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
|
|---|---|---|---|---|---|---|
Q57T38
|
EFTS_SALCH
|
Elongation factor Ts
|
Salmonella
|
MAEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGVIKTKIDGNVAFILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALVAKIGENINIRRVASLEGDVLGSYQHGARIGVLVAAKGADEELVKQLAMHVAASKPEFVKPEDVSADVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKSVGQLLKEHNADVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS
|
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.
|
Q57T38
|
A8GH24
|
ACKA_SERP5
|
Acetokinase
|
Serratia
|
MSSKLVLVLNCGSSSLKFAIIDAVNGEEHLSGLAECFHLPEARLKWKMDGAKHEAALGAGAAHSEALNYIVNTILAQKPELSAQLTAIGHRIVHGGEKFTASAVINDEVLQGIKDSVPFAPLHNPAHLIGIAEALKSFPKLADKNVAVFDTAFHQTMPEESYLYALPYSLYRDHSVRRYGAHGTSHFYVTQEAAKALNKPVEEVNLITCHLGNGGSVTAVRNGKCVDTSMGLTPLEGLVMGTRSGDIDPAIIFHLHDSLGMSVDQINKMLTKESGLLGLTEVTSDCRYVEDNYESKADAKRAMDVFCHRLAKYIGAYSALMDGRLDAVIFTGGIGENAGMVRELTLNKLGLLGFEIDHERNMAARFGKSGAITKDGSRLALVIPTNEELVIAQDASRLTA
|
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
|
A8GH24
|
Q7N545
|
ZNUC_PHOLL
|
Zinc import ATP-binding protein ZnuC
|
Photorhabdus
|
MSTLITLKNVAVNFGDRRVLNNISLHLQRGNILTLLGPNGAGKSTLVRVVLGLIEPSSGTIEQTDGLKIGYVPQKLHLDPTLPLTVKRFMMLKPGVKSGDILPALERVNAAHLLQQPMQKLSGGESQRVLLARALLNQPQLLVLDEPTQGVDVNGQLALYDLINQIRTELHCAVLMVSHDLHLVMAKTDEVLCLNQHICCSGTPEVVSTHPEFIAMFGHHGAEQLAIYRHQHDHHQHNHHHDLKGKIILENNRECHS
|
Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
|
Q7N545
|
A3NZ80
|
RL13_BURP0
|
50S ribosomal protein L13
|
pseudomallei group
|
MKTFSAKAHEVTREWYVIDATDKVLGRVASEVARRLRGKHKPEFTPHVDTGDFIIVINASKLKVTGNKTLDKKYYRHSGYPGGIYETTFGKMQERFPGRALEKAVKGMLPKGPLGYAMIKKLKVYAEATHPHSAQQPKALEI
|
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.
|
A3NZ80
|
A9WSR3
|
RS13_RENSM
|
30S ribosomal protein S13
|
Renibacterium
|
MARLAGVDLPREKRLEVALTYIYGVGKTRAHKTLAETGISPDVRVKDLSDAELVQLRDYIEVNYKVEGDLRREVAADIRRKVEIGSYEGIRHRRGLPVRGQRTKTNARTRKGPKRTVAGKKKAGR
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
A9WSR3
|
C5A5D0
|
KAD_THEGJ
|
Adenylate monophosphate kinase
|
Thermococcus
|
MNILIFGPPGSGKSTHSRRIVEEYGLTYISSGDLIRGEIERKSSLGLEMAAYLSRGDLIPDTIVNTLIISRLRRQRENFILDGYPRTPEQVIALENYLYDHGIRLDLALEIFIDEDTSVERISGRRICPNCGAVYHITYNPPKVPGICDVCGTKLIQRTDDREEVVRKRYRIYIKNMEPIIKFYRAKGIYVRVDGDGLIPDVWKRIKPLLDYIHEREKKRKEHE
|
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.
|
C5A5D0
|
E1VBT6
|
GFAL_HALED
|
Putative glutathione-dependent formaldehyde-activating enzyme
|
Halomonas
|
MLLEGSCHCGAVRFRVVSPHPYPFNRCYCSICRKTAGGGGYAINLSGDADTLVVHGAEHTSIYQAEIDGLTSPGERHFCSRCASALWVFDPRWPELVHPFASAIDSDLPRPPERVHLMLENKPDWVEIESREQDRCFAGYPDESIAEWHARLGLEEG
|
Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.
|
E1VBT6
|
B0CLJ1
|
COBS_BRUSI
|
Cobalamin-5'-phosphate synthase
|
Brucella
|
MQRNGLIGDTIRSLGFLSRLPLPQGWFDNTDDSLPRNARAFPLAGGILGLLAGVALLIANAISLPPLAAALIAIGALAAMTGALHEDGLGDTADGFFGASTPDRRLDIMKDSRIGTFAALTLVIWTGVKASLLMAIIARAGAGYALLALIGTEAASRAGMLAFWHALPSARPGGLADSMGQPQWETVVCGCGLGLALLAIGFLPSGGMVALINALVLMTVVLFGFARLCMAKIGGQTGDTLGAAQQIGSLAALIGLVMAL
|
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
|
B0CLJ1
|
Q9UK12
|
ZN222_HUMAN
|
Zinc finger protein 222
|
Homo
|
MAKLYEAVTFKDVAVIFTEEELGLLDPAQRKLYRDVMLENFRNLLSVGGKIQTEMETVPEAGTHEEFSCKQIWEQIASDLTRSQDTTISNSQLFEQDDNPSQIKARLSTVHTREKPFQGENCKQFFSDVSFFDLPQQLYSGEKSHTCDECGKSFCYISALHIHQRVHMGVKCYKCDVCGKEFSQSSRLQTHQRVHTGEKPFKCEQCGKGFRCRSALKVHCKLHMREKPYNCEKCGKAFMHNFQLQKHHRIHTGEKPFKCEICGKSFCLRSSLNRHCMVHTAEKLYKSEKYGRGFIDRLDLHKHQMIHMGQKPYNCKECGKSFKWSSYLLVHQRVHTGEKPYKCEECGKGYISKSGLDFHHRTHTGERSYNCDNCGKSFRHASSILNHKKLHCQRKPLKCEDCGKRLVCRSYCKDQQRDHSGENPSKCEDCGKRYKRRLNLDIILSLFLNDI
|
May be involved in transcriptional regulation.
|
Q9UK12
|
Q2JIL0
|
RL15_SYNJB
|
50S ribosomal protein L15
|
unclassified Synechococcus
|
MRLEDIRPQAGSTRRRRRLGRGVSAGQGASCGKGMRGQKARKGGSTRPGFEGGQTPLYRRLPKLKHFPRYRRRLEYTLVNLRALADLPAGSEVSLESLMERGIVTTNDGPLKILGDGEVSVPLTIRAAAITASAKVKVEAAGGRVEILGS
|
Binds to the 23S rRNA.
|
Q2JIL0
|
Q35160
|
CYB_NUMME
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Numida
|
MAPNIRKSHPLLKMINNSLIDLPTPSNISAWWNFGSLLAVCFMTQIITGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIYLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFVIAGITIIHLTFLHESGSNNPLGISSNSDKIPFHPYYSIKDILGLTLMLTPLLTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILLLIPFLHKSKQRTMTFRPFSQLLFWLLVANLLILTWVGSQPVEHPFIIIGQLASLSYFTTLLILFPMIGTLENKMLNH
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q35160
|
A9INV3
|
RRF_BORPD
|
Ribosome-releasing factor
|
Bordetella
|
MSVAEIRKSAETRMAKSLDTLKVNLSKIRTGRAHTGILDHVQVEYYGSPVPVSQVANVNLVDARTISVQPYEKPMAAAIEKAIRESDLGLNPMSLGDSIRVPMPALTEERRRDLTKVVKGEGEDAKIAVRNLRREANESLKKLVKDKEISEDDERRAQDDIQKLTDRNVTEIDKLITQKEAEIMTV
|
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.
|
A9INV3
|
A1RVM8
|
DPDH_PYRIL
|
D-proline dehydrogenase
|
Pyrobaculum
|
MKVAIVGGGIIGLFTAYHLRQQGADVVIIEQGEPGGWSKAAAGILEFTRFVINRINVRSYPKRYLSMALRGDARIKTWDWRWISAYLRAWGREPTQDMWEAIKTLGEYSWRQYRALAEAENDFAYSEEPLYEVGIDVAAALEEAKRDPLSPKVETGRCCGREALVYLDAAKLSTEDFVARMLRELQGVQMVRRRAQEVAGREVWLEGGDVVKADAVVVAAGYWARKFGIPVAPFKGYGFRTTAKAQSMFIEMTKGVAVVPLPKWTKVTGRFDLDGTEDHSPSARVLQRAREVLGNFEVLDMSVGYRPCTPDGFPIVDKVGEVVIVTGACRLGWTYGPALGKLAADLALGKPGVEALTARRFRR
|
Catalyzes the dehydrogenation of D-proline. Can also use other D-amino acids, but with lower efficiency.
|
A1RVM8
|
Q65TE9
|
TRPA_MANSM
|
Tryptophan synthase alpha chain
|
Basfia
|
MARFETLFAQLNAKKQGGFVPFVTLCDPDLERSFDIICTLVDNGADALELGFPFSDPLLDGPVIQAANNRALNAGCSTAESFKLLEKVRSKYPEIPIGLLLCANLIYAQTLDGFYRRCAEIGIDAVLVADIPLLAAEPYIQAAKKHGIQPVFICPPNADENTVKGVAEHSEGYTYLVSRAGVTSAENQSHAANLDSLVEQLKAHNAPPILQGFGIAKPQQVKEALNMGVAGAISGSATVKIIEANLDNHEKCLADLAEFVKNMKAATL
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q65TE9
|
Q01T92
|
FABZ_SOLUE
|
Beta-hydroxyacyl-ACP dehydratase
|
Candidatus Solibacter
|
MAILDINEIRAILPHRYPFLLVDRILEMETDRIVGIKNVTFNEPQFTGHFPDFPVMPGVMIVEAMAQTAGVLVLHSMPDRANKLVLLVAIENARFRKPVVPGDTLRMEMKIIKRKASVAKMAGIATVDGVVVAEAEVMCKLADKEEKPPAAPEIKVPAEAAV
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
Q01T92
|
A6L982
|
RSMG_PARD8
|
16S rRNA 7-methylguanosine methyltransferase
|
Parabacteroides
|
MIDKPINRCPMEQNTEKFSIPNSQFSILTSYFPDLTDRQKEQYAALYDLYTDWNAKINVISRKDIENLYPHHVLHSLGITDMLRFKPGSSVMDLGTGGGFPGIPLAILFPETHFHLVDSIGKKIKVGQAVAEAIGLENVSFRHCRGEEEKQLFDFVVSRAVMPLADLVKIVRKNIKKEQINALPNGLICLKGGELAHEILPFRNQAISMDLKDHFKEEFFETKKVVYVPL
|
Specifically methylates the N7 position of a guanine in 16S rRNA.
