Datasets:
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Prot2Text-Data

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accession
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Full Name
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147
⌀
taxon
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
Q57H68
RPOC_SALCH
Transcriptase subunit beta'
Salmonella
MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECETLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELFKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERIYRAGLASLHARVKVRITEYEKDENGEFVAHTSLKDTTVGRAILWMIVPKGLPFSIVNQALGKKAISKMLNTCYRILGLKPTVIFADQTMYTGFAYAARSGASVGIDDMVIPEKKHEIISEAEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAMMDNLQTETVINRDGQEEQQVSFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTHEGILMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADILVPRNTLLHEQWCDLLEANSVDAVKVRSVVSCDTDFGVCAHCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTFHIGGAASRAAAESSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLIDEFGRTKESYKVPYGAVMAKGDGEQVAGGETVANWDPHTMPVITEVSGFIRFTDMIDGQTITRQTDELTGLSSLVVLDSAERTTGGKDLRPALKIVDAQGNDVLIPGTDMPAQYFLPGKAIVQLEDGVQISSGDTLARIPQESGGTKDITGGLPRVADLFEARRPKEPAILAEIAGIVSFGKETKGKRRLVITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEAPHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVIVRQMLRKATIESAGSSDFLEGEQVEYSRVKIANRELEANGKVGATFSRDLLGITKASLATESFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAGEQPATPQVTAEDASASLAELLNAGLGGSDNE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q57H68
P9WMZ8
PIMG_MYCTO
Polyprenol-phosphate-mannose alpha-mannosyltransferase
Mycobacterium tuberculosis complex
MSAWRAPEVGSRLGRRVLWCLLWLLAGVALGYVAWRLFGHTPYRIDIDIYQMGARAWLDGRPLYGGGVLFHTPIGLNLPFTYPPLAAVLFSPFAWLQMPAASVAITVLTLVLLIASTAIVLTGLDAWPTSRLVPAPARLRRLWLAVLIVAPATIWLEPISSNFAFGQINVVLMTLVIVDCFPRRTPWPRGLMLGLGIALKLTPAVFLLYFLLRRDGRAALTALASFAVATLLGFVLAWRDSWEYWTHTLHHTDRIGAAALNTDQNIAGALARLTIGDDERFALWVAGSLLVLAATIWAMRRVLRAGEPTLAVICVALFGLVVSPVSWSHHWVWMLPAVLVIGLLGWRRRNVALAMLSLAGVVLMRWTPIDLLPQHRETTAVWWRQLAGMSYVWWALAVIVVAGLTVTARMTPQRSLTRGLTPAPTAS
Responsible for the addition of alpha-(1-2) mannose branches to the linear mannan core on the biosynthetic pathway to mature lipoarabinomannan (LAM).
P9WMZ8
Q8TV92
MFNA_METKA
Probable L-tyrosine/L-aspartate decarboxylase
Methanopyrus
MILQRDSDYSDGTVLGSMCTEPHPVAAEAFVAGLHVNLGDPYLFPNAYRAERECIGWLAETLLDHPAPEEAEGSIVSGGTEANILAAYAAREVTGGREIIVPATRHFSFEKAARMLRMKLVEAPLRSDYTVDVDAVQDLISRDTALIVGIVGTTETGSVDDIEALSDVAEDHGVPLHVDAAFGGFTAPFLREEYPLPRFGFDLEAVVSVTVDPHKMGLVPPPAGGIVFRDDEFPKAIEVYAPYLSGGGASQYTITGTRPGAPVLALYANILELGEEGYRRIAFRCYEETLKVAEKARELGLELAVDPPHLNLVNIRLPDRGTAERLLRESEREGWKISVSTKPLGVRIVMMPHLDAETVSRFLELVARVLGG
Catalyzes the decarboxylation of L-tyrosine to produce tyramine for methanofuran biosynthesis. Can also catalyze the decarboxylation of L-aspartate to produce beta-alanine for coenzyme A (CoA) biosynthesis.
Q8TV92
A7FG57
DAPE_YERP3
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Yersinia
MICPVIELAQQLIKRPSLSPSDAGCQEIMIQRLAAIGFTIEPMNFGDTLNFWAWRGEGETLAFAGHTDVVPTGDESHWHSPPFEPTIRDGMLYGRGAADMKGSLAAMIVAAERFVAAHPDHKGRLAFMITSDEEAKAINGTVKVVEALMARHERLDYCLVGEPSSTDRVGDIVKNGRRGSITANLRIHGVQGHVAYPHLADNPVHRAMPALNELVATQWDEGNAFFPATSMQIANLQAGTGSNNVIPGEFYVQFNFRFSTELTDSLIKQRVAALLDRHQLDYTLEWVLSGQPFLTAKGALVDAVVNAVKHYTEITPQLLTTGGTSDGRFIALMGAQVVELGPVNATIHKVNECVSAADLQLLSRMYQKIMEQLIA
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.
A7FG57
Q6DIV5
PAMR1_XENTR
Regeneration-associated muscle protease homolog
Silurana
MALLVWSSLVVASLHLLGTAAYPSRSKYTVINENCPGAEWNIMCRDCCEYDQVECACPDGNQKVGYTIPCCRNEENECDSCLIHPGCSIFENCKSCNNGSWGGTLDDFYIKGSYCSECRMGWYGGDCMRCGEVIQAARGEIMLESYPFNARCEWSIQVAPGYTVELRFGMLSLEFDYMCQYDYLEVRDGDNVDAKILKRFCGNQRPLSLRSTGNSLHLLFQSDGSKNFDGFYVTFEEVTGCSSTPCFHDGTCIADKTGSYRCACLAGYTGRHCENVIEEKSCKDPGAPMNGYRKLPDGAGLSLANHIKVGFKIHYFCNNSYVLSGNQERACLQGAQWSGKQPVCIKACKEPKVADLVRQKVLPSLVQSRETPLHQLYSASFTKEKTDILPTKKPALPPGELPPGYQHLHTQLQYDCVSPFYRRTGSSRRTCLKTGKWSGRAPSCIPICGKLENFNITQLGEQRWPWQAALYRRSNGVKDASLRKGSWVLVCSGALLNERTVVMAAHCVTDLGKSSIIKVSDMKVVLGKFYRDDDREEKSQQHLHISAVIVNPNYDPILLDSDIAVIKLLDKARVSDYVQPVCLTLATEMITSPQEYTIVISGWKILSDPRAPGSKNETIRAGAIEPVDSLQCEQQYEENGISVSVTESMFCAKQEPRPSPSICPSETGGITTVLLPSPTSPEGSWHLIGLVSWGYDKSCRKDLYTGYTKVVTFKEWLEKNMK
May play a role in regeneration of skeletal muscle.
Q6DIV5
Q9BYE3
LCE3D_HUMAN
Small proline-rich-like epidermal differentiation complex protein 6B
Homo
MSCQQNQQQCQPPPKCPSPKCPPKSPVQCLPPASSGCAPSSGGCGPSSEGGCFLNHHRRHHRCRRQRPNSCDRGSGQQGGGSGCGHGSGGCC
Precursors of the cornified envelope of the stratum corneum.
Q9BYE3
C6DHS2
THIG_PECCP
Thiazole synthase
Pectobacterium
MLHIADTTLTSRLLTGTGKFATPELMLAALEASGSQLVTMAMKRVDLNGGNDAILAPLRQLGIKLLPNTSGAKTADEAIFAARLAREALGTHWLKLEIHPDVKYLLPDPIETLKAAEQLVKEGFTVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLQTRDFLRIIIEQARVPVIVDAGIGAPSQAADALEMGADAVLVNTAIAVARDPVAMARAFRLAVEAGGLARQAGLGSKQFVASATSPLTGFLHQQAEGAVR
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
C6DHS2
Q072L7
VSP_LACST
Snake venom serine protease
Lachesis
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRSLALVYITSGFLCGGTLINQQWVLTAAHCDRGNMLIFFDVHSLKGLNKDVQSRVAKEKFICPNRKKDDEKDKDIMLIKLDSPVSNSEHIAPLSLPSNPPSVGSVCRIMGWGAITSPNVTLPGVPHCANINILDYEVCRKAYTGLPATSRTLCAGILEGGKDSCKGDSGGPLICNGQFQGIVSWGAHPCGQSLKPGVYTKVFDYTEWIQSILAGNADATCPP
Snake venom serine protease that may act in the hemostasis system of the prey.
Q072L7
A4YUJ5
1A1D_BRASO
1-aminocyclopropane-1-carboxylate deaminase
unclassified Bradyrhizobium
MLRLDKFKKYSLTFGVTPIEHLPRLTAALGGKVQIYAKRDDCNSGLAMGGNKLRKLEYIVPDAIESNADTLVSIGGVQSNHTRMVAATAAKIGMKCVVVQESWVPHEDAVYDRVGNILMTRLMGADSRIVEDGFDIGIRKSWENAIQSVKDAGGKPYGIPAGASVHKFGGLGYVGFAEEVRAQEAEMGIKFDYIIVCVVTGSTQGGMIVGFAADGRADRVIGIDASGTPEQTRAQVRQIVDNTAELVELGRKVRDDEIVILNDYAYPAYGVPSAETNEAIRLAARTEAMITDPVYEGKSMQGMIDLVKKGYFPEGSKVLYAHLGGAPAINGYSYTYRNG
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source.
A4YUJ5
K0DZ91
ECDJ_ASPRU
Echinocandin B biosynthetic cluster protein J
Aspergillus
MHFAESVQTPPPSRPSDQSLNQHVLDLGSWDQGCRDLMLVNWLCVDFRQRLLNVLYTSCQKNFNEARSLARERLLDLVQRIASSDNLHGALYTPPSLDSRSSATPPQNLPPTPDLVQCIRGCDEPFPPLSLPTPAQIDTQENERLMCTPEDITYHDRDSQVVAQARRRSPPGTGPAVLPPIAFDNHELPPGCSDFLNFDLLSDGEVFSIGTHAGVTSDVCDSMPLDHDLSEMELDPPPDATTTTTTTTVSSPNVHSTHHLAIPNPEPGTPTPPSPLAGTSLTRKPPGTPDSPSAASQRRQRQRRAAAHATYRSTPSPCQSADTHIGAENEVAEPAPPSPSTRWTHSIPTHLPSPDTVLATFTHHLGRGKQSIALLLTRLFYAIGSPDALSQLRDAVKLSREQTPAIIPVSSTNDLATTVKALDHLDSMTTLSHILRRYYLVRLLEHRTRFEQDHVTAKQAWRPPKRMLKYDCARVELIKNGGNCSSSSCSSSASKKNEEKREPPLKYRSKSQALADLMQMLYPDLKPAVAEGKDCVYSRKLTKLRNRLSCARNWYRFEQAFPGAILALIPCAGRFSVSIDQIEKLPSDTVQIFLDYLQEHRGVFSRCVSQTLGTGIFSVLARTSADAAPTFAFEKVEEEGFGDLLYDTDELVSLSIEYDRYCDLNSNA
Part of the gene cluster that mediates the biosynthesis of echinocandin B, a fungal lipidated cyclic hexapeptide that acts as an antifungal agent . Linoleoyl-AMP, produced by the fatty-acyl-AMP ligase ecdI, is transferred to the initiation carrier domain (T0) of ecdA . The linoleoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-ornithine, L-threonine, L-proline, L-homotyrosine, L-threonine, and 4R-methyl-L-proline to form the linear hexapeptide . Thereafter, the terminal condensation (C7) performs macrocyclization of the NRPS product and the cyclic scaffold is released from ecdA . All six of the amino acid residues are hydroxylated, including 4R,5R-dihydroxy-L-ornithine, 4R-hydroxyl-L-proline, 3S,4S-dihydroxy-L-homotyrosine, and 3S-hydroxyl-4S-methyl-L-prolin . In the pathway, all the hydroxylation reactions are proposed to occur following completion of the cyclic peptide, so the unhydroxylated precursor produced by ecdA will undergo six rounds of hydroxylation . Five hydroxylase genes (ecdG, ecdH, ecdK, htyE and htyF) are embedded within the echinocandin B (ecd) and L-homotyrosine (hty) clusters .
