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2.75k
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AlphaFoldDB
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A1AXS4
DCUP_RUTMC
Uroporphyrinogen decarboxylase
Candidatus Ruthia
MLFDYINALLKKPTLRTPIWVMRQAGRYLPEYRETRIKAGDFLTLCKSPELACEVTMQPIDRFDLDAAILFSDILTIPDAMGLGLYFLEGEGPKFSNPLNTLSSIEQLKKPNVGNELSYVTDAVSVIKKALNNKVPLIGFTGSPWTLATYMVEGGSSKNFVKVKGLMYENPVYMHQLLDKLSDIIIDYLNGQIQVGVDSVMIFDTWGGLLNKQSYEDFSLQYMTKIVNGIKRKFNGKTIPITLFTKGGAMWLEQIANSGCDGVALDWTVELNDAQQRIGAKVALQGNLDPCVLYASPEKIREEVKKILSQFQGDTGHVFNLGHGISPDVNPEHMKVLVDVVHEFSKR
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
A1AXS4
Q9C8Y4
ATA15_ARATH
Protein ARABIDOPSIS A-FIFTEEN
Arabidopsis
MALNVSKVVPNSPILVKSVNASRSRRVLLAYVHHPLAANKGSSIEELKQGLCCTKTVTFVSSRRCSTLCFVGKSQDTETNSQVVQKEGEKQVMPRRKSSNSSQLLVEYVSNDAKFVNERARNDFVLLSRGIMRLDARARQDVAILGSGFLKLDARAREDTEKIDRDVKRKAERLHHIATIFKNIAESKLKNAADKHWSDGALEADLRRADFRAKQRAMEDALMALEFIKNIHDMMVNKMVDSLVTSETGTTDRISLEKNGIALGFFPGEVSSDRISAIEEAYKSMASALSEADGIDYTDPEELELLVTTLIDLDAMDGKSSASLLAECSSSPDVNTRKALANALAAAPSMWTLGNAGMGALQRLAEDSNPAIAAAASRAINALKKQWEVEEGDSLRFMMNFERPNDDDDVDSDLDEI
Involved in modulation of redox homeostasis to regulate leaf senescence mediated by age and stress factors during plant development. Its function is dependent of EIN2, a central factor of ethylene signaling.
Q9C8Y4
C6E4Q6
RL4_GEOSM
50S ribosomal protein L4
unclassified Geobacter
MAKLDVFDIKKAKVGEIELDDAVFNDDVREYLIHEAVKIQLANRRQGTVAVKNRALVAGSGKKPFKQKGTGQARQGCRRAPQYPGGGVAFGPQPKDYNLSMNKKARKAALRSALSMLYKKDAITVVNSLELPSIKTKAFVEVLTAFNLDKTLVITDTATPTLELSARNVKHVKVLGPEGLNIFDIMKYQSVVFTEAAVRRVEGALQS
Forms part of the polypeptide exit tunnel.
C6E4Q6
B7KNU8
RL25_METC4
General stress protein CTC
Methylorubrum
MSATKTLEAVARDRVGKGAARAVRRQGQIPAVIYGGNQAPQAIAIDLIRARTLIYAGGFKTTVFEIDAGGKKTRAIPRDYQLDPVSGVPLHVDFLRVVAGQTVTVDVPVHFVNEDQAPGIKQKGGTLNVALHTVSLEVAPDQIPDAIEVDLAGREIGDVIHASDLRLPAGTYTGEPTDTVANLLPPTVLGADVEAEEAAVAEAQSAESAEGKAEAEAEATNEKNKSEA
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
B7KNU8
Q9XED8
ARFI_ARATH
Auxin response factor 9
Arabidopsis
MANRGGEYLYDELWKLCAGPLVDVPQAQERVYYFPQGHMEQLEASTQQVDLNTMKPLFVLPPKILCNVMNVSLQAEKDTDEVYAQITLIPVGTEVDEPMSPDPSPPELQRPKVHSFSKVLTASDTSTHGGFSVLRKHATECLPPLDMTQQTPTQELVAEDVHGYQWKFKHIFRGQPRRHLLTTGWSTFVTSKRLVAGDTFVFLRGENGELRVGVRRANLQQSSMPSSVISSHSMHLGVLATARHATQTKTMFIVYYKPRTSQFIISLNKYLEAMSNKFSVGMRFKMRFEGEDSPERRYSGTVIGVKDCSPHWKDSKWRCLEVHWDEPASISRPNKVSPWEIEPFVNSENVPKSVMLKNKRPRQVSEVSALDVGITASNLWSSVLTQPHEFAQSCITSQWSSPQQCHRDANEDAKKSDWLNNSYSVSNVAKDSTLNDQMVSPVEQKKPETTANYRLFGIDLMSSSLAVPEEKTAPMRPINISKPTMDSHSDPKSEISKVSEEKKQEPAEGSPKEVQSKQSSSTRSRTKVQMQGVPVGRAVDLNALKGYNELIDDIEKLFDIKGELRSRNQWEIVFTDDEGDMMLVGDDPWPEFCNMVKRIFIWSKEEVKKMTPGNQLRMLLREVETTLTTTSKTDNHSN
Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Q9XED8
Q87SZ2
RS13_VIBPA
30S ribosomal protein S13
Vibrio
MARIAGINIPDQKHAVIALTAIYGIGKTRSQAILAEVGIAEDVKISELTEEQIDQLRDGVAKYTVEGDLRREVSMNIKRLMDLGCYRGLRHRRSLPLRGQRTKTNARTRKGPRKPIKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Q87SZ2
A0A5Q0QN66
AGR6_AGRAE
Terpene cyclase Agr6
Cyclocybe
MPGSANWTADRFYIPDTLANWPWPRAINPAYEECKAASAAWCEKYGAFSARAQKAFNLCDFNLLASLAYAGLPADVNRVGCDLMNLFFVVDEHTDAMDARSVQDWVDIVVDALHHPHTPRPAGEPKVGEIARTFWENGIKCMGPTAQRRFVETFTTYLQSVVTQAQDRDKHLFRDVDSYMEVRRDTIGAKPSFALLEHDMELPDDVFYHPLLEKLREWAIDMLILGNDLCSYNVEQSRGDDGHNIIRLAMLQENTNVHGALRFVSKMHDDLAEKFLSNYQGMPSFTPQIDAWVTRYIDGLGNWVRANDSWSFESWRYFKGDVLRVQAERWVELLPPAPKDELTSSIPPESRWIKPAVEPSRARPNNVGIVALDTYTPTSEDDFQTLAVKTVSSLLSKYNINPVSVGRLDICIERAADPYIIYALRDAFASAGNTDVEAIVSSSKSVVGLFNAINWVESSSWDGRYAIVFAGDLSSGVSAALVGPDAPIVVEPTRGTYLGDPIASTDEAQGSYIDSLFQSYSHYRKKHPQFSKTSGAPNGAHTPTTTNGSIKSNGFVSGDTNGHANGNGHVQTRSSTPSSSSSSTSSPSFDYMILHDRHGKIPTGAGSIYLGLASLITDIAPETLAGKSIGVFGFANSTSTFFGIRVAGDCSVICKQLQA
Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to delta(6)-protoilludene.
A0A5Q0QN66
P0C7I1
CM3E_CONPI
Psi-conotoxin pr3e
Phasmoconus
MSKLGVLLTICLLLFPITALPVDGDQPADRPVERMQDNISSEQHPFFEKRAARCCTYHGSCLKEKCRRKYCCGR
Psi-conotoxins act on postsynaptic membranes, and act as non-competitive antagonist of nicotinic acetylcholine receptors (nAChR). Reversibly inhibits both adult- and fetal-types nAChR. The inhibition potency against the adult- (alpha-1/beta-1/epsilon/delta) is higher than against the fetal-type (alpha-1/beta-1/gamma/delta). Induces flaccid paralysis in goldfish, but does not induce any remarkable behavior in mice and does not block action potential in directly stimulated frog muscle preparations.
P0C7I1
C4Z520
FMT_LACE2
Methionyl-tRNA formyltransferase
Lachnospira
MRVVFMGTPDFAVGTLKAIIEAGHDVAAVVTQPDKPRGRSKSLVFSPVKDEAVAHGITVLQPERARDEAFVEELRTYNADVIVVVAFGQLLPASIINMPRYGCINVHASLLPKYRGASPIQWAVIDGCEYSGVTTMKMDEGLDTGDILMVEKVKLDAKETGGSLFDRLSDVGAHLLVKTLEGLEAGTITPVKQDDSESTYVKMLHKSFGKMDFNKSAAELERLIRGLNPWPSAFTYIDGKMLKIWDADVADNISEVQTEEVKPGQVVTVGKNTFTIACGQGYLVVNEVQLEGKKRMDSGSFLRGNQLEAGVMLGE
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
C4Z520
C1FSA8
ADDA_CLOBJ
ATP-dependent helicase/nuclease AddA
Clostridium
MSSTKWTDEQRQAIFTKNCNLLVAAGAGAGKTAVLVQRIIEKILDKEEPIDIDKLLVVTFTNAAAAEMRERIGDAISKGLDEDPESKVLRKQLTLLNKSNIMTIHSFCLQVIKNNFHTIEIDPNFRICDETEGILMKQEAIDELFDELYEIENEDFINLVESYASRKDIRLQEVVLELHRFAKSAPFPYTWLLNMAEGFNVGENFNFEETLWADMIMEDMKVLLHGFKNMLQQSIDVILNSEGIDYYYEPFKMDLSFINSLLEKSSFKEFRGEIIAYDFPKLPLKRNKDADKEAKERVKKLRDRVKKRIIELRITLNSYENEFTKKEFIFLYPSMKALSNLVILFDKKYEAKKRERDLIDFNDIEHLCLSILTDKNSEGHIIPSDIALNYRKKFAEVLIDEYQDSNLVQEVIMSMVSRVKGYWSFYNGQLIFNEEEINLEEPQIGLDIPNRFMVGDVKQSIYRFRQAKPEIFLDKYNEYSEEEGTKNRKVKLFKNFRSREEVINGVNYLFKQIMSKTIGELDYTEEEALKVGASYGEEVKGEPIELCLMDKKYEISEEVLKEYNVDEEEALDNIQLEGRLVAKKIQKLVGNNLEGGLKVFDRKLGEYRNLQYRDIVILMRATSNWAPVFVEELAKEGIPVFADTNSGYFDTAEIKTMISLLQIIDNPLQDIPLLSVLRSPIASFTDDELIDIRMVNKNITFYECMEIIYRLYKNEKLDSYYSFYIEDENKINKIIKDMNEKLKNKICSFIEKLKLWREKSIHIDIDEFIWFLYVETGYYGYAGALQAGEQRQANLRILFQRAKQYAKTSYKGLFNFINFINKLKFSSGDMGSAKILGENENVVRIMSIHKSKGLEFPVVILSGTGKNFNMMDLNKNILFHRDLGYGPDYVDTERRIAYPSLVKNIIKNKIRLETLSEEMRILYVALTRAREKLIITGLINNMDKTVEDWLNLSEDKNKVPEYAVMSGKTYLDWIGPALIKHKDAVSFREELKMTSELSNIVDDKSKWKIELWNKRELLKEKVEEDEVEISEKIKETLMNLEESDYKEEIYKRLSFKYKYDNASSIPTKLSVSDVKKQFILDEKENTEELFKKLELRKPMFMEEKKKISPSERGTIIHLFMQHLDLKKAENEEDIKEQINRLIEREFITYEQSKVISSYKILKFCRGELGKRILNSNNVNKEMPFSIEIPALEIYKELDKEIYKDEKLIIQGVIDCYFEEEDGLVLLDYKTDYVNDIEEIKNRYEIQIKYYEEALNRITGKNVKDKYLYLFSVDNYIKID
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
C1FSA8
Q9KVE0
MURQ1_VIBCH
N-acetylmuramic acid 6-phosphate lyase 1
Vibrio
MKIDLTRLVTESRNPASEQIDTLPTLDMLKVINQQDQLVALAVAQTLPQVAQAVEAIATAFAQGGRLIYMGAGTSGRLGILDASECPPTYGSQPEQVIGLIAGGHTAILKAVENAEDNRELGQSDLKALHLSEKDVLVGIAASGRTPYVIAGMEYARSVGATVVSLACNPGCPMEAYADIVITPVVGAEVVTGSSRMKAGTAQKLVLNMLTTGAMIKSGKVFGNLMVDVEATNAKLIQRQTNIVVEATGVSAEQAEAALAACGRHCKTAILMILGGFSAEQAAQKLTQHQGFIRAALNQE
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Q9KVE0
P52630
STAT2_HUMAN
p113
Homo
MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF
Signal transducer and activator of transcription that mediates signaling by type I interferons (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state . In addition, has also a negative feedback regulatory role in the type I interferon signaling by recruiting USP18 to the type I IFN receptor subunit IFNAR2 thereby mitigating the response to type I IFNs . Acts as a regulator of mitochondrial fission by modulating the phosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate and inactivate the GTPase activity of DNM1L respectively .
