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
|
|---|---|---|---|---|---|---|
P32113
|
COPA_ENTHA
|
Probable copper-importing P-type ATPase A
|
Enterococcus
|
MATNTKMETFVITGMTCANCSARIEKELNEQPGVMSATVNLATEKASVKYTDTTTERLIKSVENIGYGAILYDEAHKQKIAEEKQTYLRKMKFDLIFSAILTLPLMLAMIAMMLGSHGPIVSFFHLSLVQLLFALPVQFYVGWRFYKGAYHALKTKAPNMDVLVAIGTSAAFALSIYNGFFPSHSHDLYFESSSMIITLILLGKYLEHTAKSKTGDAIKQMMSLQTKTAQVLRDGKEETIAIDEVMIDDILVIRPGEQVPTDGRIIAGTSALDESMLTGESVPVEKKEKDMVFGGTINTNGLIQIQVSQIGKDTVLAQIIQMVEDAQGSKAPIQQIADKISGIFVPIVLFLALVTLLVTGWLTKDWQLALLHSVSVLVIACPCALGLATPTAIMVGTGVGAHNGILIKGGEALEGAAHLNSIILDKTGTITQGRPEVTDVIGPKEIISLFYSLEHASEHPLGKAIVAYGAKVGAKTQPITDFVAHPGAGISGTINGVHYFAGTRKRLAEMNLSFDEFQEQALELEQAGKTVMFLANEEQVLGMIAVADQIKEDAKQAIEQLQQKGVDVFMVTGDNQRAAQAIGKQVGIDSDHIFAEVLPEEKANYVEKLQKAGKKVGMVGDGINDAPALALADVGIAMGSGTDIAMETADVTLMNSHLTSINQMISLSAATLKKIKQNLFWAFIYNTIGIPFAAFGFLNPIIAGGAMAFSSISVLLNSLSLNRKTIK
|
Probably involved in copper import under copper limiting conditions.
|
P32113
|
Q987S0
|
KATG_RHILO
|
Peroxidase/catalase
|
Mesorhizobium
|
MDAKTDDNSAGKCPVAHGSAGRTNRDWWPNQLNVQILHQQSSLSDPMGEAFDYAEEFKSLDLDAVIKDLHALMTDSQEWWPADFGHYGPLFIRMAWHSAGTYRIADGRGGAGAGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGRKISWADLLILTGNVALESMGFKTFGFAGGRADVWEPEQDVYWGPEGKWLADERYSGDRDLQNPLGAVQMGLIYVNPEGPNGNPDPLAAARDIRDTFARMAMNDEETVALIAGGHTFGKTHGAGDASLVGVEPEGADIEQQGLGWASKFGTGKGGDAIGSGLEVIWTTTPTKWSNNFFDNLFGFDWELTKSPAGAHQWTPKGGAGAGTVPDAHNSAKRHAPSMLTTDLALRFDPSYATISKRFHENPDQFADAFARAWYKLTHRDMGPVARYLGPLVPKEELPWQDVIPVVDHVLIDEQDAEALKAEILASGLSVSQLVSTAWASASTFRGSDKRGGANGARIRLSPQKDWAVNQPAELAKVLDKLQAIAKDFNAAQTGSKKVSLADLIVLGGNAGIEKAAKAAGHSVDVPFWPGRMDASQEQTDIHSFAPLEPTVDGFRNYVSGKQRLTVEEALVDRAQLLTLTAPELTVLVGGLRVLGANAGQSKHGVFTKQPETLSNDFFVNLLDMGTEWKATSDAKDVFEGRDRKTGEVKWTGTRADLIFGSHSQLRALAEVYATADAKAKFAKDFVVAWTKVMNADRFDIAG
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
Q987S0
|
Q9LFX9
|
PTR13_ARATH
|
Nitrate transporter 1.6
|
Arabidopsis
|
MGVVENRKILPEKKLGGWRAITFILGNETLEKLGSIGVSANFMLYLRNVFHMEPVEAFNVYYLWMGLTNFAPLLGALISDAYIGRFKTIAYASLFSILGLMTVTLTACLPQLHPPPCNNPHPDECDDPNKLQLGILFLGLGFLSIGSGGIRPCSIPFGVDQFDQRTEQGLKGVASFFNWYYLTLTMVLIFSHTVVVYLQTVSWVIGFSIPTSLMACAVVLFFVGMRFYVYVKPEGSVFSGIARVIVAARKKRDLKISLVDDGTEEYYEPPVKPGVLSKLPLTDQFKFLDKAAVILDGDLTSEGVPANKWRLCSIQEVEEVKCLIRVVPVWSAGIISIVAMTTQATFMVFQATKMDRHMGPHFEIPAASITVISYITIGIWVPIYEHLLVPFLWRMRKFRVTLLQRMGIGIVFAILSMFTAGFVEGVRRTRATEMTQMSVFWLALPLILMGLCESFNFIGLIEFFNSQFPEHMRSIANSLFPLSFAAANYLSSLLVTTVHKVSGTKDHPDWLNKDLDRGKLDYFYYLIAVLGVVNLVYFWYCAHRYQYKAGSQIEDFNEEKSLLDIEPNQRHDQSPS
|
Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport. Involved in delivering nitrate for seed development.
|
Q9LFX9
|
A5VP09
|
DXS_BRUO2
|
1-deoxyxylulose-5-phosphate synthase
|
Brucella
|
MSRPSTPLLDKVPTPDRLRALPERDLPQLAEELRTELIDAVSTTGGHLGAGLGVVELTVALHHVFNTPYDRIIWDVGHQAYPHKILTGRRDRIRTLRQAGGLSGFTKRAESEYDPFGAAHSSTSISAGLGMAVASELSGEKRNVIAVIGDGSMSAGMAYEAMNNAGALDARLIVILNDNDMSIAPPTGAMSAYLARLVSGRTYRSVREAAKQVAQKLPKFLQDKARKSEEYARAFFTGGTLFEELGFYYVGPIDGHNLDHLLPVLKNVRDTQKGPVLIHVVTQKGKGYAPAEAAADKYHGVNKFDVITGKQAKPPANAPSYTKIFGTSLIEEARHDDKIVAVTAAMPTGTGLDLFGEAFPKRVFDVGIAEQHAVTFAAGLASEGYKPFCAIYSTFLQRGYDQVVHDVSIQNLPVRFPIDRAGLVGADGPTHAGSFDTGFLAALPGFVVMAASDEAELRHMVRTAAEYDEGPISFRYPRGDGVGVDLPERGSVLEIGKGRIVREGTKVALLSFGTRLQECLAAAEELGAAGLSTTVVDARFAKPLDHDLIRRLAREHEVLVMVEEGAVGGFGSHVLQFLATDGLLDRGLKVRALTLPDIYQDHGKPDAMYAEAGLDRTGIVRTVFAALHRDELGHEALPTPFRA
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
A5VP09
|
Q8IX95
|
CTGE3_HUMAN
|
Putative cTAGE family member 3
|
Homo
|
MTFKGFQMNEEKLEIGIQDASSENCQLQESQKQLLQEAEVWKEQVSELNKQKITFEDSKVHAEQVLNDKENHIETLTERLLKIKDQAAVLEEDITDDGNLELEMNSELKDGAYLDNPPKGALKKLIHAAKLNASLTTLEGERNQFIFSYLKLIKPGRA
|
Tumor-associated antigen.
|
Q8IX95
|
Q7V1T7
|
HEM1_PROMP
|
Glutamyl-tRNA reductase
|
Prochlorococcus
|
MHIVVVGLSHRTAPVEVREKLSIPDQSISESLKTLSINSDILEVSILSTCNRLEIYALVKEINIGISSIKEFLTDYSSVNFEDLNPHLFDFRQEEAVLHLMKVSAGLDSLVLGEGQILSQVKKMMRLGQENQSTGPILNRLLSQSVSAGKKVRSETNLGTGAVSISSAAVELAQLKIGQDHGVDGLVSLKSEKVLVVGAGRMSRLLITHLKSKGCNRLTLLNRNIERAVNLAGDFPDLEINCKSLNELDKNISLSSLVFTSTASEKPFIDLARVEKISLNNKLKFIDIGVPRNISNDVKHHAFIESFDVDDLEEVVSRNQEFRQKIAKEAESLVKDERIIFLEWWASLEAVPVINKLRSDLELIRKEELQKALSRMGPDFSARERKVVEALTKGIINKILHTPVTKLRSPQSRDERQASLKIVEKLFSLVDDE
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
Q7V1T7
|
Q4UKS2
|
LEPA_RICFE
|
Ribosomal back-translocase LepA
|
spotted fever group
|
MNNQKYIRNFSIIAHIDHGKSTLADRLIEHCGGLQAREMSQQVLDSMDIEKERGITIKAQTVRLVYKAKDGNTYYLNLMDTPGHVDFAYEVSRSLAACEGSLLVVDSTQGVEAQTLANVYQAIENDHEIVPVLNKIDLPASEPEQVKQQIKDIIGIDASEAVLISAKSGIGIDLVLEAIVNKLPPPKESSSDILKALLVDSWYDPYLGVVILVRIIDGTLRKNIRIKMMATNSVYTVENVGYFTPKKHISDVLHAGEIGFFTASIKQVADCKVGDTITDEKKPCEQALPGFKPNLPVVFCGLYPTDSAEFEHLKDSLAKLRLNDASFEYEMESSSALGVGFRCGFLGLLHLEIIQERLSREFDLDLITTAPSVVYKIHMRDGESLEIHNPADLSDLQKIESMEEPWIKATIMVPDEFLGAVLSLCTEKRGVQLDHSYIANRAKIIYKLPLNEIVYDFYDRLKSCSKGYASFEWQMDVYEPSELVKLGILVNGEEVDALSTIVHRSRAEQRGRALCVRLKDLIPRQQIDIAIQASIGSRIIARETIKALRKDVLSKCYGGDISRKRKLLEKQKAGKKRMRQYGNIEIPQSAFIAALKIGDE
|
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.