K0DZ91
Q0T0B7
PNP_SHIF8
Polynucleotide phosphorylase
Shigella
MLNPIVRKFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPIRPLFPEGFVNEVQVIATVVSVNPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVAGTEAAVLMVESEAELLSEDQMLGAVVFGHEQQQVVIQNINELVKEAGKPRWDWQPEPVNEALNARVAALAEARLSDAYRITDKQERYAQVDVIKSETIATLLAEDETLDENELGEILHAIEKNVVRSRVLAGEPRIDGREKDMIRGLDVRTGVLPRTHGSALFTRGETQALVTATLGTARDAQVLDELMGERTDTFLFHYNFPPYSVGETGMVGSPKRREIGHGRLAKRGVLAVMPDMDKFPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNYVVLSDILGDEDHLGDMDFKVAGSREGISALQMDIKIEGITKEIMQVALNQAKGARLHILGVMEQAINAPRGDISEFAPRIHTIKINPDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAATDGEKAKHAIRRIEEITAEIEVGRVYTGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVTDYLQMGQEVPVKVLEVDRQGRIRLSIKEATEQSQPAAAPEAPAAEQGE
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Q0T0B7
Q1R9Z5
MDTC_ECOUT
Multidrug transporter MdtC
Escherichia
MKFFALFIYRPVATILLSVAITLCGILGFRMLPVAPLPQVDFPVIMVSASLPGASPETMASSVATPLERSLGRIAGVSEMTSSSSLGSTRIILQFDFDRDINGAARDVQAAINAAQSLLPSGMPSRPTYRKANPSDAPIMILTLTSDTYSQGELYDFASTQLAPTISQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDDVRTAISNANVRKPQGALEDGTHRWQIQTNDELKTAAEYQPLIIHYNNGGAVRLGDVATVTDSVQDVRNAGMTNAKPAILLMIRKLPEANIIQTVDSIRARLPELQSTIPAAIDLQIAQDRSPTIRASLEEVEQTLIISVALVILVVFLFLRSGRATIIPAVAVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENIARHLEAGMKPLQAALQGTREVGFTVLSMSLSLVAVFLPLLLMGGLPGRLLREFAVTLSVAIGISLLVSLTLTPMMCGWMLKASKPREQKRLRGFGRMLVALQQGYGKSLKWVLNHTRLVGVVLLGTIALNIWLYISIPKTFFPEQDTGVLMGGIQADQSISFQAMRGKLQDFMKIIRDDPAVDNVTGFTGGSRVNSGMMFITLKPRGERSETAQQIIDRLRKKLAKEPGANLFLMAVQDIRVGGRQANASYQYTLLSDDLAALREWEPKIRKKLATLPELADVNSDQEDNGAEMNLIYDRDTMARLGIDVQAANSLLNNAFGQRQISTIYQPMNQYKVVMEVDPRYTQDISALEKMFVINNEGKAIPLSYFAKWQPANAPLSVNHQGLSAASTISFNLPTGKSLSDASAAIDRAMTQLGVPSTVRGSFAGTAQVFQETMNSQVILIIAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALQLFNAPFSLIALIGIMLLIGIVKKNAIMMVDFALEAQRHGNLTPQEAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGSELRQPLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKPKQAVTE
The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate.
Q1R9Z5
Q8FCQ2
UGPC_ECOL6
sn-glycerol-3-phosphate import ATP-binding protein UgpC
Escherichia
MAGLKLQAVTKSWDGKTQVIKPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTTGDIWIDRKRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKQQIAERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNGGVAEQIGTPVEVYEKPASLFVASFIGSPAMNLLAGRVNNEGTHFELDGGITLPLNGGYRQYAGRKMTLGIRPEHIALSLQAEGGVPLVMDTLEILGADNLAHGRWGEQKLVVRLAHQERPTAGSTLWLHLPENQLHLFDGETGQRV
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.
Q8FCQ2
Q2QXJ2
GL122_ORYSJ
Germin-like protein 12-2
Oryza sativa
MASSNFFLLTALIALVATQAMASDPSPLQDFCVADRNSPVHVNGFPCKDAKDVNVDDFFLAANLDKPMDTTKSKAGSNVTLINVMKLAGLNTLGISMARIDYAPKGQNPPHTHPRATEILTVLEGTLYVGFVTSNQANGENKLFTKTLNKGDVFVFPQGLIHFQFNPSYDKPAVAIAALSSQNPGAITIANAVFGSNSPISDDVLAKAFQVDKKAVDWLQAQFWENNHN
May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Q2QXJ2
Q743C2
Y663_MYCPA
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_0663
Mycobacterium avium complex (MAC)
MARTDRDRWDLATSVGATATMVAAQRALSSDANLIDDPYAAPLVRAVGIDVYVRLVDGEIQPGTSEFDPHRMAKGMACRTRFYDDFFLDAARAGVGQAVILASGLDARAYRLPWPAGTVVYEVDMPDVIEFKTLTLADLGAQPTAQRRTVAIDLRDDWAAALREERFDTQAPAAWSAEGLLVYLPEQAQDALFDNITALSAPGSRLAFDFVPDTAVFADPRWRAHHDRMSELGFEVDFNDLVYHGERSHIVDHLSGRGCSLVPLFRVG
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
Q743C2
C1F2I3
LEPA_ACIC5
Ribosomal back-translocase LepA
Acidobacterium
MDSKYIRNFAIIAHIDHGKSTLSDRLLEMTGSLTAREMQAQVLDAMDLERERGITIKAHAVRMLYKAKDGETYQLNLIDTPGHVDFSYEVSRSLASCEGALLIVDASQGVEAQTLANAYLAINNGLEIIPVINKIDLPSADITRTQEMIEQAVGLDATDAIPVSAKTGVGVPDVLEAIVKRLPPPTGDPNAPLQALIFDSWFDAYRGVIVLARVMNGTLRKGMRIRLMSNGKVFDVESMGVLTPKPMEIGELSAGEVGFFVATIKTVSDTKIGDTVTEDARPAAEPLAGFEDIKSMVFAGIYTVDSHEHTLLRDALEKLRLNDSSFFFEPESSVALGFGFRCGFLGLLHMEIIQERLEREFDLDLITTAPGVRYKITMTDGSTLEVDNPSRWPDPSEIEQVEEPVIRATILTNEEYVGGILKLVEEKRGRQQNFEYVTPTRVMLTYELPLNEIVLDFYDRLKSVSRGYASLDYQLAGTWVSPMVKMDILVSGEPVDALSIIVHRDFAYERGRALVSKMRELIPRQQFEVAIQAAIGSKIIARETVAALRKNVIAKCYGGDISRKRKLLEKQKEGKKRMKRIGKVDIPQEAFLAVLKVGEDSASKN
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.
C1F2I3
Q98N40
RS5_RHILO
30S ribosomal protein S5
Mesorhizobium
MAQERREGGRGREREERDDGMVDKLVHINRVAKVVKGGRRFGFAALVVVGDQKGRVGFGHGKAREVPEAIRKATESAKRDMIFVPLRSGRTLHHDVEGRWGAGRVLLRAAKQGTGIIAGGPMRAVFETLGMHDVVAKSMGSSNPYNMVRATFDALKSQMHPKDVAAARGIKYSTLQARRGTAVAAEE
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Q98N40
A6QCS1
RS13_SULNB
30S ribosomal protein S13
unclassified Sulfurovum
MARIAGVDLPQKKRIEYALTYIYGIGLTTSRKILDRTGIDYNTRVHELTDAQAATIRNDIQENVMVEGDLRKKVTLDIKALMDLGSYRGLRHRRGLPCRGQKTKTNARTRKGKRKTVGAA
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.
A6QCS1
P06168
ILV5_YEAST
Isoleucine-plus-valine requiring protein 5
Saccharomyces
MLRTQAARLICNSRVITAKRTFALATRAAAYSRPAARFVKPMITTRGLKQINFGGTVETVYERADWPREKLLDYFKNDTFALIGYGSQGYGQGLNLRDNGLNVIIGVRKDGASWKAAIEDGWVPGKNLFTVEDAIKRGSYVMNLLSDAAQSETWPAIKPLLTKGKTLYFSHGFSPVFKDLTHVEPPKDLDVILVAPKGSGRTVRSLFKEGRGINSSYAVWNDVTGKAHEKAQALAVAIGSGYVYQTTFEREVNSDLYGERGCLMGGIHGMFLAQYDVLRENGHSPSEAFNETVEEATQSLYPLIGKYGMDYMYDACSTTARRGALDWYPIFKNALKPVFQDLYESTKNGTETKRSLEFNSQPDYREKLEKELDTIRNMEIWKVGKEVRKLRPENQ
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes the second common step in the parallel biosynthesis of isoleucine and valine. Converts alpha-aceto-alpha-hydroxybutyrate (AHB) to alpha,beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-acetolactate (AL) to alpha,beta-dihydroxy-isovalerate (DHV) in isoleucine and valine biosynthesis, respectively.
P06168
A7H8A2
DNLJ_ANADF
Polydeoxyribonucleotide synthase [NAD(+)]
unclassified Anaeromyxobacter
MRADADRDSAETRAAELRARILDADHAYYVLDRPVLADAEYDRLVRELAEIEAAHPELATSDSPTQRVSGAPSERFERVVHREPMLSLGNIQSDGELDEFDARVHRLLGLAGDVQVGYVAEPKLDGLAVELVYEGGRLVQGSTRGDGVNGEDVTANLRTVGRTRANRGVPERLAGEVPPRVEVRGEVLLFKEHFEAMNRQILRAGDEPFANPRNAAAGSLRQLDWRVTARRPLSFIAYEALVPGAEPGGARAGPWAWRTHAEKLEALARWGFETNAENERCEGIAAVKAYRDRMAERRFALPYDTDGVVVKVDDLDWRRRLGAASKFPRWAVAFKYPPQEEATRIRRIWASVGRTGILTPVVDFEPVRLSGAMVSRATLHNEDEMRRKDVLEGDWILVRRAGEVIPEVVMPLKERRTGEERPFAFPAECPICGAKVVREEGEKVYRCTGAACPAQLVGRLTHFAQRRAMDIDGLGDKLALGLVERGLVKDFADLYAVPFPAWQELFSRPRKEERDAKAELPQKSAQNMVDALERSKATTLRRLLFALGIPQVGEATAATLARHFGELARFMDASEDALLAVRDVGPETAREIRAWTEEPQNRRVVERLLAAGVRPAPETVDAGGPFAGKTVVLTGGLAALSRDDAKAEIERRGGKVSGSVSRKTDLVVAGAEAGSKLEKAQALGVRVVGEEEFLRMLEE
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
A7H8A2
Q982Z7
IHFA_RHILO
Integration host factor subunit alpha
Mesorhizobium
MGGKTLTRADLAEAVYRKVGLSRTESAELVEAVLDEICEAIVRGETVKLSSFATFHVRSKNERIGRNPKTGEEVPILPRRVMTFKSSNVLKNRILRSHQNSKAKGGK
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Q982Z7
Q1LQS5
CH10_CUPMC
Chaperonin-10
Cupriavidus
MNLRPLHDRVIVKRLDNETKTASGIVIPDNAAEKPDQGEVLAIGPGKKDDKGNNIALDVKVGDRVLFGKYAGQGVKVDGQELLVMREEDIMAVVNK
Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Q1LQS5
B9DNC4
RL20_STACT
50S ribosomal protein L20
Staphylococcus
MPRVKGGTVTRARRKKVIKLAKGYFGAKRTLYKTAKQQVMKSGQYAFRDRRQRKRDFRKLWITRINAAARNHGMSYSKLMNGLKQADIDINRKMLSEIAISDDKAFGELVEKAKAALK
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.
