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AlphaFoldDB
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B3L145
DRE2_PLAKH
Fe-S cluster assembly protein DRE2 homolog
Plasmodium (Plasmodium)
MMNFADTLVILNEDAPCELLRKKYAQMLVPTVSVSNFKKNKQYKTYNNVFLYTYREYDFLWDLDDNVLHKIQRCLNKSGVLKLVLYISNTDGGDNKTHDEIAKRLKRECLYSGFINISNEISMAENGIIINVTAENPDFLSNEDDDEGNSSDGEAYQNAEDNKKVVNRVCANCTCGKKTNGVKLDKVTINEKEVQYLTENAVSSCGNCYLGDAFRCASCPYKGLPAFQPGENVKLNLDNEPN
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
B3L145
Q06164
MMS22_YEAST
Synthetically lethal with MCM10 protein 2
Saccharomyces
MDVDEPNPIVISDSEATDEEISIIYEPEFNENYLWAEENVQEASRSQKIVTERLSLDSTAGESCTPSVVTDTQVTTGLRWSLRKRKAIQKMPYSLERIKHRQLLEGYDISSFDSISNQLTLPKNASTVIHSNDILLTKRTGKPLDEQKDVTIDSIKPENSSVQSQRYDSDEEIPKKRHRTFKDLDQDIVFQSGDSTEDEQDLASTNLQNTQNDEVIFRGRVLNVRTGYRGVLPRVAWEKSLQKQQSSKVTKRKTQLLNHKGVAKRKMNRSAHIEDEEQNLLNDLIAPDDELDIEENAPPDIYLGNLPEDREANEKELKELQEYYESKYSEDAQSAGTSGFNLNEEYRNEPVYELEYDGPGSCISHVSYKDQPIIYLNSRHSDSGFSEQYNISAEDNQSVISLDAAEEHNDGIIDKMLVKPKRIKATNDANFLNTKSKRVRRYKYKYRNSCLAPSTKAIKVGKRSAHKSHLAANNPVSFVSKKNHVIDDYFFEELESQSLEQDDSSSLKPQKKRRKKKAPIYSSFSADLESRRKPVFNTVVEVPTNRYAFTKPNVRNRDSINHDMEFEEEDSNQELGPIMVVLDSILLKKPFEPPNFFKIQLSDKSFLLSKLNPADIATSLQKIFRVIIDKGITDTELVHFNESLIAFLVHLDMPELFDLIGEFHREFRSKVNSLRKKAKPIHFFQIAACQLMFLEISRYNKISAAAKFDMDVKLLDHIVSFFKLLSVCYDSVMKNPMQYLYTSYYILSAVVDVIHKKEALWDLFQKHPFSPHISLLLVNIFPTKVCRWQVLRLDSEFQPLSSAFRFINYCIETCNWNVTNSLILSLDRIFKRRRFSDFEEESDLSQNNKIIYPPTNQLTSRLMFNRYLHLLTLCELSSSDTQRVIPMGDISMNDSLSVLKNRLNLLIVLATRFDLNLEKRFQELTRPLYSKEYLNLHTQNTVRTITTLIMQASLSFLEISRIKNHPFSGKFIASLFDKLVLQQPSISGVTENFLKEFTNLVSKMKRKSVSMLKFLYPSLVAMSQENIFESSFFLLLQVYLKSLDVLGPTWVQNYLFQFIKSKAQENERWIECYCQIGKFLVDSGIFTWWTFFTYNGLDAALHFQLAFHSLIIDFCDTDSFELLKKPLYSIASDLLLISKDDAFYHFLSNLLKRAHIIVADLKPVSDENELLRLAYIFSKALKKNAYQDLLAVFLSLAKKHYDEGDISRNFLAKYLEFLNKNCLTELRNNQLFISLRRELGISSDEDEKCAFWDSFNEAGDILSKAAFVETGIVQACCTGNEIDGYLDNLSTLFTSTMLESPFAFFSDLVIAHIFENRPFFDVNIKNFLLSHFIDLFNKVLKMKFEQVSPDEFAELCKVYRALCIECATDDTFNSNSDLIAAKDAFLVSVLRIADGFWEHDKLLQLRMLDSNMNIPNQIPHTTLQSSLSAIVIKIIESNIGKIEASEPFKTFKNT
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.
Q06164
Q8DMN0
RL4_THEVB
50S ribosomal protein L4
Thermosynechococcus
MVACVVKDWQGADSGEATLDLATAKPETASHIVHRALVRQLANARQGTVSTKTRAEVRGGGRKPWRQKGTGRARAGSIRSPLWRGGGVIFGPKPRDYSQKMNRKERRLALRTALMSRVEDLIVVQDFADHLPRPKTKELVTALQRWGIEPEQKVLLLAADITETVALSARNVPTLKLLRADQLNVFDLLYADRIVATTGAIAKIQEVYGD
Forms part of the polypeptide exit tunnel.
Q8DMN0
P38203
LSM2_YEAST
Small nuclear ribonucleoprotein D homolog SNP3
Saccharomyces
MLFFSFFKTLVDQEVVVELKNDIEIKGTLQSVDQFLNLKLDNISCTDEKKYPHLGSVRNIFIRGSTVRYVYLNKNMVDTNLLQDATRREVMTERK
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
P38203
A7ENU3
CLU_SCLS1
Protein TIF31 homolog
Sclerotinia
MAATNEVIPTSENPSDVSGSSQKLATEETALANGVDHEEEDSGEAGGEVFQLTVVLPREPHKIPIIVSSQEAIHDVRQSIIELPGTFQYSCFHLEHKGERINDFVQISEVPGLTADSEIHLVEDPYTEKEARIHIVRVRELIGAAGDRTDTLNGIISGVSLLDSVTSAESTQNGTSTAPSHPMVGFDFQASGTLSTLLPKAQEPGPKTIKSISVSPWNPPPYHLRQKGHLLYLQVTTNEGEQFQITSHVSGFYVNKSSTGKFDPSPKSAPKAHSAHSLLALLGDLSPSFEDSFKRLQEYNNTKEPLATFQITNATPSNPWIVPSASAPLVAHQADITRTQENYLIAGIENSETLRDWNEEFQSTRELPKETVQDRVFRERLTSKLFADYNDAAARGAILVARGEIAPLNPTEGKDAQIFVYNNVFFSFGADGVGTFASEGGDEAARAAVGKDVMGVRMVNQLDIDGLFTPGTVVVDYLGKRIVGQSIVPGIFKQRDPGENQIDYGAVDGKDIVASDEKFVSVFEKLSKALKVKKHAVWDKDGKRHDLEGSIETKGLLGTDGRKYVLDLYRVTPLDITWMEEVGTALDSPKEADVASESAYPHRMTVIRPELVEAYWKVKMREWVNGELERKRQAQKTIEPTAEEKEPGAVAEASEASKSDEPTENGELAKKADESDKDAEPSKPAADQERIDIGDFKFALNPDAFSGQQPQTDEEKAEFAEDEQQVRLVCEFLRKTVLPELVNDLKEGDVGFPMDGQSLSRLLHKRGINIRYLGQVATLADGKRLESLRILAVQEMVSRAFKHVAGNYLRYLPIPLTSSCIAHLLNCLLGTDLNATPKPDVDEAMAALYPDADLKFKEVSPESLKRDIEAQILRRFRYTLDSTWTAAIKHLQLLREVSLKLGIQLEMKPYHFTKQSQTEAAAAPPTTNGEATKDAAPTGKSTNGKKKKKNAREGSPASITSVNASSPVTFNPDDILNTVPVIKEASPRSSLAEEALEAGRISLLQDQKKLGQELLLESLSLHEQIYGILHPEVARVYNSLSMLYYQLDEKEAAMELARKAVIVSERTLGVDNAETLLNYLNLGLIAHASGETKLALTYIKHALDLWKVVYGPNHPDSITTINNAAVMLQHLKEYHDSRTWFEASLKICEEVYGKHSINAATLLFQLAQALALDQDSKSAVNRMRESYNIFLTELGAEDKNTKEAEKWLEQLTQNAVSIAKHAKDVQARRNRAGIRVSPRVTLGQTQLQPQVGQTAEAAAGRDSRSSRGLDSRSIDELLKFIEGSDQANKNKKRPGRSNPKRRGGAAAAAGK
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
A7ENU3
Q8WP22
ABEC4_MACFA
Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4
Macaca
MEPTYEEYLANHGTIVKPYYWLSFSLDCSNCPYHIRTGEEARVSLTEFCQIFGFPYGTTYPQTKHLTFYELKTSSGSLVQKGHASSCTGNYIHPESMLFEMNGYLDSAIYNNDSIRHIILYCNNSPCNEANHCCISKVYNFLITYPGITLSIYFSQLYHTEMDFPASAWNREALRSLASLWPRVVLSPISGGIWHSVLHSFVSGVSGSHVFQPILTGRALTDRYNAYEINAITGVKPFFTDVLLHTKRNPNTKAQMALESYPLNNAFPGQSFQMTSGIPPDLRAPVVFVLLPLRDLPPMHMGQDPNKPRNIIRHLNMPQMSFQETKDLERLPTRRSVETVEITERFASSKQAEEKTKKKKGKK
Putative C to U editing enzyme whose physiological substrate is not yet known.
Q8WP22
Q95L05
FKBP5_CHLAE
Rotamase
Chlorocebus
MTTDEGAKNSGESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFNSSHDRNEPFVFSLGKSQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSVPKIPSNATLFFEIELLDFKGEDLLEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGERMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMRAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSSAVEEEKAEGHV
Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.
Q95L05
A0T0M2
PSBI_PHATC
PSII 4.8 kDa protein
Phaeodactylum
MLTLKILVYTTIIFFVSLFIFGLLSSDPSRNPNRKDFE
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
A0T0M2
Q6Z2X6
CAS_ORYSJ
Cycloartenol synthase
Oryza sativa
MWRLRVAEGGGDPWLRTKNGHVGRQVWEFDPAAGDPDELAAVEAARRGFAARRHELKHSSDLLMRMQFAKANPLKLDIPAIKLEEHEAVTGEAVLSSLKRAIARYSTFQAHDGHWPGDYGGPMFLMPGLIITLYVSGALNTALSSEHQKEIRRYLYNHQNEDGGWGLHIEGHSTMFGSALTYVSLRLLGEGPDSGDGAMEKGRKWILDHGGATYITSWGKFWLSVLGVFDWSGNNPVPPEIWLLPYFLPIHPGRMWCHCRMVYLPMCYIYGKRFVGPVTPIILELRKELYEVPYNEVDWDKARNLCAKEDLYYPHPFVQDVLWATLHKFVEPAMLRWPGNKLREKALDTVMQHIHYEDENTRYICIGPVNKVLNMLACWIEDPNSEAFKLHIPRVHDYLWIAEDGMKMQGYNGSQLWDTAFTVQAIVATGLIEEFGPTLKLAHGYIKKTQVIDDCPGDLSQWYRHISKGAWPFSTADHGWPISDCTAEGLKAALLLSKISPDIVGEAVEVNRLYDSVNCLMSYMNDNGGFATYELTRSYAWLELINPAETFGDIVIDYPYVECTSAAIQALTAFKKLYPGHRKSEIDNCISKAASFIEGIQKSDGSWYGSWAVCFTYGTWFGVKGLVAAGRTFKNSPAIRKACDFLLSKELPSGGWGESYLSSQDQVYTNLEGKRPHAVNTGWAMLALIDAGQAERDPIPLHRAAKVLINLQSEDGEFPQQEIIGVFNKNCMISYSEYRNIFPIWALGEYRRRVLAADK
Converts oxidosqualene ((3S)-2,3-epoxy-2,3-dihydrosqualene) to cycloartenol.
Q6Z2X6
Q5R513
MPPA_PONAB
Inactive zinc metalloprotease alpha
Pongo
MAAVVLAATRLLRGSGSWGCSRLRFGPPAYRRFSSGGAYPNIPLSSPLPGVPKPVFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTVGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVGLLADVVLQPRLTDEEVEMTRMTVQFELEDLNLRPDPEPLLTEMIHEAAYRENTVGLHRFCPTENIAKINREVLHSYLRNYYTPDRMVLAGVGVEHEHLVDCARKYLLGIQPAWGSAEAVDIDRSVAQYTGGIAKRERDMSNVSLGPTPIPELTHIMVGLESCSFLEEDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMSGTVDAVELERAKTQLTSMLMMNLESRPVIFEDVGRQVLATRSRKLPHELCTLIRNVKPEDVKRVASKMLRGKPAVAALGDLTDLPTYEHIQTALSSKDGRLPRTYRLFR
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Q5R513
Q9KTU1
CITD_VIBCH
Citrate lyase gamma chain
Vibrio
MKIAHPAFAGTLESSDLQVRIEPNNDGGIELVLDSTVEQQFGHAIRQVVLHTLDAMQVRDALVTIEDKGALDCVIRARVQAAVMRACDVQNIEWSQLS
Covalent carrier of the coenzyme of citrate lyase.
