accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
A4KWA6 | CL2D3_RAT | C-type lectin domain family 2 member D3 | Rattus | MSSSAHLQDAPPLLSGTLTQNEGQTSLRQSSSCGPSAASASESLSGYTESRIPHSKVRQGKGLRSIFPESRVKRYCCYGGVITVVAIAIVVPLSVTLSVKQMEQTSINNTSAASINNTSAASINNTSAACPSNWTEYGNKCFYFSEYTSNWTFSKDFCAAQGAELARFDTEEELNFLKRYKGSSGYWIGLHRESSEHPWKWTDNTQYNNLIPIRGDGQCGFLSDQLNISSSRVYVERPWICSKPKKYISQSQ | Lectin-type cell surface receptor. | A4KWA6 |
Q7VQX8 | SYD_BLOFL | Aspartyl-tRNA synthetase | Candidatus Blochmannia | MRTAYCGQLNLSHVGLEVTLCGWVNKYRNFGKLIFVDLRDREGCIQVYFNSDAQKKTYVRAADLKQEFCIQLTGIVRSRPVSQINKNMSTGFIEIEAKFFLVLNVSNPLPLDIHQDNIEENRLKYRYLDLRRPIMFHNIQTRSRVMALTHRFMELEGLLNIDTPVLAKSTPEGARDYLVPSRLHINKYYALPQSPQMFKQLLMIAGIDRYYQITKCFRDEDLRSDRQPEFTQIDVEISFITAKKIRELMEFFICKLWKEILNVELEVFSQFSYAEVISRFGSDSPDLRNPIEMKDVSSIFQSLGNKLFICNAGCVDTIDTQVIVMNVPSGFKLTRNEIDKYSDYAKKSGIQQFLWMKIQMNDCKEITAIDGPIINLLNKNFLQLLMAQVKIENNDILFFGFNNDKNLSTTRMLSALRSKLGYDLNLVKQDSWKPLWIVDFPMFKKNTSGKLVSMHHMFTAPKDNDLICLKRNPELAVSEAYDIVINGCEVGSGSVRIHSYKLQQAMFDILGITRENQQKKFGCLMNALKYGAPPHAGIALGLDRLVMLLTKSNNIRDVIAFPKTTGAMDLMIDAPD | Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). | Q7VQX8 |
Q49MG5 | MAP9_HUMAN | Aster-associated protein | Homo | MSDEVFSTTLAYTKSPKVTKRTTFQDELIRAITARSARQRSSEYSDDFDSDEIVSLGDFSDTSADENSVNKKMNDFHISDDEEKNPSKLLFLKTNKSNGNITKDEPVCAIKNEEEMAPDGCEDIVVKSFSESQNKDEEFEKDKIKMKPKPRILSIKSTSSAENNSLDTDDHFKPSPRPRSMLKKKSHMEEKDGLEDKETALSEELELHSAPSSLPTPNGIQLEAEKKAFSENLDPEDSCLTSLASSSLKQILGDSFSPGSEGNASGKDPNEEITENHNSLKSDENKENSFSADHVTTAVEKSKESQVTADDLEEEKAKAELIMDDDRTVDPLLSKSQSILISTSATASSKKTIEDRNIKNKKSTNNRASSASARLMTSEFLKKSSSKRRTPSTTTSSHYLGTLKVLDQKPSQKQSIEPDRADNIRAAVYQEWLEKKNVYLHEMHRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAARKGEALQAFEKWKEKKMEYLKEKNRKEREYERAKKQKEEETVAEKKKDNLTAVEKWNEKKEAFFKQKEKEKINEKRKEELKRAEKKDKDKQAINEYEKWLENKEKQERIERKQKKRHSFLESEALPPWSPPSRTVFAKVF | Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly, mitosis progression and cytokinesis. May act by stabilizing interphase microtubules. | Q49MG5 |
Q9VWR2 | CP308_DROME | CYPCCCVIIIA1 | Sophophora | MLPLVLFILLAATLLFWKWQGNHWRRLGLEAPFGWPLVGNMLDFALGRRSYGEIYQEIYTRNPGLKYVGFYRLFNEPAILVRDQELLRQILVGRNFADCADNAVYVDHQRDVLASHNPFIANGDRWRVLRADLVPLFTPSRVRQTLPHVARACQLLRDQVPLGRFEAKDLATRYTLQVVASAIFGLDAHCLGIHMRVAHEPSRWLEWLAPLFQPSVWSLLETMSLLHTPRLGRLIGHRYVPLPLQHWFRELVEARSGGDNLLQWLAESKRGLGKEELAGHATTLLLEGYETSAMLLAFALYELALNEDAQRRLHIELDEVAQRHAGNLIDPVALGELRYSEAALLEALRLHPAMQALQKRCTKTFTLPDQKSGASSELKVHLGTVLVLPVQAIHLDPALYPAPNQFRPERFLNQPPMGCRFLGFGAGPRMCPGMRLGLLQTKAALTTLLQDHCVQLADEDQCRVEVSPLTFLTASRNGIWLSFKRRTRRY | May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. | Q9VWR2 |
A4WNY9 | ATPF1_CERS5 | F-type ATPase subunit b 1 | Cereibacter | MKKLSILAALAASPAMAATGPFFSLSNTNFIVTLAFLIFMGILVYAKVPGRILGMLDRRAVQIRSELEEARALREEARTILASYDRKQKEVQEQAARIVASARDEAQAAAEQAKADLKASIARRLAAAEDQIASAEAGAVRAIREQAISVAVAAASDVLARQMTPAATSASIDESIKEVEARFH | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | A4WNY9 |
A7H422 | TRMA_CAMJD | tmRNA (uracil(341)-C(5))-methyltransferase | Campylobacter | MSLENFGNFLTLDEKHSFIKKYFKEFYTKDFKLFTSKDKHYRTRAELSFYHENDTLFYAMFDPKSKKKYIIEYLDFADEKICAFMPKLLEYLRQDDKLKEKLFGVEFLTTKQELSLTLLYHKNIEDIKSNLENLSNNLHINLIARSKGKKLIFKTENLRQTLNIQGREIFYEFNNDCFIQPNTTINEKMITWVCEILSIQKRMDLLELYCGYGNFTLALAQFFFKVLATEISKSSINFALKNCKLNNTTNIHFARLSSEELSLAIKKEREFFRLKDIRLDDFNFSHVLVDPPRAGLDKSVIDLIKKYENIIYISCNPITLKENLKELSLTHRVENFALFDQFVNTPHLECGVFLSKV | Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). | A7H422 |
Q9VIP2 | PYRD1_DROME | Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 | Sophophora | MSRKCEFLVVGGGIAGVSCAESLAIYRPNASILLLTESSIVKSVTNLVPVARYLHKFDVREQDVSEMGASFQTLVDRLDHINSREHCIRTKAGLEIKYRYLCLCTGGTPKLFSGKVVNPLVIGIRDTDSVQLLQRKLATAKDVLILGNGGIASELAYELKDVNVHWVVKDSHISATFVDPGAAEFFHIAMNECNAKDSSPVVAIKRMRYSEVLPKEQTNNHGAALGPDWHRSVDLSGAREGEENRLPKIYYKSRISSVQDLADDAGAIVKLEHEDGSFQQLTCDFIVSATGVWPNTDYTCDSPLQFSDDGGISVDEMMRTNLVDVFAAGDVCTANWPAAMHWFQMRLWTQARQMGSMAGRSMAAASEGESVYQDFCFELFGHVTKLFGYPVVLLGRFNGQDLGRDYEILVRCTRNKEYIKFVLQNGRLRGAMLIGNTDLAETCENLILNGIDLEPYGDDILNPDIDIEDYFD | Probable oxidoreductase. | Q9VIP2 |
Q95MN4 | CY24A_RABIT | p22-phox | Oryctolagus | MGQIEWAMWANEQALASGLILVAGGIVATAGRFTQWYFGTYAIAAGVLVCLLEYPRGSRAKGSTLERCGQRYLTAVLKLLGPLSRNYYFRAALHLALSVPAGFLLATILGTVCLVIASIIYLLAAVRGEQWTPIEPRPKERPQVGGTIKQPPSNPPPRPPVEARKKPGEEDATPAGGPPGGPRVNPIPVTDEVV | Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. | Q95MN4 |
Q91W89 | MA2C1_MOUSE | Neutral/cytosolic alpha-mannosidase | Mus | MAAAPFLKHWRTTFERVEKFVSPIYFTDCNLRGRLFGDSCSVTLSSFLTPERLPYEKAVQQNFSPAQVGDSFGPTWWTCWFRVELVIPEVWVGQEVHLCWESDGESLVWRDGEPVQGLTKEGEKTSYVLSERLRASDPRSLTLYVEVACNGLLGAGKGSMIAAPDPEKMFQLSQAKLAVFHRDVHSLLVDLELLLGVAKGLGEDSQRSFQALHTANQMVNICDPAQPETYPAAKALASKFFGQHGGESQHTIHAMGHCHIDTAWLWPFKETVRKCARSWSTAVTLMEQNTDFIFACSQAQQLEWVKSQYPGLHARLQEFACRGQFVPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMQGCGIKRFLTQKLSWNLVNSFPHHTFFWEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVTNNRDKGRTNHSGFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLSSPGQLFTALERDSGQLCTWVGELFLELHNGTYTTHAQLKKGNRECEQILHDVEVLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQLVAEDAMNYYEDIRSHGNPLLSAAAAALCAGEPGPKGLLIINTLPWKRTEVLALPKPCGAHSLALVTVPSIGYAPAPTPTSLQPLLPQQPVFVMQETDGSVTLDNGIIRVRLDPTGCLTSLVLVASGREAIAEGALGNQFVLFDDVPLYWDAWDVMDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQISPNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARIRSPQATYEIQFGHLQRPTHNNTSWDWARYEVWAHRWIDLSECDFGLALLNNCKYGASVRGNVLSLSLLRAPKAPDATADMGRHEFTYALMPHKGSFQEAGVIHAAYNLNFPLLALPAPGPAPDTTWSAFSVSSPAVVLETIKQAERCHQHRTLVLRLYEAHGSHVDCWLHTSLPVQEATLCDLLEQRDPTGHLSLQDNRLKLTFSPFQVRSLLLVLQSPPN | Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from glycoproteins. Involved in the degradation of free oligosaccharides in the cytoplasm. | Q91W89 |
Q9UVP6 | VPS1_PLEER | Versatile solid phase peroxidase 1 | Pleurotus | MAFAKLSAFVLALGATVALGESPTHRCLNKRVTCATGQTTANEACCALFPILDDIQTNLFDGAQCGEEVHESLRLTFHDAIAFSPALTNAGQFGGGGADGSMIIFSDTEPNFHANLGIDEIVEAQKPFIARHNISAADFIQFAGAIGVSNCAGAPRLNFFLGRPDATQIPPDGLVPEPFDDVTKILSRMGDAGFSTVEVVWLLASHTIAAADHVDPSIPGTPFDSTPSTFDSQFFLETMLQGTAFPGTPGNQGEVESPLAGEMRLQSDFLLARDSRSACEWQSMVNNMPKIQNRFTQVMKKLSLLGHNQADLIDCSDVIPVPKTLTKAATFPAGKSQADVEIVCNAAATPFPALASDPGPVTAVPPVPPS | A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. | Q9UVP6 |
