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
|
|---|---|---|---|---|---|---|
D4AL88
|
MEP3_ARTBC
|
Fungalysin MEP3
|
Trichophyton
|
MHGLLLAGLLALPMNVLAHPAEQHASNVLSRRGVDIESFRLPLKAKYMDSDATAQKIQAMSFSKDDDYVSTATKLVKSTFPKSTFRVVDDHYIGTNGIGHVHFKQTAHGLDIDNSDFNVNIGRDGKVFSFGNSFFTGEIPKENPMVKRAFSDPVKALKGAVKALNLPVKSDNAKAKTAAGKESFEFMGTTGALSAPKANLVYLQKEDGSLALTWKVETDVGDNWLLTYVDAHNSETVHNVVDYVASAEYKVFAWGLNDPTEGNPTSIRDPWTDASPYTWNSDGMTKYPTTRGNNAIAQDNPTGGSTYINNYRPQSPNLIFSYPWSPTATPPSSYKDFSITQLFYTTNRYHDLLYSFGFNEAAGNFQVNNGNKGGKGNDFAIVNAQDGSGTNNANFATPPDGSPGRMRMYNWTTARPNRDGCLEAGIVIHEYTHGLSNRLCGGPANSACLNALESGGMGEGWGDFYATAIRLKPRDTKDTNYSMGAWAANNPKGIRAYLYSTNLQTNPYMYTSVNSLREVHQIGTVWASMLYDLMWALIEAHGGTYSADPVFRNGVPQDGRHLTMKLVMDGMALQPCNPNFVQARDAILDADRALTNSANKCTIWKAFAKRGLGYGAKYDARNRTGSNKLPPGC
|
Secreted metalloproteinase probably acting as a virulence factor.
|
D4AL88
|
Q2UBD9
|
PMEA_ASPOR
|
Pectin methylesterase A
|
Aspergillus subgen. Circumdati
|
MHGSLLKLALLSFSLGSSAAVLPRDTGRTSAPSGCSTVGTSGDYSTIGDALTALGSSTADACIYIAAGTYEEQLVINYAGHLTLYGETTDTQTYKQNTVTITHTISSPEAGSLDNSATVNIKSDLVSVYNINIANGYGSGAQAVALVANADQLGFYACQFTGYQDTLYAKAGHQYYINSRIEGAVDYIFGDASAWFENCDIVSNGAGYITAMSRETTSDTAWYAIDHCNIKAASGVDLTGDVYLGRPWRVLARVIYQYSVLPDIINAKGWHSMADGATPLYYEFNNTGAGSDTSDREYLSTIDAPVTKETVLGDDYKNWVDLSY
|
Involved in maceration and soft-rotting of plant tissue.
|
Q2UBD9
|
A7ZV24
|
FRDD_ECO24
|
Quinol-fumarate reductase subunit D
|
Escherichia
|
MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGIVTI
|
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones.
|
A7ZV24
|
O13692
|
GAS5_SCHPO
|
1,3-beta-glucanosyltransferase gas5
|
Schizosaccharomyces
|
MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA
|
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
|
O13692
|
Q3Z4Y7
|
EX7S_SHISS
|
Exodeoxyribonuclease VII small subunit
|
Shigella
|
MPKKNEAPASFEKALSELEQIVTRLESGDLPLEEALNEFERGVQLARQGQAKLQQAEQRVQILLSDNEDTSLPPFTPDNE
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
Q3Z4Y7
|
P45732
|
PALY_STYHU
|
Phenylalanine ammonia-lyase
|
Stylosanthes
|
MDTHANADATFCLTANNGQQPRHDPLNWAAAAEALKGSHLDEVKRMVSEYRKPLVNLGGQTLTISQVAAIAANDQGVSVQLSEASRAGVKASSDWVMDSMNNGTDSYGVTTGFGATSHRRTKQGGALQKELIRFLNAGIFGNGTETNCTLPHTATRAAMLVRINTLLQGYSGIRFEILEAITKLLNNNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPNGETLNAKEAFQAAGIGSDFFELQPKEGLALVNGTPVGSGLASVVLFEANILAVLSEVLSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYVKAAKKLHEIDPLQKPKQDRYALRTSPQWLGPLVEVIRFSTKSIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLAVASIGKLMFAQFSELVNDFYNNGLPSNLSASRNPSLDYGFKGTEIAMASYCSELQYLANPVTSHVQSAEQHNQDVNSLGLISARKTNEAVEILKLMSPTYLIALCQAIDLRHLEENLKNTVKNTVSQVAKRTLTTGVNGELHPSRFCEKDLLKIVDREYCFAYIDDPCSATYPLMQKLRQVLVEHALANAENEKNVNTSIFQKITTFEEELKTLLPKEVEGARIAYENGQSAIPNKIKECRSYPLYKFVREELGTEMLTGEKVRSPGEECDKLFTAMCQGKIIDPLLECIGEWNGAPLPLC
|
This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
|
P45732
|
A7X5G0
|
RL2_STAA1
|
50S ribosomal protein L2
|
Staphylococcus
|
MAIKKYKPITNGRRNMTSLDFAEITKTTPEKSLLKPLPKKAGRNNQGKLTVRHHGGGHKRQYRVIDFKRNKDGINAKVDSIQYDPNRSANIALVVYADGEKRYIIAPKGLEVGQIVESGAEADIKVGNALPLQNIPVGTVVHNIELKPGKGGQIARSAGASAQVLGKEGKYVLIRLRSGEVRMILSTCRATIGQVGNLQHELVNVGKAGRSRWKGIRPTVRGSVMNPNDHPHGGGEGRAPIGRPSPMSPWGKPTLGKKTRRGKKSSDKLIVRGRKKK
|
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.
|
A7X5G0
|
Q4FTV0
|
RUVC_PSYA2
|
Holliday junction resolvase RuvC
|
Psychrobacter
|
MAIIIGIDPGSRMTGYGILQQTGDKLTYIDSGTIRTDTKEMPERLKRIFNGLTRITQHHLKYADEPIYTAIEQVFMAENPDSALKLGQARGAAIAAMVALDLEVSEYTARQIKQAVCGYGAAAKEQVQDMVCRILTLDFVPQQDAADGLACAICHAHSSHSMNKLILNSAMRGRGASKKKGRWRLTEEDLGNLR
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
Q4FTV0
|
A7H651
|
RL22_CAMJD
|
50S ribosomal protein L22
|
Campylobacter
|
MSKALIKFIRLSPTKARLIAREVQGMNAELAMASLKFMPNKGAKYIANAISSAVANGGFEANEVIVKSCRVDVAAVLKRFRPRARGSASRIRKPTSHILVEVVKAEVKAEEKKTVAKKTTTTKAPAKKTTSTKKATAKKES
|
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.
|
A7H651
|
Q7WH63
|
PDXJ_BORBR
|
Pyridoxine 5'-phosphate synthase
|
Bordetella
|
MIELGVNIDHVATLRQQRHTAYPDPVQAALRAEDAGADLITLHLREDRRHIQDADVYAIRPLLRTRMNLECAVTPEMLEIACAVKPSDVCLVPEKRTELTTEGGLDVAGAQAAVTDAVQLLAEAGIRVSLFIDPDARQIEAAARAGAPVIELHTGAYAEARDDAAVQAELARVRAAVAEGLRHGLRVNAGHGLHYGNVQAVAALDGIAELNIGHAIVAQSIFDGWDKAVRDMKALMVQARLAAVRGHA
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
Q7WH63
|
Q2NVY6
|
SYI_SODGM
|
Isoleucyl-tRNA synthetase
|
Sodalis
|
MTDYKNTLNLPDTGFPMRGDLAKREPGMLERWYEQDLYGIICQARKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIIKSKGLMGYDSPYVPGWDCHGLPIELKVEQLIGKPGEKVSAAEFRTACRRYAAEQVEGQKKDFIRLGVLGDWEHPYLTMNFATEANIIRALGKIIANGHLHKGAKPVHWCIDCRSALAEAEVEYYDRTSPSIDVAFAADDVRAVAAKFGAADFAGQISLIIWTTTPWTLPANRAIAVHPDFDYQLVEVEGQGYILAADLVDSVMARAGITCWTVLGSAKGSALELLRFRHPFMGFDVPAILGQHVTLDAGTGAVHTAPGHGPDDYVIGQQYGLEVANPVGPDGCYLPGTLPALDGLQVFKANDVVINLLCDSGALLHVEKLQHSYPHCWRHKTSIIFRATPQWFVSMDQRGLRKQSLAEIKDVQWIPGWGQARIETMVANRPDWCISRQRTWGVPMALFVHNETEALHPRTIELMESVAQRVEQDGIQAWWDLDPAEILGDDAAHYHKVPDTLDVWFDSGSTHSSIVAVRPEFEGHAPDMYLEGSDQHRGWFMSSLMISTAMHGKAPYRQVLTHGFTVDGQGRKMSKSVGNVVSPQQVMDKLGADILRLWVASTDYTGEMAVSDEILKRSADAYRRIRNTARFLLANLNGFDPARHSVSPEQMVVLDRWAVGRAQAAQAEIVAAYDSYDFHNVVQRMMQFCSVEMGSFYLDIIKDRQYTTKADSIARRSCQTALYHIIEALVRWMAPIMSFTADEIWGFMPGERAQYVFTEEWYDGLFGLDAAQPLNDAYWQILLQVRSETNKVIEQARADKRIGGSLEARVTLYAEPDLAASLRELGDELYFTLLTSNAVVADYADAGDDAVQCEGLKGLKIALAKAEGEKCPRCWHYETDIGQHADHPEICGRCVTNVAGPGEERKFV
|
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
|
Q2NVY6
|
P41579
|
6PGD_SHIDY
|
6-phosphogluconate dehydrogenase, decarboxylating
|
Shigella
|
AVMGRNLALNIESRGYTVSIFNRSREKTEEVIAENPGKKLVPYYTVKEFVESLETPRRILLMVKAGAGTDAAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIGTGVSGGEEGALKGPSIMPGGQKEAYELVAPILTKIAAVAEDGEPCVTYIGADGAGHYVKMVHNGIEYGDMQLIAEAYSLLKGGLNLSNEELAQTFTEWNNGELSSYLIDITKDIFTKKDEDGNYLVDVILDEAANKGTGKWTSQSALDLGEPLSLITESVFARYISSLKDQRVAASKVLSGPQAQPAGDKAEFIEKVRRALYLGKIVSYAQGFSQLRAASEEYNWDLNYGEIAKIFRAGCIIRAQFLQKITDAYAENPQIANLLLAPYFKQIADDYQQALRDVVAYAVQNGIPVPTFAAAVAYYDSYRAAFLPANLIQAQRDYFGAHTYKRI
|
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
|
P41579
|
A1VM55
|
RS15_POLNA
|
30S ribosomal protein S15
|
Polaromonas
|
MIAKSIKAEIVKDNARSALDTGSPEVQVGLLTGRINELMPHFKTHAKDHHGRRGLLRMVSRRRKLLDYLKSKDASRYVALIAKLGLRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A1VM55
|
Q8TJA9
|
HPPA1_METAC
|
Pyrophosphate-energized inorganic pyrophosphatase
|
Methanosarcina
|
MDMLIYLAPICALIGLIFAGISYKNVQNEGAGNDLIKKITASIHGGAMVYLNRQYRAIAVFVVFLAIIIALILPNGALTAACFVFGAVLSATAGYAGMLTATIANGRTTNAATRGIGPAFRVSFASGTVMGMSVVGLGLFGLSLSFIILESVYTDLDLLTIVNIVAGFSLGASSIALFARVGGGIFTKAADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDIAGMGADLYESYVGSILATMLLAASTAATTFPNIPVENVILVPLIISAIGILASIVGTFFVRTNKTESSAIHMAFNMGLIAAIILTVIASYFVTSMLLGEYGLNVFFATVAGLVAGFLIGQITEHYTSYDRKPTLRVANSCQTGSATNIITGFAKGMESTLWPVVIISIAIYIAFQLSGLYGIAIAAVGMLATLGISLSVDAYGPVADNAGGIAEMSHQKEEVRQITDTLDAVGNTTAAIGKGFAIGSAALTALALFASYGIAVGLSAIDVMNPNVFIGLTIGAMLPYLFSSMTILAVGNAAGEVVVEVRRQFREIAGLMEGKADPDYGKCIAISTHSALKEMIPPGLLAVIAPLLVGLVLGPGALGGLLAGSVASGFMIAITMSNAGGAWDNAKKYIELGNFGGKGSDAHKAGVTGDTVGDPFKDTAGPAINILIKLMSIVAVVFAPLFM
|
Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
|
Q8TJA9
|
Q6D913
|
ACTP_PECAS
|
Acetate transporter ActP
|
Pectobacterium
|
MKIRFMMLFGLLTLPVLAWAADALTGDVQRQPLNIQAIVMFLLFVGGTLYITYWASKKTRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQNPIRSLSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHVAVVLVGILMVMYVMFGGMLATTWVQIIKAVLLLFGATFMAVMVMKSVGFSFDALFKQAMEVHPKGAAIMSPGGLVSDPISALSLGLGLMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFMGYFYFLTFIIGFGAILLVSANPEFKDATGALIGGNNMAAIHLADAVGGNFFLGFISAVAFATILAVVAGLTLAGASAVSHDLYSNVIKKGKATERDELKVSKITVLVLGVVAISLGILFENQNIAFMVGLAFSIAASCNFPIIIISMYWSKLTTRGAMIGGWAGLLTAVILMVLGPTIWVKILGHAAPIYPYDYPALFSMLVAFIGIWFFSITDRSETGQQERARFHAQFVRSQTGVGASKGSSH
|
Transports acetate.