Q9KTU1
B4U465
MSRA_STREM
Peptide-methionine (S)-S-oxide reductase
Streptococcus
MERAIFAGGCFWCMVQPFEEQAGILSVRSGYTGGHVPNPSYEQVCSKTTGHTEAVEIIFDPSLISYSDLVELYWAQTDPTDAFGQFEDRGDNYRPVIYYTDERQREIAERSKQSLQASGRFDQPIVTSIEPAEPFYLAEDYHQGFYQKNPQRYAQSSAIRHQFLEEHWQ
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
B4U465
Q98PZ3
RL24_MYCPU
50S ribosomal protein L24
Mycoplasmopsis
MKTKLRKNDEVIVIAGSYKGTKGTILKVLPKQQRVQVKGVNVVTKHVKPSQSNSEGSIQNFEAPIHISNVAYVHKSGPKDKSGIASKISYEKRKDKKVRIARKTGKVI
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q98PZ3
P39842
BLTR_BACSU
Multidrug-efflux transporter 2 regulator
Bacillus
MSEDVKKYFTTGEFSKLCRVKKQTLFHYDEIGLFSPEIKKENGYRYYSYHQFETFQVISLFKELGVPLKEIKCLIKGKTPDKILHVLKEKSIEIDKKINELKQLQTILQTKVTLTEQALETDFSSISFEYLNEETFMLSRKTLNLPERKYVAAISELIHEVQQYELDEGYPIGGIFAREQILEKDFYNYSYFYIKVKDGAENINYHVRPKGLYAVGYEIGGNTEEAYRRIIEFIERNGMQIGENAYEEYMLDEMVVDGYENTYAKILLQVKEV
Activates transcription of the blt gene in response to structurally dissimilar drugs.
P39842
Q73IU2
AMPA_WOLPM
Leucyl aminopeptidase
unclassified Wolbachia
MYSLQLFATEIPAMKITISKISPDFKTIVMGLFEDNETVNDGGVLQGKQVIDNIKQFSDFNGSFGEFFSTALPEEKNVIVVGLGKKDEWNENKELNIGGKIYCELSRLKIKKAAVLIEGSAANVAYGAFLRSFKFDKYKTKKDEKITEVEEITVLVKDEQLSNAERSFEHLRQEGESIFLARSFITEPPNILYPESYADHIKKELTKLGLEIEVLDKKQMEEKKMGALLGVAQGSSKEPKLVVIKWNGASKEQKPIAFVGKGITFDTGGVSLKPSRGMESMKYDMAGSATVVGVMHALAGRKAKVNAIGVVALAENAVGGNAQRPSDVVTSMSGQTIEVLNTDAEGRLILADALWYTQDRFSPKFMIDLATLTGAIVVALGNNEYAGLFSNNDELANRLIDAGNEVNEKLWRFPMNETYDKIIDSPIADVQNIAPAGSGGDSIMAAQFLQRFVNETCWAHLDIAGTAWHEKGTDICPRGAVGFGVRLLNKLVEKYYEAND
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q73IU2
Q9P6K3
CUB1_SCHPO
CUB1 family protein C30C2.08
Schizosaccharomyces
MMSYEPAEPVPVEEQPILEKLIGIRQRLAVLKRDRTRFIEKNEVFHLKDELVEQMNLLDSRRSTNSTRTIVDSQLEDCLHLLSLFYLAIGRNNDLPAFFVQLGTVRRLLEYNLEGACYTQNDLKPLKERLERIRAAIVEGSKKEDASPVVVKYLNNKLAVCDRNYSEAQHNISKISPELIGIQTRLVSIHRQIDGFAVRPTSDPGFIDRTMEQLKEIEEMKDSNGMFCDADHVPLQGQELCNGILEECFSFLEDAKTKEGLSDEMKSSPKLQQIYHRLDELLNKLKHLTLTHRWTLRETDLYVYRASLAEIDSMRIDGQFLDEQGNAPAGQRILLYLLRRCYAYIYQLLSSSEPVSEELMAVHNQLRTVKRCLLEVQRSGGICSERDLYPYQMKLASLENLRVNGKFLASDHSVPEGQELVNSLLTQCHQLIEELRDEKHQHDIEEREGSENTDGNL
Involved in bleomycin tolerance with links to DNA repair and/or proteasome function.
Q9P6K3
Q9UU95
MU128_SCHPO
Meiotically up-regulated gene 128 protein
Schizosaccharomyces
MEYANLHYVKESSNLERSSTYKSSKIQDEAKQLLYDYVYIKEKLLTTSSNSLTHYQWYLIYKHTCRCFQQVVRIVYWFLGNQVIRENFSIKKRKPHNHIPQLLEQCTCIAESFEGIYTKKQILYFKCYGTFKTWKKIANFPHL
Has a role in meiosis.
Q9UU95
Q9ZJE3
UBIX_HELPJ
Flavin prenyltransferase UbiX
Helicobacter
MKLVLGISGASGIPLALRFLEKLPKEIEIFVVASKNAHVVALEESNINLKNAMKDLRPSATFFNEQDIHASIASGSYGIHKMAIIPASMDMVAKIAHGFGGDLISRSASVMLKEKRPLLIAPREMPLSAIMLENLLKLAHSNAIIAPPMMTYYTQSKTLEAMQDFLVGKWFDSLGIENDLYPRWGMN
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Q9ZJE3
Q9XSE4
CASB_TRIVU
Beta-casein
Trichosurus
MKLLILTCLVVLAVARPMVEKISESEEHVTDVPENEHRLEINRYLRPEYEMMNLYYQPFYWSEEMRNLKMTSLPKDRRMAVLKSVVSDDMLPPLQHKSLSLPKPKVLPLSHRQILPPHTLRMVPLSHKLFTIPKREMLPISERERLPAHERENLLAHEREILLAPQREMSLIPEREILLAAERVVLPEQEREIRPDNEREVLAVHKREILPASEKEKVLPLFQERVLPLHRREIVPPYQRDTIARREILPVDQRELMPEVVAVDLYPFFQPVANFYYPAELNEKN
Important role in determination of the surface properties of the casein micelles.
Q9XSE4
A1WMX6
PLSX_VEREI
Phosphate-acyl-ACP acyltransferase
Verminephrobacter
MITLAVDCMGGDHGPRVTLAACRAFLDHHPDARLLLVGQTDSLRSFTHARAALVAATEVVAMDDSVEVALRKKKDSSMRVAIQQVKDGAASAAVSAGNTGALMAIARYLLKTLDGIDRPAIATQLPNARGGATTVLDLGANVDCSAEHLLQFAVMGSALVSALQEGGEPTVGLLNIGQEAIKGSEIIKRAGELLRSAAQCGDLNFHGNVEGDDIFKGSVDIVVCDGFVGNVALKASEGLAAMIIGALKIEFSRHVFAKMAAIVAYPVLQALMKRMDYRRYNGAALLGLRGLVFKSHGSADAMAFEQALNRAYDAARNNLLDRVRARIAHAAPLLAPADAQPKPDIAATTHR
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
A1WMX6
Q9YHT2
SDHB_CHICK
Iron-sulfur subunit of complex II
Gallus
MAAAVVGVSLRRGVPARFLRAGLRPVRGLEAVHGICRGAQTAAAATSRIKKFSIYRWDPDKPGDKPRMQTYEVDLNKCGPMVLDALIKIKNELDSTLTFRRSCREGICGSCAMNIAGGNTLACTKKIDPDLSKTTKIYPLPHMYVVKDLVPDLSNFYAQYKSIEPYLKKKDESKQGKEQYLQSIEDRQKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDYTEERLAQLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKAAAA
Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q9YHT2
Q9I452
THTM_PSEAE
Rhodanese-like protein
Pseudomonas
MSSAQLLTAQQLAARLSEPDLLVLDCRFALEDPSYGARVYQENHIPGAHFADLERDLSAPVRKGVTGRHPLPDPAELALKLQAWGLRQDSQVVLYDDGPGAFAARAWWLLHWLGKRDGVYLLDGGLAAWKAAGLALTNGESSLRPGDFQGQPDASLLIDAATLQAQLGQPGLALLDARAQPRFRGEVEPIDPVAGHIPGAQCAAFTDNLGSDGRFLPPEQLHQRFSALLRGRPVDELVAYCGSGVTACHNLFALSLAGFPLPRLYAGSWSEWITDPRRPVATGD
Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a thiol-containing acceptor to form an intramolecular disulfide releasing hydrogen sulfide and pyruvate.
Q9I452
A1TNA3
PPNP_ACIAC
Xanthosine phosphorylase
Acidovorax
MTTEKIDGVSVTARANVYFDGKCVSHGITFPDGTKKSVGVILPATLTFNTGAPEIMECVGGACEYKLDGTDAWVKSGEGDKFSVPGNSKFEIRVTEAYHYICHFG
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
A1TNA3
Q48PK6
OPGH_PSE14
Glucans biosynthesis glucosyltransferase H
Pseudomonas
MSNSLPVPVSLNEYLAHLPMSDEQRAELAGCKTFAELHERLSAQPVNDPAEAAQASVGRRLTLTTADQLEDAEMLGVDASGRLCLKATPPIRRTKVVPEPWRTNILVRGWRRLTGKTNPPKPEHDDLPRDLPKARWRTVGSIRRYILLILMLGQTIVAGWYMKGILPYQGWSLVSLDEITRQTFVQTALQVMPYALQTSILLLFGILFCWVSAGFWTALMGFLELLTGRDKYRISGASAGNEPIEKGARTALVMPICNEDVPRVFAGLRATFESVAATGDLDRFDFFVLSDTNETDIAVAEQQAWLDVCRETKGFGKIFYRRRRRRVKRKSGNLDDFCRRWGGEYRYMVVLDADSVMSGECLTSLVRLMEATPDAGIIQTAPRASGMDTLYARMQQFATRVYGPLFTAGLHFWQLGESHYWGHNAIIRMKPFIEHCALAPLPGKGAFAGAILSHDFVEAALMRRAGWGVWIAYDLPGSYEELPPNLLDELKRDRRWCHGNLMNFRLFLVKGMHPVHRAVFLTGVMSYLSAPLWFFFLVLSTALLAVNTLMEPTYFLEPRQLYPLWPQWHPEKAVALFSTTIVLLFLPKLLSVILIWAKGAKGFGGKFKVTVSMLLEMLFSVLLAPVRMLFHTRFVLAAFLGWAATWNSPQRDDDSTPWIEAVKRHGPQTLLGACWALLVFWLNPSFLWWLAPIVVSLMLSIPVSVISSRTNLGVKARDEKFFLIPEEFEPPQELISTDQYTYENRWHALKQGFIRAVVDPRQNALACALATSRHRQAQPIEVVRMERVDQALKVGPAKLGNQERLMLLSDPVALGRLHERVWSEGHEEWLAAWRASIEADPHAPLLPLQPVGKASEPVPV
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Q48PK6
Q8PQ42
COQ7_XANAC
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
Xanthomonas
MTQISPTRLHSPLDRLLVEAQRALDTVFGNPPAERPNPAADTPDVVLDPEQRLHAAGLMRINHVGEVCAQGLYFGQAAVARDAHTRHHLLEAAQEETDHLAWCADRLHELDSRPSLFNPVWYAGSYALGALAGLRGDDWSLGFVVETERQVEAHLDEHLETLPQSDQRSRAILRVMKIDEARHADQAEQAGARPLPAPIPSAMALASKLMKTVAYRL
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
Q8PQ42
A4IZQ6
HTPG_FRATW
High temperature protein G
Francisella
MSEKKYTFETEVDKLLHLVIHSLYSNREIFLRELVSNSSDAIEKLRYESISNAALNEDDTDYAIRIDFDKDAKTITVSDNGIGMTEEEVIENLGTIAKSGTKKFLESLTGDKSKDNELIGQFGVGFYSSFIVADKVTVRTRKAGQDKSQATKWVSDAQNGFTVETITKEKRGTEVILHIKKEHLDLLEYHVLKGLVNKYSDCINTPIQMKKVEYDKDGKQTVKDEYETVNNTKAIWLRSKDEVTDEEYQEFYKYISHDFADALMWIHNKVEGNLEYNSLLYIPQNKPFDFWNRDKDYGLSLYVRRVFIMENKELLPPYLRFVKGVIDSADLPLNVSREILQHNKVIDKIKKAITTKILSELKKLASKDKEKYQKFWDSFGQVLKEGVSDDYSNKEKIAGLLRFATTQSGDSKQTVSLADYISRMKEGQDTIYYITSDSYKAAANNPQLEAFKKKGIEVILMTDRIDEWMMSTLTEFDGKHMKSIIKGDIDLDKFETPENKEKFEKEAKDFEKVLKEIKEVLKDKVEDVRLSKRLTDSPSCVVVNDYGMSLHMQKMMEEAGQSFMPGMGMKPILELNAEHNLVQKLKNEADTEIFADLSELLLLQAMFVEGAKIEDPMAFVKLVNKYIR
Molecular chaperone. Has ATPase activity.
A4IZQ6
A0A0N7KJT8
APL25_ORYSJ
Protein SHATTERING ABORTION 1
Oryza sativa
MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGAGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPHPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT
Transcription factor . Involved in spikelet transition and development (Probable) . Prevents lemma and palea elongation as well as grain growth . Required for seed shattering through specifying abscission zone (AZ) development .