Q2T880 | ATPB2_BURTA | F-ATPase subunit beta 2 | pseudomallei group | MGATVADLQATNGTAQAQAKHGVSDGRVVAVRGAVVDVAFDGGVLPALNDALVIPIDGAAPILAEVHAHLSDAAVRALALGPTGGLRRGAAVRATGGPIRVPVGDAVLGRLLSVTGEPGDDGAALAADVARRPIHRGAPPLAEQKSATALFATGIKVIDLLAPLAQGGKAAMFGGAGVGKTVLVMELIHAMVERYRGISVFAGIGERSREGHEMLLDMRGSGVLGRTVLVYGQMNEPPGARWRVPLTALAIAEYFRDERAQNVLLLMDNVFRFVQAGAEVSGLLGRLPSRVGYQPTLASEVAALQERIASVEGAAVTAIEAVYVPADDFTDPAVTAIAAHVDSMVVLSRAMAAEGMYPAIDPVASSSILLDPLVVGEAHVEVAIEVRRVIEHYRELQDVIALLGIDELGADDRRIVGRARRLQRFLTQPFAVTEAFTGQAGASVEIADTIAGCRAILRGDCDDWRESSLYMVGTLDDARRKEEAAREADARRDAAAGAASGSAGPQGAQHGR | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q2T880 |
Q8Y3C3 | GATA_RALSO | Glutamyl-tRNA(Gln) amidotransferase subunit A | Ralstonia | MTASTLKTLSAQLAAKEVSAVELARHYLARIEARADLNAFIHVDPEATLAQAQAADARLAAGDAGPLAGIPIAHKDVFVTRGWRATAGSKMLDSYVSPFDATVVERLAAAGMVTLGKTNMDEFAMGSSNENSHFGPVKNPWDVARVPGGSSGGSAAAVAADLAPAATGTDTGGSIRQPASFSGITGIKPTYGRVSRYGMIAFASSLDQGGPMARTAEDCALLLSAMAGFDARDSTSLEPGRGGDAEDFGRLLGRPLEGADAARPLAGLRIGLPQEYFGAGLADDVRTAVRAALAELETLGATLVDISLPKTELSIPTYYVIAPAEASSNLSRFDGVRYGHRAAAYRDLADMYRKTRAEGFGWEVKRRILVGTYVLSHGYYDAYYLQAQKIRRIIAQDFQNAFGQCDVIMGPVAPTVAWKLGEKTDDPLQMYLADIFTLSTSLAGLPGMSVPAGFGANGLPVGLQIIGNYFEEARMLQIAHAFQQATDWHTRRPAA | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | Q8Y3C3 |
P96121 | GPMA_TREPA | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | Treponema | MKLVLIRHGESEWNRLNLFTGWTDVPLTPRGESEAQEGGRVLQEAGFDFDLCYTSFLKRAIRTLNFVLQALDREWLPVHKSWKLNERHYGDLQGLNKTETAQKYGEQQVRVWRRSFDVAPPPLTVGDARCPHTQASYRGVCASGRTPVLPFTESLKDTVARVVPYFEEEIKPQMISGQRVLIVAHGNSLRALMKHIESLDETQIMEVNLPTGVPLVYEFEADFTLCGKRFLGNEADVAARAQAVADQGKSN | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | P96121 |
Q6D8D0 | LPXB_PECAS | Lipid-A-disaccharide synthase | Pectobacterium | MSSRPLTIGLVAGETSGDILGAGLIRALKEKVPGARFVGVAGPRMQAEGCEAWYEMEELAVMGIVEVLGRLPRLLKIRRDLTQRFSELQPDVFVGIDAPDFNITLEGNLKQHGINTIHYVSPSVWAWRQKRVFKIGKATNLVLAFLPFEKAFYDRFNVPCRFIGHTMADAMPLHPDKMTARATLGIAPDAHCLALLPGSRGAEVEMLSADFLNTAVLLRQHFPDLEIVVPLVNSKRREQFERIKSSVAPDLRVHLLDGQAREAMIASDAALLASGTAALECMLAKCPMVVGYRMKPFTFWLAQRLVKTPWVSLPNLLAGRELVTELLQTDCTPDKLAAALLPLFADTDKMAELRTTFVDLHQQIRCNADEQAAQAVLELVTPR | 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. | Q6D8D0 |
Q9ZL46 | MOAC_HELPJ | Molybdenum cofactor biosynthesis protein C | Helicobacter | MPLTHLNEENQPKMVDIGDKETTERIALASGRISMNKEAYDAIINHGVKKGPVLQTAIIAGIMAAKKTSELIPMCHPIMLNGVDIDILEEKETCSFKLYARVKTQAKTGVEMEALMSVSIGLLTIYDMVKVIDKSMTISGVMLEHKSGGKSGDYNAKK | Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). | Q9ZL46 |
Q9B5R1 | CYB_CEPNI | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Cephalophus | MTNIRKTHPLLKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTADTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTYMETWNIGVILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFIFPFIIAALAMVHLLFLHETGSNNPTGISSDADKIPFHPYYTIKDILGALLLILVLMTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILVLILMPLLHTSKQRSMMFRPISQCLFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLLILVLMPMASTIENNLLKW | 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. | Q9B5R1 |
Q814W0 | ATPA_BACCR | F-ATPase subunit alpha | Bacillus cereus group | MKHMSIRAEEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSDLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKKLADDDKFAAAINGFKKVFVASE | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q814W0 |
C0MAH5 | TGT_STRE4 | tRNA-guanine transglycosylase | Streptococcus | MTNYPITYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEIGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVSMDFPGYSIGGLAVGESHAEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHHCDCYTCQHYTRAYLRHLLKADETFGMRLTSYHNLYFLVNLMKQVRQAILDDNLLEFRQDFLERYGYNSSSRNF | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | C0MAH5 |
P07856 | SERI1_BOMMO | Silk gum protein | Bombyx | MRFVLCCTLIALAALSVKAFGHHPGNRDTVEVKNRKYNAASSESSYLNKDNDSISAGAHRAKSVEQSQDKSKYTSGPEGVSYSGRSQNYKDSKQAYADYHSDPNGGSASAGQSRDSSLRERNVHYVSDGEAVAASSDARDENRSAQQNAQANWNADGSYGVSADRSGSASSRRRQANYYSDKDITAASKDDSRADSSRRSNAYYNRDSDGSESAGLSDRSASSSKNDNVFVYRTKDSIGGQAKSSRSSHSQESDAYYNSSPDGSYNAGTRDSSISNKKKASSTIYADKDQIRAANDRSSSKQLKQSSAQISSGPEGTSVSSKDRQYSNDKRSKSDAYVGRDGTVAYSNKDSEKTSRQSNTNYADQNSVRSDSAASDQTSKSYDRGYSDKNIVAHSSGSRGSQNQKSSSYRADKDGFSSSTNTEKSKFSSSNSVVETSDGASASRESSAEDTKSSNSNVQSDEKSASQSSSSRSSQESASYSSSSSSSTLSEDSSEVDIDLGNLGWWWNSDNKVQRAAGGATKSGASSSTQATTVSGADDSADSYTWWWNPRRSSSSSSSASSSSSGSNVGGSSQSSGSSTSGSNARGHLGTVSSTGSTSNTDSSSKSAGSRTSGGSSTYGYSSSHRGGSVSSTGSSSNTDSSTKNAGSSTSGGSSTYGYSSSHRGGSVSSTGSSSNTDSSTKSAGSSTSGGSSTYGYSSRHRGGRVSSTGSSSTTDASSNSVGSSTSGGSSTYGYSSNSRDGSVSSTGSSSNTDSNSNSAGSSTSGGSSTYGYSSNSRDGSVSSTGSSSNTDSNSNSAGSSTSGGSSTYGYSSNSRDGSVSSTGSSSNTDASTDLTGSSTSGGSSTYGYSSDSRDGSVSSTGSSSNTDASTDLAGSSTSGGSSTYGYSSDCGDGSVSSTGSSSNTDASTDLAGSSTSGGSSTYGYSSDSRDGSVSSTGSSSNTDASTDLAGSSTSGGSSTYGYSSNSRDGSVSSTGSSSNTDASTDLTGSSTSGGSSTYGYSSSNRDGSVLATGSSSNTDASTTEESTTSAGSSTEGYSSSSHDGSVTSTDGSSTSGGASSSSASTAKSDAASSEDGFWWWNRRKSGSGHKSATVQSSTTDKTSTDSASSTDSTSSTSGASTTTSGSSSTSGGSSTSDASSTSSSVSRSHHSGVNRLLHKPGQGKICLCFENIFDIPYHLRKNIGV | Provides the silk fibroin thread with a sticky coating. Acts as a cement by sticking silk threads together. | P07856 |
A7Z6S2 | ISPG_BACVZ | 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase | Bacillus amyloliquefaciens group | MSEITHRTKTRPVKVGPLTIGGNNEVVIQSMTTTKTHDVEATVAEINRLAEAGCQIVRVACPDERAANAIADIKKQISIPLVVDIHFDYKLALKAIEGGADKIRINPGNIGRREKVEAVVKAAKEKGIPIRIGVNAGSLEKRILEKYGYPTADGMVESALHHIKILEDLDFHDIIVSMKASDVNLAIEAYEKASKAFDYPLHLGITESGTLFAGTVKSAAGLGAILSKGIGNTLRISLSADPVEEVKVARELLKSFGLASNAATLISCPTCGRIEIDLISIANEVEEYISKVKAPIKVAVLGCAVNGPGEAREADIGIAGARGEGLLFRKGQIVRKVPEETMVEELKKEIDKLAEEHYAKLEAEKAKAEQETQKA | Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. | A7Z6S2 |
Q1IF59 | DNAK_PSEE4 | Heat shock protein 70 | Pseudomonas | MGKIIGIDLGTTNSCVSVLENGTAKVIENAEGARTTPSIIAYANDGEILVGQSAKRQAVTNPHNTLFAVKRLIGRRFDEEVVQKDIKLVPYKIVKASNGDAWVQASGKDMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKAKGDHTVIVYDLGGGTFDVSVIEIAEVDGEHQFEVLATNGDTFLGGEDFDMRLIDYLVDEFKKESGMDLKNDPLALQRLKEAAEKAKIELSSAQSTDVNLPYITADATGPKHLNVKISRAKLEALVEDLVTRTIEPCRIALKDAGIDASKIDDVILVGGQTRMPMVQKAVADFFGKEARKDVNPDEAVAMGAAIQGAVLAGDVKDVLLLDVSPLTLGIETMGGVMTALIEKNTTIPTKKSQVFSTADDNQGAVTIHVLQGERKQASQNKSLGKFDLADIPPAPRGVPQIEVTFDIDANGILHVGAKDKATGKAQSIVIKANSGLSDEEVERMVRDAEANAEEDRKFEELAAARNQGDALVHSTRKMVADAGDKVTAEEKTAIEAAVVALEAAVKGDDKAAIDAKVEELSKVSAPVAQKMYAEQQAEQPQGGAQQAEPEAKHDDVVDAEFEEVKDNNKQ | Acts as a chaperone. | Q1IF59 |
B8D9I9 | METK_BUCA5 | Methionine adenosyltransferase | Buchnera | MTEYLFTSESVSEGHPDKIADQISDALLDEILKQDLKARVACETYVKTGMVLIGGEITTTAWVDVEEITRKTINDIGYVNSDAGFDANSCAVLSAIGKQSPDINQGINRFDPLKQGAGDQGIIFGYATNETEFFMPAPITYAHLLMQKQSELRKKNILPWLRPDAKSQVTFKYNNGNIIAIDTVVLSTQHQENITQKYLKEAVMDEIIKPVLPDKWLTKNTKFFINPTGRFVIGGPMGDCGVTGRKIIVDTYGGMSRHGGGAFSGKDPSKVDRSAAYAARYVAKNIVASGLAARCEIQLSYAIGIAEPISIMIDTFNTGKISNSALISLVRSIFDLRPYGLIKMLNLLQPIYLKTAVYGHFGRKEFPWENLDKVNELS | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B8D9I9 |