P52630
B9L9C2
COAD_NAUPA
Pantetheine-phosphate adenylyltransferase
Nautilia
MYTKAIYPGTFDPVTNGHLDIIKRACKMFDKIIVAVADNKDKKTMFSLEKRVELMKKATSHLPKIEVESFNSLLVDFAREKECKIIIRGLRAVSDFEYELQMGYANKSLDSEIDTIYLMPNLENAFISSSVVRSILKYNGDVSHLIPNEIIKDL
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
B9L9C2
A0A0B5LB55
MPAH2_PENBR
Mycophenolic acid biosynthesis cluster protein H'
Penicillium
MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL
Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 . MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA . The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
A0A0B5LB55
A1JKR7
NDK_YERE8
Nucleoside-2-P kinase
Yersinia
MAVERTFSIIKPNAVAKNNIGAIYARFESAGFKIIAAKMLHLTKEQAEGFYAEHKGRPFFDGLVEFMTSGPVMIQVLEGENAVQRHRDIMGATNPDNALAGTLRADFADSFTENAVHGSDAVESAQREIAYFFSENEICPR
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
A1JKR7
P20119
PSAF_PEA
PSI-F
Pisum
AISGLTPCKESKQFAKREKQ
Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
P20119
Q1DEM0
POMZ_MYXXD
Positioning at midcell of FtsZ
Myxococcus
MEAPTYSSKQVAEMLGVSPKQIPEESRKDAYTPDDIWELRTTLDRFPARLGHRRQLFLNFKGGTGKTSLSTSYAWRLAELGYAVLLIDLDSQGHATKCLGYEGEDFEKTLLDVLVRKTPLAKVIQKSSLPNLDFVPSNLTMSTVDLALMPMAGREFKLRNALKDVEAQYDVVVFDAPPSFGLLNLNALMAANDLFVPVLADFLSFHGLKLLFETVQSLEEDLNHVLDHVFIVVNSFNATFKLAKEALEALQTHYPEFLLPTIIRQCTKFAQASSEGRPVFVADPSSKGANDIQAMIDNILPRLVAAAAVAQTKGTQQAG
Spatial regulator of cell division that is involved in identifying the incipient division site, recruiting FtsZ to the division site and stabilizing the Z-ring. Binds ATP and GTP.
Q1DEM0
Q48LF6
MNMC_PSE14
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Pseudomonas
MTITRHARIDWDEQGNPRSRDFSDVYFSTESGLDETRHVFLVQNDLRRRFSELPEDGRLIIGETGFGTGLNFLCAWQLFDECAPAEARLQFVSVEKYPLSRADLQRALALWPELSRFARQLLDQYVAVHEGFQRLAFDDGRVTLTLLIGDALQMLPQLDGQIDAWFLDGFAPAKNPEMWTPELFAELARLSAPSATIGTFTSTGWVRRSLNAAGFKMKRVPGIGHKWEVLRGTFIAWPEDVAHPPAAKPWFARPAPIGGERKALVIGAGLAGCATAQSLAQRGWQVSLLERHAAPAQEASGNPQGVLYLKLSAHGTALSQLILSGFGHTRRLLERLQRGVDWDACGVLQLTFDDKEAQRQKQLADAFPESLLHLLDQPAAEAQSGVALNSGGLFYPEGGWVHPPALCHAQAAHANIRLIAHQQALELRRVDDQWQVWSDEQLIDSAPVVVLAGAADIQKFSQSADLPLKRIRGQITRLPQTQASAALRSVVCAEGYVAPARLGEHTLGASFDFNSTDLTPNLADHLGNLGLLREISEDLTSRLDTADLSPEQLQGRAAFRCTSPDYLPIVGPLADREAFLQAYAALGKDARQVPNIACPWLDGLYVNSGHGSRGLITAPLCGELIAAWVDNEPLPLPRSVAEACHPNRFALRGLIRGGGK
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Q48LF6
Q24UN9
QUEA_DESHY
Queuosine biosynthesis protein QueA
Desulfitobacterium
MKLEDFDFELPEDRIAQHPVEPRDSSRLMVMNRWTGEIEHRVFRELPELLQAGDVLVVNNTRVIPARLIGEKEGTQAKIECLLLTRRDKDVWETLIKPGKRLKAGQTVVFGDGLLRGELLEILPDGNRLVRFNYQGIFEEVLDQLGNMPLPPYITEQLQDKERYQTIYAKESGSAAAPTAGLHFTPELLERLQDKGVEIVEILLHVGLGTFRPVKVENVEEHTMHSEYYRVTPDAAERINRAKSQGRRVIAVGTTASRTLESVAGENGRIEGKEGWTDIYIYPGYTFKILDGLITNFHFPKSTLVMLVSALAGRDQILKAYQIAIAEGYRFYSFGDAMMIL
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Q24UN9
P67657
MTNN_MYCBO
S-adenosylhomocysteine nucleosidase
Mycobacterium tuberculosis complex
MAVTVGVICAIPQELAYLRGVLVDAKRQQVAQILFDSGQLDAHRVVLAAAGMGKVNTGLTATLLADRFGCRTIVFTGVAGGLDPELCIGDIVIADRVVQHDFGLLTDERLRPYQPGHIPFIEPTERLGYPVDPAVIDRVKHRLDGFTLAPLSTAAGGGGRQPRIYYGTILTGDQYLHCERTRNRLHHELGGMAVEMEGGAVAQICASFDIPWLVIRALSDLAGADSGVDFNRFVGEVAASSARVLLRLLPVLTAC
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
P67657
A7I1F0
LEPA_CAMHC
Ribosomal back-translocase LepA
Campylobacter
MENIRNFSIIAHIDHGKSTLADRLISECNAVEDRQMSSQVMDTMDIERERGITIKAQSVRLEYKMNDKKYILNLIDTPGHVDFSYEVSRSLASCEGAILVVDASQGVQAQTIANVYIAIEHNLEIIPVLNKIDLPNADPDRVKNEIEHIIGIDCTDAIEVSAKTGIGIKDLIEAIIKRIPAPKIEPKKPLKAIIYDSWFDNYLGALALIRVYDGEIHKNDEVFIMGTEKKHIVLDLMYPNPISPIKTEKISSGEIGIVVLGLKNVSDVSVGDTITLSNNKANTPIGGFERAKPFVFAGIYPIETDKFEDLRDALNKLKLNDSSISYEPETSLALGFGFRVGFLGLLHMEVIKERLEREFNLNLIATAPTVTYEIYLTNGEMLKIHNPSELPPISNIQMIKEPYSHATIITPAEFLGNLITLLNSRRGIQTKMDYITSDRVLLEYDIPTNEIIMDFYDKLKSGTKGYASFDYEPIDYKQGDLIKLDIKVAGENVDALSIIVPRDKALQKGRDLVKAMKEIVPRQLFEVAIQASIGNKIIARENVRAMGKNVTAKCYGGDITRKRKLLEKQKEGKKRMKSIGKVNLPSEAFLSVLKID
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.
A7I1F0
A9IR81
DAPE_BORPD
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Bordetella
MTADSAVLALVRELIARPSVTPDDVDCQLLLAQRLEHAGFRCETIARGDVTNLWARRGNAGPLVVFAGHTDVVPPGPRDKWDSDPFVPTERDGYLYGRGAADMKSSIAAFVVAAEEFTAAHPGHDGSIALLLTSDEEGPAVDGTVIVCDELRARGEQPDYCIVGEPTSGDVLGDTCKNGRRGSLSGRLTVKGIQGHVAYPHLARNPVHQLAPALAEMAATEWDRGNEYFPPTTFQVSNLRAGTGATNVVPGEAVVLFNFRFSTASTPEGLKQRVHALLDKHGLEYELDWELGGEPFLTPRGPLTDALVAAIRAETGVAAELSTTGGTSDGRFIAKICPQVIEFGPCNATIHKVNERIELASLEPLKNIYRRTLENLLLPR
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
A9IR81
Q2MFP3
DOIAD_STREY
2-deoxy-scyllo-inosamine dehydrogenase
Streptomyces
MKALMFKAPLQAVLTERDVPEPAPGEALVKLAYNSICGSDLSFYKGVWHGFTYPVVPGHEWSGTVVEAGGGAADLVGQNVVGDLTVACGSCRHCTVGKPTLCADLQELGFTRDGACAEYMTVPTGNLHRLPEGLSLREATQVEPLAVALNAVDRLAVTAGEKVAITGAGGIGLLLAQAVRLRGAEVTVLAEPVTERRQAAHALGVPHTVGGDPGELVGFVEKHPELTPDVVLEASGYPLAVQEAVEAVRSGGRIGLIGYRIEEAATMAPHHIVVKVLSLQASMGPGDRFGEAIELLAAGAVDVDALLSHEFGLADHDRALDVALRRADGNTRSYFNLRA
Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).
