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Full Name
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2.75k
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5.51k
AlphaFoldDB
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C9K2Q3
BSC8_ALTBR
Geranylgeranyl diphosphate synthase
Alternaria sect. Brassicicola
MKYQFSIIVDPATYDNEGLSNGIDLRKNNFTHLEDRGAIRAQQDWATHIAPIKQFKGTLGHDYSFMTVCVPECIPIRLEIISYANEFAFMYDDDTELDTENNTSAENDKLMGTFLAGTQGWSPPQDQSSSGKTRILKQLFSEMMEIDKECAIATMKAWAEFLRVGSSRQHGTVFTRLKDYLPYRIKDVGEMFWFGVVTFGMALHIPDHEMDACHKLMEPAWIAVGLANDVFSWPKERDASQRLGRTHVVNAVWVVMQEHGFSQEQARQYCRELAAQFVAQYLDNIRNIKNEESISPDLRTYVEAMQYSISGNVIWSKFCPRYNPEKRFNQTQLDWMQNGLPSTVELDGASNTSSSFLSTSTHGSPASGSQTTIESKDGWTADSSGIVSLLLNCSLPPLSHKVISAPLTYVDSLPSKGTRDMFLDALNHWLHVDEQRASQVKMAIRMLHNASLMLDDVQDGSRLRRSKPSAHRVFGVAQTTNSAAFLVNESIKLIRELAGDQGVAAVLEKLTSLFVGQAQDLHSSRNLSPPSLTEYIQTIDQKTSALFELASRLMCLCSTATVVPNSSLSRFCILLGRFFQIRDDYQNLTSPEYTKQKGFCDDLDSGTYTLPLVYAISQQSENFLLQNLLSTRLAEGTLDDDQKRLALDQMQLVKTNEFLRKILDSLYDELRAELQCISSSFASENPQMELMLMMLKL
Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
C9K2Q3
Q3Z976
RL22_DEHM1
50S ribosomal protein L22
Dehalococcoides
MEVKAIVKDTGYSALKVRLCVDMVRGKKVSEAITMLRFMTSPTAKVVSKVIKSAAANAENNFQMNPADLKISQIYADEARMLKRMRPQARGRVSPILKRSSHITVVVAD
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Q3Z976
P20944
CD44_CRIGR
Phagocytic glycoprotein I
Cricetulus
MDKFWWHAAWGLCLLPLSLAHEQIDLNITCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMVMALSKGFETCRYGFIEGHVVIPRIQPNAICAANHTGVYILTSNTSHYDTYCFNASAPLEEDCTSVTDLPNSFEGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNTTDDDVSSGSSSEKSTSGGYVFHTYLPTIHSTADQDDPYFIGSTMATRDQDSSMDPRGNSLTVTDGSKLTEHSSGNQDSGLNSTSRPGGKPRVPEWLIVLASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGKVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQFMTADETRNLQNVDMKIGV
Cell-surface receptor that plays a role in cell-cell interactions, as well as cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
P20944
P49188
CRF_XENLA
Corticotropin-releasing hormone
Xenopus
MKFQLWVSTGILLVSLLPCHECRAFIKSPASSPGALLPALSNSQPFLLRMGEEYFLRLGNLHKHSPGSFPEASAGNFVRAVQQLQAQQWSSQPGMRAASLDGADSPYSAQEDPTEKAKRAEEPPISLDLTFHLLREVLEMARAEQIAQQAHSNRKLMDIIGK
This hormone from hypothalamus regulates the release of corticotropin from pituitary gland.
P49188
Q5LPK1
GATB_RUEPO
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Ruegeria
MLDLTFETPKPKTIAGAKHDWELVIGMEVHAQVASQAKLFSGASTAFGAEPNSNVSFVDAAMPGMLPVINEFCVEQAVRTGLGLKAEINLKSAFDRKNYFYPDLPQGYQISQLYHPIVGEGEVLVEMGDGTARRVRIERIHMEQDAGKSIHDMDPNMSFVDLNRTGVCLMEIVSRPDIRGPEEAAAYIAKLRQILRYLGTCDGNMQNGNLRADVNVSICRPGAYEKYQETQDFSHLGTRCEIKNMNSMRFIQAAIEYEARRQIAIVEAGGEVDQETRLYDPDKNETRSMRSKEEAHDYRYFPDPDLLPLEIEQAWVDDIAASLPELPDDKKARFIKEFGLTDYDASVLTAEVESARYFEEVAQGRNGKLAANWVINELFGRLKKEDHDITDSPVSPSQLGGIIDLIASDAISGKIAKDLFEIVYTEGGDPAEIVEARGMKQVTDTGAIEAALDEIIAANPAQVEKAKVNPKLAGWFVGQVMKATGGKANPGVVNQMVSKKLNG
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).
Q5LPK1
Q46L69
RS15_PROMT
30S ribosomal protein S15
Prochlorococcus
MSLGTEEKQNLINTHQVHPTDTGSAEVQVAMLTTRISKLSTHLQGNIHDFSSRQGLLKMIGQRKRLLGYVRSKSEKRYTELIEKLAIRG
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Q46L69
P11987
MEMG_METCA
Methane hydroxylase
Methylococcus
MAKLGIHSNDTRDAWVNKIAQLNTLEKAAEMLKQFRMDHTTPFRNSYELDNDYLWIEAKLEEKVAVLKARAFNEVDFRHKTAFGEDAKSVLDGTVAKMNAAKDKWEAEKIHIGFRQAYKPPIMPVNYFLDGERQLGTRLMELRNLNYYDTPLEELRKQRGVRVVHLQSPH
Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
P11987
A8F801
PURA_PSELT
null
Pseudothermotoga
MLKAAVIGLQWGDEGKGKVVTYLSRRYDCVVRYSGGSNAGHTVDYGNFKMVHHLLPSADIKKQKMMYIGPGVVVDLDVLLEEIDQINNLIPESRSLLRISKQAHVVIPIYRDLDEKIDSSRANQIGTTRRGIGISYANRAMRCGLRLEDFETPARAESFLNEISRTWSIKFDVKMILDSLIEKYNKIRDLLIDSSEAVRVLKEKDLLFEGTQGVLLDVDMGTYPYVTSTNCSTTGIQPGFGYPVQVDKIFGVMKAYTTRVGEGPFPTELKDEVGENLRRLGSEYGATTRRPRRCGWLDLVLIKYAIETSACNALIMTKADILSGFEKIPICMGYKIGGKFYTQINNTAHLTEIEPVYEEIKGWKSLHSKEFDDFIYKIERELGLKFAYISTGPKIEEITEL
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.
A8F801
Q8EPQ8
QUEA_OCEIH
Queuosine biosynthesis protein QueA
Oceanobacillus
MQIEDFDFHLPEELIAQTPLKDRTSSRLCVLDKQTSEITHRSFKDITTYLQAGDCLVLNDTKVLPARLYGVKSDTGAKIEVLLLHQQEEDTWEVLVKPAKKVKVGTEIIFGNGKLKATCIDLKDHGGRIMTFSYTGIFYEILDQLGEMPLPPYIKEQLPEQDRYQTVYAKEKGSAAAPTAGLHFTDKLLEDIKAMGVNIVFVTLHVGLGTFRPVSVDSVEDHDMHSEFYSMSESAAKTLNEAKAAGRRIISVGTTSTRTLETIVRDHDGKFVATRGWTDIFIYPPYKFRAIDGLITNFHLPKSTLIMMISALAGKEAILHAYNEAVKEEYRFFSFGDAMLIL
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Q8EPQ8
Q557H3
VP35L_DICDI
VPS35 endosomal protein sorting factor-like
Dictyostelium
MAERQSASSPTPSSPPQQQQQTPQQPPQYLLNSKKNFKVKVLNGREVERHPLNSITKTEDTGKPKQSSLSSNASSLQSAAAAASSSTATTDIDPLNNNNNNNTDIDPLNNPLEKKHDPLSETIATMGGLKLIKENHLTNYVDENFMPWDTLKPSILQQYTSDDSNPIQVSFMSTGTSGKIKIPINRLNKILEELEQDKEDSKSTQFSQPDIIMDLETLHSELLKAWAAEERVRSLKIAIQTAKLLSDTSLIKFYPSKFVIATEILDTFGNLVYDRIKKRLQSSKESKNHEILLKEQAKETCRNWFYKIASIRELLPRLFVEISILKCYEFIQGDVNTEPKQVINRISEMIRGIGNPLVANYIRAYLTRRSFDLCPEYKKFVIQLLKDFVFTQKSYEKSKYLENTLSMYRITLTDYMGLYSPSLEWLLQCLAHKATPETLEEVLELFRESKNSLLLNHIISSFPPEYICSNSTMFSNFIKDADTLSYPKYQLYSTFGVNLVLGQPPKNQILSILNDVWKVVTNFENIKDYISVAEVFIEYVLTHCSEKETDVFLKDILRHIIPDKGYETIQSHLQSIVLKIFTHISDFGKLVSFTNFLPLLDLFNGESQKQISRSTLEALSTSKVMTSDPILINTFLTYGKALHDSLNSLSFQDEVRQVTQLVVNCINKIDFGRDVEKQLNFYVECRQTFINFDGVKNRLVYGVCEICEKTLNLVKGKHTPKTTSFIRACVAYCFITIPSIDDIFLKMNLYLVSSSVALQNQALSQADALLKAAITFIQEIPPILEFKQVKSTEDWTISYVSDFISLLVVTPGHPESGPFYLVKALYKVIKEYQWESSSTAKSKLFIQLLLLCSSWAQTSLPYHIEKVESNDQLFTEDPEFNTELTEFYNSLIKEILYDLNLLKDEPDNLTQKKVGIICIDLINALLNVGELNSKTASLIFNLYNMAKKIIPSTCFNEITYLKNTLAFIGTLESKMGQDIFNKLSQQQ
Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos.
Q557H3
A4YCW6
RL3_METS5
50S ribosomal protein L3
Metallosphaera
MGHRKLSSPRRGSAGLRPRKRSEELLPSPRSYPEVNLPNPVTLGFVGYKVGMTHIFMIDEDRSSSMFGKEIYVPVTVLETPPIYVLALRAYGLNNRGEHSVMGEVWGDLGDFGKFITRRIRGLKIDKEKKEHQLKDIESNLESVSYFRLLVSTQPHLIPALGKKTPDIVEVQIGGGNTKNQLEYGLKLLGNTLSVRDVFKEGQLMDIIGVTKGHGFQGVIKRYGVQELPRWHKHRKGSRKVGTKGPSLGTPSYVPQPGQMGFHRRTEYNKRILKISDDTKLINPKGGFVRYGLVKNTYLLVQGSTIGSIKRPLFLRYPIRPYSAQLPVPKVTYVDVNSKQG
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
A4YCW6
Q3SH78
GLGB_THIDA
Glycogen branching enzyme
Thiobacillus
MRKLVEATQAGSEASVALAPSAPIQRLQAGLHHDPFEVLGVHVQPDGSKLVRAFLPAAEAVEVAGVRMTRVPGTDCFERLLPPGTALEAHPLLTWQDKRSGAWQRLRSPYSFAPQLGEMDLYLFGEGRHFEIWKVLGARVKTVDGVTGCLFAVWAPAVLRVSVVGDFNDWDGRRHPMRCRGVSGVWELFIPGLEAGHAYKYEILGRHGERVTKTDPYARQMFLRPETTSRVPDERPYAWGDAEWLAARTRFDWQHRPMSVYEVHPGSWRRRADGSFYSWRELTAELIPYVRDLGYTHIELLPVAEHPFDASWGYQVSGYYAATARFGSPDDLRAFVDACHQAGLGVLLDWVPGHFPKDDFALARFTGEPLYEHADPRRGEHQDWGTLVFDFGRNEVRNFLVANALYWLEEFHIDGLRVDAVASMLYLDYSRRHGEWLPNQHGGRENLEAIHFLHEVNAEVHARFPGAITIAEESTAWPAVSRPIELGGLGFSMKWNMGWMNDTLDYIEKEPVYRKYQHNQLTFSQMYAWSENFVLPLSHDEVVHLKKSLLDKMPGDRWQRFANLRLLYAWQYAHPGKKLLFMGGEFGQWNEWREAGQLDWVLLGFPEHDGIRALLRDLNRLYRDEAALHFWDFDPRGFRWIDCHDADQSVLSLVREGPDGAPPIVVLLNFTPVPRHGYRIGVPRAGAWCEVLNSDSMYYGGSNLGNGKPLYPAAVPWMGFGQSIEVTLPPLGAIFLKPCP
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Q3SH78
Q03ZG8
RECR_LEUMM
Recombination protein RecR
Leuconostoc
MQYPEPIAKLIDSYTKLPGIGPKTATRLAFYTLGMNEEDVQDFSKALISAKTDLTFCSICGNITATDTDPCVICRDQSRDQSTVFVVENSRDVMAMENTRDYHGLYHVLNGVISPSAGTGPEDINLPSLIRRLSEHEEIKEVIVGTNANAEGEATAMYLARLLKPAGIAVTRLAHGLAVGSDIDYADELTLIKAVQGRTKL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q03ZG8
Q9BXA5
SUCR1_HUMAN
P2Y purinoceptor 1-like
Homo
MLGIMAWNATCKNWLAAEAALEKYYLSIFYGIEFVVGVLGNTIVVYGYIFSLKNWNSSNIYLFNLSVSDLAFLCTLPMLIRSYANGNWIYGDVLCISNRYVLHANLYTSILFLTFISIDRYLIIKYPFREHLLQKKEFAILISLAIWVLVTLELLPILPLINPVITDNGTTCNDFASSGDPNYNLIYSMCLTLLGFLIPLFVMCFFYYKIALFLKQRNRQVATALPLEKPLNLVIMAVVIFSVLFTPYHVMRNVRIASRLGSWKQYQCTQVVINSFYIVTRPLAFLNSVINPVFYFLLGDHFRDMLMNQLRHNFKSLTSFSRWAHELLLSFREK
Receptor for succinate.
