKFERRGEGKGHGVWDLQFKTNKSATLLG
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Q5QY61
Q8BUZ1
ABRA_MOUSE
Striated muscle activator of Rho-dependent signaling
Mus
MAPGEREREAGPAKSALRKVRTATLVINLARGWQQWANENSTKQAQEPAGWLPGATHDLPNAPKEAGPYQHAPKTLSPKPDRDGEGQHSEEATEVSHIKRKEVTRTVVSKAYERGGDVNYLSHRYENDGGVSEAIQPENDIDRILLSHDSPTRRRKCTNLVSELTKGWKVMEQEEPTWKSDSVDTEDSGYGGDMEERPEQDAAPVAPARIKRPLLSQANRYSETLNCKAHRKYSQVDNLKGRWQQWADEHVQSQKLNPFSDEFDYDLAMSTRLHKGDEGYGRPKEGSKTAERAKRAEEHIYREIMELCFVIRTMARHRRDGKIQVTFGELFDRYVRISDKVVGILMRARKHGLVHFEGEMLWQGRDDHVVITLLE
Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling.
Q8BUZ1
P59355
SCX2_LEIHE
Lqh II
Leiurus
IKDGYIVDDVNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKGPGRCR
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage-dependent. Is active on mammals and competes for alpha-toxins binding on both mammalian and cockroach sodium channels.
P59355
P58295
SC6A5_RAT
Solute carrier family 6 member 5
Rattus
MDCSAPKEMNKPPTNILEATVPGHRDSPRAPRTSPEQDLPAAAPAAAVQPPRVPRSASTGAQTFQSADARACEAQRPGVGFCKLSSPQAQATSAALRDLSEGHSAQANPPSGAAGAGNALHCKIPALRGPEEDENVSVGKGTLEHNNTPAVGWVNMSQSTVVLGTDGIASVLPGSVATTTIPEDEQGDENKARGNWSSKLDFILSMVGYAVGLGNVWRFPYLAFQNGGGAFLIPYLMMLALAGLPIFFLEVSLGQFASQGPVSVWKAIPALQGCGIAMLIISVLIAIYYNVIICYTLFYLFASFVSVLPWGSCNNPWNTPECKDKTKLLLDSCVIGDHPKIQIKNSTFCMTAYPNLTMVNFTSQANKTFVSGSEEYFKYFVLKISAGIEYPGEIRWPLAFCLFLAWVIVYASLAKGIKTSGKVVYFTATFPYVVLVILLIRGVTLPGAGAGIWYFITPKWEKLTDATVWKDAATQIFFSLSAAWGGLITLSSYNKFHNNCYRDTLIVTCTNSATSIFAGFVIFSVIGFMANERKVNIENVADQGPGIAFVVYPEALTRLPLSPFWAIIFFLMLLTLGLDTMFATIETIVTSISDEFPKYLRTHKPVFTLGCCICFFIMGFPMITQGGIYMFQLVDTYAASYALVIIAIFELVGISYVYGLQRFCEDIEMMIGFQPNIFWKVCWAFVTPTILTFILCFSFYQWEPMTYGSYRYPNWSMVLGWLMLACSVIWIPIMFVIKMYLAPGRFIERLKLVCSPQPDWGPFLAQHRGERYKNMIDPLGTSSLGLKLPVKDLELGTQC
Sodium- and chloride-dependent glycine transporter . Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals . May be responsible for the termination of neurotransmission at strychnine-sensitive glycinergic synapses .
P58295
P0A4I9
SIGA_STRPN
RNA polymerase sigma factor SigA
Streptococcus
MATKQKEVTTFDVQVAEFIRNHKQKGTATDDEINASLVIPFTLDADGIEDLLQRIQDAGISITDNEGNPSARVLSNEEEPELSDEDLIGSTSAKVNDPVRMYLKEIGVVPLLTNEEEKELALAVEAGDIEAKQRLAEANLRLVVSIAKRYVGRGMQFLDLIQEGNMGLMKAVDKFDYSKGFKFSTYATWWIRQAITRAIADQARTIRIPVHMVETINKLVREQRNLLQELGQDPTPEQIAERMDMTPDKVREILKIAQEPVSLETPIGEEDDSHLGDFIEDEVIENPVDYTTRIVLREQLDEILDTLTDREENVLRLRFGLDDGKMRTLEDVGKVFNVTRERIRQIEAKALRKLRQPSRSKPLRDFIED
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
P0A4I9
Q5PJR1
DCTA_SALPA
C4-dicarboxylate transport protein
Salmonella
MKTSLFKSLYFQVLTAIAIGILLGHYYPELGAQMKPLGDAFVKLIKMIIAPVIFCTVVTGIAGMESMKAVGRTGAVALLYFEIVSTIALIIGLIIVNVVQPGAGMNVDPATLDAQAVAVYAAQAKEQGIIAFLMDVIPGSVIGAFASGNILQVLLFAVLFGFALHRLGSKGQLIFNVIESFSQVIFGIINMIMRLAPIGAFGAMAFTIGKYGVGSLVQLGQLIICFYITCILFVVVVLGTIARVTGFSIFKFIRYIREELLIVLGTSSSESALPRMLDKMEKLGCRKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATNSHMDIFHQITLLVVLLLSSKGVAGVTGSGFIVLAATISAVGHLPVAGLALILGIDRFMSEARALTNLVGNGVATVVVAKWVKELDHQKLDDVLNNRAPDGKTHEISSYSRHLCP
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane.
Q5PJR1
P09758
TACD2_HUMAN
Pancreatic carcinoma marker protein GA733-1
Homo
MARGPGLAPPPLRLPLLLLVLAAVTGHTAAQDNCTCPTNKMTVCSPDGPGGRCQCRALGSGMAVDCSTLTSKCLLLKARMSAPKNARTLVRPSEHALVDNDGLYDPDCDPEGRFKARQCNQTSVCWCVNSVGVRRTDKGDLSLRCDELVRTHHILIDLRHRPTAGAFNHSDLDAELRRLFRERYRLHPKFVAAVHYEQPTIQIELRQNTSQKAAGDVDIGDAAYYFERDIKGESLFQGRGGLDLRVRGEPLQVERTLIYYLDEIPPKFSMKRLTAGLIAVIVVVVVALVAGMAVLVITNRRKSGKYKKVEIKELGELRKEPSL
May function as a growth factor receptor.