Q2MFP3
A1ALV7
RL18_PELPD
50S ribosomal protein L18
Pelobacter
MARTAQKLITRIKRKVRVRKKIVGTAQRPRLNVFKSARHIYAQLIDDTAGITLASCSTLSTSAESLSYTGNIAAAVHVGKEIAGLAKEKNITAVVFDRNGFLYHGRIKALADAARESGLLF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
A1ALV7
A1KB15
RL5_AZOSB
50S ribosomal protein L5
Azoarcus
MARLQQFYKDEVVPQLLKQFGYKSVMEVPRITKITLNMGVGEAVGDKKVLENAIGDMTKIAGQKPVATKARKSIAGFKIREGYPIGCMVTLRGPRMFEFFDRLVTVALPRVRDFRGIAAKGFDGRGNYNLGVKEQIIFPEIEYDKIDALRGMNISITTTAKSDDEARALLAAFKFPFKN
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.
A1KB15
C0Z887
UNG_BREBN
Uracil-DNA glycosylase
Brevibacillus
MTTILQNDWAPVLADEFEKPYYVKLRQTLKEEYQTQTIYPDMFHIFTALHLTEYQNAKVVILGQDPYHGPGQAHGLSFSVKPGIKPPPSLVNIYKELKSDVGFEIPQHGYLNHWAKQGVMMLNTVLTVRRGTPNSHKDIGWETFTDRIIHLLNDRETPLVFILWGKHAQEKAAFIDRNKHFVIASPHPSPFSANRGFFGSRPFSRTNEFLRSRGLQEIDWQLPMQVEEE
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
C0Z887
O81185
CAMT1_EUCGL
Trans-caffeoyl-CoA 3-O-methyltransferase 1
Eucalyptus
MATAGEESQTQAGRHQEVGHKSLLQSDALYQHILETSVYPREPEPMKELREITAKHPWNIMTTSADEGQFLNMLLKLINAKNTMEIGVFTGYSLLATALALPDDGKILAMDINRENYELGLPVIQKAGVADKIDFREGPALPILDQLIEDGKQGSFDFIFVDADKDNYLNYHKRLIELVKVGGLIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRIS
Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.
O81185
P0C252
I2BA_CONEM
Kappa-conotoxin-like Em11.10
Virgiconus
CFPPGIYCTPYLPCCWGICCGTCRNVCHLRIGKRATFQE
Inhibits the vertebrate voltage-gated potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3.
P0C252
O30444
PXPA_BORPE
5-oxoprolinase (ATP-hydrolyzing) subunit A
Bordetella
MNPAIDLNCDMGESYGAWRMGNDEAVLQFVTSANIACGFHGGDPSTMRQTVAAALAHGVALGAHPSLPDLAGFGRRAMQITPQEAYDLVVYQVGALAGVAASQGARLHHVKAHGALYNMAAKDAALARAICQAVRDVDSDLVLYGLAGSALIDAARAIGLRAAQEVFADRTYQADGQLTPRSQPDAMITDLDQAIAQVLGMVRDGSVRTPDGQTVALQADTLCIHGDQPDALVFARGIRLALERDGIAIQAA
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
O30444
B1KKX6
MURC_SHEWM
UDP-N-acetylmuramoyl-L-alanine synthetase
Shewanella
MGNDKEKYSKLRNIIPEMRRVKHIYFVGIGGAGMGGIAEVLVNEGYRLSGSDIAENAVTQRLASLGAKIHLGHKEEQVHGADVVVVSTAIHADNPELLEAQALRIPVVRRAEMLAELMRYRHGVAVAGTHGKTTTTSLIASVYGQAERDPTFVIGGLLNSAGTNARLGNSRYLIAEADESDASFLHLQPMVSVITNIEADHMDTYEGDFERLKSTFIDFLHNLPFYGIAVMCIDDPVVRELLPSVGRKIVTYGFSEDADVQALNFVQDGYRSRFTLRRTGVEDVEVMVNLPGEHNVLNALAAIAVASEDEIEDEAIIQALADFEGIGRRFEQLGCFDTDRGEVVLVDDYGHHPSEVAATIKAAKLGWPEKRLVMIYQPHRYSRTRDLYEDFVEVLSQVDCLLLLDVYSAGEAAIPGADSRALCRSIRLRGQLDPIFVADQEQLLTLLPDVLQEGDLLLTQGAGNIGALARQLAQNRLGFESTNNDSNRG
Cell wall formation.
B1KKX6
A9MFB6
BTUC_SALAR
Vitamin B12 import system permease protein BtuC
Salmonella
MDNMLTFARQQQRRNVRWLLSLSLLVLLATLLSLCAGEQWIAPGDWLSSRGELFVWQIRLPRTLAVLLVGASLALSGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPGWSLGLCAIAGALTITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSFDLRQLMYWMMGGFGGVDWQQSWLMTALIPVLIWICCQSQPMNILALGETPARQLGLPLWLWRNLLVVATGWMVGVSVAMAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGAIALLLADVVARLALASAELPIGVVTATLGAPIFIWLLLKSAR
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
A9MFB6
Q9FUR2
IP5P2_ARATH
Type I inositol polyphosphate 5-phosphatase 2
Arabidopsis
MKTRRGKRPERFWPSIVMNKWLNRKPKVYDFSEDEIDTEPESEDDVCSVKDVPNVHCVTDEDSHNGRRGSEADHGNNISDGGVSVRGGYQRKHRRGKSETLRAQYINTKDIKVTVATWNVAGKRPSDDLEIEDWLSTDNPSDIYIIGFQEVVPLNAGNVFGAEDRGPIPKWESIIRRTLNKSNKESVYDQSPSCNNNALHRSHSAPSSPILAQEANSIISHVMVENLVADHSLDLATNEFIDAATALPSLEPQRNPNMDWPELALDSNPQIVGSEGKLRRVFSSNATLGFKLPENPSGASRFASEARQLKRSRSFETLNLSWNDIKEEIDNRSSSSSEAEEAAKIMHDDSSDGDSSSQDEEDGDKIRNSYGLPEDLVEECRKVKDSQKYVRIVSKQMVGIYVSVWIRRRLRRHVNNLKVSPVGVGLMGYMGNKGSVSISMTLYQSRMCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFASVLDTDQPRTIPCHDQVFWFGDLNYRLNMSDGEVRKLVSQKRWDELKNSDQLIRELRRGHVFDGWREGPIKFPPTYKYEFDSDRYAGENLREPEKKRAPAWCDRILWLGKGIRQECYKRSEIRMSDHRPVTSIFNVGVEVFDHRKLQRALHVNNAAASAVHPEPSF
Has phosphatase activity toward Ins(1,4,5)P3 and Ins(1,3,4,5)P4. Seems to be involved in the abscisic acid (ABA) signaling pathway . Could also be able to hydrolyze PtdIns(4,5)P2 and PtdIns(3,4,5)P3 .
Q9FUR2
Q8KA19
RNFD_BUCAP
Rnf electron transport complex subunit D
Buchnera
MKLKKMNLPYISNTYDVRKIMFLVVLSCIPGLCTEIYFFGCGVLIQTLLFVIISLLFEIIILKMRRKNIKNSLFDYSSFLTAVLLGLSTPCALPWWMIIFSCFFAIVISKYLYGGLGQNIFNPAMIGYVVLLISFPVHMTAWNEKNSSLSFYNDIKKSINLILFYNKLNNSKKKICPDNFTEATPLDDFKTKSHFDYDFFPEESAVKKKTKIVSIAWKYINISFLIGGCFLLYKKVICWRIPLSFLSSLIFFSSITYFYSQKFFCSPLFHLFSGGTMMCAFFIATDPVTTSCTKIGKIFFGLIIGFLVWIIRNYSDYPDGIAFSVLFANMIVPLMDAYLKTSGYGHKNL
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Q8KA19
Q835U7
RBFA_ENTFA
Ribosome-binding factor A
Enterococcus
MANYRDRRVGQEIMREVNDILNKRIRDPRVQGITITDVRVTGDLQQATIYYSLLSDLASEQQKAQQGLDKAKGLIRKELGQRLTLYKTPELIFERDESVQYGNHIDELIRKLNQGE
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q835U7
Q5L8A5
RS12_BACFN
30S ribosomal protein S12
Bacteroides
MPTIQQLVRKGREVLVEKSKSPALDSCPQRRGVCVRVYTTTPKKPNSAMRKVARVRLTNQKEVNSYIPGEGHNLQEHSIVLVRGGRVKDLPGVRYHIVRGTLDTAGVAGRTQRRSKYGAKRPKPGQAAPAKKK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q5L8A5
B4FHY0
FEN1_MAIZE
Flap structure-specific endonuclease 1
Zea
MGIKGLTKLLADNAPKAMKEQKFESYFGRKIAVDASMSIYQFLIVVGRTGMETLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPDMKKQELAKRYSKRDDATKDLTEAVEVGDKDAIEKLSKRTVKVTRQHNEDCKRLLRLMGVPVVEAPSEAEAECAALCINDKVFAVASEDMDSLTFGAPRFLRHLMDPSSKKIPVMEFDVAKVLEELELTMDQFIDLCILCGCDYCDSIKGIGGQTALKLIRQHGSIESILENLNKDRYQIPEDWPYQEARRLFKEPNVTLDIPELKWTAPDEEGLISFLVKDNGFNEDRVTKAIEKIKSAKNKSSQGRLESFFKPTATTSAPLKRKETSDKTSKAAANKKTKAGGKKK
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
B4FHY0
Q3T9M1
MFS2B_MOUSE
Major facilitator superfamily domain-containing protein 2B
Mus
MSVPHGPTPAPVAEPHTQEPGSDKRDGRLSVCTKVCYGIGGVPNQVASSASAFYLQLFLLDVAQIPAAQVSLALFGGKVSGAVADPVAGFFINKSRRTGSGRLMPWALGCMPLIALAYFFLWFLPPFTSLRGLWYTSFYCLFQALATFFQVPYTALTMILTPSPRERDSATAYRMTMEMAGTLMGATVHGLIVSSAHGSQRCEDTVHPRSPAVSPDVARLYCIAAAVVALTYPVCGSLLCLGVKEQPDTSAPASGQGLNFFTGLAITSQHPPYLSLVVSFLFISAAVQVEQSYLVLFCTHASKLQDHVQNLVLIILVSAVLSTPLWEWVLQRFGKKTSAFGICVMVPFSILLAAVPSAPVAYVVAFVSGVSIAVSLLLPWSMLPDVVDDFQLQHRCGPGVETIFYSSYVFFTKLSGAGALGISTLSLEFAGCEAGACQQAEEVVVTLKVLIGAVPTCMILIGLCILLVGPTPKMPRQDTSSQLSLRRRTSYSLA
Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets . Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology . Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation . Mediates the export of different sphingosine-1-phosphate (S1P) species, including S1P(d18:0) (sphinganine 1-phosphate), S1P (d18:1) (sphing-4-enine 1-phosphate) and S1P (d18:2) (sphinga-4E,14Z-dienine-1-phosphate) . Release of sphingosine-1-phosphate is facilitated by a proton gradient . In contrast, cations, such as sodium, are not required to drive sphingosine-1-phosphate transport . In addition to export, also able to mediate S1P import . Does not transport lysophosphatidylcholine (LPC) .