|
A6L982
|
A3N0G2
|
ISPD_ACTP2
|
MEP cytidylyltransferase
|
Actinobacillus
|
MTRKIIAVIPASGVGSRMQAGLPKQYLKLQNKTILEHTLEIFLAHPDIEKIVVAVAETDPFYPQVALLDSPKIQIVFGGETRAHSVFNALQVIEDDSWVLVHDAARPCLKRSDLDKLLQIDDKQGAILATPAIDTMKRADGNKIMRTEDRSTLWHALTPQFFPTRLLKQALISAFKKNLTVTDEASAMEFSGYQPRLIAGRSDNLKITRPEDLALAEFYLTQNTEKKI
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
A3N0G2
|
Q4FQI3
|
AROB_PSYA2
|
3-dehydroquinate synthase
|
Psychrobacter
|
MATPLFHADLTVHTQSHDYPIVITENTATENAIAEESSMASQVAPYIAGQQVLIVTNETIAPLYLKALKQPLEVQFTVQVCVLPDGEQYKNQSSINQIYDVLMAAHFNRDVTLIALGGGVIGDMTGFSAASFMRGVNFIQIPTTLLSQVDSSVGGKTGINHPQGKNMIGAFWQPQMVLADMSTLKTLPARELSAGLAEVIKYALIMDADFLTWLEHNLPAMMALNLVILGEAVKRCCEYKADIVAQDERESGVRALLNFGHTFGHVIETHEGYGNWLHGEAVAAGMVQAAELSQKIGWLTSDEVARVKRVLLLANLPITPPPIAVQTALNLMGHDKKVKHGQIRLILLKSLGEAVLTNDFDPDLLTDVLSQHAIHAKDDAQATTATVL
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q4FQI3
|
Q9GMY8
|
PEPA_SORUN
|
Pepsin A
|
Sorex
|
MKWLLLLGLVALAEGLIHKVALVKKKSLRQSLWENGLLEDFLKTHSLNPASKYFPTEATTLSANQPLVNYMDMEYFGTISIGTPPQEFTVIFDTGSSNLWVPSIYCSSPACSNHNRFDPQKSSTFKPTSQTVSIAYGTGSMTGVLGYDTVQVAGIADTNQIFGLSQSEPGSFLYYSPFDGILGLAYPSISSSGATPVFDNMWNQGLVSQDLFSVYLSSNDQSGSVVMFGGIDSSYYTGSLNWVPLSSEGYWQITVDSITMNGQSIACNGGCQAIVDTGTSLLSGPTNAIANIQSKIGASQNSQGQMAVSCSSIKNLPDIVFTINGIQYPLPASAYILQSQEGCSSGFQGMDIPTSSGELWILGDVFIRQYFTVFDRANNQVGLAPVA
|
Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
|
Q9GMY8
|
P55941
|
CRG4_XENLA
|
Gamma-crystallin IV
|
Xenopus
|
IFFYEERNFQGRCYECSSECSDLSSYFNRCNSIRVESGNWILYEQPSYRGHQYYLWKGEYPDFQRWMGFNDYIKSCRFIPHPHSQYKMRIYERGDFQGQMMEFFDDCPNTYDRFRFRDIHSCNVSDGHWMFYEEPNYKGRQYYLRPGEYRRFSDWGASSARIGSFRRVHHMV
|
Crystallins are the dominant structural components of the vertebrate eye lens.
|
P55941
|
Q8W115
|
PR1A3_ARATH
|
PRA1 family protein A3
|
Arabidopsis
|
MDWDSVAAEDVIEALREVEWSASPRSLAEFFSRFAFPRSFSKWMSRLKCNLYYYRTNYFILFVFVLGLALITRPLAILGAALTALSLAFLNDSFAATFNEKMIRTIRHFSPHLAAKMRPPHMPVIRGRSATRKTVYICGQPRLVFVLLGLTASFVLWFTSCGLLWVLYALTTALLMILLHASLRTPNLKARLNTFREEFRAVWRNYSEL
|
May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
|
Q8W115
|
B2S7K6
|
ISPG_BRUA1
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Brucella
|
MSSETVSYFSHPFPRRQSVGVSVGGVIVGGSAPVVVQSMTNTDTADVDSTVAQVAALHRAGSEIVRITVDRDESAAAVPKIRERLERLGHDVPLVGDFHYIGHKLLADHPACAEALSKYRINPGNVGFKDKKDKQFADIVEMAIRYDKPVRIGVNWGSLDQELLTALMDRNQAEGAPLSAQDVMREAIVQSALISANLAEEIGLGRDKIILSAKVSQVQDLIAVYTMLAQRSNHALHLGLTEAGMGTKGIVASSAAMGILLQQGIGDTIRISLTPEPGGDRTREVQVAQELLQTMGFRQFVPIVAACPGCGRTTSTVFQELAQTIQEDIRRNMPLWREKYPGVEALSVAVMGCIVNGPGESKHADIGISLPGTGETPSAPVFVDGKKVTTLRGPGIAEDFQKMVADYIENRFGLGRKIAS
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
B2S7K6
|
Q1LI28
|
RS7_CUPMC
|
30S ribosomal protein S7
|
Cupriavidus
|
MPRRREVPKRDILPDPKFGNVEVAKFMNVLMLDGKKSVAERIVYGAFDQIEKKAGKAPIEVFSVAINNVKPVVEVKSRRVGGANYQVPVEVRPSRRLALAMRWLREAAKKRSEKSMALRLAGELLEAAEGRGGAMKKRDEVHRMAEANKAFSHFRF
|
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. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
Q1LI28
|
Q988C9
|
4PADH_RHILO
|
4-pyridoxic acid dehydrogenase
|
Mesorhizobium
|
MPHAESYDYIIVGAGSAGCVLANRLSADPRCSVLLLEAGGWDRDPMIHIPLGWGKILTERRHDWMYFCEPEDNVGGRRVECARGKVIGGSSSTNAMAYVRGNRGDYDRWAATGLSEWSYDKVLPYFRKQESWEGGANQYRGGNGPVSTQFCRYKDTLIDAFAQASVQAGYAQTKDYNGERQEGFGRLQMTISKGRRASTASAYLRPVLKRPNLTVLTEASATRIVLEGARATGVTINHRGGERTVLARKEVLLAGGVINTPQLMMLSGIGAQDELAAHGVQTRVNLPAVGKNLQDHVSVILMYRRRAPGGPFLRNMRADRIGFDFVKTYLTGRGFSGDVPGGVVAFLKSGPARPLPDVQLLFTAAPLAAWPYFKPFKAPFADGFATRIVATQPESRGAVKLASADPSAAPLIHQNFLASPKDWESLRAGFRVARDLAAQPSMQPFIEAEFFPGPKCQSDDEIDEHIRKTSITVHHPAGTCRMGADAASVVDPQLRVRGVDRLRVVDASVMPDLVCGNINAAVIMIAEKAADLIASSKEGRAVQ
|
Involved in the degradation of pyridoxine (vitamin B(6)). Catalyzes the oxidation of 4-pyridoxic acid to 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate.
|
Q988C9
|
Q601J0
|
RS11_MESH2
|
30S ribosomal protein S11
|
Mesomycoplasma
|
MATNVKKVKKLRPKNVTVGIAHIHSSHQNTIISFTDKQGNVISWASSGSIGFKGTKKKTAYAATLATAAAAQKAREHGMREVIVELKGTGQGKEAARKQIITSGLNILLTKDVTPVPHNGTRPPRKWFKRQEKR
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
Q601J0
|
P57663
|
YFGM_BUCAI
|
Periplasmic chaperone YfgM
|
Buchnera
|
MLNISKKNIIFFILFFLIISLILFNWKYFSLVNKENLESLKYEKIIKKINKKKSKNLYEVENFIVQNTSIYGTLTALSLAKKYVECNNLDKALLQLNNSLKYTKEENLKNLLKINIAKIQIQKNENNKAMNILETIQNHNWKNIIEHMKGDIFININNKKEAIKSWKKSLFIEDSNASKEIINMKLNELKEQN
|
May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region.
|
P57663
|
B2SH29
|
MDH_FRATM
|
Malate dehydrogenase
|
Francisella
|
MARKKITLVGAGNIGGTLAHLALIKQLGDVVLFDIAQGMPNGKALDLLQTCPIEGVDFKVRGTNDYKDLENSDVVIVTAGVPRKPGMSRDDLLGINIKVMQTVGEGIKHNCPNAFVICITNPLDIMVNMLQKFSGVPDNKIVGMAGVLDSARFRTFLADELNVSVQQVQAYVMGGHGDTMVPLTKMSNVAGVSLEQLVKEGKLKQERLDAIVSRTRSGGGEIVALLKTGSAYYAPAAAGIQMAESFLKDKKMILPCAAKVKAGMYGLDEDLFVGVPTEISANGVRPIEVEISDKEREQLQVSINAVKDLNKVAAEILAK
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B2SH29
|
Q88YY5
|
RPIA_LACPL
|
Phosphoriboisomerase A
|
Lactiplantibacillus
|
MNQDQLKQLVGQKAVEYIQDGMQVGLGTGSTVKFMVDALGERVKNEHLNIVGVSTSDRTAAQAKALGIPMKSVDEVDHLDLTIDGADEIADDFQGVKGGGAALLFEKIVAINSDKVMWIVDESKMVHQLGAFGLPVEVIPYGSQHVFEKMAARGYNPVFRKVNDELVRTDSNNIIIDLHIDPITDPHALAEDLIHMVGVVEHGLFLDMVNTVIVGHANGPEVIEARP
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q88YY5
|
A5IKL2
|
PFKA_THEP1
|
Phosphohexokinase
|
Thermotoga
|
MKKIAVLTSGGDAPGMNAAVRAVVRYGVRHGLEVIGVRRGYSGLIDGDFVKLEYKDVAGITEKGGTILRTSRCEEFKTEEGRELAAKQIKKHGIEGLVVIGGEGSLTGAHLLYEEHKIPVVGIPATIDNDIGLTDMCIGVDTCLNTVMDAVQKLKDTASSHERAFIVEVMGRHSGYIALMAGLVTGAEAIIVPEIPVDYSQLADRILEERRRGKINSIIIVAEGAASAYTVARHLEYRIGYETRITILGHVQRGGSPTASDRRLALSMGVEAVDALLDGEVDVMIALQGNKLVRVPIMEALSTKKTIDKKLYEIAYMLS
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
A5IKL2
|
Q4FQU7
|
MDH_PSYA2
|
Malate dehydrogenase
|
Psychrobacter
|
MSMKQPVRVAVTGAAGNISYAMLFRIASGEMLGKDQPVILQLLEIAPALDALKGVVMELEDCAFPLLAGIVQTDDATVAFKDVDYALLVGSRPRGPGMERKDLLEANAAIFSAQGKALNDVASRDVKVLVVGNPANTNALIAQRNAPDLDPRNFTAMTRLDHNRAMAQLAGKTDSTVNDVKKMIIWGNHSSTQYPDLTASTVNGKLALDLVDRTWYEGTYIPEVQQRGAAIIKARGASSAASAANAAIAHMRTWVLGTDENDWVSMGVYSNGEYGIAKGLIYSFPCTCTNGDWSIVDGVDVSSAFSKEKMAATEQELSEERDAVAHLLP
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
Q4FQU7
|
Q6GHG4
|
TRUB_STAAR
|
tRNA-uridine isomerase
|
Staphylococcus
|
MYNGILPVYKERGLTSHDVVFKLRKILKTKKIGHTGTLDPEVAGVLPVCIGNATRVSDYVMDMGKAYEATVSIGRSTTTEDQTGDTLEMKGVHSANFNNDDIDRLLESFKGIIEQIPPMYSSVKVNGKKLYEYARNNETVERPKRKVNIKDIGRISELDFKENECHFKIRVICGKGTYIRTLATDIGVKLGFPAHMSKLTRIESGGFVLKDSLTLEQIKELHEQDSLQNKLFPLEYGLKGLPSIKIKDSHIKKRILNGQKFNKNEFDNKIKDQIVFIDDDSEKVLAIYMVHPTKESEIKPKKVFN
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q6GHG4
|
A2BZD8
|
CBID_PROM1
|
Cobalt-precorrin-6A synthase
|
Prochlorococcus
|
MNQFTLPVWVVAAAKSATNILIGNKFRDKERIDLPNKEESISVPISSSALLDNGKRSLAVSHCQSGLPLDITRGVEIWAYIQLSKGSSQSKGKVQNGFPDWLDFHAGCGVGKFQSSGQPCISQFARDLLCINLYPLVPKGNSIKVEIILPEGKDRASKTSNEAFGVVDGLSLIGTQAEVQISASPDQLKNCKEILYHKCSEAKFDGCLTFVIGENGMDLAMKYGLPANQIIKTGNWLGPLLVAAAENGVKKLLLFGYHGKLIKLSGGVFHTHHHLADGRIEILTSLAFREGISFDLIELISKSTSVENALLTLEVSNPDAVSLIWSRMAKEIEIKSRSYVNRYLSSSMEIGSVLFDRKRQMRWAGLEGLKQINSLGLILKR
|
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
|
A2BZD8
|
Q5PC27
|
SLMA_SALPA
|
Nucleoid occlusion factor SlmA
|
Salmonella
|
MAEKQTAKRNRREEILQSLALMLESSDGSQRITTAKLAASVGVSEAALYRHFPSKTRMFDSLIEFIEDSLITRINLILKDEKDTSTRLRLIVLLILGFGERNPGLTRILTGHALMFEQDRLQGRINQLFERIEAQLRQVLREKRMREGEGYTTDENLLASQLLAFCEGMLSRFVRSEFKYRPTDDFDARWPLIAAQLQ
|
Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.