C3NDK6 | FAU1_SULIY | RNA-binding protein FAU-1 | Sulfolobus | MKGRVRIRGIYATALTSIFSSLSYEIVQQSVEIAERFMREVNNLPADITIKDFEYDRGKIIVMGNGTIEEDLHDVFKYSFHWKSPIKLYSVIEADESCTYGNFKVEPCLEEGIVIKPPYDGKIVLSETKAVSKYAMVWRGKGVTTFSEHINNEEERLRLLTLSSPLNRKGYNVKWRSNAKYATLNELKEDLERLVLRYENREFRDQGEDFYLITLSLPDKLHLDEVRKSIVNTVKYHHLLKLSYNREVDSLEKDKEGSPVKLLEALISDFMKIEHIKADGKAIYLRGGKVIEKEVNNDGYRITLRREINGNGVLDGIGKRIENGDYDIVEYNSDKWYQIHRYYSGIDNSLKGIYINISTPPELLKGKIRYLDLEIDIAIRDSEIIVLDEDELNKKSIYMYSSLVNKAKEVANYLIDCIQQNKLI | Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Binds to RNA in loop regions with AU-rich sequences. | C3NDK6 |
D4GU71 | AGL14_HALVD | Probable low-salt glycan biosynthesis reductase Agl14 | Haloferax | MYAFVTGANGLLGSVVVRTLREQGHAVVGSYHSEEPTFDCPLHQVDITDTERVVELLDEYDVDLVINCAAYTDVDGCESNPEVATAVNGTAPGDLAAVCDDREIPFIHYSTDYVFDGETDGFYEEGDEPAPIQEYGRSKLTGEHAVRDVNPDALILRLSFVYGARGDTSDLVGFPQWVASTLAAGDTVPLFTDQTMTPSRAGNVATTTLELLDAGVSGTFHVASQSAVTPSDFGEKICEVIGGDATLIESSVMADLDRPAARPRRSCLDVSNVEGELGCSQPTLEDDLAALEAAFSDYSS | Reductase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. | D4GU71 |
P58409 | HCXB_ECO57 | Phenylpyruvate reductase | Escherichia | MESGHRFDAQTLHSFIQAVFRQMGSEEQEAKLVADHLIAANLAGHDSHGIGMIPSYVRSWSQGHLQINHHAKIVKEAGAAVTLDGDRAFGQVAAHEAMALGIEKAHQHGIAAVALHNSHHIGRIGYWAEQCAAAGFVSIHFVSVVGIPMVAPFHGRDSRFGTNPFCVVFPRKDDFPLLLDYATSAIAFGKTRVAWHKGVPVPPGCLIDVNGVPTTNPAVMQESPLGSLLTFAEHKGYALAAMCEILGGALSGGKTTHQETLQTSPDAILNCMTTIIINPELFGAPDCSAQTEAFAEWVKASPHDDDKPILLPGEWEVNTRRERQEQGIPLDAGSWQAICDAARQIGMPEETLQAFCQQLAS | Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. | P58409 |
P13716 | HEM2_HUMAN | Porphobilinogen synthase | Homo | MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE | Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. | P13716 |
A5ESQ6 | FMT_BRASB | Methionyl-tRNA formyltransferase | unclassified Bradyrhizobium | MPLRLIFMGTPDFAVPTLLELAGHGHEIAAVYTRAPKPGGRRGLALVPTPIETEARRLGIPVVTPKTLKTEEALTAFRAHQADAAVVVAYGMILPQAILDAPKLGCYNLHASLLPRWRGAAPINRAIMAGDAETGVMVMKMDVGLDTGDVAMAERLPITDAMTASDLHDQLARIGADLMVRAMAALERGGLTLTKQADAGVTYAAKIEKAEARIDWSKPANAVLRHIHGLSPFPGAWSEVTLDGEAVRLKILRCALADGRGEPGAVINEQLTIACADGAVRVTELQRAGKGPMKAADFLRGTRVAPGLRFG | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | A5ESQ6 |
Q9QYZ8 | DKK2_MOUSE | Dickkopf-related protein 2 | Mus | MAALMRVKDSSRCLLLLAAVLMVESSQLGSSRAKLNSIKSSLGGETPAQSANRSAGMNQGLAFGGSKKGKSLGQAYPCSSDKECEVGRYCHSPHQGSSACMLCRRKKKRCHRDGMCCPGTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHSKMPHIKGHEGDPCLRSSDCIDGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI | Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. | Q9QYZ8 |
Q49YP8 | FUMC_STAS1 | Iron-independent fumarase | Staphylococcus | MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRGAALANHALGKLSDAKKDAIVYACDRVLNKELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANTYLKEQGIDESIHPNDDVNKSQSSNDTFPTAMHVALYNEVETKLEPALKTLRDTFKQKEEQYHDIIKIGRTHLQDATPIRLGQEISGWRYMLDKCETLLSESKAHILNLAIGGTAVGTGINAHPEFGDKVAKFIAENTGYPFVSSENKFHALTAHDEVVQLHGTLKALATDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTAVGIASSQGNFELNVYKPVILLNTLQSIYLLADGMDTFNNNCAVGIEPIPENIDNYLNQSLMLVTALNPHIGYEKAASIAKKAHREGLTLKESAIDSGYVTEEQFEQWIKPEDMVEPK | Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate. | Q49YP8 |
A1VPR5 | ATPB2_POLNA | F-ATPase subunit beta 2 | Polaromonas | MTDGGLQADAPHLGVVVSVRGSVVDVRFDTHLPPIHTVLHADEGRIIVEVLAQRDAHHVRAIALTPTQGLARGMPVVDTGGPLKAPVGKGILSRMFDVFGNTIDRLPAPPDIQWRSVHRAPPALARRSTRSEVFVTGIKVIDVLLPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGHQEGISIFCGIGERCREGEELYRDMKDAGVLPSMVMVFGQMNEPPGSRFRVGHAALTMAEYFRDDEHRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTMGTELSGLEERIANTDSGAITSIQAVYVPADDFTDPAAVHTFSHLSASIVLSRKRASEGLFPAIDPLQSSSKMATPGIVGERHYALAQEIRRTLAQYAQLKDIIAMLGLEQLSPQDRNVVGRARRLERFLTQPFFTTEQFTNLPGKLVSLEDALDGCERILRDEFKDCPESALYMIGKIDEARARKTEAIDVHES | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | A1VPR5 |
P43100 | NIA_BEABA | Nitrate reductase [NADPH] | Beauveria | MAVKSQLGVTYTTKTFPPSPPRTVGNSHAGSDDERDEVDATPTTPPVEKLGQLLKPYSLPPTNTPTHVLPEDLKTPDHRVNRDPRLIRLTGVHPFNVEPPLTDLYDEGFLNSENLHYVRNHGPVPHCPDDESLNWTFTVDGLVEKPFTIAVRDLIQKYDQFTYPVTLVCAGNRRKEQNVVRKSKGFSWGAAGLSTALWTGVPIGALLRMAKPKRAAKYVCFEGADKLPNGYYGTSVKLNWCMDENRGIMVAHKMNGQSLHPDHGKPVRIIIPGQIGGRSVKWLKKITITSEPSDNWYHIYDNRVLPTTISPDASANLPDVWKDEKYAIYDLNANSAICYPRHDERLVLATAPDTYKVRGYAYGGGGKRITRLEVTLNKGKSWLLAGIHYPEDDYRRAPDGDLLYGGSTDMWWRETCFCWCFWEIDIPVADLSAADDIMIRAMDEGMMVQPRDMYWSVLGMMNNPWFRVVIHKEDGALRFEHPTQPALMPGGWMERVKRRGGNLTNGFWGEKTAAEEEQVLAEPEKEICMTNPKVVRIISLEELKAHEGEMEPWFVVNGHVYNGTPYLDNHPGGATSIINAAAQDATEEFMTIHSENAKAMMPQYHIGTLNDAARKALEGSAEESPASDPTRAVFLQPKYWSKAILETKTDVSSDSKIFSFRLDHAAQSIGLPTGQHLLVRLRDPATREAVIRAYTPLSETHAKGQLDILIKIYRDVPGQPGGKMTQALDSIPLGHFVDIKGPVGKFEYLGKGHCTVSGTSRHVRRFVMICAGSGVTPIFQVLRAVTSDAQDGTECLVLDGNRCEKDILCREELDAMVARAPARTTLLHKLSRPDASWCGLRGRMDKEYLEEHIGGFRKSDGREMVLVCGPAALEETVRSVLVEMAWKPEDMLFF | Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | P43100 |
B8J4R6 | RL31_DESDA | 50S ribosomal protein L31 | Desulfovibrio | MKKDIHPKVFNATITCACGNEEKVLSTKGEQVNVEVCSACHPFFTGKQRFLDTAGRIDRFRKKYAKFEQK | Binds the 23S rRNA. | B8J4R6 |
P0CO53 | KYNU_CRYNB | L-kynurenine hydrolase | Cryptococcus neoformans species complex | MSNDLPTKKDLVKWDQEDALNWTRGEYEIPNSKACGGEADGKAIYFCGNSLGLLNKKARQHIMEELDVWSTSSVTGHFNHPYQRPWKHVDEPLTPHLAKLVGAREEEVAHTSTLTSNMHNLFTSFYQPTEKRWKIVIEKGSFPSDWYAVHSHPRLHDKVLRPEQIDNAIIALVPREGEDTLRTEDILKVLDDNKDSIAIVWLPLVQYYTGQLFDISSISPKVHEIGALLGLDMAHGIGNVECKLNEWNVDFAVWCTYKYLNAGPAAIGGFYIRSGLEDGGRRLAGWWGNDARTRFHMSPNFQPTPGAKGYQHSCTPVFSSIPLLATLQLIEAVGFSNMVEKARRLTGTLEALLKASRYYVHPADPKGKIGFKIITPAAPYRGTQLSLVILPEEEHVMPKVFDRMLRKGLVGDERKPSVIRLSPVVLYNTFEEVGRAVEIVEEALEEEEEERKR | 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. | P0CO53 |
P06131 | FDHA_METFO | Formate dehydrogenase subunit alpha | Methanobacterium | MDIKYVPTICPYCGVGCGMNLVVKDEKVVGVEPWKRHPVNEGKLCPKGNFCYEIIHREDRLTTPLIKENGEFREATWDEAYDLIASKLGAYDPNEIGFFCCARSPNENIYVNQKFARIVVGTHNIDHCARLCHGPTVAGLAASFGSGAMTNSYASFEDADLIFSIGANSLEAHPLVGRKLMRAKMNGAYFIVADPRYTPTAKQADQYIPFKTGTDVALMNAMMNVIISEGLEDKEFIEKRTKNYEELKEVVSKYTPEMAEEITQVPADVIRDIAIKYAKADKAAIVYSLGITEHSHGVDNVMQTANLAMLTGNIGRLGTGVNPLRGQNNVQGACDMGALPTDYPGYRKVADQEVMEDVTCTWGCSDLGCEPGLKIPEMIDAAAKGDLKVLYITGEDPVISDPDTHHVEEALNNLDFFVVQDIFMTDTAEFADVVLPAACWAEQEGTFTNGERRVQLIRKAVDAPGESKYDWEIFCDLAKKMGADPEMFTYESAQDIFEEVRTVTPQYAGMNRERLDRPEALHWPCPSEDHPGTAMMHIEKFAHPDGLGIFMPLEEQGPMETPDDEYPLILTTTRLLFHYHAAMTRRAATLDREVPTGYVEINTEDAAELGIANKEKVKVKSRRGEIEIAARVTDDIVKGIVNIPMHFRECSANILTNAAAIDPKSGMPEYKACAVAISKMEGSK | Catalyzes the oxidation of formate. | P06131 |