Q9BXA5
B3EP06
MDH_CHLPB
Malate dehydrogenase
Chlorobium
MKITVIGAGHVGATAAHRIAEQQLANTVVLFDILEGIPQGKALDMYESGPVGLFDTKVYGTTDYNDTADSDIILITAGMARKPGMSREDLLMKNATIVKEVTDQVVRFSKNPIIIMVSNPLDIMTHVGYIRSKLPKERVLGMAGVLDSARFRSFIAEELNVSMRDINAFVLGGHGDSMVPVVKYTSVAGIPLTELMAQDTIEQLVDRTRKGGAEIVNYLKNGSAYYAPASSAVEMIDAIVNDRKRILPCSALLEGQYGINNVYIGAPVKLGKNGIEQILEIDLDAPELDALRKSAAIVEENCNNLASLLA
Catalyzes the reversible oxidation of malate to oxaloacetate.
B3EP06
A9BPU6
ATPG_DELAS
F-ATPase gamma subunit
Delftia
MAAGKEIRGKIKSVENTKKITKAMEMVAASKMRKAQERMLAARPYSEKIRNIAVHLGQANPEYVHPFMQVNGDAKTAGVIVVTTDKGLCGGMNTNVLRAVTAKLRELQDQGVSAEAVAIGNKGLGFLNRVGAKVVSHATGLGDTPHLEKLIGPVKVLLDAYAAGKLSAVYLSYTKFINTMKQESVVEQLLPLSSESMQAEKTSGHSWDYIYEPDAQSVIDELLVRYAESLVYQAVAENMASEQSARMVAMKAATDNAGNVISELKLVYNKTRQAAITTELSEIVAGAAAV
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.
A9BPU6
Q1MIC8
RS14_RHIL3
30S ribosomal protein S14
Rhizobium
MAKTSAVEKNKRRRTTVANQAAKRAGLKAIIMNQALPIEERFKASIKLASLPRDGSKTRIRNRCEVSGRPRAYYRKLRMSRIALRELGNLGKVPGIVKSSW
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.
Q1MIC8
A4SD60
MEND_CHLPM
Menaquinone biosynthesis protein MenD
Chlorobium
MNNPQLTTVWSSVMVEELIRQGASFFCISPGSRSTPLTAAIARNPEASWKMFPDERSAGFFALGHARATGFPAVLVCTSGTAVANYLPAVVEASNDRIPMLILSADRPFELRECGANQTIRQNGIFGTFTRWQMELPEPSTSIPLQSLLSTIAHGVEKSLNSPRGPVHLNQPFREPFEPESCSTPEPWLEPLQAWQTGRRPSTVAAQPEKHPDMDSMRTLRELTGNARQPLIIAGNSTDENDSHAIAELADDLQVPLYADMTSGLRFSSSILPWQQAFASPEFRNAFRPDLVIHFGGGLISRHPSDALKQWKPDHLAVIRNHPGRYSPDHSVTLSIEASLRLTADALRGCRTGASALMAPAKRFFTEADREIAAATAPDLPVSEIGTARIVSELLPPDHLLFLSNSMPVRAMDSYAHTGKENPIKTGTNRGASGIDGIISTAAGFAEGHGQPLCLMIGDLAFLHDLNALSLINSLRVPIQLILLNNNGGGIFSFLPVSEFDDIFEPNFATPQNFSGRPAAAMFGLDYTAPLTNSEFRESLLSALNSNRSTIIEVVCSRSENVRLHRALQARLGLLATEAFFIP
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
A4SD60
O75385
ULK1_HUMAN
Unc-51-like kinase 1
Homo
MEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPSVRKSPPVPVPSYPSSGSGSSSSSSSTSHLASPPSLGEMQQLQKTLASPADTAGFLHSSRDSGGSKDSSCDTDDFVMVPAQFPGDLVAEAPSAKPPPDSLMCSGSSLVASAGLESHGRTPSPSPPCSSSPSPSGRAGPFSSSRCGASVPIPVPTQVQNYQRIERNLQSPTQFQTPRSSAIRRSGSTSPLGFARASPSPPAHAEHGGVLARKMSLGGGRPYTPSPQVGTIPERPGWSGTPSPQGAEMRGGRSPRPGSSAPEHSPRTSGLGCRLHSAPNLSDLHVVRPKLPKPPTDPLGAVFSPPQASPPQPSHGLQSCRNLRGSPKLPDFLQRNPLPPILGSPTKAVPSFDFPKTPSSQNLLALLARQGVVMTPPRNRTLPDLSEVGPFHGQPLGPGLRPGEDPKGPFGRSFSTSRLTDLLLKAAFGTQAPDPGSTESLQEKPMEIAPSAGFGGSLHPGARAGGTSSPSPVVFTVGSPPSGSTPPQGPRTRMFSAGPTGSASSSARHLVPGPCSEAPAPELPAPGHGCSFADPITANLEGAVTFEAPDLPEETLMEQEHTEILRGLRFTLLFVQHVLEIAALKGSASEAAGGPEYQLQESVVADQISLLSREWGFAEQLVLYLKVAELLSSGLQSAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDRIHSITAERLIFSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHMLSDQADIENVTKCKLCIERRLSALLTGICA
Serine/threonine-protein kinase involved in autophagy in response to starvation . Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes . Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR . Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity . May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences . Plays a role early in neuronal differentiation and is required for granule cell axon formation . May also phosphorylate SESN2 and SQSTM1 to regulate autophagy . Phosphorylates FLCN, promoting autophagy . Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation . Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B .
O75385
Q9F2F9
ELMGT_STROV
Elloramycin glycosyltransferase ElmGT
Streptomyces
MRVLAVATPALGHLFPAVPLLWALRARGDEVLVVTGGDALRVAEAGLPVVDALPGETLTTLFGAYQETDPAFFVALRRSPMTTLRDLAPVLAYLAGRLLEPARRAAERWRPDAILATHGQAAGAVVAAEHGIPLVEHGFGFVRSDGAQEAVRQLLAERLGPAGSEPPPERYFLDIAVPSMTSAIEGMSLRAVPYNGGAVLPLSGASVGGRPPRPRVLVTAGTQLLHTHGAGALAWLPEVAAGHEAEFLLAAGGADLRDLGRLPPHVRVLDWTPLATVLPTCSAVVHHGGSGTTLAALAAGVPQLVSPALADNHINARAVADRGAGLETAVPDATTLTALLREPAFAKAAREVADELRSLPAPADVAARLHTAFGLPTTQGDA
Glycosyltransferase that transfers an L-rhamnose moiety from dTDP-L-rhamnose to the elloramycin aglycone 8-demethyl-tetracenomycin C (8DMTC) in elloramycin biosynthesis, an antitumor polyketide. Possesses donor substrate flexibility: able to transfer at least 11 different sugars to 8DMTC, such as NDP-D-glucose, as well as NDP-L-digitoxose, including both L- and D-isomeric forms of some sugars.
Q9F2F9
G1UH28
CHIT_PUNGR
Pomegranate seed chitinase
Punica
MAKTLPFSRALLLSLSILLVARAISAGDIAIYWGQNGGEGTLASTCDTGRYAYVIVSFVTTFGNFRAPVVNLAGHCDPAAGTCTGLSDEIRSCQGKDIKVLMSIGGGAGDYSLVSEADADNFADYLWNNFLGGQSSSRPLGDAVLDGIDFDIELGTTTFYDTLARALSSRSTQAAKVYLTAAPQCPHPDSHLDAALNTGLFDNVWIQFYNNPLAQCQYSSGNTNDILSSWNTWTSSTTAGKIFLGLPAAPEAAGSGYIPPDVLTGQILPQIKTSAKYGGVMLYSKFYDTTYSTTIKDQV
Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination.
G1UH28
G5EGK8
PP2A_CAEEL
Serine/threonine-protein phosphatase 2A catalytic subunit
Caenorhabditis
MAAAPPSADPLDKALIVDVDQWIEQLYECKPLSENQVKTLCEKAKEILEKEPNVQEVRCPVTVCGDVHGQFHDLMELFKMGGKSPDTNYLFMGDYVDRGYYSVETVSLLVCLKIRYKDRVTLLRGNHESRQITQVYGFYDECLRKYGNSNVWKYFTDLFDCFPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHSNGLTLISRAHQLVMEGYNWSHDRNVVTVFSAPNYCYRCGNQAAMVELDDDLKYSFLQFDPAPRRGEPHVTRRTPDYFL
Protein phosphatase which plays an essential role in early embryonic cell division . Probably together with constant regulatory subunit paa-1 and regulatory subunit sur-6, positively regulates centriole duplication by preventing the degradation of sas-5 and kinase zyg-1 . In addition, plays a role in the recruitment of sas-6 and maybe sas-5 to centrioles and may dephosphorylate sas-5 and zyg-1 negative regulator szy-20 . During vulva development, may play a role with regulatory subunits paa-1 and sur-6 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation . In association with regulatory subunit rsa-1 and probably paa-1, regulates microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules . Plays a negative role in axon guidance probably by dephosphorylating unc-51, unc-14 and vab-8 .
G5EGK8
O04609
WRK22_ARATH
WRKY DNA-binding protein 22
Arabidopsis
MADDWDLHAVVRGCSAVSSSATTTVYSPGVSSHTNPIFTVGRQSNAVSFGEIRDLYTPFTQESVVSSFSCINYPEEPRKPQNQKRPLSLSASSGSVTSKPSGSNTSRSKRRKIQHKKVCHVAAEALNSDVWAWRKYGQKPIKGSPYPRGYYRCSTSKGCLARKQVERNRSDPKMFIVTYTAEHNHPAPTHRNSLAGSTRQKPSDQQTSKSPTTTIATYSSSPVTSADEFVLPVEDHLAVGDLDGEEDLLSLSDTVVSDDFFDGLEEFAAGDSFSGNSAPASFDLSWVVNSAATTTGGI
Transcription factor involved in the expression of defense genes in innate immune response of plants. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Activates WRKY 29, SIRK and its own promoters.