|
Q5PC27
|
Q28TJ9
|
ATPD_JANSC
|
F-type ATPase subunit delta
|
unclassified Jannaschia
|
MSEPASISTGIAARYATAMFELAEEAKALPALEKDVDALDAALSESADLRDLIHSPIYGRDEASAAIGGVADAMKLQDMTGNTLRLMASKRRLFVLPALLSELRERIADHKGEVTAEVTSAKALTKTQLDKLTKSLKAQVGKTVTVKETVDENIIGGLIVKIGSKMIDTSVRSKLNALQNTMKEVG
|
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.
|
Q28TJ9
|
A8ZV63
|
RS3_DESOH
|
30S ribosomal protein S3
|
Desulfosudis
|
MGQKVNPEGLRLGIVKTWQSRWYADKEYADFILEDFKLREFVKKKLHHAGIAKVEIERSLNRIRLRIFAARPGIVIGKKGNEIEQLKNEIRQKVVAGKDLAIDIQEVKKPETVAQLVAENVAGQLERRVAFRRAMKRGVSSAMRFGVKGIKIICSGRLGGAEMARREWYREGRVPLHTLRADVDYGFVEASTTYGRIGVKVFIFKGEVLKDERKKN
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
A8ZV63
|
P9WGM4
|
NARL_MYCTO
|
Probable transcriptional regulatory protein NarL
|
Mycobacterium tuberculosis complex
|
MSNPQPEKVRVVVGDDHPLFREGVVRALSLSGSVNVVGEADDGAAALELIKAHLPDVALLDYRMPGMDGAQVAAAVRSYELPTRVLLISAHDEPAIVYQALQQGAAGFLLKDSTRTEIVKAVLDCAKGRDVVAPSLVGGLAGEIRQRAAPVAPVLSAREREVLNRIACGQSIPAIAAELYVAPSTVKTHVQRLYEKLGVSDRAAAVAEAMRQRLLD
|
Member of the two-component regulatory system NarS/NarL that regulates genes involved in aerobic nitrate metabolism. Upon phosphorylation by NarS, functions as a transcription regulator by direct binding to promoter regions of target genes together with DevR to regulate their expression during aerobic nitrate metabolism.
|
P9WGM4
|
Q5YYN2
|
LGT_NOCFA
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
|
Nocardia
|
MTLRSDVLAYIPSPPQGVWHIGPIPLRAYALCIILGIVVAIWWGERRWQQRGGREGTVLDVAMFAVPFGLIGGRAYHVATDWRKYFGEGGNPVEALYIWQGGLGIWGAVFLGGIGAWIACRIYRIPLPAFGDAIAPPILLAQAIGRLGNWFNQELYGRETTLPWGLEIYPRFDAAGDPDPMNGISNGVVEKIVHPTFLYELLWNVLVVIALVQLDKRFRIGHGRLFALYVAGYSFGRFFVELMRDDEATLVAGIRINNFTSALVFLAAIAYFVFATKGREAPERLQPGGTTRPWPWQLAALRAAGVAANGPAEPGATASTATDTDGDAKDTPPSDAAATGGQGTAAKGDRGTADAADTAKDASATDSASNSASATDSDFGETAGSSDDADRAAAVKAASGATAAEKSAADKESAAGEAAADTSAADQPAADKSGSAKSAADKSAGKSGAGRGNESESTRDNESTSAGTAASATGSAGAGATDRVDSGENDA
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
Q5YYN2
|
O14022
|
CTA5_SCHPO
|
Cation-transporting ATPase 5
|
Schizosaccharomyces
|
MDSIELKQLVPENDSEPGTPRQLLFQHYDISNEETIGIKPFKSIPAKVYILRVTEILTLGLLHLILTWLPEFRLKWIEAPCSNEDVEFVAISDPSGTSSIEKVSSICLKNDIQTSSFVLPSGKTRYFEYKKLRFYLEPLNLQWVLMPLETSAYSLVTSTPAYIQNGLDTFTIAKLRQVYGSNSLVSTKKSIVTILLNEVLHPFYLFQAVSVLIWLCDSFVFYSCCIVFISSYSIFLSVKESKESENRIHSIIGAPQPVTVIRNQVKQTVLADDLVIGDLLYFSNLDLKTCPVDGILFSSSCLLDESMVTGESVPARKFPLEDNSLDSWMIASCNIFSPHLIHAGTKFLKIDSTPSTPCLISVVRTGFRSNKGQLIRNLLYPNLRPSQLYLDSMSFLKTMAILSFVSIVFIAIYLNLYNASFGHVVLRSLDVLTILVPPALPATLSVGIANSIARLSRALIYTTSPESIHNAGCLSTFVFDKTGTLTENSVQLSCVYVKSGSNGLLKQVDADSLSLDSTKLNAHAYRVATCSQSLELVGNELVGDPLEVTLFTQFNGTFCATIRASNTPHPPLFSVSNSFDGPSQIFSIYKALEFDPVLRRMSVICSTSTERSLMLFTKGAPESILAISSQQSIPSNVQEVIHTLSSKGFRIIAFASKNLITPLQELIHLSRSTLESNVTFQGLFVLESPLRESSKDVISSLLRSKMEVSICSGDSLFTSVFVAKHCGALDSCNFIYTAELADSGDDCPQIHFEKIDLQTQNFQPIPDGFSLKDVILEKDSSLCMDGKLLQRLLTMLSFNEIKILLSKLRVLARMSPFDKATYVELCQKYGCKVGFCGDGANDCIALKQADVGVSLSDSEACAAASFVSKKKSIKDVFNVLLEGRCSLILSHRCFQYMVLCAIVQFSGVFFLYLKNYNFNDNQFLFMDLLIIFPLSAAMSYFDPAQNLTSNRPNSTLFGKGRVKDLGIQSVLIWLSHGLLTLILHELNWVELPEWQLEKSNTKNVLVTSIFLLSSLQYLGICIGINQSSEFLSPIWKKKTYVCLCTTIGLCNIYLCFANENHIISRCLQITRLPTLYRFIILFMGVISCCLTSILNM
|
Plays a role in regulating calcium and manganese homeostasis responsible for cell cycle progression.
|
O14022
|
A4IZZ4
|
ISPE_FRATW
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Francisella
|
MANIKAKKYYSYAKINLFLHILNKRTDGYHNLQTWFTFLDLKDQLTFSFNNSREINISSNISIAAKQDNLVYKAIKKFQQSYRVQDIGVDIEIKKNIPMGAGLGGGSSNAATTLIALRDYYLPQLSNEEMIPLAAKLGADVSIFVYGKSAWAEGIGEILYHKDFSPQYALLIKPDIHISTKEFFTSEDLIKSSVLISKDLGFDKSIMHNDFENVFYAKYPEFSQYLKELDSDFRMTGTGSCFYLLSADKNKLEQLARKINKPLDKWLVKTLNYVY
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A4IZZ4
|
A3QFL1
|
ACKA_SHELP
|
Acetokinase
|
Shewanella
|
MSNKLVLVLNCGSSSLKFAIIDALTGDDQISGLAECFGLEDSRIKWKVDGNKFESKLGAFTAHREAVEFIVKEILGQYPDVAAQIQAIGHRVVHGGEKFTHSVVIDDSVIAGIEDCAALAPLHNPAHLIGIRAAQASFPGLPQVAVFDTAFHQTMPERAFVYALPYKLYREHGIRRYGMHGTSHLFVSREAAKALGKELADTNVICAHLGNGASVTAVKGGKSVDTSMGLTPLEGLVMGTRCGDIDPSIIYHLVDRLGYTLDEVNNLMNKQSGLLGISELTNDCRGIEEGYAEGHKGATLALEIFCYRLAKYIASYTVPLGRLDALVFTGGIGENSDLIREKVLNLLAIFNFEVDPARNQAARFGNQGQITTDNGPVAMVIPTNEEWVIAEDAVSLLK
|
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
|
A3QFL1
|
B7GG79
|
RIMP_ANOFW
|
Ribosome maturation factor RimP
|
Anoxybacillus
|
MKKVTHIVEELVTPIVTHMGLELVDIEYVKEGKNWFLRVFIDSPTGIDIDQCGVVSEQLSEKLDEIDPIPHNYFLEVSSPGAERPLKKARDFERAVGKNVYVKTYEPIDGQKEFEGLLTAFDGQTVTVEVKVKTKKKTITIPYEKVASARLAVIFS
|
Required for maturation of 30S ribosomal subunits.