A0A0N7KJT8
Q9SKX1
IBH1_ARATH
bHLH transcription factor bHLH158
Arabidopsis
MASADKLINTDVPEKDVFAFHFLQSLSNLRKQNPFDTPDQKNYRVRKIKKAAYVSMARAAGGSSRLWSRALLRRADKDDNKIVRFSRRKWKISSKRRRSNQRAPVVEEAAERLRNLVPGGGGMETSKLMEETAHYIKCLSMQVKVMQCLVDGLSPK
Atypical and probable non DNA-binding bHLH transcription factor that acts as transcriptional repressor that negatively regulates cell and organ elongation in response to gibberellin (GA) and brassinosteroid (BR) signaling. Is able to form heterodimer with BHLH49, thus inhibiting DNA binding of BHLH49, which is a transcriptional activator that regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif. Binds and inhibits HBI1, a positive regulator of cell elongation that directly binds to the promoters and activated the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening enzymes. The ability of IBH1 to inhibit BHLH49 and HBI1 is counteracted by binding to the antagonist bHLH transcription factor PRE1, restoring the transcriptional activity of BHLH49 and HBI1 and resulting in induction of cell elongation. Functions redundantly with IBL1/BHLH159 in a regulation node known as the incoherent feed-forward loop (FFL) .
Q9SKX1
A8IHV3
SLT3_CHLRE
SAC1-like transporter 3
Chlamydomonas
MAAIGWPGIVAIISVAISFIIMAADWVGPDITFTILLSWLTAFDGKIITVAKAAAGYGNTGLLTVIFLYWVAEGVTQTGGLELVMNYVLGRSRSVHWALVRSMFPVMVLSAFLNNTPCVTFMIPILMSWARRCGVPPKKLLIPLSYAAVLGGTCTSIGTSTNLVIVGMQDTRYNKQNKEDEAKFGMFDIAPYGVPYALMGFVFIILTQRFLLPGNSSRYAKDLLIAVRVLPSSPVVKKKLKDSGLRTQTGFSLAGLWRGGAMTRQVDPDTVLEANDILYCAGELDVVEFVGEEFGLGLVTAETERALTDGQAVGDSEATAFHDTGASPYKKLVQVTMTKTADLVGRTVREVSWQGRFGLIPVAIQRGNGREDGRLNDVVLAAGDVLILDTTPHFDEARDDFKINFEKLRFVKDGAAKEFVIGVKVKKNSEVVNKTVTAAGLRGVPGLFVLSVDRADGSSVDASDYLYKIQPGDTLWLAADVGAVGFLSKFPGLELVQQEQVDKTGTSILYRHLVQAAVSHKGPLVGKTVRDVRFRTLYNAAIVAVHREGVRVPLKVQDIVLQGGDVLLISCHTKWAEEHRMDKAFVLVQAVPDSSPPKRGRMAIGVLLVVGMVLTQIVGGLKEKEYIHLWPAAVLTAALMLLTGCMNADQARKAIMWDVYLTIAAAFGVSAALENTGVAGKVANAIISIGKSIGGDGPALIAIYVATAVMSELLTNNAAGAIMYPIAAIAGDQLKIPAVDISVAIMLGASAGFINPFSYQTNLMVYAAGNYSVREFATIGAPFQIWLMVVASFILCYMKQWKQVWIATWSITAFIVFVPALLTLLPHTVQNRMEAFFDRIAEAINPRAALQRRRSARAQSFGGKAMSVGSTESRTDGSSTPDVALTFIEMPKMGVR
Na(+)/sulfate cotransporter with a probable low-affinity for sulfate.
A8IHV3
A4TKK8
HIS6_YERPP
ImGP synthase subunit HisF
Yersinia
MLAKRIIPCLDVKDGQVVKGVQFRNHEIIGDIVPLAQRYAQEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSVEDASQILTFGADKISINSPALADPTLITRLADRYGVQCIVVGIDTWYDTESDSYQVYQFTGDEKRTKATTWQTEDWVKEVQLRGAGEIVLNMMNQDGVRNGYDLRQLQQMRAICHVPLIASGGAGTPDHFLEAFRDADVDGALAASVFHKKIINIGELKKYLSEQGVEIRVC
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
A4TKK8
A7MB47
CNOT9_BOVIN
Cell differentiation protein RQCD1 homolog
Bos
MHSLATAAPVPTALAQVDREKIYQWINELSSPETRENALLELSKKRESVPDLAPMLWHSFGTIAALLQEIVNIYPSINPPTLTAHQSNRVCNALALLQCVASHPETRSAFLAAHIPLFLYPFLHTVSKTRPFEYLRLTSLGVIGALVKTDEQEVINFLLTTEIIPLCLRIMESGSELSKTVATFILQKILLDDTGLAYICQTYERFSHVAMILGKMVLQLSKEPSARLLKHVVRCYLRLSDNPRAREALRQCLPDQLKDTTFAQVLKDDTTTKRWLAQLVKNLQEGQVTDPRGIPLPPQ
Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors. May play a role in cell differentiation.
A7MB47
A1JIS8
RS6_YERE8
30S ribosomal protein S6
Yersinia
MRHYEIVFMVHPDQSEQVPGMIERYSATITNAAGTIHRLEDWGRRQLAYPINKLHKAHYVLLNVEAPQEAIDELETNFRFNDAVIRSMVMRVKHAVTEASPMVKAKDERRERHDFASEANDDSEAGDSEE
Binds together with S18 to 16S ribosomal RNA.
A1JIS8
O02351
SNMP1_ANTPO
null
Antheraea
MLLPKPLKYAAIGGGVFVFGILIGWVIFPVILKSQIKKEMALSKKTDLRQMWEKVPFALDFKVYIFNYTNVDEIQKGAKPIVKEIGPYYFEEWKEKVEVEDHEENDTITYKRLDVFHFRPDLSGPGLTGEEVIIMPHLFILAMVATINREKPSMLNVVEKSINGIFDNPKDVFLRVKAMDIMFRGIIINCDRTEFAPKAACTKMKKDAVTGVIYEPNNQFRFSLFGTRNNTVNPDVVTVKRGIKNIMDVGQVVALNGKPQIDIWRDHCNEFQGTDGTVFPPFLTYKDRLQSFSFDLCRSFKAWFQKKTSYKGIKTNRYIANVGDFANDPELQCFCDTPDECLPKGIMDIRKCLKVPMYVSLPHFLETDTSVTNQVKGLTPDPNEHGIIADFEPLSGTLMDAKQRMQYNIKLLRTDKIAIFKDLPDSIVPCFWVHEGILLNKTFVKMLKHQLFIPKRIVGVIRWWMVSFGLIAVLAGVMYHFKDNIMGWAAKGESTTAKVNPEDGSNEQRGVSVIGQDREPPKVTM
Plays an olfactory role that is not restricted to pheromone sensitivity. May be involved in the odor detection properties of the olfactory receptor neurons (ORNs) rather than their differentiation and growth.
O02351
Q0I455
SSTT_HAES1
Na(+)/serine-threonine symporter
Histophilus
MNKSYLYSFFFHGSLVKRISVGLLLGLLLALIAPSLQGVLGFNLAEKAGFLGKIFVRSLRAVAPILVFLLVISAIANKQLGTKSNMKSIVVLYLLGTFLAALTSVLFSFALPTEIALKTQEGSLSPPNEVSEVLSTLVLNVVDNPINALFNANFIGILFWAIGLGIALRYASDTTKNVMNDFSEAVSRIVHFIISFAPIGVFGLVAETLTDKGLGALLDYMQLLVVLIGSMLFTAFVINPILVFWKIRRNPYPLVWTCVRESGLTAFLTRSSAANIPVNMELSKRLKLDEETYSVSIPLGANINMAGAAITITVLTLAAVHTLGIEVSFPTAVLLSVVASICACGASGVAGGSLLLIPLACSLFGIPNDIAAQVIGVGFVIGVLQDSTETALNSSTDVIFTAAVCWSEENKNS
Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Q0I455
Q8NNC6
SYG_CORGL
Glycyl-tRNA synthetase
Corynebacterium
MAQQSIIDTVVNLCKRRGLVYPCGEIYGGTRSAWDYGPLGVELKENIKRQWWRSMVTSRPDVVGVDTSVILPRQVWVTSGHVEVFTDPLVESLNTHKRYRADHLLEQYEEKHGHPPVNGLADINDPETGQPGNWTEPKAFSGLLKTFLGPVDDEEGLHYLRPETAQGIFVNFKNVMNTSRMKPPFGIANIGKSFRNEITPGNFIFRTREFEQMEMEFFVKPGEDEEWHQHWIDTRLQWYINLGIKPENLRLYEHPQEKLSHYSKRTVDIEYAFNFANTKWGELEGIANRTDYDLRVHSEGSGEDLSFFDQETNERWIPFVIEPAAGLGRAMMMFLMDAYHEDEAPNSKGGVDKRVVLKLDRRLAPVKVAVLPLSKKDTLTPLAEKLAAELREFWNVDYDTSGAIGRRYRRQDEIGTPFCVTVDFDSLEDNAVTVRERDTMEQVRVPLDELQGYLAQRLIGC
Catalyzes the attachment of glycine to tRNA(Gly).
Q8NNC6
B7KIT8
GPMA_GLOC7
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Gloeothece citriformis
MSKLILIRHGQSLWNAANKFTGWVDIPLSRRGRAEAMIAASKLQEQGYRIDVCFTSLLIRAMETAIIALTEYEQLCGGKTPIFKHDADDLDWHGWDKYDGDPKEELPIFPSQALDERYYGDLQGLNKAQTAQKYGSEQVHEWRRSYFTRPPGGESLEDTQKRVIPYFENRILTHIAHGDTVMVAAHGNSLRAMIMRLENLQPEDVPNLELATGIPLIYEVDQQAKVSNKIVLH
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
B7KIT8
B7HVW2
SYM_BACC7
Methionyl-tRNA synthetase
Bacillus cereus group
MSIFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKDIADQYHEEFERCFRSLGFTYDCYTRTDSEHHHETVQNVFLRLLEEGHIYKKTVEQAYCETCTQFLPDRYVEGICPHCHEAARGDQCDACSAILDPLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKTAVENVKQTGTWRDNAIQLTERYVKEGLQDRAVSRDLPIGVPIPVEGYEDKKIYVWIEAVTGYYSASKHWAEKTGEDDQEFWDSEAKTYYVHGKDNIPFHSVIWPAVLLGIGEGAIPRHIVSNEYLTVEKRKLSTSKNWAVWVPDILERYDPDSIRYFLTVNAPENRDTDFSWREFLYSHNSELLGAYGNFVNRTLKFIEKYYGGIVPKGSIDVELKDKVEGLYKHVGEAIEQTKFKVALESIFDAVRFANKYFDEKQPWKQREDNPVSCEETIYNCVYLIANFVNLLEPFLPFSSERIRNTLSIVNRNWEPQHTLPSRIDSVQPLFERIDVKQIEHEVEKLYGAVK
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
B7HVW2
Q6G078
PANB_BARQU
Ketopantoate hydroxymethyltransferase
Bartonella
MSIHQTIKRITAAEIRSRKGQEPIVSLTAYQAYSARIADPYCDFLLVGDSVGMVVHGFETTLPVSLDMMILHGQAVMRGAKKALVVIDMPFGSYEESPEQAFSNASRILAETGCGAVKLEGGVYIAETIDFLCKRGIPVMGHIGLTPQAVNRFGGFKTQGRNESNWQQIEADAAAIEEAGAFAVVVEGVVEPLAVRLTEMLSIPTIGIGASSQCDGQILVMEDMLGYGTWVPKFVRRYGALEQEMEKAIKSYADDVKSRAFPSEAEIYKLKQKSG
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Q6G078
Q94WW9
CYB_CTEMU
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Ctenomys
MTNTRKSHPLIKIMNHSFIDLPTPSNISAWWNFGSLLGVCLGLQILTGLFLAMHYTADTTTAFSSVTHICRDVNYGWLIRYMHANGASMFFIFLYFHIGRGIYYGSYTFMDTWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGPTLVEWIWGGFSVDKATLTRFFAFHFILPFIITAMVMIHLLFLHETGSNNPSGMNSDSDKIPFHPYYTIKDILGVLFMMITLMSLVMFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVFSILILMLFPILHSSKQRSMSFRPLSQCLMWVLVANLLILTWIGGQPVEHPFITIGQLASVTYFFTILILMPSTALMENKLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q94WW9
Q9NDH7
GLY2_CAEEL
N-acetylglucosaminyltransferase gly-2
Caenorhabditis
MRRRHRCVALLFIFSAFITPLGFFYYTISNESKRYSEESEKNYGYQTLEFTESPEEISVDFDKYSQSECSRFPSNVEIEYPECLNKMKWIKNGWKTHHCYIENHIDGSECSFRYYLSQVENYCPPMEHHGKRKGLAKISPSIRRLLPIFESIPHYMKTRINRLWKKWKEGAHEVMQKYPKSMIERRKLNVLVFIGFLANEQKLNMAKKSDHGGPLGELLQWSDLLATLSVIGHHLEVSTNKNTLRNIVWKYMSRGPCQYVNNFRQQLDIIFTDIMGFNILRQHHRQFLLSNRCRIRLLDSFGTHAEFTTKTYFVQNKKSLSGPFSQRNPWGGHGLDLRQHWTFYPHSDDNTFLGFVVDTEGIDKKNNQMIPSALVYGKEQYMWRDAEKPIDVLKRIVTVHSTVADLDLKDSNISSIFKKVQNHGFLNSEEISQLLDNITIFFGLGFPLEGPAPLEAMAHGAVFINAKFKEPKSRLNYKFLAEKPTLRKWTSQNPYMEKIGEPHVITVDIFNELELEEAIKRAISLKPKHFVPFEFTPAGMLHRVALLLEKQELCDKIAYSKRWPPIDQMKIFRTLNADDSCETICHSKQLLCEPSYFPIINSSPLLRRENLCSSTTSDSSPFAPFNCTIQQSAFLFSCASSPPISFEINRLCPCRDYIPEQHAICKKCL
Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides.