|
Q6D913
|
A4SXQ7
|
PNP_POLAQ
|
Polynucleotide phosphorylase
|
Polynucleobacter
|
MTMFKKAVKSFQWGNHQVTMETGEIARQSGGAVIVNVDDTVVMGTVVASKSAKPGQSFFPLTVDYLEKTYAAGKIPGGFFRREGRPSEGETLISRLIDRPLRPLFPEGFLNEVQVVIHVLSINPDVPSDIPALIAASAALAISGIPFAGPVGAARVGYANGQYLLNPTRTEQATSELDLIVAGTQAAVLMVESEANQLSEEVMLGAVVYGHDQMQTAINAINELVAEAGKPEWDWTAAPKDEPFIAKVTALAEAPLREAYQIRQKGARSDKLKEITKEVMAKLQEEGDVDAVAVNDILFEIEAKIVRSQILNGEPRIDGRDTRTVRPIEIRNGVLPRTHGSALFTRGETQALVVATLGTARDEQIIDALEGEYRDRFMFHYNMPPFATGETGRVGSPKRREIGHGRLAKRALIPVLPSAEDFAYSIRVVSEITESNGSSSMASVCGGCLAMMDAGVPVKAHVAGVAMGLILDGNRFAVLTDILGDEDHLGDMDFKVAGTANGITALQMDIKVQGITKEIMQVALAQAKEGRLHILSKMQEAMGSVRTELSAHAPRMVSFKIHPDKIREVIGKGGATIQALTKETGCSIDIKDDGTVTIASTSAEGMAEAKARIEGITAEAEVGKIYEGPVVKLLEFGALVNILPGKDGLLHISEISNERVKEVKDYLAEGQVVRVKLLAADERGRLRLSLKAAMADEGGTIAPLAGAAEVVAEEAPASGESA
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A4SXQ7
|
A9NDN1
|
MNMA_COXBR
|
tRNA-specific 2-thiouridylase MnmA
|
Coxiella
|
MPNFEQNQVIAVGLSGGVDSSVAALVLKEKGYEVIGLFMQNWETDSKDPFCTAEQDLSDAKAIADHIGIPLYVVNFSKAYWNHVFQHCLDEFAQGRTPNPDVWCNREIKFKSLLDHAKKLGATHLATGHYACIQNENNEYRLLKSNDSHKDQSYFLHLLNQYQLANSVFPIGGYQKSEVRAIAKKRGFINHAKKDSTGICFIGERKFKDFLNEFLLAKPGNIETSEGKIIGKHDGIMFYTVGQRKGLHIGGRPDAGEAPWYVVDKDVKRNVLIVVQGYEHPLLYSQELTCTNLHWIRDTEPSFPLTCKAKTRCRQADQTCVVTRLDNDHCHVQFEHPQRAITRGQSVVFYLGNECLGGGIIN
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
A9NDN1
|
A8AWP5
|
LEUC_STRGC
|
Isopropylmalate isomerase
|
Streptococcus
|
MAGKSIFDKLWERHVITGQEGQPQLMYVDQHYIHEVTSPQAFQGLRDAGRKVRRPDLTFGTFDHNVPTVNIYDIRDVISKAQIDKLSENVKDFGIEHAAHGSELQGIVHMVGPETGKTQPGKFIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTIWQVKPKKMLVKFTGVPPKGVYSKDFILALIARYGVAAGVGHVVEYAGDAIEHLTMEERMTICNMSIEFGSKMGIMNPDQKTYDYVQGRPGAPKDFEAAVADWKTLVSDPDAVYDKVIEIDVSQLAPMVTWGTNPSMGVEFGAAFPEIRDMNDERAYNYMDLSPGKKAEDIDLGYIFIGSCTNARLSDLQLAAKFVAGKHIAPNLTAIVVPGSRPVKRVAEKMGLDKIFMDAGFEWRDPGCSMCLGMNPDKVPDGVHCASTSNRNFEDRQGFGAKTHLCSPAMAAAAAIAGRFVDIRQLPEVQ
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
A8AWP5
|
Q9Z9J0
|
TRUA_HALH5
|
tRNA-uridine isomerase I
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MKRIGLKVAYDGTDFAGYQIQPNERTVQGELESVLKNIHKGMSIRVTASGRTDTGVHARGQIVHFDTSLSFPVDRWPIALNSQLPADICVLEAADVPADFHARYSAKTKEYRYRVLTSAQADVFRRNYTYHVRYPLDVEAMQRAAVQLLGTHDFSSFCAAKAEVEDKVRTIEDVALWREGDELIFSIRGNGFLYNMVRIIVGTLLEIGAGKRSAEEVAKILAARSREAAGKTAPGHGLISGRSNMTNGKLENNKTTNPCVTKY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q9Z9J0
|
Q46684
|
BGLX_DICCH
|
Xylan 1,4-beta-xylosidase
|
Dickeya
|
MEKSATRQKALLIALPLLFSPLASAVQQAVLDTRGAPLITVNGLTFKDLNRDGKLNPYEDWRLPAAERAADLVSRMTLAEKAGVMMHGSAPTAGSVTGAGTQYDLNAAKTMIADRYVNSFITRLSGDNPAQMAEENNKLQQLAEATRLGIPLTISTDPRSSFQSLVGVSVSVGKFSKWPETLGLAAIGDEELVRRFADIVRQEYRAVGITEALSPQADLATEPRWPRIDGTFGEDPDLTKKMVRGYVTGMQNGKNGLNAQSVISIVKHWVGYGAAKDGWDSHNVYGKYAQFRQNNLQWHIDPFTGAFEAHAAGIMPTYSILRNASWHGKPIEQVGAGFNRFLLTDLLRGQYGFDGVILSDWLITNDCKGDCLTGVKPGEKPVPRGMPWGVEKLTPAERFVKAVNAGVDQFGGVTDSALLVQAVQDGKLTEARLDTSVNRILKQKFQTGLFERPYVNATQANDIVGRADWQQLADDTQARSLVLLQNNNLLPLRKGSRVWLHGIAANAAQEVGFIVVNTPEQADVALIRTHTPYEQPHKNFFFGSRHHEGSLAFRNDNPDYQAIVRASAKVPTLVTVYMERPAILTNVVDKTRAVVANFGVSDSVLLNRLMSGAAYTAKLPFELPSSMSAVRNQQPDLPYDSAKPLFPFGYGLPH
|
Exhibits both beta-glucosidase and beta-xylosidase activities.
|
Q46684
|
C0RF32
|
ISPG_BRUMB
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Brucella
|
MSSETVSYFSHPFPRRQSVGVSVGGVIVGGSAPVVVQSMTNTDTADVDSTVAQVAALHRAGSEIVRITVDRDESAAAVPKIRERLERLGHDVPLVGDFHYIGHKLLADHPACAEALAKYRINPGNVGFKDKKDKQFADIVEMAIRYDKPVRIGVNWGSLDQELLTTLMDRNQAEGAPLSAQDVMREAIVQSALISANLAEEIGLGRDKIILSAKVSQVQDLIAVYTMLAQRSNHALHLGLTEAGMGTKGIVASSAAMGILLQQGIGDTIRISLTPEPGGDRTREVQVAQELLQTMGFRQFVPIVAACPGCGRTTSTVFQELAQTIQEDIRRNMPLWREKYPGVEALSVAVMGCIVNGPGESKHADIGISLPGTGETPSAPVFVDGKKVTTLRGPGIAEDFQKMVADYIENRFGLGRKIAS
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
C0RF32
|
Q5L1E2
|
MTNW_GEOKA
|
RuBisCO-like protein
|
Geobacillus thermoleovorans group
|
MSAVMATYLLHDETDIRKKAEGIALGLTIGTWTDLPALEQEQLRKHKGEVVAIEELGESERVNAYFGKRLKRAIVKIAYPTVNFSADLPALLVTTFGKLSLDGEVRLLDLEFPDEWKRQFPGPRFGIDGIRDRVGVHNRPLLMSIFKGMIGRDLAYLTSELKKQALGGVDLVKDDEILFDSELLPFEKRITEGKAALQEVYEQTGKRTLYAVNLTGKTFALKDKAKRAAELGADVLLFNVFAYGLDVLQALREDEEIAVPIMAHPAFSGAVTPSEFYGVAPSLWLGKLLRLAGADFVLFPSPYGSVALEREQALGIARALTDDQEPFARAFPVPSAGIHPGLVPLIIRDFGLDTIVNAGGGIHGHPDGAIGGGRAFRAAIDAVLAGRPLRAAAAENEALQKAIDRWGVVEVEA
|
Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).