|
B7GG79
|
P07326
|
APCB_ANACY
|
Allophycocyanin beta chain
|
Anabaena
|
MQDAITSVINSSDVQGKYLDTAALEKLKGYFATGELRVRAATTISANAAAIVKEAVAKSLLYSDITRPGGNMYTTRRYAACIRDLDYYLRYSTYAMLAGDPSILDERVLNGLKETYNSLGVPVGATVQAIQAMKEVTASLVGPDAGKEMGVYFDYISSGLS
|
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
|
P07326
|
P02966
|
DESS_MYXXA
|
Spore coat protein S
|
Myxococcus
|
MANITVFYNEDFQGKQVDLPPGNYTRAQLAALGIENNTISSVKVPPGVKAILYQNDGFAGDQIEVVANAEELGPLNNNVSSIRVISVPVQPRARFFYKEQFDGKEVDLPPGQYTQAELERYGIDNNTISSVKPQGLAVVLFKNDNFSGDTLPVNSDAPTLGAMNNNTSSIRIS
|
Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.
|
P02966
|
Q4UKC3
|
DHSD_RICFE
|
Succinate dehydrogenase hydrophobic membrane anchor subunit
|
spotted fever group
|
MVYDFKAEIVKAKNSGSHHWLLQRVTGIILALCSIWLIYFTLTNKNNDINIIMWELKKPFNVVALLITVAISLYHAMLGMRVVIEDYVSCHKLRNTLIVIVQLFCIVTIAAFVVAMFYRG
|
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
|
Q4UKC3
|
A0A384KG77
|
PURNU_SHIFL
|
S-methyl-5'-thioadenosine phosphorylase YfiH
|
Shigella
|
MSKLIVPQWPLPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAVHAGWRGLCAGVLEETVSCFADKPENILAWLGPAIGPRAFEVGAEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI
|
Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
|
A0A384KG77
|
Q8WWB3
|
DYDC1_HUMAN
|
DPY30 domain-containing protein 1
|
Homo
|
MESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKENVTMEQLRQKEMAKLERERELALMEQEMMERLKAEELLLQQQQLALQLELEMQEKERQRIQELQRAQEQLGKEMRMNMENLVRNEDILHSEEATLDSGKTLAEISDRYGAPNLSRVEELDEPMFSDIALNIDQDL
|
Plays a crucial role during acrosome biogenesis.
|
Q8WWB3
|
Q21878
|
NHR1_CAEEL
|
Nuclear hormone receptor family member nhr-1
|
Caenorhabditis
|
MNGTLADQLQSHLANYGQPMVNSQRNEDPSMYMNGSAASVSHTNGSSSMGNDQKFPSYKRMAQRRKVPEGELCAVCSDLATGYHYGVASCNGCKTFFRRTIVSEQTFICQYNGNCDVNKNIRCACRHCRFNKCLLVGMDAKALQIPAIQNDRDRIGPTKKIKMSSGSDDEQATTPHRLQDQEIIDQLTQVEGLCQELRRCIIPEVTGVTHALTSPCLLFETTDLKVDVSLTNTIFKELFPASMNDIRMWNIREMRICIEWAKTFDVYQRLNLFDQFALVRNFAFAFNLLNRVFYSPDHGPDKIVFQNGAFIMRQPQQQVQLSGCRPIYTRQMDEIMIPFRKLQLSVAEFATFKAALFFNPDALDLSPQAKQEVFEERNKYLGGLFTCITQKIGIPTGVQKYGSLLMMTASIQNILAQNEENMQVMELFKNWEVDPFVKELCMKRA
|
Orphan nuclear receptor which acts in concert with the insulin/IGF-1-like signaling (IIS) pathway during osmotic stress, perhaps in response to a ligand modified by the sulfotransferase ssu-1.
|
Q21878
|
Q6UX98
|
ZDH24_HUMAN
|
Zinc finger DHHC domain-containing protein 24
|
Homo
|
MGQPWAAGSTDGAPAQLPLVLTALWAAAVGLELAYVLVLGPGPPPLGPLARALQLALAAFQLLNLLGNVGLFLRSDPSIRGVMLAGRGLGQGWAYCYQCQSQVPPRSGHCSACRVCILRRDHHCRLLGRCVGFGNYRPFLCLLLHAAGVLLHVSVLLGPALSALLRAHTPLHMAALLLLPWLMLLTGRVSLAQFALAFVTDTCVAGALLCGAGLLFHGMLLLRGQTTWEWARGQHSYDLGPCHNLQAALGPRWALVWLWPFLASPLPGDGITFQTTADVGHTAS
|
Probable palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates.
|
Q6UX98
|
O27226
|
MTRF_METTH
|
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit F
|
Methanothermobacter
|
MIILSNKPNIRGIKRVVEDIKYRNQLIGRDGRLFAGLIATRISGIAIGFLLAVLLVGVPAMMSILGVI
|
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
|
O27226
|
Q5ZKG5
|
PPAC_CHICK
|
Low molecular weight cytosolic acid phosphatase
|
Gallus
|
MAAGEVKSVLFVCLGNICRSPIAEAVFRKLVTDEKVENKWRIDSAATSTYEIGNPPDYRGQTCMKKHGITMNHIARQVTKDDFQTFDYILCMDESNLRDLKRKSNQVKDCKAKIELLGAYDPQKQLIIEDPYYGNEKDFETVYEQCVRCCKAFLEKPH
|
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
|
Q5ZKG5
|
Q606N3
|
HFQ_METCA
|
RNA-binding protein Hfq
|
Methylococcus
|
MSKGQNLQDPFLNTLRKEHVPVSIYLVNGIKLQGKVDSFDQYVIMLKNTVSQMVYKHAISTIVPGRPVRVPHAGESGDEEAE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
Q606N3
|
Q13E78
|
LEPA_RHOPS
|
Ribosomal back-translocase LepA
|
Rhodopseudomonas
|
MTTVPIDNIRNFSIVAHIDHGKSTLADRLIQITGGMSDREMAGKEQVLDSMDIERERGITIKAQTVRLNYRAKDGKDYIFNLMDTPGHVDFAYEVSRSLAACEGSLLVVDASQGVEAQTLANVYHALDAGHEIVPVLNKVDLPAAEPDKVKQQIEDVIGLDASDAVMISAKTGLGVPDVLEAIVTRLPPPKGDRGATLKALLVDSWYDVYLGVVVLVRVVDGVMKKGQRIRMMGTGAAYDVERVGFFTPKMTAVDELGPGEIGFITAAIKEVADTRVGDTITDDRKPITEMLPGFKPAIPVVFCGLFPVDADDFETLRAAMGKLRLNDASFSFEMETSAALGFGFRCGFLGLLHLEIIQERLSREFDLNLIATAPSVIYKMKLNDGSEIEIHNPVDMPDVVKIAEIEEPWIEATILTPDEYLGSVLKLCQDRRGNQKELTYVGARAMVKYDLPLNEVVFDFYDRLKSVSKGYASFDYHLTDYKPADLVKMQILVNAEPVDALSMLVHRTRAEGRGRAMVEKMKELIPPHMFVIPIQAAIGGKIIARETVRALRKDVTAKCYGGDITRKRKLLEKQKEGKKKMRQFGKVDIPQEAFIAALKVDS
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
Q13E78
|
P58071
|
ERA_CAUVC
|
GTPase Era
|
Caulobacter
|
MTDTTSKTRAGFAAIIGAPNAGKSTLVNRMVGAKVSIVTQKVQTTRFPVRGVAIEGDTQIVLVDTPGIFSPRRRLDRAMVRAAWAGSEEAEATVHLVDVQAELASRADKATPGEYRSAQDVQTIIEGLKAADRKVILALNKIDGIKRDTLLAVAKDFFDTGVYSDVFMISASTGAGVEDLTAKLVSMMPEGPWLYPEDQTADLPARLLAAEITREKVYLRVHEELPYAATVETTAFEERKDGSVRIEQTILVEREGQRVIVIGKGGQTLKWIGQASREELCDILDRKVHLFLHVKVKENWAEERGLFSDIGLDFDV
|
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
|
P58071
|
Q1J890
|
MURE_STRPF
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Streptococcus
|
MITIEQLLDILKKDHNFREVLDSDGYHYHYQGLSFERLSYDSRQVDGKTLFFAKGATFKADYLKEAITNGLQLYISEVDYELGIPVVLVTDIKKAMSLIAMAFYGNPQEKLKLLAFTGTKGKTTAAYFAYHMLKESYKPAMFSTMNTTLDGKTFFKSQLTTPESLDLFAMMAECVTNGMTHLIMEVSSQAYLVDRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFYHKRLLMENSRAVVINSGMDHFSFLADQVADQEHVFYGPLSDNQITTSQAFSFEAKGQLAGHYDIQLIGHFNQENAMAAGLACLRLGASLADIQKGIAKTRVPGRMEVLTMTNHAKVFVDYAHNGDSLEKLLSVVEEHQTGKLMLILGAPGNKGESRRADFGRVIHQHPNLTVILTADDPNFEDPEDISQEIASHIARPVEIISDREQAIQKAMSLCQEAKDAVIIAGKGADAYQIVKGQQVAYAGDLAIATHYL
|
Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
|
Q1J890
|
Q251V5
|
ISPE_DESHY
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Desulfitobacterium
|
MIRNQVEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEGGIQCSCGEWSGPENLAYRAAEAFLSGLGSSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPKINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKEELMKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAAIWRERNYHVWVTHTMERGNIYG
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
Q251V5
|
Q4QPI4
|
MSBA_HAEI8
|
Lipid A export ATP-binding/permease protein MsbA
|
Haemophilus
|
MQEQKLQENDFSTLQTFKRLWPMIKPFKAGLIASGIALVFNALADSGLIYLLKPLLDDGFGKANHSFLKIMAFVVVGMIILRGVTNFISNYCLAWVSGKVVMTMRRRLFKHLMFMPVSFFDRNSTGKLLSRITYDSEMIASSSSGSLITIVREGAYIISLLAVMFYTSWELTLVLFVIGPIIAVLITIVSKIFRKLSKNLQDSMGELTATTEQMLKGHKVVISFGGQFVEEERFNKVSNNMRRKGMKMVTADSISDPVVQIIASLALVAVLFLATTPLIAEDNLSAGSFTVVFSSMLAMMRPLKSLTNVNSQFQRGMAACQTLFAILDLEPEKDNGTYKAEPAKGALEFKNVSFAYQGKEELALNNISFSVPAGKTVALVGRSGSGKSTIANLVTRFYDIEQGEILLDGVNIQDYRLSNLRENCAVVSQQVHLFNDTIANNIAYAAQDKYSREEIIAAAKAAYALEFIEKLPQGFDTVIGENGASLSGGQRQRLAIARALLRNSPVLILDEATSALDTESERAIQSALDELKKDRTVIVIAHRLSTIENADEILVIDHGEIRERGNHKALLEQNGAYKQLYSMQFSG
|
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
|
Q4QPI4
|
Q1BRL1
|
CHED_BURCA
|
Probable chemoreceptor glutamine deamidase CheD
|
Burkholderia cepacia complex
|
MSALLIATNRYFDNHFERPGVKLLPNEFYTTAEDMVLMTVLGSCVAACLHDPYAGIGGMNHFMLPDDGADPGAAASESMRYGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIRITAEDLQGVHPRKVAFMPHSGRAMVKKLRLQVPGVTEREAALAREADRLRAARTRAQVELFAAKRPAAPQPARPRIELFGGRGTAPGAGSPSAGSPYAANLSRKQEA
|
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
|
Q1BRL1
|
P15971
|
TOG2A_AGEAP
|
Omega-agatoxin-2A
|
Agelenopsis
|
GCIEIGGDCDGYQEKSYCQCCRNNGFCS
|
Omega-agatoxin are antagonist of voltage-gated calcium channels. They block insect neuromuscular transmission presynaptically. Potent blocker of N-type calcium channels (Cav2.2/CACNA1B).