Q9LS90 | LFR_ARATH | Protein LEAF AND FLOWER RELATED | Arabidopsis | MQKRELGKSGGNSGGSSGPPAKRGRPFGSTSANSAAAAAAAAAADAMSPSALLGPSLLVHNSFVEQNNRRIVLALQSGLKSEVTWALNTLTLLSFKEKEDIRRDVMPLAKIAGLLDALLLIIDDWRDIALPKDLTRGTRVRTLGTNASVTGFGNEYDALASIQPPGSGIGSSAAEALGKKSTGKHQSSQWWMEEDGLFNLDDEGRSEKQMCAIAASNVIRNFSFMPDNEVVMAQHRHCLETVFQCIHDHMTEDEELVTNSLETIVNLAHLMDLRIFSSLKQSYININEKKAVQAVVGILNSSVKAWNCAAAELLGRLIINPDNEPFISPLIPQIHKRLIDLLSIQAVDAQAAAVGALYNLVEVNMDCRLKLASERWAVDRLLKVIKTPHPVPEVCRKAAMILENLVSEPQNRGLLLAYENAFAELLFQEGKYSDSFARILYELTARSNSRVASARGIWGM | Involved in leaf and flower development . Plays roles in leaf development partly by associating with AS2 and repressing KNAT1/BP transcription . Required for the formation of anther cell layers and normal expression of genes that regulates anther development . | Q9LS90 |
A4WNA4 | RPO3_PYRAR | DNA-directed RNA polymerase subunit D | Pyrobaculum | MPRVSIVEKSQLFLKAIVEGVPPSLVNSLRRVIISELPVMAIDTVVVVNNTSVMYDEFLAQRLGLIPLTTPLHSLPTYEECATGVADPTECGTRLVLQVTADGDVTVYSGDLTSERPDVVPVYKDIPIVKLVKGQSIVIEAYAKLGIAKDHAKWQAATASYYYYPKVIIKDEKCREICKEICPDLEDPVKCTFNKAWTCKDLCKGGLDVEWEKNKYVFWVESFGNYGVDVALKEAFRILKRKFEAFTEELVKKASSGER | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A4WNA4 |
A9BPR7 | RS10_DELAS | 30S ribosomal protein S10 | Delftia | MSKQKIRIRLKAFDYKLIDQSAAEIVDTAKRTGAIVKGPVPLPTRMKRFDILRSPHVNKTSRDQFEIRTHQRLMDIVDPTDKTVDALMKLDLPAGVDVEIKLQ | Involved in the binding of tRNA to the ribosomes. | A9BPR7 |
P40319 | ELO3_YEAST | v-SNARE bypass mutant gene 1 protein | Saccharomyces | MNTTTSTVIAAVADQFQSLNSSSSCFLKVHVPSIENPFGIELWPIFSKVFEYFSGYPAEQFEFIHNKTFLANGYHAVSIIIVYYIIIFGGQAILRALNASPLKFKLLFEIHNLFLTSISLVLWLLMLEQLVPMVYHNGLFWSICSKEAFAPKLVTLYYLNYLTKFVELIDTVFLVLRRKKLLFLHTYHHGATALLCYTQLIGRTSVEWVVILLNLGVHVIMYWYYFLSSCGIRVWWKQWVTRFQIIQFLIDLVFVYFATYTFYAHKYLDGILPNKGTCYGTQAAAAYGYLILTSYLLLFISFYIQSYKKGGKKTVKKESEVSGSVASGSSTGVKTSNTKVSSRKA | Component of a microsomal membrane bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase III, which synthesizes 20-26-carbon fatty acids from 18-carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation of malonyl-CoA . The enzymes active site faces the cytosol, whereas VLCFA length is determined by a lysine near the luminal end of transmembrane helix 6 . Plays an important role in lipotoxic cell death induced by oleic acid through maintaining a balanced fatty acid composition in thr plasma membrane . Affects plasma membrane H(+)-ATPase activity. May act on a glucose-signaling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1, HXT3 and SNF3 . | P40319 |
A6ZSZ4 | IPI1_YEAS7 | Involved in processing IST2 protein 1 | Saccharomyces | MTKSRKQKQKKQDFLRKKLKVGKPKEKARNATDTSFVSKTISIRNQHLDQNPHDLTKRLTLLKHHNINVRKETLTTFQKSIPSIIKSRLMTPLLTQSIPLICDESQQVRQGLIDLVDEIGSHDAEILKLHCNIFVLYINMAMTHIVTQIQADSTKFLSHLLKYCGDEVVRKSWVKLLNGVFGVLGWGQVGKNDSASIVQTKKRNAKYVTIHLNALYTLVEYGCQDERARSDGDTAETTEDSGTLRNPYLIPDYPQPFEHLKLFTRELKVQDATSSGVNATLLSLATQDIDTRKAVFIEQFLPIVRKKIEVIIKEGGECGKSANKLKTLLAKIFD | Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA. | A6ZSZ4 |
Q3IUB3 | NAC_NATPD | Nascent polypeptide-associated complex protein | Natronomonas | MFGGGGGLNPRKMKQMMNQMGIDLEEIDAEEVVIRTADEELVFDDAEVQLMDAQGQQTYQVVGEPESRERGDSGSEDDSETESGGEFSEDDVEIVAQRAGVSESTARETLEETGDLAAAVQKLE | Contacts the emerging nascent chain on the ribosome. | Q3IUB3 |
A4G1U8 | RUVA_HERAR | Holliday junction ATP-dependent DNA helicase RuvA | Herminiimonas | MIGRLSGVLLEKNPPQLLVDCNGVGYEVNVPMSTFYNLPGLGEKVALLTHLTVREDAHILFGFGTAEERNVFKQLVKITGIGARTALSILSGMSVADLSNAITLQEAGRLTKIPGIGKKTAERLLLELKGKLGADLGAAGGVIHSDATSDILNALLALGYSDKEALLAMKQVPAGTGVSDGIKLALKALSKA | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | A4G1U8 |
Q1IZH7 | SECA_DEIGD | Protein translocase subunit SecA | Deinococcus | MFRVLNKVFDTNQRDVQRIVKTVVQPVNALEEETMKIENLAEAFMRLRQRVQEGGESLDDVLVPAFALIREAGRRAIGKRHYDVQLIGGTALHQGRIAEMRTGEGKTLVATLALALNALEGKGAHLVTVNDYLARVGAEEMGLLYRTLGLSVGLITRDMQPHQRQAAYACDITYVTNSELGFDYLRDNMAQSREQLVLRADNPLHYAIVDEVDSILIDEARTPLIISGAAEKATDLYYVYAKLVKRLQRGEPAEPGKRTEPTGDYTIDEKGKQVHLTEQGIAKIERLLSLGDLYSPENMDKAHMITQAIRARELYHREKDYIVNAEGEVVIIDEFTGRSMPGRRYGEGLHQAIEAKEGVKIENENQTLATITYQNFFRLYDKFAGMTGTAKTEEKEFLDIYGSDVLVIPTNKPVIRQDADDLVYRTRMGKYQAVVEEVKQMHATGRPILIGTASIDTSEQLSALLKQAGIRHSVLNAKYEAQEASIIAQAGRSGTVTIATNMAGRGTDIMLGGNAEFILGEAIEQNFGISRFTPEAEAFIKAIGREDPEAVTLGLRIPGMTEQFIRQAQQLQKDIIADRERVRELGGLHIIGTERHESRRIDNQLRGRAGRQGDPGSSRFYVSFEDDLMRLFASDRVVAMMDRLGMDDTQPIEAKMVTGAIERAQARVEDRNFGIRKQLLEFDNVMSKQRDIIYAQRREVLLGTDEDVEESTEGMIADFTEMQLAFYAPIDQPAESWDLETLRTNMLEAVPQLEHYDFEALRHMAPEAAHAHLLEAVADAFDARKAELGPTMLNSLARYVLLQVVDQHWKEHLHGMDVLRQGIGLRGYGQRDPFTEYKFEATNMFNDMIDNLKADVTKFIFRMQFGQAS | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | Q1IZH7 |
Q65D22 | DEOC2_BACLD | Phosphodeoxyriboaldolase 2 | Bacillus | MTIANLIDHTALKPHTQKSEIKKLIEEAKAYQFASVCVNPTWVEFAAEELKGTEIDVCTVIGFPLGANTTETKAFETKDAIAKGATEVDMVINIAALKDGNDDFVEADIRAVVEAAKGKALVKVIIETCLLTDEEKERACRLAVAAGADFVKTSTGFSTGGATAEDIALMRKTVGPDIGVKASGGIRTKEDVETMISNGATRIGASAGVSIVSGAEGKNEDNY | Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. | Q65D22 |
Q5X3L5 | NTPP_LEGPA | Nucleotide pyrophosphatase | Legionella | MSKFLQQKPIILASSSTIRHKLMKSLGLDFLVVPSNCNEEEIKTRHNSDELVELGITLAKIKALDVSQHYPEHYIIAADQLCVADKRVFNKPLNHQTAVSHLRELSGKEHQQIACLCIVKESKILWQYHETATLTLHHLSEKTIEAYLQAEKPYQSCGAYQYEGLGKWLFKEVQGSEDTILGLPLMPLVNALVNLKVVGI | Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q5X3L5 |
Q9KQ15 | FLGJ_VIBCH | Muramidase FlgJ | Vibrio | MINNSNDIGFIQDIAGLDKLRQKAVNGDENAGQSALTAAARQFESIFTSMMLKSMRDANSDFKSDLMSSQNEDLYRQMLDEQMASEFSSSGSLGLADMIVAQLSTGQTASEQKGEDGFQEAMRRVEHARKTASERSNEDLVAAVYPLRKTQAVQSTQFDSRHSFVTKLKPYADKAARMLGVDSSLLIAQAALETGWGQKMVKNARGNSNNLFNIKADRSWQGDKVATQTLEYHNNVPVVEKAAFRSYASFDESFNDYVRFLENNPRYTNALDHGGNSERFIHGIHRAGYATDPQYADKVLRVKAQIDQMNLYKSPAGIFRRHSFSSSIFSAYQS | Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space. | Q9KQ15 |
O84875 | CDUB2_CHLTR | Deubiquitinase and deneddylase Dub2 | Chlamydia | MEPIHNPPPQTCSYSRPSTTYTSFKDASCGTKVTRIIIALFLIVISCGLILCAYTFRDLLDADYSAQEGPQQATKLLQQLDKVLTGPPLPIWDNEHLFQFSCLMQNKHRRVLPIDICNPLTKFNFLEYICNCLMTKQSVNVNETDMCELFCPPTCTPENYRRLLCTSSVFPFVMWHDPSADTQEAMLTKMDQTMSSGRVGNSHWVLVIVDIEHRCVTFFDSFYDYIASPQQMREQLEGLAASLGAIYPKEGGADSDQEELLSPFQVRIGSTVKVQSPGEFTCGAWCCQFLAWYLENPDFDLEEKVPTNPSERRALLADFISTTEQAMSRYSSLSWPTTD | Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities. | O84875 |