P09758
B7GFA1
PYRDB_ANOFW
Orotate reductase (NADH)
Anoxybacillus
MNRLAVELPGLSLKNPIMPASGCFGFGREYAKFYDLSVLGAMMIKATTLEARFGNPTPRVAETPSGMLNAIGLQNPGVDYVLAEELPWLAQYDVPIIANVAGSTVEEYVEVAKRISKAPNVHALELNISCPNVKKGGIAFGTVPEVAAELTRAVKEVSDVPVYVKLSPNVTNIVAMAKAIEQAGADGLTMINTLVGMRIDVKTGKPILANGTGGLSGPAIKPIAIRMIYEVSQAVSLPIIGMGGIQSAEDVIEFFYAGASAVAIGTANFIDPYVCPNIIAELPALLDELGFDHISECTGRSWNNGQTVYCGA
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
B7GFA1
Q1QR53
YCIB_NITHX
Inner membrane-spanning protein YciB
Nitrobacter
MDKKQPHPLFKLATELGPLLVFFAANAKFNLFVATAAFMVAIVAAMIASYVVTRHIPLMALVTGIVVIVFGTLTLVLHDETFIKVKPTIIYSLFAGVLGGGLLFGRSFIAIMFDQVFNLTPRGWQVLTLRWALFFFGMAILNELIWRTQSTDFWVNFKVFGAVPLTMIFAMMQMPLTKRYHLEPATLEASDASEGDVRK
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Q1QR53
P11931
SYV_GEOSE
Valyl-tRNA synthetase
Geobacillus
MAQHEVSMPPKYDHRAVEAGRYEWWLKGKFFEATGDPNKRPFTIVIPPPNVTGKLHLGHAWDTTLQDIITRMKRMQGYDVLWLPGMDHAGIATQAKVEEKLRQQGLSRYDLGREKFLEETWKWKEEYAGHIRSQWAKLGLGLDYTRERFTLDEGLSKAVREVFVSLYRKGLIYRGEYIINWDPVTKTALSDIEVVYKEVKGALYHMRYPLADGSGFIEVATTRPETMLGDTAVAVHPDDERYKHLIGKMVKLPIVGREIPIIADEYVDMEFGSGAVKITPAHDPNDFEIGNRHNLPRILVMNEDGTMNENAMQYQGLDRFECRKQIVRDLQEQGVLFKIEEHVHSVGHSERSGAVIEPYLSTQWFVKMKPLAEAAIKLQQTDGKVQFVPERFEKTYLHWLENIRHWCISRQLWWGHRIPAWYHKETGEIYVDHEPPKDIENWEQDPDVLDTWFSSALWPFSTMGWPDTDSPDYKRYYPTDVLVTGYDIIFFWVSRMIFQGLEFTGKRPFKDVLIHGLVRDAQGRKMSKSLGNGVDPMDVIDQYGADALRYFLATGSSPGQDLRFSTEKVEATWNFANKIWNASRFALMNMGGMTYEELDLSGEKTVADHWILTRLNETIETVTKLAEKYEFGERGRTLYNFIWDDLCDWYIEMAKLPLYGDDEAAKKTTRSVLAYVLDNTMRLLHPFMPFITEEIWQNLPHEGESITVAPWPQVRPELSNEEAAEEMRMLVDIIRAVRNVRAEVNTPPSKPIALYIKTKDEHVRAALLKNRAYLERFCNPSELLIDTNVPAPDKAMTAVVTGAELIMPLEGLINIEEEIKRLEKELDKWNKEVERVEKKLANEGFLAKAPAHVVEEERRKRQDYIEKREAVKARLAELKR
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
P11931
P83674
LANA_RUMGN
RumA protein 1/2/3
Mediterraneibacter
MRNDVLTLTNPMEEKELEQILGGGNGVLKTISHECNMNTWQFLFTCC
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin exhibiting activity against a wide range of pathogenic clostridia and B.longum.
P83674
Q0VSL7
EFTU_ALCBS
Elongation factor Tu
Alcanivorax
MAKEKFERNKPHVNVGTIGHVDHGKTTLTAALTRVCAEVWGGNAVAFDGIDNAPEERERGITIATSHVEYDSPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLSRQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSDYDFPGDDTPIIKGSALKALEGDTSDIGMPAVQKLVETLDEYIPEPERAVDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEIEIVGIHDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSINPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVAKITE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q0VSL7
P0ADC7
LPTG_ECOL6
Lipopolysaccharide export system permease protein LptG
Escherichia
MQPFGVLDRYIGKTIFTTIMMTLFMLVSLSGIIKFVDQLKKAGQGSYDALGAGMYTLLSVPKDVQIFFPMAALLGALLGLGMLAQRSELVVMQASGFTRMQVALSVMKTAIPLVLLTMAIGEWVAPQGEQMARNYRAQAMYGGSLLSTQQGLWAKDGNNFVYIERVKGDEELGGISIYAFNENRRLQSVRYAATAKFDPEHKVWRLSQVDESDLTNPKQITGSQTVSGTWKTNLTPDKLGVVALDPDALSISGLHNYVKYLKSSGQDAGRYQLNMWSKIFQPLSVAVMMLMALSFIFGPLRSVPMGVRVVTGISFGFVFYVLDQIFGPLTLVYGIPPIIGALLPSASFFLISLWLLMRKS
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
P0ADC7
Q73V46
SSRP_MYCPA
Small protein B
Mycobacterium avium complex (MAC)
MAKGSGRAKAAGGKGGSKQIIATNRKARHNYSIIETYEAGVALQGTEVKSLREGQASLADAFATIDDGEVWLRNLYIPEYQHGSWTNHDPRRNRKLLLHRQQIDRLVGKIRDGNLALMPLSLYFSEGKVKVELALARGKKAYDKRQDLAQRDAQREVVRQLGRRTKGMI
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q73V46
A0L052
PURT_SHESA
Phosphoribosylglycinamide formyltransferase 2
Shewanella
MIGTPYTEGARRAMLLGCGELGKEVAIELQRLGVEVIGVDRYPNAPAMQIAHRSHVINMLDAKALRAIIELEKPHLVIPEIEAIATQTLVEMETEGLNVVPTARATQLTMDREGIRRLAAETLGLPTSPYFFCDTETEFNQAIGKIGVPCVVKPVMSSSGKGQSVIRDAAQSTKAWQYAQEGGRAGGGRVIVEGFIPFDYEITLLTISAVNGIHFCAPIGHRQEDGDYRESWQPQAMSADVLAKSQAIASKVVEALGGYGLFGVELFVKGSDVYFSEVSPRPHDTGLVTLISQDLSEFALHVRAILGLPIPNIHQHGPSASAVVLVEGKSKNIRYQGLADALAAENTQLRLFAKPEIDGRRRLGVALARDKDIESAVNKALDSASKVKVIF
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
A0L052
A4Q998
PNPH_ANOGA
Inosine-guanosine phosphorylase
Anopheles
MSKFSYLQNGKASTNGVPHANGHHQQHQNGHSNGVARNGGTATDTLPVAYQQKAATSGPFHMPRTEHVGYTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIPHFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMHLIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDERFGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVAEVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEEHCHDSIVGVGKNREKTLGEFVSRIVKHIHYEAKK
As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate . Preferentially acts on 2'-deoxyinosine and inosine, and to a lesser extent on 2'-deoxyguanosine and guanosine . Has no activity towards adenosine or 2'-deoxyadenosine .
