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
|
|---|---|---|---|---|---|---|
P17124
|
HRH2_CANLF
|
Gastric receptor I
|
Canis
|
MISNGTGSSFCLDSPPCRITVSVVLTVLILITIAGNVVVCLAVGLNRRLRSLTNCFIVSLAITDLLLGLLVLPFSAFYQLSCRWSFGKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVTDPLRYPVLITPVRVAVSLVLIWVISITLSFLSIHLGWNSRNETSSFNHTIPKCKVQVNLVYGLVDGLVTFYLPLLVMCITYYRIFKIARDQAKRIHHMGSWKAATIGEHKATVTLAAVMGAFIICWFPYFTVFVYRGLKGDDAINEAFEAVVLWLGYANSALNPILYATLNRDFRTAYQQLFRCRPASHNAQETSLRSNSSQLARNQSREPMRQEEKPLKLQVWSGTEVTAPRGATDR
|
The H2 subclass of histamine receptors mediates gastric acid secretion. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
|
P17124
|
A7GS78
|
NAGB_BACCN
|
Glucosamine-6-phosphate isomerase
|
Bacillus cereus group
|
MNILVVESQEKLAEAGYKLIENVVKSKGNPTLGMATGSSPLGIYAEIRKNKLDTSHVTTVNLDEYVNLPHEDKNSYHYFMKEQLFDHLPFKATYVPNGMANDLEEECNRYEGILAANPVDLQILGIGENGHIGFNEPGTPFHSRTHIVELTESTRQANRRFFEKEEDVPTHAITMGIGSIMKAKQILLVAMGPKKAEAVKELLQGEYSEACPATVLQRHPNVTVIADQEALSLCSEAIADEHRQVFTISDLLSDSRVGETAN
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
|
A7GS78
|
P29193
|
CAPP1_SACHY
|
Phosphoenolpyruvate carboxylase, housekeeping isozyme
|
unclassified Saccharum
|
MARNAVDKATSIDAQLRLLAPQKLSDDDKLVEYDALLLDRFLDILQDLHGEDIRETVQECYELAAEYENKLDPKMLDEIGNVLTSLDPGDSIVITKSFSHMLILANLAEEVQIAYRRRIKLKKGDFVDENSATTESDIEETLKRLMHQLKKSPLEVFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRNCLTQLYAKDITPDEKQELDEALQREIQAAFRTDEIRRAPPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGINERLPYNAPIIQFSSWMGGDRDGNPRVTPEITRDVCLLARMMAANLYNAQIEDLMFELSMWRCSDELRVKVDELHRSSKKDTTKHYIEFWKQVPPSEPYRVILSDVRDKLYNTRERARHLLASGFSEIPEEATFTDVEQFLEPLELCYRSLCACGDRSVADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVMDAITEYLGIGSYRKWTEEKRQEWLLSELNGKRPLFGPDLPKSDEIADVLDTFHVLAELPSDSFGAYVISMATAPSDVLAVELLQRECHVKKPLRVVPLFEKLADLEAAPAALARLFSVEWYRNRINGKQEVMIGYSDSGKDAGRFSAAWQLYKAQEELINVAKLYGVKLTMFHGRGGTVGRGGGPTHLAILSQPPETIHGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMHPPISPKPEWRALMDEMAIVATKEYRSIVFEEPRFVEYFRLATPEMEYGRMNIGSRPSKRKPSAGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFKHVLDKDIRNLQTLQEMYNQWPFFRVTIDLVEMVFAKGDPGIAALYDKLLVSEDLWSFGKRLRANYEETKQLLLQVAGHKDLLEGDPYLKQRLRIRDSYITALNVCQAYMLKRIRDPGFQVNPGPHLSKDIMDMGKPASELVKLNTTSEYAPGLEDTLILTMKGIAAGMQNTG
|
Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
|
P29193
|
Q2KDA1
|
RNPH_RHIEC
|
tRNA nucleotidyltransferase
|
Rhizobium
|
MRPSGRKTDQMRKVSFERNFSKHAEGSCLVKFGDTHVLCTASLEEKTPPWLRNTGKGWVTAEYGMLPRATGERMKREAAAGKQGGRTQEIQRLIGRSLRAVVDLQALGEKQITLDCDVIQADGGTRTASITGGWIALYDCLKWMESRNMIKVDRVLKDHVAAISCGVFANQAVIDLDYLEDSSAETDANFVMTGAGGIVEIQGTAEGTPFSEEEFSSLMRLAKNGIGELVALQKQAIAG
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
Q2KDA1
|
B2TLY9
|
RS20_CLOBB
|
30S ribosomal protein S20
|
Clostridium
|
MANIKSAKKRIKVTETKTLNNRMIKSALKTVIKKFEAAVAGNNVEEAKTVFVAVTKSLDVAASKGVVHKNMAARKKSRLAAKLNAMA
|
Binds directly to 16S ribosomal RNA.
|
B2TLY9
|
Q28TR2
|
FOLD_JANSC
|
Methenyltetrahydrofolate cyclohydrolase
|
unclassified Jannaschia
|
MTEPQTNRTSGAKIIDGKAFAADVRGQVAGHVQRLKDEHGITPGLAVVLVGEDPASEVYVSHKHKATVEVGMTSFEHKLPADTSEDDLFALIDKLNADPAVHGILCQFPVPDHLDERRTVARISPAKDVDGLSVTNAGLLSSGGEALVSCTPLGCLMLLRAEFDSLSGKDAVVIGRSNLFGKPMAQLLLGDNCTVTIAHSRTKDLADVCRRADILVAAVGRAEMVRGDWIKPGATVIDVGISRVPHPDKPGKTKLIGDVHFAEAVDVAGAITPVPGGVGPMTIACLLANTVTACCRAHGLDEPRGLTA
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q28TR2
|
A9W1Z5
|
URED1_METEP
|
Urease accessory protein UreD 1
|
Methylorubrum
|
MALSLDGLPEKPAPAEAPSPPVGRRVQASLVFARGGRTTVLSRQVVPYPFHITRAFRMHPESPDLATLYLQSASGGLYAADHLTLAIAARAGARAHVTTQAGTVVHRGGPEPSRQETRLTIAADAFLALNPDPLILFPGAHLAVSTEITAEPGARAIVTESVACHDPVGEGRPFDRLDLGLTIRDPEGRALVRERSRIDGRAFTAPDSPMGPHRAYGTMVVLGAPDDARLAGLHLRQAADAAGCLTGVSPLPNGAGLGLRLLAPDGGTLSAGMDAVFRIVFETLSGCAPGRRRK
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A9W1Z5
|
Q8CMQ2
|
AHPC_STAES
|
Thioredoxin peroxidase
|
Staphylococcus
|
MSLINKEILPFTAQAYDPKKDEFKEVTQEDFKGSWNVVCFYPADFSFVCPTELEDLQNQYAKLQELGVNVYSVSTDTHFVHKAWHDHSDAISKLEYSMIGDPSQTITRNFDVLDEESGLAQRGTFIIDPDGVVQAAEINADGIGRDASTLVNKIKAAQYVRQHPGEVCPAKWEEGSESLQPGLDLVGKI
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
|
Q8CMQ2
|
Q50D79
|
UNC4_DANRE
|
Homeobox protein Uncx4.1
|
Danio
|
MMDSRILEHPHAQFGGSLGSMVGMGFPYHLGHHHVYDISGHQLQSAAAVPFSIDGLLNGSCSGSVANSNPLLGSGCGVNGDSQYKLGDGGDPDKESPGCKRRRTRTNFTGWQLEELEKASNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARRELERLEKKKRKQERKLLKSQNKLLAGELFHTPGSDSDSGVSQSTDSESTPHTGPQHSAHRQQTEHICEQHARHQRASTVNETAEPMDSTRNSGLCPANGITRASTLQKLNPFSVESLLADSSPRRKTILDFSQLPPQRPLVGKGHFLLYPITQPLGFIVPQTAMKQSHDSGNSGHHCSTTDTSTSNQKNVNHLCRDNTGASDELQRETKNSSIQSPSTSSEKCFSESNSPQKESENDSESTVTNSSQKESISANLSEYSDRKSRSSADTNTDGEDVDMD
|
Transcription factor involved in somitogenesis and neurogenesis.
|
Q50D79
|
Q1RFX9
|
GLO2_ECOUT
|
Glyoxalase II
|
Escherichia
|
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAISANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTPSQMYQSIKKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLKQPEERFAWLRSKKDRF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
Q1RFX9
|
B0TQ97
|
PNP_SHEHH
|
Polynucleotide phosphorylase
|
Shewanella
|
MVHVNPIVKSFEYGQHTVTLETGVIARQADAAVLASMGDTTVLVTVVGKKFEEPGRDFFPLTVNYQEKTYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPNGFKNEVQVIITVVSVDPEISPEVISMIGTSAALSISGIPFNGPLGSARVGYVNGEYILNPTVSQLVDSQLELSVAGTDSAVLMVESEASALPEEVMLGAVVYGHDQQQVVIQAIKELQAEVNKPVWDWAAPVQDETLVAKIKDLAEAGLTEAYQIEVKQDRYAQVGVVKNAAKEALLAENPDANTREIDGLLGSLEKKVVRGRIIAGNPRIDGREPDMVRALNVMAGVLPRTHGSSLFTRGETQALVTCTLGTERDAQKIDSIMGEYTNRFMLHYNFPPYSVGETGMVGSPKRREIGHGKLAWRGINAVMPTAEEFPYSVRIVSEITESNGSSSMASVCGTSLALMDAGVPIKTSVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTRDGITALQMDIKIEGITKEIMQIALQQAYGARVHILNVMDQAIGSHRGDISEHAPRITTIKINPEKIRDVIGKGGATIRALTEETGTTIELDDDGTVKIASSNGEATKEAIRRIEEITAEVEVGTVYNGKVVRIVDFGAFVTILPGKDGLVHISQIAEERVANVSDYLEVGQEVKVKVMEVDRQGRVRLSMKEAAPKADAPAAE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
B0TQ97
|
Q39FP8
|
SURE2_BURL3
|
Nucleoside 5'-monophosphate phosphohydrolase 2
|
Burkholderia cepacia complex
|
MRILLSNDDGYLAPGLAALSDALQPLAELTVIAPEQNCSGASNSLTLSRPLSVQRAASTGFFYVNGTPTDSVHVALTGMADARPDLVVSGINNGQNMGEDTLYSGTVAAATEGIMFGVPAIAFSLVDKGWAHLPDAARVAAEIVKHYLAHPLPGQPLLNVNIPNLPYDELKGWKVTRLGKRHPSQPVIRQTDPRGEPIYWIGAAGEALDASDGTDFHAVANGFVSITPLQLDLTHTQMLPATREWARAGGRAS
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q39FP8
|
Q0SPE1
|
RUVA_BORAP
|
Holliday junction ATP-dependent DNA helicase RuvA
|
Borreliella
|
MINKIYGKVIEKKESSLVLMTAVFEFELLVSAFCLANFKLLDKVELFTYLYTKENELKLFGFLNSDERETFKSLIGVSGIGPRAALRVLSNIRYNEFKDAIDREDIELIAKIKGIGKKMAGKMFLHLQGKLLINNELESSLFRFKELEESIVSMGFDRKIVNSKLKEAFNLVEFSNLKDSEKEQFLFKEVLKRMSN
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
|
Q0SPE1
|
C6C2E5
|
DBPB_BORBN
|
Decorin-binding protein B
|
Borreliella
|
MKIGKLNSIVMVLFFDLLVACSIGLVERTNAALESSSKDLKNKILKIKKEATGKGVLFEAFTGLKTGSKVTSGGLALREAKVQAIVETGKFLKIIEEEALKLKETGNSGQFLAMFDLMLEVVESLEDVGIIGLKARVLEESKNNPINTAERLLAAKAQIENQLKVVKEKQNIENGGEKKNNKSKKKK
|
Binds to decorin which may mediate the adherence of B.burgdorferi to collagen fibers in skin and other tissues.