Q6JWR2 | S38A7_RAT | Solute carrier family 38 member 7 | Rattus | MAQVSINSDYSEWGSSTDAGERARLLQSPCVDVVPKREGEASPGDPDSGTTSTLGAVFIVVNACLGAGLLNFPAAFSTAGGVAAGIALQMGMLVFIISGLVILAYCSQASNERTYQEVVWAVCGKLTGVLCEIAIAVYTFGTCIAFLIIIGDQQDKIIAVMAKEPDGASGSPWYTDRKFTISLTAFLFILPLSIPKEIGFQKYASSLSVVGTWYVTAIVIIKYIWPDKEMRPGDILTRPASWMAVFNAMPTICFGFQCHVSSVPVFNSMRQPQVKTWGGVVTAAMVIALAVYMGTGICGFLTFGAAVDPDVLRSYPSEDVAVAVARAFIILSVLTSYPILHFCGRAVVEGLWLRYKGTPVEEDVGRERRRRVLQTLVWFLLTLLLALFIPDIGKVISVIGGLAACFIFIFPGLCLIQAKLSEMEEVKPASWWALVSYGVLLVTLGAFIFGQTTANAVFVDLLA | Mediates sodium-dependent transport of amino acids, preferentially L-glutamine. | Q6JWR2 |
Q83S80 | FLAV_SHIFL | Flavodoxin 1 | Shigella | MAIHGIFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYGEAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIDADWPTAGYHFQASKGLADDDHFVGLAIDEDRHPELTADRVEKWVKQISEELHLDEILNA | Low-potential electron donor to a number of redox enzymes. | Q83S80 |
Q3AGL2 | RL9_SYNSC | 50S ribosomal protein L9 | unclassified Synechococcus | MPKRVQIVLNEDILSLGMDGDLVEVAPGYARNFLLPFGKAVPLTPAVMKQVEHRRAKEAERQAALKQEAVDFKTALSTIGRFTVKKQTGEDNVLFGTVTNGDVAEAIETATKKEIDRRDIVVPEIHRTGKYTVTVKLHSEVTAEINLEVVGY | Binds to the 23S rRNA. | Q3AGL2 |
Q4USQ8 | PYRH_XANC8 | Uridine monophosphate kinase | Xanthomonas | MSELSYRRILLKLSGEALMGDGDYGIDPKVINRLAHEVIEAQQAGAQVALVIGGGNIFRGAGLAASGMDRVTGDHMGMLATVINALAMQDALEKLGAKVRVMSAIKINDVCEDFIRRRAIRHLEKGRIAIFAAGTGNPFFTTDSGAALRAIEIGADLLLKATKVDGVYDKDPKKHSDAVRYDSLTYDEVIMQGLEVMDTAAFALARDSDLPLRIFGMSEPGVLLRILHGAQIGTLVQGRS | Catalyzes the reversible phosphorylation of UMP to UDP. | Q4USQ8 |
C0HL02 | BR2RJ_PELRI | Brevinin-2Rj | Pelophylax | GIFLDKLKNFGKDVAGILLKKASCALSGQC | Antimicrobial peptide. | C0HL02 |
Q32M08 | DUS4L_MOUSE | tRNA-dihydrouridine synthase 4-like | Mus | MRSDSLPTTICQERKKDPIEMFHSGQLVKVCAPMVRYSKLAFRTLVRKYSCDLCYTPMIIAADFVRSIKARDSEFTTNQGDCPLIVQFAANDARLLSDAALLVCPYANGIDINCGCPQRWAMADGYGACLINKPELVHDMVRQVRNRVESPRFSVSIKIRIHDDLARTIDLCRKAEATGVSWITVHGRTVEERHQPVHYDAIKMIKENVSIPIVANGDIRSLKEAENVWQMTGTDGVMVARGLLANPAMFAGYEETPLKCIWDWVDISLELGTPFMCFHQHLMYMMEKITSRQEKRVFNALSSTSAVLDYLTDHYGDESLSKSL | Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. | Q32M08 |
P34729 | RAS1_PHYPO | Ras-like protein 1 | Physarum | MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVTIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSFDEIASFREQILRVKDKDKVPMIVVGNKCDLEGERQVTTGEGQDLARSFGCPFMETSAKSRVNVEESFYQLVREIRKDSRTDTKGPGGKGGKKTLKCLLL | Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. | P34729 |
Q32NM1 | CCNOB_XENLA | Cyclin-O protein B | Xenopus | MVTCSMRCTEEGLLGATLAFSSGKRKRDSVYSPGDATPGDRGEGEPKCPSVGTKKRAKYSRHRKQSLELRSCDSGVADLYETPSPSPVAPSPTHEPWDTCTPMYDGLGLQNFRDYGQDCYTFNKSLEDKFLAVNCLKNQPQIQAESRCKLISWLIPVHRHLNLGFESLCLTVNILDRFLACTPVASDCFQLVGVTSLLIASKQVETRPPRVKQLLALCCDAFSREQLCNLECIILLKLHFRLGAPTINFFLQHFSLLRVTNEESSDTELSETTKSVTVARGIAELSLADYAFNSYSPSLMAVCCLEIADRMLCHRNPIRARVSDYHESLIQECVGKIDLLVSLNQDSLHRLLPSQFAVKSINVDN | Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of mcidas to promote mother centriole amplification and maturation in preparation for apical docking. | Q32NM1 |
Q3UQU0 | BRD9_MOUSE | Bromodomain-containing protein 9 | Mus | MGKKHKKHKAEWRSSYEDYTDTPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHREKKKKKKKKSEKEKHLDEEERRKRKEEKKRKREKEHCDSEGEADAFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQRLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKAALLGSEDPAAEEPVPEVVPVQVETTKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKKLGDGSLLYSVVNAPEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSASTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKMVDDLLDQITGGDHSRMIFQLKQRRSIPMRPADEMKVGDPLGESGGPVLDFMSMKQYPDVSLDVSMLSSLGKVKKELDHEDSHLNLDETARLLQDLHEAQAERGGSRPSSNLSSLSTASEREHPPPGSPSRLSVGEQPDVAHDPYEFLQSPEPAAPAKN | Plays a role in chromatin remodeling and regulation of transcription. Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Orchestrates also the RAD51-RAD54 complex formation and thereby plays a role in homologous recombination (HR). | Q3UQU0 |
B7KFZ3 | DUT_GLOC7 | dUTP pyrophosphatase | Gloeothece citriformis | MKLKVTKLEKAAILPKYVHSDDSGLDLSAIEDLEIPPGESQLVPTGIAIELPPNTEAQIRPRSGLALKHQITVLNTPGTVDEGYRGEIGVILINHGKNSFKVTRGMKIAQMVIAPVIRVEVEEVDHLSDTTRGSGGFGSTGLTSD | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | B7KFZ3 |
Q057X8 | RS20_BUCCC | 30S ribosomal protein S20 | Buchnera | MANIKSSKKHISISEKRRKYNCSKRSMIKTFMKKVLFFIKEKNRIKAIKFFYIFQSLVDRYSLKKIIHINKASRYKSVLMNNIKKI | Binds directly to 16S ribosomal RNA. | Q057X8 |
Q26065 | ACT_PLAMG | Actin, adductor muscle | Placopecten | MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Q26065 |
Q17Z21 | PANC_HELAH | Pantoate-activating enzyme | Helicobacter | MQVLETISDLREYRKNVKESVGFVPTMGALHKGHQSLIERSLKENFHTITSVFVNPTQFGANEDFSAYPRPLEKDLALCEKLGVDVVFVPKISEMYPYKSEQRLKLYAPKFLSHSLEGAMRKGHFDGVAQVVLRLFHLVNPTRAYFGKKDAQQLLIIQHLVKDLLLDIEIVPCEIVRDSDHLALSSRNVYLNAVERKQALAIPKALENIQQAIDMGEKACEMLKKIGLEILKNLEVDYLEFCNHKLEPLKIIEPTNTLILVAARAGKTRLLDNLWV | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q17Z21 |
Q136T8 | NRDR_RHOPS | Transcriptional repressor NrdR | Rhodopseudomonas | MRCPNCNSLDTQVKDSRPTEDSSVIRRRRVCIACNFRFTTFERVQLRELTVIKRNGRRVPFDRDKLVRSVQISLRKRPVEPERVEQLVSAIVRELESSGEADISSETIGEIVMDHLRKLDDVAYVRFASVYRNFREAKDFEAVLGELSGEEEARPTLVRK | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | Q136T8 |
B5ZB39 | RS10_UREU1 | 30S ribosomal protein S10 | Ureaplasma | MNQELRIRLESYDHRLLDDTVKTIVDISNSTGSKLRGPIPLPTKKEIFTILRSPHVNKSSREQFERRTHKRLIILENPQPKTMEALKRLSVPFGVEVTFKI | Involved in the binding of tRNA to the ribosomes. | B5ZB39 |
P70195 | PSB7_MOUSE | Proteasome subunit Z | Mus | MAAVSVFQPPVGGFSFDNCRRNAVLEADFAKKGFKLPKARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLTTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPFSVPNKKGTRLGRYRCEKGTTAVLTEKVTPLEIEVLEETVQTMDTS | 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). Within the 20S core complex, PSMB7 displays a trypsin-like activity. | P70195 |
Q5JGC8 | SYT_THEKO | Threonyl-tRNA synthetase | Thermococcus | MRMLLIHSDYLEYEVKDKALKNPEPISDEQKTGRLDEVLAVFISVEKVDETNPDEVVEKAVKEIEDVASQIKAERIFVYPFAHLSSELAKPDVALEVLRKIEEKLREKGYEVKRAPFGYYKAFKLSCKGHPLAELSRTIVPEKAVSKEERNIALEKEEKELKSYWYILTPEGELIDVDKFDFTGHENLKKFVNYEIAKNRVADREPPHVRLMLEQELVDYEPGSDAGNLRYYPKGRLIKSLLEQYVTEKVIEYGAMEVETPIMYDFEHPALEKYLNRFPARQYVVKSGDKKFFLRFAACFGQFLIKKDATISYRNLPLRMYELTRYSFRREKSGELSGLRRLRAFTMPDMHTVARDLKQAMDEFKKQYKLSMEVLKGVGLTPEDYEVAIRFTRDFWEQNRDFIVELAKIIGKPVLIEMWDQRFFYFILKFEFNFVDNLDKAAALSTVQIDVENAERFGIKYYDEEGKERTPLILHCSPSGAIERVMYAILEKQAKLQEKGIKPMYPLWLSPIQVRVIPVSDEVMDYALYVAGKLEGAKIRVDVDDTGDRLNKKIRKAEKEWIPYIIVVGRNEKEQNTVTVRRRSDGRQVEMQLEDLIREIKGQTEGFPYKPRPLPLLLSRRPKFRG | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q5JGC8 |