A4Q998
Q5HH12
PUR3_STAAC
GAR transformylase
Staphylococcus
MVKIAIFASGSGSNFENIVEHVESGKLENIEVTALYTDHQNAFCIDRAKKHDIPVYINEPKQFDSKAAYEQHLVTLLNEDKVEWIILAGYMRLIGPDLLASFEGKILNIHPSLLPKYKGIDAIGQAYHSGDTITGSTVHYVDSGMDTGEIIEQRKCDIRPDDSKEQLEEKVKKLEYELYPSVIAKIVK
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Q5HH12
D3YTS9
PPAT_MOUSE
Acid phosphatase 4
Mus
MAEPGSQGHTVGPLLLLLLLLLPRALPEGPLLFVALVFRHGDRAPLASYPTDPHKEAASTLWPRGLGQLTKEGIRQQLELGRFLRRRYKAFLSPEYKREEVYIRSTDFDRTLESAQANLAGLFPEAAPGSPETDWKPIPVHTVPVSEDKLLRFPMRSCPRYHELLRESTEAADYQEALEGWTDFLTRLGNFTGLSLVGEPLRRAWKVLDTLICQRAHGLDLPSWASPDVLRTLSQISALDIRAHVGPPRAAEKAQLTGGILLDAILSNFSRTQRLGLPLKMVMYSAHDSTLLALQGALGLYDGNTPPYAACMAFEFRGSSREPEEEDGENVTVSLIYRNDTSRPPLPLRVPGCPAPCPLGRFQQLTAPARPPAHGAPCHGSYEPASPPATVPLLAGAVAVLAVLSLGLGLLAWRPRCLRALGGTV
May dephosphorylate receptor tyrosine-protein kinase ERBB4 and inhibits its ligand-induced proteolytic cleavage. May play a role in odontogenesis.
D3YTS9
Q58DW5
RL5_BOVIN
60S ribosomal protein L5
Bos
MGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVTGDEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFSAEVHRKHIMGQNVADYMRYLIEEDEDAYKKQFSQYIKNNVTPDMMEEMYKKAHAAIRENPVYEKKPKKEVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Interacts with RRP1B.
Q58DW5
Q6AP62
RS17_DESPS
30S ribosomal protein S17
Desulfotalea
MSENNTSRKTRTGSVVSDRMEKSVVVRVERKVRHKLYGKFMKTSVKYLADDPENQCNIGDVVLIEECRPLSKRKRWRVKTILEQAV
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Q6AP62
Q00497
SK_SOLLC
Shikimate kinase, chloroplastic
Solanum subgen. Lycopersicon
MEARVSQSLQLSSWINSDKVVRKPSGLLRFSEKWNEKPRHRVVVSCHLQPRKAAHSDRRVQLKVSCSPQNVQASVLESGCFSASIDEIETLKNKAEEVEEYLDGRCVYLVGMMGCGKTTVGRILAETLGYSFFDCDRLIEQAVGGITVAEIFELRGESFFRDNETEVLHKLSLMHRLVVSTGGGAVVRPINWRHMHKGISVWLDVPLEALAKRITTEGTKSRPLLHEESGDVYDTTLKRLTTLMETRGENYANASARVSLENIALKREKDVCHITPAEITLEVLIQIENFLKTQKSVVVL
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Q00497
O94643
CENPU_SCHPO
Sim4 complex subunit mis17
Schizosaccharomyces
MENNSHNVDERRAARMRGAERYKIQNVEFSLDQNLLANLESSTSSSTRSSPASNQQNLEIVSQSEAYHKISDLDDSTSIFSISDQENILERRISEEVVRENSVSSIENVSSSAVARETQSSANILVKDNHFFSHKQKKIQRESIPFHKRDNIETSDAYSSSILENSPPNKVQRLSSLDSSQDSFQEEHPGNVTGTTFSSQAPEERIASPISTSSPESLTNQSSSLQSSLQTSSMAPRNLLDQSTEKDIVVGASDELVRIELTKLSKEAGGSKTLNELDAVQQFFQEFIKENEPLEPYVVKVKNAFVEQVSIRLLELIDLLDANRILSTACKKAANEKLAVQRDLSKLREDRLSVQRKKIQLRNEYIKLSHQQNFLDDIDDFFSQCETVKNELENVTTTPNSTEAFSEINEYASALSKNYGLESQLVELQSLLTQFYQKFLS
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
O94643
Q0C5U1
GLMM_HYPNA
Phosphoglucosamine mutase
Hyphomonas
MARQYFGTDGIRGRVNTSPMTAETALRLSIAAARTFAPEGGREVVIGRDTRRSGDMIEAALVAGFTSMGITPVLLGVVPTPAVALMARETGAALGVMVSASHNKFEDNGLKLFSPEGIKFDDDTEEALEMAMGTALKGEYAAPAEITLPRTMAGTSNRYVRRCLDTLAGGQDFSKLKVVLDCAHGAGFETGPAALTELGAQLTVIGAAPDGININAGFGSTATGALKAAVLETGAHIGIALDGDADRLIVIDETGTEADGDQVMGLIAGEMHRTGRLKGGGMVATVMSNMGLSEYLKTEGLTLARTKVGDRYVGEHMRAHGFNLGGEQSGHIILSDVSTTGDGLLAGLQILSVLAARGGKASDMLRVFTPAPQELINIRYSGANPLESDRVKTALAEAEGLLGDRGRMVVRKSGTEPLIRVMAEALDEDLMLKALHHAANAVTAAAGNS
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Q0C5U1
Q923D2
BLVRB_MOUSE
NADPH-flavin reductase
Mus
MTVKKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPTTVMSEGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKVPPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTNEYDGHTTYPSHQYD
Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
Q923D2
Q8W4Q3
PIRL3_ARATH
Plant intracellular Ras-group-related LRR protein 3
Arabidopsis
MDHDLEIFPLLSYVLHHSDPASHAPPSLAIQQSLANRYPLLTNPYVISSLIESIPSTITQTLFVFGSLGPRPDPLAVSSARSKIREIKENDSLSPEDAAKEEQVYAAVVSLEEVHEGYEKQLRDLEEEIGRVYASAVESLSGGDEVNEEVLAVIKDAEDGGVVERIDLSDHELKLLPDALGKIVGLVSLNVSRNNLRFLPDTISGLEKLEELDLSSNRLVFLPDSIGLLLNLRILNVTGNKLTLLPESIAQCRSLVELDASFNNLTSLPANFGYGLLNLERLSIQLNKIRFFPNSICEMRSLRYLDAHMNEIHGLPIAIGRLTNLEVMNLSSNFSDLIELPDTISDLANLRELDLSNNQIRVLPDSFFRLEKLEKLNLDQNPLEYPPQEMVNQSAEAVREFMRKRWEEMVEEEQLRSVIEAEKQQGGATGWLSWGSSIVTSLFSGGTHGGAAKKPKNSFLDEQL
Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Q8W4Q3
Q1DFX4
KDPC_MYXXD
Potassium-translocating ATPase C chain
Myxococcus
MFSTFLTALRTCVVTMVLTGLLYPLAVTGLAQLLFPGEANGSWVKDGRGRVVGSALIGQGFTRAGYFHPRPSAAGAGYDGAASSGSNLGPTSLKLKERAAAELERLRRENPDAAGPVPAELVTTSASGLDPHLSPEAARWQAARVARARGVALERVLDVVDARVEGRTFGVLGEPRVNVLLLNLALDRRFGPLPDAAPGVGGRASPGQGAP
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Q1DFX4
B2UGM5
1A1D_RALPJ
1-aminocyclopropane-1-carboxylate deaminase
Ralstonia
MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVELFAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDSAGFDIGIRPSWEQAMDDVRKRGGKPFPIPAGCSEHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADKVIGIDASAKPEQTRAQILRIAQHTAELVDLGRNITERDVVLDTRYGGPEYGLPNEGTLEAIRLCARQEAMLTDPVYEGKSMHGMIDMVRNGEFPAGSRVLYAHLGGVPALNAYSFIFRNG
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source.