O04609
A9II17
NUOH_BORPD
NDH-1 subunit H
Bordetella
MEWLDILESHGQALLGPTAWLVLWTIVKIVVIAVPIILCVAYLTYWERKMIGWMHVRLGPTRVGFRGLLQPFADVFKLLTKEVVVPTQANKILFVVAPVVTLMPALAAWAVVPFGPEVVLANVNAGLLYVMAITSIGVYGVIVAGWASNSKYAFLGALRASAQMVSYELAIGFVLVTVLLVSGSLNMSEIVLGQTRGWFAEHGLTFLSWNWLPLLPLFVIYVISAVAETNRHPFDVVEGESEIVAGHMVEYSGMAFALFFLGEYANMILLSCMASIMFLGGWTSPIDIAPLTWIPGWIWLGIKTFCVVSLFVWFRASFPRYRYDQIMRLGWKIFIPLTGVWLVVVAIWMQTPWNIWR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
A9II17
P29068
CBPT_THEVU
Carboxypeptidase T
Thermoactinomyces
MRKKWLSLSLVLVLIVACVPALGFSQNIENPSIFDLGIKLYKIDGVSTKEQRSAIASTGAAIEEVGKDYVKVLATPSEAKQIKQKGFTATVDTSLTTQDFPSYDSGYHNYNEMVNKINTVASNYPNIVKKFSIGKSYEGRELWAVKISDNVGTDENEPEVLYTALHHAREHLTVEMALYTLDLFTQNYNLDSRITNLVNNREIYIVFNINPDGGEYDISSGSYKSWRKNRQPNSGSSYVGTDLNRNYGYKWGCCGGSSGSPSSETYRGRSAFSAPETAAMRDFINSRVVGGKQQIKTLITFHTYSELILYPYGYTYTDVPSDMTQDDFNVFKTMANTMAQTNGYTPQQASDLYITDGDMTDWAYGQHKIFAFTFEMYPTSYNPGFYPPDEVIGRETSRNKEAVLYVAEKADCPYSVIGKSCSTK
Able to split off hydrophobic and basic amino acids with comparable efficiency.
P29068
Q5E7K1
RF3_ALIF1
Peptide chain release factor 3
Aliivibrio
MSFLQEVGKRRTFAIISHPDAGKTTITEKVLLFGNAIQKAGTVKGRGSNQHAKSDWMEMEKERGISVTTSVMQFPFNDCLVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDAAKGVEDRTRKLMEVTRLRDTPIVTFMNKLDREVRDPMEVLDEVESELGMACAPISWPIGCGKEFKGVYHIHRDETILYESGHGHEIQEVRTIKGLDNPELDATVGADLAESVREELELVMGACPEFDHELFLAGELTPVYFGTALGNFGVDHMLEGLTDWAPAPQTRQANERDVVATEDKFSGFVFKIQANMDPKHRDRIAFMRIVSGTYTQGMKMNHVRTGKNVSISDAVTFMAGDRSRAETAYAGDIIGLHNHGTIQIGDTFTQGESLKFSGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPLQNNDLIVGAVGVLQFDVVVARLKAEYNVEAIYEGVSVATARWVDCADGKKMDEFQRKNQANLALDGGDNLTYIAPTMVNLNLASERFPDVQFRATREH
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
Q5E7K1
B7LTW5
PDUL_ESCF3
Propanediol utilization protein PduL
Escherichia
MDKQLLETAVGKVLEEMRERPIPLGISNRHIHLSAQDFAHLFPGQSISVKKALMQPDQYAAEQTLTLVGPKGKLEKVRLLGPLRSASQVEVSRTDARTLGITAPLRMSGDLQGTPGVRLVSPFAELEITSGVIVAQRHIHMSPLDALILNVSHGDKVSVAIKGDERRLIFDNVAVRVSPDMRLEMHIDTDEANAAGADNPQVCAMLVNKS
Involved in 1,2-propanediol (1,2-PD) utilization within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
B7LTW5
P37293
NAT2_YEAST
Amino-terminal, alpha-amino, acetyltransferase 2
Saccharomyces
MMVPRISASPVFKRIFLRWGFVTLPIQKTVSHTLRRDFSAPCRSMVKCLLLRPGISVHSAQDRKFYSTEEKSSQFDENKSKSNNGKKNEPHGIKGLMAKYGYSALIVYILLTCVDLPLCFLGVHSLGEEKIKIYLNRGKQLIGMGEPDESKVIQDVRRKQAHREAVQAENADKVEDASRKTFNERWQEMKDSTLLAELLIAYGIHKSLIIVRVPLTAVLTPSFVKLLQRFGIDLMKKQKKVFQTMASGAKIRYKGNNPSDFIKNEGTALDITKRKPRTKGQKWFDGLM
Maybe involved in N-terminal acetylation of proteins. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
P37293
O83361
MURC_TREPA
UDP-N-acetylmuramoyl-L-alanine synthetase
Treponema
MKRGTLPKDVSGIKIHMIGIKGTGMSALAELLCARGARVSGSDVADVFYTDRILARLGVPVRTPFSCQNLADAPDVVIHSAAYVPEENDELAEAYRRGIPTLTYPEALGDISCARFSCGIAGVHGKTTTTAMIAQMVKELRLDASVLVGSAVSGNNDSCVVLNGDTFFIAETCEYRRHFLHFHPQKIVLTSVEHDHQDYYSSYEDILAAYFHYIDRLPQFGELFYCVDDQGVREVVQLAFFSRPDLVYVPYGERAWGDYGVSIHGVQDRKISFSLRGFAGEFYVALPGEHSVLNATGALALALSLVKKQYGEVTVEHLTALRKVLALFQGCRRRSEVLGEVRGILFMDDYGHHPTAIKKTLRGLKTFFPERRIVVDFMSHTYSRTAALLTEFAESFQDADVVILHEIYASAREVYQGEVNGEHLFELTKRKHRRVYYYEAVMQAVPFLQAELKEGDLFVTLGAGDNCKLGEVLFNYFKEEV
Cell wall formation.
O83361
A4J778
METRE_DESRM
Metal reductase
Desulforamulus
MSILFSPAQIGTLQLRNRIIMTPMHLGYTPNGEVTDQLIEFYRVRARGGAGLIVVGGCGIDRIGNAYGMTQLDDDRFIPGLRRLADAVQAEGAKIVAQLYQAGRYAHSALTGQPAVAPSPIPSKLTGETPVELTEEKIAEIVASFAKAAKRAKTAGFDGVEIIASAGYLISQFLSPLTNKRTDRYGGDLQARMTFGLEVVAAVREAVGSDYPIIVRVAGNDFMPGSHTNTEAQVFCQAMEKSGVNAINVTGGWHETQVPQITMNVPPGAYAYLAYGIKQAVSIPVIACNRINTPDLAEAILQEGKADFIGMARSLMADPELPNKAMSGHPEQIRPCIGCNQGCLDHVFRMKPVSCLVNAEAGREAELSLTPTSQPGKILVIGAGAAGLEFARVAALRGHKVTIWEESDQAGGQLILAAAPPGRKDFLHLRTYLVNACRDLGVEIQYHTKATPENILSAVQEGKFNRVVIATGAHPITPPIPIEEGVKVIQAWDVLAGRSKAGQNIIIVGGGAVGVETALLLAESGTLDNETLRFLMLQQAETEKELYRLLIQGTKKITVLEMANGIGRDIGPSTRWSMLADLKRHQVNCLDETTVLEIRREGVLVKNAGTQKILPADTVILAVGSRSQNELYQALQGKVEYLSIIGDAIKPRKVMDAIHQAYNEAIKY
Metal reductase able to reduce Fe(III)-chelates to Fe(II)-chelates, as well as soluble Cr(VI) and U(VI), using NADH as electron donor. Cannot use NADPH as an electron donor. Is unable to reduce riboflavin and FMN with NADH as electron donor. May have an in vivo role in metal reduction in D.reducens, which is an organism capable of reducing contaminant heavy metals and radionuclides.
A4J778
B5Y6R9
GCH4_COPPD
GTP cyclohydrolase FolE2
Coprothermobacter
MRDVQSERDPRNVPLDYVGIENVRLPITVRTKEGGKQPTVGTFSIGVDFPHSFRGTHMSRFMEVLYQHLEEISQTRLRVTLEDIKERLKATKAMIEVAFPFAIKKSTPVTKLETVMYVDASFKAELNSTRGYVVTSTVTVPVHSLCPCSRDISEFGAHNQRVDVTVSWQGDLWIEDVIALVESSASQPLYPLLKRPDEKYVTEKAYLNPKFVEDIAKDLFLKLDPLSPCFRIKVVSYESIHPHNAVAIKEKRAEVSESSVRSNDQEHRDCT
Converts GTP to 7,8-dihydroneopterin triphosphate.
B5Y6R9
Q6P7Q1
BABA2_RAT
Brain and reproductive organ-expressed protein
Rattus
MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQQYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKEFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL
Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Within the BRISC complex, acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. The BRISC complex plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect.
Q6P7Q1
Q8P2R7
TADA_STRP8
tRNA-specific adenosine deaminase
Streptococcus
MPYSLEEQTYFMQEALKEAEKSLQKAEIPIGCVIVKDGEIIGRGHNAREESNQAIMHAEMMAINEANAHEGNWRLLDTTLFVTIEPCVMCSGAIGLARIPHVIYGASNQKFGGADSLYQILTDERLNHRVQVERGLLAADCANIMQTFFRQGRERKKNS
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
Q8P2R7
A3CVJ2
PCNA_METMJ
Proliferating cell nuclear antigen homolog
Methanoculleus
MLKATIDAEIFRESIDAIAALVTECRLHTAEDQIRTRSVDTANVAMVSLELQSTAFNSFSATAGELGLDIAKMKNIIGMMGKGDALTLTLLDEERKLELSFGGYRYSISLLDVNTIRKDPNPPGIDLPGKAVVPGDALNNAIKAAAVISDKIALGIDPDAMTFYMEAEGDTDHIKLALGEDELVALSPVQARSLFSIDYLKDMGRVMARADKVEVYLGIDHPVRFVFDIADGNGRVEYLLAPRIEAD
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
A3CVJ2
Q8VF12
OL495_MOUSE
Olfactory receptor 204-37
Mus
MAFLEDGNHTIVTEFILLGLTDDPVLRDILFTIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASVDIGISSSVTPNMLANFLVKPNTISYIGCSIQFTSAVFLATVECFLLAAMAYDRFVAICNPLLYSTKMSREACIQLVVGSYIQGLLNASFFTLSFFSLIFCGPNRINHFYCDLAPLVELSCSDVTLAVVITSISAGFITLTTVFVIAISYSCIFITIMKMHSTESRYKAFSTCTSHLTAVTLFYGTTMFIYVMPKSSYSTDQNKVLSVFYMVVIPMLNPLIYSLRNNEIKGALKRYLGKKIFSYGNLFCKTHYNDTHQV
Potential odorant receptor.