|
Q4UKS2
|
B9KSH8
|
ISPD_CERSK
|
MEP cytidylyltransferase
|
Cereibacter
|
MTTAAIIVAAGRGTRAGGDLPKQWQPLAGRPVLAHTLAAFRAAAGVSRTLLVIHPDDRARAEALPGVAEGKVELVEGGASRDASVRNALEALAGAGIERVLIHDGARPLVAPGLIARTLAALESAPGAAPAVPVSDALWRGEGGRVVGTQDRTGLFRAQTPQAFRYEAILAAHRAHPGGAADDVEVARAAGLEVAIVEGCEDNLKVTYPGDFARAERLLALAAGL
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
B9KSH8
|
A4SV71
|
MRAY_POLAQ
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Polynucleobacter
|
MLLILAQWLQDDFGFFRVFNYITFRAVMATVTALLIGLAAGPWVIRKLSELKMGQAVRTDGPLTHLVKSGTPTMGGVLILIGIFVSCMLWADLSNRFIWIVMIVTFGFGAVGWVDDYRKVVRKDPKGMASREKFFWQTLIGLFAAIYLAFSVSEINNLKVLELFFEWVKSGFALDLPAKTNLLLPFMKEVSYPLGMMGFIILSYLVIVGSSNAVNLTDGLDGLVIMPVILVGAALGAFAYVMGNAIYAKYLLFPYIPGAGELMIFCGAMGGAGLAFLWYNTHPAQVFMGDVGALALGGALGTIAVIVRQEIVLFVMGGIFVAETVSVMMQVVWFKITKKHFGEGRRIFRMAPLHHHFELGGWKETQVVVRFWIITILLVLIGLSSLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
A4SV71
|
Q0S0L4
|
METK_RHOJR
|
Methionine adenosyltransferase
|
Rhodococcus
|
MSQSGSRLFTSESVTEGHPDKICDAISDSILDALLTDDPRARVAVETLVTTGQVHVAGEVTTSAYADIPKIVRDTVLEIGYDSSAKGFDGNSCGVNVAIGAQSPEIAQGVDHSHEVRTGELSDDEIDRQGAGDQGLMFGFATTDTPELMPLPIALAHRLSRRLTEVRKSGVLPYLRPDGKTQVTIEYDGDKAVRLDTVVISTQHAADIDLDNLLTPDLREKVLGSVLAEIDMPELDVSDIRLLVNPTGKFVLGGPMGDAGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAMRWVAKNAVAAGLADRIEVQVAYAIGKAAPVGLFVETFGTEKTDPARIQQAITETFDLRPGAIIRDLDLLRPIYAQTAAYGHFGRTDIDLPWESIDRAEKLRAAAGL
|
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.
|
Q0S0L4
|
Q3YWV4
|
RL6_SHISS
|
50S ribosomal protein L6
|
Shigella
|
MSRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGVDKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
Q3YWV4
|
A7GK22
|
RL23_BACCN
|
50S ribosomal protein L23
|
Bacillus cereus group
|
MRDPRDIIKRPVITERSMEMMAEKKYTFDVDVKANKTEVKDAVEAIFGVEVEKVNIMNYKPKAKRVGRHAGFTNRRRKAIVKLTADSKEIEIFQGV
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
A7GK22
|
A5WI20
|
DNAK_PSYWF
|
Heat shock protein 70
|
Psychrobacter
|
MAKTIGIDLGTTNSCVAVMEGDKVKVIENAEGTRTTPSIIAYKDGEILVGQSAKRQAVTNPNNTLYAIKRLIGRRFDDKVVQKDIGMVPYKIVKADNGDAWVEVNDKKMAPPQISAEILQKMKKTAEDYLGEKVTDAVVTVPAYFNDSQRQATKDAGKIAGLNVKRIINEPTAAALAYGMDKKKGDSTVAVYDLGGGTFDVSIIEIADVDGEQQFEVLSTNGDTFLGGEDFDLALIDYLVEEFKKEQNFNLKGDPLAMQRLKEAAEKAKIELSSAQSTEVNLPYITADASGPKHLVVTISRSKLEALTEALVKRTIDPCKVALEDAGLKASDIDDVILVGGQTRMPLVQKTVEEFFGQEPRKDVNPDEAVAVGAAIQGAVLSGDKTDVLLLDVTPLTLGIETMGGVMTGIIEKNTMIPTKKSQVFSTAEDNQPAVTIKVFQGERKVAAQNKLLGEFNLTDIPPAPRGMPQIEVTFDINADGIMNISAKDKGTGKEQSIQIKADSGLSDEEIEQMVRDAEANAAEDEKFAALAQVRNEADGRIHAIQKALKDAEDKVTEEEKSSVETAISDLELAAKEDDHDDIKAKLEALDNAFLPISQKIYAAGQGAEGAAPQADATEANAADDDVVDAEFTEVNEDDKK
|
Acts as a chaperone.
|
A5WI20
|
P05023
|
AT1A1_HUMAN
|
Sodium pump subunit alpha-1
|
Homo
|
MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
|
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
|
P05023
|
A6VMY7
|
AROC_ACTSZ
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Actinobacillus
|
MAGNSIGQLFRVTTFGESHGIALGCIVDGVPPNMALSEADIQPDLDRRKPGTSRYTTARREADEIQILSGVFEGKTTGTSIGLIIKNADQRSKDYGDIMDKFRPGHADYTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLRERFGIEIRGYLSQIGEVKIDPQTVADVTKINWQQVADNPFFCPDKSAVEKFDELIRKLKKEGNSIGAKLTVVAENVPVGLGEPVFDRLDAELAHALMGINAVKAVEIGDGFDVVAQKGTEHRDEMTPAGFLSNHAGGILGGISNGQPIIATIALKPTSSITIPGRTVDINNKPVELITKGRHDPCVGIRAVPIAEAMVAIILLDHLLRFKAQCK
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
A6VMY7
|
A7RG82
|
CLP1_NEMVE
|
Protein CLP1 homolog
|
Nematostella
|
MDTEQDAKSEERQQWKLEKDTELRVEVAEGDREAIIVLLSGNAEVFGTELVKNKKFTFRPGSKLAIFTWQGCSVEIQGPLEVAYKSKETPMVMYLNLHMALEQMRERADKHEAVELGPRVMVVGPTDVGKSTVCQLLLNYAVRMGRRPISVDLDVGQGTASVPGSMGALLLERPADIEEGFSLQAPLVYLFGHTSPSPNEKLYNMLSSKIADIVFQRFERNKKACASGCVINTCGWVTGMGYRIIVHAATAFKVNVIVVLDQERLYNDLKNQFGDKVQIVHLPKSGGVVVRSRETRRKVRDERLRSYFYGQQANLYPHSFEVKFSDVKLFKIGAPLVPDSCLPLGMDQGQNETKLVPVVPTKDLKHCLLAISAAESLEEDLVQTNVIGFLVVNEVDLDREVMVVLSPAPRPLPRKFLLLSEIKFMDFK
|
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
|
A7RG82
|
Q8R857
|
ACPS_CALS4
|
4'-phosphopantetheinyl transferase AcpS
|
Caldanaerobacter
|
MEIFVGTDIMEVERIKKILEKRPHFLERIFTEKEREFLRKKKNPWPHLAGFFSAKESVSKVLGTGIRGFSWQDIEIIHNEYGKPEVVLKGKAKAIAAEKGIKEIKLSISHTSDYAMSVAIAVGGENS
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
Q8R857
|
Q91YY2
|
B4GT3_MOUSE
|
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3
|
Mus
|
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDPGPTFDYSHPHDVYSNLSHLPAAPGAAGAPPAQALPYCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH
|
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
|
Q91YY2
|
Q8ZXL4
|
NADE_PYRAE
|
NH(3)-dependent NAD(+) synthetase
|
Pyrobaculum
|
MFVYDVVNALDYEKARSIITAFISQYVQRAGSRGVVVGISGGVDSTVAAALAVEALGRQRVLGLLMPSLYTPPEDLKDALDVINALGVEWKRVDITPIYDAFVKTLPDFSQENRVAAGNILPRIRMTVLYYYANKYNLLVMGTGDRSELLLGYFTKYGDGGVDFLPIGSLFKLQVRELAARLGFADIAKKPSSPRLWQGHTAEGELGASYEVIDQVLYAVFDLKKPPEEVRGFFGEVVDIVITRVKKNIHKLTPPAYPDITPARRNV
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
Q8ZXL4
|
A8IM96
|
RUVC_AZOC5
|
Holliday junction resolvase RuvC
|
Azorhizobium
|
MTNGMIRIIGLDPGLRRTGWGVIEAQGTRLTYVACGTILPPENAPMAERLAELHRGLAEVLARHAPDEAAVEETFVNMNPSSTLKLGQARGVVMLAPAQAGLSVAEYAPLLVKKTVVGAGRAEKAQIRMMIGVLLPKATPQTEDAADALAVAVTHAHHRGPAALRRAAL
|
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.
|
A8IM96
|
Q9H4I8
|
SEHL2_HUMAN
|
Serine hydrolase-like protein 2
|
Homo
|
MSENAAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGGVVGGMFFCTFPEMVDKLILLDTPLFLLESDEMENLLTYKRRAIEHVLQVEASQEPSHVFSLKQLLQRLLKSNSHLSEECGELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHVLLIKAVHGYFDSRQNYSEKESLSFMIDTMKSTLKEQFQFVEVPGNHCVHMSEPQHVASIISSFLQCTHMLPAQL
|
Probable serine hydrolase. May be related to cell muscle hypertrophy.