|
C6C2E5
|
B0U4K2
|
NUSB_XYLFM
|
Antitermination factor NusB
|
Xylella
|
MSKVSGGGPCPRRRDGVDPALRSRARRRALQAVYAWQISGGVAKQVIAHFAHEQAYEVADLVYFEDLVEGVLTHCAELDEKLTPYLDRTIEEVDAIERAVLRLGAYELLYRQDVPYRVVINEAIMTAKRFGSKYGHTYVNGVLDRAALALRKVEVLG
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
B0U4K2
|
Q97EX0
|
RSMA_CLOAB
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Clostridium
|
MKEFNTRQIVEKYNFRFSKRLGQNFLTDNTVLDDIVENAEIQKDDFIIEIGPGVGTLTRRLLEKAKKVCAIELDESLIPIITNEMKEYDNFTLIHNDALKVDFNNIIGEEQSVKLVANLPYYVTTPIISKLLNEGYNFKSLTIMIQKEVGDRIAAKPSTKDYGALTLLVQYYCDVKVVRVVKPSCFIPQPKVDSLVIRLDKLEKPRVQVKDEKLFFNVIRSAFNMRRKTLWNAMKGLKLSSEDLEKAFEAAGIDSKRRGETLSIEEFGKLSDEIYR
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q97EX0
|
A8G2H7
|
RSMH_PROM2
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Prochlorococcus
|
MQTDLSDSSFFNHKSVMTDEIMASLEHYPLIHNNQLKGIDATLGGGGHSFNLLRKYSELNIIGLDQDPFARISASKKLDEFKNRIDIRASNFADFVPKEKVSFVIADLGVNSNQIDDPKRGFSFQKDGPLDMRMNPLLEVDAEKLIEALNEKDLANLIYKYGDERLSRKIARKIKLDLKENGKYSGTKELAYSIAGCFPPKQRYKKIHPATRTFQALRIAVNKEIEVLEKFLQAVPEWLLPGGIISIISFHSLEDRLVKSSFKNDQRLKNLTKKPITPSEQEVEFNKRARSGKLRIAQLK
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A8G2H7
|
C1A1J0
|
RS20_RHOE4
|
30S ribosomal protein S20
|
Rhodococcus erythropolis group
|
MANIKSQVKRIRTNEAARLRNQSVKSSLRTAIRSFREAAAAGDKDKANELLVSTSRKLDKAASKGVIHANQAANKKSALSQAANKL
|
Binds directly to 16S ribosomal RNA.
|
C1A1J0
|
Q64680
|
CP2D4_RAT
|
Debrisoquine 4-hydroxylase
|
Rattus
|
MRMPTGSELWPIAIFTIIFLLLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQIDFQNMPAGFQKLRCRFGDLFSLQLAFESVVVLNGLPALREALVKYSEDTADRPPLHFNDQSGFGPRSQGVVLARYGPAWRQQRRFSVSTFRHFGLGKKSLEQWVTEEARCLCAAFADHSGFPFSPNTLLDKAVCNVIASLLFACRFEYNDPRFIRLLDLLKDTLEEESGFLPMLLNVFPMLLHIPGLLGKVFSGKKAFVAMLDELLTEHKVTWDPAQPPRDLTDAFLAEVEKAKGNPESSFNDENLRVVVADLFMAGMVTTSTTLTWALLFMILRPDVQCRVQQEIDEVIGQVRRPEMADQARMPFTNAVIHEVQRFADILPLGVPHKTSRDIEVQGFLIPKGTTLIINLSSVLKDETVWEKPLRFHPEHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPAGQPRPSNYGVFGALTTPRPYQLCASPR
|
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
|
Q64680
|
Q5XC69
|
RF1_STRP6
|
Peptide chain release factor 1
|
Streptococcus
|
MNIYDQLQAVEDRYEELGELLSDPDVVSDTKRFMELSREEANTRETVTAYREYKQVIQTISDAEEMIKDASGDPELEEMAKEELKESKAAKEEYEEKLKILLLPKDPNDDKNIILEIRGAAGGDEAALFAGDLLTMYQKYAETQGWRFEVMESSVNGVGGIKEVVAMVSGQSVYSKLKYESGAHRVQRVPVTESQGRVHTSTATVLVMPEVEEVEYDIDPKDLRVDIYHASGAGGQNVNKVATAVRMVHIPTGIKVEMQEERTQQKNRDKAMKIIRARVADHFAQIAQDEQDAERKSTVGTGDRSERIRTYNFPQNRVTDHRIGLTLQKLDTILSGKMNEVIDALVMYDQTKKLESLNN
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q5XC69
|
Q6KI81
|
ATPG_MYCMO
|
F-ATPase gamma subunit
|
Mesomycoplasma
|
MAELQKLSSRLKSVKVTRKITKAMELVAASKIRRAKESFFSNKEYFQIIQDIFDNLASKTEQIFLKKQMKFDKENNTNSILYIVINSDLGLCGAYNSSIAKEIKKEIKSKDKLFLIGKKGLLFLGKFKTQITNLDKVKEISTNYKNIKKISEKILSMFKSGDYKSIKIVYTKYVNAFTYLPTIKHALPILKSEKNINEATFSNLEFEPDPITIFQKAIPLYFSSLLYSCVLESHVSEVSSRRIAMENATKNADELGDQLKIELNTIRQSKITQEITEIVAGSETEI
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
Q6KI81
|
A1R701
|
EFP_PAEAT
|
Elongation factor P
|
Paenarthrobacter
|
MATTNDIKNGTVLKLEGQLWNIIEFQHVKPGKGGAFVRTKMRNVMSGKVVDKTFNAGLKIETATVDRRDYQYLYQDGEDFVFMDTQDYDQITVSGATVGDATNFMLENQMVNIAIHEGTPLYIELPPSVVLEITYTEPGLQGDRSSAGTKPATVETGYEIQVPLFVEQGTKVKVDTRDGSYLGRVND
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
A1R701
|
Q4V622
|
CCH2R_DROME
|
Neuropeptide CCHamide-2 receptor
|
Sophophora
|
MYASLMDVGQTLAARLADSDGNGANDSGLLATGQGLEQEQEGLALDMGHNASADGGIVPYVPVLDRPETYIVTVLYTLIFIVGVLGNGTLVIIFFRHRSMRNIPNTYILSLALADLLVILVCVPVATIVYTQESWPFERNMCRISEFFKDISIGVSVFTLTALSGERYCAIVNPLRKLQTKPLTVFTAVMIWILAILLGMPSVLFSDIKSYPVFTATGNMTIEVCSPFRDPEYAKFMVAGKALVYYLLPLSIIGALYIMMAKRLHMSARNMPGEQQSMQSRTQARARLHVARMVVAFVVVFFICFFPYHVFELWYHFYPTAEEDFDEFWNVLRIVGFCTSFLNSCVNPVALYCVSGVFRQHFNRYLCCICVKRQPHLRQHSTATGMMDNTSVMSMRRSTYVGGTAGNLRASLHRNSNHGVGGAGGGVGGGVGSGRVGSFHRQDSMPLQHGNAHGGGAGGGSSGLGAGGRTAAVSEKSFINRYESGVMRY
|
Receptor for the neuropeptide CCHamide-2.
|
Q4V622
|
Q8BVY0
|
RL1D1_MOUSE
|
Ribosomal L1 domain-containing protein 1
|
Mus
|
MKGSASESPSASVAEATTTDVQVTPTALLQLDREQIRKAVEVISNRSKSKKNNNELLLSGSENLFLMVILWKIPEKELRVKVPLPHSILSESSDVCLFTKDEFDSPEQTEGFYKKLLKKHGVNTISQIIPFKTLKTEYKAYEAKLRLLGSFEVFITDARIRRHLPSHIGRHFYQRKKVPVSVNLLAKNLSKEINRCITGTVLNISKRGSCSTIRIGHTGMETEHIVDNILAVSEMLSEKLPEKWQSVKLLFLKTEKSVSLPIFSSFVTSQDENAVSLRSLRKQELKKRKRENAKLKKESKMLRKKSKKATSLLTQSGLASSAPAKSPGAQKKKTNKAHKKQKVTEECEEAIPQLVPIGETPDKENVKMQENITGKTPKSKSDPSTPKGKKRKALLATETPEASAPGTSGKKQKKDVQEFRKPEASSFSTPRKSGKKASNTPRDKKTKAAHSN
|
Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.
|
Q8BVY0
|
A1SU43
|
DER_PSYIN
|
GTP-binding protein EngA
|
Psychromonas
|
MLPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGQAKIDEHEFIVIDTGGITGDEEGIDALMAGQSLLAIDEADAVLFLVDARAGMTIADEAIADHLRKQDKKVFVVANKTDGVDADSVCAEFYALGLGEVYHIAAAQGKGVRQMIEIALDGFFDDVEQEDDFSDLETGLEFVEEDEALLLKEQERLAALPIKLALIGRPNVGKSTLTNRILGEERVLVYDLPGTTRDSIYIPMSRDDREYILIDTAGVRKRKKVNETVEKFSVIKTLQAIEDCNVVLLIIDARDGISDQDLSLLGFTLNAGRSLVIAVNKWDGMTEYDKERVKSELDRRLGFIDFAKIHFISALHGTGVGHLYESVEEAYDSSTKRISTSILTRIMTMAAADHEPPMVGSRRVKLRYAHAGGYNPPLIVIHGNQVKKLADSYKRYLMNYFRRSLGIMGTPIRIEFREGTNPFAGRRNKLTPNQMYKRQRLVKFHKKSKK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
A1SU43
|
A1RJD1
|
UBIG_SHESW
|
3-demethylubiquinone 3-O-methyltransferase
|
Shewanella
|
MQHNTNVDPQEIAKFERMAETWWDLNGEFKPLHLLNPLRLNYIDQTTGGIFGKKVLDVGCGGGILSESMARIGAEVDGLDMGEEPLEVARLHALETGVNITYVKNTAEAHSQDHQGYYDVVTCMEMLEHVPNPQSVIKACCDMVKPGGFVFFSTINRNLRSYVETILGAEYLLKMLPVGTHDHNKFIKPSELIELVDNTDLICKDAVGITYNPLTGIFKYTPRVDVNYMIATQKVD
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
A1RJD1
|
P34641
|
CED11_CAEEL
|
Cell death protein 11
|
Caenorhabditis
|
MDETDPVPDMSLLPDTVPVVVSGDGSAAGIQLCPALILGSPQALPGAIKHIYSRLAAAASEVDQGVPDLIISLISHGNSLSTKYMSSVENGLKSFLIGCGTWLISSGEVNDPMSRVASGALKNVLPQLEHQAEVLHILVNSDDMIASDTTNSKSVVDTSLNTLLLICRKEPNDSYETVASSIAKLRAATAVKLAHPPPALLIGVPSEPMSPSTYGNSAAILLSPSNDKRPFPVAIFAGASKESLIELLFFVEHGIPVIILQDSCELCAILHSSHLLLETSNFDNDKFISWLRSQLYPLGLADCYTLITKLLVSSNSGDVQLIEFIDSSQLSELSSVVVDRCLECYATTGEERQVLLLAAKLNSPSVLSSMDVAAQLDEELLTMILCECITKDDQLHFLSSVLQLSPPIRVTSNMLIRMMHHADEHFFTTIVLCQCMGYSYIPSEIDPRFANDIQKLVKKLSFGVDNLFDPNVFCNDSSHRDKHESIRILAIWSLLLHRPGIVKCLAAFADEPVAFSMVLSRIARSLGHESHDWHFYEKSLNTLSDSLSGSATTLFDTVFSTSPAKAYQLLCQPMEYFYGFNMTQLAFHCNAREIIAHECCQRWVHRKLYGNLQAKNFPIFLPKWAKICISAVLIIPVKFWMLVRPRERTKQDTVSPTVALLDVGKFPQKQRAISTYSVISSRSEALTALTAPLSTAFGFNSALNGAESATPQSMVFPLNIEEIDKDPRPFGKKNRIRRAHAPTLSTFYSTPIVKYWLSLLFRIVFICCLAYSVVLPGCGSNLWDTGMWVWSFFWWIENCFVLTARARKIPLSLMPWRVFDVFAFFVFLILLLVMKVFPVTPVLEVLGIDSIYSAKVVSAFFVLYVSYSTLFTYIPLSDIFGPMIVRVKLMLLRDFTNFLFMIALVMLSSAVAIQAVVFPDRPVTMEVFRKTLSWIWLSLFTTDLSNLSESETCRKSFLGAPKRYCSSVGQYANPSCPSQSLPAYLIVIEYFVILKLLLWPILFAFFSKTAKNVDDEADKIWRFQLYSLAEDFRLRPPLPPPLTIFCLICSACCRFSNSFSGFFSDFDHPDFEARDKCRTTWKFGSIYRNPSVPFKRNEFVNSFWRKLSMEQWKNTQQKAKISANKSELQELHNIHNHIRMMTLRDSYENSGTRKASELQFFEKYPESNILKISVNMVSKPWTVLVPRYNPPFYCKPAEDFPSDVQKYVDIATEQNVGELKRIWRSRQANDVTSSNDKCWKLSAAGFPLNPNGRTGMAGRGNHPRFGANRRCYYVVLSGGVEAKCQVLVDSQKNIPNEWHLENSSKDEHLTSILKMIGISDSDAHMFSMRRLDSSIITADKRIPSNDTSPAHLASEVAENENDTDNAWTEHDVWAISLRERRIITTIIGYSWLPTSAIRGTVLPWQADLVFRAKTIYGL
|
Plays a major role in programmed cell death.