Q3T9M1
Q8EPJ4
MURI_OCEIH
Glutamate racemase
Oceanobacillus
MDKSIGVIDSGVGGLTVVHELMRQLPKEQLIYLGDTARCPYGPRSKEEVRQFTWEMVDFLLTKNIKMLVVACNTATAFTLKDLKEQLDIPVIGVIQPGARAAIKSTTNNQVGVIGTEGTISSGAYSQALEKIKSDIQVSGLACPPFVPMVERGVLSGPEAKAVVSEALRPFSNNKEMDTLILGCTHYPLLKSTIQEVMGEEVTVISSSEETARETSTLLDVHQIMNRSDLVPLHQFYTTGDLEIFIEIAKTIFQESHFQMLTIKQANISTNKVW
Provides the (R)-glutamate required for cell wall biosynthesis.
Q8EPJ4
B0BPT5
GAL1_ACTPJ
Galactose kinase
Actinobacillus
MKPQQLATQKFSEHYGYSAAQTVFAPGRVNIIGEHTDYNDGFVMPCAINYGMAVSFSKRDDSVWRVYAIDIDEQDEFDLSRPIEPSEHKWANYVRGVVKYIQEKCPEFKQGADLAMTSDVPMSSGLSSSAALEISIGKTAQVLGDLPLSLAEIALIGQQAENKFVGANCGNMDQLTSALGQKDQVIMIDCRSLEITPTPVPHGYSIAIINSNVKHDLVTGEYNSRRQECEFAAKFFGVKALRDVTPAQFIERAAELQAENELAYKRAKHIISENQRVLEAVEALQAKDMVKLGQLMAGSHDSMRDDFEITIPEIDYLVELAQVAIGKNGGARMTGGGFGGCIVCLVPDEKVEHLRRIIADNYEKQTGIKETFHLCTACDGVHLI
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
B0BPT5
Q5HAK8
FOLD_EHRRW
Methenyltetrahydrofolate cyclohydrolase
Ehrlichia
MEGNIVSGKAVADNITNILATCISDLKAQHNLTPCLIVVLVGDDPASQLYVRNKQRKAEMLGLRSETMLLPSTISESSLIEKIHQLNNDDSVHGILVQLPVPRHIDKNLIINTIDPKKDVDGFHNENVGRLFTGQKKNCLVPCTPQGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLPDYCRRADILVAAVGIPRFVKYSWVKHGAIVIDVGINSIEEDGVKKFVGDVDFAEVNKIASAITPVPGGVGPMTIAFLMVNTIIAACNQSGIDGFLEKYLDL
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Q5HAK8
F4IS56
ILK1_ARATH
Ankyrin protein kinase 1
Arabidopsis
MENITAQLKRGISRQFSTGSIRRTLSRQFTRQSSLDPRRTNMRFSFGRQSSLDPIRRSPDSSKSDDEPHMSVPENLDSTMQLLFMASKGDVRGIEELLDEGIDVNSIDLDGRTALHIAACEGHLGVVKALLSRRANIDARDRWGSTAAADAKYYGNLDVYNLLKARGAKVPKTRKTPMTVSNPREVPEYELNPLEVQVRKSDGISKGAYQVAKWNGTRVSVKILDKDSYSDPERINAFRHELTLLEKVRHPNVIQFVGAVTQNIPMMIVVEYNPKGDLSVYLQKKGRLSPSKALRFALDIARGMNYLHECKPDPIIHCDLKPKNILLDRGGQLKISGFGMIRLSKISQDKAKVANHKAHIDLSNYYIAPEVYKDEIFDLRVDAHSFGVILYEITEGVPVFHPRPPEEVARMMCLEGKRPVFKTKSRSYPPDIKELIEKCWHPEAGIRPTFSEIIIRLDKIVANCSKQGWWKDTFKFPWK
Functions as a link between plant defense pathways, stress responses and potassium homeostasis. Promotes osmotic stress sensitivity, responses to the bacterial-derived pathogen-associated molecular pattern (PAMP) flg22, and resistance to bacterial pathogens. Promotes the accumulation of POT5/HAK5, a potassium transporter that mediates high-affinity uptake during potassium deficiency.
F4IS56
A9MJ57
TRUA_SALAR
tRNA-uridine isomerase I
Salmonella
MSGQQSSPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPINVFCAGRTDAGVHGTGQVVHFETTALRKDVAWTLGVNANLPGDIAVRWVKAVADDFHARFSATARRYRYIIYNHRLRPAVLAKGVTHYYKPLDAERMHRAAQCLIGENDFTSFRAVQCQSRTPWRNVMHISVTRHGPYVVVDIKANAFVHHMVRNIVGSLLEVGAHNQPESWIAELLAAKDRTLAAATAKAEGLYLVAVDYPDRFDLPKPPMGPLFLAD
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
A9MJ57
Q4ZP20
CH60_PSEU2
Chaperonin-60
Pseudomonas syringae
MAAKEVKFGDSGRKKMLAGVNVLADAVKATLGPKGRNVIIEKSFGAPLITKDGVSVAKEIELKDRFENMGAQLVKDVASRANDDAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKATIAIVAELKKLSKPCTDTKAIAQVGTISANSDHSIGDIIAEAMEKVTKDGVITVEEGSGLENELSVVEGMQFDRGYLSPYFINKPDTMVAELDSPLLLLVDKKISNIREMLPVLEAVAKAGRPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTGGTVISEEIGLSLETTTLEHLGNAKRVILNKENTTIIDGAGVKTDIDSRISQIRQQIGDTSSDYDKEKLQERLAKLSGGVAVIKVGAGSEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRSLQAIEGLKGDNADQDVGIALLRRAVEAPLRQIVANSGDEPSVVVDKVKQGSGNYGYNAASGEYGDMIEMGILDPAKVTRSALQAASSIASLMITTEAMIADVPEDKPAGGGMPDMGGMGGMGGMM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Q4ZP20
Q8S2G5
GPDH2_ORYSJ
Probable glycerol-3-phosphate dehydrogenase [NAD(+)] 2, cytosolic
Oryza sativa
MGGAEDAPRAAAANGHGNGATVEEKLDELRRLLGKADGDPLRIVGVGAGAWGSVFCALMQDAYGHLRDKVQVRIWRRPGRAVDRATAEHLFEVINAREDVLRRLIRRCAYLKYVEGRLGDRTLYADEILRDGFCLNMIDTPLCPLKVVTNLQEAVWDADIVINGLPSTDTREVFGEIGRYWKERITAPIILSLAKGIEASLDPLPRIITPTQMISNATGVPLENILYLGGPNIASEIYNKEYANARICGADKWRKPLAKFLRQPHFIVWDNSDLITHEVMGGLKNVYAIGAGMVAALTNESATSKSVYFALCTSEMIYITHLLEEEPEKLAGPLLADTYVTLLKGRNAWYGQKLAKGELTLEMGDSIKGKGTIQGVSAVNAFYELLSQDSLSVMHPEANRSVAPVEMCPILKALYKILIKRELPPDSILQAIRDETMYDPRERIEMAQGHSLYRPSLLGQPKGDAKA
May be involved in cell redox homeostasis.
Q8S2G5
Q9BPU3
KIF2_DICDI
Kinesin-14
Dictyostelium
MEKRQLYSSQSQSQPLNIITNTINSRPSLLRKPASSSSQSNDRISYPPSTDSKFIQQQYHQPLLTNTDIKLEDIESSSSNNNPLKNSINNVSMQISQLNSSHHSRALLMQKRNNPTTNIRPTVKKKLDDTHKPLTSNFKKPITPISKLNTNMNNNNINNKNNNININSNNSSNSNNNILSPVQNNTISPNSNLLNSSIKFEKSNFFSTMYSSPTTITTTSTTLNNDNNNNISISSSCSNNSSFDLQQQHALHERMNKIDQFTQTVRGNLQSQFDNISEQLKPPRLSLSIQDIKTRLDFEEKNKEVEKIKLELKNVLQSLKEKEKELMEAHYKVSQVSVLKDNMERDLQQSNQMILDLQHEIRSSSLKAIQVDEKFNNMKDVTKDLDDEILRLNQLVRERDTEIESLRKENRELLEKSRSDEKVRRKLHNTIQELKGNIRVFCRIRPDFSSGQGANGSVFNIPAGTDNLVEVKSPTIDSFNGEASIKKSTFTFDRVFGPSSTQELVFEDISQLVQSSLDGYNTCIFTYGQTGSGKTHSILGDLKVPSQRGMIPRTVEKIFSSIQDLTEKGWTYQIECFFLEIYNETINDLLNTTTTTTGGNSKSNEIKYEIKHNPDTNVTTVTNMTVVPVTHPSQVYELLNLANKNRSVAKTLCNERSSRSHTVFQLKLIGYNQQSSERTQGLLNLIDLAGSERVSRSGVEGKQLKETQAINKSLSSLGDVISALANKEQHIPYRNSKLTFLLQNSIGGNSKTLMFVNISPELKDLQESTSSLRFAAKVNSCELGAARKQKII
Microtubule-dependent motor that is probably involved in microtubule organization in the mitotic spindle.