B3PBR5 | ACCA_CELJU | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Cellvibrio | MNLNYLDFEQPIAELEGKIEELQLVGNSSDVNLADEVAKLREKSTKLTETIYSKLTAWDIVKVARHPQRPYASDYISRVFTEFDELHGDRHFGDDKAIIGGVGRLDGKPVMVIGEEKGRSVHEKVMRNFGMPRPEGYRKALRLMEMAERFKLPVLTLIDTPGAYPGIDSEERGISESIAQNLAVMSRLRTPIVCTVIGEGSSGGALAIGVGDHLNMLQYSTYFVISPEGCANIIWKTVAKAPEAAQAMGVTSKVLQDLGIVDETIPEPLGGAHRNVDEMARKLQERLVEQVEQLSREPIDALLERRYQRLMSYGN | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. | B3PBR5 |
Q67KP1 | NUOI2_SYMTH | NDH-1 subunit I 2 | Symbiobacterium | MGVTNFFGEAWRTGKSIVTGLGITFREMMFRPAITVFYPEQRDDVPPWFRGIPVLKTDLRTGEYKCTSCMQCAQACPVNVITIEWHQDPETKKKVCDRFAIDMSRCMLCNFCVEACPFDSLVMGYDYELCKVNPENLVFEFEDLLRLGLKYSKAEEPGPKATRSSTPPWVFHGLTNATEDDIQDIHGYLGRPPLPKGYEPELKPQFRKPAEEAAEAQQAEAAGQPAAEPGKTNGEEAGQP | 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. | Q67KP1 |
P05066 | PHR_YEAST | Photoreactivating enzyme | Saccharomyces | MKRTVISSSNAYASKRSRLDIEHDFEQYHSLNKKYYPRPITRTGANQFNNKSRAKPMEIVEKLQKKQKTSFENVSTVMHWFRNDLRLYDNVGLYKSVALFQQLRQKNAKAKLYAVYVINEDDWRAHMDSGWKLMFIMGALKNLQQSLAELHIPLLLWEFHTPKSTLSNSKEFVEFFKEKCMNVSSGTGTIITANIEYQTDELYRDIRLLENEDHRLQLKYYHDSCIVAPGLITTDRGTNYSVFTPWYKKWVLYVNNYKKSTSEICHLHIIEPLKYNETFELKPFQYSLPDEFLQYIPKSKWCLPDVSEEAALSRLKDFLGTKSSKYNNEKDMLYLGGTSGLSVYITTGRISTRLIVNQAFQSCNGQIMSKALKDNSSTQNFIKEVAWRDFYRHCMCNWPYTSMGMPYRLDTLDIKWENNPVAFEKWCTGNTGIPIVDAIMRKLLYTGYINNRSRMITASFLSKNLLIDWRWGERWFMKHLIDGDSSSNVGGWGFCSSTGIDAQPYFRVFNMDIQAKKYDPQMIFVKQWVPELISSENKRPENYPKPLVDLKHSRERALKVYKDAM | 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. | P05066 |
F0SLK8 | NNRE_RUBBR | NAD(P)HX epimerase | Rubinisphaera | MSRVLSRDQSREVDQIAIEQFHLPGVVLMENAGRNCAELIRQLSPAGQILILAGKGNNGGDGFVIARHLHNAGLNVKLLVFANPEDYSGEAESNWRIITAMQLPAVSNATAADLSQALAELPESSLIVDALLGTGIRGQVRAPFDEIITAVNAYRDDHPHAIVFAVDVPSGLDCDTGLPCGVAIKADQTATFVMLKQGFVTGDGPEYTGTTHVIDIGIPPALLDRLTAE | Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. | F0SLK8 |
P0C299 | TX32_ANDCR | Toxin Acra III-2 | Androctonus | ADVPGNYPLNTYGNMYYCTILGENEFCKKICKVHGVSYGYCYNSYCWCEYLEGKDINIWDAVKNHCTNTNLYPNGK | Binds to sodium channels (Nav) and affects the channel activation process. | P0C299 |
Q035A8 | RS11_LACP3 | 30S ribosomal protein S11 | Lacticaseibacillus | MAGRKTTRKRRVRKNVESGVAHIHSTFNNTLVMITDPRGNAIAWSSAGALGFKGSRKSTPFAAQMAAEAAAKESMEHGMKSVEVAVKGPGSGREAAIRSLQATGLEVTAIRDVTPVPHNGSRPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | Q035A8 |
P93568 | SSY1_SOLTU | Soluble starch synthase I | Solanum | MGSLQTPTNLSNKSCLCVSGRVVKGLRVERQVGLGFSWLLKGRRNRKVQSLCVTSSVSDGSSIAENKNVSEGLLLGAERDGSGSVVGFQLIPHSVAGDATMVESHDIVANDRDDLSEDTEEMEETPIKLTFNIIFVTAEAAPYSKTGGLGDVCGSLPMALAARGHRVMVVSPRYLNGGPSDEKYANAVDLDVRATVHCFGDAQEVAFYHEYRAGVDWVFVDHSSYCRPGTPYGDIYGAFGDNQFRFTLLSHAACEAPLVLPLGGFTYGEKCLFLANDWHAALVPLLLAAKYRPYGVYKDARSIVAIHNIAHQGVEPAVTYNNLGLPPQWYGAVEWIFPTWARAHALDTGETVNVLKGAIAVADRILTVSQGYSWEITTPEGGYGLHELLSSRQSVLNGITNGIDVNDWNPSTDEHIASHYSINDLSGKVQCKTDLQKELGLPIRPDCPLIGFIGRLDYQKGVDIILSAIPELMQNDVQVVMLGSGEKQYEDWMRHTENLFKDKFRAWVGFNVPVSHRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPIVHSTGGLRDTVKDFNPYAQEGIGEGTGWTFSPLTSEKLLDTLKLAIGTYTEHKSSWEGLMRRGMGRDYSWENAAIQYEQVFTWAFIDPPYVR | Plays a minor role in starch synthesis in storage organs (tubers), but may contribute to the deposition of transient starch in chloroplasts of leaves. | P93568 |
P55992 | GYRB_HELPY | DNA gyrase subunit B | Helicobacter | MQNYQSHSIKVLKGLEGVRKRPGMYIGDTNVGGLHHMVYEVVDNAVDESMAGFCDTINITLTDEGSCIVEDNGRGIPVDIHPTEKIPACTVVLTILHAGGKFDNDTYKVSGGLHGVGVSVVNALSKRLIMTIKKEGQIYRQEFEKGIPTSELEIIGKTKSAKESGTTIEFFPDESVMEVVEFQAGILQKRFKEMAYLNDGLKISFKEEKTQLQETYFYEDGLKQFVKDSAKKELLTPIISFKSMDEETRTSIEVALAYADDYNENTLSFVNNIKTSEGGTHEAGFKMGLSKAILQYIGNNIKTKESRPISEDIKEGLIAVVSLKMSEPLFEGQTKSKLGSSYARALVSKLVYDKIHQFLEENPNEAKIIANKALLAAKAREASKKARELTRKKDNLSVGTLPGKLADCQSKDPLESEIFLVEGDSAGGSAKQGRDRVFQAILPLKGKILNVEKSHLSKILKSEEIKNMITAFGCGIQESFDIERLRYHKIIIMTDADVDGSHIQTLLMTFFYRYLRPLIEQGHVYIAQAPLYKYKKGKTEIYLKDSVALDHFLIEHGINSVDIEGIGKNDLMNLLKVARHYRYALLELEKRYNLLEILRFLIETKDALSLDMKVLEKSILEKLEGLNYQILRSFATEESLHLHTQTPKGLVEFNLDDNLFKEVLFEEANYTYQKLMEYNLDFLENKDILAFLEEVENHAKKGANIQRYKGLGEMNPNDLWETTMHKENRSLIKLKIEDLEKTDAVFSLCMGDEVEPRRAFIQAHAKDVKQLDV | A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | P55992 |
Q01771 | STADS_BRANA | Acyl-[acyl-carrier-protein] desaturase | Brassica | MALKFNPLVSQPYKLASSARPPVSTFRSPKFLCLASSSSPALSSKEVESLKKPFTPPREVHLQVLHSMPPQKIEIFKSMEDRAEQNLLPHLKDVEKSWQPQDFLPDPASDGFEDQVKELRERARELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAVWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFVSHGNTARQAKEHGDLKLAQICGTIAADEKRHETAYTKIVEKLLEIDPDGTVVAFADMMRKKISMPAHLMYDGRDDNLFDNFSSVAQRLGVYTAKDYADILEFLAGRWRIESLTGLSGEGNKAQEYLCGLTPRIRRLDERAQARAKKGPKIPFSWIHDREVQL | Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons Delta(9) and Delta(10) of the acyl chain. | Q01771 |
A7ZKF0 | OPGC_ECO24 | Glucans biosynthesis protein C | Escherichia | MNPVPAQREYFLDSIRAWLMLLGIPFHISLIYSSHTWHVNSAEPSLWLTLFNDFIHSFRMQVFFVISGYFSYMLFLRYPLKKWWKVRVERVGIPMLTAIPLLTLPQFIMLQYVKGKAESWPGLSLYDKYNTLAWELISHLWFLLVLVVMTTLCVWIFKRIRNNLENSDKTNKKFSMVKLSVIFLCLGIGYAVIRRTIFIVYPPILSNGMFNFIVMQTLFYLPFFILGALAFIFPHHKALFTTPSRGCTLAAALAFVAYLLNQRYGSGDAWMYETESVITMVLGLWMVNVVFSFGHRLLNFQSARVTYFVNASLFIYLVHHPLTLFFGAYITPHITSNWLGFLCGLIFVVGIAIILYEIHLRIPLLKFLFSGKPVVKRENDKAPAR | Necessary for the succinyl substitution of periplasmic glucans. Could catalyze the transfer of succinyl residues from the cytoplasmic side of the membrane to the nascent glucan backbones on the periplasmic side of the membrane. | A7ZKF0 |
Q9SEV2 | TBBN_GUITH | Nucleomorph beta-tubulin | Guillardia | MREIVHVQVGQCGNQIGAKFWEVISHEHGVDTNGTYFGNKDNQIEKIDVYYNEVSGNRFVPRAVLVDLEPGTMDSVRASNYGRLFRPDNFVFGQSGAGNNWAKGHYTEGAELIESAMDIIRKESEQCECLQGFQIAHSLGGGTGSGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNCTLSIHQLVENADEVFCIDNEALYDICFRTLKLVTPSYGDLNHLVSAVMSGITCSLRFPGQLNADLRKLAVNLVPFPRLHFFMVGFAPLGSRGSQQYRSMTVNDLTQQMFDSKNMMAACDPKNGRYLTAAAYFRGKISTKEVDDQMIEIQNKQSEHFVEWIPHNIKSSVCDIPPKGMKMSAAFIGNSTSIQELFKRVGEQFQAMFRRKAFLHWYTGEGMDEMEFTEAESNMQDLVSEYQQYQDAKMDNDAFEDQDLY | 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. | Q9SEV2 |
Q941L2 | BAP1_ARATH | BON1-associated protein 1 | Arabidopsis | MIYFGRSIDNHYTTMMTKTLEIDLRSAEGLKLNRRPIKKKTFAVVKIDEKCRKSNLDESRRSNPTWNYKSEMPINGNEQFIFIEVFYRTGSGHDKKIGEAKIPTNDFMGRYSPEGHLNFLSYRLRDEFGDKCGIVNLSILVKSDPTRDYGACSSQAAVTGLWRPRLETASIDGYGGRTVTGVPVWGLYQRQF | Negative regulator of cell death and defense responses. Exhibits calcium-dependent phospholipid binding properties. | Q941L2 |