|
Q9H4I8
|
Q0BKM8
|
MURD_FRATO
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Francisella
|
MFSFYFNDNKITKLLMVGYGSTGKSVCDFLANFIDITVDISQNDDEFVNYDLNSYDLITVSPGIPLNKSPYRALTKFKDKIVSDIDIFYQYIKDTKAKTIAVTGSNGKSTVVTMTDFVLKDLGYKSILVGNIGTPALNKIGEKFDYCVVEVSSFQINLFNCVRFDLGCIINVSPDHLDRYQNFEQYKQSKLNLAKFSNDFFVYDVHNGIKYAGEYQIIRGAIYRNSTKLLDIVETKLFGEHNLENIIVVLNILDRLGLDINQAIDSIKKFKGLEHRCKIVKKVNGTTYINDSKGTNVGATIAALNSITNSKNIILLLGGVAKGGDFSLMIKSLDKYVKYVYIYGADKEYIESYIKGYCKYQLCNNMKQAFELASQKANSNEIVLLSPACASFDEFSGYAQRGEVFQNLVAQLEQKS
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q0BKM8
|
P00318
|
APCB_MASLA
|
Allophycocyanin beta chain
|
Mastigocladus
|
MQDAITAVINSSDVQGKYLDTAALEKLKSYFSTGELRVRAATTIAANAAAIVKEAVAKSLLYSDITRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLGVPISATVQAIQAMKEVTASLVGPDAGKEMGVYFDYICSGLS
|
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
|
P00318
|
A6US28
|
KAE1B_METVS
|
Serine/threonine-protein kinase Bud32
|
Methanococcus
|
MGNSNELICIGLEGTAEKTGVGVITSNGEVLFNKTVIYTPKIQGIHPREAADHHAETFIKLLNEVSGVIPLDKIDLVSFSQGPGLGPSLRVTATTGRALALSLKKPIIGVNHCVSHVEIGKLKTDALDPLTLYVSGGNTQVLAYTGKKYRVIGETLDIAIGNCLDQFARYCNLSHPGGVFVEQYAKEGKKFLKLPYTVKGMDISFSGLLTASMKKYDSNEKIEDVCYSLQETAFSMLTEITERALSHTNKPEIMLVGGVAANDRLKEMLEIMCNEQNVDFYVPEKQFCGDNGAMIAWLGILQYINGKRMDILDTKTIPHFRTDMVDVNWVVKSTENELDILNKKRQIPRHLIGKGAEADILKGRYLEWESITKERIKKGYRTAELDEMIRTRRTVKEARFLSIIKDFSVNSPHIFDIDIENKKITMEYIHGKLLKDLIEEGNLEFCKSIGELIGKMHEGKIIHNDLTTSNFIVNTDAYMIDFGLGKYSDLIEDKAIDLIVLKKSIMSIHYDKFGEIWDKIIEGYSKYGHSELVLQYIKEVEKRGRYL
|
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 a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function.
|
A6US28
|
Q9KCM0
|
RHAB_HALH5
|
Rhamnulose kinase
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MNYSLAVDIGASSGRLIVGECNKKIQLTEIHRFENQIIEKNGQFCWDVDALFSEIKTGLKKCREAGIEPVSMGIDTWAVDFVLLDEHDKPLTDAVSYRDPRTDGVMEEVIEQFMKERLYLETGIQFQQFNTIYQLYALKKQHPDIFKKAKSFLMIPDYFHFLLTGKKANEYTNATTTQLVNAFTKKWDKDIIEALGFNPDMFQEIKLPTESLGKLKSEWVEEVGFDLEVILPATHDTGSAVVAVPKVADTIYLSSGTWSLIGVENSFPICVTKALDYNFTNEGGMNYQFRFLKNIMGLWMIQEVRRNYDNRYSFAQLVELSKGISFKSTVDVNDPRFLKPTNMIKEIQRYCQETGQQAPELPGEVAKCVFESLAESYTSAVAEIEDIFEKDFKSINVIGGGCRNELLNQLIADRTKKDVFAGPIEATAIGNLVAQWMALGEIESIQQARKLIYDSFDVKRYVSADRE
|
Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
|
Q9KCM0
|
Q4QK81
|
TTCA_HAEI8
|
tRNA 2-thiocytidine biosynthesis protein TtcA
|
Haemophilus
|
MTQLAQQEKKQTYNFNKLQKRLRRNVGNAITDFGMIEDGDKVMVCLSGGKDSYTLLDILLNLQQNAPIKFDIVAVNLDQKQPGFPEHVLPEYLESIGVDYKIVQENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGATKIALGHHRDDMLATLFLNMFYGGKMKSMPPKLISDDGKQIVIRPLAYCKEKDIEKYAIAKEFPIIPCNLCGSQPNLQRQVVKEMLNTWDRQYPGRLETMFSAMQNITLSHMCDPKLFDFKGIKHGQLIDGIEGDTAFDEEKITPMQFEDEDQTDFSNNEMINFKEVN
|
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
|
Q4QK81
|
F7J187
|
NVD2_CIOIN
|
Neverland 2
|
Ciona
|
MLIEYLIRITVMVITSERLLILMGLCDESFHFPVMIRVVFNAAVAIVIALVMSKLYKVLFAPLDLRRKLEDVGYVHHDHSVSREENIRDTQRRKKLGNTPPVFPNGWFKVADSTWIKKGQVKSIYFFGEQLALFRNKRGLLRALDAYCPHLLANMAAGGKVVNSDCLECPFHGWKFSGETGKLVDVPYAQKVPTFVSVKKWSCCEVDGMAYLWYHCDGGEPKWVLPSSVTINTLKYAGKTEHIINSHIQDIPENAADISHLDHLHKPVIGSDVEKTNESLLNNLIFHSIQASWKPPTDPNEPHRSTMSIKDNIHLSIFNIKIPLLYLEFEIDQIGPGAVHIHVRTPFFRGLMLQNVTPIEPFVQKLTHSFYVSPWVPVCIAKAFYLLETTQIERDILMWNNKTYFRQPVLVKEESALAKHRRWYQQFYSENSPRMNHRGDLVYPGKPKLADW
|
Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. Essential regulator of steroid biosynthesis as this reaction is the first step in the synthesis of the steroid hormone Delta(7)-dafachronic acid.
|
F7J187
|
O69717
|
VPB50_MYCTU
|
Putative antitoxin VapB50
|
Mycobacterium tuberculosis complex
|
MTSLLEVLGAPEVSVCGNAGQPMTLPEPVRDALYNVVLALSQGKGISLVPRHLKLTTQEAADLLNISRPTLVRLLEDGRIPFEKPGRHRRVSLDALLEYQQETRSNRRAALGELSRDALGELQAALAEKK
|
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC50.
|
O69717
|
A1KSN6
|
HIS6_NEIMF
|
ImGP synthase subunit HisF
|
Neisseria
|
MALAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNSENTRWEIFTHGGRNPTGLDAVEWAIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGIFHFGEIAIREAKRAMREAGIEVRL
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
A1KSN6
|
Q0DJA3
|
DRB3_ORYSJ
|
dsRNA-binding protein 3
|
Oryza sativa
|
MKKKSAPTPLPPETANTSPAPIGATAGIRVENCYVFKSRLQEYAQKAGLQTPEYHTSKEGPSHEPVFKSTVVINNTSYGSLPGFSNRKAAEQSAAEVALMEIVKSIPANANIPAVQETGLCKNLLQEYAQKMNYAIPSYICTKPASGLAPFLCTVEIGGIQYIGAAARTKKDAEIKAARTALLAIQGQSEGSANGATKYIVVPGKRVGKEVEKRPIETPKPLKAKKGGFKKKWNKRKFMKKDGQAVDVEKDEARVAGDAHDSDVLMQPTVITQEASCGTLFLQPCEEAKRVEDEPPRDIEMVQPDKENQHSDAALVQPDDEARVEQEPSRDISVVQPNEEAISAKQEPSIDAATLQPKEEAMKTGCVALVLCLNISVDPPDVIKISPCVRKECWIDPFSMAAPKALETIGKTLHSQYERWQPKARYKLQLDPTLEEV
|
Binds double-stranded RNA.
|
Q0DJA3
|
Q8F4I2
|
DDL_LEPIN
|
D-alanylalanine synthetase
|
Leptospira
|
MAKIAVFFGGSSTEHSISILTGCFICKTLHTMGHSVKPILLTKDGGWVVPSEYRMSIPFEVSNSPDLFQEEFQKRYGVSRTNQIFSLDADIVFLGLHGGQGEDGTIQGFLEILGIPYTGSGVLASAIAMDKTRANQIFLQSGQKVAPFFEIDKLEYLNSTDAVITKLETLGFPQFLKPVEGGSSVSVYKITNREQLKEKLALIFESDSKVMSQSFLTGIEVSCGVLERYRDGKFKKIALPATEIVPGGEFFDFESKYKQGGSHEITPARISEQEMKRVQELAIAAHRSLGCSGYSRTDFIIVNGEPHILETNTLPGMTETSLIPQQAKAAGISMEEVFSDLIEIGLKRSLY
|
Cell wall formation.
|
Q8F4I2
|
Q9M2S0
|
GMPP2_ARATH
|
Probable mannose-1-phosphate guanylyltransferase 2
|
Arabidopsis
|
MKALILVGGFGTRLRPLTLSLPKPLVDFANKPMILHQIEALKAIGVDEVVLAINYEPEQLLVMSKFSNDVEATLGIKITCSQETEPLGTAGPLALARDKLVDGSGQPFFVLNSDVISDYPLEEMIAFHNAHGGEASIMVTKVDEPSKYGVVVMEEATGRVERFVEKPKLFVGNKINAGIYLLNPSVLDRIELRPTSIEKEIFPQIAEAEKLYAMLLPGFWMDIGQPRDYITGLRLYLDSLRKKSPSKLATGPHILGNVLVDETAEIGEGCLIGPNVAIGPGCVVESGVRLSHCTVMRGVHVKRYACISSSIIGWHSTVGQWARVENMSILGKNVYVCDEIYCNGGVVLHNKEIKSDILKPDIVM
|
Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants.
|
Q9M2S0
|
B5YJH1
|
PYRDB_THEYD
|
Orotate reductase (NADH)
|
Thermodesulfovibrio
|
MPVLEVKIGNLSFKNPVLTASGTFGYGLEYSQFVDLNILGGIVVKGLSLKPKQGNPPPRIYETPCGMINSIGLQNIGLEAFKKEKLPFLKKFNTNIIVNFFGENLDEYIEVAKLLDETEGVHALEMNVSCPNKTSEWRKMGLEPELLREAIKRVRLHIKKPLIVKLAPQVTEIALMARICEEEGADAVSLINTIPAMVIDIKTRKSMIGTLTGGLSGPAIRPVALRAVWEVAQAVKIPVIGVGGIVSAEDALQFLIAGAKAIQVGTANFINPIATVEIIEGIKQFLIEENIKDINEIIGSFKE
|
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
|
B5YJH1
|
B4SBU9
|
RL23_PELPB
|
50S ribosomal protein L23
|
Pelodictyon
|
MINPLLRPLLTEKSTGLTEKKGQYVFVVKPDADKTDIKKAVEKKFGVEVKSIRTINCLGKSRAQNTRKGRVTGKKSDWKKAIITLEKGQSIDYYSNTAQKSEG
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
B4SBU9
|
Q04557
|
HYIN1_AGRVS
|
Indole-3-acetamide hydrolase
|
Agrobacterium
|
MVEISSISQTLRALRRKQYSCRDLVESLVSRSESATHLNAFAATDWLHLRNEADRVDRNGSGGVGLMGIPLCFKANIATGIFPTSAGTQGLLRHKPAIPAKIVERLHSAGALIGASGNMHELSFGITNDNKTFGPARNPWNQALISGGSSGGVAVSVAANLMLGGIGTDTGASVRLPAALCGVVGFRPTFGNYPTDGIVPVSPSRDTPGLIVRSVEDAVLLDRIIRNKCPTQNMSLKGLRLGLPRSHFFDNLEPHVAAASERAIRRLATNQMTFVEADIPNVAELTRKVSLPVAIYEFPRALMAYLSFHGIGNTFDELIQNIQDPQVYDLVQSQLSKGLISESVYRRALRCYKPRLKATYENYYSSNGLDAVLFPSVPLTAKPVGLQTTLVHNGVETDTFGIFVRNLDPSSNIGLPSLSVPVSLTPDRLPVGIQIEGPFGSDDMVLAIGRAVEEMVKFGQEY
|
Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA).