Q9NDH7
Q84HC6
NCSB_STRCZ
Naphthoic acid synthase
Streptomyces
MSCRYAPDLDSPDKFWDFLVNGRSTVGDMPDKRWEPYASGSPQATAAMRDTVRRGAFLDDIEGFDAEFFGISPREADFLDPQQRFMLELAWEALADAGVPPLTLRNTDTGVYAAANSNDYGRRLLEDIPRTGAYAVNGTTLYGIANRVSYFLDLHGPSMAVDTACAGALTALHLARQSLLTGETPLAIVGGLNIMSTPSLNVALNDAGAMSPDGRSKAFDEDADGYGRGEGAGVLVLKRLSDARRDNDPVHAVIRGSGVFQDGRSDGMMAPDGDAQEHMLRQAYHRAGVDPATVDYVEAHGTGTPTGDREEITALAKVFGAGRSPHAPCLIGSVKPNVGHVEGGSGITGVIKTVLALRNELIPPTLHDRPRTDVDWDAWGVRLVGQVQEWPSCGRPRRAGVSSYGVGGTISHVILEESPVPAATSSADASTGVRTPALFPLSAASEAGLRALAGEAAGWVASRPDTPLPSVGHTLTQRRSHLAQRAAVVADSAEQLVDRLREVAEGRNGPGIVSARTSAGRADDAVWVFSGHGAQWSGMGRRLLASEPVFAATLDALDEVFREELGWTPREAVTEGGPWTAAHVQALTFAVQIGLADVWRSKGLRPGAVIGHSVGEIAAAVVAGSLDRDEAARFACRRAAALQRLDGRGAMVMVGLPFEEAALRLGDRRDVEAAISAGPHSTVLSGDRSAVLRVAEEWQASEVWTRTVDSDIAFHSVHVDEVTGDIESAARLLTPRPPTVPLYTTALSDPRSRAPRDSGYWAANLRKPVRFTEAVRAAAEDGHRLFLEVSSHPVVAHSVSETLLDLGIEDAAVAGTLRRDTDEVESLLENLAELHCHGVAVDWARHHTDGELVGLPAAVWQHRPYWIFPETTADAGLGRGHDPASHSLLGGRMTVSGSPTRQVWQTRLDMDSRPYPQSHGLVGVEVTPAASIINTFAAAVEEDGPSALTDIVLRTPLAVEPPRVVQVVREGRSLSLATRVAEDADADGSEWITHTTAAVTPGVRPAGGRLDTEAIRSRLPEGSLTRADEMFERMGVEGYAFPWDLEELRHDDHEQLAVLQIEPSPAQRATSWAHVIDGALTISAMVVSPGDATVLWMSRSIDQVTWSGEPPARLTVHSTRSLRSPHDTVDVRVADERGDVVCEVVGLRFAAVEHIGAAVLPSELVHEIVWRPWDPEDHEGAEDAPVEQVILVGDPEATVPLAEQLESAGMTCVQVGDSPETGLRPDLFARPGAVVVAPALAGSDTAPEEEAERVSWLLVRTVQRVAEIRADVTGDAPAQRVWCVTSDVRRARDERSVAHGPLWGLARIVAGDHPELWGGAVDIGPSADGIGARLVALLDGAAGTEDVISLTGEGAEVARLSRIDRSADGTPLQCSPSGTVLITGGLGALGLEVARWLVDRGARRLVLVSRRALPNRTEWPAVTDAETRRRIDGVLALEALGVTVRVLALDITDVDQVSAALAPEALGLPPVRGVVHAAGVVNNALVDKVDLEGLREVLAPKVRGAMVLHRLFPPGDLDFFVLFSSCGQFARLSGQASYAAANSFLDTLASHRNAGEHTETVSLGWTAWRGLGMSSNIDTTMFEANSRGLEAVSATEAFGAWSFGDRFQSDYQAILRVVPTPVHTPRLPVFRDLPVSGETDGPTGDQLFTTTLEGLPEQEARERITADVREQVAGVLNFDPSEVEVKRPLVELGVDSVMTVALRVRLQRRYGLELPPTILWAKPTVAALSEHVCDSLRWDGEEHGDLAAPTAAA
Iterative type I polyketide synthase that catalyzes the synthesis of the naphthoic acid moiety during the biosynthesis of the neocarzinostatin (NCS) chromophore.
Q84HC6
Q5F9L0
RLME_NEIG1
rRNA (uridine-2'-O-)-methyltransferase
Neisseria
MAVRSKSSKAWLHEHINDQYVHMAQKDGYRARAAYKLLEINEKDKIIKPGTVLADLGSAPGSWSQVAAKLTGTSGAVFALDILPMEAIGGVSFIQGDFRENDVLAQFETLLDNRPLDLVICDMAPNMSGNAVSDQARSFYLCELALDFASQHLKTGGSFLVKVFQGAGYQEYMAAMREIFGTVQTRKPEASRNRSSEIYLLGKNKR
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Q5F9L0
P50976
PTLCB_STRMU
Lactose-specific phosphotransferase enzyme IIB component
Streptococcus
MNTLIAQIEKGKPFFEKISRNIYLRAIRDGFISAMPVILFSSIFLLIAYVPNIFGFTWPKGIENMLMTPYNYTMGIIGFLVAGTTAKSLTDSMNRQLEKTNQINFISTMLASMAGFLIMAADPAKEGGFLSAFMGTKGLLTAFIAAFITVNVYKICVKNNVTIRMPEEVPPNISQVFKDIFPFAFSIIILYAIQLAIKAVIGVNVAQSIGTLLAPLFSAADGYLGITIIFGAYALFWFVGIHGPSIVEPAIAAITYSNVELNAHLIHAGQHADKVITSGTQMFIVTMGGTGATLVVPFMFMWLCKSKRNKAIGRASVVPTFFGVNEPILFGAPIVLNPVFFIPFILAPIVNVWIFKFFVDTLGMNSFFANLPWTTPGPIGIVLGTGFAVLSFVLAALLILVDTVIYYPFVKVYDEQILAEEAEGKSSSDALKEKVAANFDTKKADAILEGAESKEEPATHAITEETNVLVLCAGGGTSGLLANALNKAAEEYGAPVKAAAGSYGAHREILDQYQLVILAPQVASNYEDMKAETDKLGIKLAKTEGAQYIGLTRDGKGALAFVEEQFKD
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport.
P50976
Q16877
F264_HUMAN
Fructose-2,6-bisphosphatase
Homo
MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSEEGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ
Synthesis and degradation of fructose 2,6-bisphosphate.
Q16877
Q67N40
LIPM_SYMTH
Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase
Symbiobacterium
METNWRLLDTGHRPGPENMAIDEAIAMAHGRGEVPPTLRFYGWNPPAVSIGYFQSMLGEVDLDAVRAGGYGYVRRPTGGRLIFHHMELTYSVVIREELLPGGVIETYREISRGLLAGMAELGVPAALSGGDRDPRRADPDGFHTACFDTASAYELQVGGRKVAGSAQTRRDGVILQHGSILLDIDVPLLFRLMRLPEGIPAERLMARFRAKSTTLAEALGRPVSWAEARDAFAAGFARALGLTLTPGQLTEREEKEAQTLVEAKYGCDNWNMRK
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation.
Q67N40
P48946
RS18_SYNY3
30S ribosomal protein S18
unclassified Synechocystis
MNYYRKRLSPLPPNQPIDYKDTELLRKFITERGKILPRRITGLTAKQQRDLTTAVKRSRLVALLPFVNKEI
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.
P48946
A5GE10
ISPH_GEOUR
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Geotalea
MKVILAKQAGFCFGVKRATQMAFEAADKGGKTYTLGPIIHSPQVVQKLEEMGVKALKDISGMDDGTIIIRSHGVASGELEEAVRKELEIVDATCPFVKKAQEHVESLSQAGYDVVVVGDADHPEVQGIVSYASGKVYVVGSGDEAAKLPKMAKIGVVAQTTQSFENLKNVVDACLTKGGEIRVFHTICDATAVRQEEAKELASQVDCMIVIGGYNSANTKRLAEVCTELQPRTYHIEMAQQLNPRWFEGVGKVGVTAGASTPKWLIDEVLEQIEKINKDKNH
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
A5GE10
Q5ATH1
APDC_EMENI
Aspyridones biosynthesis protein C
Aspergillus subgen. Nidulantes
MIPPKQQTALKITPEGRIAAVSSPLPSLQDNELLVCVKSIALNPFDAKSAEMSPTIGATLGCDFAGKIVATGSNANDFNFSIGDRVCGCVFGNNPNRLDNGAFAEYVAVPADLLLRIPEHMDYNEAATLGVGLATVGMSLYHCLRLPMKPEQAGKSPSGYAAITTCSPHNFNLVKSLGATAAFDYHSPTCGRQIRDFSSGNLWYALDCITDTRSMAVCYEAIGPSGGRYLSLDPFPIRGHTRRSVKPNWVLSVTMYNQPIPWKRPFKRDACPQDLEFAKSWFQIAQRMIDAGEIRPHTSDVKAGGWNGIPGGLELLQKGEVSGRKLVYEVASH
Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of aspyridones . The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA . The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit . The growing polyketide chain then elongates into a tetraketide . The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation . Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules . The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide . The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product . Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC . ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps . A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A . The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (Probable).
Q5ATH1
A5EWA3
CSRA_DICNV
Carbon storage regulator
Dichelobacter
MLILTRRVGETIIIDDQIKVTVLAVKGNQVRLGVQAPDEIAIHREEIYHRLMNGVGDDAEMEKK
A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
A5EWA3
Q9AEM9
XFP_BIFAS
Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
Bifidobacterium
MTNPVIGTPWQKLDRPVSEEAIEGMDKYWRVANYMSIGQIYLRSNPLMKEPFTRDDVKHRLVGHWGTTPGLNFLLAHINRLIADHQQNTVFIMGPGHGGPAGTAQSYIDGTYTEYYPNITKDEAGLQKFFRQFSYPGGIPSHFAPETPGSIHEGGELGYALSHAYGAIMDNPSLFVPCIIGDGEAETGPLATGWQSNKLVNPRTDGIVLPILHLNGYKIANPTILARISDEELHDFFRGMGYHPYEFVAGFDNEDHLSIHRRFAELFETIFDEICDIKAAAQTDDMTRPFYPMLIFRTPKGWTCPKFIDGKKTEGSWRAHQVPLASARDTEAHFEVLKGWMESYKPEELFNADGSIKEDVTAFMPKGELRIGANPNANGGRIREDLKLPELDQYEITGVKEYGHGWGQVEAPRSLGAYCRDIIKNNPDSFRVFGPDETASNRLNATYEVTKKQWDNGYLSALVDENMAVTGQVVEQLSEHQCEGFLEAYLLTGRHGIWSSYESFVHVIDSMLNQHAKWLEATVREIPWRKPISSVNLLVSSHVWRQDHNGFSHQDPGVTSVLLNKTFNNDHVTNIYFATDANMLLAIAEKCFKSTNKINAIFAGKQPAATWITLDEVRAELEAGAAEWKWASNAKSNDEVQVVLAAAGDVPTQEIMAASDALNKMGIKFKVVNVVDLIKLQSSKENDEAMSDEDFADLFTADKPVLFAYHSYAQDVRGLIYDRPNHDNFTVVGYKEQGSTTTPFDMVRVNDMDRYALQAKALELIDADKYADKINELNEFRKTAFQFAVDNGYDIPEFTDWVYPDVKVDETSMLSATAATAGDNE
Phosphoketolase using both fructose 6-phosphate and xylulose 5-phosphate as substrate.
Q9AEM9
A5D1P3
ADDA_PELTS
ATP-dependent helicase/nuclease AddA
Pelotomaculum
MEQTGPDVPERVGAMSGGWTAEQLEAISARGGDVLVAASAGTGKTAVLAERIIRRITDPIKPVDVDRLLVVTFTSAAAAEMRERIRLALAREISRRPESGHLQRQAALLGRACISTVHSFCLDLLRQHFYRIGLDPSFRVADETEAALIQTGALEEVFERRYAAEDNIFAALVDCYGGRHDDALLQELVLDAYKFARSTPWPEDWLDGLAEGFNLPGGASFDRTPWSAVLKQAAEIELAGARADLEAALRIAREPGGPQAYLANLEQEHDLVCRLLQSCRTNAPWAELYSYFKEVVFSPLKQCRKEDADLKLAGQARNFRESAKKKVMQVKSRYFSLPPEDLCADLRRMAPLIKELAGLVREFDATYRKAKAARGVVDFNDLEHYCLQVLAEKGPSGAVPSQVAHELQEKFVEVLVDEYQDINAVQETILQMVSRKGEGQSNLFMVGDVKQSIYRFRLAEPGLFLKKYASFSAGTGGGQGRRLALTANFRSRQGVVSAVNFIFKQIMTPAVGEMAYGSDAMLVYGADYPPVPEGQGNYEEAVELHLVERGPAGKDGGGDDPAGEEADGGVEAVEEIEEELEAGQKEARLVARRIKELLGGSPGGEHALEIYDRELKKYRPLTYRDVAVLLRATAGYANSFVEEFRREGIPAYAELSTGYFESTEVETVISLLKVIDNPRQDIPLAGVLRSPAVGLKAGDLARIRLASPRGDFYDAVVAASLAGQGELSERLADFLKKLEEWRTIARQGTLADLIWAVYRDTGYYDFTGCLPGGGQRQANLRALHDRARQFETTAFRGLFLFLRFIERLREGGRDFGAARLLSEKENVVRIMSIHKSKGLEFPVVFVAGLGRNFNFRNLNKAVLFHKDLGLGPQLVDAEARVTRPTAAKLALKHRLKMEALAEEMRILYVAMTRAQEKLILVGSARNLPGCARRWCGPAGTAGWALPDGFLAGAGTCLDWLMAALARHRDGAAIRELAACAEEPPAEVAADRSRWRVFFSDSRGRSAEMAEEPVLLAKVRRMEPLEPAGPLAGMIKARLEWSYPAIAVLGRPAKAAVTELKRRFDQLAAGEEQYGEGHFESFRLTAGRPLFMQEKRGLTAAEAGEALHLVMQHLDLTGSLDITAVRSQIEDMVWRELLTPEQAAAVPAEKIAAFFAGPLGRRLLAGFQVLRELPFTMAVQAAEIYPELVPYPGEAVLVQGVIDCLVDEGDGYLLLDYKTGKRPLGRPEEAARRYCGQLNIYARAVESILGRKVKEKYLYLFEPGLEIRCD
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.