Q9BPU3
P22663
VATB_METBA
V-ATPase subunit B
Methanosarcina
MVKEYKTITQIAGPLVFVEKTEPVGYKEIVTINLPDGTTRRGEVLDSSSDIVVIQIFEGTTGLDKECGVVFTGETLKLPASIDLLGRILSGSGEPLDGGPRIVPDQLLDINGAAMNPYARLPPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPHNEIALQIARQAAVPGSESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGAARNEIPGRRGYPGYMYTDLATLYERAGIVKGAKGSVTQIPILSMPGDDITHPIPDLSGYITEGQIVVSRELHRKGIYPPINVLPSLSRLMNSGIGAGKTREDHKAVSDQMYAGYAEGRDLRGLVAIVGKEALSERDVKFLEFADLFEQQFVTQGRNENRTIADTLDIGWKILAHLPENQLGRIDNKYIQKYHPAHRKGQ
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
P22663
Q6LT88
MINE_PHOPR
Cell division topological specificity factor
Photobacterium
MALLEFFRPKKTTTASVAKERLQIIVAERRSAGQSTPSYLPQLKLDLLEVIRKYVNINPDQVSVNLDQKDEDLSVLELNVTLPEDK
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Q6LT88
Q7VXD7
RIMM_BORPE
Ribosome maturation factor RimM
Bordetella
MSEAAHSGAAPADLVELGRIASAYGVKGWVKVQPHSAQAEVLRTVSHWWLTRPAPQAARDVVASVPRAYQVLQARVHGGAVVAQLAGIDDRDQAEALRGCFVQAARSAFPAPADDEYYWVDLIGCALYSDADGEPRLLGVVDEVFDNGAHAVLKVLRQQIQPGQPGPVPLLDPKGRPLEELVPFVRAHIRHVDLAARRIDSDWPLDY
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Q7VXD7
O75586
MED6_HUMAN
Renal carcinoma antigen NY-REN-28
Homo
MAAVDIRDNLLGISWVDSSWIPILNSGSVLDYFSERSNPFYDRTCNNEVVKMQRLTLEHLNQMVGIEYILLHAQEPILFIIRKQQRQSPAQVIPLADYYIIAGVIYQAPDLGSVINSRVLTAVHGIQSAFDEAMSYCRYHPSKGYWWHFKDHEEQDKVRPKAKRKEEPSSIFQRQRVDALLLDLRQKFPPKFVQLKPGEKPVPVDQTKKEAEPIPETVKPEEKETTKNVQQTVSAKGPPEKRMRLQ
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
O75586
Q9ZKZ0
HLDE_HELPJ
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
Helicobacter
MKKILVIGDLIADYYLWGKSERLSPEAPVPVLEVKKESKNLGGAANVANNLTSLKAKVFLCGVVGDDLEGKHFISTLKTRGIDTSGVLIDKTRCTTLKTRIIAQNQQIVRVDKEIKDPLNADLRKNLLDFIAEKIQEIDGVILSDYNKGVLDFELTQTIITLANKHHKLILCDPKGKDYSKYSHASLITPNRAELEQALHLKLDSHANLSKALQILQETYHIAMPLVTLSEQGIAFLEKGELVNCPTIAKEVYDVTGAGDTVIASLTLSLLESKSLKEACEFANAAAAVVVGKMGSALASLEEIALILNQTHPKILPLEKLLETLERNQQKIVFTNGCFDILHKGHASYLQKAKALGDILVVGLNSDNSIKRLKGDKRPIVSEKDRAFLLASLSCVDYVVVFGEDTPIKLIQALKPDILVKGADYLNKEVIGSELAKETRLIEFEEGYSTSAIIEKIKRTHND
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Q9ZKZ0
A7ZG10
RL23_CAMC1
50S ribosomal protein L23
Campylobacter
MADITDIKTIIYTEKTLGLQEQGVVVIQTSPRVTKNSLKAVLQEYFGVTPVRVNSLRISGKVKRFRGRAGQRDEIKKFYVKLPEGVSLENTEA
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.
A7ZG10
Q9Y7U9
CCA2_SCHPO
tRNA adenylyltransferase cca2
Schizosaccharomyces
MYSRIVLNDVEKKVVNLLKKTADFIESKSSSSSSLEVRLAGGWVRDKLLGLSSDDLDVTLNKVTGVDFANSIFEYVHSLDSDSVIPYKDALGKLTVNPDQSKHLETATLSLFDLDIDFVGLRAESYDDKSRIPSVTPGTVETDALRRDFTVNTLFFNIRTEKIEDITKRGYKDLQTKVLVTPISPLQSFLEDPLRILRGIRFASRFEFTIDPSVVSAIQDPKVCKAFEKKVSKERVGEEIEKMLKGANAKLALQLLYSTNTYQFTFDTLPAEKEFQIPKALEATESLFQSLALTFPKLMKLSEDEKIGLWLYVALIPWSSQTVMVKKKQFYIPAIIAKDKLKLRSTYVNQLNQCCTFNPIFDELVNDTSTKNCSSIGSLIRQLNKSWEVVFLTSVIYSCCKTPAASVSNTFSSYKSLYDFIYDKNLQNAYNMKPLLDGKQIMKNVGVKPGPQLKETMDNMISWQFKHPEGSVEDCVAYLQSLKI
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. In contrast to what is usually observed in eukaryotes for which one enzyme synthesizes the whole tRNA CCA terminus, in S.pombe, cca1 specifically adds two cytidine residues to a tRNA substrate lacking this sequence while cca2 specifically adds the terminal adenosine residue thereby completing the CCA sequence.
Q9Y7U9
Q1HPS4
EIF3K_BOMMO
eIF-3 p25
Bombyx
MTDTMAETMKQTVASILKSIERYNPANLEILERYVEMQSRENTYDWGANLAVLKLYQFNPEKFNADITCQILLKALTNFPHTDFTLCKCLLLESVVENETISQIKYLADILEQCDFAQFGNRVHQMPELCSRISGFHDSIRKFVCHVVGITFQTIDKNNLANLLGGIDDVTLKHWVKKYGWRDDGSLIFIANQDENIKTKNITEKIEFDHLAPLMALL
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Q1HPS4
Q9L0Q8
ISPD_STRCO
MEP cytidylyltransferase
Streptomyces albidoflavus group
MSDESRPSPAETPATTFAETSAETSAAGRSPARTAAVIPAAGRGVRLGPGAPKALRALGGTPMLIHAVRAMAASRAVSLVVVVAPPDGAGEVKSLLDAHALPERTDFVVVPGGETRQESVRLGLDALPPEYGIVLVHDAARPLVPVDTVDAVIDAVREGAPAVVPAVPLADTVKQVEPAAAPGEPEPVVATPERARLRAVQTPQGFDRATLVRAHGTVTDDVTDDASMVEQLGLAVVVVPGHEEAFKVTRPLDLVLAEAVLARRRLNDGF
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q9L0Q8
P14490
REPM_STAAU
Replication initiation protein
Staphylococcus
MSKNNYTNHSNHLENHDSDNFSKTGYSNSRLDAHFVCTSNPKLSFDAMTIVGNLNKNSAKKLSDFMSLDPQIRLWDILQTKFKAKALQEKVYIEYDKVKADTWDRRNMRVEFNPNKLTHDEMLWLKHNIIDYMEDDGFTRLDLAFDFEDDLSDYYALSEKALKRTVFFGTTGKAETKYFGSRDSNRFIRIYNKKKERKENADVDVSAEHLWRVEIELKRDMVDYWNNCFNDLHILKPAWATLESLKEQAMVYLLLHEESKWGELHRNSRRKYKQIIQEISSIDLTDLMKSTLTDNEENLQKQINFWQRKFEFWK
This protein is probably a specific topoisomerase involved in initiating replication. This protein is specifically required and may be rate-limiting for replication of the plasmid in vivo.
P14490
Q8XIT6
PRMA_CLOPE
Ribosomal protein L11 methyltransferase
Clostridium
MEGTWIEVRVITKSEALEPISGIFYGLDCKGVAIEDPNDILGREQGPLTWDFADINILEHKGKVAVVKGYFSEEDNIDDVIAYVKERVEELKESGLDVGEGTVEAEKMFEEDWANNWKKYYKPIKIGEKIVIKPIWEEYEPTGEEMVVELDPGMAFGTGDHETTRMCVQALDKYVKADTTVFDIGTGSGILALVASKLGAKHVVGVDLDPVAVDSAKENISFNNVDNIEVLYGNLLDVVDGKADIVVANIIAEIICILVDDVKKALNKDGIFITSGIIHERRQMVIDKLEQEGFEVMEVNKDGEWNCIVAKLK
Methylates ribosomal protein L11.
Q8XIT6
Q9Y3E1
HDGR3_HUMAN
Hepatoma-derived growth factor 2
Homo
MARPRPREYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEGLWEIENNPGVKFTGYQAIQQQSSSETEGEGGNTADASSEEEGDRVEEDGKGKRKNEKAGSKRKKSYTSKKSSKQSRKSPGDEDDKDCKEEENKSSSEGGDAGNDTRNTTSDLQKTSEGT
Enhances DNA synthesis and may play a role in cell proliferation.
Q9Y3E1
Q28MN0
GLGA_JANSC
Starch [bacterial glycogen] synthase
unclassified Jannaschia
MTRVLSVASECAPLVKTGGLADVVGALPGAMAALGDELRTLVPGYATMPVVGGAVVAAFDDLFGGPATVDALTHEGLDLLILRAPHLFDRPGGLYIDAFGADWPDNAERFAALSYAAAHVAAKGAGDWRADVVHGHDWQAGLVPEYLAGLGCDTPFILTIHNVAFHGNTGAEKLDALRLDPDRFNADQYEFWGQISALKAGLMGAAQITTVSQTYAEELMTPQFGMGMDGVLRHRRDALTGIVNGIDLDVWNPETDPQITPYTTFKGKAANKAALQAEFGLSKAPGPLCVLVSRLTDQKGIDLLLDAMHVVLERGGQVAVLGSGAPDLEVCLLERADAEPNLAVKIGYDEALSHRMMAGGDCILVPSRFEPCGLTQLYGLRYGTLPLVALTGGLADTVINASPAALARRVATGIQFSPITAEALANAFSRLCDLYADRKTWTAMVRNAMKQPVGWDMSASRYHALYKATARK
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Q28MN0
Q0VN37
LIPB_ALCBS
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Alcanivorax
MHSWPYTSPMDALIRYFPQVDYSSCWHAMRDLTDHRDAQQSDEFWVLEHPPIFTLGQAGKPEHVLNAGEIPVVNSDRGGQVTYHGPGQTVVYLMLDIKRLGLGSRGLVSAIEQGIIDFLASLGITAVNRDDAPGVYVQGAKIASLGLRIRRGATYHGLAINRDMDLSPWHRINPCGHVDQPMTTLKAQGVDLDRHSMEQQLVSFLAKRLGLTPRTAALPDWYNTRQENVTTGGDPGSALTQQPERL
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Q0VN37
Q72I19
RL6_THET2
50S ribosomal protein L6
Thermus
MSRIGRLPIPVPKGVSVEVAPGRVKVKGPKGELEVPVSPEMRVVVEEGVVRVERPSDERRHKSLHGLTRTLIANAVKGVSEGYSKELLIKGIGYRARLVGRALELTVGFSHPVVVEPPEGITFEVPEPTRVRVSGIDKQKVGQVAANIRAIRKPSAYHEKGIYYAGEPVRLKPGKAGAKK
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.