|
P34641
|
A1U1Y9
|
NQRE_MARN8
|
NQR-1 subunit E
|
Marinobacter
|
MEHYLSLLLKAIFVENMALAFFLGMCTFLAISKKIEAATGLGIAVVVVLTVTVPVNNLLYNTILREGALDWAGLPNVDLSFLGLLTYIGVIAAIVQIMEMVLDKYIPALYAALGVFLPLITVNCAILGASLFMVERDYTFGESLVYGFGAGVGWALAIIALAGIREKLKYSDVPNGLRGLGITFITVGLMSLGFMSFSGISL
|
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.
|
A1U1Y9
|
P0ABS7
|
DNAG_SHIFL
|
DNA primase
|
Shigella
|
MAGRIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELAAMHNLEVPFEAGSGPSQIERHQRQTLYQLMDGLNTFYQQSLQQPVATSARQYLEKRGLSHEVIARFAIGFAPPGWDNVLKRFGGNPENRQSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHKGRQLYGLYEAQQDNAEPNRLLVVEGYMDVVALAQYGINYAVASLGTSTTADHIQLLFRATNNVICCYDGDRAGRDAAWRALETALPYMTDGRQLRFMFLPDGEDPDTLVRKEGKEAFEARMEQAMPLSAFLFNSLMPQVDLSTPDGRARLSTLALPLISQVPGETLRIYLRQELGNKLGILDDSQLERLMPKAAESGVSRPVPQLKRTTMRILIGLLVQNPELATLVPPLENLDENKLPGLGLFRELVNTCLSQPGLTTGQLLEHYRGTNNAATLEKLSMWDDIADKNIAEQTFTDSLNHMFDSLLELRQEELIARERTHGLSNEERLELWTLNQELAKK
|
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
|
P0ABS7
|
A4QA27
|
URED_CORGB
|
Urease accessory protein UreD
|
Corynebacterium
|
MTQTQPVGTLRLTIDDQGPQGQSRAVEQFHQGALRVIRPHYLDDSGQVSYTIIAIGGGYLGGDVYEQQFTVKDNAKALITTQSATKIYRTPQGPVTQYTEINVGENAVLEYLADQTIAYRESTYHQFTKVTLHPTSTFVMSEQITPGWHPDGKHFAYDEMRLHTEITDSTTGRLVLLDNLLLRPDSREGSFGWTEQYTHSGQMIVMGEGVDKQLVAELNEQLAAHPDVYGAVNFLSAPGTLLRGFIARTLSNRTEELINLHEHIASLLRGRWRGQEPVNLRKY
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A4QA27
|
C1CSC8
|
ATPB_STRZT
|
F-ATPase subunit beta
|
Streptococcus
|
MSSGKIAQVIGPVVDVLFAAGEKLPEINNALVVYKNDERKTKIVLEVALELGDGMVRTISMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARARRIQFFLSQNFNVAEQFTGQPGSYVPVAETVRGFKEILDGKYDHLPEDAFRGVGSIEDVIAKAEKMGF
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
C1CSC8
|
Q9XDP0
|
DSBI_LELAM
|
Protein-disulfide oxidoreductase DsbI
|
Lelliottia
|
MVDIKGMWKDLRATPVETLVRWQEQRFLWLLMAVAMGGLIILAHSFFQIYLYMAPCEQCVYIRFAMFVMVFGGLIAAINPKNIILKLIGCLAAFYGSIMGIKFSVKLNGIHYAVHNPDPDALFGVQGCSTDPTFPFGLPLAEWAPEWFRPTGDCGYDAPVVLTRNAQFCPAVVCGNVSALRRLVSDPALAFYEYGAGVPAGVWAMFCTVADYERRLGNQAD
|
Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.
|
Q9XDP0
|
Q54824
|
DNRS_STRPE
|
2,3,6-trideoxy-3-aminohexose transferase
|
Streptomyces
|
MKVLVTAFAMDAHFNGVVPLAWALRAAGHDVRVASQPALTDSITRAGLTAVPVGTDHQVQAAMGAMAPGVFALHLNPDYLENRPELLDLEFLEASTSMLTAAFYAQINNDSMIDEMVDFAAWWRPDLVVWEPFTFGGAVAAQVTGAAQARLLWGPDLFLRVHDRFQQVLHEVPAERRDDALEEWLTWTLERHGAAFGPEVISGHWTIDQMPPSVRFATARPTVPMRFVPYNGPVPAVVPPWLRADPGRPRVLLTQGITERSTGFTGLPRAGELLASIAELDAEVVATVKAEEREGLPPLPGNVRVVDSLSLHVVLPSCAAVVHHGGAGTWATAALHGVPQLALAWQWDDVFRAGQLEKLGAGIFLPPHGEGASAGRVRDRLAQVLAEPSFRQGAARIRAEMLRTPAPGAVVPTLEQLTARHRAPAGQGVRH
|
Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the addition of the TDP activated glycoside, L-daunosamine-TDP (2,3,6-trideoxy-3-aminohexose-TDP) at position C-7 of epsilon-rhodomycinone to yield rhodomycin D. Glycosylation is a prerequisite for biological activity of anthracyclines and requires DnrQ which seems to act as an activator.
|
Q54824
|
Q5PAY2
|
TRUB_ANAMM
|
tRNA-uridine isomerase
|
Anaplasma
|
MQSARVKYGWLNVDKPLHMSSGSVVGRVKKIFNCKVGHAGTLDPLATGVLPVAVGEATKTIPYAVDGLKSYAVTVQWGSQRSTDDAEGEIIKTSSLRPSADSIREALGQFVGNIRQVPPAFSAVRVRGVRAYRLARRGEAVSLPPKEVCIVSIDLLSADEESNTADFLIVCKKGVYIRSFARDLGASLGCFGYVSFLRRKSVGPFSEENSVTLDRLEALADADVLNEALLPISYVMGDALLRLHVDAEVAEIVKKGQSVSLQRTSLNGLYAAENYDMCYLSRVGGVPVAVCKVVNGTARPVRVFDV
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q5PAY2
|
Q06GR3
|
PSBZ_PIPCE
|
Photosystem II reaction center protein Z
|
Piper
|
MTIAFQLAVFALIATSLILVIGVPVVFASPDGWSSNKNIVFSGTSLWIGLVFLVGILNSLIS
|
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
|
Q06GR3
|
P40988
|
FET4_YEAST
|
Low-affinity Fe(II) transport protein
|
Saccharomyces
|
MGKIAEFLGNPGARPDVHHRAPTVDCKQYEEFGDSNDYKNDDVVRVVSHSDESTDDELCNVNLTETGAIFTSKGFTGLSKGFTDKTLDFLVRVAGSQAVFFIVWIILIIWVVIGIVYNAPFNWQVVMQDGQSIQSYVWDTLLMRQQLMSTHEQILICGRLKSRLASFKNYLTRSTPEEEKADCTVEANEVSSVENHIDPSAINGELPVENWYDRLSNVASRYMGSIAAMVIFWIGIFVWIGCGAIPKDAGNTPPYTGETTGSNPRLKKFSDAWQMYINTAVAVSLLICTTFLQNIRARHDYFTGRFLVDIFDMDEKIDYRIRKHFNDFETPHPVVTIESKKRSTGRKMIDWYADIIGTGIGVLIGVAVFATWIGIGSPMKWDDNWWLIIGTYTGLIGFLDGFVLREVYFRIVQHEEKNYSDVAKEDLELFQELGIECPEEFSGKAPEINTIGYRTSQYINRICSTPWSVLVSVIIIIGLICIASGLRWSTTGQLIANTPTMIIEEFFLLVLLQAHNWADRQRRVEVTALYARRRILLSYVEKRFPEVMMLEK
|
Required for Fe(2+) ion low affinity uptake.
|
P40988
|
P48169
|
GBRA4_HUMAN
|
GABA(A) receptor subunit alpha-4
|
Homo
|
MVSAKKVPAIALSAGVSFALLRFLCLAVCLNESPGQNQKEEKLCTENFTRILDSLLDGYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWIDKRLKYDGPIEILRLNNMMVTKVWTPDTFFRNGKKSVSHNMTAPNKLFRIMRNGTILYTMRLTISAECPMRLVDFPMDGHACPLKFGSYAYPKSEMIYTWTKGPEKSVEVPKESSSLVQYDLIGQTVSSETIKSITGEYIVMTVYFHLRRKMGYFMIQTYIPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNIQMEKAKRKTSKPPQEVPAAPVQREKHPEAPLQNTNANLNMRKRTNALVHSESDVGNRTEVGNHSSKSSTVVQESSKGTPRSYLASSPNPFSRANAAETISAARALPSASPTSIRTGYMPRKASVGSASTRHVFGSRLQRIKTTVNTIGATGKLSATPPPSAPPPSGSGTSKIDKYARILFPVTFGAFNMVYWVVYLSKDTMEKSESLM
|
GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
|
P48169
|
Q214W4
|
PIMT_RHOPB
|
Protein-beta-aspartate methyltransferase
|
Rhodopseudomonas
|
MPIGPPPPEKMMFQLSLRRRGISDQAVLRAMDEVPRDAFVEPGQRAEAWLDTALPIACGQTISQPFVVAYMTEQMQLRPEHRVLEIGTGSGYQAAILSRLSRAVLTLERFKTLADQARARLAALHCDNVEVRIGDGFAVPADAGLFDRIIVTAAMEEVPASLLDRLDLDGVLIAPVGPHNATQTLLRIRKSKSGIERKELVAVRFVPALPGLAREL
|
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
|
Q214W4
|
A4IJK7
|
RL15_GEOTN
|
50S ribosomal protein L15
|
Geobacillus
|
MKLHELQPAPGSRKKAVRVGRGIGSGNGKTAGRGHKGQKARSGGGVRLGFEGGQTPLFRRLPKRGFTNINRKEYAVVNLDRLNIFEDGTEVTPELLLEKGVISKLKSGVKILGKGQIEKKLTVKAHKFSASAKEAIEAAGGKTEVI
|
Binds to the 23S rRNA.
|
A4IJK7
|
A0A291NVT7
|
CESS1_CONMO
|
Conophysin
|
Strategoconus
|
MQMGRPTLLPCLLLLLVLSTQACFIRNCPEGGKRDVHMIQPTKPCMNCSFGQCVGPRVCCGAGRCEIGSTEADRCEEENEDPVPCKVLGQHCVLNNPGNVNGNCVDGGIGICCVDDTCAIHRRCD
|
Targets vasopressin-oxytocin related receptors.