A5D1P3
Q7NZD1
UBIB_CHRVO
Ubiquinone biosynthesis protein UbiB
Chromobacterium
MSISRSLKIVATLYRYGLDDFLEGHSRLAFLHKLFGLCPVRRDTSAPLPQRVRLALESLGPIFVKFGQVLSTRRDLLPPEYADELALLQDRVPPFDGDIARQVVERSLGRKVEELFVDFDLKPVASASVAQVHKAWLRQPDGGRGREVAVKVLRPGILPVIEQDLSLMRTLAGWVEKLFADGKRLKPREVVAEFDKYLHDELDMMHEAANASQLRRNFKGSDMLIVPEVFYDYSSREVLTLEWMHGIPVGQIERLREAGVDLQKLSRFGVEIFFTQVFRHGFFHADMHPGNIFVAADGRYIALDFGIVGSLTDTDKHYLAVNFLAFFNRDYHRVATAHIESGWVPRDTRAEELEAAVRTVCEPIFEKPLSEISFGMVLLRLFETSRRFNVEIQPQLVLLQKTLLNIEGLGRQLDPELDLWDTAKPFLTKWMNEQIGWRGLLRTLKHEAPQWATTLPTLPRKLNEALGSAKTDLLVEGYIQLMREQKRQNFLLLLIAILLAALLAKSLL
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
Q7NZD1
Q3IFW0
GCSH_PSET1
Glycine cleavage system H protein
Pseudoalteromonas
MSNIPSELKYASSHEWVRNEGDGTFTVGITEHAQELLGDMVFVELPEVGDEVDAGEECAVAESVKAASDIYAPIGGEIVAINEELEDAPETVNTDAFGDGWLFRIKASDESELENLLNAEDYANTIDED
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Q3IFW0
Q89AK7
BIOC_BUCBP
Biotin synthesis protein BioC
Buchnera
MIDKKKIAEAFGKAAANYDNFSVIQRIAGNILLSKIETFFNISILDAGCGTGWFSKKWRQLGNTVTALDFSKNMLLTAKNTNSADYYLHADMEQLPICDNIFDLSWSNLSLQWCNKFNKAISELCRVTKPGGMVVFSTIAHGSLYEFNKAYRTINSSYQENKFLSINDIKLSCCNKKTLIDNILITFSFSKILEAMYSFKKIGANYISSNHSKILTKKKIRQLQENWPYNPNGYLLSYRFVFGVIYL
Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Q89AK7
P38710
INM1_YEAST
Inositol-1(or 4)-monophosphatase 1
Saccharomyces
MTIDLASIEKFLCELATEKVGPIIKSKSGTQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVITDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLESMGSLILNKSVVALQPGSAREGKNFQTKMATYEKLLSCDYGFVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGANPGEWSIDVDNRTYLAVRGTINNESDEQTKYITDFWNCVDGHLKYD
Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides.
P38710
Q9CDG1
EFG_LACLA
Elongation factor G
Lactococcus
MAREFSLANTRNIGIMAHVDAGKTTTTERVLYYTGKIHKIGETHEGASQMDWMEQEQERGITITSAATTAEWKGNRVNIIDTPGHVDFTIEVQRSLRVLDGAVTVLDAQSGVEPQTETVWRQATEYGVPRIVFANKMDKIGADFYYSLSTLGDRLGANAHPIQIPIGAEDDFIGIIDLVTMKSEIYTNDLGTDIKETVVGSDEFNAELAALDFNAEEYTELANEWREKLIEAIADFDEDIMEKYFAGEEIPEAELKAAIRKATINVDFYPMLAGSAFKNKGVQMMLDAVIDYLPSPLDIPAIQGVNPDTDEEDERPASDEEPFAALAFKIMTDPFVGRLSFFRVYSGTLDAGSYVLNTSKGKRERIGRILQMHANTRKEIQTVYAGDIAAAVGLKNTTTGDSLTDEKAKIILESIEVPEPVIQLMVEPKTKADQDKMGVALQKLAEEDPTFRVETNPETGETVISGMGELHLDVLVDRMKREFKVEANVGAPQVAYRETFRAGTSARGFFKRQSGGKGQYGDVWIEFTPNEEGAGFEFENAIVGGVVPREFVPAVEKGLVETMANGVLAGYPMVDIKAKLYDGSYHDVDSSETAFKVAASLAMKEAAKTAKPAILEPMMKVTITVPEENLGDIMGHVTARRGQVNSMEAHGKSQIVNAFVPLAEMFGYATTLRSSTQGRGTFMMVFDHYSDVPKSVQEEIIAKNGRNAD
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.
Q9CDG1
Q94A28
ACO2M_ARATH
Citrate hydro-lyase 2
Arabidopsis
MYRRATSGVRSASARLSSSLSRIASSETASVSAPSASSLRNQTNRSKSFSSALRSFRVCSASTRWSHGGSWGSPASLRAQARNSTPVMEKFERKYATMASEHSYKDILTSLPKPGGGEYGKYYSLPALNDPRIDKLPFSVRILLESAIRNCDNYQVTKDDVEKILDWENTSTKQVEIAFKPARVILQDFTGVPVLVDLASMRDAVKNLGSDPSKINPLVPVDLVVDHSIQVDFARSEDAAQKNLELEFKRNKERFTFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNSKGFLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLDGKLKEGVTATDLVLTVTQILRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLEYLKLTGRSDETVSMIESYLRANNMFVDYNEPQQERAYTSYLQLDLGHVEPCISGPKRPHDRVPLKDMKADWHACLDNPVGFKGFAVPKEKQEEVVKFSYNGQPAEIKHGSVVIAAITSCTNTSNPSVMIGAALVAKKASDLGLKVKPWVKTSLAPGSRVVEKYLDRSGLRESLTKQGFEIVGYGCTTCIGNSGNLDPEVASAIEGTDIIPAAVLSGNRNFEGRVHPQTRANYLASPPLVVAYALAGTVDIDFEKEPIGTRSDGKSVYLRDVWPSNEEVAQVVQYSVLPSMFKSSYETITEGNPLWNELSAPSSTLYSWDPNSTYIHEPPYFKNMTANPPGPREVKDAYCLLNFGDSVTTDHISPAGNIQKTSPAAKFLMDRGVISEDFNSYGSRRGNDEVMARGTFANIRIVNKLLKGEVGPNTVHIPTGEKLSVFDAASKYKTAEQDTIILAGAEYGSGSSRDWAAKGPLLLGVKAVIAKSFERIHRSNLAGMGIIPLCFKAGEDAETLGLTGHERYTVHLPTKVSDIRPGQDVTVTTDSGKSFVCTLRFDTEVELAYYDHGGILPYVIRSLSAK
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance . Involved in acetate assimilation .
Q94A28
Q2NGG1
THIM2_METST
4-methyl-5-beta-hydroxyethylthiazole kinase 2
Methanosphaera
MLEQCSKNIEKLRNKCPLTHCITNYVTINDCANVVLAIGGSPAMANEAPEIEEFVEAAGVTIINMGTLLEDQIEPMQIAACHTKKTNTPLVLDPVAVGVSKLRNDITIDLINKSSVDVIRGNMSEIKAIANLFNITDEKSVAKGVDVSSDDIITKDNIKSNASLVKAVADKLNTTIAVSGAIDIISDGVSIYLIDNGEEVMSKITGSGCMLTCVIGSFCAITSPLEAAIIGSLSMAISGELARRKMEINNEGSGSFRTYLIDMMYNMNDETIMKYGKLYKLE
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Q2NGG1
Q5F783
PRMB_NEIG1
N5-glutamine methyltransferase PrmB
Neisseria
MVHIMFNQAAQELTTIRDVLRFAVSRFNEAGLFFGHGTDNAHDEAVYLILHTLNLPLDMLAPYLDAKLLEAEKEEVLAVIERRAVEHIPAAYLTHQAWQGEFDFYVDERVIVPRSFIYELLGDGLRPWIEYDELVHNALDLCTGSGCLAIQMAHHYPDAQIDAVDVSLDALEVAGINIEDYGLEERIQLIHTDLFEGLEGTYDLIVSNPPYVDAESVGALPEEYLHEPELALGSGADGLDATRQILLNAAKFLNPKGVLLVEIGHNRDVLEAAYPELPFTWLETSGGDGFVFLLTREQLLGEE
Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue.
Q5F783
Q9TZI4
GBAS1_CAEEL
G-protein alpha subunit activating protein gbas-1
Caenorhabditis
MRSVRSSSRTPKPVKRFVFDEDEDLEEIDLDEVDNADFEREDDEEEVLSEPSESPYTSTPKSSKRVNKTRGTKDFFKKDESLQLFRFVLNECRSQKPGRVGRVAKKRVGVNSMKYWERYKREIQGYRLPKQYRYHYSFYSKCFYKVLGLTPEEKVDLYYACEMPVVTDAEKQWLVEQFHVEFDEFGVIIGSDVCTHWDEEHSDSEDDSGKKEEKAREVSRYTEYHDDMMWKFIVDKISEGAQPIIDKHPIWDEFVKLNEENDVISKKSGRNHYDRFRRILVPNLHFMPYDDFTKAVLYERLEYPIPEEYRKILFTTTGADINESGFIEYLPPSTIHQISPIVPIPCHKSNPKFSQLKEPKDLILWSERKKFTPREDSQIWEFVRRKCVDSAGIFVKNDVLRGRGTLFFKDFRNTERKYESITQRFVVLRKLIMDTDYSLKQKLEIYYAISQPVDEDALDAFKSIACLVLNPDGTIRFAISKSFLIGRISDEPAKLEAENYSYVYDLFIFNETFGTAENPEPLCSVSQNRAEKFMLVSQLVFRFISRFEALEDRRIAWITPNAQVAPKEPVPAPSKKKSAFEAYQSSPQTFDTIQRFSTKRPFFCGDNFQIPPKKPFLAEEDVKLEPMEYENSEQIVENAEIKLEPAEELLDAETVTVEEFLMNSYSTAAPSTSTAPAPPKAPVTAPPAPQKSAQLLGKIDFAIGKMRENFDRFLQFAQQNSADLTVVQRYRYDAQMQQMTEKFTKDVSKVLSGDSIKR
Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates G-protein alpha subunit goa-1.
Q9TZI4
B8EBI6
RL15_SHEB2
50S ribosomal protein L15
Shewanella
MRLNTLSPAAGSKHAPKRVGRGMGSGLGKTAGRGHKGQKSRSGGGVRPGFEGGQMPLKIRLPKFGFTSRRAMVTAEVRVLELAKVNGDVIDLNALKDANVITRNIQFAKIVLSGTIERPVTVKGLKVTKGARAAIEAAGGKIEE
Binds to the 23S rRNA.
B8EBI6
Q9HL07
RL13_THEAC
50S ribosomal protein L13
Thermoplasma
MRVIDASGAIYGRLSAYVAKRLLEGEEITIVNASKAVITGNKEFIIEKFKERLDIGSVRKGPYYPKTPENILRRSIGDMLPKKITKGKEALARCRVYRNTPPDIEKEKVEKVDGVVTDKVSGIITLGDLSKELGGY
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Q9HL07
P62214
RECA_DESVH
Recombinase A
Desulfovibrio
MAKKPSLSPEEMRREALETALSTIERKYGLGAVMKLSDEAHVAIPVIPTGSIGLDLALGVGGVPRGRVTEIYGPESSGKTTLTLHIIAEAQKRGGTAAFIDAEHALDVAYARRLGVNTEELLISQPDFGEQALDIADMLVRSAAVDLVVIDSVAALIPQAELEGSMGDTQVGGQARLMSHALRKLTGTIHKSRTAVIFINQIRMKIGTMGYGSPETTTGGNALKFYSSVRMDIRKIQTLKDKEEVYGSRTRVKIVKNKVAPPFREALFDILYGTGISRTGEIIDLGSDAGIIDKSGSWFAFGSERLGQGKENVRALLEENAPLREAIEAKLIEHLGMTPTKFASSGEEPANDEENDL
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
P62214
Q2FQH4
PELO_METHJ
Protein pelota homolog
Methanospirillum
MKAEIEELQRSFGEIRLFPENSDDLWHLHNLITPGSLVYATTLRSVEGSQDKIRPEKQEKRPVRLGIRVEDVEFHEYSIRLRVFGTIESGVDIGSHHTLNLEPGYEISVIKSWSGSDLERIDRAIKGSTSEAIHILTVEEGEAELYRVQSYGPKQVWSLAAGSGKTAEVSSREEFSEAVVSQVSQLTGPLVIAGPGFVKEEIIAKFKRKNPSRSAPLVIGDTRAGGRRAVQEVIGQGILEKLNGDLQLAREVTCLDELMRRIGKDEPVAYGIDAVRDATGCGAVQTLMVVDTLLRDPDAADLIRQAEAMRSEVVIFSSRFEPGERLAGLGGIAALLRYSIA
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Q2FQH4
Q57TP3
DNAK_SALCH
Heat shock protein 70
Salmonella
MGKIIGIDLGTTNSCVAIMDGTQARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPYKIIGADNGDAWLDVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDTRLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDINDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTPLITKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAESDRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALNALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQAGSAEASANNAKDDDVVDAEFEEVKDKK
Acts as a chaperone.