Q72I19
Q9HAI6
TASL_HUMAN
TLR adapter interacting with SLC15A4 on the lysosome
Homo
MLSEGYLSGLEYWNDIHWSCASYNEQVAGEKEEETNSVATLSYSSVDETQVRSLYVSCKSSGKFISSVHSRESQHSRSQRVTVLQTNPNPVFESPNLAAVEICRDASRETYLVPSSCKSICKNYNDLQIAGGQVMAINSVTTDFPSESSFEYGPLLKSSEIPLPMEDSISTQPSDFPQKPIQRYSSYWRITSIKEKSSLQMQNPISNAVLNEYLEQKVVELYKQYIMDTVFHDSSPTQILASELIMTSVDQISLQVSREKNLETSKARDIVFSRLLQLMSTEITEISTPSLHISQYSNVNP
Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 . Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons . Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes .
Q9HAI6
Q1GF45
COBQ_RUEST
Cobyric acid synthase
unclassified Ruegeria
MIQGTGSNVGKSMLVAGLARALRKRGLSVAPFKPQNMSNNAAVTSDGGEIGRAQALQARAAGLAPHTDMNPVLLKPETDTGAQVIVQGKRRGTRAAGSFMRDKAGLLEATLESFHRLAAQHDIVLIEGAGSPAETNLRKGDIANMGFAEAAGVPVLLVGDIHRGGVIAQIVGTHTVLEPSDRARIKAFAVNRFRGDLSLFDGGRDDIARWTGWPSLGVVPWFWDAWKLPAEDMMDIASHKGGACKVVVPQLERMANFDDLDPLAAEPAVTVEIVPPGRALPGDADLVLIPGSKSTIGDLAYLRTQGWDIDILAHHRRGGHVLGLCGGYQMLGQSIDDPEGVDGHPGKVAGLGLLDVHTVMAGDKRVTLSAARTLEGDLPVSGYEIHMGRTTGPDCARAWLALEGRAEGATSADGRVRGSYLHGLFTSDAFRAQFLSDLGHQSDLDYDAGVEATLDELAAHLEQYMDVEGLLELAEPIPVPES
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Q1GF45
A5D7U4
SCNNB_BOVIN
SCNEB
Bos
MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFVLTLLFTSLVCWQWGLFIKTYLNWEVSVSLSIGFKTMDFPAVTICNASPFQYSKVQHLLKDLDELMEAVLGRILGPELSQVNDTRALNLSIWHHTPLVFINEQNPHHPVVLDLFEDNFNGSASNSPAPGRPCSAHRCKVAMRLCSHNGTTCTFRNFSSATQAVTEWYTLQATNIFAQVPNQELVAMGYPAERLILACLFGAEPCNYRNFTPIFHPDYGNCYIFNWGMTEKALPSANPGTEFGLKLILDMGQEDYVPFLTSTAGARLMLHEQRSYPFIKEEGIYAMAGMETSIGVLVDKLQRKGEPYSQCTKNGSDVPIQNLYSNYNTTYSIQACIRSCFQEHMIRECGCGHYLYPLPHKRKYCNNQEFPDWAHCYSALRISLAQRETCIYACKESCNDTQYKMTISMAVWPSEASEDWIFHVLSQERDQSSNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEFGEIIIDFVWITIIKLVALAKSVRQKRAQARYEGPPPTVAELVEAHTNFGFQPDLATPGPDVEAYPHEQNPPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.
A5D7U4
Q2SU28
RL4_BURTA
50S ribosomal protein L4
pseudomallei group
MELKLLNSNGQEGAVVNASDVVFGRDYNEALIHQVVVAYQANARQGNRAQKDREQVKHTTKKPWRQKGTGRARAGMSSSPLWRGGGRIFPNSPDENFSHKVNKKMHRAGLCSIFSQLAREGRLSVVEDIVLEAPKTKLLADKFKAMGLDSVLVITDTVDENLYLASRNLPHVAVVEPRYADPLSLIYFKKVLVTKAAVAQIEELLS
Forms part of the polypeptide exit tunnel.
Q2SU28
Q6KZP8
RS13_PICTO
30S ribosomal protein S13
Picrophilus
MAEENKNNENFQYIVRIANKDLNGERPLKLALADLKGIGLRLSETIAKKLDLDPDQRIGELGEDKIEELRKYIEGKVYDGIPYWMYNHRRDITTGKDFNLVSNDLDLQINDDINLMKKMRSYKGIRHERGLKVRGQRMRSNGRKGLAIGVVRKKEEKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement.
Q6KZP8
Q13Z72
SURE_PARXL
Nucleoside 5'-monophosphate phosphohydrolase
Paraburkholderia
MRILLSNDDGYLAPGLAALYEALKPIADVTVMAPEQNCSGASNSLTLSRPLSVLRSANGFYYVNGTPTDSVHIALTGMLDHRPDLVVSGINNGQNMGEDTLYSGTVAAATEGIMFGVPAIAFSLVDKDWVHLEDAVRVSAEIVAHYLEQPLPGHPLLNVNIPNLPYDQLGDWQITRLGKRHPSQPVIRQTNPRGEPIYWIGPAGSARDASEGTDFHAVANGHVSITPLQLDLTHTQMLPAARDWARAGSGAS
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q13Z72
A2S5J7
DAPB_BURM9
4-hydroxy-tetrahydrodipicolinate reductase
pseudomallei group
MSSMKIAIAGASGRMGRMLIEAVLAAPDATLAGALDRTGSSQLGQDAGAFLGKQTGVALTDDIERVCAEADYLIDFTRPEGTLAHLDAALRHDVKLVIGTTGFSEPQKAQLRAAGGKIALVFSANMSVGVNVTMKLLEFAAKQFAQGYDIEIIEAHHRHKVDAPSGTALMMGETIAAATGRTLDDCAVYGRHGVTGERDPSTIGFSAIRGGDIVGDHTVLFAGIGERIEITHKSASRVSYAQGALRAARFLAGHQAGFFDMQDVLGLR
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
A2S5J7
A2BK98
NDK_HYPBU
Nucleoside-2-P kinase
Hyperthermus
MPVERTFVMIKPDGVKRGLVGEIIARFERKGLKIKALKMKWLTREEAEKLYEVHRGKPFFEDLVNFVTSGPVVAMILEGDSAIEVVRLMIGPTDGRKAPPGTIRGDYALDIGANVIHASDSKESYEREYKVFFSDDEIVGDY
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
A2BK98
Q3B0J2
SSRP_SYNS9
Small protein B
unclassified Synechococcus
MAKGGVKKAAAAAARAAANRLMADNRQARHQYEILETLETGIELVGTEVKSIRNGKANLRDGFCLIRNGELQLHNVHISPHSHASAYFNHDPLRTRKLLAHRREIDKLRGQLDKKGLALIPLNIHLKGSWIKITIGVGKGRKLHDKRAADKEKQSKKEVRSAMAKYQ
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q3B0J2
A3QEN9
RNFE_SHELP
Rnf electron transport complex subunit E
Shewanella
MSNYRDIAWQGLWKNNPGLVQLLGLCPLLAVTATLTNAIGLGLATLVVLVGSNVLVSLVREFVPKEIRIPVFVMIIAALVTCVQLLINAYAYGLYLSLGIFLPLIVTNCVIIGRAEAFASRNSVVKAAFDGLMMGLGFTLVLMLLGACREILGQGTLFDGADLLLGDWAKGLTIHLWQVDTNFLLAMLPPGAFIAMGFLIAIKNMIDKQLEARKPALEAAPAVTRARITKVS
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
A3QEN9
P08253
MMP2_HUMAN
PEX
Homo
MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
P08253
A8AC29
VATA_IGNH4
V-ATPase subunit A
Ignicoccus
MAVKGKVLRVRGPVVIAEDMQGVQMYEVVEVGKDGLVGEVTRITGDKAVIQVYEDTTGITPGEPVVGTGSPFSVELGPGLLSHIFDGILRPLESIHEVAKSPFIKRGIKVPSLDRSKKWEWRPNPELKPGDKVSGDDILGTVPETPLIEHKVMVPPNVVPVDKAATLKWLAPAGEYTIEDTIAVVEYEGKEIELKMYHRWPIRRPRPVKEKFEPVTPLITGVRVLDTLFPMAKGGTGAIPGPFGSGKTVTLRTLAAWSDAKVVIYVGCGERGNEMTDVLVNFPHYKDPWSGRPLMERTILVANTSNMPVAAREASIYVGVTLAEYYRDMGYDSLLIADSTSRWAEALRDIAGRMEEMPAEEGFPPYLASRLAEYYERAGRARIPGRPERVGSVTIASAVSPPGGDFSEPVTSHTRRFVRVFWALDASLAYARHYPAINWLVSYSLYVDTVAKWWHENISPKWKEYRDEMMSILLKEDELKEIVRLVGPESLSEPDKLIIETARIIKEAFLQQNAFDPIDAFCSPKKQFLMMKIIIDFYRKAKELVNAGVPVATIREAVKEEVAELIRSRFTVRNEELEKLEDLYARFMEKLSSLSP
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
A8AC29
A5D4K5
THIC_PELTS
Thiamine biosynthesis protein ThiC
Pelotomaculum
MNYATQMEAARKGIITREMETVARKEMVDPAKLRELIAEGRVVIPANKNHASLDPCGIGQGLRTKINVNLGVSRDCCNIGMELEKARLAIELKADAIMDLSCYGRTEEFRRRLIEMSPAAVGTVPVYDAVGFYGKELKEISAEEFLGVVEKHAQDGVDFMTIHAGINRETAARFKKNPRLTNIVSRGGSLLFAWMELNGRENPFYEYFDELLEICRKYDVTISLGDACRPGSVKDATDASQIQELIVLGELTKRAWEKDVQVMIEGPGHMPLNEIIPNMLLEKKLCHGAPFYVLGPLVTDVAPGYDHITSAIGGAIAAASGADFLCYVTPAEHLRLPTLEDMKEGIIASRIAAHAADIAKGVPGARQWDDKMSEARRNLDWQKMFELALDPEKARRYRAESQPESEDTCTMCGKMCAVRNMNRVLSGAGPDG
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
A5D4K5
Q7NMC7
HEMH_GLOVI
Protoheme ferro-lyase
Gloeobacter
MAEVGVLLLNLGGPDKQEDVRPFLYNLFADPEIIRIPVPPLQKPLAWLISTLRAPKSRKNYQAIGGGSPLRAITNQQGRVLKKALAARGLDIEVYVGMRYWHPFTEEAVRKIKADGIRRLVLLPLYPQYSISTSGSSFKLLDQIWARDPSLKAIERITINSWYSRPGYIRAMGERVREGLDKFDNPDGVHILFSAHGVPRTYVDQDGDPYQRQTEETVDLVMQSLGRPNAHSLAYQSRVGPVEWLKPYTEDTINELAQKGVRSLLAVPVSFISEHIETLQEIEIEYREVAEAAGIHDFRRAKALNVNKTFIDDLAEMVIENLGVYSR
Catalyzes the ferrous insertion into protoporphyrin IX.