Q8VF12
C1CTY2
MUTS_STRZT
DNA mismatch repair protein MutS
Streptococcus
MAIEKLSPGMQQYVDIKKQYPDAFLLFRMGDFYELFYEDAVNAAQILEISLTSRNKNADNPIPMAGVPYHSAQQYIDVLIEQGYKVAIAEQMEDPKQAVGVVKREVVQVITPGTVVDSSKPDSQNNFLVSIDREGNQFGLAYMDLVTGDFYVTGLLDFTLVCGEIRNLKAREVVLGYDLSEEEEQILSRQMNLVLSYEKESFEDLHLLDLRLATVEQTASSKLLQYVHRTQMRELNHLKPVIRYEIKDFLQMDYATKASLDLVENARSGKKQGSLFWLLDETKTAMGMRLLRSWIHRPLIDKERIVQRQEVVQVFLDHFFERSDLTDSLKGVYDIERLASRVSFGKTNPKDLLQLATTLSSVPRIRAILEGMEQPTLAYLIAQLDAIPELESLISAAIAPEAPHVITDGGIIRTGFDETLDKYRCVLREGTSWIAEIEAKERENSGISTLKIDYNKKDGYYFHVTNSQLGNVPAHFFRKATLKNSERFGTEELARIEGDMLEAREKSANLEYEIFMRIREEVGKYIQRLQALAQGIATVDVLQSLAVVAETQHLIRPEFGDDSQIDIRKGRHAVVEKVMGAQTYIPNTIQMAEDTSIQLITGPNMSGKSTYMRQLAMTAVMAQLGSYVPAESAHLPIFDAIFTRIGAADDLVSGQSTFMVEMMEANNAISHATKNSLILFDELGRGTATYDGMALAQSIIEYIHEHIGAKTLFATHYHELTSLESSLQHLVNVHVATLEQDGQVTFLHKIEPGPADKSYGIHVAKIAGLPADLLARADKILTQLENQGTESPPPMRQTSAVTEHISLFDRAEEHPILAELAKLDVYNMTPMQVMNVLVELKQKL
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
C1CTY2
Q4UJN0
LPXB_RICFE
Lipid-A-disaccharide synthase
spotted fever group
MTKIYFIAGETSGDFIGGRIIQHLKDNIEIKCMGVGGKYMEEAGSFKSLFSITSINLMGFVEILPHIFKLKKLIDKTVEDITNSRADLLITIDSPGFTYRVAKRVRKLLPKLKMIHIVAPSVWAYKEDRAVKYAQIYDCLFALLPFEPPYFTRLGLDCRYIGHPIMEQEFYSDKVALRKEFKIDENERVLCVTLGSRKGEILRHLPVFVSSIEEIFKSCNNLKVIFTLANPAHEAIIKPFLEDVKFNYLFSSERLKTYAVADAALAKSGTNTLEIAASGTPMIVAYKVNLISFFIIRLLIKIKYVTLINIIAGSEIIPEFIQFNCRASLISNKLQELLFNSKKAYEQVIESQKILQKLGFESNRSPSYIAAEIIKQEFLKPKIKLLKEKD
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q4UJN0
Q9Z8T3
RIMO_CHLPN
Ribosome maturation factor RimO
Chlamydia
MTTKSLGSFNSVISKNKIHFISLGCSRNLVDSEVMLGILLKAGYESTNEIEDADYLILNTCAFLKSARDEAKDYLDHLIDVKKENAKIIVTGCMTSNHKDELKPWMSHIHYLLGSGDVENILSAIESRESGEKISAKSYIEMGEVPRQLSTPKHYAYLKVAEGCRKRCAFCIIPSIKGKLRSKPLDQILKEFRILVNKSVKEIILIAQDLGDYGKDLSTDRSSQLESLLHELLKEPGDYWLRMLYLYPDEVSDGIIDLMQSNPKLLPYVDIPLQHINDRILKQMRRTTSREQILGFLEKLRAKVPQVYIRSSVIVGFPGETQEEFQELADFIGEGWIDNLGIFLYSQEANTPAAELPDQIPEKVKESRLKILSQIQKRNVDKHNQKLIGEKIEAVIDNYHPETNLLLTARFYGQAPEVDPCIIVNEAKLVSHFGERCFIEITGTAGYDLVGRVVKKSQNQALLKTSKA
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
Q9Z8T3
Q8ZMF5
CYSN_SALTY
Sulfate adenylate transferase
Salmonella
MNTILAQQIANEGGVEAWMIAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTLQIYEDQLSSLHNDSKRHGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTERRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFISTLLGIKHLVVAINKMDLVDYREETFARIREDYLTFAEQLPGDLDIRFVPLSALEGDNVAAQSANMRWYSGPTLLEVLETVDIQRAVDRQPMRFPVQYVNRPNLDFRGYAGTLASGSVKVGERIKVLPSGVESSVARIVTFDGDKEEACAGEAITLVLNDDIDISRGDLLLAANETLAPARHAAIDVVWMAEQPLAPGQSYDVKLAGKKTRARIEAIRYQIDINNLTQRDVESLPLNGIGLVEMTFDEPLALDIYQQNPVTGGLIFIDRLSNVTVGAGMVRELDERGATPPVEYSAFELELNALVRRHFPHWDARDLLGDKHGAA
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Q8ZMF5
Q9LVB0
AHL6_ARATH
AT-hook motif nuclear-localized protein 6
Arabidopsis
MEEKGEISPSGVVTVKGDEALVPRTEFQQNPSFLQFVSPTTVVTPLPPPPAPSSAPVPTTVTPGSATASTGSDPTKKKRGRPRKYAPDGSLNPRFLRPTLSPTPISSSIPLSGDYQWKRGKAQQQHQPLEFVKKSHKFEYGSPAPTPPLPGLSCYVGANFTTHQFTVNGGEDVTMKVMPYSQQGSRAICILSATGSISNVTLGQPTNAGGTLTYEGRFEILSLSGSFMPTENGGTKGRAGGMSISLAGPNGNIFGGGLAGMLIAAGPVQVVMGSFIVMHQAEQNQKKKPRVMEAFAPPQPQAPPQLQQQQPPTFTITTVNSTSPSVNTVEEQKPQAYGGGIVRPMAQMPSSFQNDNSTMNNFTPAYHGYGNMNTGTTHKEEHEDEDGGDDDDDSGDTRSQSHSG
Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Q9LVB0
A4XVG4
LPXH_PSEMY
UDP-2,3-diacylglucosamine diphosphatase
Pseudomonas
MILLISDLHLEEKRPDITRAFLHFLATRARQAEALYILGDFFEVWIGDDGMTPFQHEIAGALRELSDSGTRIYLMHGNRDFLIGKRFCREAGCTLLGDPHRVQMNGEPVLLMHGDSLCTLDVGYMKLRRWLRNPLSLLILRNLPLATRQKLARKLRNESRAQTRMKASEIVDVTPEEVVRVMGEYDVRTLIHGHTHRPAVHELEVNGQPARRIVLGDWDRQGWALQVDGEGFNQAPFELTPA
Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A4XVG4
Q8FBP9
WECF_ECOL6
TDP-Fuc4NAc:lipid II Fuc4NAc transferase
Escherichia
MTVLIHVLGSDIPHHNRTVLRFFNDALAATSEHAREFMVAGKDDGLSDSCLALSVQFFPGKKSLAEAVIAKAKANRQQRFFFHGQFNPKLWLALLSGGIKPSQFFWHIWGADLYELSSGLRYKLFYPLRRLAQKRVGCVFATRGDLSFFAKTHPKVRGELLYFPTRMDPSLNTMANDRQREGKMTILVGNSGDRSNEHIAALRAVHQQFGDTVKVVVPMGYPPNNEAYIEEVRQAGLELFSEENLQVLSEKLEFDAYLTLLRQCDLGYFIFARQQGIGTLCLLIQAGIPCVLNRENPFWQDMTEQHLPVLFTTDDLNEDIVREAQRQLASVDKNTIAFFSPNYLQGWQRALAIAAGEVA
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis.
Q8FBP9
Q83HY0
ATPB_TROW8
F-ATPase subunit beta
Tropheryma
MTGDAVGRIVRVTGSVVDVEFSRNNLPGVFNALKTRVNRSGKEIEITLEVAQHLGDDLVRTVAMQSTDGLIRGQEVLDTGGHITVPVGDATKGRVFNVVGEVLNSNGEDIKFDEYWSIHRKPPEFSLLESKTQLFETGIKVIDLLTPYVQGGKIGLFGGAGVGKTVLIQEMIQRVAQDHGGVSVFAGVGERTREGNDLIREMQDAGVFDKTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSTLLGRIPSAVGYQPNLADEMGVLQERITSTRGHSITSLQAIYVPADDYTDPAPATTFAHLDATTELSREIASKGLYPAVDPLASTSRILDPKYIGKDHYRVAVTVKQILQRDKELREIIAILGIDELSEEDRVTVARARRIEQFLSQNTYMAKKFTGVDGSTVPLQETIDGFDAICRGDCDHIPEQAFFNVGGLEDVERKWSKLQKELG
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Q83HY0
P18296
CUT1_SCHPO
Separase
Schizosaccharomyces
MSTRSIVTSKVSWTPEKFISALSYPEHCSITLVKRLKASVKLKDLKQNISRDAPSWTFEHLFVAFKCAVSNLAKQWAELSTTDKEKTRRMFCTPSRLNTAHRPEVFYLLECCTYILEQMQVVTKNTSHLYDCIRSGVSICNRLLDMEIFEPAISLLMKTHKNLIILLTYRDHDAIPTATLLNPTLDVSEIQLESCLFVPMVPASYFLNIGTIVVTFQLNVLRCLSLSQINGLSLNTINNLQSEDGPFQWIERSFPSQVQLANSRREILARLLTRFSMIQNNALQSFKLLILSIALWLNILSSQRADDKEFDVNQLETRILQLFSKVVQLCKSEDIEGSILNKDMTQLHHLLENLSKESRLHILLQLSQLYYKYNDFQLSAAYVIRGYSLSFEDISFKLKFLLFSFRLSIHDNSICFPFNLIQELSSLQQLFVENALPYSEALHLLDSIERSFRLFNDSTVFDDTVFALNISEILSWILSSVVRDILVEDELLNLQLKIRKFLMFTFHIIRSFSELTKFQSSLEGCLNLAAYYEDAEFPQKLSNHLYNLCVKSSNVNYARECISLSIKIAVSHKLTNDETYLLKILKNFQLRYHDSLQLQEKCDVLHTTFNQLDLYVGTTSVGKSSVLDNILKRIFNSLTSINDSNIEKLLESISYSLLKLFFKCANEGSRYNASAALSFKLSLMLHEKEEVLLLKTNVSCVLANHGYNDIKFEEMVLCVIKGDQNLLEHNSNNNAKLALNESLLCSWENLLCYRRAEDDSRILTIIESWTIFISRFSSVISRCSFTDFEINSILNFFFCFLHTVEPSGKLTFELAFLEIFYELFNCLLHLQFSKYLVIIGTLLSDKYMTLGFSGKAHLFYTKCYSYLRQCKSSPFINFWNVSYGKYLILTGNTDKGILQLKKYSLSSEEDFNSNGLSRTVSLNLLLYERIQLSDALFQLGYTTVSLGFIMQNLKVIKGLFSKSSKEHFNGGKYITWRLFAVSAHSNVCAARIYEHMGQAREAEFFYRQACSISEKMPFSCFSATFQLRLCSLLTRAGKLEKGEKILFDLTEAMKSTDTYHKLLWNYGAAEVCATKSELDGAICHYSECVKLLEIIKSEYYLFFNRNREKSLTKGIKRLSLSSQPTFVTESNTTEFDDWSILQNTAANLLRLISMFELKRGNLEIAKALMTDSTKCSIASFFNIVSANILKSKLIVCEADSTLFGDPVLRTLPDSVISLPGISHKFQKNQSKTKALGENTGFRKGSKRLDYLRERLKINLQNVRLSCEIIFSNAYERSSVCVCREVNELISYSTIMQSALTTIGETTDVDSSSASFFLEIPKALGFHRRREAQKFRNQHKELHFSSLEQILNSRLSIPDVRTFQDNFIDSLPSIWNVVSITINNSGEDLFISKIRKGHSPLIFRLPLQRHNSRDADEEILVFTKAQTELFRIISKSNQMAQNGKHYTRREDKETWWKERRHLDQCLQQLLENIEISWLGGFKGIFNPHKIDTSLFAKFSSQFQNIIAKNFNMDKKTPVPTLSPEILELFITLGKPGYEGYEQLLEDLIYFILDIFQFRGLHFAYDEIDTDQLSMDLQDALNAYFNNYVSEENRSHTVLVLDKSVHQFPWESLPCLNRQSVSRVPSLSILRDILSQSFVVNGEYVEVRKEAGSYILNPSLDLKHTQEMFEHKLVEGGWKGLIASQPSNRDFIKMLSGNDFFLYFGHGGGEQYTTSYDLATLKRCAVTILMGCSSGALYECGSFEPWGTPLDYLSAGCPTLVANLWDVTDKDIDRFSLKMLESWGLFENKAPFVNSTSICTAVSESRSCCHLRYLNGAAPVIYGIPAYIIP
Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation.