|
A0A291NVT7
|
B2J1M7
|
MOAA_NOSP7
|
Molybdenum cofactor biosynthesis protein A
|
Nostoc
|
MNQVDYLRISLIDRCNFRCQYCMPEGVELDYILKQQLLTNEELLTLIREVFIPVGFNRFRLTGGEPLLRPRVVDLVSAIATLPQTQDLSMTTNGFLLAPMAQNLYNAGLRRINISLDSLDADTFDQIIGNQGRSRWQQVWHGIQAAHSVGFDPLKLNVVVIPGVNDHEILDLAALTIDKQWHVRFIEFMPIGNVDLFGDRGWVSSAELRQQIRDRWGLTESQVRGAGPADVFKIPGAKGTLGFISQMSECFCDRCNRMRLSADGWLRPCLLNETGQIDLKTALRSGTSTAQLQEQVRHLLRMKPEINFKGRDSGIVGTYTRTMSQIGG
|
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
|
B2J1M7
|
Q8E6W4
|
YIDC1_STRA3
|
Membrane protein YidC 1
|
Streptococcus
|
MKKKLKTFSLILLTGSLLVACGRGEVSSHSATLWEQIVYAFAKSIQWLSFNHSIGLGIILFTLIIRAIMMPLYNMQMKSSQKMQEIQPRLKELQKKYPGKDPDSRLKLNDEMQSMYKAEGVNPYASVLPLLIQLPVLWALFQALTRVSFLKVGTFLSLELSQPDPYYILPVLAALFTFLSTWLTNKAAVEKNIALTLMTYVMPFIILVTSFNFASGVVLYWTVSNAFQVFQILLLNNPYKIIKVREEAVRVAHEKEQRVKRAKRKASKKRK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
|
Q8E6W4
|
A8WHP3
|
SC5A9_DANRE
|
Solute carrier family 5 member 9
|
Danio
|
MPASPEPVTATPEPEEVPAKFTLEAADIAVVVVYFVFVLAVGIWSSIRANRGTVGGYFLAGRSMTWWPIGASLMSSNVGSGLFIGLAGTGAAGGLAVGGFEWNAAWVLIALGWIFVPVYISAGVVTMPEYLRKRFGGQRIRIYMSVLSLILYILTKISTDIFSGALFIQVSLGWDLYLSTVILLAVTALYTIAGGLTAVIYTDALQTVIMVIGAFVLMFIAFDKVGWYEGLLVQYEKAAPALTVPNTTCHLPRSDAFHIFRDPVTGDIPWPGLIFGLTVLATWVWCTDQVIVQRSLSAKNLSHAKAGSVLGGYLKVFPMFFVVMPGMISRALYPDEVACVDPDECQKICGAKVGCSNIAYPKLVVELMPVGMRGLMIAVMMAALMSSLTSIFNSSSTLFTMDIWQRIRPRASEKELMVVGRVFILLLVALSIVWIPVIQTANSGQLFDYIQAITSFLSPPITTVFIMAIFWGRVNEQGAFWGLMVGLVVGMVRMIMEFVYGTPSCGETDLRPSLLKDVHYLYFALILLALTVLIITAVSLCTAPIPEKHLVRLTWWTRHSKEERVELEDPWAKPAGSDLSTTESEGSDEDAPAWWKRAGMWLCGLSQTTKQDLTEEERQALEKKLTSIEEDHMWKTVCNVNALILLTANVFLWGYFA
|
Probable sodium-dependent sugar transporter.
|
A8WHP3
|
P29644
|
COX1_ATRSP
|
Cytochrome c oxidase polypeptide I
|
Atractosteus
|
HLFWFFGHPEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWDTPLLWALGFIFLFTVGGLTGIVLANSSLDIMLHDTYYVVAHFHYVLSMGAVFAI
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
P29644
|
A4JAP1
|
RL4_BURVG
|
50S ribosomal protein L4
|
Burkholderia cepacia complex
|
MELKLLNENGQEGAVVNASDVVFGRDYNEALIHQVVVAYQANARQGNRAQKDREQVKHTTKKPWRQKGTGRARAGMSSSPLWRGGGRIFPNSPEENFSHKVNKKMHRAGLCSIFSQLAREGRLSVVEDIILEAPKTKLLADKFKTMGLDSVLIITDTVDENLYLASRNLPHVAIVEPRYADPLSLIYFKKVLVTKAAVAQIEELLS
|
Forms part of the polypeptide exit tunnel.
|
A4JAP1
|
C4ZF43
|
APT_AGARV
|
Adenine phosphoribosyltransferase
|
Lachnospiraceae incertae sedis
|
MKTVKDYIRTIPDFPEKGIMFRDVTSVIQDADGLKLAIDEMIKRLDGLDFDVIAGAESRGFVFGMPIAYALHKPFVMVRKAGKLPCETVSKTYDLEYGTATIEMHKDSVKPGQKVVLVDDLIATGGTMQAAAELVEELGGEVVKMLFLIELAGLNGRKLLSKYDVDAVVSYDGK
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
C4ZF43
|
A5UBC8
|
FDHE_HAEIE
|
Protein FdhE homolog
|
Haemophilus
|
MSIKILSESEIKQVANSYQAPAVLFANPKNLYQRRAKRLRDLAQNHPLSDYLLFAADIVESQLSTLEKNPLPPQQLEQLNAIEPLNAKTFKRDSIWREYLTEILDEIKPKANEQIAATIEFLEKTSSAELEEMANKLLAQEFNLVSSDKAVFIWAALSLYWLQAAQQIPHNSQVENAENLHHCPVCGSLPVASIVQIGTSQGLRYLHCNLCESEWNLVRAQCTNCNSHDKLEMWSLDEELALVRAETCGSCESYLKMMFQEKDPYVEPVADDLASIFLDIEMEEKGFARSGLNPFIFPAEEA
|
Necessary for formate dehydrogenase activity.
|
A5UBC8
|
Q8NS92
|
PDXR_CORGL
|
HTH-type pyridoxine biosynthesis transcriptional regulator PdxR
|
Corynebacterium
|
MLADLPIALNPHEPTSIPTQLTEQIRRLVARGILTPGDPLPSSRSLSTQLGVSRGSVVTAYDQLAGEGYLSTARGSGTTINPDLHLLKPVEIEKKETSRSVPPPLLNLSPGVPDTATLADSAWRAAWREACAKPPTHSPEQGLLRLRIEIADHLRQMRGLMVEPEQIIVTAGAREGLSLLLRTMDAPARIGVESPGYPSLRRIPQVLGHETIDVPTDESGLVPRALPHDLNALLVTPSHQYPYGGSLPADRRTALVAWAEANDALLIEDDFDSELRYVGMPLPPLRALAPDRTILLGTFSSVITPQVACGYLIAPTPQARVLATLRGILGQPVGAITQHALASYLASGALRRRTQRLRRLYRHRRSIVQDTLGDLPNTQLRPINGGLHAVLLCDKPQDLVVTTLASRGLNVTALSHYWGGTGADNGIVFGFGSHDEDTLRWVLAEISDAVSLG
|
May have a regulatory function in pyridoxine biosynthesis. Is said to also have an aminotransferase activity in valine biosynthesis as a double inactivation of ilvE and pdxR results in an auxotrophic requirement for valine.
|
Q8NS92
|
A8G3Q9
|
CHLB_PROM2
|
Light-independent protochlorophyllide reductase subunit B
|
Prochlorococcus
|
MELTLWTYEGPPHVGAMRIASSMKDIHYVLHAPQGDTYADLLFTMIERRGQRPPVTYTTFQARDLGGDTAELVKKNIKEAVERFKPKTLLVGESCTAELIQDQPGALAKGMGFDMPIVNLELPAYSKKENWGASETFYQLTRTLLKEKVGSSEKISPLRWKELGRRPKVNILGPSLLGFRCRDDVIEIQRILSEQGIDTNVVAPLGANPNDIERLIDAEINICLYQEIAEASCEWLKRNFGMEYTNTIPIGIKNTIEFINEVHNKLDLPLTNKKELEHKSKLPWYSKSVDSNYLTGKRVFIFGDGTHAIAAAKIAKDELGFEVVGIGTYSREMARQVRATAKELNVEALITNNYLEVEDAMKKAAPELVLGTQMERHSAKRLGIPCAVISTPMHVQDVPARYSPQMGWEGANVIFDDWVHPLMMGLEEHLIDMFKHDFEFVDGHQSHLGHTATKTKDLINSDNKKDNNPKEGIIWTESGRAELTKVPFFVRGKVKTNTEKYAILRGIPEISDETLYDAKAYFS
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
A8G3Q9
|
Q317V2
|
PYRG_PROM9
|
UTP--ammonia ligase
|
Prochlorococcus
|
MSKFVFVTGGVVSSIGKGIVAASLGRLLKSRGYSVSILKLDPYLNVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFTDTAMTRLNSVTTGSIYQAVINKERRGSYNGGTVQVIPHITREIRERIHRVASNSNADIIITEIGGTVGDIESLPFLEAIREFKNDVNRNDVAYIHVTLLPYIKTSGEIKTKPTQHSVKELRSIGIQPDLLVCRSDKSINEGLKKKLSGFCGVNINSVIEALDADSIYSVPLSLKKEGLCKETLKYLELEDKECDLKNWEKLVHNLRNPGTPIKVALVGKYIELGDAYLSVVEALRHACIEQKALLDLHWVSAEMIEKDSAETYLNEVDAIVVPGGFGNRGVNGKISAIKFARENKIPFLGLCLGMQCAVIEWARNVANLPDASSSELDPKTPNPVIHLLPEQEDVVDLGGTMRLGVYPCRLTNNTIGKKLYDEDVIYERHRHRYEFNNYYKQSFLNSGYKISGTSPDGRLVELIELDNHPYFLACQYHPEFLSRPGKPHPLFKGLIKSSQENLTQSN
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
Q317V2
|
Q3UP24
|
NLRC4_MOUSE
|
Ice protease-activating factor
|
Mus
|
MNFIRNNRRALIQRMGLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFVYQDLTGQNLSYQVTEEDLNVLAQNLKDLYNSPAFLNFYPLGEDIDIIFNLEKTFTEPIMWKKDHRHHRVEQLTLGSLLEALKSPCLIEGESGKGKSTLLQRIAMLWASGGCRALKGFRLVFFIHLRSARGGLFETLYDQLLNIPDFISKPTFKALLLKLHKEVLFLLDGYNEFHPQNCPEIEALIKENHRFKNMVIVTTTTECLRHIRHVGALTAEVGDMTEDSAKDLIEAVLVPDQVERLWAQIQESRCLRNLMKTPLFVVITCAIQMGRQEFQAHTQTMLFQTFYDLLIQKNSHRYRGGASGDFARSLDYCGDLALEGVFAHKFDFEPEHGSSMNEDVLVTIGLLCKYTAQRLKPTYKFFHKSFQEYTAGRRLSSLLTSKEPEEVSKGNSYLNKMVSISDITSLYGNLLLYTCGSSTEATRAVMRHLAMVYQHGSLQGLSVTKRPLWRQESIQSLRNTTEQDVLKAINVNSFVECGINLFSESMSKSDLSQEFEAFFQGKSLYINSENIPDYLFDFFEYLPNCASALDFVKLDFYERATESQDKAEENVPGVHTEGPSETYIPPRAVSLFFNWKQEFKTLEVTLRDINKLNKQDIKYLGKIFSSATNLRLHIKRCAAMAGRLSSVLRTCKNMHTLMVEASPLTTDDEQYITSVTGLQNLSIHRLHTQQLPGGLIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHLSDIGEGMDYIVKSLSEESCDLQEMKLVACCLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELIGRLGVLGELTTLMLPWCWDVHTSLPKLLKQLEGTPGLAKLGLKNWRLRDEEIKSLGEFLEMNPLRDLQQLDLAGHCVSSDGWLYFMNVFENLKQLVFFDFSTEEFLPDAALVRKLSQVLSKLTLLQEVKLTGWEFDDYDISAIKGTFKLVTA
|
Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. It senses pathogenic proteins of the type III secretion system (T3SS) and type IV secretion system (T4SS) such as flagellin and PrgJ-like rod proteins via the Naip proteins (Naip1, Naip2 or Naip5): specific Naip proteins recognize and bind pathogenic proteins, driving assembly and activation of the NLRC4 inflammasome. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri and fungal pathogen C.albicans. In intestine, the NLRC4 inflammasome is able to discriminate between commensal and pathogenic bacteria and specifically drives production of interleukin-1 beta (IL1B) in response to infection by Salmonella or P.aeruginosa. In case of L.pneumophila infection the inflammasome acts by activating caspase-7.