B9DNC4
A7FZ44
RPOA_CLOB1
Transcriptase subunit alpha
Clostridium
MLEIEKPKIECVENAEDGSYGKFVIEPLERGYGITLGNALRRILLSSLPGVAADHIKIDSVLHEFSTVQGVKEDVTELILNIKCLALTMNGEGPKTIYIDEVGPKEVTAADIKTDGDVEVINKDLHIATLDENGKMYMEINVNRGRGYVTQNKNKTKDMPIGSIAVDSIYTPVKRVNFSVENTRVGQITDYDKLTIEVWTNGTIRPEEAVSLSAKILIEHFKLFMTLTDHADDMEIMVEKEEDKKEKVLEMTIEELDLSVRSYNCLKRAGINTVQELCERSMDDMMKVRNLGKKSLEEVEQKLEALGLGLRKSED
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A7FZ44
Q3MBG1
PURA_TRIV2
IMP--aspartate ligase
Trichormus
MANVIVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVKGQTFKLHLIPSGILYPDTECMIGCGTVIDPQVLIKELDQLESLNISTKNLLISETAHVTMPYHRLIDKASEERRGSHKIGTTGRGIGPTYADKSERTGIRVLDLMDPAALRDQLAWTINNKNLILEKLYNLPPLDTEEVVKEYLGYAERLRPHVVDTSLKIYDAIQRRRNILFEGAQGTLLDLDHGTYPYVTSSNPVAGGACVGTGLGPTMIDRVIGVSKAYTTRVGEGPFPTELDGELGELLCDRGAEFGTTTGRKRRCGWFDAVIGRYAVRINGMDCMAITKLDVLDELEEIQVCIAYEIDGDRCDHFPTSARQFARCRPIYKTLPGWQVPTSECRTLEDLPQQALDYLKFLAELMEVPIAIVSLGASRDQTIIVEDPIHGPKRALLHPDGTPASLLSA
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Q3MBG1
Q0V8N6
P3_BOVIN
Solute carrier family 10 member 3
Bos
MVFRSGEGHSLQWPGPEGGTGCTGPQSMLRATLLLVSLLWGARGTPSASLSPALGHPMPLTRGRYLSIGDGSVMEFEFPEESEGIIVITSQYPGQGNGTGPSPMLRVTSLDPEVLAIKNVSSIALGSGGSFVVSIRSGLPGIAPLHIQLTDPREAPPRLIEERRDFCIKVSPAEDTPITLGTDLVHFSENPILYLLLPLIFVNKCSFGCKVELEVLKGLLQNPQPMLLGLLGQFLVMPFYAFLMAKVFMLPKALALGLIITCSSPGGGGSYLFSLLLGGDVTLAISMTFISTVAATGFLPLSSAIYSRLLSIHETLHVPVSKILGTLLFIAIPIAAGVVIKSKLPKFSQLLLHVIKPFSFVLLLGGLFLAYRMGVFILAGVRLPIVLVGFTVPLVGLLVGYGLATCLKLPVAQRRTVSIEVGVQNSLLALAMLQLSLRRLQADYASQAPFLVALSGTSEMLALVIGHFIYSSVCAVP
The ubiquitous expression and the conservation of the sequence in distant animal species suggest that the gene codes for a protein with housekeeping functions.
Q0V8N6
A6UPB5
PYRI_METVS
Aspartate carbamoyltransferase regulatory chain
Methanococcus
MKVELKVKPIENGTVIDHIESSKALKVYDLLKINESMPVTLALNVSSKKGSLKDILKIEGLALSKADVNKIALVSPNATINIIKDGKVVSKFKVGIPNKIDGIVKCTNPNCITNKEGIKSKFTVEQKDTLKIRCDYCEKFINSIIISR
Involved in allosteric regulation of aspartate carbamoyltransferase.
A6UPB5
Q1LRP1
HPRK_CUPMC
HPr(Ser) kinase/phosphorylase
Cupriavidus
MELTGVTSQSIFDDNAADIKLSWVAGLEGADRAFDVEFAREATSAADLVGHLNLIHPNRIQVLGKPEILYYQRLDDEPRKRQMGELILLEPPFLVVADGMEPPPDLELRCTRSSTPLFTTPVSSAAVIDHLRLYLSRISAPRVTMHGVFLDILGMGVLIMGESGLGKSELGLELISRGHGLVADDAVDFVRLGPDFIEGRCPPLLQNLLEVRGLGLLDIKTIFGETAVRRKMKLKLVVQLVRRNDGEFERLPLDSQYLDVLGLPIHMVKIQVAAGRNLAVLVEAAVRNTILRLRGIDTLRDFMDRQRAAMQADVVSRGQGRLL
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
Q1LRP1
Q1MLG8
CHEB1_RHIL3
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
Rhizobium
MSAPARVLVVDDSATMRGLITAVLSSDPEVNVIGQAGDALEAREAIKRLNPDVLTLDIEMPNMNGLDFLEKIMTLRPMPVIMVSTMTHRGAEATLAALEIGAFDCVGKPAPGELRPFGDLAEKVKAAARTQRQYSQPVVAVAPPPSVADFRVGRKIVAIGSSTGGVEALIAVLQKFPANCPPTVITQHMPPTFTKSFAERLNRLCAPVVQEATDGARLEIGKIYLAPGGERHLQVSGASAPCCRLIDRAPVNGHRPSVDVLFDSVAELAGRNAVGVILTGMGRDGAAGLLKMRHAGARTLGQNEKTCVVYGMPRVAHELGAVEQQLPLSAIGEEILKMTAARKEGTE
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Q1MLG8
P52333
JAK3_HUMAN
Leukocyte janus kinase
Homo
MAPPSEETPLIPQRSCSLLSTEAGALHVLLPARGPGPPQRLSFSFGDHLAEDLCVQAAKASGILPVYHSLFALATEDLSCWFPPSHIFSVEDASTQVLLYRIRFYFPNWFGLEKCHRFGLRKDLASAILDLPVLEHLFAQHRSDLVSGRLPVGLSLKEQGECLSLAVLDLARMAREQAQRPGELLKTVSYKACLPPSLRDLIQGLSFVTRRRIRRTVRRALRRVAACQADRHSLMAKYIMDLERLDPAGAAETFHVGLPGALGGHDGLGLLRVAGDGGIAWTQGEQEVLQPFCDFPEIVDISIKQAPRVGPAGEHRLVTVTRTDNQILEAEFPGLPEALSFVALVDGYFRLTTDSQHFFCKEVAPPRLLEEVAEQCHGPITLDFAINKLKTGGSRPGSYVLRRSPQDFDSFLLTVCVQNPLGPDYKGCLIRRSPTGTFLLVGLSRPHSSLRELLATCWDGGLHVDGVAVTLTSCCIPRPKEKSNLIVVQRGHSPPTSSLVQPQSQYQLSQMTFHKIPADSLEWHENLGHGSFTKIYRGCRHEVVDGEARKTEVLLKVMDAKHKNCMESFLEAASLMSQVSYRHLVLLHGVCMAGDSTMVQEFVHLGAIDMYLRKRGHLVPASWKLQVVKQLAYALNYLEDKGLPHGNVSARKVLLAREGADGSPPFIKLSDPGVSPAVLSLEMLTDRIPWVAPECLREAQTLSLEADKWGFGATVWEVFSGVTMPISALDPAKKLQFYEDRQQLPAPKWTELALLIQQCMAYEPVQRPSFRAVIRDLNSLISSDYELLSDPTPGALAPRDGLWNGAQLYACQDPTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFTAHPEGKHHSLSFS
Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A and STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion.
P52333
A9NEE9
RL18_ACHLI
50S ribosomal protein L18
Acholeplasma
MINKKSSNETRQKRHLRIRKHVIGTPDRPRLNVFRSNTAIYVQIINDETHNTLTSANTKELKVGANIEGAAALGKAVAEQALKLGITKVVFDRGGYLYHGRIKALADAARAAGLEF
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.
A9NEE9
Q8NHU3
SMS2_HUMAN
Sphingomyelin synthase 2
Homo
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYIQIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDYIDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFIKEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGEDNEKST
Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane . Does not use free phosphorylcholine or CDP-choline as donors . Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) . Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting . To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1 . Required for normal bone matrix mineralization .
Q8NHU3
B9DVG5
GATB_STRU0
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Streptococcus
MNFETIIGLEVHVELNTNSKIFSPSSAHFGQEANANTNVIDWSFPGVLPVINKGVIDAGIKAALALNMDIHKKMHFDRKNYFYPDNPKAYQISQFDEPIGFNGWIDITLEDGTSKKIRIERAHLEEDAGKNTHGTDGYSYVDLNRQGVPLIEIVSEADMRSPEEAYAYLTALKEIIQYTGISDVKMEEGSMRVDANISLRPYGQKEFGTKTELKNLNSFSNVRKGLEFEVERQAKVLRSGGVIRQETRRYDEASKGTILMRVKEGAADYRYFPEPDLPLYEIDDVWIEEMRHELPQFPAQRRATYINDLGLSSYDANQLTATKAMSDFFEKAVALGGDAKQVSNWLQGEVAQYLNAEGKAIQEISLTPANLVEMIGIIADGTISSKIAKKVFVHLAKNGGSAREYVEKAGLVQISDPDVLIPIIHRVFEEQEAAVVDFKSGKRNADKAFTGFLMKATKGQANPQVAQQLLAQELQKLLD
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
B9DVG5
Q0SNW3
DDL_BORAP
D-alanylalanine synthetase
Borreliella
MKKNLMLIFGGVSFEHEISCKSAYSVYLALLDLNKYNIYSAYIDKCTGIWYLLDSVSDPPKPIDTDVLPIVSLLPGFGIFSNNKNLEIDVVFPVVHGRTGEDGAIQGVLKVMDIPCVGAGIIGSAISSNKYFCKLLLKSFNIPIVPFIGFRQYDYSLDKEEIKRNVKEVLGYPVIVKPAVLGSSIGINVAYSENQIESCIEEALKYDLTIVIEKFIEAREIECSIIGNEKMKIFSPGEVVVQDFIFYDYDAKYSVIPGNSIIFNIPAHLETNQLLSIKEYAFLVYKNLELRGMARVDFFVEKKSGTIYLNEINTIPGFTDISMFSKMCSHDGLQFKDLIDNLIDYAFQSYINRKKRINFKD
Cell wall formation.
Q0SNW3
Q6DJC8
TM53B_XENLA
Transmembrane protein 53-B
Xenopus
MGDPELDYTIEFPEPSLQGCPWDPEREPVVILLGWGGCKDQYLAKYSAIYHNQGCTVIKYTAAWNAVFISESLGFSSLREDAKKLLELLFDYEIEKSPILFHVFSNGGFMLYRYIVELLHSHCRLNKLHVVGTIFDSAPGNRNVIGSVRALDTILRTSTNNAIRFLALAAFAIMVIILRIVLYPVTKFLHENHYDAMKKDSSRWPQLYLYSRADPIISYIDVESMIAARRRCCLPTEALDFGKSEHVSHFRRFPHRYSEMCTSFLRDCVRKAAVSMLTSEHPVSF
Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD proteins.
Q6DJC8
U3KRF2
DHQS_ACTCC
3-dehydroquinate synthase, chloroplastic
Actinidia
MAAFSLSAKQILSPSTHRPSLSKTTTADSSLRFRNPHSLSLRCSSLSSSSNVGRTRLMRASASSTAPVMDTSPTKAVSSAPTIVDVDLGDRSYPIYIGSGLLDQPDLLQRHVHGKRVLVVTNSTVAPIYLDKVVGALTNGNPNVSVESVILPDGEKYKNMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNLIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVVKYGLIRDANFFEWQEKNMPALMARDPSALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGFGYGQWLHGEAVAAGMVMAVDMSYRLGWIDESIVNRAHNILQQAKLPTAPPETMTVEMFKSVMAVDKKVADGLLRLILLKGPLGNCVFTGDYDRKALDETLHAFCKS
Catalyzes the second step in the shikimate pathway.