|
Q5L1E2
|
Q5YW64
|
GCS21_NOCFA
|
Gamma-glutamylcysteine synthetase 2-1
|
Nocardia
|
MDAPTVGVEEEFLLVDPRTGAPTARNEAVAHTAGELGIDLQLELTRCQVETSTAVHSDIGALFGQLRDLRCGVARCAQANESRLLAVAIPPTVPHEFPVTDTPRYRRIAESFGMIAHEQGLCGCHVHVAVPDRETAVQVSNYLRPWLPMLLALTANSAIYRGSDTGYASWRSILWRRWPSAGPPPYFRTAADYDAMVTMMLSSGIVLDEKMVYWDARPSINYPTIEVRVSDVPATVGETVLLAALVRATVHTARRFLAEGNTAPAVPAEVLRAAYWKAARSGIGGDAVAPLDGRVLPARDLLDELLETVDPALEELGDRGFVSDALTALLARGNGAQRQVRAFGADHDVAAVIAELGAATLEGCAPEPANSGGGEHVPVEGRH
|
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
|
Q5YW64
|
Q0ZB77
|
EIF3D_BOMMO
|
Eukaryotic translation initiation factor 3 subunit 7
|
Bombyx
|
MSEHVLPAEGPMRFISPIIQDNPTGWGPYEMPDQFRDMPYQPFSKGDRLGKISDWTMVQDKKYQNKYASQFGAGSSYAYFHDEDESTFHLVDTTRVQKPYQSYQRGRARGQRGRGARGARTPGGMTTLNKPRERKLGKRWGQRGAPMKIRDASVTVRPTWVTIEDMDFPRLAKLSLPGIKEGEDIVSCGTLEYYDKAYDRVNVKHEKPLQRIDRIFHTVTTTDDPVIRRLSKTAGTVYATDAILATIMCCTRSNYSWDIVIEKIGDKLFLHKRDNTEFDLLTVNETSVEPPADDGNSINSPRNLALEATFINHNFSQQVLKSGPTEPKYKFQEPNPFVSEQEDGEVASVGYRYRKWILNNGVVLIARCEHDAVMQGPQGETQFLTIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNSCKLAKWTVQALLAGSDQIKFGYVSRAQVRDNSRHVILGTQQFKPHEFAAQINLSMDNAWGILRCIIDICMKQKDGKYLIMKDPNKPLIRLYDIPDNTFESDASEESGDEQADTPFAPLYSYGNSKRV
|
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
|
Q0ZB77
|
Q8H4L3
|
CHS2_ORYSJ
|
Naregenin-chalcone synthase
|
Oryza sativa
|
MVTSTVKLEEVRRMQRAEGMAAVLAIGTATPANCVYQTDYPDYYFRVTNSEHLTNLKERFQRMCESSQIRKRYTHLTEEILQENPSMCVFTAPSLDARQDMVVAEVPKLGKAAAEEAIKEWGQPMSRITHLVFCTTNGVDMPGADYQVAKMLGLPTSVKRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEIMAMAFRGPSESHLDSLVGHALFGDGAAAVIVGSDPDEAADERPLFQIVSASQTILPGTEDAIVGHLREVGLTFHLPKDVPEFISDSVEGALTDAFMPLGVHDWNSIFWVVHPGGPAILDQVEEKVALHKARMRASRNVLSEYGNMASATVLFVLDEMRKLSADDGHATTGEGMDWGVLFGFGPGLTVETIVLHSVPITAAAPLIMQ
|
The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
|
Q8H4L3
|
A0A348G5W2
|
TX16A_ODOMO
|
Poneratoxin
|
Odontomachus
|
MRRSYVLLAFAIVLIISIISAQVEADASSDAFADAVADAVADPIKGKKIMKNMGKAMKIAGKVAKAMAPIVVPLIVSAAGK
|
Cationic amphipathic alpha-helical peptide with antimicrobial activities against E.coli (MIC=3.1), and S.aureus (MIC=3.1 uM). Also shows histamine-releasing activity (33.6% at 10 uM). Does not have activity against S.cerevisiae. Does not show hemolytic activity, even at 50 uM.
|
A0A348G5W2
|
Q2TLZ3
|
MACOI_BOVIN
|
Transmembrane protein 57
|
Bos
|
MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAAASPLSPVSPHYSSKFVETSPSGLDPNASVYQPLKK
|
Plays a role in the regulation of neuronal activity.
|
Q2TLZ3
|
Q0I591
|
TPIS_HAES1
|
Triose-phosphate isomerase
|
Histophilus
|
MARRPLVMGNWKLNGSKAFTKELITGLKDELNAVSGCDVAIAPPVMYLAEAETALVSSDIALGTQNVDLNKQGAFTGDISTEMLKDFGVKYVIIGHSERRQYHHESDEFIAKKFGVLKDAGLVPVLCIGESEAENEAGKTEEVCARQIDAVMNTLGVEAFNGAVIAYEPIWAIGTGKSATPAQAQAVHAFIRGHIAKQSQAVAERVIIQYGGSVNDANAAELFTQPDIDGALVGGASLKASAFAVIVKAAAKAKN
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q0I591
|
Q03YJ8
|
IXTPA_LEUMM
|
Nucleoside-triphosphate pyrophosphatase
|
Leuconostoc
|
MKLIIASNNAHKITEIEALLASISIDLPVVSLQEIGDVPEIVEDGTTFEENAVKKVETIAKVAPNDYILADDSGMSVDALNGEPGVYSARYAGDHDDQANIDKVLQKLAKVPNEQRTAHFNSVIALHSPKGSNLIVNGQVDGYITESERGQDGFGYDPIFFVPSMNKTFAEMSASEKNTISHRGLALQELGKKLPVWLKGE
|
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
Q03YJ8
|
Q8CX45
|
MIAB_SHEON
|
tRNA-i(6)A37 methylthiotransferase
|
Shewanella
|
MSKKLHIKTWGCQMNEYDSSKMADLLGEYQGYTLTEEAEEADILLLNTCSIREKAQEKVFHQLGRWKTLKDKNPDLIIGVGGCVASQEGKAIKDRAQCVDIIFGPQTLHRLPEMIEQVRRGEKAVIDVSFPEIEKFDRLPEPRAEGPTAFVSIMEGCSKYCSFCVVPYTRGEEVSRPSDDIILEIAQLAEQGVREVNLLGQNVNAYRGATHDGGICTFAELLRYVAAIDGIDRIRFTTSHPIEFTQDIIDVYEDTPELVSFLHLPVQSGSDRILTAMKRGHMAIEYKSIIRRLRKARPDIQISSDFIIGFPGETQEDFADTMKLIEDVAFDHSFSFIYSARPGTPAADLPDDVDMEEKKQRLAILQDRITQQAMRYSRHMMGTVQRILVEGPSVKNPMELRGRTENNRVVNFEGLPKHIGTFVDVEIVDVYTNSLRGKFIRGEDEMDLRRNLRPSDILAKHKQDDDLGVTQFKP
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
Q8CX45
|
Q6AP58
|
RS14Z_DESPS
|
30S ribosomal protein S14 type Z
|
Desulfotalea
|
MAKKSIIAKAKRKQKFAVREYNRCPLCGRPRAFIRKFGICRICFRKLASSGEVTGVTKSSW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
Q6AP58
|
Q14HI8
|
TRUA_FRAT1
|
tRNA-uridine isomerase I
|
Francisella
|
MKNYLLQIEYFGKNYCGWQRQSHSPSVQEELEKALSKIANQNIEVTCAGRTDTGVHATSQIVNFYSNADRPLSAWQRGVNALLPQDIKILAVQQVDNNFNSRFTAINRTYNYIIYNSATSSPIFAEHCLWENRELDIDKMNQACEYLLGEQDFSSFRSSQCQSNTPFRNIQKAEFIKQGSFIVFEVVGNAFLHHMIRNLVGSLLKVGLGFESPEWIKVVLEAKDRTQAAETAKAHGLYFVGVEYPEFSFKRQIIKLFC
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q14HI8
|
Q8DVT0
|
TSAD_STRMU
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Streptococcus
|
MIDRYILAIESSCDETSVAILKNEDQLLSNIIASQVESHKRFGGVVPEVASRHHVEVITLCIQDALQEAGITAGDLSAVAVTYGPGLVGALLVGMAAAKAFAWANHLPLIPVNHMAGHLMAAQSIADLQYPLLALLVSGGHTELVYVAAPGDYRIVGETRDDAVGEAYDKVGRVMGLTYPAGKEIDQLAHQGQDIYDFPRAMIKEDNLEFSFSGLKSAFINLHHNARQKGEQLRLEDLCASFQAAVLDILMVKTKKALAAYPVKTLVIAGGVAANQGLRERLKEDIKDINVVIPPLRLCGDNAGMIAYAAAVEYEKGHFAELDLNAKPSLAFEGLE
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q8DVT0
|
P70266
|
F261_MOUSE
|
Fructose-2,6-bisphosphatase
|
Mus
|
MSREMGELTQTRLQKIWIPHSSSSSLLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYRNYEFFRPDNMEAQLIRKQCALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPDIIAENIKQVKLGSPDYIDCDQEKVLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTPRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNVEAVNTHRDKPENVDITREPEEALDTVPAHY
|
Synthesis and degradation of fructose 2,6-bisphosphate.
|
P70266
|
Q42831
|
HBL_HORVU
|
Non-legume hemoglobin
|
Hordeum
|
MSAAEGAVVFSEEKEALVLKSWAIMKKDSANLGLRFFLKIFEIAPSARQMFPFLRDSDVPLETNPKLKTHAVSVFVMTCEAAAQLRKAGKITVRETTLKRLGGTHLKYGVADGHFEVTRFALLETIKEALPADMWGPEMRNAWGEAYDQLVAAIKQEMKPAE
|
May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule.