|
Q3UP24
|
Q9K8E8
|
LEU1_HALH5
|
Alpha-isopropylmalate synthase
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MRKISVFDTTLRDGEQSAGVNLNFEEKMEIAKQLERLGVDIIEAGFPASSQGDFQSVKAIAETVKGSSVTGLARSVQKDIDAAWEALKSAEEPRIHLFIATSPIHMEHKLRMTPEQVIEKAVESVKYAASRFKHVQWSAEDASRSDFPFLAQIIEAVIQAGATVINLPDTVGYTTPQEIKRMFQYMKQNVPSIDKVSLSTHNHDDLGMAVANSLAAIQGGADQVECTINGIGERAGNASLEEIAVALNIRKDHYETETGLILKEIKRTSSLVSKLTGMVVPNNKAVVGANAFAHESGIHQDGVLKNKQTYEIITPEMVGVSSNSMVLGKHSGRHAFKTKVQELGFTGTDEQLNNIFKAFKDLADKKKEITEDDLFALMTEQTVGGETNHYELQTLQVNYGSNLTNTATITMKLPSGEVAEEAATGSGSVEAIYNTLERLLDAPVKLLDYRIQSITGGRDALADVYVQMDYQGVVSSGRGTAHDVLEASAKAYLNAVNRTINRKKYAEVYGSKVEV
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
Q9K8E8
|
C6BYQ6
|
RL31_MARSD
|
50S ribosomal protein L31
|
Maridesulfovibrio
|
MKKDIHPKLHKATVRCHCGYESELYSTIGEEVSTEICSNCHPFYTGKQRFVDTAGRIDRFKKKFANFDAASKVKGN
|
Binds the 23S rRNA.
|
C6BYQ6
|
C1A3W7
|
GUAA_GEMAT
|
Glutamine amidotransferase
|
Gemmatimonas
|
MNSRILILDCGSQFTQLIARRVREARVYSEIHPPTKSLDWIRAWKPTGIILSGGPSSVTDEGAPTIPPALLDVAPVLGVCYGMQLIAHLEGGSVVGGGRREYGRAEVTVDEASGMFAGFTAGEKTTVWMSHGDHVEQVPPGYVATAHSGNTCAGFRHKTKPIHAVQFHAEVHHSARGAEIIENFLFDICHCAPDWTPGHFIDLEVAKIREMVGDRQVICGLSGGVDSSVAAALVHKAIGDQLTCIFVDTGLLRLHEREQVERTMRAHLGIKLITVRAEDRFLNGLAGEGDPEKKRKIIGHTFIDVFEDASAEAGKNAEFLVQGTLYPDVIESVSAKGGPSATIKTHHNVGGLKPDMKFKLIEPLRELFKDEVRNVGRELGLPEEMVGRHPFPGPGLAIRVLGEVTPHALDVLRRSDAIYLEEIRAAGLYPDIWQAFAVFLPVKSVGVMGDGRTYENVVALRAVTSTDGMTADWYPFPYEVLGRISNRIINEVDGVNRVVYDISSKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
C1A3W7
|
Q6B8V3
|
RK3_GRATL
|
50S ribosomal protein L3, chloroplastic
|
Agarophyton tenuistipitatum
|
MKIGLLGKKIGMTQIFDPGGKALPVTILKLGPCLITDIKKMESHGYAAIQIGYVKVNGNKLNKAQIGHLNKYNMPLVKFLKEYKVASTENYQIGKWITVEDLSINQNISVSGTSIGKGFTGCIKRHNFSRGPMSHGSKNHRQPGSIGAGTTPGKVFAGKKMAGRMGGKKVTIQNLKIIDIKINNNLIIVKGSVPGKPGNIVSIYQ
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q6B8V3
|
Q5VVP1
|
S31A6_HUMAN
|
Protein FAM75A6
|
Homo
|
MENLPFPLKLLSASSLNAPSSTPWVLDIFLTLVFALGFFFLLLPYLSYFHCDDPPSPSPGKRKCPVGRRRRPRGRMKNHSLRAGRECPRGLEETSDLLSQLQSLLGPHLDKGDFGQLSGPDPPGEVGERAPDGASQSSHEPMEDAAPILSPLASPDPQAKHPQDLASTPSPGPMTTSVSSLSASQPPEPSLPLEHPSPEPPALFPHPPHTPDPLACSPPPPKGFTAPPLRDSTLITPSHCDSVALPLGTVPQSLSPHEDLVASVPAISGLGGSNSHVSASSRWQETARTSCAFNSSVQQDPLSRHPPETCQMEAGSLFLLSSDGQNVVGIQVTETAKVNIWEEKENVGSFTNQMTPEKHLNSLGNLAKSLDAEQDTTNPKPFWNMGENSKQLPGPQKCSDPRLLQESFWKNYSQLFWGLPSLHSESLVANAWVTDRSYTLQSPPFLFNEMSNVCPIQRETTMSPLLFQAQPLSHRQPFISSTPQFLPTPMAQAEAQAHLQSSFPVLSPAFPSLIKNTGVACPASQNKVQALSLPETQHPEWPLLRKQLEGRLALPSRVQKSQDVFSVSTPNLPQESLTSILPENFPVSPELRRQLEQHIKKWIIQHWGNLGRIQESLDLMQLRDESPGTSQAKGKPSPWQSSTSTGESSKEAQKVKFQLERDLCPHLGQILGETPQNLSRDMKSFPRKVLGVTSEESERNLRKPLRSDSGSDLLRCTERTHIENILKAHMGRNLGQTNEGLIPVRVRRSWLAVNQALPVSNTHVKTSNLAAPKSGKACVNTAQVLSFLEPCTQQGLGAHIVRFWAKHRWGLPLRVLKPIQCFKLEKVSSLSLTQLAGPSSATCESGAGSEVEVDMFLRKPPMASLRKQVLTKASDHMPESLLASSPAWKQFQRAPRGIPSWNDHGPLKPPPAGQEGRWPSKPLTYSLTGSTQQSRSLGAQSSKAGETREAVPQCRVPLETCMLANLQATSEDVHGFEAPGTSKSSLHPRVSVSQDPRKLCLMEEVVSEFEPGMATKSETQPQVCAAVVLLPDGQASVVPHASENLVSQVPQGHLQSMPTGNMRASQELHDLMAARRSKLVQEEPRNPNCQGSCKSQRPMFPPIHKSEKSRKPNLEKHEERLEGLRTPQLTPVRKTEDTHQDEGVQLLPSKKQPPSVSHFGENIKQFFQWIFSKKKSKPAPVTAESQKTVKNRSCVYSSSAEAQGLMTAVGQMLDKKMSLCHAHHASKVNQHKQKFQAPVCGFPCNHRHLFYSEHGRILSYAASSQQATLKSQGCPNRDRQIRNQQPLKSVRCNNEQWGLRHPQILHPKKAVSPVSPPQHWPKTSGASSHHHHCPRHCLLWEGI
|
May play a role in spermatogenesis.
|
Q5VVP1
|
A0B8A0
|
DGGGP_METTP
|
Geranylgeranylglycerol-phosphate geranylgeranyltransferase
|
Methanothrix
|
MTLLEIMRPANCVMAGAASLTGMLVSGALLQSLHTPVLVFSAVLLITGGGNAINDYFDREIDAVNRPDRPIPSGRISPRAALIWSVALFIAGCLIAGLINQSCLALALLNSFVLIIYAARLKGLPVAGNIAISYLTGTTFLFGGLAASPSSITAFLSILSALATLSREIVKDIEDLPGDLAHGAKTLPAFIGKRKSFVLASLVLIVAMLLSYLVPLGIDYQAAVSIANLAFLLSIKRMLCGDASGSQRWIKMGMGMALVAFLIGYHI
|
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
|
A0B8A0
|
B3DQ62
|
DXR_BIFLD
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Bifidobacterium
|
MSIASNSTVIILGSTGSIGTQGLDVISRHPERFTVTGLAAGGAHIELLAQQAAQFHVSEAAVFDETKVPALQAALAQAGAQGVRVTGGPDSVIAMAGSGANVVLNGITGSIGLEPSIAALKAGSQLALANKESVVAGGHLLFSAQVRENQINPVDSEHSAIWQSLRSGTHAEVAKLVVTASGGPFRGWKRADMENITPEQALHHPTWNMGPVVTINSSTLMNKGLEVIEASRLFNVPPERIDVTVHPQSIVHSMVEFVDGATICQASPPDMRLPIALGLSAPDRMTNVAAACDWTQAATWTFEPLDDEAFPAVQLARHCLAASEKHTAVLNAANEQAVHAFLEHRLPYLGIVDTVKAVLDQMDAELRGNPLFTDVEEMNQLELEARRRADDLINKQ
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
B3DQ62
|
Q9GZV3
|
SC5A7_HUMAN
|
Solute carrier family 5 member 7
|
Homo
|
MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGYGLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVDMHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSWLDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMILPIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTKTVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFKTLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNKEAFLDVDSSPEGSGTEDNLQ
|
Transmembrane transporter that imports choline from the extracellular space into the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion-dependent.
|
Q9GZV3
|
Q8BK72
|
RT27_MOUSE
|
Mitochondrial ribosomal protein S27
|
Mus
|
MAAPMVRCGMLLARRLDASRLCLAGKRCLLSAAYVDSHQWEAREKEEYHLADLASLMDKAYERKLPVSSLSISRFVDNIASREDLDSAEYYLYKFRHSPNCWYLRDWTIHSWIRQCLKYGAQDKALYTLVNKVQYGIFPDNFTFNLLMDYFIKKGNYKDALSVVFEIMMQEAFDVPSTQFLSLYVLYRCLAEKTELTWEEERDFGASLLLSGLKQRNTVGLSSQLYGYALLGKVELQRGVRAVYHGMPLMWTPGYLDRALQVMERVASSPEDLKLGREVLDVLDGVLKVVTSPDVQTSEAQPQEGEDGLGSANLVEQLDTEEPEQSKLPRYLERFQASRSKLQELNRVESESLLTLTTQLVKEKLPACEAEDLATYEQKLREWHLERVQLIQREQEQREKAKQEYQALSAAEKAA
|
RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain. Binds to the mitochondrial 12S rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular carcinoma tissues compared with adjacent non-tumoral liver tissues.
|
Q8BK72
|
Q04EY4
|
ECFA3_OENOB
|
Energy-coupling factor transporter ATP-binding protein EcfA3
|
Oenococcus
|
MEINFRNVSFSYQLNTPFSTAALKDVSFDIPDGSFTSIVGHTGSGKSTVLQLIDGLLIPEKGHIQAGSFQMNSGSNAKHLKKFRKNVGFIFQFSENQLFEETVEKDLIFGPKNFGVEEKIAKEKARKVLKIVNLPESFLQKSPLDLSGGQRRRVAIASILISDPQLLLLDEPVIGLDPGSKDEIMNLFSRLNQQGKTIVMVSHEMDDVADYSDQIIVLNAGRISKVGSPEEIFSDESYLRKEKLRLPSAIDFAKQLKKVGFPINVSIKNKRELLREIKKQFEIEKDKK
|
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
Q04EY4
|
Q6MNY2
|
PDRP_BDEBA
|
Putative pyruvate, phosphate dikinase regulatory protein
|
Bdellovibrio
|
MDGDNKTYTIYILSDSTGETAATMIRAALVQYTTKDVNIIRCKNVRTDTQAEAVIEECFERRGMLAYTVASQGLRAKIREMASGKGIPYFDLLGPLLSTLDTFFGQHSEDTVGALRAVDERYFKRIEAIEYTVKHDDGKTFAELDKADIVLVGISRTSKTPLSIFLSHKGWKVANVPLVLDTPLPEELFKIDQRRIVGLIIDMDSLQRIRKSRLEKFGQDPGGSYASMSHIAKEIEYAEKIFKVNRRWPVFNVTERALEETASEIVRIIAARLGLPDSVIF
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
|
Q6MNY2
|
Q9SEH5
|
PMT3_TOBAC
|
Putrescine N-methyltransferase 3
|
Nicotiana
|
MEVISTNTNGSTIFKNGAIPMNGYQNGTSKHQNGHQNGTSEHRNGHQNGISEHQNGHQNGTSEHQNGHQNGTISHDNGNELQLLGSSNSIKPGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPTIEKIDIVEIDDVVVDVSRKFFPYLAANFSDPRVTLVLGDGAAFVKAAQAGYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEVDFKNPVNPIDKETTQVKSKLAPLKFYNSDIHKAAFILPSFARSMIES
|
Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) . Methyltransferase that mediates the conversion of putrescine to N-methylputrescine . Promotes leaves ripening .