U3KRF2
P44506
PLPHP_HAEIN
Pyridoxal phosphate homeostasis protein
Haemophilus
MNIQHNLNLIQQKIETACKEENRNQNTVKLLAVSKTKPISAILSAYQAGQTAFGENYVQEGVEKIQYFESQGINLEWHFIGPLQSNKTRLVAEHFDWMQTLDRAKIADRLNEQRPTNKAPLNVLIQINISDEESKSGIQPEEMLTLAKHIENLPHLCLRGLMAIPAPTDNIAEQENAFRKMLELFEQLKQVLPNQQIDTLSMGMTDDMPSAIKCGSTMVRIGTAIFGARNYSTSQNK
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
P44506
Q8EGR9
DXS_SHEON
1-deoxyxylulose-5-phosphate synthase
Shewanella
MSLDISQFPVLAQANTPNELRQLPQALLPQLADELREFLLKSVGMSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTGRRDRMHTIRQKNGLHPFPWREESEYDTFSVGHSGTSISAALAMAVAAEKEQAGRKVVAVIGDGAMTGGMVFEAMNHAGDLHNDMLMVLNDNEMSISENVGALNNHLAQLMSGRFYTTIRESSKKVLKGMPVIKEMAKRTEEHLKGMVVPGTLFEELGFNYIGPIDGHDVDALVETLRNMRNLKGPQVLHIMTKKGRGYEPAEKDPIGWHAVPKFDPSLFKKPATKPGLPTFSQVFGKWLCDIAEQDEKVLGITPAMREGSGMVEFSQRFPKQYFDAAIAEQHAVTLGAGFACEGYKPVVAIYSTFLQRGYDQLIHDVALQRLPVLFAIDRGGIVGADGPTHQGAFDLSFMRCIPNMVIMAPSDENECRQMLYTGYCYDAGPSAVRYPRGSATGATQVEAMTALPIGKGVIKRLGKRIALLNFGTTLAAALTAAESLDATVVDMRFVKPLDVDLVKEMAQTHDVLVTVEENAIMGGAGSGVLELLQQLKMPKPVLQIGLPDEFIKHGSPDEVIHDLQLDAEGMLAQINAYLAN
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Q8EGR9
Q7VTF0
TRPA_BORPE
Tryptophan synthase alpha chain
Bordetella
MTTTDRIAAAFARVSEAGRAAALIPYIAAGDPSPQATVPLMHALVRAGADLVELGVPFSDPMADGPVVQRAAERAIAQGVGLRRVLELVADFRRDDSVTPVVLMGYANPIERMGQRAFAQAAQAAGVDGVLVVDYPPEEVDEFAVMLAEAGVAPIFLLAPTSTEARIEAIGRVARGYVYYVSLKGVTGAGSLDTDDVARKLALIRRHVHIPVGVGFGIRDAASAQRIAAHADAVVIGSKLIETMEQAGAQAGADQKNEAAIAAAQQWLHTIRLALDDVKRENAPA
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Q7VTF0
A1R665
IOLG1_PAEAT
Myo-inositol 2-dehydrogenase 1
Paenarthrobacter
MTKTLRVAVIGAGRMGADHIKRLSTRIHGAEVAAVVDVDLARAQAAIEGIDRAVALASADEALNNGDVNAVLIATPGFLHEEILYKALEKDFPILCEKPLTPDAGSAWKVVQAEQALGHKRIQVGFMRRFDAEYSALGAIIRNSELGELLMLHHQHRNPSTPEGFTNEMLINDSVVHEFDAIRFFTGEEITSVQVRLGKPTRSAPSGQHDPQHVLLETESGVLADVEIYVNAKFGYQVATQASFEEGIVSIGSDNGPYVQTAGKWGGNVTPGFEERFGAAYDVEVQAWVDAALRGEIGGPTAWDGYATAACCEAGVEAQKSGEKVKVQLNTKPDLYK
Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
A1R665
A3DNN7
PGP_STAMF
Phosphoglycolate phosphatase
Staphylothermus
MIRLAAFDIDGTLTINRSSTVLCLEAIDALRKLEKNGVIVVLVSSNALPVVVGLKKYIGLSGPAIGETGALIYYGEEEIVATTKYSAKQAYLDVLEKYNEYVYGSWQNMFRLHDYALKIRKQYLSKDNEIYSLIKEYVENKYPYIKVGYSGYAIHLTPKDTGKGKALKQIMEKHGIRREETMGVGDSIMDWEFIKETKIKVAVANADPELRRKADIVTTKPSGYGVVEIVEKILDKPP
Catalyzes the dephosphorylation of 2-phosphoglycolate.
A3DNN7
A0R2D1
TATB_MYCS2
Sec-independent protein translocase protein TatB
Mycolicibacterium
MFANIGWGEMLVLVIAGLVILGPERLPGAIRWTSGALRQARDYVSGATSQLRQDLGPEFDDLREPLQELQKLRGMTPRAAITKHLLDGDDSFLTGKFDDERPKQQPQTPAAQDKPEEKPDKPAGPVFDPDAT
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
A0R2D1
B3E5N0
GMHA_TRIL1
Sedoheptulose 7-phosphate isomerase
Trichlorobacter
MQSFIAKQLQDHLALFQKMEAELTAPVAELAERLIETFKIGNKLLIMGNGGSAADAQHFAGEIVSRFRIERPGLPAIALSTDTSIITAIGNDYGFERIFSRQVEALAVPGDAVIGISTSGNSPNVQKALEVARQAGCTTIGLLGKDGGSIKAVCDIPLIIPSNDTPRVQEGHIAVIHILCDLIEQGLFGIFAGEGR
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
B3E5N0
A0PRD3
AROA_MYCUA
5-enolpyruvylshikimate-3-phosphate synthase
Mycobacterium
MSSIEPWPAPFAPTPVHATVTVPGSKSQTNRTLVLAALAAAQGQGSSTITGALRSRDTDLMIEALQTLGLRVDGTGSELTVSGRIRPCPEARVDCGLAGTVLRFAPPLAALSAAPITFDGDEQARARPIAPLLDALRGLGVPVDGAGLPFRVQGTGSVAGGTVAIDASASSQFVSGLLLSGASFTDGLTVQHTGSELPSAPHIAMTVQMLRQAGVDVDDSIPNRWLVRPGALRPRHWDAEPDLTNAVAFLAAAVVTGGTVTITGWPADSVQPAKNILDILQTLNSTVRHIDSCLQVQGPQSYRGFDVDLRDVGELTPSVAALAALASPGSVSRLAGIAHLRGHETDRLAALSTEINRLGGNCEQTSDGLVITATPLRPGSWRAYADHRMAMAGAIVGLRVAGVEVDDIGATSKTLPEFPQLWTEMVEGSSG
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
A0PRD3
Q31QR8
SIGA4_SYNE7
RNA polymerase sigma factor SigA4
Synechococcus
MNVQERRNLNAAVERHTSDHVSWYLSSIGRIPLLTAEEEVELSRKVQLMMALLENPDAESNSENQAVLQAGQRAKTKMLKANLRLVVSVAKKYQNQGLELLDLIQEGSLGLERAVEKFDPALGYKFSTYAYWWIRQSMTRAIDNHARTIRLPIHVSEKISRIKKMTRELTHQLKRLPSRAEIAEALKLPLQDVEMLLSQSTPCTSLDAQARGDDGRSFLGDLIPDPKSLEPMDAMDRHIQHEQISTWLAHLTEREQQVLQLRFGLHDGEQHTLAEIGRRLNVSRERIRQVEARALQKLRVLSQQPLCPEAC
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Q31QR8
A9VH11
GCSPA_BACMK
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
Bacillus cereus group
MLHRYLPMTEEDKKEMLQTIGVQTIDELFSDIPESVRFKGDLKIKEAKSEPELLKELSQMASKNANLKEYASFLGAGVYDHYAPVIVDHVISRSEFYTAYTPYQPEISQGELQAIFEFQTMICELTGMDVANSSMYDGGTALAEAAMLAAGHTRKKKILVSAAVHPESRAVLETYAKGQNLEVVEIDHKNGVTDLEVLQSEVDDTVACVIVQYPNFFGQVEKLADIEKIVHQQKSLFIVSSNPLSLGALTPPGKFGADVVIGDAQPFGIPTQFGGPHCGYFATTKAFMRKIPGRLVGQTVDSDGKRGFVLTLQAREQHIRRDKATSNICSNQALNALAASVAMTALGKQGVKEMARQNISKAQYAKRQFEAKGFTVTFAGPFFNEFVVDCKRPVKEINDVLIQKNIIGGYDLGRDYKEHENHMLVAVTELRTKEEIDTLVNEMGAIQ
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
A9VH11
P08821
DBH1_BACSU
HB
Bacillus
MNKTELINAVAEASELSKKDATKAVDSVFDTILDALKNGDKIQLIGFGNFEVRERSARKGRNPQTGEEIEIPASKVPAFKPGKALKDAVAGK
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Binds evenly across chromosome, does not display a preference for AT content .
P08821
Q5X118
LGT_LEGPA
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Legionella
MLTYPNINPIAFSLGPLKVHWYGLMYLIGFIGAWLLGYWRIKHYKLNWNNDQLSDLIFYSALGVILGGRVGYMLFYDIQEFIHHPWVLFKIWEGGMSFHGGLLGVVIAAWLFCRKYGKTFLEVGDFVAPLVPLGLAAGRLGNFINGELWGRVTDVPWGMIYPHVDDQPRHPSQLYEFGLEGVALFILIWCYASKPRQQGRVCALFLMGYAICRLIAESFRQPDSQLGFVAFGWLTMGQVLSIPMLLIGIWLWWAKR
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Q5X118
O97571
CXCR2_CANLF
High affinity interleukin-8 receptor B
Canis
MEYINWDNYSLEDLFGDIDNYTYNTEMPIIPADSAPCRPESLDINKYAVVVIYVLVFVLNLLGNSLVIMVVLYSRVSHSVTDVYLLNLAIADLLFALTLPIWAVSKVKGWIFGTPLCKIVSLLKEVNFYSGILLLASISMDRYLAIVHATRRLTQKKHWVKFICLGIWALSLILSLPIFVFRRAINPPYSSPVCYEDMGTNTTKLRIVMRALPQTFGFIVPLMIMLFCYGLTLRTLFEAHMGQKHRAMRVIFAVVLVFLLCWLPYNLVADTLMRLQAIEETCQRRNDIGRALDATEILGFFHSCLNPLIYAFIGQKFRHGLLKIMAFHGLISKEYLPKDSRPSFVGSSSANTSTTF
Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2.
O97571
Q2JNP0
FTSH_SYNJB
ATP-dependent zinc metalloprotease FtsH
unclassified Synechococcus
MSQKGKNKKWRSAGLYALLAIVLISLATTFLGNRPPERLEISYSDLISRVERGEVSKVLVETAPDGRQVAIAEAEINNRATQVQVNLPPLTPEFENTLVANGVELAVRPVQEEGLLGRILSTFFLPVLLLLGLFFLLRRAQNGPGSQALNFGKSRARVQMEPKTQITFNDVAGIDQAKLELAEVVDFLKNSERFTALGAKIPRGVLLVGPPGTGKTLLARAVAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFEQAKQNAPCIVFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLTEMDGFEGNSGIIVIAATNRPDVLDAALLRPGRFDRQVTVDRPDFQGRLEILKVHARGKTLSADVDLEKLARRTPGFTGADLANLLNEAAILAARRNLTEISMDEINDAVDRVLAGPEKKDRLMSERRKELVAYHEAGHALVGSLLPNYDPIQKVTIIPRGQAGGLTWFMPSDDDMGLTTRAHLKNMMTVALGGRVAEEVVYGESEITTGAASDLQQVARIARNMVTRFGMSDRLGNVALGRQYANIFLGREIAAERDFSEETAALIDEEVRRLVNEAYQRATYLIRENRALLDRIARRLVEAETIDGEELQAIIDNSEVVMLPPEEEPEPLTLPMAVNAGA
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Q2JNP0
Q5U9S1
MBL1_PIG
Mannose-binding lectin A
Sus
MLLFSSLPVLLLCVVTASYSEIKTCEDAQKTCSVITCGIPVTNGTPGRDGRDGPKGEKGEPGPGFRGSQGPPGKMGPPGNIGETGPLGPKGQKGDPGDTSGVEAKLANLEGQIRILKSELDHVKKLQTFSLGKKSRKKLYVTNGEMMPFSKVKTLCAELQATVATPKNAEENKAIQDMAPDVAFLGITDEVTEGQFMYVTGGRMTYSNWKSNEPNDHGSGEDCVILQRDGLWNDISCSSSFLAVCEFPA
Calcium-dependent lectin. Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine on bacteria, including strains of A.suis, H.parasuis and A.pleuropneumoniae, and activates the lectin complement pathway. According to some authors, it only binds mannose .