Q57TP3
B5RFM6
UBIB_SALG2
Ubiquinone biosynthesis protein UbiB
Salmonella
MTPGEVRRLYFIIRTFLSYGLDELIPRMRLTLPLRLWRYSLFWMPNRHKDKLLGERLRLALQELGPVWIKFGQMLSTRRDLFPPQIADQLALLQDKVAPFDGRLAKAQIEEAMGGLPVDAWFDDFDIQPLASASIAQVHTARLKSNGKEVVIKVIRPDILPVIQADLKLIYRLARWVPRLLPDGRRLRPTEVVREYEKTLIDELNLLRESANAIQLRRNFENSPMLYIPEVYSDYCSQNMMVMERIYGIPVSDVAALEKNGTNMKLLAERGVKVFFTQVFRDSFFHADMHPGNIFVSHEHPENPQYIGIDCGIVGSLNKEDKRYLAENFIAFFNRDYRKVAELHVDSGWVPPDTNVEDFEFAIRTVCEPIFEKPLAEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGVGRQLYPQLDLWKTAKPFLESWIKDQVGIPALTRALKEKAPFWVEKMPEIPELVYDSLRQGKYLQHSVDKIARELQVNHVRQSQSRYLLGIGATLLLSGSFLLVNRPEWGLMPSWLMVGGVVVWLVGWRKTR
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
B5RFM6
E2JA31
DDAF_ENTAG
ATP-dependent N-fumaramoyl-DAP-amino acid ligase
Pantoea agglomerans group
MSILNNKEVIVIIDAWSGGKHLIPAFQALGYFCLHVQSTFLPEVFIADNQLAIARSDRHIVHDGNIETLLSQLQPYTIKAILAGSEGAVGLADCLNDALELTFSNQFELSAARRNKYLMQEQLALKGVASINQQLAGHSDELKQWLAGHAHWPVVLKPIQSAGTDGVFICHDLAQALQAFEAILAKKDFFGSPNREVLCQEFLAGEEFVVNGIACQGEYFFTELWQSKKQQRNGFPVYETQYLHYQNDAGFDVLTAYTVQVCQTLGINNGAFHAEVMMTSGGPVLIEIGARVAGGADPYIIEECLGHSQISKLAQAVLHPAKFLQECRRQHDFSGHRRAAYVYMISPSPGRVQVSPEEKFIKIDGVISINYHYAPGDIQQETCDLLSSPGVIIAIRDNPALLKQTIAEIRDVEADFYHLGLIDE
Involved in dapdiamide antibiotics biosynthesis . Ligates N-beta-fumaramoyl-DAP and valine, isoleucine or leucine to form dapdiamides A, B or C, respectively . Also ligates N-beta-epoxysuccinamoyl-DAP and valine to form dapdiamide E .
E2JA31
Q0AYK2
PYRH_SYNWW
Uridine monophosphate kinase
Syntrophomonas
MQKPKYKRIVLKLSGEALAGHNTYGIDNEVLNSIARQVVEVVRQEVQVAIVVGGGNIWRGVAGSAKGMDRATADYMGMLATVINALALQDALEQEGMGTRVMSAIEMKEVCEPYIRRRAIRHLEKGRVTIFAAGTGNPYFSTDTAAALRSAEIEAEVILMAKKVDGVYDADPVKNPAALKFDRLNYIDVLSRGLGVMDSTAASLCMDNGIPIIVFDLTREGNILKAVLGEEIGTYVGR
Catalyzes the reversible phosphorylation of UMP to UDP.
Q0AYK2
A8G207
Y019_PROM2
Nucleoid-associated protein P9215_00191
Prochlorococcus
MAGFGLPNFGQLTEAFKKAKQIQQDAQKLQDELENMEIEGKSDDEMIKVWISGNQLPLKVEVQENILNADKEKIEKNILQAIQKAHESSTTTMKERMNDLTGGLNLNLPGFDNSDS
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
A8G207
Q4V0S8
DNAA_XANC8
Chromosomal replication initiator protein DnaA
Xanthomonas
MDAWPRCLERLEAEFPPEDVHTWLKPLQAEDRGDSIVLYAPNAFIVEQVRERYLPRIRELLAYFAGNGEVALAVGSRPRAPEPLPAPQAVASAPAAAPIVPFAGNLDSHYTFANFVEGRSNQLGLAAAIQAAQKPGDRAHNPLLLYGSTGLGKTHLMFAAGNALRQANPAAKVMYLRSEQFFSAMIRALHDKAMDQFKRQFHQIDALLIDDIQFFAGMDRTQEEFFHTFNALFDGRQHIILTCDRYPREVEGLEPRLKSRLAWGLSVAIDPPDFETRAAIVLAKARERGAEIPDDVAFLIAKKMRSNVRDLEGALNTLVARANFTGRSITVEFAQETLRDLLRAQQQAIGIPNIQKTVADYYGLQMKDLLSKRRTRSLARPRQVAMALAKELTEHSLPEIGDAFAGRDHTTVLHACRQIRTLMEADGKLREDWEKLIRKLSE
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
Q4V0S8
Q0T1H5
SURE_SHIF8
Nucleoside monophosphate phosphohydrolase
Shigella
MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFENGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLDGHKHYDTAAAVTCSILRALCKEPLRTGRILNINVQDLPLDQIKGIRVTRCGTRHPADQVIPQQDPRGNTLYWIGPPGGKCDAGPGTDFAAVDEGYVSITPLHVDLTAHSAQDVVSDWLNSVGVGTQW
Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
Q0T1H5
Q6ZPY5
ZN507_MOUSE
Zinc finger protein 507
Mus
MEESSSIAMLVQEIGEPEAVLTAEGVLSPSSEVDQQRKAKADPLVHVIQKLSKIVGHEKSQKCLLIGKKRPRPSETANSLEKLENCEIPAKATESPAAGVRKTEMSQASSTLASNDGKAMSYQCSLCKFLSPSFSVLKEHVKQHGQQHDVMLMCSECHATSRSQQELEAHVVSEHENSASSQARSSPSGQGATERKSETMVDIPVNMGSPQTHAVQSAAMAESGRRKWYAYEQYGMYRCLFCSYTCGQQRMLKTHAWKHAGEVNCSYPIFENENEPLGLLASSMSAAPGGVDAVVIAIGDSELSIHNGPSVQVQICSSDPPSSSPLEQSTEEGVHLNQAVTLDANEEEMLEVMSDSEENLFADSLLSSAQKIISSSPNKKGHVNVIVERLPSAEETLPPKHFLINAEMEEGKSPSPSEAQTGCVGAGNMYHADKCTVDIGGLIIGWSSAEKKDSELSKGLAPDENAPPGRRRTNSESLRLHSLAAEALVTMPIRAAELTRASLGHYGDINLLDPDTGQRQVSGPLATYSKKIMSPLKNSTDGVTSFNQSNSTVVALPEGRQELSDGQVKTGISMSLLTVIEKLRERTDQNASDDDILKELQDNAQCQPNSDGSLLGSNVVEYIPDAERPYRCRLCNYSSGNRGYIKQHLRVHRQRQPYQCPICEHIAENSKDLESHMINHCKTRIHQCKQCKESFHYKSQLRNHEREQHCLPNTLSVASNEPRISRDAADGKCAQEGNKPSTQKQYRCDVCDYTSTTYVGVRNHRRVHNSDKPYRCSLCGYVCSHPPSLKSHMWKHASDQNYNYEQVNKAINDAISQSARVLGKSRGKPLLTSSEERTGPTTGSPENLVSSSELTSQLPGEVMDASELEKLNPTGCSSDVSGRSCSLAAPGTEYCVLLFCCCICGFESTSKESLLDHMKEHEGEIVSIILNKDHSTALNAN
May be involved in transcriptional regulation.
Q6ZPY5
E9F5F1
SUBF_METRA
Subglutinol biosynthesis cluster protein E
Metarhizium
MTRLSLQIIAGLAGQAWLVNSDTPSHDAFASCLSDASVPIATKGTPEWTQHTTPFNTRLQYEPIAVAVPTEISQIAAAVTCAKTNGIPVTAKSGGHSFTSLGLGGEDGHLVIQLDRMYNVELAQNGTAMIQAGARLGHVAVELYNQGKRALSHGYCPAVGVGGHAAHGGYGMVSRKYGLTLDWMKDATVVLHNGTIVYCSESEHSDLFWAIRGAGSSFGIVAEYGFETFPAPEKVTNFGIVLDWNPETAPAGLLAFQDFAQTMPSELSCQIDVRSTGYTLNGSYVGNEASLREALVPLLGKIGGHLEVHEGNWLEYVKFWALGQPNIDITPPADNVHLSLYTTGALTPSLSANQFRSFADYIATDAIKRGNSWSIQMFIHGGQYSAISGPKITDTAYAHRDKFLIFQFTDFVWPSQEYPEDGLALGREFRDIITNSFTNGQWGMYANVPDSQLSSGEAQKLYWGKNLERLETIKAKYDPNNLFRNPQSVKAAARCATRPLPLQGQSLLF
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside chain . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase subA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations . The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase subD through the action of the prenyltransferase subC to yield a linear alpha-pyrone diterpenoid . Subsequent steps in the subglutinol biosynthetic pathway involve the decalin core formation, which is thought to be initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase subE (Probable). The following cyclization cascade would be catalyzed by the terpene cyclase subB (Probable). Lastly, the FAD-dependent dehydrogenase subF probably catalyzes the five-membered cyclic ether formation to complete the formation of subglutinol A (Probable). Subsequent redox reactions appear to give rise to subglutinol C and D, however, it remains unclear which enzymes are responsible for these transformations (Probable). SubD may have secondary function in the conversion of the identified subglutinols to subglutinol analog 45, which seems to be the major product of the cluster .
E9F5F1
B3MKS0
IHOG_DROAN
Interference hedgehog
Sophophora
MPSIVSSLLLVVLLTSPLGAIPVLYPSPPPLPAYPSPGVRILRPPESLVAPLGDEVVLECETSLPPERFEWSYRRWTPNGTAVNGSPGAGFKYLKTSSMKANVTQEAAISRLKVLVRQDTLGEYRCNGWFGPLLVTSTTARLELATTSVKSQEPVTSLQWQITNGNSVLWPCGQPVRSNPAASWTFYRNGVELGPEYSGTGGNLFLRNVSVDSSGSYSCQATNPASGERIKSTSSMELQVVPSRGSQVKAPYLLPGQPGSQTVTAIEGGTLLLLCPGVGSPPPTAVWSSPDIVGAVNNKRTRVLAHALEISNVQIGDSGTYICYLDNGVRPPLEHFIQVKVEQPPQIVRPPWIDMVNEGERVQLECEATGVPTPEIYWLLNGKSSIYDTEAEQLPNGHLVLHSVLKRHAGYVQCFARNSLGEHSAGMSLQVTPKPIHSESTQQSDHNHSKANRGRRPAQMIPPSAPNVTRLSDESVMLRWMVPRNDGLAILFFKVQYRTVGEGKRKNWQTTNENIPYGRPEWNSEMGKSFTASVTDLKPQRTYRFRIMAVYTNNDNKESNMSAKFFLQPGAALDPMPVPEMLEIDEYSETAVVLHWRLDSDADEQLITGYYAYYRPSSSAGEYFKATIEGASSRSFTIGNLEAGTVYEFKLQSFSAESASEFSALKQGRTQRPMVSTTEEATLQTGVRDTTTPSHNETFSMSPIVTGTIGGGAVLILFVVTTCLCMWRRRNSRAHRGGGQNKPRMAELREDFVPLDSCSPTKQRQRSRHIHITLNPLAQQQQQALDEKNDAEHDMTYFQRQPTYDYDPGLRRMSSSSLRRSQRTLERAGSSNGNNNNLNQSADMGPVDNPGKPGRVLMKRPRLSSRSENLSSGSLNSVGV
Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc).