|
Q9SEH5
|
Q75KA9
|
CCS1_ORYSJ
|
C-type cytochrome synthesis protein 1
|
Oryza sativa
|
MPSPTCYLLLNPTASRSHHRPRLPLPAAAPPRRRVHVSCDARRTGGGGGGGGVKREAIPAGTGKAKKQVVFFDAAPPVSQRGGGGGGEGEGEGEGEGKVARRKENAALGLVRRLTKRTLSLLSNLPLAISEMFAIAALMALGTVIDQGEAPSYYFEKFPEDNPVFGFITWRWILTPGFDHMFSSPVFLGLLALLAASLMACTYTTQIPIVKVARRWSFMHSAGSIRKQEFAESLPRASIQDLGVILMGYGYEVFTKGPSLYAFKGLAGRFAPIGVHIAMIFIMAGATLSATGSFKGSVDVPQGLNFVIGDVMKPKGVLSFVPDVFNTEVHVNRFYMEYYDSGEVSQFYSDLSLFDLDGKEVMRKTIKVNDPLRYGGVTIYQTDWGFSALQVKKNGEGPFNLAMAPLKLNGDKKLFGTLLPLENSGSSNVKGISMLARDLQSIVLYDQEGKFVGVRRPSSKLPIEIDGNEIVIEDAIGSTGLDLKTDPGIPIVYAGFGALMLTTCISYLSHSQIWALQDGSTVVIGGKTNRAKLEFSEEMNRLLDKVPELISVNEKKIDSKQSAT
|
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
|
Q75KA9
|
Q92561
|
PHYIP_HUMAN
|
Phytanoyl-CoA hydroxylase-associated protein 1
|
Homo
|
MELLSTPHSIEINNITCDSFRISWAMEDSDLERVTHYFIDLNKKENKNSNKFKHRDVPTKLVAKAVPLPMTVRGHWFLSPRTEYSVAVQTAVKQSDGEYLVSGWSETVEFCTGDYAKEHLAQLQEKAEQIAGRMLRFSVFYRNHHKEYFQHARTHCGNMLQPYLKDNSGSHGSPTSGMLHGVFFSCNTEFNTGQPPQDSPYGRWRFQIPAQRLFNPSTNLYFADFYCMYTAYHYAILVLAPKGSLGDRFCRDRLPLLDIACNKFLTCSVEDGELVFRHAQDLILEIIYTEPVDLSLGTLGEISGHQLMSLSTADAKKDPSCKTCNISVGR
|
Its interaction with PHYH suggests a role in the development of the central system.
|
Q92561
|
A0L8Q7
|
PYRH_MAGMM
|
Uridine monophosphate kinase
|
Magnetococcus
|
MDVARAKRVLLKLSGEALMGEQAYGIAPEFLSYLVEEVQSAIALDIELALVIGGGNIFRGISGSANGMGRTRADQMGMLATVINGLALQSALMLSGTEAVVQTALEMPRVAEPFDHDSAKSHMKQGRVVIFVAGTGNPFFTTDTAAALRACEIEADLLLKATKVDGVYDSDPVKNPKAKRFETLTYHEVLTKNLKVMDMTAITLCRENHIPIGVFSIFERGALTAVLRGEPKATIIEERKE
|
Catalyzes the reversible phosphorylation of UMP to UDP.
|
A0L8Q7
|
Q3B4Y9
|
RNY_CHLL3
|
Ribonuclease Y
|
Pelodictyon
|
MGIVINLFLIIFASVVFFAAGFFLGRFFLERLGTTKVLEAEERAVQIVQEAQKEANEYKELKVTEVNQEWKKKRREFDQEVVIKNNKFNQLQKQVQQREAQLKKQLQDVRDTERKLQDQQKELDQAMETVGIRATELERIITEQNQRLESISNLQADEARQMLVDNMITKAREEATETIHKIHEEAEENAGRLAEKTLLTAIQRISFEQATENALSVVHIQSDELKGRIIGREGRNIKAFENATGVDIIVDDTPEVVILSCFDPLRREHAKLTLKKLLADGVIHPVAIEKAYLDAGKEMADVIMSAGEEALASLQIPDMPAEIVRLIGTMKFHSVYGQNLLQHSREVAMLAGIMATELKLDPRLAKRAGLLHDIGLVLPDTDQPHALAASEFLRKFKESAVVLNAIAAHHGEAEKESPIAELVDAANVISLARPGARGAVTADGNVKRLESLEEIAKGFPGVLKTYALQAGREIRVIVEGDNVSDSQADVLAHDIAHKIESEAQYPGQIKVSIVRERRSVAYAK
|
Endoribonuclease that initiates mRNA decay.
|
Q3B4Y9
|
P05123
|
KCRM_CANLF
|
M-CK
|
Canis
|
MPFGNTHNKFKLNYKPEEEYPDLTKHNNHMAKALTPEIYKKLRDKETPSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEESYQVFKDLFDPIIQDRHGGYKPTDKHKTDLNHENLKGGDDLDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSIEALNSLTGEFKGKYYPLKSMTEQEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNEHLGYVLTCPSNLGTGLRGGVHVKLAHLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDISNADRLGSSEVEQVQLVVDGVKLMVEMEKKLEKGQSIDDMIPAQK
|
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
|
P05123
|
Q95741
|
CYB_ARTOB
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Artibeus
|
MTNIRKTHPLLKIINSSFVDLPAPSSLSSWWNFGSLLGVCLGVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWLLRYLHANGASMFFICLYLHVGRGLYYGSYTYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFLLPFIVTALVMVHLPFLHETGSNNPTGIPSDPDMIHSHPYYTIKDILGFLVMLTALASLVLFSPDLLGDPDNYIPANPLITPPHIKPEWYFLFAYAILRSIPNKLGGVLALVMSILILAIVPILHMSKQRSMMFRPLSQCLFWLLVAVLFTLTWIGGQPVEHPYIIIGQTASTLYFLIILFLMPMISLVENYLLKW
|
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.
|
Q95741
|
Q7W183
|
LOLB_BORPA
|
Outer-membrane lipoprotein LolB
|
Bordetella
|
MSVCPAPRSPVRWLHAFTLCLLLAVLAGCVSVPKPMAGAGEDVFSRVGRFAITVTESDGKQQAVQGGFAWRDDGGSYLLDLTNPLGSTEARVEGRPGMAVLTRANGERLAAEHPDALAEDALGSPVPVTGLRDWLRGRLMAGAAPDGLERDAQGRPTAFEQDGWNARLSRYDAQGPQLLVLQRQEPGRRILVRLVITQP
|
Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
|
Q7W183
|
Q47W53
|
UPP_COLP3
|
UPRTase
|
Colwellia
|
MSVFEIKHPLVQHKISLMRAKDMSTRSFRQLSAEVGSLLTYEATKDLELENFQMEGWDGEITGQRLVGKKATVVPILRAGIGMLDGVLELMPSAKISVVGLYRDEETLEPVTYFEKLAGDIDQRLALIIDPMLATGGSMNATIDILKKAGCNDIRALVLVAAPEGIEKVKSAHPDVDIYTASIDDHLNESGYIIPGLGDAGDKIFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q47W53
|
A4FWL3
|
RS11_METM5
|
30S ribosomal protein S11
|
Methanococcus
|
MSQKWGLVHIYASYNNTILHVTDLTGAETIAKVSGGMIVRNQRDESSPYAAMQAAFKIADLMRDKGIDQVHVKVRATGGQKSKNPGPGAQAAIRALSRAGIRIGRIEDATPIPHDGTTPKRKNR
|
Located on the platform of the 30S subunit.
|
A4FWL3
|
Q0SX30
|
DEOC_SHIF8
|
Phosphodeoxyriboaldolase
|
Shigella
|
MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIEIALAETRAAIAYGADEVDVVFPYRALMAGDEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALGHGDGKSASSY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
Q0SX30
|
P53552
|
THO2_YEAST
|
Zinc-regulated gene 13 protein
|
Saccharomyces
|
MAEQTLLSKLNALSQKVIPPASPSQASILTEEVIRNWPERSKTLCSDFTALESNDEKEDWLRTLFIELFDFINKNDENSPLKLSDVASFTNELVNHERQVSQASIVGKMFIAVSSTVPNINDLTTISLCKLIPSLHEELFKFSWISSKLLNKEQTTLLRHLLKKSKYELKKYNLLVENSVGYGQLVALLILAYYDPDNFSKVSAYLKEIYHIMGKYSLDSIRTLDVILNVSSQFITEGYKFFIALLRKSDSWPSSHVANNSNYSSLNEGGNMIAANIISFNLSQYNEEVDKENYERYMDMCCILLKNGFVNFYSIWDNVKPEMEFLQEYIQNLETELEEESTKGVENPLAMAAALSTENETDEDNALVVNDDVNMKDKISEETNADIESKGKQKTQQDILLFGKIKLLERLLIHGCVIPVIHVLKQYPKVLYVSESLSRYLGRVFEYLLNPLYTSMTSSGESKDMATALMITRIDNGILAHKPRLIHKYKTHEPFESLELNSSYVFYYSEWNSNLTPFASVNDLFENSHIYLSIIGPYLGRIPTLLSKISRIGVADIQKNHGSESLHVTIDKWIDYVRKFIFPATSLLQNNPIATSEVYELMKFFPFEKRYFIYNEMMTKLSQDILPLKVSFNKAEREAKSILKALSIDTIAKESRRFAKLISTNPLASLVPAVKQIENYDKVSELVVYTTKYFNDFAYDVLQFVLLLRLTYNRPAVQFDGVNQAMWVQRLSIFIAGLAKNCPNMDISNIITYILKTLHNGNIIAVSILKELIITVGGIRDLNEVNMKQLLMLNSGSPLKQYARHLIYDFRDDNSVISSRLTSFFTDQSAISEIILLLYTLNLKANTQNSHYKILSTRCDEMNTLLWSFIELIKHCLKGKAFEENVLPFVELNNRFHLSTPWTFHIWRDYLDNQLNSNENFSIDELIEGAEFSDVDLTKISKDLFTTFWRLSLYDIHFDKSLYDERKNALSGENTGHMSNRKKHLIQNQIKDILVTGISHQRAFKKTSEFISEKSNVWNKDCGEDQIKIFLQNCVVPRVLFSPSDALFSSFFIFMAFRTENLMSILNTCITSNILKTLLFCCTSSEAGNLGLFFTDVLKKLEKMRLNGDFNDQASRKLYEWHSVITEQVIDLLSEKNYMSIRNGIEFMKHVTSVFPVVKAHIQLVYTTLEENLINEEREDIKLPSSALIGHLKARLKDALELDEFCTLTEEEAEQKRIREMELEEIKNYETACQNEQKQVALRKQLELNKSQRLQNDPPKSVASGSAGLNSKDRYTYSRNEPVIPTKPSSSQWSYSKVTRHVDDINHYLATNHLQKAISLVENDDETRNLRKLSKQNMPIFDFRNSTLEIFERYFRTLIQNPQNPDFAEKIDSLKRYIKNISREPYPDTTSSYSEAAAPEYTKRSSRYSGNAGGKDGYGSSNYRGPSNDRSAPKNIKPISSYAHKRSELPTRPSKSKTYNDRSRALRPTGPDRGDGFDQRDNRLREEYKKNSSQRSQLRFPEKPFQEGKDSSKANPYQASSYKRDSPSENEEKPNKRFKKDETIRNKFQTQDYRNTRDSGAAHRANENQRYNGNRKSNTQALPQGPKGGNYVSRYQR
|
Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.