B2UGM5
Q4UWX9
MURD2_XANC8
UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase
Xanthomonas
MRISQLEGKAVALWGWAREGRAAYRALRQQLPAQPLTVFCNAEEARDVAALADPALQVQTEASAQALAAFEVVIKSPGISPYREEARAAAAQGARFIGGTALWFAEHAQPDGYVPGAICVTGTKGKSTTTALLAHLLRADGHRTALVGNIGQPLLEVLSPQPPPAYWAIELSSYQTGEVGRSGARPELALVLNLFPEHLDWHGSEAAYVRDKLALVTDGRPRIALLNAADPHLAQLQLPESEVRWFNHPDGWHLRGDVVYRGQQPIFDTANVPLPGEHNRRNLCAVLAAVEALGLDAAALAPAALTFRPLPNRLQWLGSVDGIAYVNDSISTTPHASLAALACFAQQRVALLVGGHDRGLDWQEFAAHMAQQAPLEIVTMGANGPRIHALLAPLAQSAGFGLHAADDLAHAMQLARSALGAQGGVLLLSPGAPSFGVYSDYVARGRHFAQLAGFDPAAISAIPGLGVQ
Cell wall formation. Catalyzes the addition of L-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
Q4UWX9
P56297
ATPH_CHLVU
Lipid-binding protein
Chlorella
MNPIVAAASVIAAGLAVGLAAIGPGMGQGTAAGYAVEGIARQPEAEGKIRGALLLSFAFMESLTIYGLVVALALLFANPFAG
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
P56297
Q6PFQ0
KS6A6_DANRE
S6K-alpha 6-like
Danio
MISFGPAQESSLKMEVQSVSSEVNGHQIMDEPMEEESYTHCDEGAYKEIPITHHVKEGCEKADPSQFELLKVLGQGSFGKVFLVRKLMGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVMFTEEDVKFYLAELALALDHLHNLGIVYRDLKPENILLDEAGHIKLTDFGLSKESVDQDKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSLGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSLEAQGLLRMLFKRNPSNRLGAGPDGVEEIKRHTFFSTIDWNKLYRRELQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGIPPSANAHQLFKGFSFVAPVSLEESKSAPLVNILPIVQVHGSSAQFSDVYELKEDIGVGSYSICKRCIHRVTAMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDEGRFVYLVTELMKGGELLDKILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSGNPDSIRICDFGFAKQLRGDNGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDSVSDSSKDLLSHMLHVDPHHRYTAEQVLKHSWIACRDQNPHFQLTRHEAPHLVKGAMAATYSALNHKTCKPVLEPVAASSLAQRRNMKKLTSTDMS
Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of the transcription factor CREB.
Q6PFQ0
O13498
MDM10_PODAN
Mitochondrial inheritance component MDM10
Podospora anserina
MREFMQYVRNAFYGATGWSEDNSYKDLNVTARELIDFPLPRGIRLSLSSLATPHFATSYQLCNVGVVDGSISYLHSSVPLAAVPAQSNKIPLGALMRSYRGLHQLGSRGGTPWSWETGPQIGTIPQVPAVADMGQIPNKDKSSLLYGRLYLPQSLLEAMVIKRFSPALQVQISAVSEQSLRNGGTMLSVVQYDRGKYGVEGLYSTDGGLLGLRGLYNFGGDASVAVMSSQNGTGSPESTEKERIYGRFSAGGEMYYGTLNKSGGMSLGARFATLPTHKGTPLTATLTINPLMGNINTTYAVLAKDFLAMATRMEFNAYSYESDWAVGLELWSNRRPAGFLLGAEPSLDLESDQPELPSKKERSFQAKMEWRLDDPEPEPEPVKIAEKPTEGKEEYLGVFKARLSSNLDLGLVWEGRAKSLIFSLGTGVDLQRLGEPFRSLGLEVQYSS
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
O13498
Q978F3
PGMI_THEVO
Phosphomannose isomerase
Thermoplasma
MQFSEELLTLKDQVRFDKSFKVGKYDKIVIAGMGGSGIAGRIFSEIYDEKPVFLVDDYDIPSFVDDKTEFIAISYSGNTEETISASEEAAKKHANVHAITSGGSLSKMGFDTIIIPSGLQPRSSIGYLLMPLVNTFIKPKIGDVDEAYRLLSETDKDNEEEKSIASEIYNGEHIPVIYGSRPFRAIAYRWKTQFNENAKVLAYSNYFSELNHNDTMPLKDTYRKDEFYFLVFRSDDSRFSKRITVTEKITGNSFRMVDVRGSSLLAKLFYLIHFGDYLTYHLAELRGVDPQDVSLIEKLKKEIA
Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
Q978F3
Q4UMT0
RS10_RICFE
30S ribosomal protein S10
spotted fever group
MKNKIKIRLKSFDHRSLDQATKEIVSAVKRTFANINGPIPLPRKIERFTVNRSPHVHKKSREQFEIRKHKRLLVIDDPNPAVVDALSKVDLAAGVDVVIELESGE
Involved in the binding of tRNA to the ribosomes.
Q4UMT0
B7GFT8
PURL_ANOFW
Phosphoribosylformylglycinamidine synthase subunit II
Anoxybacillus
MSLLLEPSPTMIKEQKMYRDMGLTDEEFAMIERILGRLPNYTETGIFSVMWSEHCSYKNSKPVLKKFPTEGKHVLQGPGEGAGIVDIGDGLAVAFKIESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPIALLNSLRFGELTSPRVKYLFERVVAGIAGYGNCVGIPTVGGEVQFDAAYEGNPLVNAMCVGVIRHEDIQKGIASGVGNTVMYVGAKTGRDGIHGATFASEELTEQSEQKRPAVQVGDPFMEKLLLEACLEVIHCDALVGMQDMGAAGLTSSSAEMASKAGSGIELNLDLVPQRETGMTPYEMMLSESQERMLLVVKKGREQEIMDVFSKYGLEAKAIGRVTDDHMLRLYHRGEVVAEIPVDALAKDAPVYHKPSQEPAYYREFQTMEYVPTVDNYEETLLALLSQPTIASKEWVYEQYDYMVRTNTVVAPGSDAAVLRIRGTNKALAMTTDCNSRYVYLDPEVGGKIAIAEAARNIVCSGAQPLAVTDCLNFGNPEKPEIFWQLEKAVDGMSEACRILETPVISGNVSLYNETNGEAIYPTPIVGMVGIVEHVDHITTQAFKQPGDLIYIIGEAKQEFGGSELQKWLTGRIFGKAPTIDLHVEVKRQQQLLTAIRAGVVASAHDVSEGGLAVALAECVMSAQGLGARVEMKGDVVAELFSETQSRFIVSVKKEHQQMFERLVQAVRIGEVTNDGTLHVTAEDTCILHVPVETMRNVWKGAIPCLLKSKD
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
B7GFT8
Q7XAD0
HSY1_SOLLC
TomHypSys III
Solanum subgen. Lycopersicon
MISFFRAFFLIIIISFLIFVGAQARTLLGNYHDDEMLIELKLESGNYGRTPYKTPPPPTSSSPTHQEIVNGRHDSVLPPPSPKTDPIIGQLTTITTTPHHDDTVAAPPVGGRHDYVASPPPPKPQDEQRQIIITSSSSTLPLQASY
Activates a lipid-based signal transduction pathway in which linolenic acid is converted to jasmonic acid, a potent activator of defense gene transcription. Induces synthesis of proteinase inhibitors I and II in leaves when supplied through cut stems.