|
Q42831
|
S0ECK8
|
FUJ4_GIBF5
|
Fujikurins efflux protein FFUJ_12242
|
Fusarium fujikuroi species complex
|
MATNVGGAVDNSRRSISDNRHDPEKPAELPDTLSGSETERPQDANPEAALDQQASDAAKAHDEGPPDGGTAAWMVVLGAWCCSFCSPGWINSMGSFQEYYQREPLKDYSSSEIAWIPSLEIFFLFGLGPIVGIIFDRYGPRPLIIGGTIFHVFGLMMASLAKTYYQFLLSQGVCSAIGVACLYSPALACISTWFLKRRGAAMGIMATGSSVGGVIFPIMITRMIERNGYPWALRTAAFLILGLQVIACLTVRPRQKPVPKKLPAGRLAAPFTEPAFALLLAGIFILTYGMYIPIDYLPLSGLQEAHMSVNMSQYLVAIMNAASLFGRLGAGYGADIIGRWNMFIIACGVTGISNLAVWIPATKSSITIGYAIMFGFASGAFVSLVGALPVSVSPIPELGYRMGIVFLVISIPALTMAPIGGAILQHASNGWVSLKVFAGVMCLVGSAIILGSRMLYTEKRLIKAF
|
Efflux pump that may be involved in the secretion of fujikurins .
|
S0ECK8
|
Q8ZKP3
|
GLPK_SALTY
|
Glycerokinase
|
Salmonella
|
MTEKKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGITNQRETAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGTRIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLITIACGPSGEVNYALEGAVFMAGASIQWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTERNYRYSGWKKAVKRAMAWEEHDK
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
Q8ZKP3
|
A6LLP0
|
RS4_THEM4
|
30S ribosomal protein S4
|
Thermosipho
|
MARYTGPQCKLCRREGMKLYLKGERCFTDKCAFDRRPFAPGDHGREKKKLTQYGIQLRAKQTMKRIYGVLEAQFRRYYEKAAKKSGDTRENLVVQVERRLDNVVYRLGFAVNRTTARQLVSHGHFLVNGKKVNIPSYQVRPGDVIEVREKSKDILPIKNAIELNKDKNRMPWLSVDFENYKGVYERHPKLEEVIDLPVDVQAIIELYSR
|
With S5 and S12 plays an important role in translational accuracy.
|
A6LLP0
|
C4YJE1
|
ENOPH_CANAW
|
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
|
Candida
|
MTTTAKTDDIPIDTVILDIEGTVCPITFVKDTLFPYFIEKLPSILDKFQYPLSNTSASSDDQVLNILKQLPDNITKSSESIYKHFKNLVDQDIKDPILKSLQGLIWKQGYENNELQAPIYQDSVEFIESFPTKSSTNNKIYIYSSGSIKAQILLFGHVKSTTTTTTTTTTITNEVIDLNPKLNGYFDITTAGFKNQSNSYKKILQEINKSSTPKSVLFLSDNINEVNAAIEAGMKSYIVIRPGNPPIDDDDDGNDDKINHKIIYSLDELDL
|
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
|
C4YJE1
|
Q501I9
|
DIRC2_XENTR
|
Disrupted in renal carcinoma protein 2 homolog
|
Silurana
|
MGLEWSSPGERQPLLYPGGPRAPRVFGRRWLVLLLFSLLAFLQGLVWNSWGPIQNSARTAYNFSGLDIALLVLWGPIGFLPCFLFMWLMDNRGLRVTVLLTALLMVLGAGLRCVPVQDLAVRRKLIHGGQLLNGFAGPTVMNAAPFLSTTWFSPDERATATAIASMLSYLGGACAFLVGPLVVPAPNSTSGLLLYSGSVGAIRDRIEAVMYAEFGIIFVVFAAILAYFPSRPPVPPSVAAASRRLSYRTSILRLLSNVRFLLIVLAYAIPLGFYAGWSGVLDLILTPVHVTQVDAGWVGFWSIVGGCVVGIAVGRFADSIRGVLKPILLLLFSGAALSSTWFTLTFLSNVTHLPLTTATLYTSCILIGVFLSGTVPIFFEMFVETVYPIPEGITCGVVTFLSNLFMGVLLLFLTLYQTNLSWLNWCLTGSCFLSLLFIACFRESYDRLYLDVFVSV
|
Electrogenic metabolite transporter.
|
Q501I9
|
A8F4R4
|
RL2_PSELT
|
50S ribosomal protein L2
|
Pseudothermotoga
|
MGLRKYKPATPGVRFMIRNDFSGLTKKEPEKSLLVPLKKTGGRNHYGRITVRFRGGGHKRQYRLIDFKRDKIGIPAKVSAIEYDPNRSARIALLVYADGEKRYILAPNGLQVGDTVLSGIDAEIRVGNALPLENIPLGTLLHNVEIRPGSGGKIARSAGVSCQLMAKEGNYALLRMPSGELRKVHIKCYATIGVVGNEDHKNEVFGKAGRTRWIGRKPHVRGMVMNPVDHPMGGGEGRGKGQHPVTPWGMPTKGYKTRRGRRASDKFIVRRRNQV
|
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.
|
A8F4R4
|
B7ULH2
|
TDH_ECO27
|
L-threonine 3-dehydrogenase
|
Escherichia
|
MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLASIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMTELGMTEGFDVGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
B7ULH2
|
A9BDU5
|
PSBF_PROM4
|
PSII reaction center subunit VI
|
Prochlorococcus
|
MTNSSSPLQAVEVRTYPIFTVRWLAVHALAIPTVFFLGAIAAMQFIRR
|
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
A9BDU5
|
Q2JFH8
|
EFTU_FRACC
|
Elongation factor Tu
|
Frankia
|
MAKQKFERTKPHVNIGTIGHIDHGKTTLTAAITKVLHDAYPDLNPFTPFDQIDKAPEEKARGITISIAHVEYQTDTRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTKEHVLLARQVGVPYIVVALNKADMVDDEEILELVELEVRELLSSYEFPGDDVPVVRVSALKALEGDKEWGAKLLELMAAVDESIPEPQRDIDRPFLMPIEDVFTITGRGTVVTGRVERGIVKVNETVEIVGIKPETTSTTVTGVEMFRKLLDEGRAGDNVGLLLRGIKREDVERGQVIVKPKSITPHTVFEARVYILNKDEGGRHTPFFKNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTEMTVELIQPIAMEEGLRFAIREGGRTVGAGQVTKVLK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q2JFH8
|
B3LNU5
|
SNAPN_YEAS1
|
SNAPIN-like protein 1
|
Saccharomyces
|
MAGDSISADGTGVHPVELSVYSVLSTDLDGLYQSINELRESQALLILMLRKVRDKLRREGQVLYDPEPFKPTMDKLADLSARVRMLSQRYEELQGNARALNN
|
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex involved in endosomal cargo sorting.
|
B3LNU5
|
B8CNE2
|
RS17_SHEPW
|
30S ribosomal protein S17
|
Shewanella
|
MSDNIRTLQGRVLSNKMDKSITVAIERKVKHPLYGKFLKRTTKIHAHDEQNQCNAGDVVTIRECRPLSKTKSWTLVEVVSKA
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
B8CNE2
|
Q5L5H9
|
RL11_CHLAB
|
50S ribosomal protein L11
|
Chlamydia
|
MSNKKVIKLIKLQIPGGKANPAPPIGPALGAAGVNIMGFCKEFNAATQDRPGDLLPVVITVYSDKTFTFITKQPPVSSLIKKALNLESGSKIPNRNKVGKLTQAQVTAIAEQKMKDMDVVLLESAKRMVEGTARSMGIDVE
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
Q5L5H9
|
Q06091
|
SN309_YEAST
|
Synergistic to PRP19 mutation protein 309
|
Saccharomyces
|
MDGLSFVDKGKIPDGYKNEIDQLVKKEFANIKREPVHPEIRGILAKRKGADNSVSTLTNALYTEYLKQRNNKKRRTPDFNDDDDTLFLEEYRRKYPRIDTSRYIPNESSEVSLLGIVDSYLKHQEIVLDTLLPQTVSNQWRINNDYIRQTCTIVEEMNIQQRKQINDLEIYRKRL
|
Involved in pre-mRNA splicing by stabilizing the NTC (or PRP19-associated complex). As a component of the NTC complex, associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation.
|
Q06091
|
Q8X8H6
|
KTHY_ECO57
|
dTMP kinase
|
Escherichia
|
MRSKYIVIEGLEGAGKTTARNVVVETLEQLGIRDMVFTREPGGTQLAEKLRSLVLDIKSVGDEIITDKAEVLMFYAARVQLVETVIKPALANGTWVIGDRHDLSTQAYQGGGRGIDQHMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDKSIHTIDATQPLEAVMDAIRTTVTRWVKELDA
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
Q8X8H6
|
Q6LPL4
|
MUKE_PHOPR
|
Chromosome partition protein MukE
|
Photobacterium
|
MPEKLAKAIANPLFPALDNALRSGRHVSSEDLDNHALLIEFERELGMFYRRYNTELIRAPEGFFYLRPRSTSLIGRSVLSEIDMLVGKVLCFLYLSPERLAHEGIFTNQELFDELLVLADEKKLMKFVTHRASGSDLDREKLYDKVKTSLRRLRRIGMLIPIGENGKFRISESVFRFGADVRTGDDVREAQLRLIRDGEAVVHQQEPSQSSLLDGFDADDTGHHDSELTMQEGEV
|
Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF.
|
Q6LPL4
|
Q318T8
|
ATPF2_PROM9
|
F-type ATPase subunit b'
|
Prochlorococcus
|
MLAFNFFGATEGGLFDINATLPLMAIQVVALTYILNSLFFKPVGNVVEKREKFVSNNIIEAKNKLSEVKKLEAELLTQLQSARTEAQRIVGEAENESDKLYKEALELANNEANASKEKARLEIESQTSAARDQLSKQADDLSELIVNRLILEK
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
|
Q318T8
|
Q87KN5
|
STHA_VIBPA
|
NAD(P)(+) transhydrogenase [B-specific]
|
Vibrio
|
MAHVNHYDVIVIGSGPGGEGAAMGLTKAGLNVAIVEKESSVGGGCTHWGTIPSKALRHAVSRIIEFNSNPLFCRNNTSLHATFSDILGHAKTVIDKQTRLRQGFYDRNDCTLLFGTARFIDTHSIAVMQNDGTEETYSADKFVIATGSRPYRPSDVDFLHERIYDSDSILSLKHDPRHIIIYGAGVIGCEYASIFRGLGVKTDLINTRDRLLEFLDNEVSDALSYHFWNSGVVIRNDETYEKIEGTEDGVIIHLQSGKKMRADCLLYANGRTGNTDKLSLDVVGLESDSRGQLKVNRNYQTAVEHIYAVGDVIGYPSLASAAYDQGRFVAQAITKGQAENYLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRSSFKHLARAQIAGKDVGSLKILFHRETKEILGIHCFGERAAEIIHIGQAIMEQKGQANTIEYFVNTTFNYPTMAEAYRVAALNGLNRLF
|
Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
|
Q87KN5
|
Q08692
|
OSW1_YEAST
|
Outer spore wall protein 1
|
Saccharomyces
|
MRAPPSPRKSKSGHFFYLYFRLCQLFSGRKLKRRWHVHKLHIHQYNTRWNLSPLSEIHIEDMINEPSGLCPGSSKKKPLLIARFPKGCQESPRVYVLQRNNLSRLKLSKRKYALRFYHNEIFGNNLKRKDGSIHKVEHQQCAETVRKIKKVTANHADVKIIFHDKNTIRSDKLGGRSNKMQTRPSVLEEDVEEEVSSVYIRFCDDHSLRVKDYHSLHRHSKKSSKEKRNNQEIGKSKLLGKLFEEETSRQNKGVEKKLDTIVIQKFQNYPIVSFSRVI
|
May be involved in a late step of spore wall assembly.