|
Q04557
|
B2FPX7
|
RECO_STRMK
| null |
Stenotrophomonas maltophilia group
|
MMIEDDTGFVLHARAYRETSLLVEVLSAQHGRVGLLARGVSTAKGQVLRAALQPLQWIRFSAQQRGELAQLRGAEALDAAPRLVGQAMLAGFYLSELTLRLAPRQDPLPELYLAYGEARARLAVGAGLAWTLRRFERELLTALGLGFELDSASDGQPIDPAARYELDPQEGAQRLLSERGGERRAAATGSALLALAADEEPAAADLASLRLPMRRVLAHHLGPRGLKSWEMLEQLAPRR
|
Involved in DNA repair and RecF pathway recombination.
|
B2FPX7
|
Q5QQX7
|
CP19A_CANLF
|
Estrogen synthase
|
Canis
|
MLLEMLNPMHYNITSMMPEVMPVATMPILLLTGFLLLVWNYEDTSSIPGPGYCMGIGPLISHCRFLWMGIGSACNYYNKMYGEFMRVWICGEETLIISKSSSMFHIMKHSHYSSRFGSKLGLQCIGMHENGIIFNNNPTLWKAIRPFFTKALSGPGLVRMVTVCVGSIITHLDRLEEVSNELGYVDVLTLMRRIMLDTSNILFLGIPLDESAIVVKIQGYFDAWQALLLKPDIFFKISWLYKKYEKSVKDLKDAMEILIEEKRHRISTAEKLEDHMDFATELIFAEKRGDLTRENVNQCILEMLIAAPDTMSVSVFFMLFLIAKHPKVEESIMKEIQAVVGERDIRIDDMQKLKVVENFIYESMRYQPVVNLVMRKALQDDIIDGYLVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRSCAGKYIAMVMMKVVLVTLLRRFHVQTLQGECIENMQKKYGLSLHPDETNNLLEMVFVPRNSEKCLER
|
A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
|
Q5QQX7
|
B7UKK1
|
LPXH_ECO27
|
UDP-2,3-diacylglucosamine diphosphatase
|
Escherichia
|
MATLFIADLHLCVEEPAITAGFLRFLAGEARKADALYILGDLFEAWIGDDDPNPLHHQMAAAIKAVSDSGVPCYFIHGNRDFLLGKRFARESGMTLLPEEKVLELYGRRVLIMHGDTLCTDDAGYQAFRAKVHKPWLQTLFLALPLFVRKRIAARMRANSKEANSSKSLAIMDVNQNAVVNAMEKHQVQWLIHGHTHRPAVHELIANQQPAFRVVLGAWHTEGSMVKVTADDVELIHFPF
|
Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
B7UKK1
|
Q48HY8
|
ARNE_PSE14
|
Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE
|
Pseudomonas
|
MTWLMLLSACLLTCLGQIAQKYAVEGWRETFPGVLAALRSMWLWLAIACLGLGLLVWLLVLQRMDVGIAYPMLGLNFVLITLVGRYVFKEPVDPQHWLGIALILVGVFQLGRQA
|
Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
|
Q48HY8
|
O24407
|
IAA16_ARATH
|
Indoleacetic acid-induced protein 16
|
Arabidopsis
|
MINFEATELRLGLPGGNHGGEMAGKNNGKRGFSETVDLKLNLSSTAMDSVSKVDLENMKEKVVKPPAKAQVVGWPPVRSFRKNVMSGQKPTTGDATEGNDKTSGSSGATSSASACATVAYVKVSMDGAPYLRKIDLKLYKTYQDLSNALSKMFSSFTIGNYGPQGMKDFMNESKLIDLLNGSDYVPTYEDKDGDWMLVGDVPWEMFVDSCKRIRIMKGSEAIGLAPRALEKCKNRS
|
Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
|
O24407
|
O33950
|
CATA2_ACILW
|
CDI2
|
Acinetobacter
|
MNKQAIDALLQKINDSAINEGNPRTKQIVNRIVRDLFYTIEDLDVQPDEFWTALNYLGDAGRSGELGLLAAGLGFEHFLDLRMDEAEAKAGVEGGTPRTIEGPLYVAGAPVSDGHARLDDGTDPGQTLVMRGRVFGEDGKPLANALVEVWHANHLGNYSYFDKSQPAFNLRRSIRTDAEGKYSFRSVVPVGYSVPPQGQTQLLLDQLGRHGHRPAHIHFFVSAPGFRKLTTQINIDGDPYLWDDFAFATRDGLVPAVRQAEVRKANRTAWTVSSR
|
Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at lower rates than catechol, but has no activity with 4-nitrocatechol or protocatechuic acid.
|
O33950
|
Q9S714
|
PSAE2_ARATH
|
Photosystem I reaction center subunit IV B, chloroplastic
|
Arabidopsis
|
MAMTSAATGFILTANVPAAIGGGSSKSTTIVSFLPMRSFGSRLVVRAAEDTPPATASSDSSSTTAAAAPAKVPAAKAKPPPIGPKRGSKVKILRKESYWYKNVGSVVAVDQDPKTRYPVVVRFAKVNYANISTNNYALDEVEEVK
|
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
|
Q9S714
|
Q1I7D4
|
FADB_PSEE4
|
3-hydroxyacyl-CoA dehydrogenase
|
Pseudomonas
|
MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVDAIKADASVKGVIVSSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFSDFEDLEVPTVAAINGIALGGGLEMCLAADYRIMSSSAKIGLPEVKLGIYPGFGGTVRLPRLIGSDNAIEWIAAGKENRAEDALKVGAVDAVVAPELLQAGALDLIKRAISGELDHKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFAKLARTSVAESLIGLFLNDQELKRKAKAHDEIAHDVKQAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEAIQLGLNEASKLLGKRVEKGRLTPAKMAEALNAIRPTLSYGDFGNVDIVVEAVVENPKVKQAVLAEVEGQVKEDAILASNTSTISINLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSEVAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAVDALYEANRLGQKNGKGFYAYETDKRGKPKKVADASVLDVLKPVIFEQREVSDEDIINWMMVPLCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADKYADLGPLYHATAKLREMAKNGQRFFN
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
|
Q1I7D4
|
O35594
|
IFT81_MOUSE
|
Carnitine deficiency-associated protein expressed in ventricle 1
|
Mus
|
MSDQIKFIVDSLNKEPFKKNYNLITFDSLGPMQLLQVLNDVLAEIDPKQDVDIREEMPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKELESKKKELHFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVELRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSPASIGQVIQEGGEDRLVL
|
May play a role in development of the testis and spermatogenesis.
|
O35594
|
Q2G8X7
|
RL2_NOVAD
|
50S ribosomal protein L2
|
Novosphingobium
|
MALKSYNPTSPARRGLVLVDKSALWKGKPVKALTEGKRKTGGRNNKGHVTSRGIAGGHKQKYRYVDFKRRKWDMPATVERLEYDPNRTAFIALVKYEDGELAYILAPQRLGVGDQVIAGEKTDVKPGNAMLLSQMPVGTIIHNVEMKPGKGGQIARSAGTYVQLVGRDRGMVIVRLNSGEQRYLRGDCMGTVGAVSNPDNGNQNLAKAGRNRWLGKRPLTRGVAKNPVDHPHGGGEGRTSGGRHPVTPWGKPTKGARTRHNKATDKMIIRSRHAKKKR
|
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.
|
Q2G8X7
|
C6C3U9
|
ZAPC_MUSP7
|
Cell division protein ZapC
|
Musicola
|
MKLIPDDNWRWYFDADQARLMLDLANGMTFRSRFSATMLTPDAFNPSDFCVEDAALFFTYQEKCLTLNIDAQAKAELVLNALVANRFLKPLMPKSWHFAALGHGEYCPQLGELVWVRLNERLEDACFMVVDTGDKASLCLLAQAELALSGKVMVLGEAIKIMHDRLCPVDEGADHAQSSLHFAHAG
|
Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.
|
C6C3U9
|
P13659
|
MBEB_ECOLX
|
Mobilization protein MbeB
|
Escherichia
|
MSNLLQTGAEFEKKLKERAESTEKMLNNEFRRLGESVSEAVTSNETKIRDAIALFTASTEESLEKHREGVKEAMMQHRRDVLKLAGNTGMMLLGIVFLLFTASGGTLWYLGGRIQANLEEIRKQEETLQKLNAKTWGVEFVQDGNRKFLVLPYGKSAEVIPFQGKEWVHLKE
|
This protein is essential to promote the specific transfer of the plasmid in the presence of conjugative plasmids.