Q7XAD0
P0DF80
SSRP_STRP3
Small protein B
Streptococcus
MAKGEGHILAQNKKARHDYHIVETVEAGIVLTGTEIKSVRAARIQLKDGFAQIKNGEAWLVNVHIAPFEQGNIWNADPERTRKLLLKKREITHLENELKGSGMTLVPLKVYLKDGFAKVLIGLAKGKHEYDKRETIKRRDQERDIKKQMKHYNAR
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
P0DF80
P35449
NHX9_CAEEL
Na(+)-H(+) exchanger protein 9
Caenorhabditis
MSSRLFVFFLICYATADKIEKELISDGFQLFTWKWDDVHHVYVITVWLLIASLAKILFNLMKPISKWCPDSSLLIIVGLALGWILHQTSLSGATLDSHTFFLYLLPPIIFDAGYFMPNRALFENFDSVLVFSVFGTIWNTFAIGGSLLLMAQYDLFTMSFTTFEILVFSALISAVDPVAVIAVFEEIHVNEFLFINVFGEALFNDGVTVVLYQMFKSFALIGSENLSVLDYATGGLSFFVVALGGAAVGIIFAIAASLTTKYTYDVRILAPVFIFVLPYMAYLTAEMVSLSSIIAIAICGMLMKQYIKGNVTQAAANSVKYFTKMLAQSSETVIFMFLGLSTISSQHHFDLYFICATLFFCLIYRAIGIVVQCYILNRFRAKKFEMVDQFIMSYGGLRGAIAYGLVVSIPASITAKPMFITATIAVIYFTVFLQGITIRPLVNFLKIKKKEERDPTMVESVYNKYLDYMMSGVEDIAGQKGHYTFIENFERFNAKVIKPVLMRHQKRESFDASSIVRAYEKITLEDAIKLAKVKNNIQNKRLERIKSKGRVAPILPDKISNQKTMTPKDLQLKRFMESGENIDSLYTLFSDLLDRKLHEMNRPSVQITDVDGQDDIQDDYMAEVGSRSNLSAMFRSTEQLPSETPFHSGRRQSTGDLNATRRADFNV
Serves some physiological function other than regulation of cellular pH.
P35449
B1YI73
RRF_EXIS2
Ribosome-releasing factor
Exiguobacterium
MSQAIMKQAEERMEKAHLSLKKELATLRAGRANVSILDPVQVDYYGSPTPLNQVANVNTPEARLILITPWDKSMVTEIEKAIQRADLGLAPSSDGTVIRLAIPPLTEDRRKELVKLVKKYTEEGKVALRNIRRDTNEQLKKQEKDGVLTEDDLRGYTEDVQTLTDKFVKVLDQTAADKEQEIMEV
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.
B1YI73
B4S937
RECF_PROA2
DNA replication and repair protein RecF
Prosthecochloris
MRLDEIKIQNFRKHSELIFSPSEGINLIFGPNGSGKTNILEAIHYCALTKGFNRTTDRQCMNFSAESFLLKSLFTSDTGCQYRVHVDFSTNGGKSISLNNSQLEKFSALIGLIPCILFSPAEITIVHGSPQERRRFLDNALCQISKSYLEQLLQYRRILQQRNALLHSSWDRSSPAPDMNIWTELLAESGAFIIKERMDFLDEFQPYFSNAYAILDTGEIPRLTYRSSLGKALVSSDRAGIADSLMHRFGEIQHQEQVRKQTLLGPHRDEILFYLDGSDVKKYASQGQTRTFLIALKVALQRFLFDKKGEQSIFLLDDIFSELDQRRVERVLEMIAGFGQSLITSTEKTGLSFLHEISIHDMLYKHGDPL
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
B4S937
A1IGV8
AAGAR_THASX
AgaraseA33
Thalassotalea
MITSSKKIVSAMLSTSLWIGVASAAYAETTNVEAEGYSTIGGTYQDGNPQPINIYSVNGVQAINFVNRGDFAEYDVSVSTAGEYSIEYLIGTSIASGSAVEISVLVDGNWQSAGSTNVPLGQWDNFQALAANNNISLAQGTNRIKITGAGTHDWQWNLDAFSLTLVTPENPDNPDNPDNPDDGNTGQPGTPFTIEMEAFDATGSDDPRAQGMVIGERGYPEDKHTVVDSNQTTDWVDYNINFPVSGNYRIEMLASGQTSHATAILFVDNVQINEVAVDTGNQAVFLDFELTDSTYISAGAHTIRVQSGSQINEFSWMWFGDALTFTPLDGGSTDGDADNDGVLDSVDTCPNTPAGAQVDANGCEIIVDNDTDNDGVDNSIDQCPNTPAGAQVDANGCEIVAVVDADNDGVEDSLDMCPNTPAGAPVNGQGCADSQLDADNDGVSDDIDQCPSTPAGSVVDGTGCIVVTPPADSDNDGVVDTLDMCPNTAAGLTVDSQGCALSQLDSDNDGVTDDIDQCANTPSGETANATGCSSSQEGGGTDPDTPQPGLLYGELAGAMNVSDTNPNWERTTDLLQTEDSVKGNTTEVYTGFIYDADGHISFYEHIDDSVRLYIDGVLVLSNDSWEASSQTTDLNLTPGTHEIELRIGNADGGSGAVDGIGFGIDVDGGTNFVHPSTLSESIFTSVGEETGNPDLEQEGDIIVELESFVFTSTNGRVGSDSVEGFSPTATGVNWVTNGDYGDYMVTFEEPGTYGAYITISAANDGSYGARVDVDGWPVAWGYFGGTGSWDVSSENLLYGGTFVVEQAGEKVVRVEAIGGSDWQWSGDRVRFTRLGDVTAIPSPIYNPDDHFVAEIQGPQTDVTYLKKPVEIPANKKVLKSDVWYTYPQNRELEGYDNFGATGAFWGHPPEHDFYDDTVIMDWAVDAVYAFQAEGYEYTARGEFDWGYGWFTEYTTNPQPHYVRTLDDRNVRMTFMGYLSHDGYNNNWLSNHSPAFVPFMKSQVDQILKANPDKLMFDTQTNSTRSTDMRDFGGDFSPYAMENFRVWLSKKYSTGELAALGINDINSFDYGDFLRAQGVTHTSWSNAGDTLSGNIPLQEDYIYFNRDVWNQKFAEVLDYIRQQQPDIEIGASTHLFESRGYVFNENLTFLSGELNLGARTTISELPTNILVHLKGAQAVDKTLVYFPYPWEFDELRLQDAPRFGRGWVAQAYAYGGLFSIPANVWVGGEVWTWSPGADNYRDIYLFVRAQADLLDDYTSYSKVGLVHAMYSSMKAGFIDGGNQIQSSTKLLTEGNINFDLLVFGDEGYPVVPRPEDFDKFDHIFFDGDEQYLTAEQQALLDQQGDKVRHIGQRGTVSGIEITVSISGTESNETVSAVSRIHETDAAAPYVVHLVNRPFAGGVTPTLNNVEVAIPQSYFPEVVTGATLHLPDGTSTSLTLSTNADGDVVLPVNNLEVWGILELAH
Alpha-agarase. Hydrolyzes agarose, agarohexaose, neoagarohexaose and porphyran. Hydrolysis of porphyran by this enzyme improves its antioxidant activity. Does not hydrolyze kappa-carrageenan, iota-carrageenen or lambda-carrageenan.