|
P15971
|
Q046K2
|
GLMU_LACGA
|
Glucosamine-1-phosphate N-acetyltransferase
|
Lactobacillus
|
MNKYVVILAAGKGTRMKSQLYKVLHKVCGKTMVEHVVNAAKGTNPDKIITVVGNGADSVKDVLAGQSDFAFQEQQLGTGDAVLAASDLLENLDGSTLVATGDTPLFTAETFNNLFKKHEESGNSATVLTAKAPNPFGYGRIIRDEDGNVLRIVEQKDGTPEELAVDEINTGVFCFDNKELFKALKQVGNDNAQGEYYLTDVLEIMRKAGHKVGAYEMPDFSESLGVNDRIALAQATKIMQRRINEEHMKNGVSFIDPDTAYIDSDVKIGNDTVIEGNVVIKGNTEIGSDCYITNSSRIVDSKIGNHVTITSSTLQEAQMDDNTDIGPNSHLRPKAVIRKGAHIGNFVEIKKAEIGENSKVGHLTYVGDATLGKDINIGCGTIFSNYDGVKKFHTNVGDHSFIGAGATIIAPVNIADHSFVAADSTITKDVARYDMAIARGRQTNKPDYWHKLPLSKDKEWE
|
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
|
Q046K2
|
A9M8R3
|
MDH_BRUC2
|
Malate dehydrogenase
|
Brucella
|
MARNKIALIGSGMIGGTLAHLAGLKELGDVVLFDIAEGTPQGKGLDIAESSPVDGFDAKFTGANDYAAIEGADVVIVTAGVPRKPGMSRDDLLGINLKVMEQVGAGIKKYAPEAFVICITNPLDAMVWALQKFSGLPAHKVVGMAGVLDSARFRYFLSEEFNVSVEDVTAFVLGGHGDSMVPLARYSTVAGIPLPDLVKMGWTSRDKLDKIIQRTRDGGAEIVGLLKTGSAFYAPAASAIQVAESYLKDKKRVLPVAAQLSGQYGVKDMYVGVPTVIGANGVERIIEIDLDKDEKAQFDKSVASVAGLCEACIGIAPSLK
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
A9M8R3
|
Q6D645
|
HMUV_PECAS
|
Hemin import ATP-binding protein HmuV
|
Pectobacterium
|
MTDSALDRTLVARHLRFQTNGRYLTDDVSLELNCGEIVAIIGPNGAGKSTLLRLLTGYLTPDDGECLLAGQPFSHWQPSALAKTRAVMRQHSGMAFAFSVQDVVAMGRSPHGRYPKNDDVVQQVMAQTGCLELATRDYRHLSGGEQQRVQLARVLAQLWHPEPTPGWLFLDEPTSALDLYHQQHLLRLLKQLTREQPLAVCCVLHDLNLAALYADRILLLHEGKLVAQGSPADVLQAETLAHWYRADLSVGSHPDYAIPQVYLRQ
|
Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
|
Q6D645
|
P59105
|
SLEB_OCEIH
|
Spore cortex-lytic enzyme
|
Oceanobacillus
|
MHQSYKAFMIILVVCSSLTMYFTQTDNTKTYAFSDQVIQQGAVGEDVIELQARLQYLGFYNGKIDGVFGWGTYWALRNFQYEFGMEIDGLAGQTTKDKLVQASNYDKEYVTEQINKGNQFTHYGGGDRNTDGQSNSGGGSGNSGEDTGGTPSVNVPQGYSQNDIQLMANAVYGEARGEPYEGQVAVAAVILNRLNSALFPDTVSGVIFEPRAFTAVADGQIWLEPNDKAREAVLDAINGWDPSGNALYYFNPDTATSGWIWTRPQIKQIGKHIFCK
|
Required for spore cortex hydrolysis during germination.
|
P59105
|
Q2RWE9
|
UBIG_RHORT
|
3-demethylubiquinone 3-O-methyltransferase
|
Rhodospirillum
|
MSATTSGTASAAELAKFSAMADAWWDPEGDFKPLHKFNPVRIAFLRDHFAAHFGRDIEAPRPFEGLSLLDIGCGGGLLCEPFARLGFAVTGIDAAERNIGTASVHAERAGLPLTYRCAMPEDLVAEGKTFDAVLTMEVVEHVADVRLFLDSVGQLCRPGGAVGAATLNRTLKSLALAKVGAEYVLRWLPRGTHDWRKFMKPSELTAGLREAGLSVDAIAGMTFDPFSGTWSQTTDVSVNYMLFATRAAA
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q2RWE9
|
P49428
|
UBCX_PICPA
|
Ubiquitin-protein ligase
|
Komagataella
|
MSAEKRLLQEYRSILKEQRQKGSASTLSSNGILDLKPVSEDNFYKWTAKLKGPTDTGYQDAFWELQIDIPSNYPTQPPKFTFIVSDDIPRNRRQRQTNQIQDDDEFEGAEKEVLRHCYRMPHPNIAFNTGEICLDILQAKWTPAWTLSSALTAIVLLLNDPEPLSPLDIDMANLMKINDLKAYNSLIEYYVGRYSIEEEVYILN
|
Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis.
|
P49428
|
F8S1H3
|
C7BL1_HELAN
|
Cytochrome P450 71BL1
|
Helianthus
|
MELFTIFSIVVSSLILFTFWSLKVPKNLPPGPPKLPIIGNIHLLDKIAPHRNLRNLARKYGPIMHLRLGQVSTVVISSPRLAHEIMKTQDLSFADRPTTTTSQIFFYKASNIAWARYGNYWRQMKKICTLELLSAKKSRSFFYIREEELTRTYKFLDFSSGTPITLRDTIQEMVNNVVSRATLGDVSEDRQFIIDSTYTMLKSFNSFNLFNYYPSLSFINVISGKQAQWLKMHKEVDVILEKILREHRSRPRGKNDHEDLVDVLIRIKETGDLDMAITDDNIKAIILEMLTAGTSSSSMTIEWAFTEMMRNPKIMKKAQTEVRSVVKGDRVTEADIQNLDYTKLVIKETLRLHGVPILVPRENQEDCVVNGYDIPAKTRLLVNAWACATDPDSWEDPDSFIPERFENNSIGYSGADFEFIPFGAGRRICPGMNFGMGTVEYVVANLLLHYDWKLPDGMKPHDIDMREITGISTLPIHPLKIVPISLSK
|
Involved in the biosynthesis of germacrene-derived sesquiterpene lactones . Hydroxylates germacrene A acid to 8-beta-hydroxy-germacrene A acid . Unlike 6-alpha-hydroxy-germacrene A acid, this compound cannot undergo spontaneous lactonization .
|
F8S1H3
|
B0JHY6
|
RL15_MICAN
|
50S ribosomal protein L15
|
Microcystis
|
MKLHEIAPQPGSTKRRRRVGRGVSAGQGASCGLGMRGQKSRSGTGTRPGFEGGQMPLYRRVPKLKHFPLVNPRQYTIVNLRKLASLPANTEVTLESLLKAKILTSNDGPLKVLGDGEITVPLKVKAAAFSNSAKEKITAAQGTWEEI
|
Binds to the 23S rRNA.
|
B0JHY6
|
Q8EZJ0
|
COAE_LEPIN
|
Dephosphocoenzyme A kinase
|
Leptospira
|
MQNSDSGKKTFLIGITGMIGGGKSTATKILEEMGCFGINADRLAKRYTEPDSPILIELVELLGSEILDEQGKPDRKKISEIVFNNPEKLSRLNQLIHPLVRKDFQKILETTAKGKMVIWEVPLLFETDAYTLCDATVTVDSDPEESILRTISRDKVKKEDVLARIKNQLPLTEKLKRADYILRNRGNIDSLREECKSLYSTLLGKML
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
Q8EZJ0
|
Q864J6
|
MSHR_MACSY
|
Melanocortin receptor 1
|
Macaca
|
MPVQGSQRRLLGSLNSTPTATPHLGLAANQTGARCLEVSVPDGLFLSLGLVSLVENVLVVTAIAKNRNLHSPMYCFICCLALSDLLVSGSNMLETAVTLLLEAGALAARAAVVQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVLCSTLFIAYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRLAHQGFGLKGAATLTILLGIFFLCWGPFFLHLTLIVLCPQHPTCSCIFKNFNLFLALIICNAIIDPLIYAFRSQELRRTLKEVLLCSW
|
Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes.
|
Q864J6
|
Q4VY51
|
SYM8_PEA
|
DMI1 protein homolog
|
Pisum
|
MAKSNEEPNSNLNTNKPPLKRTKTLAQQPSLNLRVSIAAADNGIGNSSSSSTKTDFEQQQRNYPSFLGIGSTSRKRRPPPPPKPSNITPNVKPPASDFQTKPHSEPKTSPSSSSPPSLPIAITKQQQQQHSISSPIFYLFVITCVIFVPYSAFLQYKLAKLKDMKLQLCCQIDFCSGNGKTSLQKDVVDDGSFSYYILNADSRTISLYIVLFTLVLPFILYKYIDYLPQMINFSRRTNSNKEDVPLKKRVAYMVDVFFSIYPYAKLLALLFATLFLIAFGGLALYAVTGGSMAEALWHSWTYVADAGNHAETEGMGQRIVSVSISAGGMLIFAMMLGLVSDAISEKVDSLRKGKSEVIERNHVLILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKEEMEMDIAKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEALRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGLLFKDILISFPDAIPCGVKVSADGGKIVINPDDNYVLRDGDEVLVIAEDDDTYAPGPLPEVRKGYFPRIRDPPKYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKQRERKLAAGELDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYRDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIKPAEFYLFDQEELCFYDIMIRGRTRKEIVIGYRLASQERALINPSEKSMTRKWSLDDVFVVIASGE
|
Required for both rhizobial and mycorrhizal symbiosis. Involved in Nod-factor-induced calcium spiking. May induce a change in membrane polarization that activates the opening of a calcium channel required for calcium spiking. Might be calcium gated.