P18296
Q7VQX1
HIS1_BLOFL
ATP phosphoribosyltransferase
Candidatus Blochmannia
MLDKSRLRIAMQKSGRLSKESQKLLEQCGIKINLQQQQLLAFAENMTIDIMRVRDDDIPGLIMDGVVDLGIIGENVLEEALLTRQSQGDNPCYVTLRRLDFGDCRLSMALPMDKPWNGPKCLQGKRIATSYPHLLKQYLDKLGINFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRSGNLSKTKQSLIDKLMIRIQGVIQARESKYIMLHAPAERLEEIINLLPGAESPTVLPLAGNQHRVAIYMVSNEALFWETMENLKNLGASSILVLPIEKMME
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q7VQX1
P20802
TBB_ACHKL
Beta-tubulin
Achlya
MRELVHIQGGQCGNQIGAKFWEVISDEHGVDPTGSYHGDSDLQLERINVYYNEATGTYVPRAILMDLEPGTMDSVRAGPYGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKIREEYPDRIMCTYSVCPSPKVSDTVVEPYNATLSVHQLVENADEVMCLDNEALYDICFRTLKLTNPTYGDLNHLVCAAMSGITTLLRFPGQLNSVLKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQQFDAKNMMCAADPRHGRYLTAACMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKASVCDIPPKGLKMSTTFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFDEDEEMDEMM
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P20802
P59108
CPNE2_MOUSE
Copine II
Mus
MAYIPDGGAPTAGAIPLGSQCCVCKVELSVSGQNLLDRDVTSKSDPFCVLFIEDNGRWMEFDRTETAVNNLNPAFSKKFVLDYHFEEVQKLKFALFDQDKSSAQLDEHDFLGQFSCSLGTIVSSKKITRPLLLMNDKPAGKGVITIAAQELSDNRVITLSLAGRKLDKKDLFGKSDPFLEFYKPGDDGKWMLVHRTEVIKYTLDPVWKPFTVPLVSLCDGDLEKPIQVMCYDYDSNGGHDFIGEFQTSVLQMSEARDGVPLEIECINPKKQRKKKSYKNSGIIILRSCKIHRNYSFLDYILGGCQLMFTVGIDFTASNGNPLDPSSLHYINPMGTNEYLSAIWAVGQIIQDYDSDKMFPALGFGAQLPPDWKVSHEFAINFNPTNPFCSGVDGIAQAYSACLPHIRFYGPTNFSPIVNHVARFAAQATQQQTATQYFILLIITDGVISDMEETRHAVVQASKLPMSIIIVGVGNADFAAMEFLDGDNRRLRSHTGEEAARDIVQFVPFREFRNAAKETLAKAVLAELPQQVVQYFKHKNLPPTNSEPA
Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Exhibits calcium-dependent cell membrane binding properties .
P59108
A8LRT3
ALR_DINSH
Alanine racemase
Dinoroseobacter
MATATLSIDLDAIAANWRALDRASNRRVATGAVVKADGYGLDAGRVARTLAQAGARQFFVAVAEEGVTLRKALGPGPAINVFSGHMEGDTQAIAGARLTPMINSAEQLARHFEALPRHPFGIQLDTGMNRLGMEADEWAAVAEFALGQGPKLVMSHLACADEPGHAANAAQLAEFHRLTDGITVPRSLSATGGILLGEAYHFDMTRPGIGLYGGAPFGAAEPVVRLSIPVVQVRAVTAGESVGYGCSWVAQSDGAIATLSAGYADGLIRAMSNRAMLYAGDVACPLAGRVSMDLLTVDVSHLDEVPEALDLLCPAQGVDRLAEAAGTIGYEILTSLGPRYARHYAGGVA
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
A8LRT3
Q11KP9
KATG_CHESB
Peroxidase/catalase
unclassified Chelativorans
MDAKTDDSAGKCPFTGGGRRGHRNRDWWPEQLDLDVLHRNSTLSDPMGEDFDYAEEFKSLDLNAVIQDLHALMTDSQDWWPADFGHYGGLMIRMAWHSAGTYRITDGRGGAGAGQQRFAPLNSWPDNANLDKARRMLWPIKQKYGRKISWADLMILAGNVALESMGFKTFGFAGGRKDVWEPEELFWGPEGTWLGDERYSGERQLSEPLAAVQMGLIYVNPEGPNGNPDPVAAAKDIRETFYRMAMNDEETVALIAGGHTFGKTHGAGDPSLIGPDPEGAAIEDQGLGWKSGHGTGFGADTITGGPEVTWSQTPTRWSNYFFENLFGYEWELTKSPAGAWQWKAKNAEATVPDAHDPSKKHVPTMLTTDLSLRFDPIYEKISRRFLENPDQFADAFARAWFKLTHRDMGPKVRYLGPLVPKETLIWQDPIPEVDHVLVDDQDIAGLKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEVNDPAQLAKVLQRLEAIQGEFNAAQAGGKKISLADLIVLGGCAAVEKAARDAGVDVKVPFTPGRMDASQEQTDIDSFRALEPRADGFRNYLSGRQFMMPEEALVDRAQLLRLTAPEMTVLLGGLRVLGANSGGSEHGVLTKQVGKLTNDFFVNLLTMNTQWQPIADGTYEGRDRKTNELKWRATRVDLIFGAHSQLRALAEVYACGDSQEKFVQDFVAAWTKVMNADRFDLA
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Q11KP9
P13911
RPOA_PEA
Plastid-encoded RNA polymerase subunit alpha
Pisum
MIREKLKVSTQTLQWKCVESRVDSKRLYYGRFILSPLMKGQADTIGITMRRILLGEIEGTCITRAKSEKIPHEYSTIVGIQESIHEILMNLKEIVLRSNLYGTREASICFKGPGYVTAQDIILPSVEVIDNTQHIANLTEPINLCIELQIERKRGYRIKTLNNIQDGSYTIDAVFMPVRNANHSIHSYVNGNQKQEILFLEIWTNGSLTPKEALYEASRNLIDLFIPFLHAEEENLNFENNQHKMTLPLFTFHDHDRFVKDKLRKNQKEITLKSIFIDQLELPPRIYNCLKKSNIHTVLELLNKSQEDLMKIEHFRVEDLKFILNILQIENHFV
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
P13911
A7H644
RL5_CAMJD
50S ribosomal protein L5
Campylobacter
MMRLKEKYNQSIKPALVKEFDIKNPMLIPVIEKVVISVGAGELAKDQKVLQNVADTISLIAGQKAVITKAKKSVAGFKVREGFPIGVMVTLRKENMYAFLDKLISIALPRVKDFRGLSRDGFDGRGNYNFGLDEQLMFPEVEYDKILRTHGMNISIVTTAQNDKQAQKLLELIGVPFTKGK
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
A7H644
E7FHN9
HYD2B_PYRFU
Sulfur reductase subunit ShyB
Pyrococcus
MRYVKLHSEYFPEFFNRLKEVGRVYGPVRHNSTYRFEEVNSIDELSLDYTRTILPPKKFFIRPRDAMFKIQKNEVTEVDGDGKFVLFGVHSCDIHGIKILDKVYLSNPPDPYYERRRKNAFIVGISCMPDEYCFCKSLGTDFAMDGFDIFLHELPDGWLVRVGSVKGHEFVWENQDIFDDVTEEDLRNFKEFEEKRAKAFKKSLNKEGLADILDLAFTSKVWKKYAEKCLGCGNCTIVCPTCRCYEVCDTWVRAYEALRMRRYDSCFMPTHGLVAGGHNFRPTRLDRFRHRYYCKNYFDPEAGFNCVGCGRCDEFCPARIEHVKVLDEVREGLI
Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The beta and gamma subunits form the sulfur-reducing component that catalyzes the cytoplasmic production of hydrogen sulfide in the presence of elemental sulfur.
E7FHN9
B2GC51
RNH2_LIMF3
Ribonuclease HII
Limosilactobacillus
MSKQSVAQVRALLSSITDPQDPRLAEFKDDPRKGVQAALNQFAKRLEKRAEARAAFLNRFRYENQLWQAGHQYVAGIDEVGRGPLAGPVVTCAVVLDSQFDLVGVTDSKQLSRHEREQLYLRILDEAVEVSLAVSPAQEIDRLNIYAATQTAMIRSVKALHHQPSHLIVDAVPLDIPVPQTTLIKGDQKSISVAAASIVAKEYRDHLMAIYDRLYPGYGFKDNMGYGTAAHLAGLEQLGACPIHRRTFRPVPDYVN
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
B2GC51
Q481S6
GLYA2_COLP3
Serine hydroxymethyltransferase 2
Colwellia
MFYKNDQIAGFDDSIWQAMEQEDKRQQDHVELIASENYTSARVMQAQGSQLTNKYAEGYPGKRYYGGCEHVDVIEQLAIDRAKELFGADYANVQPHSGSQANAAVFMALLKPGETVLGMSLAHGGHLTHGSKVSFSGKIYNAVQYGLNEATGEIDYEEVERLAKEHQPKMIIAGFSAYSRVVDWQRFRDIADSIGAWLFVDMAHVAGLVAAGLYPNPVPIADVVTTTTHKTLRGPRGGLILAKQNDELAKKLNSAVFPAGQGGPLMHVIAAKAICFKEALGEGYVEYQQQVIDNAREMAKTFQTRGYNVVSGGTDNHLFLLDLIDKGITGKDADAALGRANITVNKNSVPNDPQSPFVTSGLRIGTPAITSRGFGLEEAAALTGWICDVLDDISNEQVIDDVRSKVLDLCEKNPVYR
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Q481S6
Q09FZ1
NU1C_PLAOC
NADH-plastoquinone oxidoreductase subunit 1
Platanus
MIIDTTEVQAINSFSRSESLKEAYGLIWLLVPIFTPVSGITIGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKEDLLPSRGDTRLFSIGPSIAIISILLSYSVIPFGYRLVLADLSIGVFLWIAISSIAPIGLLMSGYGSNNKYSFSGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFAVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWNLSIPYIFIPELFEINKVSGVFGTTIGIFITLAKAYLFLFISITTRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSSQLFSL
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q09FZ1
Q04911
CYB_MONDO
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Monodelphis
MTNLRKNYPLMKIINHSFIDLPAPSNISAWWNFGSLLGMCLIIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNYGWLIRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILMLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGNTLVEWIWGGFSVDKATLTRFFAFHFILPFIILALVIVHLLFLHETGSNNPTGINPNSDKIPFHPYYTIKDALGLILMLLILMSLAMFSPDMLGNPDNFTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASLLILLIIPLLHTSKQRSLMFRPISQIMFWLLVANLLTLTWIGGQPVEQPFIIIGQLASTLYFSLIIIFMPLAGMYEDHLLEPKFP
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.