Q5U9S1
Q8EQM5
LEXA_OCEIH
LexA repressor
Oceanobacillus
MTKLSKRQQMIFDFIKSEVKLKGYPPSVREIAVAVGLASSSTVHGHLERLENKGYIRRDPTKPRAIEIIDLEMEQQLPKDEARYAPVIGKVTAGIPITAVENIEEFVPIPSSSAGPDDNVFVLVIDGESMIEAGILDGDMVIVKQQNTAVNGEIVVAMTEENEATVKRFFKEENRIRLQPENATMEPLFYDNVTILGKVIGLYRNIH
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Q8EQM5
O02073
TBX18_CAEEL
Signal element on autosome protein 1
Caenorhabditis
MDTIININNNNQKYPQSAEEYHKVLCNYFITLQSAMQSTSRPSSSSPPSLPAVSSELLSSSFPTNAPESSSRDLAPKQNQFTINVVLFDEKKKKNPEENLPANGDQLATLRSLMMQINPSSPPSIPATSPQLPLAESENVPESSSTLKDHKFSLNTMLFNVKKNDAVKISLANQEQWAKFHEIGTEMMVFNSGRRLFPLLAYKVSGLDPHKLYCAGVHMIPDSAYKQEYDHDLQQWVNCLNQKKTIFKPTSEILGRIENGFKLMSLGIDMSDVKIFNIAIRKKTPLQIEKSRKPNLDKTIEVLIQYKYLPVIKIYELSNSGMEKKEIAQATFPETSFVTVSIYRNQKIKEMKTLGNKYCRTDRKQIVMEQRGELEQ
Transcriptional regulator involved in developmental processes . Directly binds to the promoter region of the sex-determining factor xol-1 to activate its transcription . Its activation of xol-1 transcription controls sex determination and X chromosome dosage compensation to promote male development . Has a role in the fox-1-sex-1-mediated determination of sexual fate .
O02073
A7MNY7
IHFA_CROS8
Integration host factor subunit alpha
Cronobacter
MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKEN
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
A7MNY7
A1RQB1
ATPG_SHESW
F-ATPase gamma subunit
Shewanella
MAGAKEIKTKIASVKNTQKITSAMEMVAASKMRRAQERMAASRPYAESMRKVIGHVAQGSLEYKHPYLEVREAKRVGYIVVATDRGLCGGLNVNLFKKVLLDLKNWKEQGAEVEFCPIGARSVQFFKSFGGTMPAHASGLGDAPSIADLIGTVRVMLKAYNEGKLDRLFIVFNKFVNTMTQAPVIEQLLPLPKSEEVANKHPWDYIYEPDPKVLLDTLLVRYIESQVYQGVVENIASEQAARMVAMKAATDNAGELINDLQLVYNKARQAAITQELSEIVSGASAV
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.
A1RQB1
B9KHQ6
RUVA_ANAMF
Holliday junction ATP-dependent DNA helicase RuvA
Anaplasma
MIGTLSGTVEEVVCSNRIILCVGGVGYLVQLPGRVLSGCQHGDHVRLYIETYVGRDGVSQLYGFANREEQNCMRMLIKVSGVNYKTAMAILDVLTPEQVFSAIVSEDRAALKVGGVGEKLISRIISELTPQVQKFELNRFAATTRTDSEAVAALLSLGYERTAALGALQKVGVCDSTEDAVRRALLELSK
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.
B9KHQ6
Q6L1I0
RFCS_PICTO
Clamp loader small subunit
Picrophilus
MINIWTEKYRPKRLDDVIGEDENINTLKSFVKNGDLPHLIFAGPAGTGKTSTAIALTIELFGDDWKENFLELNASDERGIDIIRNNIKDFAKIRPSNKLGFKIIFLDEADQLTNEAQAALRRTMEMFYSTTRFIFSCNYSSKIIPPIQSRCVVLRFRPLDKEAMERKLREIAKNEKFDIDDDSLDAIYEISDGDMRKAINVMQAIQSTGEIKPSKIYEISGEINKNEYKNLISLSLNGAFSDAKSLLDKMLVDYGLSGIDIIRGMHSAIRNERIANRQKLEILIALAEFEFRISQGGSDNVQMDALLARISYIGSEIT
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Q6L1I0
Q9ZQV6
NAS4_HORVU
S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 4
Hordeum
MDGQSEEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLAPEAQAMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGVFPYYSNYINLSKLEYELLARYVPGRHRPARVAFIGSGPLPFSSYVLAARHLPDTVFDNYDLCGAANDRATRLFRADKDVGARMSFHTADVADLTDELATYDVVFLAALVGMAAEDKAKVIAHLGAHMADGAALVARHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSNDVHEYGLGSGRGGRYARGTVVPVVSPPCRFGEMVADVTQKREEFANAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZQV6
Q5U4X3
MEI3A_XENLA
Homeobox protein meis3-A
Xenopus
MAQRYDEMLHYPTLDGMPLAGFGDAHTGRALQHHSLSQSAPYGSTGAGHRVPMPPGMGSNDGLKREKDEIYGHPLFPLLALVFEKCELATCSPRDNSGSFPGGDVCSSDSFNEDIAVFAKQVRTEKPLFSSNPELDSLMIQAIQVLRFHLLELEKVHDLCDNFCHRYITCLKGKMPIDLVIDDRDGSSKSDLEDFTGSCTSLSDQNNSWLRDHDETGSAHSGTPGPSSGGLASQSGDNSSEQGDCMDNSVASPSTGDDDDLDRDKKRNKKRGIFPKVATNIMRAWLFQHLSHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRTGQGGAPYSPDGQNMGGYVMDGQQHMGIRPPGFQGIPGDYTAAPSTMPMGFPPAGYTPAIPPHSAGLRHGPSLHSYLPGHPHHASMILPAGASPHHLVSAQSPADALLNGQNIDIHAH
Caudalizing protein which is required to pattern the anterior/posterior (A/P) axis during central nervous system (CNS) formation. Inhibits anterior neural expression and acts as a transcriptional activator to induce posterior neural gene expression. Maintains a proper A/P balance required for hindbrain formation by activating the FGF/MAPK pathway, which modulates the planar cell polarity (PCP) pathway. Interacts with retinoid signaling during hindbrain patterning.
Q5U4X3
C6DKP5
LPLA_PECCP
Lipoate--protein ligase
Pectobacterium
MSSLRLLISDSYDPWFNLAVEECIFRQMPTTQRVLFLWRNAETVVIGRAQNPWKECNTRRMEEDGIKLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKSVSTQIVLDALSALGLKASASGRNDLVVETADGVRKVSGSAYRETKDRGFHHGTLLLNADLNRLADYLNPDIKKLQAKGITSVRSRVANLVELLPSVDHQVICQAVTQAFFDYFGEQCEPEIISPSAYPDLPGFSEQFARQSSWEWNFGQAPDFSHLLDNRFTWGGIELHFDVERGVIIRAQVYTDSLNPAPLEALACALQGTAYRPENMAATCQALITAFPEQQNELQELAEWLEQSLR
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
C6DKP5
Q4QP20
NQRE_HAEI8
NQR-1 subunit E
Haemophilus
MEHYISLFVKAVFIENMALSFFLGMCTFLAVSKKVSTAFGLGIAVTFVLGIAVPVNQLIYANVLKENALIEGVDLSFLNFITFIGVIAGLVQILEMVLDKFMPSLYNALGIFLPLIAVNCAIFGGVSFMVQRDYNFPESIVYGFGSGLGWMLAIVALAGLTEKMKYADIPAGLKGLGITFISVGLMALGFMSFSGIQL
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.
Q4QP20
Q6TLJ0
DRD4_MUSPF
Dopamine D4 receptor
Mustela
MGNRSAADADGLLAGRGPGTGGGAGSPGAAAALVGGVLLIGAVLAGNALVCVSVAAERALQTPTNYFIVSLAAADLLLALLVLPLFVYSEVQGGVWQFSPGLCDALMAMDVMLCTASIFNLCAISADRFVAVAVPLSYNRQSGGGRQLLLIGATWLLSAAVAAPVLCGLNDARGRDPAVCRLEDRDYVVYSSVCSFFLPCPVMLLLYWATFRGLRRWEAARRTKLHGRRPRRPSGPGPPPPEAVETPEAPEAIPTPDATLAEPALPASEERRAKITGRERKAMRVLPVVVGAFLVCWTPFFVVHITGALCPACAVPPRLVSAVTWLGYVNSALNPLIYTVFNAEFRAVFRKALRLCC
Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs. Agonist binding triggers signaling via G proteins that inhibit adenylyl cyclase. Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells.
Q6TLJ0
Q9HCJ1
ANKH_HUMAN
Progressive ankylosis protein homolog
Homo
MVKFPALTHYWPLIRFLVPLGITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSKRDRTKAVLCMVVAGAIAAVFHTLIAYSDLGYYIINKLHHVDESVGSKTRRAFLYLAAFPFMDAMAWTHAGILLKHKYSFLVGCASISDVIAQVVFVAILLHSHLECREPLLIPILSLYMGALVRCTTLCLGYYKNIHDIIPDRSGPELGGDATIRKMLSFWWPLALILATQRISRPIVNLFVSRDLGGSSAATEAVAILTATYPVGHMPYGWLTEIRAVYPAFDKNNPSNKLVSTSNTVTAAHIKKFTFVCMALSLTLCFVMFWTPNVSEKILIDIIGVDFAFAELCVVPLRIFSFFPVPVTVRAHLTGWLMTLKKTFVLAPSSVLRIIVLIASLVVLPYLGVHGATLGVGSLLAGFVGESTMVAIAACYVYRKQKKKMENESATEGEDSAMTDMPPTEEVTDIVEMREENE
Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter.
Q9HCJ1
Q9ZQ46
WAVH1_ARATH
RING-type E3 ubiquitin transferase WAVH1
Arabidopsis
MLNGWRRAFCTSIPKETNQNDVDDDGLVGLRHKSTSRFGFFSTPSTPRSDSGTGTYSLRCRTSTATAVSTTSSLPGTPKLKCKTTTTGETTPRNRSLVSLLTPSSSSISPASFTLLKSKLRFKQSSSNKCGICLQSVKSGQGTAIFTAECSHTFHFPCVTSRAAANHNRLASCPVCGSSLLPEIRNYAKPESQIKPEIKNKSLRVYNDDEALISSPISPAGFHTILESDENEDCEEFTGFSVNTPSPLTAKLLTDRNVDVKLSPESAIVASGKGYETYSVVMKVKSPPFPTARGFARRVPVDLVAVLDVSGRNSGGKLEMLKQTMRIVLSNLREMDRLSIIAFSSSSKRLSPLRRMTANGRRSARRIVDIITVPGSVSGVGIDFSGEGMSVNDALKKAVKVLDDRRQKNPFTAVFVLTDRQAHQVAQLAHSRIPIHTIWLSHAIPEDAFARTINGYLSLSVQDLGLQLGIVSGLGQGEITSVYSLSGRPAWLGTGSIRLGDMYAEEERALLVEIKSPVNNSLTGSRSHKIMTVRSRYVDPTTQELRNPEDRALLIPTPLTVRSSSNPNISRLRNLHVSTRAVAESRRLIERNHYSGAHRLLTSARALLVQHGLSSSDACIRGLDAEIADLNSVKGRHVAASESLESLTPTSAWKAAERLAKVAMVRKHMNRVSDLHGFENARF
E3 ubiquitin-protein ligase involved in the regulation of root growth. Acts as positive regulator of root gravitropism. Possesses E3 protein ligase activity in vitro.