A1IGV8
O80362
RK10_TOBAC
CL10
Nicotiana
MEATFFTLPSSTSHSYPFSLKSHFNNSLTLPTHPHFKPKSKNLTIRSAISRTKKEETVETVKQQLEDCYLLAGIGYKGLTVKQFQELRSQLPDTTKLLVAKNTLVLKAIEGTKWEALKPCMKGMNAWLFVHSEEIPAALKPYRTFQKEKKLEENDFTGAVFEGKFYGPEEFKALETLPTRAEIYAQLLGSLKGPASAVVGTIQAPARNLVMVLKAYVKKLEEEGGSQ
This protein binds directly to 23S ribosomal RNA.
O80362
A6TB83
MTFA_KLEP7
Mlc titration factor A
Klebsiella
MFKWPWKADDESGNAEMPWEQALAIPVLAHLSSTEQHKLTQMAARFLQQKRLVALQGLELTPLHQARIAMLFCLPVLELGIEWLDGFHEVLIYPAPFIVDDEWEDDIGLVHNQRVVQSGQSWQQGPVVLNWLDIQDSFDASGFNLVVHEVAHKLDTRNGDRASGVPLIPLREVAGWEHDLHAAMNNIQDEIDLVGESAASIDAYAATDPAECFAVLSEYFFSAPELFAPRFPALWQRFCHFYRQDPLARRRENGLQDEGDRRIVH
Involved in the regulation of ptsG expression by binding and inactivating Mlc.
A6TB83
A8G795
PANCY_PROM2
Cytidine monophosphate kinase
Prochlorococcus
MKKVIIRKTEEIENWKRNINNEINFIPTMGNLHNGHIKLISTAKNDNSNVNLVSIFINPLQFDNKLDLENYPKTIDNDIKISFSNGADAIFIPSNEDIYPPNNKNIKFLKAPIELSSALCGLNRIGHFDGVCTVVYRLLNLIKPKNLYLGEKDWQQLLILKNLVLKEKLNVAIKSIPTQRDFDGIPLSSRNVHLSKNERKLIRFFSSELLEAKKNFQQEKNINLNEIIKKLSAKKISIEYLEHLHPHTLQKARLEDNISLLAGAIRCGETRLIDHVFLMKRRPIIAIDGPAGSGKSTVTKLIAKKLKLLYLDTGAMYRALSWLLLKENIDYKKEKKLLNIFKDISIVFKSNTNSHQDVYVNNCCVTEEIRSQKISSIVSKISSIKEVRKFLVEEQRKIGESGGLVAEGRDIGTTVFPNAELKIFLTASIDERAKRRKSDKQSKDSQEIDLDTLKELIEKRDFEDSNREISPLIKANDAIEIISDGYTINEVVDKIIDLYNDKIPKETEIK
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
A8G795
Q4A0J9
URED_STAS1
Urease accessory protein UreD
Staphylococcus
MSNNKQAWTGQLDLSVFNNGKKSVARDVFFEKALKVMRPVYLNQSDIPTFYIVNVGGGYLDGDRYTMNFNIDSDAKVILTSQGATKIYKTLNDHVEQYQTFNIKNNGYAEYVGDPIIAFENAKFYQHNVFNLESTASLFYTDILTPGYSKSDKRFSYTYMHLLNEIYVDDALVTFDNMLLDPQKQNVDGLGYMEDYTHLGSCYFIHPSVNQKFIEQVYEEIKHFQHKYDCRFGITHLPTHGFSLRILSNKTQVIESIITAVQCYVVKQIFDRDVDFLRKY
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q4A0J9
Q92FZ9
TRUA_RICCN
tRNA-uridine isomerase I
spotted fever group
MYRYKITIEYLGTDLAGWQRQAGVMSVQQILEEAIYKFSGEQVILFGSGRTDAGVHAIGQVAHFDLSKYLEPHKIITAINYFARPYAVGVWNCELAPNNFHARFSATSRYYIYRIINRPYPSVIDLNRAWWISAPLDVPAMQQAAVYLLGKHDFTSFRASSCQSKSPIKTLTELNIIKEDEEIKLYLSAPSFLHHMVRNIVGSLVLVGKNIWQAEQIKDVLEAKDRKAAGPTAPASGLYFVKTAY
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q92FZ9
A2BDG9
SPRN_GASAC
Shadow of prion protein
Gasterosteus
MSGMNQVVATCWTCLLLSAFLCEPVLSKGGRGGSRGSSRGSHSRSPKAGGYRGGGPHNGGTRGSRYRGRSSPVRVASAAAAGAAVALTADKWYASAYRRSKADGSDEELDYYNRTNYFDAQMSSSTQNGSSLSQLVSIIIATFSPKYGLLMDSIL
Prion-like protein that has PrP(C)-like neuroprotective activity.
A2BDG9
P40491
FMC1_YEAST
Formation of mitochondrial complexes protein 1
Saccharomyces
MDRPRTLRTYRGLIRAILKYERPSKIVNWGNLRKAMITKLEYAKKQNQRDSHENINRQLEKWKKLDPVSDRSLNLFIADSKSLRSILQNDIKWEKKVAQGQNVDEIFEHALDIIKFLDNQREYEELVDRYNPGNKLTQDEKVKRTANVVGLDVPT
Needed for the assembly of the mitochondrial F1-F0 complex at high temperature.