Q04911
Q82TP1
UBID_NITEU
Polyprenyl p-hydroxybenzoate decarboxylase
Nitrosomonas
MKYKDLRDFLVQLEQRGDLKRVDIEVDPHLEMTEICDRLLKQAGPAVLFERPAGHTIPVLGNLFGTPERVALGMGQTSVSALREVGKLLAYLKEPDPPKGLRDAWEKLPVLKQVLNMAPKQLASAPCQEIIWEGADVDLGKLPIQTCWPGDVAPLITWGLTVTRGPHKSRQNLGIYRQQVIAPNKVIMRWLAHRGGALDYRDFCQIYPGQPYPVAVALGADPATILGAVTPVPDSLSEYQFAGLLRGAKTEVVKCLTHDLQVPASAEIVLEGYIHPDEMAVEGPYGDHTGYYNEQETFPVFTIERITMRRNPIYHSTYTGKPPDEPAILGVALNEVFVPLLQKQFTEITDFYLPPEGCSYRLAVVSMKKQYPGHAKRVMFGIWSFLRQFMYTKFIIVTDDDIDIRDWKEVVWAMTTRVDPVRDTLIVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETTREWGCPIEMDAAVKTRIDHLWQQLPF
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
Q82TP1
B9KH09
ATPA_ANAMF
F-ATPase subunit alpha
Anaplasma
MSIVSSGDILKILKERIEGFDSPVKTSSVGDVVAIKDGIALVYGLSGVKFGETVAFSSGVRGVVAGLERDTCSVVVFGEDREIREGDSVQCTGELMTVPAGLSVLGRVVNPLGSPVDGGNAIVADSRLPVEAKAPGIMARQPVCEPLQTGIKTVDMLIPIGRGQRELVIGDRKTGKTAIALDTIINQKKTNDTADAKNRMYCIYVAIGQKNSSIARVVHKLKETGAMDYTIVVAAGASDPVSIQYLAPYAACAMGEFFRDNGMHCLIVYDDLSKHAVAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLSDDLGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFHKGFRPAINVGLSVSRVGSAAQVKSVKKVAGSMKLTLAQYRELEDFARFGSDLDPSSQAMLEKGRRFMELLKQGQYSPLSVEEQVAVVLAGADDCVNGIPVSEISKFERGLLERLRAEHGGLMSSLSADIADDIKGKLLEVIRGFAASF
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
B9KH09
Q60773
CDN2D_MOUSE
p19-INK4d
Mus
MLLEEVCVGDRLSGAAARGDVQEVRRLLHRELVHPDALNRFGKTALQVMMFGSPAVALELLKQGASPNVQDASGTSPVHDAARTGFLDTLKVLVEHGADVNALDSTGSLPIHLAIREGHSSVVSFLAPESDLHHRDASGLTPLELARQRGAQNLMDILQGHMMIPM
Interacts strongly with CDK4 and CDK6 and inhibits them.
Q60773
P24718
RECF_ACTPL
DNA replication and repair protein RecF
Actinobacillus
MPLSRLIINNFRNLQSLDLELSPNFNFIVGHNGSGKTSLLEAIFYLGHGRSFKSHISNRIIHYQAEDFVLHARIDEGQHQWSVGIQKKRSGDTLLKINGEDGNKISDLAHLLPMQVITPEGLTLLNGGPTFRRAFLDWGLFHQYTEFYSCWANLKRLLKQRNAALHQVRSYAELKPWDIELAKLAEIVSQMRASYAEGLRPEIEKTCQFFLPELEIGVSFHQGWEKGTDYAEILAQGFERDKAMGYTMIGPQKADFRFRANGLPVEDVLSRGQLKLLMCALRLAQGEYLVAQKERQCLFLIDDFASELDPIKRELLAHRLRESGSQVFVTAITKDQLNQMQWQESEQDSLFQVQQGMLTK
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
P24718
Q3KP22
MAJIN_HUMAN
Membrane-anchored junction protein
Homo
MSLKPFTYPFPETRFLHAGPNVYKFKIRYGKSIRGEEIENKEVITQELEVPVEKKAVGAVMRKRKHMDEPSSPSRPGLDRAKIGTSSQGPSKKKPPVETRRNRERKTQQGLQETLASDITDVQKQDSEWGHSLPGRIVPPLQHNSPPPKERAATGFFGFLSSLFPFRYFFRKSSHS
Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane.
Q3KP22
D0LHE3
BMCT1_HALO1
Bacterial microcompartment protein trimer-1
Haliangium
MDHAPERFDATPPAGEPDRPALGVLELTSIARGITVADAALKRAPSLLLMSRPVSSGKHLLMMRGQVAEVEESMIAAREIAGAGSGALLDELELPYAHEQLWRFLDAPVVADAWEEDTESVIIVETATVCAAIDSADAALKTAPVVLRDMRLAIGIAGKAFFTLTGELADVEAAAEVVRERCGARLLELACIARPVDELRGRLFF
A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. This protein does not form stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior.
D0LHE3
Q3BVY7
RL19_XANC5
50S ribosomal protein L19
Xanthomonas
MSKLNKTILADFEAAQIQRKLPEFNQGDTVVVNVKVKEGNRERVQAYEGVVIGTKNAGLNSSFTVRKISHGFGVERVFQTHSAIIDSVEVKRRGKVRAGKLYYLRGLEGKAARIKEDLAAAAQAKAARQAAAKVE
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Q3BVY7
P16451
ODPX_YEAST
Pyruvate dehydrogenase complex component E3BP
Saccharomyces
MLSAISKVSTLKSCTRYLTKCNYHASAKLLAVKTFSMPAMSPTMEKGGIVSWKYKVGEPFSAGDVILEVETDKSQIDVEALDDGKLAKILKDEGSKDVDVGEPIAYIADVDDDLATIKLPQEANTANAKSIEIKKPSADSTEATQQHLKKATVTPIKTVDGSQANLEQTLLPSVSLLLAENNISKQKALKEIAPSGSNGRLLKGDVLAYLGKIPQDSVNKVTEFIKKNERLDLSNIKPIQLKPKIAEQAQTKAADKPKITPVEFEEQLVFHAPASIPFDKLSESLNSFMKEAYQFSHGTPLMDTNSKYFDPIFEDLVTLSPREPRFKFSYDLMQIPKANNMQDTYGQEDIFDLLTGSDATASSVRPVEKNLPEKNEYILALNVSVNNKKFNDAEAKAKRFLDYVRELESF
Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
P16451
B1LEG3
OPGB_ECOSM
Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase
Escherichia
MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGDGINDAVLYTLTNSLTGAGVSKYILPGIGIVLGLTAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSRDGDPDFAAYYKEPSKTIPDPKLNLVYIYGESLERTYFDNEAFPDLTPELGALKNEGLDFSHTQQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLFGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKKYDFDGKPNQSFSAVSCSQENIATFINKIKASPWFKDTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVIRGDKPQQETLAVKRNTMDNGATVLDILGGDNYLGLGRSSLSGQSMSEIFLNIKEKTLAWKPDIIRLWKFPKEMKEFTIDQQKNMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLADFAPRDNFVWVDRCYKMAQLWAPELALSTNWCVSQGQLGGQQIVQHVDKTTWKGKTAFKDTVIDMARYKGNVDTLKIVDNDIRYKADSFIFNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYKHPLPKKFDLVITAKAYGNNASRPIPVRVGNEEQTLVLGNEVTTTTLHFDNPTDADTLVIVPPEPVSTNEGNILGHSPRKLGIGMVEIKVVEREG
Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones.
B1LEG3
Q9I1W9
RGVIR_PSEAE
Putative virulence-regulating protein PA2146
Pseudomonas
MAQHQGGKGNFAEDPKRASEAGKKGGQASGGNFKNDPQRASEAGKKGGQRSHGGN
May be involved in the regulation of the production of pyocyanine, one of the major virulence factors secreted by P.aeruginosa, and other virulence factors.
Q9I1W9
Q8XEC1
MHPD_ECO57
2-hydroxypentadienoic acid hydratase
Escherichia
MTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDNAEAAYAIQHINVQYDVAQGRRVVGRKVGLTHPKVQQQLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATDITFDELYNAIEWVLPALEVVGSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKNCAMKMTRNNEEVSSGRGSECLGHPLNAAVWLARKMASLGEPLRAGDIILTGALGPMVAVNAGDRFEAHIEGIGSVAAAFSSAAPKGSLS
Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.
Q8XEC1
C4ZZN7
MUTS_ECOBW
DNA mismatch repair protein MutS
Escherichia
MSAIENFDAHTPMMQQYLRLKAQHPEILLFYRMGDFYELFYDDAKRASQLLDISLTKRGASAGEPIPMAGIPYHAVENYLAKLVNQGESVAICEQIGDPATSKGPVERKVVRIVTPGTISDEALLQERQDNLLAAIWQDSKGFGYATLDISSGRFRLSEPADRETMAAELQRTNPAELLYAEDFAEMSLIEGRRGLRRRPLWEFEIDTARQQLNLQFGTRDLVGFGVENAPRGLCAAGCLLQYAKDTQRTTLPHIRSITMEREQDSIIMDAATRRNLEITQNLAGGAENTLASVLDCTVTPMGSRMLKRWLHMPVRDTRVLLERQQTIGALQDFTAGLQPVLRQVGDLERILARLALRTARPRDLARMRHAFQQLPELRAQLETVDSAPVQALREKMGEFAELRDLLERAIIDTPPVLVRDGGVIASGYNEELDEWRALADGATDYLERLEVRERERTGLDTLKVGFNAVHGYYIQISRGQSHLAPINYMRRQTLKNAERYIIPELKEYEDKVLTSKGKALALEKQLYEELFDLLLPHLEALQQSASALAELDVLVNLAERAYTLNYTCPTFIDKPGIRITEGRHPVVEQVLNEPFIANPLNLSPQRRMLIITGPNMGGKSTYMRQTALIALMAYIGSYVPAQKVEIGPIDRIFTRVGAADDLASGRSTFMVEMTETANILHNATEYSLVLMDEIGRGTSTYDGLSLAWACAENLANKIKALTLFATHYFELTQLPEKMEGVANVHLDALEHGDTIAFMHSVQDGAASKSYGLAVAALAGVPKEVIKRARQKLRELESISPNAAATQVDGTQMSLLSVPEETSPAVEALENLDPDSLTPRQALEWIYRLKSLV
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
C4ZZN7
Q8DSG6
GATB_STRMU
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Streptococcus
MNFETIIGLEVHVELKTNSKIFSPAPAHFGEDPNANTNIVDWSFPGVLPVMNKGVIDYGIKAALALNMDIHQRMHFDRKNYFYPDNPKAYQISQFDEPIGYNGWIEIELEDGSTKKIRIERAHLEEDAGKNTHGADGYSYVDLNRQGVPLIEIVSEADMRSPEEAYAYLTALKEIIQYTGISDVKMEEGSMRVDANISIRPYGQEAFGVKTELKNLNSFNFVRRGLAYEEKRQAEVLRSGGQIQQETRRYDEATGETLLMRVKEGSADYRYFPEPDLPIFEIEDEWIEKVRAELPAFPKERRAKYVNDLGLSAYDAAQLTSSKAISDFFESALAQGADAKAVSNWLQGDVAQYLNTENQTIDQIGLTPENLTEMLQLVADGTISSKIAKKVFVHLAKNGGSAKEYVKSAGLIQISDPAQLLPIIQEVFANNEKALNDYKGGNKNAAKSLVGQIMKATRGQANPQVAQKLLNEELAKLTD
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).