B3MKS0
Q475Q3
SURA_CUPPJ
null
Cupriavidus
MKRQEFALFSLTLMLSPWRRVLLPAVLAAMAGPALAQLKAPSQASRATGIFVPQSSDVAVPSSQPQLGVPQPSSGGKRSQLVDEVVAVVNNSVITRRELLDRADEIEAQLRTANRPAPPRADLLGEVLERLIMERVQTQAAQDAGIKVTDQELDRAIESVAQQNRLSATELRRRVEASGMTWTKYRDELRKQVQVIRLREREVDSKVQVYDGEIDNYLAARGGQGAAATGPTEFNVSQILVRVPENASDAQKQELQKKAEQLLKQAQGGADFAQLAQANSQGPEAAQGGAIGFREIGRLPALFANAVVDLQPGAVAPEVVESANGFHILKLTAKRVAPASTSASSPAAASRITQTQVRHILIRTGPNMPEAEARRQLGTLRDRITHGGDFADAAKRFSQDGSAQAGGELGWVSPGELVPEFEQAMNRLRPGEISEPVVTQFGVHLIQVENRRETEMAPEKQRDFARAEIREQKLRAAYDDWVRQLRSQAYVEYRVNRQR
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Q475Q3
P0AGI3
RBSC_ECO57
Ribose import permease protein RbsC
Escherichia
MTTQTVSGRRYFTKAWLMEQKSLIALLVLIAIVSTLSPNFFTINNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAVAASIVGIEVNALVAVAAALALGAAIGAVTGVIVAKGRVQAFIATLVMMLLLRGVTMVYTNGSPVNTGFTENADLFGWFGIGRPLGVPTPVWIMGIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKIKIIVYSLCGLLASLAGIIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVDNKKQ
Part of the ABC transporter complex RbsABC involved in ribose import. Probably responsible for the translocation of the substrate across the membrane.
P0AGI3
A3D147
DPO4_SHEB5
DNA polymerase IV
Shewanella
MRKIIHIDMDCYFAAVEMRDFPEYRGKPLAVGGSSDRRGVISTCSYEARKFGVRSAMATAYAFKLCPDLILVPGRMQVYKDVSLQIREIFSRYTQLVEPLSLDEAYLDVSECQQYKGSATLIAQAIRRDILAETGLTASAGIAPVKFLAKVASDLNKPNGQYVITPETLPEFVKTLSLRKIPGVGKVTAEKLSSLGLNTCGDVQAYSKPELLARFGKFGGVLIERSQGIDERGISADRERKSVGVETTLAKDIYSLEQCQQVMPGLIQELALRLSRSAKERKIHKQVVKLKFNDFKQTTIEHRSDEVSIVMFYDLLAQAMARQEGRGIRLLGISVGLADSILAVSEIPNAQTQLDLAL
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
A3D147
Q4JVB5
DXS_CORJK
1-deoxyxylulose-5-phosphate synthase
Corynebacterium
MGILDKVSSPADLKGLDADQLEQLAAEIREFLIQKVSATGGHLGPNLGVVELTIAMHRVFDSPSDPLIFDTGHQSYVHKILTGRRDLFDTLRQKDGLSGYPDRAESPHDWTESSHASASLSYADGLAKAFELTGQVHRHVVALVGDGALTGGMTWEALNNIAAAKNRSLVVVVNDNGRSYSPTIGGLAENLAALRLQPMYDRVMDTGKNALGRMGWVGDRAFQVIHGLKEGVKHTVIPHEMFPELGLKYIGPVDGHDLKQVENALRYAKDYGGPVIVHTVTQKGKGFDPAEQDEADQMHSTGVIDPITGESMAKKTEGAISWTKVFSNHLIDIANDREDIVAITAAMAGPTGLADFAKVHPSRTYDVGIAEQHAVTSAAGLALGGLHPVVAVYSTFLNRAFDQLLMDVALLKLGVTLVLDRAGITGSDGASHNGMWDLSITGIVPGIHVAAPRDARTLELALDRAVAVDDAPTVVRFPKGDAPAGIPAVREEDDYDVLFEQSGDKSEGRVLIVSFGALSKQALGAAQALCDANFSATVVDPHWVVPTADSLLEFARGFDLIVTIEDNGVHGGAGSRLHYDLSQAGIDVPVRNLGVPQEFLAHGSRGEVLEDLGLDAETVARTVVGYAEKL
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).
Q4JVB5
Q8U476
NTPPA_PYRFU
Nucleotide pyrophosphatase
Pyrococcus
MKKIILASSSPRRREILSRFFDIIVHPSNVNEDKIKEKDPTETAIKIAKAKAFDLAVKFPTDTIIAADTIVTLNGKILGKPKDSEEARKMLKQLSGKTHEVVTGYCIISGDKIIEGAEITKVKFRELSDDLIEWYISTQEWRDKAGGYGIQGFGAILVEHIEGDYYNVVGLPIIVIIKLIELGHKLKRIF
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q8U476
Q65IJ4
R14Z2_BACLD
30S ribosomal protein S14 type Z 2
Bacillus
MAKTSMIVKQKREQKFKVREYTRCERCGRPHSVIRKFKLCRICFRELAYKGHIPGVKKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Q65IJ4
Q0TL77
FRSA_ECOL5
Esterase FrsA
Escherichia
MTQANLSETLFKPRFKHPETSTLVRRFSHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAERTDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEEDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEAAQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWKLTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRFGANVAVRLAYLESPRLKVVACLGPVVHTLLSDFKCQQQVPEMYLDVLASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDKGLQEITDWIEKRLC
Catalyzes the hydrolysis of esters.
Q0TL77
P17077
RL9_RAT
60S ribosomal protein L9
Rattus
MKTILSNQTVDIPENVDITLKGRTVIVKGPRGTLRRDFNHINVELSLLGKKKKRLRVDKWWGNRKELATVRTICSHVQNMIKGVTLGFRYKMRSVYAHFPINVVIQENGSLVEIRNFLGEKYIRRVRMRTGVACSVSQAQKDELILEGNDIELVSNSAALIQQATTVKNKDIRKFLDGIYVSEKGTVQQPDE
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
P17077
F4HZB5
NET1D_ARATH
Protein NETWORKED 1D
Arabidopsis
MTAVVNGNSKRYSWWWDSHISPKNSKWLQENLTDMDSKVKQMIKVIEEDADSFARRAEMYYKKRPELMKLVEEFYRAYRALAERYDHATGVIRHAQQTMAEAFPNQDPMMFGEESPLGSSTDGFDPQTPDSYPPIRAPVYPDDLRKGAFGISSSHLSTVKRNIAFMEDPQSVSSGKGFKTAKARKGLNFNNVDGKEINAKVLSESERASKAEAEIVALKDALSKVQAEKEASLAQFDQNLEKLSNLESEVSRAQEDSRVLIERATRAEAEVETLRESLSKVEVEKESSLLQYQQCLQNIADLEDRISLAQKEAGEVDERANRAEAETLALKQSLVSSETDKEAALVQYQQCLKTISNLEERLHKAEEDSRLTNQRAENAEGEVESLKQKVSKLIEENEAYELQYQQCLDTIADLKLKLFHAQEETQRLSREIEDGVAKLKFAEEKCVVLERSNQNLHSELDGLLEKLGNQSHELTEKQKELGRLWTCVQEENLRFMEAETAFQTLQQLHSQSQEELSTLALELQNRSQILKDMEARNNGLQEEVQEAKDQSKSLNELNLSSAASIKSLQEEVSKLRETIQKLEAEVELRVDQRNALQQEIYCLKEELSQIGKKHQSMVEQVELVGLHPESFGSSVKELQEENSKLKEIRERESIEKTALIEKLEMMEKLVQKNLLLENSISDLNAELETIRGKLKTLEEASMSLAEEKSGLHSEKDMLISRLQSATENSKKLSEENMVLENSLFNANVELEELKSKLKSLEESCHLLNDDKTTLTSERESLLSHIDTMRKRIEDLEKEHAELKVKVLELATERESSLQKIEELGVSLNAKDCEYASFVQFSESRMNGMESTIHHLQDENQCRVREYQVELDRAHDAHIEIIVLQKCLQDWLEKSSSLIAENQDIKEASKLLEKLVSELEEENIGKQVQIDSSINCIKILRTGIYQVLMKLEIIPGIGSGDENSRDQRNMHDILNRLEDMQTMLLSIRDENQHSAIENLVLIEFLRQLKSEAVGIETEKKILEEELESQCQQLSFSRDETQKLIFVNGELTTKVNQGVNREKVLMVEIEDFHRQVLQLRDDYTILQGDNNKTLDEKAYLTKSTLQLEEEKCKLEDDISLLLSETIYQSNLIILLEDVILEKLSGAMKLNEDLDRLSIVKCKLEEEVRELGDKLKSADIANFQLQVVLEKSNAELLSARSANVHLEHEIANVKVQKEKELLEAMLMISIMQNEKSELSKAVEGLECRYKEAKAIEEDRDKQVLRLRGDYDEQVKKNSHSNEANLKLEADLMNLLMELEEIKVEKENLNQELFTERNEIELWESQSATLFGELQISAVHETLLEGLTNELVEACKNLESRSTLKDREIEQLKGRVNNLEDANKGQNDLMCKYAQAIFLLKESIQSLEKHAMLHEFENGPATETASLVDNSDGFLEIQELHLRIKAIEEAITKKLAMEELKTSSARRSRRRNGSLRKQNHEIYSEETEMITKDIVLDQVSDCSSYGISTRDILKIEDDHSLEAKSQNPPKGKSLSEESLVVDKLEISDRFTDPNKDANKRKVLERLNSDLQKLSNLHVAVEDLKIKVETEEKDEKGKENEYETIKGQINEAEEALEKLLSINRKLVTKVQNGFERSDGSKSSMDLDENESSRRRRISEQARRGSEKIGRLQLEIQRLQFLLLKLEGDREDRAKAKISDSKTRILLRDYIYSGVRGERRKRIKKRFAFCGCVQPPPSP
Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex.
F4HZB5
Q4QNB3
NUDC_HAEI8
NADH pyrophosphatase
Haemophilus
MKILQQDDFGYWLLTQGSNLYLVNNELPFGIAKDIDLEGLQAMQIGEWKNHPLWLVAEQESDEREYVSLRNLLSLPEDEFHILSRGVEINHFLKTHKFCGKCGHKTQQTQDELAVQCIHCGYQTYPVICPSIIVAVRRGHEILLANHKRHYSPNGGIYTTLAGFVEVGETFEQAVQREVFEETGISIKNLRYFGSQPWAFPNSQMVGFLADYESGEITLQESEIHDAQWFSYDQPLPELPPTGTIARKLIHVTLELCKAEHKCD
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Q4QNB3
Q9BYE7
PCGF6_HUMAN
RING finger protein 134
Homo
MEGVAVVTAGSVGAAKTEGAAALPPPPPVSPPALTPAPAAGEEGPAPLSETGAPGCSGSRPPELEPERSLGRFRGRFEDEDEELEEEEELEEEEEEEEEDMSHFSLRLEGGRQDSEDEEERLINLSELTPYILCSICKGYLIDATTITECLHTFCKSCIVRHFYYSNRCPKCNIVVHQTQPLYNIRLDRQLQDIVYKLVINLEEREKKQMHDFYKERGLEVPKPAVPQPVPSSKGRSKKVLESVFRIPPELDMSLLLEFIGANEGTGHFKPLEKKFVRVSGEATIGHVEKFLRRKMGLDPACQVDIICGDHLLEQYQTLREIRRAIGDAAMQDGLLVLHYGLVVSPLKIT
Transcriptional repressor . May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase . Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility . Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity .
Q9BYE7
A9A135
DNAK_NITMS
Heat shock protein 70
Nitrosopumilus
MGKVIGIDLGTSNSAAAVMMGGKPTIIPAAEGQTAAGKAFPSVVAFSKEGELLVGEPARRQAVTNPDNTIIAAKRKMGSDYTFKIQDKEYKPQQISSFILQKIKKDAEAFVGETVEKAVITVPAYFDDNQRQATKDAGTIAGLDVVRIINEPTAASLAFGLDKAKEDMKILVFDFGGGTLDVTIMEMGGGVFEVMSTSGDTQLGGTDMDKVLIDYIVDEFKKKEGVDLSQDTTAMTRIREAAEKAKIELSTVMETDVNLPFIAHDPSSGAKNLELRLTRSKLDELIGPIVDRCKPSIQKALEDAKLSNSDINKIVMIGGPTRIPLVKKFVSEVIGKEVESGVDPMEAVAMGAAIQAGIIAGDVTSDIVLLDVTPLTLGIETLGGVREPLIERNTTIPTSKGKVFTTAADNQTAVTIHVVQGERPMATDNVSLGSFNLTDLPPAPRGVPQIEVKFDIDANGIINVTAKDLGTQKEAKITIETKTKLSEEEIEKLKEDAEKFSEEDKKKKEKIDLKNEAESYIYTTEKLVNHDLKDKISQEQGIKITDAVKEVKEVLDKEPEELKPKLEALQSIVNEVTTELYKNAAPPPGADGQQGADGQQGADGQQGADGQQGADGQQGADGQTTESSSNDETKTN
Acts as a chaperone.
A9A135
Q4ULR6
ISPT_RICFE
Isoprenyl transferase
spotted fever group
MQQHLKYKIMTNIKHLAIIMDGNARWADQHNLTKSEGHKAGADKIRELLPEFINLNIPYITLYTFSSENWQRSSTEVDFLIKLLSIYFKNELNSLHKNGVKIKVIGRLNLLSSSLQKQINNAIELTKNNNKITLCIAFSYGSRQEIVDACTKIIASGKKEISESDIGHALYDPEMPDVDLLIRPGGVYRISNFLLWQAAYAELYFSPKYWPAFNKDDIIEAINDYSKRKRTFGKR
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Q4ULR6
B1WBM3
TM138_RAT
Transmembrane protein 138
Rattus
MLQTSNYSLVLSLQFLLLCYDLFVNSFSELLRMAPVIQLVLFIIQDIAILFNIIIIFLMFFNTFVFQAGLVNLLFHKFKGTIILTSVYLALSISLHVWVMNVRWKDSSSFRWTNGLQTLFVFQRLAAVLYCYFYKRTAVRLGDPRFYQDSLWLRKEFMQVRR
Required for ciliogenesis.