|
P53552
|
F1Q4R9
|
MEOX1_DANRE
|
Protein choker
|
Danio
|
MEQSASSCMRSPHTGGALWGCVRSPHSGGSGAGIQPYQQAPFALHQKHDFLAYTDFSSSCLVPAPHAYPREDRLYPETHSGYQRTEWQFSPCEPRGRGQEPCQGAAEAVGAEMDSAGGDRLAGAVTGCLEGDYSPQSVPAVDTEKKSSKRKREVTDIQDSSFKADSNCKARKERTAFTKEQLRELEAEFTHHNYLTRLRRYEIAVNLDLTERQVKVWFQNRRMKWKRVKGGQPASPHDLEADELDSAASPSSE
|
Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints. Binds specifically to the promoter of target genes and regulates their expression. Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome. Acts by mediating specification of endothelial cells of the endotome within the nascent somite, notably by repressing expression of cxcl12b.
|
F1Q4R9
|
Q6F1W5
|
ECFA1_MESFL
|
Energy-coupling factor transporter ATP-binding protein EcfA1
|
Mesoplasma
|
MDSLKKFKTTKLTSQDLNDFKIKLHAKYIEMLEANNNFFKFKEAEKQGKISKEELVEYKNKSIKAKKAFKAICQDKSFSENLKNITKIYNSTTRKNSSVILEQAKEELIEAKNLKREARDSVKDHGRGAQLTKLDKVAIKVENLKFKYAPDFPYALNDVSFEINDGEYVAVIGHNGSGKSTLSKMLIGVLSAQEGHVSIYGNVVTQDNLDQARKFLGIVFQNPDNQFIGSSVEADIAFGLENKRVNPKEMQKIIYDSAKKVGMENFLDKEPLNLSGGQKQRVAIASALALNPDILIFDEATSMLDPKGNREIKEIMVELRDKMKKTIISITHDMDEILNADKVIVMNGGRMVKIGKPEEVLKEKEFLRSIKLEIPFLSLVEEALGNEGIKVKHSQNMDELVKQLCK
|
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
Q6F1W5
|
Q8CFK6
|
DEN1C_MOUSE
|
Connecdenn 3
|
Mus
|
MGSTETRHPPAMFDWFFEAGCPNSLEEDPPILRQFPPDFQEQEAMQMVPRFCFPFDIEREPPSPAVQHFTFALTDLVGNRRFGFCRLRAGARSCLCILSHFPWFEVFYKILNNVGDLLAQNQVAEAEELLQNLQQHPLLGPRFSGRSEMDSSITVRSECGILPPALGNSKLLSCFVAPDAASLPSIPENRNLTELVVAVTDENIVGLFAALLAERRVLLTASKLSTLTACVHASCALLYPMRWEHVLIPTLPPHLLDYCCAPMPYLIGVHGSLAERVREKALEDVVVLNADSNTLETPFDDVQALPPDVVSLLRLRLRKVALSPGEGVSRLFLKVQALLFGGYRDALVCIPGQPVTFSEEAFLAQKPGAPLQAFHKKAVHLQLFKQFIESRLEKLNAGEGFSDQFEQEIIACRGASSGTLRSYQLWVDSLKKGSDALLHSMKTKTQPAVRNMYRSGDSLQEYCASKAKSGLKGMQNLLTIKDGDSGLQRGGSLRTPSLTSRSDRLQQRLPISQHFGQNRPLRPSRRLKTEEGPSEPLRERSPTLSPGDTQNPWAEDTLDGSFLGSGEELDLLSEILDSLNVETKSGDLQRASQSLDCCQRGAASESCSSLPDIPVGLPWQLEEDKRSQDPQPWSLPGDLSLLQDTPFSEVVSYSKNSCSQPFQQSPPSQGDPGPSLSKLDPRPSQSPCPKLLRVPTRHSPPESPQLLVSTEPNSDAVQRLQSISSPSCSHSAENPRNQPPQVLLGQACVQPLEELGAPTYVSHVSTQQRPQDKQPRVADLKKCFEN
|
Guanine nucleotide exchange factor (GEF) which may activate RAB8A, RAB13 and RAB35. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form.
|
Q8CFK6
|
Q9ZKX5
|
CATA_HELPJ
|
Catalase
|
Helicobacter
|
MVNKDVKQTTAFGAPVWDDNNVITAGPRGPVLLQSTWFLEKLAAFDRERIPERVVHAKGSGAYGTFTVTKDITKYTKAKIFSKVGKKTECFFRFSTVAGEKGSADAVRDPRGFAMKYYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHTQKRDPQTNLPNPDMVWDFWSNVPESLYQVTWVMSDRGIPKSFRHMDGFGSHTFSLINAKGERFWVKFHFETMQGVKHLTNEEAAEVRKYDPDSNQRDLFDAIAGGDFPKWKMSIQVMPEEDAKKYRFHPFDVTKIWYLQDYPLMEVGIVELNKNPENYFAEVEQAAFTPANVVPGIGYSPDRMLQGRLFSYGDTHRYRLGVNYPQIPVNRPRCPFHSSSRDGYMQNGYYGSLQNYTPSSLPGYKEDKSARDPKFNLAHIEKEFEVWNWDYRAEDSDYYTQPGDYYRSLPADEKERLYDTIGGSLAHVTHKEIVDKQLEHFKKADPKYAEGVKKALEKHQKMMKDMHAKDMHHMKKKK
|
Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
|
Q9ZKX5
|
Q65TI7
|
RL25_MANSM
|
50S ribosomal protein L25
|
Basfia
|
MAFKFNAEVRSAQGKGASRRLRHNGQIPAIVYGGNEDAVSIVLNHDELNNAQAHDSFYSEVITLVINGKEVAVKVQAMQRHPFKPKLVHIDFKRA
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
Q65TI7
|
P24343
|
HXD12_CHICK
|
Homeobox protein Hox-4F
|
Gallus
|
MCDRSLYRSGYVGSLLNLQSPDSFYFPNLRANGSQLAALPTISYPRSSIPWTCPSPCAAQPQGHAFGGAAQPYLPGSVPISISSNSNKECLEENSKYYAHDASSKQEERCRQRQSFANDPTITHAANLKPAKYDHSSLPRSLHGSAALFEVNSCTSSLKEDIKNSVNLNLTVQPAAVQSCLRPSVQDGLPWCPTQGRSRKKRKPYTKQQIAELENEFLLNEFINRQKRKELSNRLNLSDQQVKIWFQNRRMKKKRVVMREQALSMY
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
P24343
|
B2GIZ5
|
RL23_KOCRD
|
50S ribosomal protein L23
|
Kocuria
|
MSVIYNKDPRDVIIRPVVSEKSYGLIDEGKYTFQVDPSANKTEIKYAIEHIFGVKVASVNTLNRPGKRKRTRFGWGQRKATKRAVVSLREGSIDIFGGPLS
|
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.
|
B2GIZ5
|
Q9ESY9
|
GILT_MOUSE
|
Lysosomal thiol reductase IP30
|
Mus
|
MSWSPILPFLSLLLLLFPLEVPRAATASLSQASSEGTTTCKAHDVCLLGPRPLPPSPPVRVSLYYESLCGACRYFLVRDLFPTWLMVMEIMNITLVPYGNAQERNVSGTWEFTCQHGELECRLNMVEACLLDKLEKEAAFLTIVCMEEMDDMEKKLGPCLQVYAPEVSPESIMECATGKRGTQLMHENAQLTDALHPPHEYVPWVLVNEKPLKDPSELLSIVCQLYQGTEKPDICSSIADSPRKVCYK
|
Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds. Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation.
|
Q9ESY9
|
A6WK72
|
PURT_SHEB8
|
Phosphoribosylglycinamide formyltransferase 2
|
Shewanella
|
MIGTPYTEGARRAMLLGCGELGKEVAIELQRLGVEVIGVDRYANAPAMQVAHRSHVINMLDANALRAVIELEKPHLVIPEIEAIATQTLVDMEAEGVNIIPTARATKLTMDREGIRRLAAETLGLPTSPYFFCDTETEFNQAISEIGVPCVVKPVMSSSGKGQSVIRDIALSHKAWQYAQEGGRAGGGRVIVEGFIPFDYEITLLTISAVNGIHFCAPIGHRQEDGDYRESWQPQAMSDEVLAKSQAIASKVVEALGGYGLFGVELFVKGHEVYFSEVSPRPHDTGLVTLISQDLSEFALHVRAIQGLPIPNIHQHGPSASAVILAEGTSSNIRYQGIAAALEAVNTQLRLFAKPDIDGRRRLGVALARDIDIDSAVSKALDSASKVKVIF
|
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
|
A6WK72
|
A4WEI9
|
UPPP_ENT38
|
Undecaprenyl pyrophosphate phosphatase
|
Enterobacter
|
MSDMHSLLVAAILGVVEGLTEFLPVSSTGHMIIVGHLLGFEGETAKTFEVVIQLGSILAVVVMFWRRLFGLIGIHFGRPPQHEGEGKGRLTLIHILLGMVPAVVLGLIFHDAIKSLFNPINVMYALVVGGVLLIAAELLKPKEPKAPGLDDMTYRQAFMIGCFQCLALWPGFSRSGATISGGMLMGVSRYAASEFSFLLAVPMMMGATALDLYKSYHFLTAADFPMFAVGFVTAFLVALVAIKTFLQLIKRISFIPFAIYRFIVAAAVYVVFF
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A4WEI9
|
A0PP03
|
BIOD_MYCUA
|
Dethiobiotin synthase
|
Mycobacterium
|
MTVLCVTGTCTGVGKTVVTAALASQANQAGIDVVVCKPVQTGTGNGDDDLAEIGRLSGVTELVGLARYPLPMAPVAAAEQAGQPLPSRDQLVQHIRGLDRPGRLTLVEGAGGLLVELADSGGTLRDLAVDLGAAMLVVVAAGLGTLNHTALTLEALAAQKVSCAGLVLGSWPAHPGLVESSNRDALARLAPMRAVLSAGAAQLSVADFAVMSAGAFDREWVATLVG
|
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
|
A0PP03
|
Q8P4H2
|
RPOD_XANCP
|
Sigma-70
|
Xanthomonas
|
MANERPAQQSDIKLLISKGLEQGYLTYAEVNDHLPDDLVDPEQIEDIISMINGMGIDVHEVAPDAETLLLNDGNTGNREVDDTAAEEAAAALTALDTEGGRTTDPVRMYMREMGTVELLTREGEIAIAKRIEEGLSQVQAALGTFPLSTELLLSDYEAHKEGKKRLAEIVVGFNDLIEEADAAAAALAAAGPVAVDEDAVDEDADEDGDDDAAEEEAGPTGPDPVEVATRMENLANEYAKFKKAYVKYGAEHKNVAKAREDMAAIFTTLKLPLPLTDALVTQLRGVVNGIKDHERKVLHLATTVARMPRKDFIRSWEGNQTNLEWVEDALKRKQKWSSALRDVKDQIVSEQQGSIEMEKANYLTLAEIKDISRAMAYGEAKARKAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQQFGREATPEELAKEMDMPEDKIRKVMKIAKEPISMETPIGDDEDSHLGDFIEDTNVESPIDNTTNINLSETVRDVLAGLTPREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEQLRSFLDID
|
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
|
Q8P4H2
|
B0BUJ0
|
RL20_RICRO
|
50S ribosomal protein L20
|
spotted fever group
|
MTRAKSGKISKNRHKKILKLAKGYRGRANSCFRVAIEKVEKALQYAYRDRRNRKRDFRGLWIQRINAAVREHGLVYSQFMGALKKTEIAIDRKVLAELAVNNSDGFVSIVEKAKAHI
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
B0BUJ0
|
P67084
|
PLPHP_MYCBO
|
Pyridoxal phosphate homeostasis protein
|
Mycobacterium tuberculosis complex
|
MAADLSAYPDRESELTHALAAMRSRLAAAAEAAGRNVGEIELLPITKFFPATDVAILFRLGCRSVGESREQEASAKMAELNRLLAAAELGHSGGVHWHMVGRIQRNKAGSLARWAHTAHSVDSSRLVTALDRAVVAALAEHRRGERLRVYVQVSLDGDGSRGGVDSTTPGAVDRICAQVQESEGLELVGLMGIPPLDWDPDEAFDRLQSEHNRVRAMFPHAIGLSAGMSNDLEVAVKHGSTCVRVGTALLGPRRLRSP
|
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
|
P67084
|
P82292
|
Z13_BOVIN
|
Spermadhesin Z13
|
Bos
|
DSTDGLLVKDKYLCGDLYGEEYGVIFPYLGLKTECLWTIKMDPLYRILLTVRDVHENCNKESLEIIEGPPESSNSRKICDTSHAEYTSCTNTMTVKYTRKPNHPAPDFFLIFRRVL
|
May be involved in the fertilization process.