Q8DSG6
B0SAC5
PANB_LEPBA
Ketopantoate hydroxymethyltransferase
Leptospira
MKNIILQYKKKYDAGEPISVVTCYDYTFATLFNRTDVDCLLVGDSLGMVIQGNQSTLPVTLDEIIYHTKAVCKGAPDKTIIADLPFLSYQTSIEEGIRSAGRVLKETNASCVKLEGDSEFIIELTKRMTESGIPVFAHLGLTPQSVHTLGGHRVQGKTEAARNKMIRKSRELAEAGAFALLLEMVPESLGKEITESIRIPTIGIGAGKYTSGQVLVMQDLLGLNEDFHPKFLKKFGNLSGAVKEAVNAYHKEVTKREYPSEAHVFLDT
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B0SAC5
B6JGU6
TIG_AFIC5
PPIase
Afipia
MQVNETLSEGLKHEFQISIPAAEIDAKVNERLAGMKDKVRLNGFRPGKVPVAHLKKVYGKSVAAETLEETIRETNQKIFTDRGFRLANEAKVTMPTDQAEIEGILDGKKDLTYSVAIEVVPPITLADFKTFKVEKLVADVTDAEVDDAIKRIADQNRPYAPKSEGAKAENGDRVTLAFKGTIDGEAFEGGSGENIPLVLGSNSFIPGFEDQLTGIGVGETRVIKVPFPKNYGAAHLAGKDAEFETTATLIEAPQDATIDDEFAKTLGVESLDKLKEAMRERLTQEYAGATRQKLKRELLDRLDETHKFDPPESLVNDEFDLMWKSIHAEMESAGKTFADEDTTEDEAKTEYRKIADRRVRLGLVLSEIGDKNKITVTDDEVSRAVIERARQMPGREKEVWDYYRSNPGAVAQLRAPIFEDKVVDFILELAEVSEKKVSREELFKEEDDKAAA
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
B6JGU6
Q2NHB4
TRUA_METST
tRNA-uridine isomerase I
Methanosphaera
MRRVALKIAYIGSNFHGYQRQPNYRTVEGELLRVFKETNIIEDTWTAHYSVAGRTDKGVHSTGNVISFITDEDIHINQLNGLLPDDIKIIGEARVPYGFKVRFPLTRTYTYIQPISPFEKKNLDITKMHVAMESFIGKHNFRNFSKRNEKNPNRKIIDVNLEVDEDVLIFTIVGESFLWNMVRKMVTSIMEVGYGKLDINDINELLKPKELRQFIRLQPAPANGLILSDMEYKNIKFKDSEYAKNKLVEFLKKEYMLHEQEKKADCRLIKILKK
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q2NHB4
Q8KBK4
RL13_CHLTE
50S ribosomal protein L13
Chlorobaculum
MSKTLSFKTYSAKPGEVKRTWHIIDAENQVLGRMAAQIANVLRGKHKPQFTPHIDTGDFVVVTNAAKVALSGKKRDDKTYFSHSHYPGGVRIDSVKDLLQKKPEKVIEHAVWGMLPHNNLGRQLFKKLKVYAGPEHPHAAQMPVEMKINQ
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.
Q8KBK4
A4QLM9
RR8_LOBMA
30S ribosomal protein S8, chloroplastic
Lobularia
MGKDTIADIITSIRNADMNRKGTVRIGSTNITESIVKILLREGFIENVRKHRENNQYFLILTLRHRRNKKESHKTILNLKRISRPGLRIYSNSQRIPRILGGIGIVILSTSQGIMTDREARLKRIGGEILCYIW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
A4QLM9
B1KRQ3
RF3_SHEWM
Peptide chain release factor 3
Shewanella
MSGNKVEVDKRRTFAIISHPDAGKTTITEKVLLFGNALQKAGTVKGKKSGQHAKSDWMEMEKDRGISITTSVMQFPYNDALVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDSAKGVEQRTIKLMEVTRLRDTPIVTFMNKLDRDIRDPLELMDEVEEVLNIACAPITWPISSGKEFKGVYHLLRDEVILYQSGQGHTIQDSRIIKGLNNPELDEAIGAYAAEVREELELVLGASNEFDLEMFLAGELTPVFFGTALGNFGVDHILDGIVEWAPKPQARETEVRDIQPEDEKFSGFVFKIQANMDPKHRDRVAFMRICSGRYEQGMKMHHVRLGKDVNVSDALTFMAGDRNRAEVAYPGDIIGLHNHGTMRIGDTFTQGEKFRFTGIPNFAPEMFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPIDSNDLIVGAVGVLQFEVVVGRLKSEYKVEAIYEGISVATARWVYCDDERKLEEFRRKCSNNLALDGGDNLTYIAPTMVNLNLSMERYPDIQFAKTREN
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
B1KRQ3
Q6L6X6
IL6_TAKRU
Interleukin-6
Takifugu
MASISYLLAPLVLAAVLQPTAGAPLDAPTESPAGETSGEEAETGSPDDALAVALESVLGATKLHKNEFLVEFQGEVKYDFLDRYKIPSLPAKCPYSNFGKDACLRRLLEGLLIYSVLLKRVEEEFPSSSILSEVRFYSNILIKELENKVRDRDQVMRLTSSQEEQLLKDTDYPDTFHRKMTAHGILYNLHYFLVDCRRVINKRAKHRESAGSRVVRAVTFYHPKKRS
Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
Q6L6X6
Q31XA7
TRUD_SHIBS
tRNA-uridine isomerase D
Shigella
MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDLSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQHRVNDKELMITAALPGSGEWGTQRKALAFEQAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGDYAHIAE
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q31XA7
Q92QI0
RL1_RHIME
50S ribosomal protein L1
Sinorhizobium
MAKIAKRVQKSREGVDPTKLYGLTEAVTLVKERATAKFDETIEVAMNLGVDPRHADQMVRGVVNLPNGTGRSVRVAVFARGAKADEAKAAGADVVGAEELVEIVQGGKIDFDRCIATPDMMPLVGRLGKVLGPRGMMPNPKVGTVTMDVTGAVKASKGGAVEFRVEKAGIVHAGIGKASFDAKALEENIRAFADAVIKAKPTGAKGNYVKRVAVSSTMGPGLKVDPATISAA
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Q92QI0
Q3Z800
NUOB_DEHM1
NDH-1 subunit B
Dehalococcoides
MELDSGKPLSLLTLDEIDQHEGGIIQSFRTGHTTPYPDPADWLNSEEPPPGVFVTSVEKVLNWSRHYSLWPVMFGLACCAIEMMCMAASRWDLARFGMDIFRASPRQADLMIVAGTLTWKMAPWLKRIYDQMPEPKWVLAMGACGTSGGLFRDSYSVVPGFNMVVPVDVYVPGCPPRPEALLRAIMDIHEKIDKTRIIKR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q3Z800
Q9U2M4
HOT_CAEEL
3-Hydroxypropionate-oxoacid transhydrogenase
Caenorhabditis
MSASLARGILSKMGGSCCPHHAPATNPFKLAKLHGNNKSTDYAFEMVCSTLRFGKGVTLEIGYDVRNLGAKKTLLITDKNVQNTIAFKNAEQALKMVNIEYEVFDDVLIEPTVNSMQKAIAFAKSKQFDSFIAVGGGSVIDTTKAAALYASNPEADFLDFVGPPFGKSMQPKNPMLPLIAVPTTAGTGSETTAAAIMDLPEHKCKTGIRLRCIKPYLAVVDPLNVMSMPRNVAIYSGFDVLCHALESFTALPFDQRSPRPENPGVRPLYQGSNPISDVWSKEALRIIGKYFRRSIFDPTDEEARTEMLKASSFAGIGFGNAGVHLCHGLSYPISSQAKSCVADDYPKEKNLIPHGLSVMTTAVADFEFTTAACPDRHLISAQTLGADIPNNASNEYISRTLCDRLRGYMRDFGVPNGLKGMGFEFSDIEMLTEAASHSVPNIAISPKSADREIISTLYEKSLTVY
Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG.
Q9U2M4
D7UTD1
BSC9_ALTBR
null
Alternaria sect. Brassicicola
MASTSSTSTDGHLNIRPMVHGSDKKLNFGAYITGLDLNNASDAEVDQLREAILRHKIVVIKGQQAEKPDKNWEMIKKLDPMHHMITQEEFGQLFHPTGEGLIAMLKLATVPTTEHGHIHLMGKGYQGDDHYGLKKLNLGEAFAGNYYSKPLAEEDFRAGVTRFQSWHMDGPLYKVHPPYISSLRFIQLPDGEQTVEWADGSGLSLKTKPGRTAFFSTSQLYDMLTDEERAMVDNSAVEYMYYPYEWIRGCRGNPNGLNVADEGREKPLDAMEEIARDERWTKTYPMVWFNELTKEKSLQVQPNCVRRLLIRRSADQKEPEIIEGPERVREFMNKLQQRIVRPEYVYVGPEEEGDHVFWYNWGMMHSKIDYPIAYGPRIVHQGWIPSHRVPRGPTAVAH
Alpha-ketoglutarate dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
D7UTD1
Q2U038
KYNU1_ASPOR
L-kynurenine hydrolase 1
Aspergillus subgen. Circumdati
MGSRLHVQEIKKGPPLPFKDDIRAFTREYAESLDAQDPLRHFRDEFIIPSKKDLKRKTLNANENIEDSSDPRSIYLCGNSLGLQPRNTRKYLEHYLRTWAIKGVTGHFTPHDDQLLPPFVDVDDAGAKLMAPIVGALESEVAVMGTLTANLHFLMASFYQPTKEKYKIILEGKAFPSDHYAVESQIQHHNLDPKDAMVLIELENLDRPILDTEKILRVIDEHASSTALILLSGIQFYTGQYFDIEKITAYAHSKGIIIGWDCAHAAGNVELKLHDWNVDFAAWCNYKYLNSGPGGMAGLFVHENHGRVDMTKVGSKDEPFRPRLSGWWGDDKKTRFRMENRFVPQPGAAGFQLSNPSVLDMNAVAASLEIFNRTSMAEIRKKSLDLTGYLEHLLLKYPLDAAPEDKPFSIITPSNPAERGAQLSLRLGPGLLDNVLEVLEENGVVIDERKPDVIRVAPAPLYNTYADVWQFCQIFFDACQKAVRARK
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Q2U038
Q9CD75
G6PI_MYCLE
Phosphohexose isomerase
Mycobacterium
MTSMQAIPDITATPAWDALRRHHDEIGATHLRQFFADNPNRGRELVITVGDLYIDYSKHRITHDTVQLLVDLARAANLEQRRDQMLAGVHVNTSENRSVLHTALRLPRDTELIVDGQNVVQDVHAVLDVMGDFTDRLRSGEWTGATGKRINTVVNIGIGGSDLGPVMVYQALRHYADAGISARFVSNIDPADLTAKLSDLEPGTTLFIVASKTFSTLETLTNATAARRWLTDALGEAAVSKHFVAVSTNKRLVKDFGINTANMFGFWEWVGGRYSVDSAIGLSLMAVVGRESFADFLSGFHIVDQHFQNAPLESNAPVLLGLIGLWYSDFLGAQSRAVLPYSNDLARFAAYLQQLTMESNGKSTRADGTPVTTNTGEIYWGETGTNGQHAFYQLLHQGTRLVPADFIGFSQPIDDLPTVDGIGSMHDLLMSNFFAQTQVLAFGKTAEEIAAEGTPAEVVPHKVMPGNRPTTSILANRLTPSVLGQLIALYEHQVFTEGVIWGIDSFDQWGVELGKKQAEALLPVITGNASPAQQLDSSTDTLVRRYRTERGRTS
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q9CD75
Q6INS5
RN168_XENLA
RING-type E3 ubiquitin transferase rnf168
Xenopus
MTKEKTLPLPRSECICPICQEILLEPVTLPCKHTLCNPCFQMTVEKASLCCPFCRKRVSTWARLHSRTRTLVNTELWERIQKQYPKECQRRASGQESDDLADELASCPAPLLCQPGEIRQEYEAEVSKIEAERLAQEEAERKASEDYIQKLLAEEAAQDRLHSEAVQREMEEQLKIDEELARTLSVDLDVSNASCSSVSSVTSKKVVVSKSSKNVKNKQRVSGDIERFLTPRAVAVVGIDESMNSDSSECFIVFDEGEDEMPELSPQCPSTSLIQERGVELIMPYLSDCYKVESNTTSQQDRCSERSQVCNGTYSSCSDSIDMEESMAIKKQSTTAGLFPERGYHSPENGMESNTMNCSTPKHLGMTGTLKRKCEDCSIDLEEKAGSCRNVKKKKLSLTEDCPVPSVHAGKLIELEENLYERRRQEEQDRLLALQLQRELDKELKQVNRGKGSPDEYELRTKRGLKLQECLKLQECQDSPLPLRKEIPVQDNSRNTQSEYSPDENKKPSRKNSVRSARVRQSRAVANTEGSSDGINVLKPINKQPTILDLFQRSAGK
E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with ube2n/ubc13 to amplify the rnf8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the rnf8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of tp53bp1 and brca1. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively).