Q9ZQ46
P31997
CEAM8_HUMAN
Non-specific cross-reacting antigen NCA-95
Homo
MGPISAPSCRWRIPWQGLLLTASLFTFWNPPTTAQLTIEAVPSNAAEGKEVLLLVHNLPQDPRGYNWYKGETVDANRRIIGYVISNQQITPGPAYSNRETIYPNASLLMRNVTRNDTGSYTLQVIKLNLMSEEVTGQFSVHPETPKPSISSNNSNPVEDKDAVAFTCEPETQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLLSVTRNDVGPYECEIQNPASANFSDPVTLNVLYGPDAPTISPSDTYYHAGVNLNLSCHAASNPPSQYSWSVNGTFQQYTQKLFIPNITTKNSGSYACHTTNSATGRNRTTVRMITVSDALVQGSSPGLSARATVSIMIGVLARVALI
Cell surface glycoprotein that plays a role in cell adhesion in a calcium-independent manner . Mediates heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 . Heterophilic interaction with CEACAM8 occurs in activated neutrophils .
P31997
A0KU08
TYPH_SHESA
TdRPase
Shewanella
MFLAQEIIRKKRNGLALSTEEIQFFVKGITTNAVSEGQIAALGMAVYFNDMNMDERIALTTAMRDSGTVLNWQSLGLNGPVIDKHSTGGVGDVISLMLGPMAAACGGYVPMISGRGLGHTGGTLDKFDAIPGYQTEPSSELFRKVVKDVGVAIIGQTGDLVPADKRFYSIRDNTATVESISLITASILSKKLACSLDALAMDVKVGSGAFMPTYEASEELARSIAAVANGAGTKTTALLTDMNQVLASCAGNAVEVKEAIDFLTGAYRNPRLYAVTMGLCAEMLLLGGLASDEADARAKLNRVLDNGRAAEIFGKMVSGLGGPVDFVENYSKYLPQSQIIRPVFADTQGYAYSMDTRELGLAVVTLGGGRRKPGDALDYSVGLTQVCALGDKIDASTPIAVIHAQSEEAFAQAEEAVKKAIHIDEVAPEKTPEIYAYIRASDL
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
A0KU08
Q3KLZ0
AROA_CHLTA
5-enolpyruvylshikimate-3-phosphate synthase
Chlamydia
MVSSNQDLLISPSIPYGEIAVPPSKSHSLRAILFASLSKGTSIIENCLFSPDSQAMLTACEKMGAHVRRIGDSLHIQGNPDPHHCHPRYFHMGNSGIALRFLTALSTLSPTPTLITGSHTLKRRPIAPLLSSLKQLGAHIRQKTSSSIPFTIHGPLSPGHVTISGQDSQYASALAITAALAPYPLSFSIENLKERPWFDLTLDWLHSLNISFLRDQDSLTFPGGQSLESFSYSVPGDYSSAAFLASFGLLSSSSKPTILRNLSSQDSQGDKLLFSLLKQLGAHILIGKHHIEMHPSSFSGGEIDMDPFIDALPILAVLCCFAKNPSRLYNALGAKDKESNRIEAIAHELQKMGGSVHPTRDGLYIKPSRLHGAVVDSHNDHRIAMALAVAGVHASSGQTLLCNTQCINKSFPYFVIAAQTLHANVRHYQADFPLRSSFCR
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Q3KLZ0
Q32AJ7
GPH_SHIDS
Phosphoglycolate phosphatase
Shigella
MNKFEDIRGVAFDLDGTLVDSALGLAAAVDMALYALKLPIAGEERVITWIGNGADVLMERALTWARQERATLRKTMGKPPVDDDIPAEEQVRILRKLFDRYYGEVAEEGTFLFPHVADTLGALQAKGLPLGLVTNKPTPFVAPLLEALDIAKYFSVVIGGDDVQNKKPHPDPLLLVAERMGIAPQQMLFVGDSRNDIQAAKAAGCPSVGLTYGYNYGEAIDLSQPDVIYQSINDLLPALGLPHSENQESKND
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Q32AJ7
Q1IFU1
RPOA_PSEE4
Transcriptase subunit alpha
Pseudomonas
MQISVNEFLTPRHIDVQVVSPTRAKITLEPLERGFGHTLGNALRRILLSSMPGCAVVEAEIDGVLHEYSAIEGVQEDVIEILLNLKGLAIKLHGRDEVTLTLSKKGSGVVTAADIQLDHDVEIVNPDHVIANLASNGALNMKLTVARGRGYEPADSRQTDEDESRSIGRLQLDASFSPVRRIAYVVENARVEQRTNLDKLVIDLETNGTLDPEEAIRRAATILQQQLAAFVDLKGDSEPVVVEQEDEIDPILLRPVDDLELTVRSANCLKAENIYYIGDLIQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLDNWPPASLKKDDKATA
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q1IFU1
B7HUR5
AMPA_BACC7
Leucyl aminopeptidase
Bacillus cereus group
MFYVQKELASHEAVIVALFEEEQTSSFVQELDKAFEGQLQVLLEEKELSTKKKAISKVHSLGKTEVKRYYFVGLGKKESYTTETLRSALGKTFKTLQAAKVQDAAILLDSFVTKKLDAIDVAHIAAEVQGLGTYELQTYKSDKKDRVELEKFTAITAEDAQEIEAALTVGYVHGRATNSARTLVNMPPNVLTATKLAEYAVELAEKYDMDYKVLEKEEMEELGMGALLAVNQGSVEPPKMIALIYKGKEEWTDVIGFVGKGITYDTGGYSLKPREGMVGMKGDMGGAAAVLGAMEIIGELRPEQNVIAVIPSTDNVVSGTAFKPDDVITSMSGKTIEVLNTDAEGRLALADGITYAKKLGANYLIDVATLTGGVIVALGNHTTGAMTNNEELFEQVLEASMETDESIWQLPIFDRDKERVRNSKFADLNNSPGREGHAVMAGTFLSEFAEDTPWVHLDIAGTSESSGAHDLGPAGATGAMVRTLATLVERFGEE
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
B7HUR5
Q2YZB8
MNME_STAAB
tRNA modification GTPase MnmE
Staphylococcus
MDLDTITSISTPMGEGAIGIVRLSGPQAVEIADKLYKGKHLLNDVPSHTINYGHIIDPESKEVVEEVMVSVLRAPKTFTREDIIEINCHGGILTINRVLELTMTYGARLAEPGEFTKRAFLNGRIDLSQAEAVMDFVRSKTDRASKVAMNQIEGRLSDLIKKQRQSILEILAQVEVNIDYPEYDDVEDATTEFLLEQSKEIKQEINRLLDTGAQGKIMREGLSTVIVGKPNVGKSSMLNNLIQDNKAIVTEVAGTTRDVLEEYVNVRGVPLRLVDTAGIRETEDIVEKIGVERSRKALSQADLILFVLNNNEALTQEDYTLYEVVKNEDVIVIVNKMDLEQNIDINEVKDMIGDTPLIQTSMLKQEGIDELEIQIRDLFFGGEVQNQDMTYVSNSRHISLLKQARQTIQDAIDAAESGVPMDMVQIDLTRTWEILGEIIGETASDELIDQLFSQFCLGK
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q2YZB8
B9LZ17
GATC_GEODF
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Geotalea
MKINKDEVEKVALLARLELTGEEAEMFTGQMDAILAYVDKLNELNTDGIVPTAHAVPMENAFRADEVRDSIGIDNALANAPKRAESFFRVPKVIE
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
B9LZ17
A4SMX4
PURT_AERS4
Phosphoribosylglycinamide formyltransferase 2
Aeromonas
MFGTATRPSATRALLLGSGELGKEVAIELQRFGIEVIAADRYPNAPAMQVAHKAHVLDMLDGNALRALVTLVKPDLIIPEIEAIATDTLAQLEQEGVKVVPNARATQLTMNREGIRRLAAEELGLPTSPYRFAQSKEEFIAAVEAIGLPCVVKPVMSSSGKGQSVLRDLAKLDESWTYAQEGGRAGRGKVIVEGFVPFEYEITLLTVRAVDGIHFCDPIGHRQEDGDYRESWQPQAMSTLALARSKEVAAKVVGALGGYGLFGVELFIRGDEVWFSEVSPRPHDTGMVTLISQDLSEFALHVRAILGLPIGTITQYGPSASAVVLRDGHSQDIRYQGIGAALALVSGAQLRLFGKPEIAGRRRLGVALARGQQCEEAVEKAKAVAARVEVIC
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.
A4SMX4
Q7MCN7
SYY1_VIBVY
Tyrosyl-tRNA synthetase 1
Vibrio
MNSQLLFDDLAQRGLIAQTTDLEQLIALFRQPQTLYCGFDPTAGSLHIGHLVPLIMLKRFQDAGHQGIALIGGATGMIGDPSFKASERSLNSAETVAAWVNALATQIQQLMTPHLTQPLVMVNNADWMQSIGVIAFFRDIGKHFSVNAMIQRESVKQRLARPDQGISFTEFSYSLLQSYDFAQLNQTHQCALQIGGNDQWGNIVSGIDLTRRLNGTTVHGLTLPLITKSDGTKFGKTEGGAIWLDAAKTSPYMFYQFWLNCDDADVYRFLRYYTFLSVEQIEQIEATDKAQVGKPSAQRILAEEMTRFVHGHAGLESAQRISQALFSGQLNQLNLAELKQLEQDGLPCRQLAHVSDVVTLLLETGLASSKRQAREWLENGAIRINGERWNEQTLAQTFALYDQYYIVQRGKKQFAMVKLAQV
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q7MCN7
Q8LG30
CST11_ARATH
Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 11
Arabidopsis
MSDPKYAYPYPAPGNYPQGPPPPVGVPPQYYPPPPPPPPPPPPPRKVGFLEGLLAALCCCCLVDECCCDPTIICFD
Involved in resistance to abiotic stress.
Q8LG30
B7GYM8
EFG_ACIB3
Elongation factor G
Acinetobacter calcoaceticus/baumannii complex
MARQTPITRYRNIGISAHIDAGKTTTTERILFYTGVSHKIGEVHDGAATMDWMEQEQERGITITSAATTCFWSGMGNQFPQHRINVIDTPGHVDFTIEVERSMRVLDGACMVYCAVGGVQPQSETVWRQANKYKVPRLAFVNKMDRTGANFFRVVEQMKTRLGANPVPIVVPIGAEDTFTGVVDLIEMKAIIWDEASQGMKFEYGEIPADLVDTAQEWRTNMVEAAAEASEELMDKYLEEGDLSKEDIIAGLRARTLASEIQVMLCGSAFKNKGVQRMLDAVIEFLPSPTEVKAIEGILDDKDETKASREASDEAPFSALAFKIMNDKFVGNLTFVRVYSGVLKQGDAVYNPVKSKRERIGRIVQMHANERQDIDEIRAGDIAACVGLKDVTTGDTLCDEKNIITLERMEFPDPVIQLAVEPKTKADQEKMSIALGRLAKEDPSFRVHTDEESGQTIIAGMGELHLDIIVDRMKREFGVEANIGKPMVAYRETIKKTVEQEGKLVRQTGGKGKFGHVYVRLEPLDVEAAGKEYEFAEEVVGGVVPKEFFGAVDKGIQERMKNGVLAGYPVVGVKAVLFDGSYHDVDSDELSFKMAGSYAFRDGFMKADPVLLEPIMKVEVETPEDYMGDIMGDLNRRRGMVQGMDDLPGGTKAIKAEVPLAEMFGYATQMRSMSQGRATYSMEFAKYAETPRNVAEGIIAKFQAGGKKGDDE
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.