|
Q08692
|
Q9CZV8
|
FXL20_MOUSE
|
F-box/LRR-repeat protein 2-like
|
Mus
|
MRRDVNGVTKSRFEMFSNSDEAVINKKLPKELLLRIFSFLDVVTLCRCAQVSRAWNVLALDGSNWQRIDLFDFQRDIEGRVVENISKRCGGFLRKLSLRGCLGVGDNALRTFAQNCRNIEVLSLNGCTKTTDATCTSLSKFCSKLRHLDLASCTSITNMSLKALSEGCPLLEQLNISWCDQVTKDGIQALVRGCGGLKALFLKGCTQLEDEALKYIGAHCPELVTLNLQTCLQITDEGLITICRGCHKLQSLCASGCSNITDAILNALGQNCPRLRILEVARCSQLTDVGFTTLARNCHELEKMDLEECVQITDSTLIQLSIHCPRLQVLSLSHCELITDDGIRHLGNGACAHDQLEVIELDNCPLITDASLEHLKSCHSLERIELYDCQQITRAGIKRLRTHLPNIKVHAYFAPVTPPPSVGGSRQRFCRCCIIL
|
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates neural transmission by binding and ubiquitinating RIMS1, a modulator of presynaptic plasticity.
|
Q9CZV8
|
A8FYJ2
|
XNI_SHESH
|
Flap endonuclease Xni
|
Shewanella
|
MNTFLIIDGMNLVRRMHAAQPNENDVNGLDIRVGSACKKLVKYHQPTHVAVVWDGDDISWRKHLFEDYKKGRKPMPEALSNTLPALKSYLAEQGVNSIDAASEADDVIATLASKLVANGGKAIIVSTDKGFTQLSDPYIQRWDHFNQHYMTIEEREEKLGVEHSQFIDYLALAGDSGNKIPGVPGIGPKSAIELLRTFRSLANIYASLDKIGAKQAKKLEAGKQMARLSYKLVQLQTDIPLNINLSQFRLPNPNA
|
Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
|
A8FYJ2
|
O43272
|
PROD_HUMAN
|
p53-induced gene 6 protein
|
Homo
|
MALRRALPALRPCIPRFVQLSTAPASREQPAAGPAAVPGGGSATAVRPPVPAVDFGNAQEAYRSRRTWELARSLLVLRLCAWPALLARHEQLLYVSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
|
Converts proline to delta-1-pyrroline-5-carboxylate.
|
O43272
|
P60030
|
DEF1_MACMU
|
RMAD-1
|
Macaca
|
MRTLVILAAILLVALQAQAEPLQARTDEATAAQEQIPTDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRIPACLAGERRYGTCFYLGRVWAFCC
|
Has bacteriostatic activity against Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative bacterium E.coli and antifungal activity against C.neoformans. Has microbicidial activity against Gram-positive bacteria S.aureus and L.monocytogenes.
|
P60030
|
P0DTQ7
|
APOC1_MIRAN
|
Truncated apolipoprotein C-I
|
Mirounga
|
MRLFLSLPVLVVVLAMVLEGPAPTQAAPEISSTLGRIPEKLKEFGNTLEDKARAAVESIKQSDIPAKTRNWFSETFNKVKEQLKTAFS
|
Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein.
|
P0DTQ7
|
Q38W91
|
HRCA_LATSS
|
Heat-inducible transcription repressor HrcA
|
Latilactobacillus
|
MLTERQLMILKEIIRLFTESGQPVGSKKLMSELPMHVSSATIRNDMADLENVGLIEKTHSSSGRVPSMKGYRYYLDHLIQPAVLNPMDVATVQQSFGRHYHKIDEIVSQSANILSNLTSYTAITLGPEMAAIRLTGFRLVPLGNHQVMAIIVTSAGTVDNQVFTIPNAISGDELEKAIRVVNDHLIGLPLTVVSQKLKIEVPALLMQYMGSPGGFLNIFDDVLKQASQERLYVGGQSNLLNFSELTDVSQLKSIYNIINQSDDLAKLLELSPGEANSQVQVRLGNEMTNDLLKNYSLMTVNYDVGEHGQGLIALLGPTSMPYSRMIGLLDLFREELAKKLIDYYADFDDSQS
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
Q38W91
|
Q6ITC1
|
VKTH1_PSEAU
|
Kunitz-type serine protease inhibitor homolog mulgin-1
|
Pseudechis
|
MSSGGLLLLLGLLTLWEVLTPVSSKDRPRFCELPADPGPCNGLFQAFYYNPVQRTCLKFRYGGCKGNPNTFKTIEECKRTCAA
|
Serine protease inhibitor homolog that only shows inhibitory activity against MMP2.
|
Q6ITC1
|
Q88CF3
|
DAPF_PSEPK
|
PLP-independent amino acid racemase
|
Pseudomonas
|
MLLRFTKMHGLGNDFMVLDLVSQHAHIQPKHAKQWGDRHTGVGFDQLLIVEAPNNPEVDFRYRIFNADGSEVEQCGNGARCFARFVLDKRLTAKKRIRVETKSGIIVLDVQNDGQVSVDMGPPRFIPAEIPFVADAQALNYPLEVDGQLHSIAAVSMGNPHAVLRVDDVQTAPVHELGPKIENHPRFPQRVNAGFIQVIDRHRANLRVWERGAGETQACGTGACAAAVAAISQGWMDSPVSLDLPGGRLHIEWAGPGKPVMMTGPAVRVYEGQVRL
|
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
|
Q88CF3
|
A7HBP3
|
RS11_ANADF
|
30S ribosomal protein S11
|
unclassified Anaeromyxobacter
|
MTPKKGKKRVKKNIATGIVHIASTFNNTMITICDASGNVISWSSAGARGFKGSRKSTPFAAQVAAGDAAAKAMEHGLKTVSVVVKGPGAGRESALRALSAAGLKITLIRDVTPIPHNGCRPPKRRRV
|
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.
|
A7HBP3
|
Q21126
|
MEGG1_CAEEL
|
Maternal effect germ cell defective 1
|
Caenorhabditis
|
MDNRGHFSSNGNFPPQGYHRREQSQEGMRIGNHHGPFSSGNMRSIGGSAQNQQQRHWTNMLNGSNNVENSWVCFSGNTSLADDPNVLSNFSALAQQRVNHFDTIVQERDNRNASFLNGSAVGNNLNTSFSVFGNLRGGDQDHRVLSDHTGIYTGLGSTGQNAVGTGIRLAADVANGNFLEQRAPTAMGHNQSYSALNQSLAPTLLDQYNQALLDQYNQSSQMAQGRGYPAPNIAYGLQNAGFPAPQIAHRPNTQNADPQAMNMNNRLRDHTFQMPHTNAQVPMSSLPGLFNLSMNHGSGNQQFQMNQSSSGPAPQLPNLSESFQMAQGSSQVTMSSRPAHSNTSMNHSSRNQYNHVDQRPSRPAPHLPTLTKEEEAFLETPDFEQFGRQLYNYLLPGILPNGAADTFSDAPKHQLLKLAKTLKPMLYDYWRKTMQMQNRGANINIIQWIIDFNAKFAALNSSVAKASNSSDVLNQTLPTAAEVSDVAREDASTSQPSKSRSMYIRPAASLDNTLETLDENLDSSQSHAGPVPAASTKPKTPSFEKMIRYSGIKKRSTMDMDNFVRMLDEKINFSPEPSTSSDIASSVKGYMSQSFLHQQDDEAPDCTKNVHSESDLKQAEPQESDKQSDKELPSNE
|
P granule component, which acts redundantly with P granule component meg-2 to promote P granule segregation during embryogenesis, and germ cell proliferation and differentiation in larval stages . In its phosphorylated form, and together with meg-2, promotes the disassembly of zygotic P granules in the anterior cytoplasm of pre-gastrulation embryos . In its dephosphorylated form, and together with meg-2, promotes the assembly and accumulation of zygotic P granules in the posterior cytoplasm of pre-gastrulation embryos . May function with the nanos family members nos-2 and nos-3 to promote germ cell proliferation during larval development . Required for fertility .
|
Q21126
|
B2ABX7
|
CEL6A_PODAN
|
Exoglucanase CEL6A
|
Podospora anserina
|
MAKRLLLTAALAATTLAAPVIEERQNCGSVWSQCGGQGWTGATCCASGSTCVAQNQWYSQCLPGSQVTTTAQAPSSTRTTTSSSSRPTSSSISTSAVNVPTTTTSAGASVTVPPGGGASSTASYSGNPFLGVQQWANSYYSSEVHTLAIPSLTGPMATKAAAVAKVPSFQWMDRNVTVDTLFSGTLADIRAANRAGANPPYAGIFVVYDLPDRDCAAAASNGEWAIADGGAAKYKAYIDRIRHHLVQYSDIRTILVIEPDSLANMVTNMNVPKCQGAANTYKELTVYALKQLNLPNVAMYLDAGHAGWLGWPANIGPAAELFAGIYKDAGRPTSLRGLATNVANYNGWSLSSAPSYTTPNPNFDEKRFVQAFSPLLTAAGFPAHFITDTGRSGKQPTGQLEWGHWCNAIGTGFGPRPTTDTGLDIEDAFVWIKPGGECDGTSDTTAARYDHHCGFADALKPAPEAGQWFQAYFEQLLTNANPPF
|
Exoglucanase that plays an important function in biomass degradation by catalyzing the hydrolysis of the non-reducing end beta-1,4-glucosidic linkages in cellulose and cellotetraose to release cellobiose. Hydrolyzes crystalline and amorphous cellulose but is inactive on hydroxyethyl cellulose, mannan, galactomannan, xyloglucan, arabinoxylan, arabinan, xylan, and pectin.