P40491
Q2GL54
RL22_ANAPZ
50S ribosomal protein L22
phagocytophilum group
MSIVIAAKGLGLRSTPAKLNLVADLIRGKDVAVAAMYLKFCKKKAALLIDKVLKSAIANARANYGVDADNLYVKEVLVGKAFTLRRVQPRARGRACRISKRYGSVVVKLLER
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Q2GL54
Q022F6
RECR_SOLUE
Recombination protein RecR
Candidatus Solibacter
MPDFAEPLARLITEFKRLPGIGQKSAQRLAFHVLRAKREDAEHLSQAILDVKDKLGLCAVCNNIADGEICQYCSDSNRDPSVVCVVEEPHNIVGIETTRQFEGRYHVLHGALSPLRGVGPDMLKIKGLVERIGQGEVREVIVATNPNVEGEATAVYLARLLKPLGVKVTRIGMGIPVGSDLEFADEVTISKAMEGRREM
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q022F6
Q12V48
HIS3_METBU
Phosphoribosyl-AMP cyclohydrolase
Methanococcoides
MIDLDTLKFDGNGLIGAIAQDNRTGEVLMFAFMNREALEKTIETGIAHYWSRSRQKLWKKGESSGHMQKVHELLIDCDMDAIILKISQEGGACHTGYRSCFYRNIEGDVVGEKVFDPADVY
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Q12V48
A7FMZ8
EFP_YERP3
Elongation factor P
Yersinia
MASYYSNDFRPGLKIMFEGEPYAVESSEFVKPGKGQAFARVKMRRLLTGGRVEKTFKSTDSLEGADVNDMNLTYLYNDGEFWHFMNNETYEQLQADAKAVGDNGKWLIDQAECIVTLWNGQPIAVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQVGEIIKVDTRSGEYVSRVK
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
A7FMZ8
Q8GYY1
HSFA3_ARATH
AtHsf-17
Arabidopsis
MSPKKDAVSKPTPISVPVSRRSDIPGSLYVDTDMGFSGSPLPMPLDILQGNPIPPFLSKTFDLVDDPTLDPVISWGLTGASFVVWDPLEFARIILPRNFKHNNFSSFVRQLNTYGFRKIDTDKWEFANEAFLRGKKHLLKNIHRRRSPQSNQTCCSSTSQSQGSPTEVGGEIEKLRKERRALMEEMVELQQQSRGTARHVDTVNQRLKAAEQRQKQLLSFLAKLFQNRGFLERLKNFKGKEKGGALGLEKARKKFIKHHQQPQDSPTGGEVVKYEADDWERLLMYDEETENTKGLGGMTSSDPKGKNLMYPSEEEMSKPDYLMSFPSPEGLIKQEETTWSMGFDTTIPSFSNTDAWGNTMDYNDVSEFGFAAETTSDGLPDVCWEQFAAGITETGFNWPTGDDDDNTPMNDP
Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Involved in heat stress response. Activated by DREB2A under heat stress.
Q8GYY1
Q9UTL6
JAC1_SCHPO
J-type accessory chaperone 1
Schizosaccharomyces
MLKQAGNQSFRPFISFAQKSLFNRQITGNHWIFARFKFYPLNKIVNYNHFHSSSCQSEAKNFYKQFEGDISDPPPKGPFDIDLGALKSSYLRKMKTLHPDVAQGKDAALAQRDSAELSKAYNTLKAPLTRAEYILQLQGINPVSEDISNSDPEFLMEIMDVHENISASRDSPEKLLQLSQENQGRKVQEINEIRKAMESSNWDSALLYVNRLRYWNTIDKILHDL
Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria . Stimulates the ATPase activity of the mitochondrial Hsp70 chaperone ssc1, to mediate the transfer of iron-sulfur clusters from isu1 to grx5 .
Q9UTL6
B6HYQ4
KDPC_ECOSE
Potassium-translocating ATPase C chain
Escherichia
MRGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFQGRPSATAEMPYNPQASGGSNLAVSNPELDKQIAARVAALRAANPDASTNVPVELVTASASGLDNNITPQAAVWQIPRVAKARNLSVEQLTQLIAKYSQQPLVKYIGQPVVNIVELNLALDKLDE
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
B6HYQ4
Q6F9J0
PQQD_ACIAD
Pyrroloquinoline quinone biosynthesis protein D
Acinetobacter
MASKRIIRMSDLLHTTPVFNRGYRFQWEQAQQSYVILYPEGLVRLNESATLILKQIDGKLTVHDIIQNLSAQFPDATGLDQDIVEFLKQAESRQWICLQ
Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
Q6F9J0
Q96TA0
PCDBI_HUMAN
PCDH-psi2
Homo
MWKTWLQGGARVIFDDYKPYLRLDPQNGDLLLNEQLDREALCDLTEPCILHFQVLFENPLQFFRAELLVKDINDHTPTFLNNHMLLKISEGATLGTLFQIDSAQDLDVGKNGVQNYTISPNPHFHLKLRDSDEGRKYPELVLDQSLDREKVSEFSLTLTAVDGGSPPRSGTTLINVVVLDISDNAPEFEKPVYEVLVPESSPLDSLIIKASATDLDAGINGELSYSFSHVSRDVRKTFEIHPISGEVYLKAPLDFEIIQSYIINIQAIEGGSLSGKSSILVRVVDVNDNPPEIAMTSLTSPIPENSSPEMVVAVFSIRDQDAGDNGRTVCSIQDNLPFVLKPTFKNFYALVTEHPLDREVRNEYNITITVTDLGTPRLKTEHNITVLVSDVNDNAPIFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLTSLVSINADNGHLFALRSLDYEALQEFGFRVGAADHGSPALSSEVLVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEGRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVEGFSQPYLPLTEAAPSQAQADSLTVYLVVALASVSSLFLFSVFLFVAVRLCRRSRAASMGRCSVPECPFPGHLVDVSGTGTLSQSYQYEVCLTGGSGANEFKFLKPVIPNLLSRDSEMEKAPPF
Potential calcium-dependent cell-adhesion protein.
Q96TA0
Q01515
AAC3_SERMA
Gentamicin-(3)-N-acetyl-transferase
Serratia
MNTIESITADLHGLGVRPGDLIMVHASLKAVGPVEGGAASVVSALRAAVGSAGTLMGYASWDRSPYEETLNGARMDEELRRRWPPFDLATSGTYPGFGLLNRFLLEAPDARRSAHPDASMVAVGPLAATLTEPHRLGQALGEGSPLERFVGHGGKVLLLGAPLDSVTVLHYAEAIAPIPNKRRVTYEMPMLGPDGRVRWELAEDFDSNGILDCFAVDGKPDAVETIAKAYVELGRHREGIVGRAPSYLFEAQDIVSFGVTYLEQHFGAP
Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
Q01515
Q6ZVE7
GOT1A_HUMAN
hGOT1b
Homo
MISITEWQKIGVGITGFGIFFILFGTLLYFDSVLLAFGNLLFLTGLSLIIGLRKTFWFFFQRHKLKGTSFLLGGVVIVLLRWPLLGMFLETYGFFSLFKGFFPVAFGFLGNVCNIPFLGALFRRLQGTSSMV
May be involved in fusion of ER-derived transport vesicles with the Golgi complex.