|
Q4VY51
|
A7I2T7
|
MNMC_CAMHC
|
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
|
Campylobacter
|
MKFINGILFNENFKDFYSNFKNPFGESEFVFGSAVNEILKTQNRVIVAELGFGLGRNFLNIAAKFKNSDKILHFVSIEKFPLQKEILAKFYENFKFEGAKKLLKLYPTLESGFHRIKFSKNITLDLLFGDAECVLKECEFKADIWLMDGFSPSKNPDMWSDEITSQIARLCRIKAKIATYSASKKVQKSLENAGFCVVKTPGFNGKREMIRAYFNGNSGEIKDYFFERPSFKSGKNVLIIGAGIAGIVTAIKFQNLGYKTVIAEKACSVAANASGNFCGVLEPLITKKGVKLGEMHKYAFKMAVKFYKKNVPKNLAKFCGAKEFAYNDDILKRFETHDKSEIFDFNRKDLPYASIFIKNAALLRPRKICEFFSKKLNIKFGYEFSDFVESNGGYIVNFVGKKPLKCDILIFAMGSESEELFGGGKNVRANFDDAMQISSVRGQITLLRPFLKTPIPLGARGYICPKIGKRQLIGATYDRKDYENQARTFDDERNLQNVAELLNKNFVKNTDTRNLNDKKFKFEILDKNVDFNVSKQNLNFKMHTQNKELAFKNQILNVKILGSRVGFRGYSGDRFPLIGALPDCEYFKEKYKILPWQKNRAKNLPPKYLKNIYINTSHGARGLCTAILGAEILADLVTNRPFCLPKSLINELAPSRFLIRKLKKGLK
|
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
|
A7I2T7
|
P54791
|
ORC4_YEAST
|
Origin recognition complex 56 kDa subunit
|
Saccharomyces
|
MTISEARLSPQVNLLPIKRHSNEEVEETAAILKKRTIDNEKCKDSDPGFGSLQRRLLQQLYGTLPTDEKIIFTYLQDCQQEIDRIIKQSIIQKESHSVILVGPRQSYKTYLLDYELSLLQQSYKEQFITIRLNGFIHSEQTAINGIATQLEQQLQKIHGSEEKIDDTSLETISSGSLTEVFEKILLLLDSTTKTRNEDSGEVDRESITKITVVFIFDEIDTFAGPVRQTLLYNLFDMVEHSRVPVCIFGCTTKLNILEYLEKRVKSRFSQRVIYMPQIQNLDDMVDAVRNLLTVRSEISPWVSQWNETLEKELSDPRSNLNRHIRMNFETFRSLPTLKNSIIPLVATSKNFGSLCTAIKSCSFLDIYNKNQLSNNLTGRLQSLSDLELAILISAARVALRAKDGSFNFNLAYAEYEKMIKAINSRIPTVAPTTNVGTGQSTFSIDNTIKLWLKKDVKNVWENLVQLDFFTEKSAVGLRDNATAAFYASNYQFQGTMIPFDLRSYQMQIILQELRRIIPKSNMYYSWTQL
|
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
|
P54791
|
B7UN33
|
FABA_ECO27
|
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
|
Escherichia
|
MVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTANDLKVGLFQDTSAF
|
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.
|
B7UN33
|
C1DPG2
|
AMPA_AZOVD
|
Leucyl aminopeptidase
|
Azotobacter
|
MQLVVKSTSPQTLKTATLVVAVGEGRKLGATAKAIDQAADGALSAALKRGDLAGKVGQTLLLHAVPNLKAERVLLVGAGKEGELSDRQFRKIAAATYGALKGLGGSDAALTLGELQVKGRDTYGKTRLLAETLLDATYAFDRFKSEKASAPVLKKLVLLCDKAGQAEVERAASHAQAIVDGMALTRDLGNLPPNLCHPTSLASEAKALAKTYDTLKVEVLDEKKLKELGMGAFLAVAQGSDQPPRLIVLDYQGGKKDEQPFVLVGKGITFDSGGISLKPGSGMDEMKYDMCGAASVLGTFRALLELALPINVVGLLACAENMPSGGATRPGDIVTSMSGQTVEILNTDAEGRLVLCDALTYAERFKPQAVIDIATLTGACITALGTQASGLMGNDDDLIRQVLEAGEHAADRAWQLPLFEEYQEQLDSPFADMANIGGPKAGTITAACFLSRFAKNYHWAHLDIAGTAWISGGKEKGATGRPVPLLTQFLLDRSAP
|
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
|
C1DPG2
|
P29643
|
COX1_AMICA
|
Cytochrome c oxidase polypeptide I
|
Amia
|
QHLFWFFGHPEVYILILPGFGMVSHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGVKVFSWLATLHGGAIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHPTWSKIHFGVMFV
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
P29643
|
P11926
|
DCOR_HUMAN
|
Ornithine decarboxylase
|
Homo
|
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
|
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
|
P11926
|
A0KF84
|
HUTI_AERHH
|
Imidazolone-5-propionate hydrolase
|
Aeromonas
|
MNKELLNCERVWLNVTPATLRSDLADYGLLEPHALGVHEGRIHALVPMQDLKGPYPAHWQDMKGKLVTPGLIDCHTHLIFAGSRAEEFELRQKGVPYAEIARKGGGIISTVRATRAACEEQLFELALPRVKSLIREGVTTVEIKSGYGLTLEDELKMLRVARRLGEALPIRVKTTLLAAHAVPPEYRDDPDSWVETICQEIIPAAAEAGLADAVDVFCEHIGFSLAQTEQVYLAADQYGLAVKGHMDQLSNLGGSTLAANFGALSVDHLEYLDPEGIQALAHRGVVATLLPTAFYFLKETKLPPVAALRKAGVPMAVSSDINPGTAPIVSLRMAMNMACTLFGLTPVEAMAGVTRHAARALGEQEQLGQLRVGMLADFLVWNCGHPAELSYLIGVDQLVSRVINGEETLHG
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
A0KF84
|
Q081G8
|
LFTR_SHEFN
|
Phenyalanyltransferase
|
Shewanella
|
MNSLSYLNQSIGFPPPEQALTDPNGLLAIGGDLRPDRLAQAYYQGIFPWFNANDPILWWSPDPRAVFTPSHPFGSKSLIKFLKKSAWRFTINQAFLDVVAGCAGPRNTQDGTWISAEIQMAYYELHLQGHAHSIEVWDGEQLVGGLYGIPVGGIFCGESMFHRQTNASKAAFAILNQHLVKHDFQLIDAQVMNPHLVSLGAKALPRSEFLTILHQYRDRATSASMWNKQEVFIEF
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
|
Q081G8
|
P07171
|
CALB1_RAT
|
Vitamin D-dependent calcium-binding protein, avian-type
|
Rattus
|
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALILSAGDN
|
Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
|
P07171
|
Q9BTC0
|
DIDO1_HUMAN
|
Death-associated transcription factor 1
|
Homo
|
MDDKGDPSNEEAPKAIKPTSKEFRKTWGFRRTTIAKREGAGDAEADPLEPPPPQQQLGLSLRRSGRQPKRTERVEQFLTIARRRGRRSMPVSLEDSGEPTSCPATDAETASEGSVESASETRSGPQSASTAVKERPASSEKVKGGDDHDDTSDSDSDGLTLKELQNRLRRKREQEPTERPLKGIQSRLRKKRREEGPAETVGSEASDTVEGVLPSKQEPENDQGVVSQAGKDDRESKLEGKAAQDIKDEEPGDLGRPKPECEGYDPNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNCTILQVQDETHSETADQQEAKWRPGDADGTDCTSIGTIEQKSSEDQGIKGRIEKAANPSGKKKLKIFQPVIEAPGASKCIGPGCCHVAQPDSVYCSNDCILKHAAATMKFLSSGKEQKPKPKEKMKMKPEKPSLPKCGAQAGIKISSVHKRPAPEKKETTVKKAVVVPARSEALGKEAACESSTPSWASDHNYNAVKPEKTAAPSPSLLYKSTKEDRRSEEKAAAMAASKKTAPPGSAVGKQPAPRNLVPKKSSFANVAAATPAIKKPPSGFKGTIPKRPWLSATPSSGASAARQAGPAPAAATAASKKFPGSAALVGAVRKPVVPSVPMASPAPGRLGAMSAAPSQPNSQIRQNIRRSLKEILWKRVNDSDDLIMTENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISLAKLVRLKPEELVSKELSTWKERPARSVMESRTKLHNESKKTAPRQEAIPDLEDSPPVSDSEEQQESARAVPEKSTAPLLDVFSSMLKDTTSQHRAHLFDLNCKICTGQVPSAEDEPAPKKQKLSASVKKEDLKSKHDSSAPDPAPDSADEVMPEAVPEVASEPGLESASHPNVDRTYFPGPPGDGHPEPSPLEDLSPCPASCGSGVVTTVTVSGRDPRTAPSSSCTAVASAASRPDSTHMVEARQDVPKPVLTSVMVPKSILAKPSSSPDPRYLSVPPSPNISTSESRSPPEGDTTLFLSRLSTIWKGFINMQSVAKFVTKAYPVSGCFDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSAQDPVPSKLLPFEGPGLESPRPNIILGLVICQKIKRPANSGELDKMDEKRTRLQPEEADVPAYPKVATVPQSEKKPSKYPLCSADAAVSTTPPGSPPPPPPLPEPPVLKVLSSLKPAAPSPATAATTAAAASTAASSTASSASKTASPLEHILQTLFGKKKSFDPSAREPPGSTAGLPQEPKTTAEDGVPAPPLLDPIVQQFGQFSKDKALEEEEDDRPYDPEEEYDPERAFDTQLVERGRRHEVERAPEAAAAEREEVAYDPEDETILEEAKVTVDDLPNRMCADVRRNSVERPAEPVAGAATPSLVEQQKMLEELNKQIEEQKRQLEEQEEALRQQRAAVGVSMAHFSVSDALMSPPPKSSLPKAELFQQEQQSADKPASLPPASQASNHRDPRQARRLATETGEGEGEPLSRLSARGAQGALPERDASRGGLVGQAPMPVPEEKEPASSPWASGEKPPAGSEQDGWKAEPGEGTRPATVGDSSARPARRVLLPTPPCGALQPGFPLQHDGERDPFTCPGFASQDKALGSAQYEDPRNLHSAGRSSSPAGETEGDREPQARPGEGTAPLPPPGQKVGGSQPPFQGQREPGPHALGMSGLHGPNFPGPRGPAPPFPEENIASNDGPRGPPPARFGAQKGPIPSLFSGQHGPPPYGDSRGPSPSYLGGPRGVAPSQFEERKDPHGEKREFQDAPYNEVTGAPAQFEGTEQAPFLGSRGGAPFQFGGQRRPLLSQLKGPRGGPPPSQFGGQRGPPPGHFVGPRGPHPSQFETARGPHPNQFEGPRGQAPNFMPGPRGIQPQQFEDQRVHSPPRFTNQRAPAPLQFGGLRGSAPFSEKNEQTPSRFHFQGQAPQVMKPGPRPLLELPSHPPQHRKDRWEEAGPPSALSSSAPGQGPEADGQWASADFREGKGHEYRNQTFEGRQRERFDVGPKEKPLEEPDAQGRASEDRRRERERGRNWSRERDWDRPREWDRHRDKDSSRDWDRNRERSANRDREREADRGKEWDRSRERSRNRERERDRRRDRDRSRSRERDRDKARDRERGRDRKDRSKSKESARDPKPEASRASDAGTASQA
|
Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes.