|
P13659
|
P57688
|
KDPC_THEAC
|
Potassium-translocating ATPase C chain
|
Thermoplasma
|
MKSYLKALVFAVLFLFILGFVYPTVTSLITEHALPFQSEGQPVEIDGHIYGSYLLAEAFNSSFFFHPRPSAIDYNLSESGSYDYSLGNPAMLNLTEKYLHRFLSENPGVNISEIPYAMISYSGSGLDPGIPLQGAIIQIPRISIAIHNITNLSVSDLYSYLYNLVNSTKTQNFPFFGSYYVNVVRLNVDIVEFLLKGGYISQSQI
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
|
P57688
|
Q21MS9
|
PDXA_SACD2
|
4-(phosphohydroxy)-L-threonine dehydrogenase
|
Saccharophagus
|
MSHPAIIALTPGEPAGIGPDLTVMAAQQARDYPLVALCDPQLLKDRAKLLGLPLTVSTYIQGSAVTTSAQHISVMPIPLGAPCEAGTLDSTNAAYVIETLKQATEGCLSGEFAAVVTGPVQKSVINEAGINFSGHTEYFADNSNTPRVVMMLATEGLRVALATTHLPLKDVSAAITTASLTETLNILLADLQLKFGLSQPRVLVCGLNPHAGEGGHLGMEEIDTIIPVLEQFRARGHNLVGPLPADTLFNPKYLSDADAVLAMYHDQGLPVLKYKGFGNAVNITLGLPFIRTSVDHGTALDLAGTGKANIGSLQVALGYAQNLAMQQASINEIAG
|
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
|
Q21MS9
|
P18834
|
COL14_CAEEL
|
Cuticle collagen 14
|
Caenorhabditis
|
MAKRARLRLILLAKLVSLKMSDEKEKRSLRPVAFVAVVFSTVAITSCLITFPLILHYIQTLESQVQLDLEFCQARARDMWKEMLDIETGGKKDSAKLANIVLNHRRLEKRDTLQDFWARRLHDQELRDQPVGYDNPSVGVESFNSEGGGCCTCHRGPPGPAGDGGRDGADGVDGTPGEIGPPGPPAPPGPDPHSLFPPQCPCEAPPGDGGPPGQPGPDGPPGAPGNAGEDGKPGDQGPRGPPGIPGAPGQPGRPGPPGEPGTYKTEVGPAGRAGAPGRPGPPGQPGPAGPPGENGKGGGQGPSGLPGPPGQPGQNGAPGEVGQPGDNGAPGSCDHCPPARLAPGY
|
Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment.
|
P18834
|
B5Y341
|
RSGA_KLEP3
|
Small ribosomal subunit biogenesis GTPase RsgA
|
Klebsiella
|
MSKNKLSKGQQRRVNANHQRRLKTTAEKADYDDNLFGETSEGIVISRFGMHADVESADGSVHRCNIRRTIRSLVTGDRVVWRPGKDAADGVNVKGIVEAVHERASVLTRPDFYDGVKPIAANIDQIVVVSAILPELSLNIIDRYLVACEAQDIEPLIVLNKIDLLDDDGLRFVNEQMDIYRNIGYRVLMVSSRTQDGLKPLEAALTDRISIFAGQSGVGKSSLLNALLGLNEDQILTNDVSDVSGLGQHTTTAARLYHFPHGGDVIDSPGVREFGLWHLEAEQITHGFVEFHDYLGHCKYRDCKHDNDPGCALREAVENGKIAESRFENYHRILESMEQVQVKTRKNFSSSDD
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
|
B5Y341
|
B1J1X7
|
GMHA_PSEPW
|
Sedoheptulose 7-phosphate isomerase
|
Pseudomonas
|
MDMQSRIRRLFQASIDTKQQAMDILAPHIEQASLVMVNALLNEGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTLTSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPSTVTARIQEVHLLAIHCLCDLIDSQLFGSEE
|
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
|
B1J1X7
|
Q84RF2
|
OPF17_ARATH
|
Ovate family protein 17
|
Arabidopsis
|
MRVKATLINFKSKLSKSCNRFVSLFRFRVKRPVFIRPLRARHGNVKPRHQHHHSKKPICSCLCFLNSSKNHKMSNAKHRSSSFSVNDDDYSKFMQSPLTPATAKKLFTSPITTPYSSRTRKSLNARDTFEDNAVEDACRSFENYLIHLIVEEGKIDDLMDIEELLFCWKNLKSPVFIELVSRFYGELCRDLFSGE
|
Transcriptional repressor that may regulate multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors.
|
Q84RF2
|
Q7U4J7
|
RL2_PARMW
|
50S ribosomal protein L2
|
Parasynechococcus marenigrum
|
MAIRNFRPYTPGTRTRVVTDFSEVTGRKPERSLVVSKHRRKGRNNRGVITCRHRGGGHKRLYRVVDFRRNKHGITAKVAAIHYDPHRNARLALLFYADGEKRYILAPAGVQVGQTVVSGPDAPIENGNAMPLSAVPLGSSVHCVELYAGRGGQMVRTAGASAQVMAKEGDYVALKLPSTEVRLVRRECYATLGEVGNSEVRNTSLGKAGRRRWLGRRPQVRGSVMNPCDHPHGGGEGRAPIGRSGPVTPWGKPALGLKTRKRNKPSNRYVLRKRRKTSKRSRGGRDS
|
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.
|
Q7U4J7
|
Q4VZH2
|
NDHJ_CUCSA
|
NADH-plastoquinone oxidoreductase subunit J
|
Cucumis
|
MQGNLSSWLVKHGLVHRSLGFDYQGIETLQIKPEEWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGIDQPEEVCIKVFAARINPRIPSVFWVWKSADFPERESYDMLGIYYDNHPRLKRILMPESWVGWPLRKDYIAPNFYEIQDAH
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q4VZH2
|
Q6MHJ5
|
PIF1_BDEBA
|
ATP-dependent DNA helicase pif1
|
Bdellovibrio
|
MNSESKCYRFYICFARLGSGMIAGLMPVHEIELSPEQASALDLLRSGENVFLTGGAGSGKSFLIRQFMRELDPKEMPILASTGAAAVLLGGRTFHSFFGLGIMEGGADATYERASKDKRLMSRLRKVEGVIIDEISMIPGQALMIAEALSQRARESKLPWGGMRVIAVGDFAQLPPVTHTGQRDWCFLNGVWEVSGFQTVMLSHNQRVSDNLFLDVLSDVRHGKVTERVREFLNEHVQDHDEDDPGTRLFPRKINAEKFNERKLAEIDETEVVIESIYSGSERHIETLKKASPIAEKLILKIGCQVMFLQNDPQRRWVNGTRGTVVDITADQITVRKDRGREVQVSKSSFAIQDAEGNIMAQVEQFPLTLAYATTIHKSQGATLDDLWCDLSQLWEPGQAYVALSRLRSAKGLHLIGWNPRSIIVDPKVLHFYKQFEGL
|
DNA-dependent ATPase and 5'-3' DNA helicase that efficiently unwinds G-quadruplex (G4) DNA structures. May be involved in resolving commom issues that arise during DNA replication, recombination, and repair.
|
Q6MHJ5
|
P41732
|
TSN7_HUMAN
|
Transmembrane 4 superfamily member 2
|
Homo
|
MASRRMETKPVITCLKTLLIIYSFVFWITGVILLAVGVWGKLTLGTYISLIAENSTNAPYVLIGTGTTIVVFGLFGCFATCRGSPWMLKLYAMFLSLVFLAELVAGISGFVFRHEIKDTFLRTYTDAMQTYNGNDERSRAVDHVQRSLSCCGVQNYTNWSTSPYFLEHGIPPSCCMNETDCNPQDLHNLTVAATKVNQKGCYDLVTSFMETNMGIIAGVAFGIAFSQLIGMLLACCLSRFITANQYEMV
|
May be involved in cell proliferation and cell motility.
|
P41732
|
A9WSE6
|
RUVC_RENSM
|
Holliday junction resolvase RuvC
|
Renibacterium
|
MRVFGVDPGLTRCGFGVVDVAANRSASLVAVGVIGSSSELPLSQRLLVISESIDQWLDTHSPDVLAVERVFSQTNLSTVMGVAQASGIVIAAAAKRGIAVALHTPSEVKAAVTGNGRADKIAVTAMVTRILKLKVAPTPADAADALALAITHAWRSGPGSTAAAGELTPARKLWLEAEAKARKNVEKSSKQRR
|
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.
|
A9WSE6
|
Q02548
|
PAX5_HUMAN
|
B-cell-specific transcription factor
|
Homo
|
MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQTTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTLPGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPYYYSAAARGAAPPAAATAYDRH
|
(Microbial infection) Plays an essential role in the maintenance of Epstein-Barr virus genome copy number within the host cell by promoting EBNA1/oriP-dependent binding and transcription . Participates also in the inhibition of lytic EBV reactivation by modulating viral BZLF1 activity .
|
Q02548
|
A5GTY4
|
PSBA1_SYNR3
|
Photosystem II Q(B) protein 1
|
unclassified Synechococcus
|
MQTTIQQRSGASAWQQFCEWVTSTDNRLYVGWFGVLMIPTLLAATTCFIVAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPFQLVIFHFLIGIYAYMGREWELSYRLGMRPWICIAYSAPVAAASAVFLVYPFGQGSFSDAMPLGISGTFNYMLVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTESESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGVSTMAFNLNGFNFNQSILDSQGRVLNTWADILNRAGLGMEVMHERNAHNFPLDLAAAESAPVALQAPAIG
|
Photosystem II (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. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
A5GTY4
|
Q9UTC3
|
PSF3_SCHPO
|
DNA replication complex GINS protein psf3
|
Schizosaccharomyces
|
MDYYDIDSILSENQKVPCTSTVSIPGLGHEGRMVPTGSKVELPFWLAEVLAINSFVSIHMPAPFSSVVRNALKANPNSVSIRDITTHYYHFAEKMLHLISDDSLVQISLNTLRSRAMLIADASLNPQGALQQNSQFIEGLDDFEKHILRVSHNAHRSLINWQNSTS
|
The GINS complex plays an essential role in the initiation of DNA replication.