|
B2ABX7
|
P01955
|
HBA_LOXAF
|
Hemopressin
|
Loxodonta
|
VLSDNDKTNVKATWSKVGDHASDYVAEALERMFFSFPTTKTYFPHFDLGHGSGQVKAHGKKVGEALTQAVGHLDDLPSALSALSDLHAHKLRVDPVNFKLLSHCLLVTLSSHQPTEFTPEVHASLDKFLSNVSTVLTSKYR
|
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
|
P01955
|
Q4JTL6
|
NTPP_CORJK
|
Nucleotide pyrophosphatase
|
Corynebacterium
|
MQLTLASTSPAREKVLNAAGVIPRKVSPGVDEEAAVADLVNPTPAQYVQHLATAKARAVDGELVLGGDSMLLIDGELQGKPHTREETVRRWRQQRGKRAELVTGHALFDAATGQIYEEVVATQIQFAEVSERAIEAYAATGEPLECAGAFTLEALGGWFIESIDGHPSAVIGLSLPALRRGLDYFGYDFSDLWG
|
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
Q4JTL6
|
Q4R5H5
|
RS24_MACFA
|
40S ribosomal protein S24
|
Macaca
|
MNDTVTIRTRKFMTNRLLQRKQMVIGVLHPGKATVPKTEIREKLAKMYKTTPDVIFVFGFRTHFGGGKTTGFGMIYDSLDYAKKNEPKHRLARHGLYEKKKTSRKQRKERKNRMKKVRGTAKANVGAGKKK
|
Required for processing of pre-rRNA and maturation of 40S ribosomal subunits.
|
Q4R5H5
|
Q1BYQ6
|
HGD_BURCA
|
Homogentisicase
|
Burkholderia cepacia complex
|
MTLDLSKPATAGYLSGFANEFATEALPGALPHGRNSPQRAPYGLYAEQLSGTAFTAPRGHNRRSWLYRIRPAAVHRPFEPYAGAQRLVSEFGDSADVPPTPPNQLRWDPLPMPVEPTDFVDGLVTMAGNGSAAAMNGCAIHLYAANRSMQDRFFYSADGELLIVPQQGRLFIATEFGRLDVEPFEIAVIPRGVRFAVALPDGNARGYICENFGALLRLPDLGPIGSNGLANPRDFLTPQAAYEDREGAFELIAKLNGRLWRADIGHSPLDVVAWHGNYAPYKYDLRLFNTIGSISFDHPDPSIFLVLQAQSDTPGVDTIDFVIFPPRWLAAEDTFRPPWFHRNVASEFMGLVHGAYDAKAEGFVPGGASLHNCMSGHGPDADTFEKASASDTTKPHKVDATMAFMFETRTLIRPTRYALDTAQLQADYFECWQGIKKHFNPEQR
|
Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
|
Q1BYQ6
|
Q72DX1
|
GATA_DESVH
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Desulfovibrio
|
MSALHTLSLAAIRDALARREVRAEDAVLDCLARIETTEPRIDALLHLRAEAAIEEARALDAAGPDASRPLWGVPVTVKDALTTAGTPTTAGSRILEDFVPFYDAFAVQRLREAGAIILGKNNMDEFAMGSSTENSAYKPTRNPWDTARVPGGSSGGSAASVAAGQCFASLGTDTGGSIRQPASLCGCVGLKPTYGRVSRYGLIAYGSSLDQIGPMTRTVEDAAIVMGVIAGHDKRDSTCADRPVEDFAAALASRHDLAGVRIGVPAEFWGEGLSPEVATSCRAALDAARDLGATIVDVALPHTPQSIAAYYIVASAEASSNLARYDGVRYGKRAHAPEDLMDLYVRSRSEGLGDEVQRRIMLGTYVLSSGYYDAYYRKAAQVRRRILEDYRNAFATCDVICGPVSPVTAWPLGALTADPLQMYLMDVFTLSLNLAGLPGLSLPVGLGTESGMPVGIQLLGRSFDEATLLSVGNVLSRALPPLGSPAGLR
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
Q72DX1
|
B3CMU6
|
PLSY_WOLPP
|
Lysophosphatidic acid synthase
|
unclassified Wolbachia
|
MEKYIILILSYVIGSIPFSLIIAKINGINLREVGSGNIGATNVARTGNKRLAVLALFLDSLKGFVAVYTAQQFCDNNDLYIYVSAILAVLGHMFPIWLRFNGGKGVATTLGVLIALNISIALAFVFVWLIVFFIFRYSSLASLAATAAAVIASFFFQKELFLILLTVAILIFLKHYKNIANLLQGRERKFL
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
B3CMU6
|
Q8GXW1
|
RGL2_ARATH
|
Scarecrow-like protein 19
|
Arabidopsis
|
MKRGYGETWDPPPKPLPASRSGEGPSMADKKKADDDNNNSNMDDELLAVLGYKVRSSEMAEVAQKLEQLEMVLSNDDVGSTVLNDSVHYNPSDLSNWVESMLSELNNPASSDLDTTRSCVDRSEYDLRAIPGLSAFPKEEEVFDEEASSKRIRLGSWCESSDESTRSVVLVDSQETGVRLVHALVACAEAIHQENLNLADALVKRVGTLAGSQAGAMGKVATYFAQALARRIYRDYTAETDVCAAVNPSFEEVLEMHFYESCPYLKFAHFTANQAILEAVTTARRVHVIDLGLNQGMQWPALMQALALRPGGPPSFRLTGIGPPQTENSDSLQQLGWKLAQFAQNMGVEFEFKGLAAESLSDLEPEMFETRPESETLVVNSVFELHRLLARSGSIEKLLNTVKAIKPSIVTVVEQEANHNGIVFLDRFNEALHYYSSLFDSLEDSYSLPSQDRVMSEVYLGRQILNVVAAEGSDRVERHETAAQWRIRMKSAGFDPIHLGSSAFKQASMLLSLYATGDGYRVEENDGCLMIGWQTRPLITTSAWKLA
|
Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Acts as a major GA-response repressor of seed germination, including seed thermoinhibition. Promotes the biosynthesis of abscisic acid (ABA), especially in seed coats to maintain seed dormancy. Delays flowering and adult leaf production. Also regulates the floral development, petal, stamen and anther development, by repressing the continued growth of floral organs. Its activity is probably regulated by other phytohormones such as auxin and ethylene. Involved in the regulation of seed dormancy and germination, including glucose-induced delay of seed germination . Promotes salt tolerance. Acts as a repressor of positive regulators of trichome initiation. Required during the flagellin-derived peptide flg22-mediated growth inhibition. Contributes to the susceptibility to the biotrophic pathogen P.syringae pv. tomato and to the resistance to the necrotrophic pathogens B.cinerea A.brassicicola, probably by repressing the SA-defense pathway and preventing cell death. Prevents stress-induced reactive oxygen species (ROS) accumulation (e.g. salt stress) by acting on the ROS scavenging system, and delays ROS-induced cell death, thus promoting stress tolerance.
|
Q8GXW1
|
O17486
|
THIO_ECHGR
|
Thioredoxin
|
Echinococcus granulosus group
|
MSVEAVVKQVDGDALEAAIKGDKLLVCDFFATWCGPCKSLAPKLDAMAKENEKVIFVKLDVDECQDVAEKYRVTAMPTLIVFKNGCEIGHVVGANEAGIRELIQANA
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
O17486
|
B6YSM9
|
RS8_THEON
|
30S ribosomal protein S8
|
Thermococcus
|
MTLLDPLANALSHITNSERVGKKEVYIKPASKLIGEVLRVMQENGYIGEFEFIDDGRAGIYRVQLIGKINKAGAIKPRFPVKAREYEAWEKRFLPAFEFGILIVSTSQGVMTHKEAIEKGIGGRLIAYVY
|
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.
|
B6YSM9
|
Q4K6L6
|
DSBB1_PSEF5
|
Disulfide oxidoreductase 1
|
Pseudomonas
|
MSDDRLGLGRERRFLVLLGIICLALIGGALYMQVVLGEAPCPLCILQRYALLLIALFAFIGAAMSSRRGVTVMETLVVICALAGAGVAGHHVYTQFYPSVSCGIDVLQPIVDSLPLAKIFPLGFQVDGFCSTPYPPILGLSLAQWALVAFVLTVILVPLGVVRNRKKTY
|
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
|
Q4K6L6
|
E0T5V0
|
FTSP_EDWTF
|
Cell division protein FtsP
|
Edwardsiella
|
MSLSRRRFIQASGLALCAGGLPLQARASGAQAVLPVPPLLESRRGQPLFLSLERTHWAFMGGRKVGTWGVNGVYLGPTVRVHSGDDVKLIYSNRLSESVAMEVAGLLVPGPLAGGPARQMSPGVDWSPVLPIRQAAATLWYHADTPRHMAPQVYSGLAGLWLVEDQYSKNAPLPNHYGVDDFPLILQDKRLDNFGVPEYDPPSSGGFLGDTLLVNGVQDPYVEVSRGWVRLRLLNASNARRYLLQLSDGRPFFVIASDQGLLPAPLQADTLPLAPGERREVLIDMSKGEEISITAGEAAGIMDRLRGLFEPSSMLVSTRVLTLRPTGLLPLMTDTLPARLAADPLPEGDVVNNRSIMLGSASSPGINGALWDPGRIDVQARQGTWERWTVRADTPQSFYIQGAQFLVKSVNNAPPLVEDRGWKDSVWVDGEVSLLVYFPQPSSEHFPFLFYSGTLELADRGSVGQMVVQPAQ
|
Cell division protein that is required for growth during stress conditions. May be involved in protecting or stabilizing the divisomal assembly under conditions of stress.
|
E0T5V0
|
Q9ZEE1
|
PDRP_RICPR
|
Putative pyruvate, phosphate dikinase regulatory protein
|
typhus group
|
MTKLIIHLVSDSSVQTAKHAANSALAQFTSIKQKLYHWPMIRNCELLNEVLSKIESKHGIVLYTIADQELRKTLTKFCYELKIPCISVIGKIIKEMSVFSGIEIEKEQNYNYKFDKTYFDTLNAIDYAIRHDDGQMINELSESDIILIGPSRTSKTPTSVFLAYNGLKAANIPYVYNCPFPDFIEKDIDQLVVGLVINPNRLIEIREARLNLLQINENKSYTDFNIVQRECIEVRKICNQRNWPVIDVSTRSIEETAALIMRIYYNRKNKYHK
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
|
Q9ZEE1
|
Q5JDU3
|
GLMD_THEKO
|
GlcN6P deaminase
|
Thermococcus
|
MHATLREIKRTPEGIKTAQRAFEEFVTNSDFLLPREVVYTGCGSSHFLSQPLAMATTRLGGRGVALPCSELLYSREYYPVGKPELLVSISRSGETTEAVKALESLDVPKFALTAYESTLSRKADYALIVPTHEESVVMTHSFTAFYFAFLQLLNASFGLETYDAEMTSELTREALKNEGYIREITGEFDFRNVIFLGSGILYPIALEAMLKMKEMALFWSEAYQTFEVRHGFKSVADEGTLVVLLVNEPFDWHEKLTKEFQGQGARVLTIGNGDTGADYFIDLPKVDELLTPILHLPIIQLLSYYKAIKRGLNPDQPRFLSKVVKW
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. Involved in chitin degradation.