|
Q9BTC0
|
Q896K4
|
VATA1_CLOTE
|
V-ATPase subunit A 1
|
Clostridium
|
MDLKTGRVVKVSGPLVVAEGMEEANLFDVVRVGDERLIGEIIEMREDKASIQVYEETSGLGPGAPVVTTGAPLSVELGPGLIEAMFDGIQRPLDAIEAKAGDFITRGIDVPSLSREKVWHFNPTKKAGDKVETGDILGLVQETSVIEHRIMVPPGIKGEIISLNEGDYTVIDKIGEIKTDKGIEDLTLMQKWPVRRGRPYKRKLNPSAPMVTGQRVVDTFFPVTKGGTACVPGPFGSGKTVVQHQLAKWADAQIVVYIGCGERGNEMTDVLNEFPELKDPKTGESLMKRTVLIANTSNMPVAAREASIYTGITIGEYFRDMGYSIALMADSTSRWAEALREMSGRLEEMPGEEGYPAYLGSRLAEFYERAGNVICLGQDGREGALTAIGAVSPPGGDLSEPVTQATLRIVKVFWGLDSQLAYRRHFPAINWLNSYSLYLDKVGPWMNENVAEDWVELRQKAMALLQEEANLQEIARLVGIDALSEEDRLKLEVAKSLREDYLQQNAFHDVDTYAPLNKQYRMLKAVLQFGDEARKALESGVYLKDILNLPVRDKIARAKYIDEKDILSIDEISKELTKDIEDLISKGGILDA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.
|
Q896K4
|
O94142
|
KO1_GIBFU
|
Cytochrome P450-4
|
Fusarium fujikuroi species complex
|
MSKSNSMNSTSHETLFQQLVLGLDRMPLMDVHWLIYVAFGAWLCSYVIHVLSSSSTVKVPVVGYRSVFEPTWLLRLRFVWEGGSIIGQGYNKFKDSIFQVRKLGTDIVIIPPNYIDEVRKLSQDKTRSVEPFINDFAGQYTRGMVFLQSDLQNRVIQQRLTPKLVSLTKVMKEELDYALTKEMPDMKNDEWVEVDISSIMVRLISRISARVFLGPEHCRNQEWLTTTAEYSESLFITGFILRVVPHILRPFIAPLLPSYRTLLRNVSSGRRVIGDIIRSQQGDGNEDILSWMRDAATGEEKQIDNIAQRMLILSLASIHTTAMTMTHAMYDLCACPEYIEPLRDEVKSVVGASGWDKTALNRFHKLDSFLKESQRFNPVFLLTFNRIYHQSMTLSDGTNIPSGTRIAVPSHAMLQDSAHVPGPTPPTEFDGFRYSKIRSDSNYAQKYLFSMTDSSNMAFGYGKYACPGRFYASNEMKLTLAILLLQFEFKLPDGKGRPRNITIDSDMIPDPRARLCVRKRSLRDE
|
Catalyzes three successive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid, a key step in gibberellin (GA) biosynthesis.
|
O94142
|
A4WS83
|
RL9_CERS5
|
50S ribosomal protein L9
|
Cereibacter
|
MQVILLQRVAKLGQMGEVVNVKDGYARNYLLPQGKALRANESNIKSFEARKAQLEAQNLETKKEAAAVAEKLDGQSFVVIRSASDAGALYGSVTTRDAADAATEAGFTVDRGQVVLDRPIKELGLHTVTVTLHPEVAVKITLNVARSPEEAELQASGKSIQELAAEAEAAADFEIAELFDEIGAASQDE
|
Binds to the 23S rRNA.
|
A4WS83
|
I1JNS6
|
GIP1_SOYBN
|
Glucanase inhibitor protein 1
|
Glycine subgen. Soja
|
MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK
|
(Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.sojae XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.sojae xyloglucanase XEG1 when hijacked by XLP1 binding.
|
I1JNS6
|
A0ZZ25
|
RPOC2_GOSBA
|
Plastid-encoded RNA polymerase subunit beta''
|
Gossypium
|
MAERANLVFHNKVIDGTAIKRLISRLIDHFGMAYTSHILDQVKALGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLILEKHHHFGNVHAVEKLRQSIEIWYATSEYLRQEMNPNFRMTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVLTSDAGYLTRRLVEVVQHIVVRRTDCGTTRGISVSPQKRTLPERIFIQTLIGRVLADDIYMGPRCIAIRNQDIGLGLVDRFRAFRTQPISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRAPFNGKIKFNEDLVHPTRTRHGHPAFLCYRDLYVIIESEDIIHKVTIPPKSFLLVQNDQYVESEQVIAEIRAGTYTLNLKERVRKHIYSDSEGEMHWSTDVYHSPEYTYSNVHLLPKTSHLWILSGGSYKFSVVPFSLHKDQDQINIHYLSAERRYISRFSVNNDQVRHNLFSSDFSDEKEERIYDYSELNRIIGTGHCDFIYSAILHENADLLAKRRRNRFIIPFQLIQDQEKELMLHSHSGISMEIPINGIFRRKGILAFFDDPRYRRKSSGITKYGTLGAHSIVKREDVIEYRGVKKVKPKYQMKVDRFFFIPEEVHILSESSSIMVRNNSIIGVDTPITLNTRSQVGGLVRVERKKKRIELKIFSGNIYFPGERDKISRHSGILIPPGTGKTNSKESKKLKNWIYVQRITPTKKKYFVLVRPVTPYEIPDGLNLATLFPQDPFQEKDNMQLRAVNYILYGNGKPTRRISDTSIQLVRTCLVLSWDQDNKSSFAEEVCASFVEVRTNGLIRDFLRIDLVKSHIFYIRKRNDPSGSELISDNRSDRTNKNPFYSIYSNARIQQSFSQNHGTIHTLLNRNKESQSLIILSASNCFRMGPFNDVKYHNVIKQSIKKDPLIPIKNLLGPLGTAPKIANFYSSFYPLITHNQTSVAKYFELDNLKQAFQVLNYYLIAENGRIYNFDPCRNIFLNAVNLNWYFPHHHYNYCEETSTIISLGQFICENVCIAKSGPRLKSGQVFIVQADSIVIRSAKPYLATPGATVHGHYGETLYEGDTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISMNLEKRIEGWNECITRILGIPWGFVIGAELTIVQSRLSLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEDGMSNVFLPGELIGLLRAERTGRALEEAICYRAVLLGITRASLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGMIPAGTGFKGLVHRSRQHNNILLETKKKNFFGGEMRDIFFHHRELFDSCFSNNLHDTSGRSFIGIEFNDS
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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A0ZZ25
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Q20616
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SKPO1_CAEEL
|
ShKT and peroxidase domain-containing protein 1
|
Caenorhabditis
|
MKSLLFSILLIYLIQLVRSEECTDKHIHCFFWSQEGECEVNPRWMKKHCQKACGTCSLTSPTPLTRQQDVPTARTFDDQQDRQFLPSRPSSIPEGCNSVMTVEAETRRIFSSGQLTARFRQQMCAEEQVAPDCSINQCFHKKYRSMDGTCNNLQNPVKGAAFTAFTRLMPAAYDDGFNTLVSASRRNRPNPREVSVFLLSSERSLPGHVNSLLMLFGQFVSHDITSNAAQNFCGCQNSGPMCASIFAPPSDRSRRCIPFTRSFPICGTGQFGRVREQLNMNTAAIDASLIYGSEAITARSLRFAAMLRTSMIGGRMFPPNTNPGSLTAGDGRAILFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGDASKTILGAYNGYNPNVEIGVLNEFAAGAYRLHGMIQETYPLVNSQFQEVNRYRFIDGVNNINHVLNNIDAIYRGMMTVPVRSPQRLTTSVTERLFGGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVPDENVRQRIGQLYRTPDDLDFYVGGILEQPAAGSLLGATFACVIGKQFERLRDGDRFYYENPGVFTSPQLAELKRTTLSWVLCQTGDNMVRVGRRAFDIENGSRAVPCSSITGLNLEAWRE
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Involved in hypodermal immune response against some types of bacterial infection. Probably utilizes H(2)O(2) produced by the NADPH oxidase bli-3. May play a role in cuticule biosynthesis.
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Q20616
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B2UFQ3
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CLPX_RALPJ
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ATP-dependent Clp protease ATP-binding subunit ClpX
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Ralstonia
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MADKKGSTGEKLLYCSFCGKSQHEVKKLIAGPSVFICDECIDLCNEIIRDEAAISEKEGGLAVKSDLPTPHEIRQSLDQYVIGQEQAKKILAVAVYNHYKRLKHLGKKDDVELSKSNILLIGPTGSGKTLLAQTLARLLNVPFVIADATTLTEAGYVGEDVENIIQKLLQNCNYEVDKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLVEGTMASVPPQGGRKHPNQDFLQVDTTNILFICGGAFDGLEKIIMQRSDKTGIGFGAEVQSKEERDVSEVLPQVEPEDLIKFGLIPELIGRLPVVATLAKLDEAALMEILVEPKNAIVKQYQKLLAMEGVELEIRPSGLTAIARKAIKRKTGARGLRSIVEHALMDVMYDLPNHKGVQKVVIDESTISDEGKPLLIYEEQPKVAGSN
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ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
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B2UFQ3
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Q71BH0
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TM2R_SOLLC
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Disease resistance protein Tm-2
|
Solanum subgen. Lycopersicon
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MAEILLTSVINKSVEIAGNLLIQEGKRLYWLKEDIDWLQREMRHIRSYVDNAKAKEAGGDSRVKNLLKDIQELAGDVEDLLDDFLPKIQQSNKFNYCLKRSSFADEFAMEIEKIKRRVVDIDRIRKTYNIIDTDNNNDDCVLLDRRRLFLHADETEIIGLDDDFNMLQAKLLNQDLHYGVVSIVGMPGLGKTTLAKKLYRLIRDQFECSGLVYVSQQPRASEILLDIAKQIGLTEQKMKENLEDNLRSLLKIKRYVFLLDDIWDVEIWDDLKLVLPECDSKVGSRIIITSRNSNVGRYIGGESSLHALQPLESEKSFELFTKKIFNFDDNNSWANASPDLVNIGRNIVGRCGGIPLAIVVTAGMLRARERTEHAWNRVLESMGHKVQDGCAKVLALSYNDLPIASRPCFLYFGLYPEDHEIRAFDLINMWIAEKFIVVNSGNRREAEDLAEDVLNDLVSRNLIQLAKRTYNGRISSCRIHDLLHSLCVDLAKESNFFHTAHDAFGDPGNVARLRRITFYSDNVMIEFFRSNPKLEKLRVLFCFAKDPSIFSHMAYFDFKLLHTLVVVMSQSFQAYVTIPSKFGNMTCLRYLRLEGNICGKLPNSIVKLTRLETIDIDRRSLIQPPSGVWESKHLRHLCYRDYGQACNSCFSISSFYPNIYSLHPNNLQTLMWIPDKFFEPRLLHRLINLRKLGILGVSNSTVKMLSIFSPVLKALEVLKLSFSSDPSEQIKLSSYPHIAKLHLNVNRTMALNSQSFPPNLIKLTLANFTVDRYILAVLKTFPKLRKLKMFICKYNEEKMDLSGEANGYSFPQLEVLHIHSPNGLSEVTCTDDVSMPKLKKLLLTGFHCRISLSERLKKLSK
|
Inhibitor of viral mouvements which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. isolates L, W3 and SL-1) and tobacco mosaic virus (TMV), but not to resistance-breaking isolates (e.g. B7, LT1, LII, Ltbl, ToMV2, and ToMV1-2) ToMV and tomato brown rugose fruit virus (ToBRFV) . Elicits a hypersensitive reaction in response to avirulent (Avr) movement proteins from resistance inducing tobamoviruses (e.g. ToMV and TMV) strains, thus leading to programmed cell death .