|
Q9UTC3
|
B7V5C7
|
UBID_PSEA8
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Pseudomonas
|
MTFKDLRDFIAQLEQRGALKRIQVPISPVLEMTEVCDRTLRAKGPALLFEKPTGFDMPVLGNLFGTPERVALGMGAEDVGALREIGKLLAQLKEPEPPKGLKDAWAKLPMYRKVLSMAPKVLKDAPCQEVVEEGEDVDLGRLPVQTCWPGDVGPLITWGLTVTRGPNKERQNLGIYRQQVIGRNKVIMRWLSHRGGALDYREWCQKHPGQPYPVAVALGADPATILGAVTPVPDTLSEYAFAGLLRGHRTELVKCRGSDLQVPASAEIVLEGVIHPGEMADEGPYGDHTGYYNEVDRFPVFTVERVTRRQKPIYHSTYTGRPPDEPAILGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMLGVWSFLRQFMYTKFVIVTDDDIDARDWNDVIWAITTRMDPKRDTVMIDNTPIDYLDFASPVSGLGSKMGLDATHKWPGETSREWGRAIVKDEAVTRRIDALWSSLGID
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
B7V5C7
|
A4VTL1
|
SEPF_STRSY
|
Cell division protein SepF
|
Streptococcus
|
MALKDTFKNLFNYFEVDEVNEVEEQADAYSMPNDRPKMRVANTTVAPVREQQPKVETRREARSESQLQRLHERQQELMTNNNEKEIVKTTIDIKFPKRYEDAPEMVNLLLDNASILIDFQYMSEQQARRCLDYLDGARSVLSGNLKKVSNTMWLLTPVNVTVNIEELRNAGTTTGVADSNFEFDIKR
|
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
|
A4VTL1
|
O88413
|
TULP3_MOUSE
|
Tubby-like protein 3
|
Mus
|
MEAARCAPGPRGDSAFDDETLRLRQLKLDNQRALLEKKQRKKRLEPLMVQPNPEARLRRLKPRGSEEHTPLVDPQMPRSDVILHGIDGPAAFLKPEAQDLESKPQVLSVGSPAPEEGTEGSADGESPEETAPKPDLQEILQKHGILSSVNYDEEPDKEEDEGGNLSSPSARSEESAAASQKAASETGASGVTAQQGDAQLGEVENLEDFAYSPAPRGVTVKCKVTRDKKGMDRGLFPTYYMHLEREENRKIFLLAGRKRKKSKTSNYLVSTDPTDLSREGESYIGKLRSNLMGTKFTVYDHGVNPVKAQGLVEKAHTRQELAAICYETNVLGFKGPRKMSVIIPGMNMNHERIPFRPRNEHESLLSKWQNKSMENLIELHNKAPVWNDDTQSYVLNFHGRVTQASVKNFQIVHGNDPDYIVMQFGRVADDVFTLDYNYPLCALQAFAIGLSSFDSKLACE
|
Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. Not involved in ciliogenesis. During adipogenesis, regulates ciliary trafficking of FFAR4 in preadipocytes.
|
O88413
|
D2Z025
|
DCSB_STRLA
|
hydroxyarginase
|
Streptomyces
|
MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDDWSVALPQARETLVAVREAATESIKGDNLTVLVNNTCSVSLATLPVVAREHPDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQAVLVGSRDIDEGERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWDVLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELAELNAPADSERAEQAVAVILDMVAPAFDAAAARP
|
Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the hydrolysis of N(omega)-hydroxy-L-arginine (NHA) to yield hydroxyurea (HU) and L-ornithine.
|
D2Z025
|
Q5ZM55
|
FEM1B_CHICK
|
FEM1-beta
|
Gallus
|
MEGLAGYVYKAASEGRVLTLAALLLNRSESDIKYLLGYVSQHGGQRSTPLIIAARNGHTKVVRLLLEHYRVQTQQTGTVRFDGFVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQHADPNAKAHCGATALHFAAEAGHLEIVRELVKWKAAMMVNGHGMTPLKVAAESCKADVVELLLAHAGCNRRSRIEALELLGASFANDRENYDIMKTYHYLYLAMLERYRDSENIIEKEVLPPIEAYGNRTECRTPQELESIRQDRDALHMEGLIVRERILGSDNIDVSHPIIYRGAVYADNMEFEQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNEPVKAKDIESVLRCSVLEIEQGMSRIKATQDDDIHTAVDNYECNIFTFLYLVCISTKTQCSEEDQSRINKQIYNLIHLDPRTRDGSTLLHHAVNSSTPVDDFHTNDVCSFPNALVTKLLLDCGADVNAVDNEGNSPLHLIVQYHRPISDFLTLHSIIISLVEAGAHTDMTNKQKKTPLDKSTTGVSEILLKTQMKLSLKCLAARAVRIYNISYQNQIPRTLEEFVKFH
|
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1B) complex specifically recognizes proteins ending with -Gly-Leu-Asp-Arg, leading to their ubiquitination and degradation.
|
Q5ZM55
|
Q8WHM7
|
MATK_SPIIN
|
Intron maturase
|
Spirodela
|
MEEFKGYLQKGGFKQQHFLYPLLFQEYIYVLAHDHGLNVNASTLNEPSEISGYDNKSSLLLVKRLITRIYQQNSLIHSVNDSNQNRFVGHNNNFYYKMISEGFAIVVEIPFSLRLISSLKEKKEIPKSQNLRSIHSIFSFLEDKFAHLNYVSDILIPYPVHLEILVQILQCWIQDVPSLHLLRFLFHEYHNGNNCITPKKSSYGFSKDNPRLYRFLYNSYVVECESIFVFLRKSSSYLQSTSFGTLLERTYFYGKIKHIGVTHSNDFQKTLWLFKDPFMHYVRYQGKSIMASKGTHLLMKKWKSYFVNLWQCHFHFWSQPSRIHINQFSHFSFYFLGYLSSVPINRSSVKSQMLENSFLIDTVTKKFETMVSIIPMIGSLSKAKFCNLSGNPISKPVWADLSDSDIIDRFGRICRNLSHYYSGSSKKQSLYRIKYILRLSCARTLARKHKSTVRAFLQRLGSEFLEEFFMEEEKVLSLMLPRTSYSLHKLYREPIWYLDIIRINDLVNHL
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q8WHM7
|
B8EBJ3
|
RL5_SHEB2
|
50S ribosomal protein L5
|
Shewanella
|
MAKLHDKYQETVVAELAKKFGYTSVMQVPRIEKITLNMGVGEAVADKKIMDHAVRDMTAIAGQKPVVTVARKSVAGFKIREGYPIGCKVTLRGERMWEFLERLVDIAIPRIRDFRGLSAKAFDGRGNYAMGVREQIIFPEIDYDKIDKIRGMDIVITTTAKNDEEGRALLDAFNFPFKK
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
B8EBJ3
|
A1SME0
|
CLPX_NOCSJ
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Nocardioides
|
MARIGDGGDLLKCSFCGKSQKQVKKLIAGPGVYICDECIDLCNEIIEEELSEGAEVSLDELPKPKEIFEFLNSYVIGQEQAKKSLAVAVYNHYKRVQAGLQPMSGKHSKEEVVEVAKSNILVIGPTGCGKTYLAQTLARMLNVPFAIADATALTEAGYVGEDVENILLKLIQAADYDVKKAETGIIYIDEIDKVARKAENPSITRDVSGEGVQQALLKIIEGTTASVPPQGGRKHPHQEFIQIDTTNILFVVGGAFAGLEHIIEQRVGKKTLGFTAEVRGKAEREAEDLLAQVRPEDLTKFGLIPEFIGRLPLIASVSKLDQEALVQILTEPRNALVKQYQKLFELDGVELEFTPDAIEAIADNALERGTGARGLRAIIEEVLLHVMYDVPSRGDIAKVIVTREVVMDGVSPTLIPRESEKKKKSA
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
A1SME0
|
P45167
|
UUPL_HAEIN
|
ATP-binding protein Uup-like
|
Haemophilus
|
MEAIEWLENFLLDFQGSIVFISHDRSVIRKMATRIVDLDRGQLQSYLGNYDLYLTTKEENLRVEALQNELFDKRLAQEDVWIRQGIKARRTRNEGRVRALKAMREERRQRREVMGTAKLQLDTSSRSGKIVFEMEDVSYEIAGKTLLKDFSTTILRGDKIALVGPNGCGKTTFIKLLLGEIQPTSGKIRCGTKLEIAYFDQYRADLDPEKIVMDNVADGKQDIEINGVKRHVLGYLQEFLFPPKRAMTPVKALSGGERNRLLLAKLLLKPNNLLILDEPTNDLDVETLELLEEILTDYQGTLLIVSHDRQFIDNTATECYLFEGEGRLNKYVGGFFDAKQQQANFWASKAVEEQAKAKKSEPLKEESAVKNDRTSKPKSVKLSYKEQRELEQLPQLLEELETKITTLQAEIADPAFFQQAHDITDAKLKALADTEAELETAFLRWEELEEKKNLADGKA
|
Might play a role in ribosome assembly or function; this is missing the first ABC transporter domain compared to paralogs.
|
P45167
|
A5U036
|
RL10_MYCTA
|
50S ribosomal protein L10
|
Mycobacterium tuberculosis complex
|
MARADKATAVADIAAQFKESTATLITEYRGLTVANLAELRRSLTGSATYAVAKNTLIKRAASEAGIEGLDELFVGPTAIAFVTGEPVDAAKAIKTFAKEHKALVIKGGYMDGHPLTVAEVERIADLESREVLLAKLAGAMKGNLAKAAGLFNAPASQLARLAAALQEKKACPGPDSAE
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
A5U036
|
I0B6F5
|
CYC8_CHACT
|
Cyclotide chaC8
|
Chassalia
|
MAKFANYLMLFLLVASLVMLEAQSSDTIKAPDWGKRLLMNHDSDLGAIPCGESCVWIPCISTVIGCSCSNKVCYR
|
Probably participates in a plant defense mechanism (Probable). Active against E.coli ATTC25922 but not against S.aureus ATCC 12600 or S.epidermidis ATCC 14990 . Has cytotoxic and hemolytic activity .
|
I0B6F5
|
Q9HKT2
|
LPLAC_THEAC
|
Lipoate--protein ligase subunit 2
|
Thermoplasma
|
MVLNYTMHMMYSKNWKAKKGLIRVTLDLDGNRIKDIHISGDFFMFPEDSINRLEDMLRGSSIEKINDIIRDFYNQGVITPGVEPEDFIQALRVI
|
Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.
|
Q9HKT2
|
F1S5L4
|
GPAT1_PIG
|
Glycerol-3-phosphate acyltransferase 1, mitochondrial
|
Sus
|
MDESALTLGTIDVSYLPNSSEYSIGRCKHASEEWGECGFRPPVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDRFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATEMNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGQKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNTIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSDAVDEGTDMSINESRNAADESFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCITITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGSGGPASPSLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILTVAEQDDQEDISPSLAEQHWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFIHNFSGPVPEPEYLQKLHKYLINRTERRVAVYAESATYCLVKNAVKMFKDIGVFKETKQKKVSVLELSSTFLPQCNRQKLLEYILSFVVL
|
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids.