Q7NMC7
A7ZQD8
NORR_ECO24
Anaerobic nitric oxide reductase transcription regulator NorR
Escherichia
MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSDEELRLIAALAAGALSNALLIEQLESQNMMPGDATPFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVDVRVLAATNRDLREEVLAGRFRADLFHRLSVFPLSVPPLRERGDDVILLAGYFCEQCRLRLGLSRVVLSAGARNLLQHYSFPGNVRELEHAIHRAVVLSRATRSGDEVILEAQHFAFPEVTLPPPEAAAVPVVKQNLREATEAFQRETIRQALAQNHHNWAACARMLETDVANLHRLAKRLGLKD
Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54.
A7ZQD8
B2SQB3
ATPD_XANOP
F-type ATPase subunit delta
Xanthomonas
MSQALTLARPYGRAAFAIAREGGTFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLCFLGVLADAQRLSLLPEVAGLYEHLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
B2SQB3
Q0MQF8
NDUC2_GORGO
NADH-ubiquinone oxidoreductase subunit B14.5b
Gorilla
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEDKKTYGEIFEKFHPIR
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q0MQF8
A8ZRZ3
RNPA_DESOH
Protein C5
Desulfosudis
MTAFSFKKEDRLLKRYEFIEIFTSGKTVHSSCFLAGIKKNRKERIRLGITVSKKVGKAARRNRIKRHVREFFRLHRDNLSNCWDINVIAKKKAVNASPAELERSLAELFHKSSREFPSDRQ
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
A8ZRZ3
Q9PBJ8
RNT_XYLFA
Exoribonuclease T
Xylella
MMNQSITPPTHPPMSQRFRGYLPVVVDVETGGFNWNHHALLEIACIPIEMDDTGRLYPGEVTSTHVIPAPGTDIDPKSLEVTGIILDHPFRFAKEEKLALEHIFTPVRATMKKYKCQRAILVGHNAHFDLNFLNAAVTRTAYKRNPFHQFSVFDTVTLAGMAYGQTVLARAVQAAGLDWNAADAHSAVYDAEKTAHLFCTITNTWPLVVAG
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Q9PBJ8
C0HLS7
IBBA6_HYAOR
Bowman-Birk type proteinase inhibitor A6
Hyacinthus
WPPVEDRPCCERCTACTLMLPDEANTCVCGDIVPKCHQGCSLCERVDTPSGYQCKSFEYYNCGTKCP
Serine protease inhibitor . Strongly inhibits trypsin (Ki = 4 nM) and elastase (Ki = 4.8 nM) . Also inhibits chymotrypsin with a Ki of 22 nM . Does not inhibit bacterial subtilisin .
C0HLS7
A4FIS6
BIOB_SACEN
Biotin synthase
Saccharopolyspora
MNAPFHQLADAILAGTPATPEDALAVLRADDAELMSVVAAAGRLRRAHFGNTVKVNYLVNLKSGLCPENCNYCSQALGSDAPILKYSWLSKDETLKQTGAGLRGGASRVCLVSSGRGPSTRDIDKVTEMVVALKEEYPGVEVCACLGLLKDGQAQRLKDAGVDAYNHNINTAESNHDNIVQTHTYADRVDTVEKAKGGGLSPCSGLIAGLGETDEQLVEALFALRELGSDSIPVNFLMPFDGTPFENTWELSPTRCVKILAMARFVCPDKEIRIAGGREMHLRSLQSIALQVANSVFLGDYLTSEGQDAKADLEMIRDNGFVVLGSEEDLAQQAREPIDPAIRQRGAGTDVVPNA
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
A4FIS6
C4L7T3
RL2_TOLAT
50S ribosomal protein L2
Tolumonas
MAIVKCKPTSPGRRHVVKVVTPELHKGKPFAGLLEEKRKTGGRNNNGRITTRHIGGGHKQHYRLIDFKRNKDGIPAKIERLEYDPNRSANIALVLYADGERRYILAPKNLKAGDPIVSGVDAPIKAGNALPMRNIPVGTTVHAVEMKPGKGAQIARSAGASVQILAREGAYVTLRLRSGEVRKVLAECRATVGEVGNAEHMLRQLGKAGANRWRGIRPTVRGMAMNPVDHPHGGGEGRNKGIQPVSPWGTPAKGYRTRSNKRTDKYIVRRRNK
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.
C4L7T3
Q06815
MRL1_YEAST
Mannose 6-phosphate receptor-like protein 1
Saccharomyces
MLKRSSLIYLSCVLIITIPILLHVYNGPGLSHEANEHRASHKQKRTLANPDKPKSENDEDLFCAVTNPVTGSYIDLSQLSSTPNKLREGQKQISGNNKHESSKTKWSVRGWGYDTNFTLGICSSPVGEAESQQLSNLTGAFYVDQLNENNLVSIGDFSTRPALVGGSTAKKLTLKYENGSMCPNGKDKKATLLNFVCDKEIQSKAQISYIGNLHNCSYFFEVRSIHACPTSNKKNEVNVLGIFIGIFAIFFLVEFAGRRWIYAKLNRHLKNDDELHDISPSLNEQPHWDLIEDGSRWSKFFNGIIKTTRRFTKSLMRSLVRGRNSRQGGIRLRSSPSASSSSLANREFFRDMEAQNEIIDSLDINSHTTESDHPTLADNSV
Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole. Involved in the delivery and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar proteinase B).
Q06815
Q2J829
EFP_FRACC
Elongation factor P
Frankia
MATTNDLKNGMTLDIDGVLWNVVGFQHVKPGKGGAFVRTTLKNVLTGKVVDRTFNAGVKVDVATVDRREMTYLYRDGADFVFMDSESYDQIPIPPDVVGGTADYMLENTVATVALHDGAPLYVELPASVELTISQTDPGVQGDRSTGGTKPATLETGATINVPLFITSGEKVKVDTRDGRYLGRVTS
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.
Q2J829
B9MPC6
RISB_CALBD
6,7-dimethyl-8-ribityllumazine synthase
Caldicellulosiruptor
MRTFEGSFCGKDLKFAIVISRFNSFITDELLKGCLDGLKRHEVDSENIDVYYVPGAFEIPLVCKKLAKSKKYNAIIALGAVIRGSTPHFEYVSAEVSKGIANVSLEQEVPVIFGVLTCDTVDQAIERAGTKAGNKGFDAAMSALEMANLMKNISS
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
B9MPC6
A8F8Z5
KTHY_BACP2
dTMP kinase
Bacillus
MSGMFITFEGPEGAGKTTVIRKVHEEMERQGYAVMATREPGGIDIAEQIREVILNEKNTKMDAKTEALLYAAARRQHLAEKVEPALQRGETVLCDRFVDSSLAYQGYARGLGIDQVRSINDFAIDGTMPQMTIYFSITPEEGLKRIHANQGREKNRLDMETLNFHQLVREGYELLIAQSPERFHVVDASKPMQDVYEEVLRVIQDTLKKNQI
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
A8F8Z5
Q923Q2
STA13_MOUSE
START domain-containing protein 13
Mus
MFSQVPRTPAAGCYYLNPLTPESQEMYLRFDQTARRSPYRMSRILARHHLVTKIQQEIEAKEACDWLRAAGFPQYAQLYEDSQFPINIAAVKKDHDFLERDLVEPLCRRLNTLNKCASMRLDVNFQRKKGDDSDEEDLCISNKWTFQRTSRRWSRVDDLHTLFPVADRNGSPGGPRMRNTASSESVLTDLSEPEVCSIHSESSGGSDSRSQSGHHSADSTHALEATLVSSSLPQSTREGLNQSFHPKNEKPTRTRAKSFLKRMDTLRVKGALGRHKGPGRTGGLVISRPVLQQEPESFKTMQCVQIPNGDLQTSPPAACRKGLPCSSKSSGESSPLENSSTVSTPCMKERKCHHEANKRGGMYLEDLDVLAGTALPDTSDQNHMHGFHSQENLVVHIPKDHKPGTFPKALSIESLSPTDNSNGVNWRTGSISLGRQQGPGMREPRLMSSCHRASRVSIYDNVPSSHLYASTGDLLDLEKDGLLPQLDDILQHVNGIQEVVDDWSKNILPELQSHSTLAGDPGLSPFPSPNQVTLDFEGNSVSEGRTTPSDVERDRTSLNESEATGVRERRDSGVGASLTRPNRRLRWSSFQLSHQPQPSPATPHISSQTAAQLNLLQRFSLLRLTAIMEKYSMSNKHGWTWSVPKFMKRIKAPDYRDKAVFGVPLIVHVQRTGQPLPQSIQQALRYLRSNCLDQVGLFRKSGVKSRIHALRQMNENFPDNVSYEDQSAYDVADMVKQFFRDLPEPLFTNKLSETFLHIYQYVPKEQRLQAVQAAILLLADENREALQTLLCFLHDVVNLVDENQMTPMNLAVCLAPSLFHLNLLKKESSPKVIQKKYATGKPDQKDLNENLAAAQGLAHMITECNRLFEVPHEMVAQSRDSYLEAEIHVPSLEDLGAQLAESGATFHTYLEHLVQGLQKEAKEKFKGWVTCSSPDNTDLAFKKVGDGHPLKLWKASVEVEAPPSVVLNRVLRERHLWDEDFVQWKVVERLDKQTEIYQYVLNSMVPHPSRDFLVLRTWKTDLPKGMCTLVSLSVEYEEAQLMGGVRAVVMDSQYLIEPCGSGKSRLTHICRIDLKGHSPEWYSKGFGHLCAAEVTRIRNSFQPLVAEGPETKI
May function as a GTPase-activating protein.