B1WBM3
Q47279
HRPN_PECCC
Harpin-Ecc
Pectobacterium
MLNSLGGGASLQITIKAGGNGGLFPSQSSQNGGSPSQSAFGGQRSNIAEQLSDIMTTMMFMGSMMGGGMSGGLGGLGSSLGGLGGGLLGGGLGGGLGSSLGSGLGSALGGGLGGALGAGMNAMNPSAMMGSLLFSALEDLLGGGMSQQQGGLFGNKQPSSPEISAYTQGVNDALSAILGNGLSQTKGQTSPLQLGNNGLQGLSGAGAFNQLGSTLGMSVGQKAGLQELNNISTHNDSPTRYFVDKEDRGMAKEIGQFMDQYPEVFGKAEYQKDNWQTAKQEDKSWAKALSKPDDDGMTKGSMDKFMKAVGMIKSAIRGDTGNTNLSARGNGGASLGIDAAMIGDRIVNMGLKKLSS
Elicits the hypersensitive response (HR) in the plant upon infection. Harpin elicits HR in non-hosts and is also required for pathogenicity in host plants.
Q47279
O08537
ESR2_MOUSE
Nuclear receptor subfamily 3 group A member 2
Mus
MEIKNSPSSLTSPASYNCSQSILPLEHGPIYIPSSYVESRHEYSAMTFYSPAVMNYSVPSSTGNLEGGPVRQTASPNVLWPTSGHLSPLATHCQSSLLYAEPQKSPWCEARSLEHTLPVNRETLKRKLGGSGCASPVTSPSAKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRIVRRQRSASEQVHCLNKAKRTSGHTPRVKELLLNSLSPEQLVLTLLEAEPPNVLVSRPSMPFTEASMMMSLTKLADKELVHMIGWAKKIPGFVELSLLDQVRLLESCWMEVLMVGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTARFRELKLQHKEYLCVKAMILLNSSMYPLATASQEAESSRKLTHLLNAVTDALVWVISKSGISSQQQSVRLANLLMLLSHVRHISNKGMEHLLSMKCKNVVPVYDLLLEMLNAHTLRGYKSSISGSECCSTEDSKSKEGSQNLQSQ
Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.
O08537
B3E3I1
PYRC_TRIL1
Dihydroorotase
Trichlorobacter
MNLLIKGGRVIDPSQGIDDTLDVVVENGLVKEIGKGLATSAGAETIDASGKYVVPGLIDMHVHLRDPGLEYKEDIISGTRAAVAGGFTSVCCMPNTKPAIDNKAIASYIINKAKTEGACNVFPVGTITQGMHGDRLAEMGELKESGCVAVSDDGKPVKNSELMRRALQYAAGIGIMVISHAEELELVGEGVMNEGFTSTELGLKGIPRVAEDIATAREIMLAEYVGAPIHIAHVSTKGAVRIIREAKGRGVKVTCETAPHYFTLTDDAVRGYNTNAKMNPPLREADDLAAIKAGLKDGTIDCIATDHAPHHLDEKDVEFNEAMNGIVGLETSLPLSLKLVDEGVLNLSQLIEKMSCKPSELLGLGRGSLKAGNVADITVIDPAKQWTVTESALASKSKNSPWLGATMAGAAACTVVGGKIVFSGR
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
B3E3I1
Q74JY0
SEPF_LACJO
Cell division protein SepF
Lactobacillus
MAFDKLGRFFGISEDDEMNEVPYTESEEQQEEIPQTQKNERRANVVSINSGVSATSKIVLYEPRVYSDAKEVAQNLLNNKAVIINFARMDDEQARRIVDFITGTVYALNGEIQRVGDKIFLATPPKFETDGKIAELVEKKDKMD
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Q74JY0
B9LPV1
RFCL_HALLT
Clamp loader large subunit
Halorubrum
MADWTEKYRPSTLSEVRGNDKARDAFADWARSWDDHHEAVVLHGSPGVGKTSAAHALANDMGWETVELNASDQRTADVIERFAGRAARNATLGGSAAGGGAAGGDTASRQLVILDEADNIHGNYDRGGASAITELVKESGQPIVLIANDYYDMARGLRNATQEIEFRDVSARSIVPVLRDICRKEGIEFESDALERIAERNRGDLRGAINDLQAATEGRDSIAVEDVVTGDRDKALGLFPYLDAVLKEESAEEALQSAYAVDETPDDLTKWIENNVLDVYDPSEVVRAYDFLANADVWLGRVRATQNYSYWRYATDNAAAGVAAARDGTKGGWTRYGRPQFWSPSDATADEVVGQIAAKSGCSVATARREVLPFLEAVTHHCKPRELTVAMAAAYDLDEAGIAFVTGSGESTNKVASIAEDAQALREERMEDHAEGAFAGGRHAADDLGASDGETTNASGTASSSGDDGDADGTTDGDGSDANDGNDDDDDGQAGLSDFV
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
B9LPV1
Q1LLK0
HISZ_CUPMC
ATP phosphoribosyltransferase regulatory subunit
Cupriavidus
MSNRWLLPENIADVLPSEARKIEELRRRMLDLFRTYGYELVMPPMLEYLESLLTGTGHDLDLRTLKLVDQLSGRTLGLRADITPQVARIDAHLLNRPGVTRLCYAGNVLHARPAGFNATREPIQIGAEIYGHAGLEADVEIQELMLAALQVAGLSDIRLDLCHAGILEALLAALPSIRQIEEAMFAALETKDVPALRELTQGLPDTERDALLALPTLYGGVEVIERARATLPASPAIGRALDELAALAAQVSNASVNIDLSDLRGYHYHSGVMFTAYVSGLPNYVARGGRYDKVGEAFGRARPATGFSLDLREVAALSPVEVRAQAIFAPWDADPALRFAITTLRANGEIVIQSLPGHTHELDEFNCDRQLQRQGANWVVVPR
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Q1LLK0
Q3BPR2
PEPQ_XANC5
Proline dipeptidase
Xanthomonas
MPQPSLSSLYSDHLRTLTARADEALQRGGFEHLVVPSGSTHYQLFDDRDYPYAVNPQFKAWVPLTRVPNSWLVYTPGKRPTVIFYQPFDYWHVVPDAPSGWWVDHCDIHIIRTPEQALALLPKHAERCAILGEPQSTLGAYVPNNPQPVLDYLEYQRAFKTPYELALLRIAQQLAVRGHRAAEAAFRAGQSEFGIHMAYCAAVGQDANDLPYGNIIALNEHGAVLHYTELGQQPPQPLRSFLIDAGASAYGYASDITRTYAADPGSDFQALIDAVDAAQLRMGQNVRAGVDYKQLHIEAHLALMGILKEFGVLTVSPEAALATGVSAAFFPHGLGHLIGLQVHDVAGFAASDRGGRIERPAGHPYLRLTRVLEPGMVVTIEPGVYFIDMLLDEVKKNGHAASVNWQRVEAFKPYGGIRIEDEVVCTDGSAENLTRPVFASA
Splits dipeptides with a prolyl residue in the C-terminal position.
Q3BPR2
Q67JD0
PTH_SYMTH
Peptidyl-tRNA hydrolase
Symbiobacterium
MAKLIVGLGNPGPRYAATRHNAGWMLLDAFARKHGVAIEQRGFEGLYGELRWGAEAEKVILLKPLTYMNLSGRSVAQAARFYRIAPADILVLFDDLDLEPGRLRLRAKGSAGGHNGVKSVIAELGTAEFPRLRIGIGRPAPGWEVIDWVLAPFGPDDAAAVAAALPRAVEAVECFLTEGILAAMNRYNT
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q67JD0
P58818
PHR_METTM
Photoreactivating enzyme
Methanothermobacter
MIHDERIRSLNTEKPARDGKYVIYWMQASVRAHWNHALEYAIETANSLHKPLIVIFGLTDEFPNANSRHYRFLIEGLRDVGDALMKRGARLVVENERPPSAVMRYSDEASAVVVDRGYLDIQKEWVDELAESLHVPLMQVESNVIVPVETASPKEEYSAGTFRPKITRELERFMVPLKERRLAVDSLDLDPGPDLNDVTGKFRASEELEPSIFSGGASEAIRLFDEFLSEKLACFEKYRNDPVKNCLSNMSPYLHFGHISPLYLAMKASKTGECPEFLEELIVRRELSMNFVHYSDNYSSIRCLPEWAQKTLMEHARDPKEYEYTLREFEEARTHDPYWNAAQKEMVITGKMHGYMRMYWGKKILEWTDHPERAYDIAIYLNDKYEIDGRDPNGFTGVAWCFGKHDRAWAEREIFGKVRYMNDRGLERKFRIGEYVRRVQELEE
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.
P58818
P9WEV6
PAPS_PHOAM
Methyl phomopsenonate biosynthesis cluster protein PaPS
Diaporthe
MEYRYSYVIDPSSYDNQGLCNGIPLRVHRNADIEEYATISLRNDWRKHVGPLPLTSYGGNLGPKYNFTAVTLPECRPDRLEIVSYIMEFAFLHDDLVDTAQVDEALALNDTWRDGITEGLDTTSAKGKKSGEGLILRNILKEVTAIDPVRAAELMKFWKRDLDVSRDRKHFRDFDDYMEYRIVDCASYFLIALSTFAMALTIPAEDKDEVFTLLTRPVWAAAALTNDVQSWEKEDKLFQKDNATDMTNGVWMLMKQYSIGVEEAKRRILGKAREHVAEFVKTLSQIHNRLDLSLDSRLFVEAMQYMISGNLMWGISTPRYHSDQSLDEMMVARMKYGWPNHREVTKLTSDLENRGTKRTHQDDTEGVQSVKRFNGASTKNGINGTNGINGLNGINGSNGVKIKRHKNKEYSGALTKDSDLVLNMDLNGLSSAIICAPADYIGSLPSKGIRDNVADALSIWLDVPAKELNQIKRAINLLHNASLMLDDVQDGSVLRRAQPTTHTVFGPAQTINSAGHQIIQAMNEIRKLGSDDCLDIFSEELEKLYVGQSHDLYWVYNDSCSPTIEDYFKMVDYKTGGLFNMLARLMTAKSSSSSSPDLTALVGLLGRYFQIRDDYMNLTSADYTVEKGFCEDLDEGKFSITLLHALSAAPEPEALLLRNLMSGRRNDGKLSVVQKNLALSIIEGARSLEYTAAVLQKLYKAIVRELESTERQFGENKPFRFLLSLLKV
Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene methyl phomopsenonate . At first, the universal precursor of diterpene, geranylgeranyl diphosphate (GGPP) is provided and is cyclized by the unusual bifunctional terpene synthase PaPS to give phomopsene . The C-terminal prenyltransferase domain of PaPS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase domain catalyzes the cyclization of GGPP to phomopsene . Since the oxidation of a methylgroup to a carboxyl group is frequently catalyzed by a cytochrome P450 monooxygenase, the C-16 methyl group would be oxidized by the cluster-specific cytochrome P450 monooxygenase ORF3 (Probable). Subsequently, oxidation of the allylic position and methylation of the carboxyl group may give methyl phomopsenonate (Probable). Although further study is necessary to identify genes such as a monooxygenase and a methyltransferase, the predicted functions of genes on the cluster are correlated with the structure of methyl phomopsenonate (Probable).
P9WEV6
A8GAP2
DXS_SERP5
1-deoxyxylulose-5-phosphate synthase
Serratia
MSLDIAKYPTLALAENPDELRSLPKESLPKLCDELRQYLLDSVSRSSGHFASGLGTVELTVALHYVYQTPFDHLVWDVGHQAYPHKILTGRRDKIATIRQKNGLHPFPWRAESEYDVLSVGHSSTSISAGLGMAVAAAREGKNRRTVCVIGDGAITAGMAFEAMNHAGDIDPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSTLREGGKKVLSGLPPIKELVKRTEEHLKGMVVPGTLFEELGFNYIGPVDGHDVQGLVATLKNMRDLKGPQLLHIMTKKGRGYAPAEKDPISFHAVPKFDPASGTLPKSAGGLPTYSKVFGDWLCETAAKDSSLMAITPAMREGSGMVQFSRDYPQQYFDVAIAEQHAVTFAAGLAIGGYKPVVAIYSTFLQRAYDQLIHDVAIQKLPVMFAIDRGGIVGADGQTHQGAFDLSFMRCIPTMVIMTPSDENECRQMLYTGYHYNEGPSAVRYPRGNGTGAPLEPLNSLPIGKGVVRREGEKLAILNFGTLLPEAAQVAETLNATLVDMRFVKPLDEQLILELAASHDALVTLEENAIMGGAGSGVNELLMARRRVVPVLNIGLPDFFVSQGSQEEVRSDLGLDAAGIQRQIEVWLAQ
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).
A8GAP2
A0QVY5
LEXA_MYCS2
LexA repressor
Mycolicibacterium
MSDDTGEFTDGSTESPADADGAGRRRAVDNGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRAADDPAAAAVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRARGQVWLMPHNPAYDPIPGNEAAVLGKVVTVIRKI
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.
A0QVY5