Q01066 | PDE1B_RAT | 63 kDa Cam-PDE | Rattus | MELSPRSPPEMLESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELRELRSDAVPSEVRDWLASTFTQQTRAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTAVGPTYSTAVHNCLKNLDVWCFDVFSLNRAADDHALRTIVFELLTRHSLISRFKIPTVFLMSFLEALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLTDDDSKSKSQPSFQWRQPSLDVDVGDPNPDVVSFRSTWTKYIQENKQKWKERAASGITNQMSIDELSPCEEEAPSSPAEDEHNQNGNLD | Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate. | Q01066 |
Q0K6P9 | RPPH_CUPNH | (Di)nucleoside polyphosphate hydrolase | Cupriavidus | MLDREGFRPNVGIILLNARNEVFWGKRIGEHSWQFPQGGIKYGETPEQAMYRELHEEIGLLPEHVRIVGRTRDWLRYEVPDKFIRREIRGHYKGQKQIWFLLRMAGRDCDIHLRATEHPEFDAWRWSHYWVPLEAVIEFKRDVYQLALTELSRFLNRHARVPLSPYGTHGPHGMHGRHGGPRSQALSRAQQAQQADADCNAEAAHATEHDSPATPVSTSRSTDD | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. | Q0K6P9 |
Q9ZNU6 | DET1_SOLLC | tDET1 | Solanum subgen. Lycopersicon | MFKTNNVTARLFERQICTPAPGTSIHRARRFYENVVPSYTIYDVECPDHSFRKFTDDGLYFVSFSRNHQDLVVYRPTWLTFSCKEEDCDTHDLPLKARKFESFFTQLYSVTLASSGELICKDFFLYMESNQFGLFATSTAQIHDAPPTGGAIQGVPSVEKITFHLLRLVDGAILDERVFHNDYVNLAHSIGAFLYDDLLAIVSLRYQRIHILQIRDSGDLVDVRAIGEFCREDDELFLNSNSQVLVNHVGNGFHHSLPQSETSFLSGIKQRLLSYIFRGIWNEADQTMRVQCLKKKFYFHFQDYIDLIIWKVQFLDRHHLLIKFGSVDGGVSRNADIHPSFFAVYNMETTEIVAFYQNSADELYFLFELFSDHFHVSSKSSLHMNFMSSHSNNIHALEQLRCTKNKATNFSQFVKKMMASLPCSCQSQSPSPYFDQSLFRFDEKLISAIDRHRQSTDHPIKFISRRQPNILKFKMKPGPEAGSTDGRTKKICSFLFHPILPLALSVQQTLFLQASVVNIHFRR | Component of light signal transduction machinery. Involved in fruit pigmentation and fruit nutritional quality. Acts as a negative regulator of fruit pigmentation. Probably acts by participating in the CDD complex, a complex probably required to regulate the activity of ubiquitin conjugating enzymes. Repression of photomorphogenesis is probably mediated by ubiquitination and subsequent degradation of photomorphogenesis-promoting factors such as HY5. | Q9ZNU6 |
P93703 | C71C3_MAIZE | Protein benzoxazineless 5 | Zea | MALQAAYEYLQQAVGHGAWSSTQTLTLLLIAVPTVLLLLASLAKSTSSSGRGKPPLPPSPPGTLPIVGHLHHIGPQTHISLQELVAKYGHNGFLFLRAGAVPTLIVSSPSAAEAVMRTHDHICASRPWSMASHILRYNTCDVAFSPLGEYWQQTRKLMNTHLLSNKKVYSFRHGREEEVCLVVDNLREAAAKSPSTAVDMSEVLAAYTNDVVSRSVLGSTHRKKGRNTLFREMTMTNVDLLVGFNLEYYIPRWPLTDLLFRLVCWKVTRHLKRWDALLEEVIHEHVEMRKLSGDKEKESDDFIDIFLSRYEEYGFTMDNVKSLLMNVFEAAIETSYLVLESAMAELMNHRRVMKKLQAEVRAYGAEKKLDMIREDDLSSLPYLKASMKEALRLHPPGPLLLPHYSTADCQIDGYHIPANPRVLVNGWAIGRDPAVWEKPEEFMPERFMRDGWDKSNSYSGQDFRYLPFGSGRRICPGANFGLATMEIMLANLMYHFDWEVPNEKEDGCWKVSMDEKFGLMLRRNELLYLVPRASS | Catalyzes the conversion of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) to 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA). | P93703 |
Q71ZX3 | GCSPA_LISMF | Glycine dehydrogenase (aminomethyl-transferring) subunit 1 | Listeria | MAKHRYLPMTEQDEKEMLDVIGVKSIDDLFQDIPEKIRFKRDYDLKPAKSEPALLRELSKLASKNANTTEYASFLGAGVYSHYIPTVVDHVISRSEFYTAYTPYQPEISQGELQAIFEFQTMIAELTGMDLANSSMYDGGTALAEAAMLASGHTKRKKILISGAVHPESSNVLKTYATGQHIEVEVIPELDGKTDIEALKKALSDDIAGFVVQYPNFYGQVEPLAELEKLVHENNSLLLVSSNPLSLGLLTPPGEFGADIVVGDSQVFGIPESFGGPHCGFFAVTNKLMRKVPGRLVGETVDENGKRGYVLTLQAREQHIRRDKATSNICSNQALNALASSVAMATLGKTGLVEMAKQNLDKSHYAKQKFREKGFEVLFSDGFFNEFVVKLSKPIKEVNESLLDEGIIGGYDLGFYEEKYENHMLVAVTEMRTKEEIDAFVASLEGAK | The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. | Q71ZX3 |
B5F8P1 | GLPE_SALA4 | Thiosulfate sulfurtransferase GlpE | Salmonella | MEQFECITVEEAYQKLRQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGAFMRKHGFDTAVMVMCYHGNSSKGAAQYLLQQGYDAVYSIDGGFEAWHRRFPANVANGA | Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. | B5F8P1 |
Q9W6A7 | OPSR1_DANRE | Red cone photoreceptor pigment 1 | Danio | MAEHWGDAIYAARRKGDETTREAMFTYTNSNNTKDPFEGPNYHIAPRWVYNVATVWMFFVVVASTFTNGLVLVATAKFKKLRHPLNWILVNLAIADLGETLFASTISVINQFFGYFILGHPMCIFEGYTVSVCGIAALWSLTVISWERWVVVCKPFGNVKFDAKWASAGIIFSWVWAAAWCAPPIFGWSRYWPHGLKTSCGPDVFSGSEDPGVQSYMVVLMITCCIIPLAIIILCYIAVYLAIHAVAQQQKDSESTQKAEKEVSRMVVVMIFAYCFCWGPYTFFACFAAANPGYAFHPLAAAMPAYFAKSATIYNPVIYVFMNRQFRVCIMQLFGKKVDDGSEVSTSKTEVSSVAPA | Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Q9W6A7 |
Q1KXR9 | RK22_HELAN | 50S ribosomal protein L22, chloroplastic | Helianthus | MLNKRTTEVYALGQHISMSAHKARRVIDQIRGRSYEETLMILELMPYRACYPIFKLVYSAAANASSNMGSNEANLVISKAEVNKGTIMKRLKPRARGRSFAIQKPTCHITIVMKDISLDEYIDTDSIAWSQNKKKDTTMSYYDMYSNGGTWDKK | 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. | Q1KXR9 |
A2WWV5 | ERG1_ORYSI | Rpp17 | Oryza sativa | MAGSGVLEVHLVDAKGLTGNDFLGEIGKIDPYVVVQYRSQERKSSVARDQGKNPSWNEVFKFQINSTAATGQHKLFLRLMDHDTFSRDDFLGEATINVTDLISLGMEHGTWEMSESKHRVVLADKTYHGEIRVSLTFTASAKAQDHAEQVGGWAHSFRQ | May play a role in plant defense signaling. Isoform 2 binds to phospholipids in a Ca(2+)-dependent manner in response to pathogen elicitors. | A2WWV5 |
K9NBS6 | AAM_RHOER | Acylamidase | Rhodococcus erythropolis group | MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA | Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency. | K9NBS6 |
O94609 | UBA1_SCHPO | Poly(A)+ RNA transport protein 3 | Schizosaccharomyces | MSNNMNIDQTDQNTIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGGAVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQIAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTDMDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERVGPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLGTKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLFEGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSFEECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLSFDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKSGIKIQVNENEEAPETAANKDKQELKSIADSLPPPSSLVGFRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRKHLVLEICCDDANGEDVEVPFICIKL | Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. | O94609 |
Q8GYP8 | FB310_ARATH | F-box protein At1g56610 | Arabidopsis | MGFALVLIFLFGFYLFLMKSSSIFPQRPFTFLYDLWVLLLVLRFLFSLIQILILCLFNFRFVEMTSNNKKKKTELCDLPKCLAPHILSWLPTKTAVTVSLLFMKGWWRSEMKNLSSLKFSFSDDQEEEHFVRFVDQVLRQRGNRKLDSFSLTLNDEIDGGFVTHLVDYPLDNGVEKLKLSIYDIKGNFQLSSRVFSQATLVTLKLATNRSLIWINGDDVAAAHLPCLKTLWLDDVLVADVKVFVRLLSRCPILEELVMIDMKWHNWEACFVVSASLRRLKIVWTDYVEMDEYDRCPQSVLFDTPNVLYLEYTDHIAGQYPLLKFSSLIEAKIRLEMIDEKEEEDEGQEVIVGDNATAFITGITSVRKLYLYANTIQVLHHYFDPPIPEFVYLTHLTIQSDKELGWDAIPELLSKCPHLETLVLEGLFHLATDVCGDVCPCRRNMEQAISYLVKSPVTHLEIYEGVVGKKRGEVTEDAARFGEQVRWFLMRMLHLQQVKIYGQTEDSVTALYDIATELRRLEGKASPNVQISVLQA | Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. | Q8GYP8 |