Q923Q2
Q8FZ45
FUR_BRUSU
Ferric uptake regulation protein
Brucella
MNKPYTKPDYEQELRRAGVRITRPRRIILNILNETEDHPDALEIFRRAVEEDDSISLSTVYRTIKLLEERGAIHRHAFAGGPSRFEQASGAHHDHIIDMDSGDVVEFHSDKIEKLQEEIARSLGFEIVHHRLELYCKKLKS
Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
Q8FZ45
B0UWY1
PXPA_HISS2
5-oxoprolinase (ATP-hydrolyzing) subunit A
Histophilus
MKQIDLNVDLAEGCANDQQLLQLVSSANVCCGLHAGDYNEIREAILWAKENDVRIGAHPSFPDRENFGRTNMQLPDDELKACLFYQLGAVKALCDASGVTMEYVKPHGALYNMAAKDPHLAALIAETVKSVDPSLKLMGLSGSIMLTVAEQHGLATISEVFADRHYLADGSLVPRTRDDAMVENDEEAISQVLQMVLEGTVPTVDGGNVAIKADSICLHGDGEHAVVFATRIRRELKEKGILVTSSI
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
B0UWY1
B4SBU4
EFG_PELPB
Elongation factor G
Pelodictyon
MARLVDLDKVRNIGIMAHIDAGKTTTTERILYYTGRLHRMGEVHDGGATMDWMDQEKERGITITSAATTCFWMPKFGNYIGVNHRINIIDTPGHVDFTVEVERSLRVLDGAVALFCAVGGVEPQSETVWRQANKYGVPRIAYINKMDRTGANFFETVKAIRERLGANPVPLQIPIGEGEIFAGFVDLIRMKGIIYNKEDGSTYDEVEIPHDLQNEARTWRINMLEAVSEHDDTLLEKYLNGEDITESEVRNVLRQATLKVTIIPVLCGSSFKNKGVQFMLDAVVEYLASPVDVGAVEGHHPRTEEPVTREPKDEEPFAALAFKIATDPFVGKLTFFRVYSGVLKAGSYVLNTMTGKKERIGRVLQMHSNKREDIDCVYCGDIAAAVGLKDVRTGDTLCDENSPVVLEKMVFPEPVIEIAIEPKTKSDSDRLGMSLAKLAEEDPTFKVKTDDETGQTLIAGMGELHLEILVDRLKREFKVEANVGKPQVAYRETIRKSVEFEGKFVRQSGGKGQFGLVVLRVEPLEEGKGYEFVDAVKGGVIPREYIPAVNAGVQQAMKSGVVAGFPMQDIKVTLLDGKYHEVDSSEMAFKIAGSIGFKGGAKKADPVLLEPIMKVEVVTPDEYLGDVMGDLSSRRGHIEGMGQRAGAQFVNAKVPLSAMFGYSTDLRSMSQGRANYSMEFDCYREVPRSIAEALQEKRTSKDSD
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
B4SBU4
Q71RH2
TLC3B_HUMAN
TLC domain-containing protein 3B
Homo
MLTPMVAGGVVFPGLFLLSKNTLQRLPQLRWEEADAVIVSARLVSSVQAIMASTAGYIVSTSCKHIIDDQHWLSSAYTQFAVPYFIYDIYAMFLCHWHKHQVKGHGGDDGAARAPGSTWAIARGYLHKEFLMVLHHAAMVLVCFPLSVVWRQGKGDFFLGCMLMAEVSTPFVCLGKILIQYKQQHTLLHKVNGALMLLSFLCCRVLLFPYLYWAYGRHAGLPLLAVPLAIPAHVNLGAALLLAPQLYWFFLICRGACRLFWPRSRPPPACQAQD
Involved in ceramide synthesis.
Q71RH2
Q5KWI6
IXTPA_GEOKA
Nucleoside-triphosphate pyrophosphatase
Geobacillus thermoleovorans group
MKEIVIATKNAGKVREFAALFAKRGVEVKSLLDFPDAPDVAETGSTFAENAVLKAEAASRRLKRPVIADDSGLVVDALGGRPGVHSARYAGEDKNDARNIAKLLRELDGVPMEQRTARFHCALAVAIPGRPTAVVEATCDGYIAEAPRGEGGFGYDPVFYLPERGKTMAELAPEEKNQISHRAKALTKLDEQWEEIVGGKGRTE
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Q5KWI6
P0DJ24
RL37_TETTS
60S ribosomal protein L37
Tetrahymena
MTRGTPAFGKRHQKTHTLCRRCGKATYHKQKLRCAACGYPDAKMRRYDGWGQKVRDRKGQGTGRMRYMKTIARRAKNGFRSGTQAAPKVKAATN
Binds to the 23S rRNA.
P0DJ24
Q7MHN8
RNC_VIBVY
Ribonuclease III
Vibrio
MNSPIEKLTRQLGYQFQDDELLNLALTHRSANSKHNERLEFLGDSILSFVIADELYHRFPKVNEGDMSRMRATLVRGNTLAELGREFGLGDYLKLGPGELKSGGFRRDSILADAVEAIIGAVYLDSDLEVVRGIVLNWYASRLEAIKPGVSQKDPKTRLQEFLQGRRKPLPVYTVTNIKGEAHNQEFTVECDIAGMDKPVVGRGTSRRKAEQAAAELALEQLTNG
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Q7MHN8
A9VPT9
HUTP_BACMK
Hut operon positive regulatory protein
Bacillus cereus group
MLLQGTHRIGRMAMLLALADENESPVLSIPKGWKYCTGKVGSMNSQKVVAAMETAAKSNRVIETDVYRETHALYHAIMEALYGVTRGQIQLADVLRTVGLRFAIVRGTPYDGKKEGEWVAVALYGTIGAPVKGSEHEAIGLGINHI
Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.
A9VPT9
Q0TCA9
KEFG_ECOL5
Putative quinone oxidoreductase KefG
Escherichia
MSQPAKVLLLYAHPESQDSVANWVLLKPATQLSNVTVHDLYAHYPDFFIDIPREQALLREHEVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGNQLAGKYWRSVITTGEPESAYRYDALNRYPMSDVLRPFELAAGMCRMHWLSPIIIYWARRQSAQELASHARAYGDWLANPLSPGGC
Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB.
Q0TCA9
Q7W0A6
MUTL_BORPE
DNA mismatch repair protein MutL
Bordetella
MSDRRPIATLPDLLISQIAAGEVIERPASVLKEILENAIDAGARAIEVRLEGGGIRRIAVTDDGSGIPPEELPLALTRHATSKIRSLDELESVASMGFRGEALASIASVADLTIISRTRGAEHAWQIDGGSLQVSPASGPPGTTIDVRQLFDRVPARRKFLRSEATEFGHCVDAMERIALAHPEVAFRLFHHDRAQRQWLPADHGQRIRDVLGAEFVGHVLPVLAAAGAIALMGMVTRPTAARARADRQYLYVNGRFVRDRTVSHALRSAYADVLHGDRQPAYVLYLDIDPGAVDVNVHPAKHEVRFRDSGAVHRFVSQVVGQTLAQTGGAEAVPAGVPDGAAPDTAYAGEPAAAAPGLAEPRAPYPAAYPSPGQSPYQGSPARPHTQVPFRLHGEPAGIPATDWQSLYRPLPGDAAPAATALRAAPATPLPTADEHPLGQALAQLHGIYILAQNSRGLVLVDMHAAHERVVYEQLKRALDDRALPRQDLLVPVVFHAAEKDVALVEEHETQLNELGFEMRPSGPASIAVRSVPALLARGDIESLARAVLRDLGAVGVSRLLTEQRNELLSTMACHGSVRANRRLTLEEMNALLRQMEITERADQCNHGRPTWVQWSVNDLDKLFLRGQ
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Q7W0A6
Q8XVD1
HEM1_RALSO
Glutamyl-tRNA reductase
Ralstonia
MQLLTLGINHHTAPLSLREKVAFPLEQLKPALGTLRQHLPHRKSTAEAAILSTCNRTELYCATDGNLPEDTAHEHAIRWLAHHHNIDAGELAPHVYALGQSQAVRHAFRVASGLDSMVLGETQILGQMKDAVRTATEAGALGTYLNQLFQRTFAVAKEVRGTTEIGAHSVSMAAAAVRLAQRIFESIAEQRVLFIGAGEMIELCATHFAAQKPRETVVANRTLERGEKLAEALSNQGLNARAVRLAELPARLGEFDIVVSCTASTLPIIGLGAVERAIKQRRHRPMFMVDLAVPRDIEPEVARLSDVFLYTVDDLGAIVREGNALRQAAVAQAEAIIETRVQNFMHWLDARSVVPIIRDLHAHAEALRQGELERAQRMLARGDDPALVLEALSQALTKKFLHGPTHALNHAQGEGREQLIDLLPGLFRQSSHSER
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Q8XVD1
Q8Z2X3
LSRK_SALTI
Autoinducer-2 kinase
Salmonella
MARLCTHTESGHYLMALDAGTGSVRAVIFDLQGKQIAVGQAEWQHLAVPDVPGSMEFDLAKNWQLACQCIRQALQKAAIPATAIAAVSACSMREGIVIYDSNGEPIWACANVDARAAHEVSELKELHDNTFEEEVYRCSGQTLALSAIPRLLWLAHHRPDIYHRASTVTMISDWMAFMLSGELAVDPSNAGTTGLLDLVTRNWKRSLLQMAGLRSDILSPVKETGTLLGHISQKAAEQCDLQAGTPVIVGGGDVQLGCLGLGVVRPAQTAVLGGTFWQQVVNLPAPVTDPNMNVRINPHVIPGMVQTESISFFTGLTMRWFRDAFCAEEKLIAERLGIDAYSLLEDMASRVPPGAHGVMPIFSDVMRFKRWYHAAPSFINLSIDPEKCNKATLFRALEENAAIVSACNLQQIAAFSGVQADSLVFAGGGSKGKLWSQILADVTGLTVHVPVVKEATALGCAIAAGVGVGIWPSLAETGEKLVRWDREHKPNPENFAVYQQAREKWQAVYQDQRALVDGGLTTSLWKAPGL
Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position.
Q8Z2X3
A8LXG1
RS18_SALAI
30S ribosomal protein S18
Salinispora
MAKAAALRKPKKKVNPLDKDGITYIDYKDTALLRKFISDRGKIRARRVTGVTSQQQRQIARAVKNAREMALLPYTATAR
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
A8LXG1