|
F1S5L4
|
Q9XIC5
|
NAC17_ARATH
|
Protein REGULATORS OF AOX1A 2
|
Arabidopsis
|
MADSSPDSCFKGGKFSAPGFRFHPTDEELVMYYLKRKICRKRLRVNVIGVVDVYKMDPEELPGQSMLKTGDRQWFYFTPRSRKYPNAARSNRGTENGYWKATGKDRVIEYNSRSVGLKKTLVFYRGRAPSGERTDWVMHEYTMDEDELGRCKNPQEYYALYKLFKKSGAGPKNGEQYGAPFQEEEWVDDDNEDVNAIAVAVPEQPVVRYEDARRVDERRLFNPVILQLEDIDELLNGIPNAPGVPQRCIPQVNSEEELQSTLVNNSAREFLPNGQQYNRPSSFDSLETAEVTSAPLVFEKEDFIEMDDLLLIPEFGASSTEKAAQFSNHGEFDDFNEFDQLFHDVSMSLDMEPIDQGTSANLSSLSDSANYTSDQKQQLLYQQFQDQTPENQLNNIMDPSTTLNQITSDIWFEDDQAILFDQQQSFSGAFASPSSGVMPDSTNPTMSVNAQGHEIQNGGGTTSQFSSALWALMDSIPSTPASACEGPLNRTFVRMSSFSRMRFNGKANGTPVSTTIAKKGIRNRGFLLLSIVGALCAIFWVLVATVRVSGRSLLLKD
|
Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Transcriptional activator that acts as positive regulator of AOX1A during mitochondrial dysfunction. Binds directly to AOX1A promoter. Mediates mitochondrial retrograde signaling.
|
Q9XIC5
|
A0JZA2
|
RL1_ARTS2
|
50S ribosomal protein L1
|
Arthrobacter
|
MAKRSKAYEAAAAKIDAEKFYAPFEAVTLAKDTNPSKFDATVEVAFRLGVDPRKADQMVRGTVNLPHGTGKVARVLVFATGDKAEAAIAAGADFVGSDDLIEKIAAGWTDFDAAVATPDLMGKVGRLGKVLGPRNLMPNPKTGTVTPDVTKAVNDIKGGKIDFRVDKHSNLHFIIGKVSFDAIKLAENYAAALEEVLRLKPSASKGRYIQKATVATTFGPGISVDPNVTKVLTEV
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
A0JZA2
|
A9WH80
|
RS8_CHLAA
|
30S ribosomal protein S8
|
Chloroflexus
|
MSVNDPIGDMLTRIRNACMARHTTVSMPASNMKEAIARILKREGFIRDYAVIDDGKSHKTITITLKYLPDRRPAITGLRRVSKPGLRIYTKRTDIPRVRGGLGLCILSTPKGVLADHEAWRERVGGEVLCYVW
|
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.
|
A9WH80
|
Q65VU4
|
NQRA_MANSM
|
NQR-1 subunit A
|
Basfia
|
MITIKKGLDLPINGKPEQVIRDGNAVTEVALLGEEYVGMRPSMKIHEGDTVKKGQILFEDKKNPGVVFTAPVSGTVTAINRGAKRVLQSVVIRVEGNDQETFAKYSPAELVSLSSEQVRQNLQTSGLWTALRTRPLSKIPAVDAVPSSIFVNAMDTNPLCADPAVIINEYQADFTNGLTVLTRLHNKVNLCKAAGSNIASVDNVDSHEFAGVHPAGLVGTHIHFIDPVGINKSVWHINYQDVIAIGKLFTTGELFTDRVVALAGPQVKNPRLVRTNIGANLSQLTANELADGNNRVISGSVLYGAKAEGAHDYLGRYALQVSVIAEDTEKEFFGWISPQANKYSITRTVLGHFGRKLFNFTTAENGGHRAMVPIGSYERVMPLDILPTLLLRDLEVGDTDSAQALGALELDEEDLALCTFVCPGKADYGSFLRQALDKIEKEG
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
|
Q65VU4
|
Q9JZ38
|
CLPP_NEIMB
|
Endopeptidase Clp
|
Neisseria
|
MSFDNYLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVAQLLFLESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQAASMGAFLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELLKIKEKLNRLMAKHCDRDLADLERDTDRDNFMSAEEAKEYGLIDQILENRASLRL
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q9JZ38
|
C0Q0Y1
|
SYM_SALPC
|
Methionyl-tRNA synthetase
|
Salmonella
|
MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSADQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWKKDSDAELYHFIGKDIVYFHSLFWPAMLEGSHFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLKHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLAAELADPQLYKTFTDAAAVIGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPTLSERVEAFLNSELNWDAIEQPLLSHKVNTFKALYNRIDMKQVEALVEASKEEVKAAAAPVTGPLADFPIQETITFDDFAKIDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSSYPDPQALIGRQTVMVANLAPRKMRFGVSEGMVMAAGPGGKDIFLLSPDDGAKPGQQVK
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
C0Q0Y1
|
C8V7P3
|
IVOC_EMENI
|
Ivory mutation-related protein C
|
Aspergillus subgen. Nidulantes
|
MLSLDLVFSFPAWALLLVLTLLYTLYLATTRLLLSPIRHIPGPTLAALSFWPEFYYDVVQRGQYFRQIDKMHQTYGPLVRINPFEIHIQDPSFYPVLYTGPTRRRHKWLWAARMFGNNTSAFATVRHEHHRLRRSALNPLFSKSAIQRLTPHLQHTLARLCSRLDGFAFTRQDVDLGIGLTAFAADVITEYCFGQSLELIGKDNFGKEWIDMVSAPSELGHLVKQCPWILVVCKWAPKALVRALLPGVALLFQIQERMSAQIQPLVDRAAAVDKPADPLTVFDFLLSSTLPQHEKTVDRLKGEGQTLIGAGTLTTGNALKTIIFHVLNDPDIFRKLRAEVDGALENMDILSMSDTAYLERLPYLSACIKEGLRISYGVTHRLQLIAEEPLIYSGVTIPAGTPVGMTSIFMHDNPVVFPQPREFRPERWFEADFETVQAMNRHFVPFSKGSRMCLGMNLAYAEIYLVLAVLFRRYEISLSGVTREDIEMAHDFFDPAPKEGARGLIVQLQKRG
|
Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment . The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion . While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function . D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC . N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment .
|
C8V7P3
|
B9IW60
|
DAPEL_BACCQ
|
N-acetyldiaminopimelate deacetylase
|
Bacillus cereus group
|
MVVSKFVQIRRDLHKIPEIGFKEWKTQRYILDYIGTLSNEHVEVKVWRTGVIVKVKGKNPEKVIGYRADIDGLPITEETGYEFASVHEGMMHACGHDLHTTIGLGLLTAAVTERIDDDLVFLFQPAEEGPGGALPMLESEELKEWKPNIILGLHIAPEYPVGTIATKEGLLFANTSELYVDLKGKGGHAAYPHTANDMIVAASHLVTQLQSVISRNVNPLDSAVITIGKITGGTVQNIIAEKSRLEGTIRTLSVESMSRVKSRIEGIVAGIEASFQCEAIIDYGAMYHQVYNHEALTREFMQFVSEQTDMKVITCTEAMTGEDFGYMLQEIPGFMFWLGVNSEYGLHHAKLKPDEEAIEKAIVFLDQYVKWKGTRK
|
Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
|
B9IW60
|
Q73G09
|
PDXH_WOLPM
|
Pyridoxal 5'-phosphate synthase
|
unclassified Wolbachia
|
MAVALIFATRARIKILFFDMIFSLEKDPFDLFSKWYKAVLNSPCEQPTAMTLATCSKDCIPSARVVLLKEYSKEGFVFFTNVNSKKGKELTENPKAALVFHWIEFARQVRIEGEVKLLNDERTDKYFSSRALGSQISAWCSKQSSILKDWQDFEQAIKLKEKEFHNTQVSRPDFWVGFCVIPKVIEFWQEGEYRKHIRFRYTLVEGSDWKVEQLYP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
Q73G09
|
B2A3L2
|
RLMH_NATTJ
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Natranaerobius
|
MKFRVVAVGKIKEKYLIRGIEEYQKRLRPYTGLEITEVKDSVLPNKLYQAEIEKVLIEEENRIKSKLSSRDYIIALDSEGSQFTSENFAQQIENLTLEGINQFTFIIGGTLGLSNSLKKEANMLLSFSKFTFPHQLMRLILTEQLYRAIKIIHNEPYHY
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
B2A3L2
|
Q7U322
|
MURG_HELHP
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Helicobacter
|
MFAITGGGTGGHLAIAKALAQEAQKNNQQSIYIGSQIGQDKTWFEGSSLFTHCYFLDSTGVVNKKGLGKIKAIFKQLKAAWEARNILKKHKIEYVISVGGFSAGGASIGAILSNTPLFIHEQNAIKGKLNEILTPFAKAIFGSFEGKSKNFIHTSYPVRDEFFTHSRVREKLHHLLFLGGSQGAKGINDFALQIVPELLKRGITIAHQCGERDFERIKKAYEHIGILDKVDVFAFDKEIVLRLQKADLCIARSGASSLWEMSANGLIGIFVPYPYAAKDHQYYNALHFTKQGLGLLLRESQLDMLRVFTFIESLQKQEDSLSEKSHLLMSKIQPNGAKEILEHITSLMSH
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
Q7U322
|
P36955
|
PEDF_HUMAN
|
Serpin F1
|
Homo
|
MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP
|
Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
|
P36955
|
B7VI55
|
HFQ_VIBA3
|
RNA-binding protein Hfq
|
Vibrio
|
MAKGQSLQDPFLNALRRERIPVSIYLVNGIKLQGQIESFDQFVILLKNTVNQMVYKHAISTVVPARAVSHHSGEQQRAPSDRPEKTED
|
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.