|
Q5JDU3
|
Q97B38
|
KAD6_THEVO
|
ATP-AMP transphosphorylase
|
Thermoplasma
|
MGKIACITGPPGAGKSTVCSKLREYGYNCKEGNELAKEYGCLFDEEVDVECLEEKLAEDRFDGIICSHYSHLLGCSTVFILEADLNDLIDRMRARGYSEEKIQENIETQMSSIFYYESLERLPANRIFTLYNGNIDETAKRIISIIERSRNNK
|
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
|
Q97B38
|
Q087Q9
|
METK_SHEFN
|
Methionine adenosyltransferase
|
Shewanella
|
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEVTTSAWVDIEEITRKTVREIGYTNSDMGFDADSCAVLNAIGKQSPDINQGVDRSDPAEQGAGDQGLMFGYASNETDVLMPAPITYAHKLVKRQSEVRKDGTLPWLRPDAKSQVTFAYDDGKIIGIDAIVLSTQHREDVTQADLIEAVMETIIKPVLPAQWLNKDTKYFINPTGRFVIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCELQVSYAIGVAEPTSISIETFGTGKVSEEVLIKLVRQHFELRPYGLTAMLDLARPIYQQTAAYGHFGRDIFPWEATDKAEALRADAGL
|
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
|
Q087Q9
|
Q1K7M0
|
PFF1_NEUCR
|
FXNA-related family protease 1
|
Neurospora
|
MINPISFRPGPVTFWTTLIYLALLIPIVIINEKTPAAPKTAEPFKGVNLTEAWLDLTTITRAYHPYNSKFNEEVRRYLLEKVETILEENGASWVSDGQMTTVKDGKSAAVTVFDDNVSNSTFVMGKSNGTTFTRTDSINNAAYFEGTNILVYIRGKEDDEGEWWEADYAHGMRRNAKGLTLVNAHYDSVSTGFGATDDGMGVVTALQVLKYFTAPGHQPQRGIVVMLNNGEEDWLYGAHALGQHKLNPFIHTFLNLEGAGAGGRAIVFRATDREVMAAYARTSHPFGTVIASDAFGLGFISSGTDYSVLVDAYGQRGIDLAFFKPRARYHTNQDDTRHTSKGSLWHMLSAAIHTTKQFSGDTGNTFIGQRPDKAHGKVANGRSSNGVWFDLFGKSFVLFGLRGMFAWSLTLLIATPLVLVGITWLLRNLDKDYFFTSTVKTKEHPEYEAVPIGGWKGFFRFPFALGVAVFFTISSALLMNKVNPLIVYSSRYSVWVMMVSIFYFSFWMIMRGANFVRPSALHRGYANLWLFVFGWIVLVAVTALEDRRRIAAGYIFVFLESAIFLSCLISFVELLAVPRKSSYALQVQEDYDGQEHDHNGYQGFRDSTDEPSLRARAESSASAASPPSPTVAQEPSKSKAPAGTTNGLSTAPSVAAHSSQPQPAPTTPIPGRSSGAPSTASRDENESEDDDEPTERTPLVGGNGTNDRGRTTFATTYRRSITALVHGARKMEEDGEPYDHEQEWSGHLPSWAWFFQFLLLGPFMIILAAQTGLMLTDAVYQTGSDGSKLITPYLIIFVFTVLLILPLTPFIHRVTHHIPVFLLVVFIVTLTYNLIAFPFSANNRYKTFFGQYIDVATGDNKVCYTGIEEYVRPIIAELPSASGREVTCGKSLRRGSTISTCCFDGSAVPPKLGSEDDNGLPEDSYADLITINATRSTKRGDSSRTTARIEITADNTKSCFLQFKKPVSALAIENGSGWDDRFGQYPEDGVGLVRLWHREFGKTWVVNAEWKGSETRKEYDENDGTVICMWSDANTPGTIPALDEALQFVPSWAAVTKFSEGLVEGRKAFKIV
|
May be involved in vacuolar sorting and osmoregulation.
|
Q1K7M0
|
Q1DK03
|
MDM10_COCIM
|
Mitochondrial inheritance component MDM10
|
Coccidioides
|
MIDFMDYIQLTFSDATHWNRDNSYTALTDTANALLDFSIPERLRVHLSSLSTPQFATTYTLGTVGLIDGSISYLFSTLPLESTPSRSTLIPLRRLVPGYRQIHPPLAPESPNESRHAEPNERSEKALQSWRKETMLHATLHLPPPTTLNGLFLRRISPTTQLSLAVCSTQATPLSKSTPQASILTQLSHDTGKYSAEFLFSTDNALLGFKGLWNFGPDPRHAATAQRPRTASQSVSLLSAGGEMYYSPLSSVVGLSTGLRFTTLPAASESTHSSSSTHPAQSPISTFPYTLTLTLTPLTGSLSTTYSLLASPNLAFSSRFGFNVYSWESEMVAGCELWRRKKKRHASTLSDKDDLSWAKRKMGLLPPLPPSPVKGTSASAVTPAGEQKESDSVIKLRVDQSLNVRLLWEGRVKDLLVSAGVGLGPSLPSIGGTTYGWTGVGVSVLYST
|
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.
|
Q1DK03
|
A2C664
|
PSBU_PROM3
|
PSII-U
|
Prochlorococcus
|
MKRLLSLLTGVLVMTGLLMALIFPQSAYANVSDEKLGDRGEKVDLNNSSVRAFRQFPGMFPTIAGKIVVGGPYSSVSDASSVLDASQKSVFDKYKDNFTVTDQEIAVNEGFDRINDGQYR
|
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
|
A2C664
|
Q6HEP6
|
RSMH_BACHK
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Bacillus cereus group
|
MFNHVTVLLKETVDGLDIKPDGTYVDCTLGGGGHSSYLLSQLTEGGRLIAFDQDEIAIQNAKEKFSSYGEQFITVKSNFRYLSEKLQELGITEVDGILFDLGVSSPQLDTPERGFSYHHDAPLDMRMDQDASLTAYDVVNSWSYEQLVRIFFQYGEEKFSKQIARKIEAYRENKAIETTGELVELIKEGIPAPARRTGGHPAKRVFQAIRIAVNDELKVFEEALESAIEMVKPGGRVSVITFHSLEDRICKTTFKRNSTTPQLPPGLPIIPDEFKPKLKLITRKPILPSDIELEENNRARSAKLRIAEKR
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q6HEP6
|
A9ISM1
|
LPXD_BART1
| null |
Bartonella
|
MADTFFFTPSRQLTVANVAELTGAKLLNPEFSHKVINTLSSLENAVEGSLVFVEHRKFSDALQGSSAVAVFCTNEIVFKVPDTMAVLVTSTPQRDFAQIGRILFPDSVKPMPWFGQKEISPHAHIHPTAKFAHDVCIEAGAVIGRNVEIGAGTLISSTAVIGENCRIGRDCYIAPKVTVQCSLIGDTVQLYPGVCIGQDGFGYVGGISGIEKIPQLGRVIIEDGVEIGANTTIDRGTFQDTVIGEGSKIDNLVQIAHNVKIGRYCLIAAQCGIAGSTSIGDMSQLGGGVGVADHIVIGKCVQIAARSGVMNDIPDGEKWGGSPARPFKQWFREVATLRSMGKVKKERS
|
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
A9ISM1
|
Q2NYU4
|
HEM3_XANOM
|
Pre-uroporphyrinogen synthase
|
Xanthomonas
|
MTTLRIATRKSPLALWQSEHVAAALRQHHPGLEVVLVPMSTRGDEVLDRSLAAIGGKGLFLKELELAMLRGDADCAVHSFKDVPMELDDPFVLPAILERGDPADALVSNLYASLQALPLGARVGTSSLRRQAQLRAARPDLELIDLRGNVNTRLAKLDNGGYDAIVLACAGLQRLGLDERISARLDAPEWLPAPAQGAVAVECRGDDARIHSLLAVLDAGRTRACVEAERAMNRALHGSCHVPVAALARWEGEGLFLQGMVGSASDGRLIHADAHGSADDTEDLGRRVAQGLFDKGAAQLLAAL
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q2NYU4
|
B0B969
|
TILS_CHLT2
|
tRNA(Ile)-lysidine synthetase
|
Chlamydia
|
MITRLFENDKQLEGFFSSLDKKKKYLLALSGGSDSLFLMYLLKSRAIFFTAVHVDYGWRETSYQEASDLAALCEQEQIPFILDRPEATDPMDSRDIENAARRYRYELFYRLCKEKCFSGVFLGHHADDQAETILKRVFEGAHLGNLKGMSAQVMYRDVALLRPLLHIPKHKIVEALDSHQVQYVQDITNCNERFLRARMRERLFPYLQDVFGKNIRDPLLSLAGDSAELREYLDQQTAPFLLRVVDNERGKLLPIEQELLKTPFLAKWVCKQFFLNEGLVASKSFLQTVYDHLMTGSTARLRLRNRTVLVKARGVIIESIY
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
B0B969
|
B7MAJ7
|
LEUC_ECO45
|
Isopropylmalate isomerase
|
Escherichia
|
MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMARIQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAEKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNIK
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
B7MAJ7
|
Q9VC57
|
ATLAS_DROME
|
Atlastin
|
Sophophora
|
MGGSAVQVINASEEHTFVLNEDALSEVLMRDEVKDRFVCVVSVAGAFRKGKSFLLDFFLRYMYSKYVHHDATDWLGGESDPLEGFSWRGGSERDTTGILMWSDIFLHDYPNGDKIAIILLDTQGAFDSQSTVRDCATVFALSTMLSSVQIYNLSQNIQEDDLQHLQLFTEYGRLALADTGKKPFQRLQFLVRDWSFPYEAEYGALGGDKILKRRLEVSDKQHPELQSLRRHISSCFTEVACFLMPHPGLNVATNPKFDGRLQDITPEFKSSLRSLVPMLLAPDNLVYKEISGQRVRARDLIQYFQSYMNIYKGNELPEPKSMLVATAEANHLTAVAAAKELYGQLMEEVCGGTRPYLSTAHLQTEHLRVKDKALFQFAAKRKMGGEEFTEKFRKQLEDDLEEVFTNYQAHNESKNIFKAARTPAVYFACAVIMYILSGIFGLVGLYTFANFCNLVMGVALLTLALWAYIRYSGELSDFGGKLDDFATLLWEKFMRPIYHGCMEKGIHHVATHATEMAVGGGAASYRSQTSVNASNGKVKRS
|
GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate microtubule polymerization and Golgi biogenesis. Required for dopaminergic neurons survival and the growth of muscles and synapses at neuromuscular junctions.