Q56RZ6 | LTMM_EPIFI | Lolitrem B biosynthesis cluster 1 protein M | Epichloe | MTSDFKVIIVGGSVAGLSLAHCLEKIGVSFMVLEKGNQIAPQLGASIGILPNGGRILDQLGIFHSIEDEIEPLESAMMRYPDGFSFKSQYPQALHTSFGYPVAFLERQRFLQILYDKLKSKDCVFTNKRVVSIASGQDKVTAKTSDGAKYLADIVIGADGVHSIVRSEIWRHLKENSQISVLEAPNASIKHDYSCIYGISLNVPQIILGIQLNCLDDGVSIHLFTGKQSKLFWFVIIKTPQASFAKVEIDNTHTARCICEGLRTKKVSDTLCFEDVWSRCTIFKMTPLEEGVFKHWNYGRLACIGDAIRKMAPNNGQGANMAIEDACSLANILQKKISHGSIRDQDINSMFQEFSMAQRARTESVCAQSEFLVRMHANQGIGRRLLGRYLIPFLYDAPAGLSGFSISGATRIEFIDLPTRSLRGAWGKSWRGSWEFILQSLVYLRPKFRIVYALYLVAAAAFILYCLSSLFP | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts . The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitremB biosynthesis . LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP . GGPP then condenses with indole-3-glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline . Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases . The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmB, to paspaline . The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F . Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F . LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes . The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation . The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation . The multi-functional prenyltransferase ltmE is required for C20- and C21-prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures . The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ . While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway . | Q56RZ6 |
B9L8Z0 | DNAK_NAUPA | Heat shock protein 70 | Nautilia | MGKVIGIDLGTTNSAMAYYDGKDAKIIANKEGRNTTPSVVAFTDKGEVLVGEPAKRQAITNPERTIYSVKRIMGMMCNEPKAQEAKKHVQYKIVDKNGACAVEVDGKVYTPQEISAKILMKLKKDAEEFFGEEVTEAVITVPAYFNDSQRKATQEAGKIAGLNVLRIINEPTAAALAYGLDKKGEEKILVYDLGGGTFDVTVLEIGDGTFQVLATDGNAFLGGDDFDNRIVDWLISEFKAETGIDLSQDKMALQRLKDAAEQAKKELSTKEETEINLPFITADASGPKHLVKKLTRAKFEAMIDDLLQETLRHIDTALEDAGLSKDEIDEIVMVGGSTRIPKVQELVSNYFNGKKLNKSVNPDEVVALGAAIQAGVLKGDVKDVLLLDVTPLSLGIETLGGVMTKIIEKGTTIPVKKSQVFSTAEDNQTAVTIHVLQGEAELAKDNKSLGQFNLEGIPPAPRGVPQIEVTFDIDANGVLNVSAKDKTSGKEQKITITGSSTLSEEEIERMVREAEEANRKEKARIEAIKARNELDAVAYQAEKFINDNKDKLGDVSALEAKIKEAKELIEQQSEDKAKIEALKNEINTELQNVAQNMAQQQQAQGGAQQQNQNKGGDDDVIDAEVE | Acts as a chaperone. | B9L8Z0 |
Q74JU6 | EFTU_LACJO | Elongation factor Tu | Lactobacillus | MAEKEHYERTKPHVNIGTIGHVDHGKTTLTAAITTVLAEDGLAQAEDYSQIDAAPEEKERGITINTAHVEYETKNRHYAHMDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVQYIVVFLNKVDLVDDPELIDLVEMEVRDLLSEYDYPGDDVPVIRGSALKALEGDPEQQDVIRKLMETVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEIVGLTDKIEKSTVTGLEMFHKTLDLGEAGDNVGVLLRGIDRDQVERGQVLAAPGSIQTHKNFKGQVYILNKDEGGRHTPFFSDYRPQFYFHTTDVTGKIELPEGTEMVMPGDNVEFTVELIKPVAIEKGTKFTIREGGKTVGAGQVTEILD | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q74JU6 |
B3H2C0 | UBID_ACTP7 | Polyprenyl p-hydroxybenzoate decarboxylase | Actinobacillus | MKYKDLREFLTLLEGQGELVRIKQEIDPYLEMAEISDRTLRKGGPAILFENPKGYRMPVLCNLFGTPKRVALGMGQEDTHALRELGKLLAFLKEPEPPKGFKELIGQLPQWKQVLNMPSKVLGKADCQQVVLSGDEVDLHKLPIMHCHQGDVAPLVTWGLTITQGPYKKRQNLGIYRQQLIGKNKLIMRWLSHRGGALDFHEWKEANPDKPFPVSVAIGADPATILAAVTPIPDTLSEYAFAGLLRGQKTEVTKSISNDLEIPASAEIVLEGYIDPNETALEGPYGDHTGYYNEQEYFPVFTVTHITMRRDAIYHSTYTGRPPDEPAVLGEALNEVFIPILQKQFPEIVDFYLPPEGCSYRLAVVTIKKQYAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWKDVIWAITTRCDPSRDTTLIDHTPIDYLDFASPIAGLGSKMGIDATNKWPGETSREWGTPIKKDPNVVKLVDEIWDQLGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | B3H2C0 |
Q2NJ19 | EFG_AYWBP | Elongation factor G | Candidatus Phytoplasma asteris | MARQFSLEKTRNIGIIAHIDAGKTTTTERILFHTGKIHKIGETHDGASQMDWMEQEQERGITITSAATTAFWKNHRINIIDTPGHVDFTVEVSRSLRVLDGAVTVIDAQAGVEPQTETVWRQASEYKVPRVIFVNKMDKVGADFAYAIETLKQRLGVHASAIQWPIGSENDFNGIIDLVEMNAFEYDNTSQETGKVVSIPSDLESITQTKRKELIETLSTLDEELMIYYLEEKPISSEMLKNSIRKATLQASFFPVLCGSSFKNKGVVKMLDAVVDYLPAPCDVAAIVGFDSDNQEIVRTGLDEEPFTALAFKVMTDPYVGKLTFFRIYSGSVKAGSYVTNTTKGTKERFGRLLQMHANSREEVKEAYTGDILAVVGLKATTTGDTLASEGQTIILESMNFPEPVIEIAVEPKTKADQDKMGIALAKLAEEDPTFKVFSNHETGQTIIAGMGELHLDIIIERLKREFKVQANVTEPQVAYRETITQETETEGKFIRQSGGRGQYGHVWMRFEPNPGKGFEFVNKIVGGVVPREYVPAVQKGIQEALAGGILAGYQIIDVKATLFDGSYHDVDSSEIAFKIAASMALKETKTKGNPVILEPIMDVEVVTPNDYVGNVIGDLTSRRGRLENQESRTNAVAIRAFVPLSEMFGYATVLRSNTQGRATFIMQFAKYEKAPKSITEEIIKKRA | 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. | Q2NJ19 |
B3Q9W8 | GATC_RHOPT | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Rhodopseudomonas | MSVDAATVRRIAHLARIAVTEDEVPHLQGELNAMLAFVEQLSEVDVDGVEPMTSVTPMQMKKRADVVNDGEIADQVVANAPSTEDHFFLVPKVVE | 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). | B3Q9W8 |
A8G7H8 | RL9_PROM2 | 50S ribosomal protein L9 | Prochlorococcus | MAKRVQLALTESIASLGKEGDLVEVAPGYARNFLLPYGKAMNVTPAVLKQIERKKEKEKIAADKLKQEALDFQTALSTIGRFTIKKQVGEDGVLFGTVTNGDVAEAIEEATKKEIDRRNITVPDIHNLGSFTAKIKLHPEVNAEVNIEVTS | Binds to the 23S rRNA. | A8G7H8 |
Q9PH24 | LEXA_XYLFA | LexA repressor | Xylella | MSLSDIQQAILSLITNHINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRVPRQARGIRLKHLTEVDETALALQSEDVLRLPVLGRVAAGQPIGADIGEGRVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTQDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR | 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. | Q9PH24 |
A0A193H329 | CZS8_CRUCA | Cruzioseptin-8 | Cruziohyla | MAFLKKCLFLVLFLGLVSLSICEEEKREEENEEVQEDDDQSEEKRGFLDVIKHVGKAAGKAALNAVTEMVNQGEQ | Has antimicrobial activity. | A0A193H329 |
P62150 | CALM_ORYLA | Calmodulin-A | Oryzias | EQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFV | Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. | P62150 |
B7V0S0 | TRPA_PSEA8 | Tryptophan synthase alpha chain | Pseudomonas | MSRLQTRFAQLKQENRAALVTFVTAGDPDYASSLEILKGLPAAGADVIELGMPFTDPMADGPAIQLANIRALDGGQTLARTLQMVREFRSGESETPLVLMGYFNPIHHYGVERFIAEAKEVGVDGLIVVDLPPEHNEDLCHPAQAAGLDFIRLTTPTTGDQRLPTVLEGSSGFVYYVSVAGVTGANAATLEHVEEAVARLRRHTDLPIGIGFGIRSAEHAAAVARLADGVVVGSALIDRIAKARDNAQAVKDVLALCGELAEGVRNAR | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B7V0S0 |
A8LC57 | RS10_FRASN | 30S ribosomal protein S10 | unclassified Frankia | MAAQKIRIRLKAYDHEVIDSSARKIVETVTRTGAQVAGPVPLPTEKNVYCVIRSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDSLMRLDLPAGVDIEIKL | Involved in the binding of tRNA to the ribosomes. | A8LC57 |
Q8PYQ9 | PURA_METMA | IMP--aspartate ligase | Methanosarcina | MFTIITGAQFGDEGKGKIVDLLAKDYDVVARFQGGNNAGHTVKVGDEVYKLHLIPSGILLDARVLIGPGVVLNPEVLAEEIEMFEKHGVKVNSEKLGVDAKTSIIMPYHIELDGLREASRETKIGTTKRGIGYAYIDKVARDEIRMAELVDKERFLARLEELAPQKEKEIEAMGGDPRIVRDPELIKRYLELGEQFAAYITDVSREINQALDEGKNVMAEAAQGTHLDVIHGTQKFVTSSSTIAGSACANLGVGPTRVDNVIAIVKAYITRVGEGPLPTELIGELGERIQKAGGEFGTTTGRGRRCGWFDLPLLKKAIALNGYTEISLTKLDVLTGLDPLRSAQVMSIKGKNWTILRNLRKTSRHAALCMKTCQDGKKN | 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. | Q8PYQ9 |
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