B7GYM8
B8DFG3
PCRB_LISMH
Glycerol-1-phosphate heptaprenyltransferase
Listeria
MKHLFKLDPAKNLPMNDLTKLVHSGTDGFIIGGTDNVQIEAVQKLYELLGETDLPIFLEISNESMILPEADHFLIPVVLNTENSKWTHGLHQELIKEMGAFIPWKRVTAEGYVILNKDAKVAHLTEAKTDLTDEDIVAYARLAENIFHLPIFYVEYSGMYGDPEVVRKAGAALSNTKFWYGGGIRSKEQAAEMAKYADTIIVGNIIYEDLEKALETATIFRKKTV
Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales.
B8DFG3
P10129
RS10_MYCCT
30S ribosomal protein S10
Mycoplasma
MAENKMRIKLKGYDHAIVDQSITKIIQAAEGTGAKVRGPIPLPTEKQVITILRAVHKYKDSREQFEMRTHKRLLEILNPTAATMDVLKRVQLPSGVDIEIKL
Involved in the binding of tRNA to the ribosomes.
P10129
Q9VXY7
LSD2_DROME
Lipid storage droplets surface-binding protein 2
Sophophora
MASAEQKHATGNGTTGNGTAMNDVDQPKDAKDLLPHLESLERIIKLPVVNAAWDKSQDVYGKVKGKNRVFEWALTAAEDCVTRAVTTAAPFVTKLDRPIAYVDQTLVKGIDKLEVKAPIIKDTPQEIYNQAKSKVIDVVQPHLERVVKFKAAGQQKAASLKDLAWQKANEVLATQYGSLAVNGVDTTTALAERLLEYYFPKCESDVEEDNDDKQNAVVQNGKSSENDMPVPASEDPVLHTVQTVGRLSNKISRRVYRNVSRQIKQVQKGNINDYLSSLIAALKLHQYINFINSSMGTNVEQSGGSSSDACSPFGTTTSTTTTTTTSSTSNNKPVVALPHVAKSKRAPAVSSQ
Essential for embryogenesis. Required for normal deposition of neutral lipids in the oocyte.
Q9VXY7
Q97DC6
LDH2_CLOAB
L-lactate dehydrogenase 2
Clostridium
MNFVKNKLVVVGAGMVGSAVLNSVLSLNLLSEVVIIDINDNKAKGEALDASHTTSFAYSPNVKVRAGNYEDCADAQIIVITAGPSLKPDDKLDRLVLADTNVKVTDSIMKNICKYTKDAIIIVVTNPVDIATYYCQNNFDYPKNKIIGTGTLLDTARMRKIIGKKYNVDSKNVHGYVLGEHGGSSFTSWSDVNIAGIPFNQLNDIFKDHYKVDKDEVDKEVRDSGIEVLKLKGYTSAGIAMSVSRLVKAMLLNEQSILPVSSTLEGEYGINDVALSIPCIITSNGIEKKLEIPLSKDEVEKLNKSADNLKSIIKGLNTNK
Catalyzes the conversion of lactate to pyruvate.
Q97DC6
B5RFW6
GLMU_SALG2
Glucosamine-1-phosphate N-acetyltransferase
Salmonella
MLNSAMSVVILAAGKGTRMYSDIPKVLHTLAGKPMVQHVIDAATKLGAAQVHLVYGHGGELLKQTLKDDKLNWVLQAEQLGTGHAMQKAAPFFSDDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPSGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADLKRWLSKLTNNNAQGEYYITDIIALAYQEGREIAAVYPARISETDGVNNRLQLSRLERIYQAEQAEKLLLSGVMLRDPARFDLRGTLHCGMDVEIDANVIIEGYVTLGHRVKIGAGCIIKNSVIGDDCEISPYSVVEDAHLEAACTIGPFARLRPGAELLAGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTVIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNVADNELVLSRVPQVHKQGWQRPVKKK
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
B5RFW6
P77579
PTFC1_ECOLI
PTS system fructose-like EIIC component 1
Escherichia
MAIKKRSATVVPGASGAAAAVKNPQASKTSFWGELPQHVMSGISRMVPTLIMGGVILAFSQLIAYSWLKIPAEIGIMDALNSGKFSGFDLSLLKFAWLSQSFGGVLFGFAIPMFAAFVANSIGGKLAFPAGFIGGLMSTQPTQLLNFDPSTMQWATSSPVPSTFIGALIISIVAGYLVKWMNQKIQLPDFLLAFKTTFLLPILSAIFVMLAMYYVITPFGGWINGGIRTVLTAAGEKGALMYAMGIAAATAIDLGGPINKAAGFVAFSFTTDHVLPVTARSIAIVIPPIGLGLATIIDRRLTGKRLFNAQLYPQGKTAMFLAFMGISEGAIPFALESPITAIPSYMVGAIVGSTAAVWLGAVQWFPESAIWAWPLVTNLGVYMAGIALGAVITALMVVFLRLMMFRKGKLLIDSL
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
P77579
Q9Y2E8
SL9A8_HUMAN
Solute carrier family 9 member 8
Homo
MGEKMAEEERFPNTTHEGFNVTLHTTLVVTTKLVLPTPGKPILPVQTGEQAQQEEQSSGMTIFFSLLVLAICIILVHLLIRYRLHFLPESVAVVSLGILMGAVIKIIEFKKLANWKEEEMFRPNMFFLLLLPPIIFESGYSLHKGNFFQNIGSITLFAVFGTAISAFVVGGGIYFLGQADVISKLNMTDSFAFGSLISAVDPVATIAIFNALHVDPVLNMLVFGESILNDAVSIVLTNTAEGLTRKNMSDVSGWQTFLQALDYFLKMFFGSAALGTLTGLISALVLKHIDLRKTPSLEFGMMIIFAYLPYGLAEGISLSGIMAILFSGIVMSHYTHHNLSPVTQILMQQTLRTVAFLCETCVFAFLGLSIFSFPHKFEISFVIWCIVLVLFGRAVNIFPLSYLLNFFRDHKITPKMMFIMWFSGLRGAIPYALSLHLDLEPMEKRQLIGTTTIVIVLFTILLLGGSTMPLIRLMDIEDAKAHRRNKKDVNLSKTEKMGNTVESEHLSELTEEEYEAHYIRRQDLKGFVWLDAKYLNPFFTRRLTQEDLHHGRIQMKTLTNKWYEEVRQGPSGSEDDEQELL
Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.
Q9Y2E8
Q04225
RRB1_YEAST
Ribosome assembly protein RRB1
Saccharomyces
MSKRSIEVNEEQDRVVSAKTESHSVPAIPASEEQDAPKNDLEEQLSDEFDSDGEIIEIDGDDEINDEDDLRKKQEEAETLVQKDQSEGNKEKIQELYLPHMSRPLGPDEVLEADPTVYEMLHNVNMPWPCLTLDVIPDTLGSERRNYPQSILLTTATQSSRKKENELMVLALSNLAKTLLKDDNEGEDDEEDDEDDVDPVIENENIPLRDTTNRLKVSPFAISNQEVLTATMSENGDVYIYNLAPQSKAFSTPGYQIPKSAKRPIHTVKNHGNVEGYGLDWSPLIKTGALLSGDCSGQIYFTQRHTSRWVTDKQPFTVSNNKSIEDIQWSRTESTVFATAGCDGYIRIWDTRSKKHKPAISVKASNTDVNVISWSDKIGYLLASGDDNGTWGVWDLRQFTPSNADAVQPVAQYDFHKGAITSIAFNPLDESIVAVGSEDNTVTLWDLSVEADDEEIKQQAAETKELQEIPPQLLFVHWQKEVKDVKWHKQIPGCLVSTGTDGLNVWKTISV
Involved in regulation of L3 expression and stability and plays a role in early 60S ribosomal subunit assembly. May be required for proper assembly of pre-ribosomal particles during early ribosome biogenesis, presumably by targeting L3 onto the 35S precursor rRNA.
Q04225
B7J1T5
LGT_BORBZ
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Borreliella
MPNYINYPSWLHPEVIQGIPITWYSLSYILIILISYKFIWYQIQSDNVDIKKEDYEIFMFSLVLGAILGGRLASTLVYDKSGIYYSNPWLILLPFDQHWNFTGFRGMAIHGGFLGAIIAPLITINTKLKNTNVQKYFLKLTDYGSIAFSSGYILGRLANFANAELYGRVMKGGIIFPNAEPFDTNIPGVKEFASSVGLEISPHDLLINLPRIPSQLIEGFFEGPVTFLLLWFLFKKIKKYDGFIFGVYVMLYAFFRFFIEYLREPDKELGFIITYKPITSLSEFSFLNISMGQILSLTLMLSGLIWIIVTKKIADKKIKNNTNLAYKN
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
B7J1T5
Q126M3
TRUA_POLSJ
tRNA-uridine isomerase I
unclassified Polaromonas
MRIALGISYSGSAYEGWQSQLSGNTVQDKLESALARFAAQPVRTLCAGRTDAGVHGLMQVVHFDTVLHRDMGSWVRGTNAFLPSDIAVQWAREVPDTFHCRGSAIARRYAYVVLESPVRPSVEAGRVGWVYRPLDGAAMRQAITHLVGEHDFSSFRAAQCQAKSPVKTINRIEISERAGTGSKYWHFEFEANAFLHHMIRNIMGCLVAIGQGSHEPGWLLDVMAARSRDAAAPTFSPNGLYFLGPVYEDHYGLPNRTAAYDWLP
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q126M3
O94640
SIR2_SCHPO
Silent information regulator 2
Schizosaccharomyces
MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHYFSDGDSESSEDDLAQPGIMKPDITFFGEALPDSFFNKVGSGELEETDLLICIGTSLKVAPVSELISVIPPTTPQIYISRTPVRHTQFDVNFLSPYCDWVIVEICKRAGWLNELQALCDLPECHSGSKTRAFETDLDIKFEEPSTYHITSTTNGSC
Involved in silencing within the mating-type region, at the telomeres, and according to PubMed:12867036 also within centromeric DNA regions. Required for the localization of swi6 to the telomeres, silent mating type region, and according to PubMed:12867036 to the centromeric DNA regions. According to PubMed:15545655 not required for the localization of swi6 to centromeric foci. Deacetylates histone H3 on 'Lys-9' and 'Lys-16' of histone H4. This has a direct role in heterochromatin assembly.
O94640
Q58D56
DRG2_BOVIN
Translation factor GTPase DRG2
Bos
MGILEKISEIEKEIARTQKNKATEYHLGLLKAKLAKYRAQLLEPSKSSSSKGEGFDVMKSGDARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVVIMMLDATKGEVQRSLLEKELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPDSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQRPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK
Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation.