Q6INS5
P40402
SSUD_BACSU
FMNH2-dependent aliphatic sulfonate monooxygenase
Bacillus
MEILWFIPTHGDARYLGSESDGRTADHLYFKQVAQAADRLGYTGVLLPTGRSCEDPWLTASALAGETKDLKFLVAVRPGLMQPSLAARMTSTLDRISDGRLLINVVAGGDPYELAGDGLFISHDERYEATDEFLTVWRRLLQGETVSYEGKHIKVENSNLLFPPQQEPHPPIYFGGSSQAGIEAAAKHTDVYLTWGEPPEQVKEKIERVKKQAAKEGRSVRFGIRLHVIARETEQEAWEAAERLISHLDDDTIAKAQAALSRYDSSGQQRMAVLHQGDRTKLEISPNLWAGIGLVRGGAGTALVGDPQTIADRIAEYQALGIESFIFSGYPHLEEAYYFAELVFPLLPFENDRTRKLQNKRGEAVGNTYFVKEKNA
Catalyzes the desulfonation of aliphatic sulfonates.
P40402
O00469
PLOD2_HUMAN
Lysyl hydroxylase 2
Homo
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
O00469
Q6ING2
PUS10_XENLA
tRNA-uridine isomerase
Xenopus
MLLIEEKYRSVAQVLLSSGTCSRCVLRFCCVGSPANYRLPCKEVTYELQKYLSHGDPAEENDTPPSKKAKIEEDTSSNEHLGNCEDVNGSQVVRICPLCLGILQQFCEPEFIEKVFVKINSAVYELKDFVLSISLPAQLSVREHSAWLQAKQEMGKHGHSLDKTDIVQLKEAYKWIIHPLLSDQLGIQADSKSLFEVAVVFTHPETDGDCHFLATVCRDCFKPTKNKQSVFTRMAVVKALEKIKEEDFRVQFPFPPSSPETTCEVVDIQCNHSPVFVAGRYNKYSRNLPQTPWIIDGERKIESSVEELITDHLVAAFRSSSFNFSSSGREDVDVRTLGKGRPFAIELLNPHKVQFTGQEIKALQQKINTSDKIKVRDLQIVSREAVAHMKEGEEEKTKCYCALIWIEKMVRNEDLQLLDGLEELTIAQKTPLRVLHRRPLASRSRTIHTMRTEYVDEHHFRLYLKTQAGTYIKEFVHGDFGRTKPNVGSIMETNADILELDVESVDVDWPPSLDD
Protein with different functions depending on its subcellular location: involved in miRNA processing in the nucleus and acts as a tRNA pseudouridylate synthase in the cytoplasm. In the cytoplasm, acts as a pseudouridylate synthase by catalyzing synthesis of pseudouridine(54) and pseudouridine(55) from uracil-54 and uracil-55, respectively, in the psi GC loop of a subset of tRNAs. tRNA pseudouridylate synthase activity is enhanced by the presence of 1-methyladenosine at position 53-61 of tRNAs. Does not show tRNA pseudouridylate synthase activity in the nucleus. In the nucleus, promotes primary microRNAs (pri-miRNAs) processing independently of its RNA pseudouridylate synthase activity. Binds pri-miRNAs.
Q6ING2
B8EA98
IHFB_SHEB2
Integration host factor subunit beta
Shewanella
MTKSELIEKLATRQSQLSAKEVEGAIKEMLEQMATTLESGDRIEIRGFGSFSLHYRAPRTGRNPKTGSSVDLEGKYVPHFKPGKELRERVDAVNV
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.
B8EA98
Q5SJE2
MTNA_THET8
S-methyl-5-thioribose-1-phosphate isomerase
Thermus
MDRVLPFRFAEEEGVFWLLDQRRLPQEEVYVPVRTAREMAQAIRDMVVRGAPAIGVSAAFGMVLAHLAGEDLEEADRRLRASRPTAVNLFHALDRMRPFWGDLAGSLLEARRIWREVEETEAAISRHGAQVLWGQVLTHCNTGPLATGGYGTALGAIVEAYRLGRVRHVWVDETRPYLQGARLTAYELQKAGVPATLITDGMAGWLMARGAVDAVVVGVDRMALNGDFANKVGTYALAVLAHHHGIPFYAALPLSSVDPRLASGEGIPIEERSPEEVVAFRGVRIAPEGFPAYHPAFDVTPHRYLTGIITEKGVLYPPFAEGLRRALGLD
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Q5SJE2
A5CQM6
METXA_CLAM3
Homoserine transacetylase
Clavibacter
MTDAQIRSLIGRPPASGAWREGDPVADRLFASVGGVDLEAGGRIPSVRVAYETFGERDPDGGNAVLVLHALTGDSHLRGPAGPGQPTGGWWSGIVGPGLAIDTDRWFVVAPNMLGGCQGTTGPASLAPDGAEWGARFPFITIRDQVAVQAALADALGIDVWAAVVGGSMGGMQALEWGVGLPGRMRRLAILAAPAIASADQIALNSVQAEAIRMDPAYRDGDYFDAADGDGPHRGLALARRMALLNYRSPDELNQRFSRSWQSGISPMGDEGRYAVESYLDFHGNKFTRRFDATSYIRLIDAMSSHDVGRDRGGVEAALASVRAATLVVGIDSDRLFPVPDQRLVARHVPGSVDGGEVVVISSDYGHDGFLIENEAVGRALARLLDTPA
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
A5CQM6
A0QKT1
GLMM_MYCA1
Phosphoglucosamine mutase
Mycobacterium avium complex (MAC)
MGRLFGTDGVRGVANRELTAELALALGAAAARQLASGSAPGRRVAVIGRDPRASGEMLEAAVIAGLTSQGVDALRVGVLPTPAVAYLTGAYDADFGVMISASHNPMPDNGIKIFGPGGHKLDDGTEDRIEALVGDAGPRPVGAGIGRVIDAEDAADRYLRHLSKASTLRLDGLTVVVDCAHGAASSVAPRAYRAAGARVIAINADPNGLNINDNCGSTHLDSLRAAVVAHRADLGLAHDGDADRCLAVDADGNLVDGDHIMVVLALAMREAGELASDTLVTTVMSNLGLHLAMRSAGITVRTTGVGDRYVVEELRAGDYSLGGEQSGHIVMPALGSTGDGIVTGLRLMTRMAQTGSPLSDLASAMQTLPQVLINVTVADKATAATAPSVQTAVGQAAAELGDTGRILLRPSGTEPMIRVMVEAPEKDIAQRLATRVAEAVSAAR
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
A0QKT1
P0DPD7
EFMT4_HUMAN
EEF1A lysine methyltransferase 4
Homo
MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVSRVLVPGGRFISMTSAAPHFRTRHYAQAYYGWSLRHATYGSGFHFHLYLMHKGGKLSVAQLALGAQILSPPRPPTSPCFLQDSDHEDFLSAIQL
Protein-lysine methyltransferase that efficiently catalyzes three successive methylations on 'Lys-36' in eukaryotic translation elongation factor 1 alpha (EEF1A1 or EEF1A2).
P0DPD7
Q9RXK7
RS12_DEIRA
30S ribosomal protein S12
Deinococcus
MPTTQQLLRKGRKVLQKKSKVPALKGSPFRRGVCTVVKTTTPKKPNSALRKIARVRLSSGFEVTAYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGSLDTQGVKDRNKSRSKYGTKKPKAGAAAAKK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q9RXK7
P53695
EXO1_SCHPO
Exodeoxyribonuclease I
Schizosaccharomyces
MGIKGLLGLLKPMQKSSHVEEFSGKTLGVDGYVWLHKAVFTCAHELAFNKETDKYLKYAIHQALMLQYYGVKPLIVFDGGPLPCKASTEQKRKERRQEAFELGKKLWDEGKKSQAIMQFSRCVDVTPEMAWKLIIALREHGIESIVAPYEADAQLVYLEKENIIDGIITEDSDMLVFGAQTVLFKMDGFGNCITIRRNDIANAQDLNLRLPIEKLRHMAIFSGCDYTDGVAGMGLKTALRYLQKYPEPRAAIRAMRLDKSLKVPVSFEKEFALADLAFRHQRVYCPKDKTLVHLSPPERELSVHEDAFIGSFFDNQLAIDIAEGRSNPITKCAFDIKDSSMQSFTKTTITISKRKGISKTDISNFFMKSIPPSKRPTKSTSLIDVTNVKVQRTHLANDISSEKQSIKSANEKAYVTPKSNSLKPGFGKSLSDISNSATKNENVPFLPPRTGVSKYFKLQKNTEKEIDEQVPSQSNNTTPTSAKSDSASPQNWFSSFSYQTPNSASPPFSSLSHTLPISALAKIGHDALNRKNHASLPSRRIVYKPPSSPSTPISMNPRPKGILSLQQYKFR
5'->3' double-stranded DNA exonuclease that could act in a pathway that corrects mismatched base pairs.
P53695
Q4ZU60
GCH4_PSEU2
GTP cyclohydrolase FolE2
Pseudomonas syringae
MNKPLPDVALTEISPALVSLDWVGMQGVEVPIRLAEASIRHPVHAHVDLQVDLADPSVKGIHMSRLYRLLDGYAERQIVSPDTLAALLEAMVESHLDCHSSHARLTLSFNLLCRRPALITEGLSGWKSYPVKLDATWHAGRLCLDSSVDITYSSTCPCSAALSRQLLEEAFAARFGRQSFVDPMQVATWLRENASFATPHSQRSVATVQVRVAEQAAELGLMTLIDLVEQALGTPVQTAVKRADEQAFARLNGQNLMYVEDAARKVQQALEGRYAASSVSVRHFESLHPHDAAAQTSNYLS
Converts GTP to 7,8-dihydroneopterin triphosphate.
Q4ZU60
A6X0A5
RL11_BRUA4
50S ribosomal protein L11
Brucella
MAKKIAGQLKLQVAAGAANPSPPIGPALGQRGINIMEFCKAFNAASQEMEKGSPIPVVITYYQDKSFTFVMKTPPVTYFLKKAANLKSGSKTPGKASAGTISRDKVRTIAEAKMKDLNAADIEAAMRMIEGSARSMGLEVVG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
A6X0A5
Q5HRL5
RL11_STAEQ
50S ribosomal protein L11
Staphylococcus
MAKKVEKVVKLQIPAGKANPAPPVGPALGQAGVNIMGFCKEFNARTQEQAGLIIPVEISVYEDRSFTFITKTPPAPVLLKKAAGVEKGSGEPNKTKVATVTKDQVREIAQTKMQDLNAADEEAAMRIIEGTARSMGITVQ
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q5HRL5
Q3U2S8
HVCN1_MOUSE
Voltage sensor domain-only protein
Mus
MTSHDPKAVTRRTKVAPTKRMSRFLKHFTVVGDDYHTWNVNYKKWENEEEEEEPAPTSAEGEGNAEGPDAEAGSASTPRQSLDFRSRLRKLFSSHRFQVIIICLVVLDALLVLAELLLDLKIIEPDEQDYAVTAFHYMSFAILVFFMLEIFFKIFVFRLEFFHHKFEILDAFVVVVSFVLDLVLLFKSHHFEALGLLILLRLWRVARIINGIIISVKTRSERQILRLKQINIQLATKIQHLEFSCSEKEQEIERLNKLLKQNGLLGDVN
Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis.
Q3U2S8
B8HD07
RS10_PSECP
30S ribosomal protein S10
Pseudarthrobacter
MAGQKIRIRLKSYDHEVIDVSARKIVETVTRAGATVVGPVPLPTEKNVYCVIRSPHKYKDSREHFEMRTHKRLIDIIDPTPKAVDSLMRLDLPADVNIEIKL
Involved in the binding of tRNA to the ribosomes.
B8HD07
Q4R7D9
PSA7L_MACFA
Proteasome subunit alpha type-7-like
Macaca
MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGIPRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDNEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV
Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.
Q4R7D9