|
Q71BH0
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C5BPA3
|
TRPD_TERTT
|
Anthranilate phosphoribosyltransferase
|
Teredinibacter
|
MNIQQALARVVAGNDLSQDEMVEVMTAVMSGQATPAQIGGFLVALRMKSESLDEITGAAMVMRELATKVEVSANNLVDTCGTGGDGANLFNVSTAAAFVVAAAGGHVAKHGNRSVSSSTGSADVLEAAGVNLSAAPDVVARAIENVGVGFMFAPAHHSAMKHAIGPRKELALRTIFNMLGPMTNPAGVKRQVIGVFTPALCRPMAEVLGRLGSEHVMIVCSDDGLDELSIAAPSHVAELKNGVVTEFKVDPADYGFGYSDLDGLSVTSAEESLGLIRGAFKGDTTELSQKAAAIIAINAGAAIYVAGLAGSMKDGVAMAEDALSSGLAAEKLKELIEFTNV
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Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
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C5BPA3
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Q2S0I2
|
RSMA_SALRD
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Salinibacter
|
MERSHVGRDCGSRSSPRAFSVPTSNVPMKMSIPFRPKQSLGQNFLHDPNMAEKIVGTLTAPPEAHVVEVGAGTGVLTERLAERHDRLTALEIDERAVEVLRERVPEADVRETDVRETDWAALADEKGGPLRVISNTPYYLTSPILFALLGQRDCLAEAVLTMQKEVAERIVAEPSTKAYGILSVLLQLFAEPTLCFTVPPQVFSPQPDVTSAVVRIRFGPDTEPEDLHFDDARRYVRAAFNQRRKMLRNSLSAWTKEQDVGFPNDWGRKRAEALTPDEFATLARHLDAHADPVPDA
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
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Q2S0I2
|
Q91X17
|
UROM_MOUSE
|
Uromodulin, secreted form
|
Mus
|
MGIPLTWMLLVMMVTSWFTLAEASNSTEARRCSECHNNATCTVDGVVTTCSCQTGFTGDGLVCEDMDECATPWTHNCSNSSCVNTPGSFKCSCQDGFRLTPELSCTDVDECSEQGLSNCHALATCVNTEGDYLCVCPEGFTGDGWYCECSPGSCEPGLDCLPQGPDGKLVCQDPCNTYETLTEYWRSTEYGVGYSCDAGLHGWYRFTGQGGVRMAETCVPVLRCNTAAPMWLNGSHPSSSEGIVSRTACAHWSDQCCRWSTEIQVKACPGGFYIYNLTAPPECNLAYCTDPSSVEGTCEECRVDEDCISDNGRWRCQCKQDSNITDVSQLEYRLECGANDIKMSLRKCQLQSLGFMNVFMYLNDRQCSGFSESDERDWMSIVTPARNGPCGTVLRRNETHATYSNTLYLANAIIIRDIIIRMNFECSYPLDMKVSLKTSLQPMVSALNISLGGTGKFTVRMALFQSPTYTQPHQGPSVMLSTEAFLYVGTMLDGGDLSRFVLLMTNCYATPSSNSTDPVKYFIIQDSCPRTEDTTIQVTENGESSQARFSVQMFRFAGNYDLVYLHCEVYLCDSTSEQCKPTCSGTRFRSGNFIDQTRVLNLGPITRQGVQASVSKAASSNLRLLSIWLLLFPSATLIFMVQ
|
In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.
|
Q91X17
|
Q47187
|
EXPI_DICD3
|
Autoinducer synthesis protein ExpI
|
Dickeya
|
MLEIFDVSFSLMSNNKLDEVFALRKGTFKDRLDWTVNCINGMEFDEYDNEHTTYLLGVKEGKIICSVRFIEMKYPNMITGTFFSYFDGLNIPEGNYIESSRFFVDRDRVRNLIGTRNPACLTLFLAMINYARKYHYDGILTIVSHPMLTLLKRSGWRISIIQQGLSEKQEKIYLLHLPTDDESRYALIERITRITNAESEQLTTLPLLVPLA
|
Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-homoserine lactone), an autoinducer molecule which binds to ExpR and thus acts in virulence (soft rot disease) through the activation of genes for plant tissue macerating enzymes.
|
Q47187
|
A0A061FMF5
|
BTS1_THECC
|
Theobromine synthase BTS1
|
Theobroma
|
MEVKEMLFMNKGDGENSYVKTSGYTQKVAAVTQPVVYRAAQSLFTGRNSCSYQVLNVADLGCSSGPNTFTVMSTVIESTRDKCTELNWQMPEIQFYLNDLVGNDFNTLFKGLSVIQDKYKNVSCFAMGAPGSFHGRLFPQNSMHLIHSSYGVQWLSKVPKMTSEGGLSPPNKGKIYISKTSPPAVWKAYLSQFQEDFLSFLRCRSPELVPDGRMVLIIHGRKSADPTTRESCYTWEVLADAISYQVSQGLIDEEKLNSFNVPYYIPSQEEVRDLVNKEGSFLTEFVDTIEVELEGIWTGPENGAKNLRSFTEPMISHQFGEEVMDKLYDKVKDILVEDCKQEKQSTRGVSIVLELKKKESHLS
|
Involved in the biosynthesis of theobromine . Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine but not able to convert paraxanthine to caffeine .
|
A0A061FMF5
|
C5D8T9
|
Y1086_GEOSW
|
UPF0122 protein GWCH70_1086
|
unclassified Geobacillus
|
MLEKTMRMNYLYDFYQALLTPKQRSYMSLYYLDDYSLGEIAQQYEVSRQAVYDNIKRTEAMLEEYEKKLSLFQKFQKRKQLMNQLKDYVLQKYGEDKQLFDMIKELEELE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
|
C5D8T9
|
Q8S8V8
|
RR8_ATRBE
|
30S ribosomal protein S8, chloroplastic
|
Atropa
|
MGRDTIAEIITSIRNADMDRKRVVRIASTNITENIVQILLREGFIENVRKHQENNKYFLVLTLRHRRNKKRPYRNILNLKRISRPGLRIYSNYQRIPRILGGMGIVILSTSRGIMTDREARLEGIGGEILCYIW
|
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.
|
Q8S8V8
|
A2BN59
|
PFDA_HYPBU
|
GimC subunit alpha
|
Hyperthermus
|
MSQAGQSSRTITLEEALEQLSLLESQLNQLQATIREIEVRIAQLTAVEDALASLAEGAEDALIPLDGRGTVLVPASIKKLERILVHAGLNVFVEVDREKALEYLRDEKAALSKLLDAYSREYARLAQYYSALRSAIESALQAAPPQAKSQQSQQ
|
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
|
A2BN59
|
A4VRY9
|
MDCC_PSEU5
|
Malonate decarboxylase subunit delta
|
Pseudomonas
|
METLSFEFAAGQPARGKALVGVVGSGDLEVLLEPGQAGKLAIQVVTSVNGAEQRWQQLFERMFREQTPPALNIDIHDFGATPGVVRLRLEQGLEEVGHD
|
Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
|
A4VRY9
|
Q6P298
|
NUBP1_DANRE
|
Nucleotide-binding protein 1
|
Danio
|
MADVPNDAPEHCPGTSSDQAGKSSACQGCPNQSICASGATKAPDPAIEEIKQKMTSVKHKILVLSGKGGVGKSTFSAHLSHALASDSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLAVMSIGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLSGAGIDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFPPTTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSPAAAAYQSIVQKIRDYCASHSASDDSC
|
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
|
Q6P298
|
B4RW28
|
KATG_ALTMD
|
Peroxidase/catalase
|
Alteromonas
|
MNMNRFRKTTLSALVALSLGATGAIANDQISKPAGAKGTGMTKAFQPKSNQFWWPDQLDLSPLRDHDNRSNPLGEDFDYAKAFSKLDLDQVKSDINELLTTSQDWWPADFGNYGPFFIRLSWHSAGTYRTLDGRGGGDGGQMRFDPLNSWPDNGNLDKARRLLWPIKQKYGESLSWGDLMILAGTVGMENMGFDTYGFAGGRTDDWEPDMVYWGPEVEMLASDREEREGKLQRPLGATHMGLIYVNPEGPKGVPDPMGSAKNIRTAFARMAMNDEETVALIAGGHTFGKMHGAHKPADCLEAEPGGAGLEEQGLGWKNNCGKGNAEDTVTSGLEGAWTQLPTKWTSLYLQNLLGFEWKQTRSPAGAIQWVPTDESLHTSVPDAHVEGKKNPPVMTTADLALKYDPEYRKIAERFLADPKEYQTAFAKAWFKLTHRDMGPKERYLGNDIPRENFIWQDPVPKADYKTISDKDVKKLKADILDSGLTVQQLVKTAWAGASSFRASDLRGGANGARIALEPQMSWEANEPETVKAVVAKLKELQEDYNSRMFSKKKVSLADLIVIGGAAAIEKAAADAGVEVSVPVVPGRTDATQEQTDVNSFSLLEPTADAFRNYYNAEASYRSPTDMLVDKADQLNLTVPEMTVLLGGLRSLGANTGGTNHGVFTDNVGTLNNDFFVTLLDMGVKWRKTDDASVYEGVNRSTGEVMYTGTPVDLVFGSNSELRAVAEVYAYDNAKTRFVEDFVDAWTKVMTLDRFDLRHDLNAKLAK
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
B4RW28
|
Q87DY3
|
ISPF_XYLFT
|
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
|
Xylella
|
MSGLFRGRVMTGLNVRIGQGYDVHAFGPSDHVMLGGVRVPHRCGVLAHSDGDVILHALCDAMLGALGLGDIGQHFPPSDVRWKGADSGVFVRHCNLLLRERDWCVGNVDATAICESPKIAPYVNAMREGIARLLEVQPECVSVKATTSEGLGFIGRGEGLAAQVVVLLYRLNGVVV
|
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
|
Q87DY3
|
P39058
|
CEFG_ACRCH
|
Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2
|
Acremonium
|
MLPSAQVARLKPDPFPPSLSPIPHGAVTFAALAPCHNLPIFSSRQMLRDSLTYSHTSPTMSPQIANRFEASLDAQDIARISLFTLESGVILRDVPVAYKSWGRMNVSRDNCVIVCHTLTSSAHVTSWWPTLFGQGRAFDTSRYFIICLNYLGSPFGSAGPCSPDPDAEGQRPYGAKFPRTTIRDDVRIHRQVLDRLGVRQIAAVVGASMGGMHTLEWAFFGPEYVRKIVPIATSCRQSGWCAAWFETQRQCIYDDPKYLDGEYDVDDQPVRGLETARKIANLTYKSKPAMDERFHMAPGVQAGRNISSQDAKKEINGTDSGNSHRAGQPIEAVSSYLRYQAQKFAASFDANCYIAMTLKFDTHDISRGRAGSIPEALAMITQPALIICARSDGLYSFDEHVEMGRSIPNSRLCVVDTNEGHDFFVMEADKVNDAVRGFLDQSLM
|
Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.
|
P39058
|
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