Q58D56
Q2IPT7
SYY_ANADE
Tyrosyl-tRNA synthetase
Anaeromyxobacter
MQNLLEALVPRSLVHDQTPGLQARLAQGPITGYVGFDPTADSLHVGHLLAVMSLAWLQRCGGTPIIVVGGGTGMVGDPSGKRSERPVLSVEEIDRNVAAIRAQLERFVSFEGQNAARVRNNADWLRSIGLMEFLRDVGKHFTVNYMLAKDSVKGRMESGISFTEFSYQLIQAYDFWHLFHAERCELQMGGSDQWGNITAGAELVSRKDGASVHGLTFPLLTTASGTKFGKTEGGAVWLDPARTSPYKFFQFWLNTDDRDVERLLKFFTFLSLDEIAALLAEQARDPGKRPAQRRLAEDVTARVHGPDVTRSVIEASRILFGGTDLRAAGVDVLDVLAGEIPSATVTGDELAALTVADLLVKVGLAASKGEVRRGVAGRGFSLNGAVLESGDAKVAAGELLAGGYALLQKGKRNYALVKVR
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q2IPT7
Q0J7J7
CAF2M_ORYSJ
CRS2-associated factor 2, mitochondrial
Oryza sativa
MLLPRDLLLLPWRRATAAGEAIARRLNHHRAPPFSDPDDDPPFTRLAERPPRAPSKKKKKEEEDQGGRIRPPEPASSDLPFDFRYSYSETDPAWRPIGFREPTRFSPFGPGRLDRPWDGVAAAAARGEGAGAAATSREEVLGEPLAEEEVAQLVERYRHSDCSRQINLGKGGVTHNMIDDIHNHWKRAEAVRIKCLGVPTLDMDNICFHLEDKTGGKVIYRNINILILYRGRNYDPKQRPQIPLMLWKPLAPIYPRLVQNVADGLTFEKTKELRNTGLNSSPLMKLTRNGVYVNVVDRVREAFKTVEVVRLDCSHVGSSDCKKIGVKLRDLVPCVPLLFKDEQIILWRGKVKQENSVSLQFSPEPS
May be involved in the splicing of group IIB introns in mitochondria.
Q0J7J7
A0A024B3G5
FRA16_FRAAN
Class 10 plant pathogenesis-related protein Fra a 1.06
Fragaria
MGVFTYETEFTSVIPPPRLFKAFILDADNLIPKIAPQAVKCAEIVEGDGGVGTIKKITFGEGSQFGSVTHKIDGIDKENFVYSYSLVEGDALSDKIEKISYETKLVASSDGGSVIKSTSNYHTKGDVEIKEEHVKAGKEKASHLFKLVEDYLLANPNEYC
Possesses ribonuclease activity in vitro.
A0A024B3G5
Q2PP75
LEC8_MEDTR
Agglutinin LEC8
Medicago
MANSNPKLLVTQNPFSVFLLTFLLLITNVKSDSFSFNFPKFDTDTKSIIIDGDANTTNGVLQLTKKDQLGNPSPHSFGLSFFLGAIHLSDKQSGKVADFTTEFSFVVNPKGSQLHGDGFTFFIASLDYEFPEKSSDGGFLGLFDKESAFNTSQNSIVAVEFDSFRNEWDPQIAGNSPHIGIDINTIRSSATALWPIDRVPEGSIGKAHISYNPASKKLTALVTYLNGPVIEETAVSYTVDFAAILPEYVLVGFSGATGELAETHDILSWSFTSNL
May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Q2PP75
P90755
ENPP2_CAEEL
Ectonucleotide pyrophosphatase/phosphodiesterase C27A7.3
Caenorhabditis
MSNRVVDVNSKKTGTSWKKKLMKIVIWSLAMLSFIAGLVLLGLVAAATISGSKNLPTAEYKWAGCENLGKCQIDGFSTPPLVILSFDGFAKEYLERRIVKSLELIAECGVKADRVYPSFPSKTFPNHYTMVTGLYPESHGITDNYVFDPNLYPELLAMRKHEAKEFYQAEPIWSAYKRLTGNRVHCLFWVGCYYNITGYMPDVSPDYNQELPLKERIDTLIGWLKLPETERPALITAYLHEPDQAGHMQKNVNQELEEVNNYIDILMKALHDENLLECVNLVIVSDHGMQALNNSIEVETIVNMDGLVLSKGVVARIHLNETDRSIDEVAGEIRCKIDGVKVNTINDIPLRKHYSKSKRVGDIIIEGKPGTSFYKSETNLGDHGYDYHNENMHTVMFARGPSFLQNVTVPSFQNVQYMNLWLYLLGLEGTVDNNGTIGFFDSILKNPPIRENKWDSMEECLNFGSAEVLQCDKAEGHDLKKLSLHLENCKEHQNLPIYSKNNCFQSYCENSLIIHKNRQDVRKGVIESLTFSFSRNQSVFENSFSFVNTKYSIECPKLDTKDNFFTAGSEAISKLANAQYKFPSSFMKSELISSLLSLKDETIKFVDIWVPLSIKTDEYLKHYGKLFVLSGLAVDRNLDGIADDEESKEPTHFYRILITCTGNWLSTNPPLCKKYSDTKALAFVFPILNKKTTMDCMDSDAILLDYTSTIEDVENIASFQFQIGALSHQQNVYLRRNITTSLW
Probable phosphodiesterase.
P90755
C4KZP5
RL4_EXISA
50S ribosomal protein L4
unclassified Exiguobacterium
MPKVALLNQTGSQVGEIELAEAIFGIEPNESVLYDAIVMQQASRRQGTHDTKGRSEVRGGGRKPWKQKGTGRARQGSIRSPQWVGGGTVFGPTPRSYSYKLPKKVRRLALLSALSSKVQNNEIIVLEGLAFDAPKTKDMAAVLNSLSVERKALVVTADYNETIALAARNIPGVTVIDAAGVNVLDLVANDKVIFTKDAVAKVEEVLA
Forms part of the polypeptide exit tunnel.
C4KZP5
P33238
MX_ANAPL
Interferon-inducible Mx protein
Anas
MTTQRNTDKPHSKPEDQWNMYNRNPKFKATAKRCSPNLMKDGFQSLSSPVCIEASAVPLPPDSDDEIYFPVPEQTTKESQHEQKVSMKLHEEQDVQAAEHTLYNQYEEKIRPCIDLIDSLRALGIEKDLSLPAIAVIGDQSSGKSSILEALSGVSLPRGNGIVTRCPLELKLKKIPTSQEWKGKISYRNISTDLQHASEVENAIRNAQDVVAGTKGNISGELISLEICSPYVPDLTLIDLPGIARVAMRNQPQDIGEQIKKLIKKIISSKETINLVVVPCNVDIATTEALKMAQEVDPKGERTLGILTKPDLVDIGTEEYIISIVQNEVIPLRKGYMVVKCRGQRDIHNKLTLASAIHQERQFFETHKCFSILLDQNKATIPHLAMKLTNELVAHIIKTLPTIESQIREVLQKSVQELQKYRRGTPTIETEKLAFLTDLIKLFNQDVSRVICGEEHLFGNEIRLFAKLRKEFQTWGLLLLENAAKVQKSIPSKMWKYEDQYRGREFPGFINYRTFEDIIKEQILDLEEPAIVILNNVIRLVEEKFLELTNKHFANFKNLNRAAQTKIDVIRNTQAMNAENHIRNQFKMERIVYCQDNIYLDDLRSTKAEILGKDSGKEISFASVSDKNAIFIQEMISHTKAYFTGASKRLSNQIPLIILSAVLHDFGDNLQSSMLHLLQEREKLNSLLQENSEAAKMRNYLSGRVNRLSKAYQCLKDFSCL
Does not show activity against influenza virus or VSV.
P33238
Q4UWA1
RBFA_XANC8
Ribosome-binding factor A
Xanthomonas
MTMPTKSFHRTDRVSAQVRRDLGTIVHAAVRDHGLPSVSVSDVEISRDLAHAKVFVTALQQERSAEAVKGLKEIAGQLRTQLARAMKLRHVPELHFHYDDSVDRGERIDNLLRDLDDIGPEAAPDAQDAEPR
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.
Q4UWA1
Q04449
PHR_ALKPO
Photoreactivating enzyme
Alkalihalophilus
MGNSDSLKAVWFRRDFRLHDHTALKHAIEAIEKHGGKWLAFFYLDPKTASVEPVHHDYFFQTVMQFKQMLKTNGGDLYIITGTIEGALSKLLQAFPEIDAVYANDDRVGDGRLRDEAAEHFLAKQSIPFYTFEDAYLTEPDQVLKKDGTPYKVFTPYYKAWAKERKRTPAVIKRDVLLGSVHKGTAPDREAETLFNNLIKKCSYDWSAIGEEHAIKRLQMFTKKRLSGYKANRDFPSITGTSRLSPYIKTGAVSSRSIYYHILNAEADSYSAETFLKELAWRDFYRMVHFYEPDCKDREIMEGYRELNWSHDQDDLTSWKRGETGFPIVDAGMRQLLNEGWMHNRLRMITASFLTKDLLIDWRLGERYFERMLIDYDPSSNIGGWQWAASVGTDAVPYFRIFNPVTQSKRFDENGTYIRTYIPELNHVPDHYIHEPWKMSEEEQVKYKCRLDEDYPLPIVDHSKQRKKALSFFKGDDEE
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Q04449
Q9LKP7
CHSY_DIAMO
Naringenin-chalcone synthase
Dianthus
MASIEEIRQAQRADGPATILAIGTATPPNAIYQADYPDYYFRVTKSEHMTELKEKFRRMCDKSMIKKRYMYLTEEILKENPNLCEYMGSSLDTRQDMVVSEVPRLGKEAAVKAIKEWGQPKSKITHVIMCTTSGVDMPGADYQLTKLLGLRPSVRRFMLYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAICFRGPTEAALDSMVGQALFGDGAGALIVGSDPDLSIERPLFQMAWAGQTLLPDSEGAIDGHLREVGLTFHLLKDVPGIISKNITNALEEAFSPIGVSDWNNLFWIAHPGGPAILDQVEAKLGLKEEKLAATRNVLSDFGNMSSACVLFILDEMRKKSLRDGATTTGEGLDWGVLFGFGPGLTVETVVLHSVPLNC
The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Q9LKP7
B2TR25
GLGC_CLOBB
ADP-glucose synthase
Clostridium
MGNTEIVAMILAGGQGSRLGVLTKKLAKPAVPFGGKYRIIDFPLSNCANSGIYTVGVLTQYKPLELNAHIGIGLPWDLDRKDGGVSILPPYQEEKGGNWYKGTANAIYQNIEFVDRYDPEYVLILSGDHIYKMNYTKMLEFHKEKNADATIGVIEVPVNEASRFGIMNTRDDMSIYEFEEKPKIPKSNLASMGIYIFNWKTLKKYLRNDEANKGSSNDFGKDIIPSMLNDGGKMVAYPFEGYWKDVGTIESLWQANMDLLKSDNKLNLHDQDWRIYSTNPVRPAQYIGENAKVTNSLIVEGCTVNGTVQNSVLFQGVQVGKNTIIKDSVIMTNAKIGDNVIIEKAIIGNDAVIRKDCVIGTGDEIEIVAAKEEVKMGSIMKNNKAV
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
B2TR25
Q8UEM1
MNTH_AGRFC
Divalent metal cation transporter MntH
Agrobacterium tumefaciens complex
MFFMRMICNCINSISMKAQKMDKPVFGWRRNGDDLSLSDVHSSIRIKPDASTFRRAMAFFGPGYLVAVGYMDPGNWATSLAGGSKFGYTLLAVALVSNIMAIVLQSLCARLAIASGRDLAQACRDAYPKPVAMVLWLLAEIAIIATDIAEVIGTAIGLNLIFGIPLELGVLITALDVFLILYLQKLGFRWVEALVITLLGVIAVCFAIQLALADPDWGQVILGFAPTTEIVTNPDMLYLALGILGATVMPHNLYLHSGIVQTREIGPTIAEKREALKFATLDSTIALMFALLINASILILAAATFNKTGQTNVAELGEAHSLLAPLLGLAIAPTLFGVALLCCGINSTVTATLAGQIVMEGFLKMRLAPWLRRLITRAIAIVPAAGVTIFYGDSGTGQLLILTQVVLSLQLSFAVFPLVMFTSDKAKMGELRSPLWLSAIAWLIAVVIAALNVKLLMDFMG
H(+)-stimulated, divalent metal cation uptake system.
Q8UEM1