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 |
|---|---|---|---|---|---|---|
D2KQB0 | HHEX_PATMI | HEX homeodomain transcription factor | Patiria | MSTLQYPGPPPPSSMNLHNPHMNHHHGLVGPGLAPLSAPNGIQSLNTLHNGSGPPSHTPFYIDNILGSRLNMTGPARPTPTLPSPTFPAHMNSAYNSYYEQAVHPGLAAPTPISYGSGAFSSPPPYPFARGDYPHGLIDRHDPYSKVPGKPFLWNPFIQRPLHKRKGGQVRFSNDQTMELEKKFESQKYLSPPERKKLAKLLQLSERQVKTWFQNRRAKWRRVKQEVPTGKGEGDENSHEKPRDLDRDDFSREQVLSNGAACAFTHGGGSEADSLEEKEA | Transcription factor that may play a central role in activating or maintaining gene expression in the vegetal pole. Part of a gene regulatory circuit with Erg and Tgif that operates early in mesoderm development. | D2KQB0 |
Q6B8V8 | RK22_GRATL | 50S ribosomal protein L22, chloroplastic | Agarophyton tenuistipitatum | MTNKTTNIQATGKYVRLSTAKTRRVLNQIKGKKYQEAILILEFMTYKPCKIIKKILESAGNNALNLKYEKQNLIIKQAFANDGPKLKRFQPRAQGRAFRIQKPTCHITINLSIN | 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. | Q6B8V8 |
A8LX76 | SEPF_SALAI | Cell division protein SepF | Salinispora | MGALRKAGVWLGLVEEDDERAYDDAGYDKGGYRESRYRSSRYSEDFGDEDDEDEEAAVPRSRRGDRSRLERAAARSGDVDHNVEGEQPERVERASVRSITRSAEPSESLTYHTRDNLALAPQPVRERVPADEEQRYQITTLHPTTYREARTIGEHFRDGVPVIINLTEMDEADARRLVDFAAGLAFGLRGTIERVTNRVFLLSPANVQVTAEDKAKIAEGGFFSLS | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. | A8LX76 |
Q3ZBV3 | MGN_BOVIN | Protein mago nashi homolog | Bos | MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI | Required for pre-mRNA splicing as component of the spliceosome. Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. | Q3ZBV3 |
A7I4V4 | DPCKG_METB6 | Dephospho-coenzyme A kinase | Methanoregula | MFVLPDESRQLFKDPFGTLHRDIGTVLPELAGRTIYSVGDVVTHSLQQNGITPAIAVVDGQTMRSPCIKMPEIAGPCIHVKNPPGTITDELVSALTHAVDHTPVTILVDGEEDLAVIPLVIAAPLSSIVIYGQPNEGVVLRIVDDQAKTAARRLLTQFTKTESPIPHN | Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). | A7I4V4 |
Q0BCH2 | KDSB1_BURCM | CMP-2-keto-3-deoxyoctulosonic acid synthase 1 | Burkholderia cepacia complex | MTHPQPFIAVIPARLASTRLPNKPLADLGGKPMVVRVAERAREAGAQQVLIASDAQSVLDAARDHGFEAVLTRADHPSGTDRLAEVAATFGWSDDTVVVNVQGDEPLIDPVLVRDVASHLAAHPDCAIATAAHPIHDAADVFNPNVVKVALDARNVAMYFSRAPIPWSRDAYLPHWPDVSAMPAPAFPVHRHIGLYAYRARFLRTYPSLAQAPVEQAEQLEQLRAMWHGERIAVLITEHAPEAGIDTPADLARVQALFRPGSK | Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | Q0BCH2 |
A3PHR7 | RSMH_CERS1 | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Cereibacter | MAEADTERRPHIPVLLRPLLAAVAPVEGTWLDGTFGAGGYARGLLEAGADRVIGVDRDPLALKMASGWAGDYGDRLRLVAGTFSQLDSHAGAPLDGVVLDLGVSSMQLDLAERGFSFQKDGPLDMRMSQEGESAADLVNTASEESLADILYHYGEERASRRIARAIVEARAAAPITRTLALAEIVARCLPRPKPGQMHPATRSFQAIRIAVNAEFSELVEGLEAAERALRPGGRLAVVTFHSLEDRIVKRFLQLRSGGEGQGNRYAPETRAYAPRFTLPLRRAISPDEAELAENPRARSARLRVGVRTDAPAGKVDPQALGTPLIPKKGRR | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | A3PHR7 |
A6UW70 | GGGPS_META3 | Phosphoglycerol geranylgeranyltransferase | Methanococcus | MFGKVEEKLNNVLKTEGALYFILIDPDEKNCLEIAEKVKDYADAIILGGSIGITNLDETTKQIKEIIGDIPIILFPGNVDGLTPYADAVFFMSFMNSNNTYWTTTAPTLGAITVKKYNLEPISMAYLGIEPIKRTAVGFVGEVNEIPQRKPEIAGMYCLSAKYFGMRWAYLEAGSGAELPVSNEIIGISKKLSGINIIVGGGIRTPETAYQKVLSGADAIVTGTLIEDNPDAVKEMRNAIKKAGIDKL | Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | A6UW70 |