|
B7VI55
|
Q5FPL0
|
GUAA_GLUOX
|
Glutamine amidotransferase
|
Gluconobacter
|
MTLTQQDASTVEKLDETLHEDRILILDFGSQVTQLIARRVRESGVYCEIWPFTATEEKIRAFNPRGIILSGSPASVHDENAPPIPNVVFALNRPVLGICYGQQAMCQMLGGKVESHEHREFGRAYIDIAEDCSLFRGVWARGKREQVWMSHGDRVTQLPPGFRAVAHSEGAPFAIIADEGRRLYGVQFHPEVVHTPHGAALIRNFTHNVAGCSGTWTMAGFRELEIARIRKQVGSGRVICGLSGGVDSSVAAKLIHDAIGDQLTCIFVDPGIMRTGEADEVVKTFRGRFNIRLVHRDASELFLKELAGVTDPETKRKTIGRLFIEVFEEEAAKLGGAQFLAQGTLYPDVIESVSFSGGPSVTIKSHHNVGGLPDRMNMELVEPLRELFKDEVRMLGRELGIPESIVGRHPFPGPGLAIRIPGDVTKEKLDLLRKVDAIYLEEIRRAGLYDAIWQAFAVLLPVRTVGVMGDGRTYDQACALRAVTSTDGMTAEVYPFDFAFLNRVAGRIVNEVRGINRVTYDITSKPPGTIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q5FPL0
|
Q5B8A3
|
PKFD_EMENI
|
Aspernidine A biosynthesis cluster protein pkfD
|
Aspergillus subgen. Nidulantes
|
MGSLWSSPSLLPSQQDNETEPFSHLPKEIGTDPTLREDSNVSNRNSEAASTSTDSSTNTNENHASTSQSSLEGAPDSGPIKIAIIGGGIIGIITALGLIHRGINVTVYERAPKYTETSAGFSFSKGARKAMEIVSPRVLEALLRVAAPNKHPFIRYFDGFTPGADEAQWQIPAERPDYYGCLRAAFLESLGQEVPEGIVKFGKVLESYEDNEEGKVLLRFRDGSTAEVDAVIGCDGIKSRTRRIMLGDTHPAAAPGYTEIVAYRAVLPLEGVVAALGEDRGHSHCLAVGPDAYTVSYPIANKPLANMILFRKQRGSWANSDKLLETCHRSTAQDAVKDWKPEIQRLVDLLPENPNKWAIFDTSDNPVPSYVSASGRVCIAGDAAHASTPFLASGAAMGVEDAAVLATVLNTALKEQSYNKTTVVKRKAITAAFQAYSGIRMQRSQRVVKDSRTVGEVCMWQDAETARDPEKCFQAIWQRYTQIWEFDVEEMVERARSECVRLFS
|
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
|
Q5B8A3
|
A1JRE8
|
MDTJ_YERE8
|
Spermidine export protein MdtJ
|
Yersinia
|
MMIYWIFLGLAIVAEIIGTLSMKYASVSGELTGHIVMYFMITGSYIMLALAVKKVALGVAYALWEGIGILIITVFSVLWFDESLSPLKIAGLVTLVGGIMLVKSGTRKPKKPNSPNRNSGEHHATA
|
Catalyzes the excretion of spermidine.
|
A1JRE8
|
Q47ZE0
|
FOLD1_COLP3
|
Methenyltetrahydrofolate cyclohydrolase
|
Colwellia
|
MSALILDGKSVTKKSEEDLRSRVARLKELSNGAVPILATILVGNDPSSATYVKMKSNACTRVGMDSLKVEMSEETTTEELLAEIAKLNANPNIHGILLQHPVPPQINERQCFDSIDLSKDVDGVTCWGFGRMAMNETSYGSATPKGIIRILEAYDIQLEGKHAVVVGRSPILGKPMAMMLLNKNCTVTICHSKTVGLDKIIKTADIVVGAVGKPEFIKADWIKDDAVVIDAGYHEGGIGDIELQPLMSRVKAYTPVPGGVGPMTINTLIYQTVEACELKLAQ
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q47ZE0
|
A4XKI9
|
YBEY_CALS8
|
Endoribonuclease YbeY
|
Caldicellulosiruptor
|
MKIIIQNQQDKYQIDESISKIIEDSVLNTLKIFMDDENYEISVMIVDNQFIKELNKHYRSIDKETDVLSFPIFEFKNGELQEDIAIVEEEIPLGDIVISIEKAYEQAKEFGHSVEREIAYLTVHSVLHLLGFDHIEEEDRMLMRKYEEMVLEGMGLTR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A4XKI9
|
Q46A53
|
FOLD_METBF
|
Methenyltetrahydrofolate cyclohydrolase
|
Methanosarcina
|
MLDEGYESRIIDGKVLAKKIEDEVRSGVEALVSGRGITPGLATVLVGDDPASKMYVRLKHRACERVGIQAEDHFLPAETSQEELISLINTLNKDQNVHGILLQLPLPKHLFPQEAMEAIAPEKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYNVPVKGKNVVIVGHSNVVGKPLAAMFLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEKDGVYGDVDFENVIKKAALITPVPGGVGPLTVAMLMKHVLGCAETNY
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q46A53
|
Q0TPJ9
|
DER_CLOP1
|
GTP-binding protein EngA
|
Clostridium
|
MSKPIVAMVGRPNVGKSTLFNKLAGKRISIVQDTPGVTRDRVYAESEWLNRKFTMIDTGGIEPESSDIIVKQMRRQAQIAIEMADVIVFVVDGKEGLTAADQEVAQMLRKSKKPVVLVVNKIDRLALEENSYEFYNLGIGDPITISASQGLGLGDMLDEVVKYFNDPSEDEEDDEYIRIAMIGKPNVGKSSLINRLLGEERVIVSNVPGTTRDSIDSYLETEDGKFILVDTAGLRRKSKVKEEIERYSVIRTYAAIEKADVAILVIDAEQGITEQDEKIIGYAHEMNKAIMVVVNKWDLIEKDDKTLSNYQKDLQQKLKFMPYAKYLFISALTGQRVHKILSTAKYCYDNYSKRVSTGLLNDVISKAVLMKEPPVVALKRLKIYYATQVATKPPKFVFFVNDPNLLHFSYGRYLENQLRESFDFDGTGIEIEYRARKE
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q0TPJ9
|
P16362
|
CYB_POMSU
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Pomatostomus
|
TALLLAAHYTADTSLAFASVTHMCRNVQFGWLIRNLHANGASFFFICIYLHIGRGLYYGSYLNKETWNIGVILLLTLMA
|
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.
|
P16362
|
A7MXE5
|
RL11_VIBC1
|
50S ribosomal protein L11
|
Vibrio
|
MAKKVEAYIKLQVAAGMANPSPPVGPALGQHGVNIMEFCKAFNAKTESLEKGLPTPVVITVYNDRSFTFVTKTPPAAVLLKKAAGVKSGSGRPNTEKVGTVTDAQIQEIAETKAADMTGADIEAMKRSIAGTARSMGLVVEG
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
A7MXE5
|
B7N727
|
SYDP_ECOLU
|
Protein Syd
|
Escherichia
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRAHLASNLAEFLNQLKPLL
|
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
|
B7N727
|
Q4WJ90
|
ACON2_ASPFU
|
Aconitase 2
|
Aspergillus subgen. Fumigati
|
MVRQLVWQRATASRRLAPKCLSPQQLFARRGLATEASAARMPPYPKIVRNLEQVRKVLGSSRALTLAEKILYAHLDNAEESLLTGTNNGKDIRGKANLKLKPDRVAMQDASAQMALLQFMSCGLPSTAVPASIHCDHMIVGERGADTDLPASIEGNREVFDFLESAAKRYGIEFWPPGAGIIHQSVLENYAAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALVDAPWELKAPRILGVRLEGRLSGWASPKDIILHLAGKLTVRGGTGYVIEYHGPGVETLSCTGMATCCNMGAEVGATTSVFPFSPSMVPYLQATHRGHVAQAAAEIAASGPKNLLRADDGAEYDQLITIDLSTLEPHVNGPFTPDLSVRLSDFANTVRENKWPETLGAGLIGSCTNSSYEDMTRAEDLVKQASAAGLKPKADFFITPGSEQIRATLDRDQTLASFSEAGGTVLANACGPCIGQWKRTDGVAKGEDNAIFTSYNRNFPGRNDGNRRTMNFLASPEIVTALAYSGSTTFNPMTDTLKTPSGEEFKFRPPQGSDLPSAGFADGNPALQPSAGVPDASVEVIVSPTSERLALLEPFAPFPEGELSGLKVLYKVKGQCTTDTISAAGPWLKYKGHLPNISANTLIGAVNAATGETNVAYDDAGNKHSIPDLAARWKADGIEWLVVAEDNYGEGSAREHAALQPRYLGGRIIVAKSFARIHETNLKKQGVVPLTFADKADYDRIDACDQVDTVGLYETLQSGGQGSIQLQVTKKSGEKLTIPVNHTLSKDQCGFILAGSALNLLAKRAHQ
|
Has no detectable activity towards cis-acontiate or cis-homoaconitate.
|
Q4WJ90
|
Q7WZY5
|
NREB_STACT
|
Nitrogen regulation protein B
|
Staphylococcus
|
MKSISNRDKLQDLLTQYYLNTNEKMVFLNSTGEVIALNEAAEEVFADDNDYSQMTNAVCRRCEGYSNEYDIMSCENCFLEALEIGKGSFQVFIRTKDNKIQPYTASYELIDHEKGIYAFTLHNVSPQIQRQERMYQRKMMQKTISAQENERKRISRELHDGIVQELINVDVELRLLKYQQDKDELIDNSKRIEGIMSRLIDDVRNLSVELRPSSLDDLGLDAAFRSYFKQFEKNYGIHVNYHTNFSAQRFDNEIETVVYRVVQEALFNALKYAQVDIVEVSLQLNENNIIAEVSDRGVGFKRGDDPKGTGLGLFGMNERAELVNGTVNIDSQINRGTIVTLEVPITD
|
Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
|
Q7WZY5
|
B9KIN8
|
TRUA_ANAMF
|
tRNA-uridine isomerase I
|
Anaplasma
|
MRYRAVVEYDGTAFIGWQRQKGVAGRSVQESIEDAIYRLSQQHVTVFAAGRTDAGVHALGQVVHFDLNTSLQDYVIKNALNHYLRSDMVSILSLEEAAEGFHARFSAKKRHYMYKIVNRDAPPCLDRLRMWHVPKQLNVSDMQEAASHMVGEKKDFASFRAKECQSKSSVRTVDRIDCVREGNNIFVHVSAKSFLHKQVRIIVGTLVQCGHGAFPPSYVLEILERKNRAAAGITAPPHGLYLVLVEY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
B9KIN8
|
Subsets and Splits
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