|
P82292
|
Q8DI06
|
SURE_THEVB
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Thermosynechococcus
|
MRLLIANDDGVFAPGIRTLADTLAIAGHEVVVVCPDRERSATGHSLTVFDPIRAEVVSDRFHPRIKAWACSGTPSDCVKLALGALLEQPPDFVVSGINQGSNLGTDILYSGTVSAAMEGVIEGIPSIAISLASFTVHDFQPAADFTNRLLKALENAPLPPKVLLNVNVPALPASEIAGVVITRQGIRRYHDLFQKRVDPRGKTYYWLAGEVVEEYPQDPNQAPTDVEAIAQNLISITPLTFDLTYGQGVQDLTEWLRTVQPLFNL
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q8DI06
|
Q822I4
|
EFTU_CHLCV
|
Elongation factor Tu
|
Chlamydia
|
MSKETFQRNKPHINIGTIGHVDHGKTTLTAAITRALSAEGLANFCDYSSIDNTPEEKARGITINASHVEYETPNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGAMPQTKEHILLARQVGVPYIVVFLNKIDMISQEDAELVDLVEMELSELLEEKGYKGCPIIRGSALKALEGDASYVEKIRELMQAVDDNIPTPEREVDKPFLMPIEDVFSISGRGTVVTGRIERGIVKVGDKVQIVGLRDTRETIVTGVEMFRKELPEGQAGENVGLLLRGIGKNDVERGMVICQPNSVKSHTQFKGAVYILQKEEGGRHKPFFTGYRPQFFFRTTDVTGVVTLPEGTEMVMPGDNVEFEVQLISPVALEEGMRFAIREGGRTIGAGTISKIIA
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q822I4
|
Q750S3
|
PUS5_ASHGO
|
Uracil hydrolyase PUS5
|
Eremothecium
|
MNRWAVPILHEHKHYYIVNKVHGIVCQPPDLRTWYKYHDYEPPVLLDLLRKQHPNFGGEVWRTVHRLDEPVTGGVLVSRNKRAAAMFSRSLALGGNRGFPLTRRYVALLAREAKGLPSEGRITMGDMITDYKRLENDLVLLQLQTGRKHQIRKQMAQVFGQPVVNDKMYGGDSVDGIVDNLIGLHSAFIGAQCGLQARTYLIPIPRTQDAFKLWDKYIDEQGGFIPSVQKELRDFSLPSKLENTITLLSGGQGGIQISYK
|
Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
|
Q750S3
|
A1XIM1
|
MEP3_TRISD
|
Fungalysin MEP3
|
Trichophyton
|
HNVVDYVASAEYKVFAWGLNDPTEGNPTSIRDPWTDASPYTWNSDGMSKYPTTRGNNAIAQDNPTGGSTYINNYRPQSPNLIFSYPWSPTATPPSSYKDFSITQLFYTTNRYHDLLYSFGFNEAAGNFQVNNGNKGGKGNDFAIVNAQDGSGTNNANFATPPDGSPGRMRMYNWTTARPNRDGCLEAGIVIHEYTHGLSNRLCGGPANSACLNALESGGMGEGWGDFYATAIRLKPRDTKNTNYSMGAWAANNPKGIRAYLYSTNLQTNPYMYTSVNSLREVHQIGTVWASMLYDLMWALIEAHGGTYSANPVFRNGVPQDGRHLSMKLVMDGMALQPCNPNFVQARDAILDADRALTNSANKCTIWKAFAKRGLGYGAKYDARNRTGSNK
|
Secreted metalloproteinase probably acting as a virulence factor.
|
A1XIM1
|
B7KUT4
|
NRDR_METC4
|
Transcriptional repressor NrdR
|
Methylorubrum
|
MRCPFCGGPDTQVKDSRPSEDSSAIRRRRVCPDCGGRFTTFERVQLRELVVLKRSGKRVPFDRDKLQRSIDVALRKRTVDPERVERLVSGITRRLESGGEGEVTSEAIGEAVMEGLKGLDDVAYVRFASVYKNFREAQDFQDLLGTLGERLDGEGDLPEQGDAVPAPPDEAVAAPRRGRPARKRA
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
B7KUT4
|
Q9V076
|
RNJ_PYRAB
|
Pab-RNase J
|
Pyrococcus
|
MWEEINMIKIYTLGGYEEVGKNMTAVEYNGEVVIVDMGIRLDRVLIHEDVEFQKMSSKDLRKLGAIPDDRPIRNKKVVAIALSHGHLDHIGAVGKLAPHYPDVPIYGTPYTIRLAKSEIKGEEYFEVTNPLYETNYGEIVQVSENLAIEFVQITHSIPQSSIVVIHTPEGAVVYACDYKFDNNHPYGERPDYKRLKELGKEGVKVLIAESTRVAEETKTPSEAVAKMLLEDFFLYEGMEADGLIATTFASHIARLQELIEIANKMGRQAIFIGRSLAKYTGIAKQLGLIKMKGSRVLRSPNAVSKVLKEVSQARENYLLIVTGHQGEPGAILTRMANGELYDIGPRDTVVFSAGVIPNPLNVAQRYALETKLRMKGVRMIKNLHVSGHASKEDHRYLIRMLNPEYIVPAHGEFRMLTHYAELAEEEGYMIGKEVFISRNGHVVEIPGSLEG
|
A highly processive 5'-3' exoribonuclease; no evidence has been seen for endonuclease activity. Prefers 5'-phosphate or 5'-hydroxyl ends; 5'-triphosphate substrates are very poorly degraded, does not degrade circular RNA. Does not degrade pre-tRNA(Trp) suggesting it is inhibited by strong secondary structures. Also degrades ssNDA but not dsDNA.
|
Q9V076
|
O98462
|
RPOA_SPIMX
|
Plastid-encoded RNA polymerase subunit alpha
|
Spirogyra
|
MGQYTINLRESYPVWKIGSKIDSTKEECLDYMLFIASPLLAGQATTLGVAIRRTLLESIQGTAIVAAKIYGAAHEYSTLEGIQESIHDILLNLKQVIIKNKICEFQKCLISIIGPKKVTAADIELSQNITISNPYHHIATITKPIRFQVELIINKGRGYLIQDGNDVQDGYFPVDALFNPVRNVNFSIHNLAEQQEALILEIWTNGAITPLDALRQGSENLIHLFLPPFGLEDDTYMTSLGSQDYNIHIKNSLKEKFELHSIERIEDSHLIKDQFLEYSKTPIELLELSTRPFKCLKNANIYTINDLLKLSQQDLLKISNMGPSSVKQIVEALDKRFGINLKLK
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
O98462
|
A8AHD6
|
ASTE_CITK8
|
Succinylglutamate desuccinylase
|
Citrobacter
|
MDNFLAQTLAGISPDITQGETESFHWRWQMPGVLELTPAVEVDRALVLSAGIHGNETAPVEMLAALLSALFEGKIPLRWRLLVILGNPPALAEGVRYCHSDMNRMFGGRWQMFEESGETLRARELEQLLEDFYSRRKTRIRWHLDLHTAIRGSRHVRFGVLPQRSIPWDEHFLSWLGAAGLEALVFHQTPGGTFTHFSCEHFGALSCTLELGKALPFGHNDLTQFTPTAQALATLLAGEKPMEGGTRPIRYRVVAQITRRSDAFVLCMDNQTLNFTPFKKGTLLAQDGDEQVIVTHDVEYVLFPNPNVACGLRAGLMLEKLA
|
Transforms N(2)-succinylglutamate into succinate and glutamate.
|
A8AHD6
|
A8FP46
|
DNAA_SHESH
|
Chromosomal replication initiator protein DnaA
|
Shewanella
|
MAVSLWQQCIGRLQDELSAQQFSMWIRPLQAQMDGDTLVLYAPNRFVLDWVRDKYINIINQFFTEQMGSDAPKLRFDIGSRPSAPRPVQATAAVERPKFEQNTKPAKTSFNVNSPEPAMAANHRSNINRTYQFENFVEGKSNQLGKAAAMQVAENPGGAYNPLFLYGGTGLGKTHLLHAVGNGIIKNNPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALFIDDIQFFANKDRSQEEFFHTFNALLEGNHQIILTSDKYPKEIDGVEDRLKSRFGWGLTVAIEPPELETRVAILMRKAQESGINLPDEVAFFIAKRLRSNVRELEGALNRVIANANFTGRPITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKMADMLSKRRSRSVARPRQVAMALSKELTNHSLPEIGDAFGGRDHTTVLHACRKIAQLREESHDTKEDYANLIRTLSS
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
A8FP46
|
P07334
|
CDR1_SCHPO
|
Protein kinase nim1
|
Schizosaccharomyces
|
MVKRHKNTIGVWRLGKTLGTGSTSCVRLAKHAKTGDLAAIKIIPIRYASIGMEILMMRLLRHPNILRLYDVWTDHQHMYLALEYVPDGELFHYIRKHGPLSEREAAHYLSQILDAVAHCHRFRFRHRDLKLENILIKVNEQQIKIADFGMATVEPNDSCLENYCGSLHYLAPEIVSHKPYRGAPADVWSCGVILYSLLSNKLPFGGQNTDVIYNKIRHGAYDLPSSISSAAQDLLHRMLDVNPSTRITIPEVFSHPFLMGCTSLSSMDSTTPPTPSLSIDEIDPLVVDCMCVLWKKSSSKKVVRRLQQRDDNDEKYVYKVLSEILRDDMLKKQRFDENKYLSLYDLIHDNNLFTKASISTTSLVKSNVSTNSRKSSNFEDELARRVSSPLSALNQMSQSPIPIRVSSDKDYDSYACHEVVSNPSTLDDDYNYMFVCPPEEYTYSTDNVRTDSLDLQSLPTPTLEQLESVPFNRYGYVRIFPSTTLSSTASGYYTPDSLSTPEPSIDGLTNLDDVQVGGFVQGSGNQNRRPISFPVISNMQPNITNVRSASAPLCSSPVPSRRYSQYATNARYTPRKVSSGSVLRKISSFFRKD
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This protein, a dose-dependent mitotic inducer, appears to function as a negative regulator of mitosis inhibitor wee1 by phosphorylating and inactivating it.
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P07334
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A6TVQ2
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MURQ_ALKMQ
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N-acetylmuramic acid 6-phosphate lyase
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Alkaliphilus
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MLNNLEQLTTEKVNLETLNIDEKSPLEIVKVINEEDKKVALAVEKELPNIAKAVEKIIEAFKTNGRLIYLGAGTSGRLGILDAAECPPTFGTSKEQVIGLIAGGREALLEAVEGAEDSKEEGIKDLKNIKLTSQDIVVGIAASGRTPYVVGGLNYANNIGATTVALCCNKDAVITRVADIAIVPVVGPEVIAGSTRLKSGTAQKLVLNMLTTASMIGVGKVYKNLMVDVQTTNEKLEDRSKRIVMMATGVGEIEATEILKNSNYQPKVAILMINTGCSFVEATAKLQEAGGFVKKALEYIKEGEEIC
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Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
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A6TVQ2
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