Q6ZVE7
A5GD90
DAPB_GEOUR
4-hydroxy-tetrahydrodipicolinate reductase
Geotalea
MVKIAVCGAAGRMGGRIIAAISETEGAVVSGALERLGHPMVGQDAGFNAGLGAIGVTISDDLTAVVQGCDVLIDFTTPKVSLKNLEVCGLNKKSIVIGSTGFTPEERALAAELAKDIPVVLAPNMSVGVNVCFKVLADVAKILGDDFDVEIVEAHHKMKKDSPSGTAVRMGEVVAEALGRDYNKVANFHREGICGERTKDEIGMQTIRGGDIVGEHTVYFIGMGERIEITHRAHTRDMFSRGSVRAAKWVVSQKPGLYDMQDVLGLR
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
A5GD90
O31817
FOSB_BACSU
Fosfomycin resistance protein
Bacillus
MEIKGINHLLFSVSHLDTSIDFYQKVFGAKLLVKGRTTAYFDMNGIWLALNEEPDIPRNDIKLSYTHIAFTIEDHEFEEMSAKLKRLHVNILPGRERDERDRKSIYFTDPDGHKFEFHTGTLQDRLRYYKQEKTHMHFYDETAF
Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
O31817
P35516
MTL1_LACLL
Type II methyltransferase M.LlaI
Lactococcus
MRYLGNKTNLLNFIQQVIKKHDIQGQTFADLFAGTGSVGDYFKGEYTVLSNDYMYFSKVISEAKLLNSEKPKFDSFVKRYGKTPFQWLNEREYTPNDGYFVYNNYTPRAERMYLTEENALKIDGMRLDIEELFQEGVISKAEYSYLLASLLESVTKVSNTSGTYQAFFKFWESRALKKFTIMPLEMKDSLSVSKDNRCFNKNTNRLVREISGDIAYIDPPYTITQYTNSYHVLETIARYDNPELFGKTGRRVKREFSGYSNKSKAYYEFEDLFRQINFTHVLVSYSNQSIVPLDELVDLARRFAVDGIVEVETNEYREYSTNNSSMKGEGKKLQEVIIYFKKNLETNKSPLNYAGSKDDVIPRIFKLLPKHVTTFVDAMGGAFNVGANRTALNKVVYNEYHPFVFEMMQMIVNTPADELIRNVEQIVTRYSLEKKGKEAFNRLRDHYNNEEQTPINLYTLNIYSFQNILRFNQAKKYNTPIGNNEFNEGYKDRITRFVTRAPEVEMRLGSYSAINFNEYDDDTVFYFDPPYLVTTAGYNDGKRGFDGWDAEQEASLLKYLTELDSAGKKFMLSNVLEHKGKTNHLLMEWIQHHGFNVNTIGETGIKYPRREILVTNYNTFER
An alpha subtype methylase that modifies unknown specific adenine residues, and protects the DNA from cleavage by the LlaI endonuclease.
P35516
P81488
DRS9_PHYBI
Dermaseptin-gene related 3
Phyllomedusa
MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDEEEQEDDEQSEEKRALWKTIIKGAGKMIGSLAKNLLGSQAQPESEQ
Has antimicrobial activity. Exhibits a bactericidal activity towards several species of mollicutes, firmicutes and gracilicutes. This peptide is membranotropic and it efficiently depolarizes the plasma membrane.
P81488
Q9Z690
ATPD_CLOAB
F-type ATPase subunit delta
Clostridium
MYEFLDRRYALALYEVGEKNQKLEEYINDFGEIVHLLKNDENINQVVNHPQISTSEKKKIFMEIFKGKIDEKLLNFLLLLLEKKRIHDAEGILTQLNKISLEKHNKVVAEVRTVIPLTDNEKTTLASKLSAKYNKIIIFKEIIDKTIIGGVYVRVGDDVIDGTIKFKLESMKKVMLKEE
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Q9Z690
B5YFA5
VATE_DICT6
V-ATPase subunit E
Dictyoglomus
MSLERIVERLETEKRTKIEEIKNKKEKEFQEFVAKKEKELEEWKEKQKRSLKEKLNREENTLAAQLKLKYNAEKLRIESDAIAKVKNLVLERLKSSSNEVYNKIWENLLERESIKSGEMILTKNEDKIDVDYFCKKYSLTLSKDRMEGNGGFVIQKDNLVIDLTVDTIIEELVNKNILEIAQILHGER
Produces ATP from ADP in the presence of a proton gradient across the membrane.
B5YFA5
P84672
PPK5_DERCR
FXPRL-amide
Derocalymma
DGDMSGEGKGMWFGPRL
Myoactive.
P84672
B9HRL7
PCBER_POPTR
Phenylcoumaran benzylic ether reductase POP1
Populus
MASKILFIGGTGYIGKFIVEASAKAGHPTFVLVRESTLSNPAKSVVIYNFKNLGVNFLIGDLFDHESLVKAIKQVDVVISTVGHAQLVEQDRIIAAIKEAGNVKRFFPSEFGNDVDRVNAVEPAKSAFATKANVRRAIEAEGIPYTYVSSNFFSGYFLLSFNQPGATAPPRDKVVILGDGNPKAVFNKEDDIATYTIKAVDDPRTLNKILYIKPPANTISFNDLVSLWEKKIGKTLERIYVPEEQLLKNIQEASVPVNVVLSIGHSVFVKGDHTNFEIEPSFGVEASELYPDVKYTTVDEYLKQFV
Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC).
B9HRL7
C0ZVQ6
RPOB_RHOE4
Transcriptase subunit beta
Rhodococcus erythropolis group
MLEGRILAVSSQTKAVSGIPGAPKRVSFAKVREPLEVPGLLDVQTDSFEWLIGAQSWRERAAALGDNAVSGGLEDILAELSPIEDFNGTMSLSFSDPRFDEVKASTDECKDKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTDKGTFIINGTERVVVSQLVRSPGVYFDMSVDKSTEKDLHSVKVIPGRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTTEQITERFGFSEILMATLEKDNTAGTDEALLDIYRKLRPGEPPTKESAQTLLENLFFKDKRYDLARVGRYKINKKLGLNAGQPIVASTLTEEDIVATVEYLVRLHAGDTSMTAPGGVEVPVEVDDIDHFGNRRLRTVGELIQNQIRVGLSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIREFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRRVVDGQVTDEVDYLTADEEDRHVVAQANSAIDREGRFTDSKILVRRKGGEVEFVASSDIDYMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVRSEAPLVGTGMELRAAVDAGDVIITEKTGVVEEISADYVTVMADDGSRKTYRMRKFARSNQGTCANQRPIVDEGQRVEAGQVLADGPCTENGEMALGKNLLVAIMPWEGHNYEDAIILSQRLVEEDVLTSIHIEEHEIDARDTKLGAEEITRDIPNVSDEVLADLDERGIIRIGAEVRDGDVLVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGETGKVIGIRVFSRDEDDDLPPGVNELVRVYVAQKRKIQDGDKLAGRHGNKGVIGKILPQEDMPFLSDGTPVDIILNTHGVPRRMNIGQVLETHLGWIGKTGWNIQIASDGTRPDWAATLPEEMLSAPADSNIATPVFDGAKEDELTGLLGATLPNRDGEQMVGPDGKATLFDGRSGEPFPYPVSVGYMYIIKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDVVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAITMADGDDEDLERAAANLGINLSRNEAATVDDLAN
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
C0ZVQ6
Q88VP9
PRMA_LACPL
Ribosomal protein L11 methyltransferase
Lactiplantibacillus
MKWTEVTVSTSNEAVEAVANILMEAGASGVKIDDALDYQNLKPDRYGEIIDLATIPHVTSGAKISAYYPETVFVPEVIPTIKQRVSQLTDFGLNPAPNEVSMTALSDEDWATAWKKYYHPVRVTRYLTIVPSWEQYQPVQSGELVLRLDPGQAFGTGTHPTTKLCLQALETVINGGEHLIDVGTGSGVLSIAAKAMGVGAVEAYDLDDVAVASAQTNLDLNPVAKDVHVAANDLLAGIDTQADIIVANILAEIIIPLVPQARQNLKRGGYFIASGIIDDKFQVVMTTIKEAGFQITQHTQMGDWHGIVAYLPTAED
Methylates ribosomal protein L11.
Q88VP9