|
Q9VC57
|
Q0VNE0
|
ISPG_ALCBS
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Alcanivorax
|
MEPEVKIERRKTRQVMVGNVPVGGDAPISVQSMTNSETCDVDATVGQIRRLQDAGVDIVRVSVPSMEAAEAFGKIRKQVDVPLVADIHYDYKIALAVAEQGVDCLRINPGNIGREDRIKAVIQCAKDKGLPIRIGVNAGSLEKELQRKYGEPTSDALVESALRHADILDRYDFQNFKVSVKASNVFMTLQAYRKLSSQLEQPLHLGVTEAGTFRSGTVKSAVALGALLMEGIGDTIRVSLAADPVEEVRVGFDILKSLNLRKKGVNIIACPSCSRQNFDVIKTVNELEARLEDINESVDLAVIGCLVNGPGEAREVDVGLTGGTPNNLAYRDGEKSHHITADDLVDELERMVRAKVKKQREDEEKGIIARSE
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q0VNE0
|
Q569E7
|
ZN697_MOUSE
|
Zinc finger protein 697
|
Mus
|
MEQEDNQGVCEYQTSEDRGMDSDLENSEDREGDPEERGMGSNPWDTEDRGHLEQEVDSNPQDDDLRGDSRERDRASTVCSEGRLSEEERAILREEEDDQPGVADMALFPGLSESDSISRSPRGEEDEEEEDEEEESAGENRLIEEEDPLPTPVLPWRRHLSLGGRHRGDKPAHRRFHRLHHPMAMDLGELDSLMASIMDAPTICPDCGESFSPGAAFLQHQRIHRLAEAAAVASLEPFGLAGECGGVVGMMGMGMGVGMGVAGGFGAGPTLARPPREKPFRCGECGKGFSRNTYLTNHLRLHTGERPNLCADCGKSFSWRADLLKHRRLHTGEKPYPCPECGEAFSLSSHLLSHRRAHAAAGGGAGSAGSAAALRPFACGECGKGFVRRSHLANHQRIHTGEKPHGCGECGKRFSWRSDLVKHQRVHTGEKPYMCSECGETFSVSSHLFTHKRTHSGERPYVCRECGKGFGRNSHLVNHLRVHTGEKPFGCGQCEKRFSDFSTLTQHQRTHTGEKPYTCLECGKSFIQSSHLIRHRRIHTGNKPHKCAGCGKGFRYKTHLAQHQKLHLC
|
May be involved in transcriptional regulation.
|
Q569E7
|
B0XY69
|
EIF3K_ASPFC
|
eIF-3 p25
|
Aspergillus subgen. Fumigati
|
MGVAFDKCDTRPAHIDAILNGLDRYNPETTTVFQDYVVQQCEERTFDCYANLALLKLYQFNPHLLQPETVTNILAKALTVFPSPAFSLCLALLPAHTQPFPTADTDASQTSDFVESIQKLARLSTLLESAQYAQFWSTLNSDDLYADLVADVAGFEELVRIRIAIEVGKAFREINAEVLEQWLDLRSREALEKFVTEVCSWEVDKTGPNGTVVKVPTNKENEARSEVKSERVGVEMFGRVIRRGFEQAA
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
B0XY69
|
Q5AVF0
|
AMPP1_EMENI
|
Prolidase
|
Aspergillus subgen. Nidulantes
|
MLFSRPPARLSWILAFQPSQKLPRYSPRFFSISVSRFAIDMEAVDTTKRLSSLRQLMREHKVDVYIVPSEDSHQSEYIAPCDGRREFISGFSGSAGTAIISLNEAALSTDGRYFNQAAKQLDNNWTLLKRGVEGVPTSQEWITQQAEGGKVVGVDPALITGAAARSLSDALQKSGASLIGVSQNLVDLVWGNDRPAPPREKVRVHPEKYAGKSFQEKVSDLRKELENKKAAGFVISMLDEIAWLLNLRGSDIPYNPVFISYCIVTPTKVELYIDDEKLTPEVKAHLGDDVIIKPYDSIFADAKALFEAKKKDPDAPSSKFLLSNRASWALNLSLGGEDHVEEIRSPIGDAKAVKNEVELAGMRACHIRDGAALIEYFAWLENELVNKKSTLDEVDAADKLEQLRSKQELFAGLSFDTISSTGPNGAVIHYKPEKGSCSVIDPNAIYLCDSGGQYLDGTTDVTRTFHFGQPTELEKKAFTLVLKGCIGLDSAVFPKGTSGFALDVLARQHLWKEGLDFLHGTGHGIGSYLNVHEGPVGIGTRVQYTEVPLAPGNVISDEPGFYEDGKFGIRIENVIMVREVQTTHKFGERPWLGFEHVTMCPIGQNLIEPSLLSDSEIKWLNDYHAEVWEKTHKYFENDEVTRKWLERETRPISK
|
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
|
Q5AVF0
|
A5F5X3
|
RLMG_VIBC3
|
rRNA (guanine-N(2)-)-methyltransferase RlmG
|
Vibrio
|
MKTELTLLEQTLTLHRFPKRNNETLQAWDAGDEYLIQHVEQLALPESSHIVIINDHFGTLSCWFSQKHKVSMMSDSYIAHQATQANLQQNQRPPVQLLTTLDPVPNDASVVLLQLPKSNRHLVWILSQLRKALSPNIPIIAVNKAKEIHTSTLNLFEKHLGPTTTSLAWKKHRLVFSSATVNPANEVNPECGWSIEPYAITLTNLPNVYSGESLDLGSRFILEHLPADPTLEDFIDLGCGNGVLSVRLGQLNPQAKITCVDESFMAIASAQKNLHDNLGKRDIHCIANNCLDGFPAHSSSMIVCNPPFHQQQTITDHIAWQMFCDSKHVLKKGGKLWVIGNRHLGYDVKLARLFGKSHVRVIANNSKFVILQAIKS
|
Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
|
A5F5X3
|
Q1H058
|
DSBB_METFK
|
Disulfide oxidoreductase
|
Methylobacillus
|
MCNKLFAGRRGYFLGFVASFGLVGLALFLQQKYNLEPCPLCISQRIAFMALGILFLLAALHNPGRVGRKVYGLLHVIAAATGIGIAARHIWIQANPDKVMAECGAGFDYIMETFPLKKALDLIFKGTGECSAIDWTLFGLTIPQLSLIAFVGLGLFAVLLAFHKKA
|
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
|
Q1H058
|
A7FYA5
|
DAPH_CLOB1
|
Tetrahydrodipicolinate N-acetyltransferase
|
Clostridium
|
MSYNLTDPYEIARYIKEAKKSTPIKAYIEGDLSNCDFTNIEKFNSGDLYILFGESEEILVIIEKNKDKIKNCRIEQDRRKSAIPLLDMLKINARIEPGATIRDKVIIGENAVIMMGAVVNIGAEIGEGTMVDMNAVVGARGKLGKNVHLGAGAVVAGVLEPPSSDPCTIEDNVLIGANAVILEGVKIGKGSVVAAGSIVTTDVPENVVVAGAPAKIIKEVDVKTKDKTKLLDDLRK
|
Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.
|
A7FYA5
|
P82345
|
HBB0_PAGBO
|
Hemoglobin beta-0 chain
|
Pagothenia
|
VEWTDFERATIKDIFSKLEYDVVGPATLARCLVVYPWTQRYFAKFGNLYTATAIAENAMVSKHGITILHGLDRAVKNMDDIKNTYAELSVLHSEKLHVDPDNFKLLADCLTIVVAARFGSAFTGEVQAAFEKFMAVVVSSLGRQYH
|
Involved in oxygen transport from gills to the various peripheral tissues.
|
P82345
|
B5F118
|
HCP_SALA4
|
Prismane protein
|
Salmonella
|
MFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIAALQGLSAWAVKAREYGIINHDVDNFAPRAFFSTLTNVNFDSPRIVGYAREAIALREALKAQCLSVDANAHCDNPMADLQLVSDDLGELQRQAAEFTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECAMEIGQMNFKVMSILDAGETTKYGHPTPTQVNVKATEGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIIDPTVGSYDDRIWTRSIVGWPGVSHLEGDDFGPVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLVGGCDGARGERNYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFFTPDLLAILNEKFGLRSVTTVEEDMKQLLSA
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
B5F118
|
O43719
|
HTSF1_HUMAN
|
HIV Tat-specific factor 1
|
Homo
|
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFRDPEEADYCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEANRGLRRSDSVSASERAGPSRARHFSEHPSTSKMNAQETATGMAFEEPIDEKKFEKTEDGGEFEEGASENNAKESSPEKEAEEGCPEKESEEGCPKRGFEGSCSQKESEEGNPVRGSEEDSPKKESKKKTLKNDCEENGLAKESEDDLNKESEEEVGPTKESEEDDSEKESDEDCSEKQSEDGSEREFEENGLEKDLDEEGSEKELHENVLDKELEENDSENSEFEDDGSEKVLDEEGSEREFDEDSDEKEEEEDTYEKVFDDESDEKEDEEYADEKGLEAADKKAEEGDADEKLFEESDDKEDEDADGKEVEDADEKLFEDDDSNEKLFDEEEDSSEKLFDDSDERGTLGGFGSVEEGPLSTGSSFILSSDDDDDDI
|
Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus.
|
O43719
|
Q9CNB2
|
RL13_PASMU
|
50S ribosomal protein L13
|
Pasteurella
|
MKTFVAKPETVKRDWYVVDATGKTLGRLATELARRLRGKHKAEYTPHVDTGDYIIVINAEKVAVTGNKESDKLYHWHTGYVGGIKQATFKEMIARRPEAVIEIAVKGMLPKGPLGRAMYRKLKVYAGSEHNHAAQQPQVLDI
|
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.
|
Q9CNB2
|
Q7SDA6
|
CGR1_NEUCR
|
rRNA-processing protein cgr-1
|
Neurospora
|
MSSTTTTTQTTSQVETKAVSKPLGMRVNGKQWHAPKKAFRPGSGLTSYEKRAKERQLLAAVKAKEKELKDEKEAERKRRIEALKEKRAKKEEKERYEKMAEKMHKKRVERLKRKEKRNKLINS
|
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
|
Q7SDA6
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.