C4L0W8 | AZOR_EXISA | FMN-dependent NADH-azoreductase | unclassified Exiguobacterium | MTKVLYVSANPKPTELSYSKQVAETFVSTLKAENASIEVEAIELYDVDVQEIDGDVLSAWGKFASGEALTDVEAKKVGTMSGMLEKFMEADLYVFATPMWNFFFPARMKMFLDSVLMAGKTFRYTEQGPVGLLENKQAIHIQGTGGIYTGTDLNFADAYLRQALAFVGVSEVTTVAVEGMNQYPDKIEEIVADAKAKAEALAKEVAGAVTV | Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. | C4L0W8 |
A7MAQ2 | DIOA3_DIOJA | Tuber storage protein dioA3 | Dioscorea | MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI | Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities . Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2) . Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages . | A7MAQ2 |
P13854 | MGF_CHICK | Myelomonocytic growth factor | Gallus | MCCLTPVLALALVLGAPWQALHGAPLAELSGDHDFQLFLHKNLEFTRKIRGDVAALQRAVCDTFQLCTEEELQLVQPDPHLVQAPLDQCHKRGFQAEVCFTQIRAGLHAYHDSLGAVLRLLPNHTTLVETLQLDAANLSSNIQQQMEDLGLDTVTLPAEQRSPPPTFSGPFQQQVGGFFILANFQRFLETAYRALRHLARL | Hematopoietic growth factor that stimulates the proliferation and colony formation of normal and transformed avian cells of the myeloid lineage. | P13854 |
P83264 | PRT1_SCOSC | Scombrine alpha-1 | Scomber | MPRRRRRASRPVRRRRRARRSTAVRRRRRVVRRRR | Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. | P83264 |
Q9BT25 | HAUS8_HUMAN | Sarcoma antigen NY-SAR-48 | Homo | MADSSGRGAGKPATGPTNSSSAKKKDKRVQGGRVIESRYLQYEKKTTQKAPAGDGSQTRGKMSEGGRKSSLLQKSKADSSGVGKGDLQSTLLEGHGTAPPDLDLSAINDKSIVKKTPQLAKTISKKPESTSFSAPRKKSPDLSEAMEMMESQTLLLTLLSVKMENNLAEFERRAEKNLLIMCKEKEKLQKKAHELKRRLLLSQRKRELADVLDAQIEMLSPFEAVATRFKEQYRTFATALDTTRHELPVRSIHLEGDGQQLLDALQHELVTTQRLLGELDVGDSEENVQVLDLLSELKDVTAKKDLELRRSFAQVLELSAEASKEAALANQEVWEETQGMAPPSRWYFNQDSACRESGGAPKNTPLSEDDNPGASSAPAQATFISPSEDFSSSSQAEVPPSLSRSGRDLS | Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. | Q9BT25 |
Q4KL97 | ANKR1_XENLA | Ankyrin repeat domain-containing protein 1 | Xenopus | MLLKMEEMVIEKKNEMKQTGDFVSGVSKNGEYETAVALEKQEDLKTTSKSLIELEEEKQSKEKQLKSELLKKKLEERPKLDNLEDLQTIINLKKRKRVKKVKVPVVKEPEPEETIGDVDQMTFFKAALDNKMSIIEKYLADGGDPNTCDEYKRTALHRACSEGHTAIVEKLIEAGANIEFKDMLESTALHWTCRGGSVETLKLLLNKGAAINARDKLLSTPLHVAVRTGYYECGEHLIACEADLNAKDREGDTPMHDGVRLNRYKMIRLLILYGVNLNIKNCAGKTPMELVMQWQNGAKEIFNGLQNKSYKNSHISKF | May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes. | Q4KL97 |
A1BJ37 | EFG_CHLPD | Elongation factor G | Chlorobium | MARLVALDKVRNIGIMAHIDAGKTTTTERILYYTGRLHRMGEVHEGGATMDWMEQEKERGITITSAATTCFWSPNYGNYSGLRHRINIIDTPGHVDFTVEVERSLRVLDGAVALFCAVGGVEPQSETVWRQANKYGVPRIAYVNKMDRTGANFFDTVKAIRERLSANPVPIQIPIGEGEIFAGFVDLIRMKGVIYDKDDGSTYNEVEIPHDLQNEARTWRINMLEAVSEVDETLLEKYLNGEDITEEEIRVVLRKATLNVSIIPVLCGSSFKNKGVQFMLDAVVEYLASPVDVGAVEGHHPRTEETVVREPRDEEPFAGLAFKIATDPFVGKLTFFRVYSGVLHAGSYVLNTVTGKKERIGRVLQMHSNKREDIECVYAGDIAAAVGLKDVRTGDTICDENNPVVLEKMIFPEPVIQIAIEPKTKADSDRLGMSLAKLAEEDPTFKVKTDDETGQTLIAGMGELHLEILVDRLKREFKVEATVGQPQVAYRETIRKAVEFEGKFVRQSGGKGQFGLVNLKVEPLEEGKGYEFVDAVKGGVIPREYIPAVNAGVQQAMKDGVVAGYAMQDIKVTLFDGKYHEVDSSEMAFKIAGSIGFKGAAKKADPVLLEPIMKVEVVTPDEYLGDVMGDLSSRRGHIEGMGQRAGAQFVNAKVPLSAMFGYSTDLRSMTQGRANYSMEFECYREVPRSIAESLQEKRVSKETV | 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. | A1BJ37 |
A6NMB1 | SIG16_HUMAN | Siglec-P16 | Homo | MLLLPLLLPVLGAGSLNKDPSYSLQVQRQVPVPEGLCVIVSCNLSYPRDGWDESTAAYGYWFKGRTSPKTGAPVATNNQSREVAMSTRDRFQLTGDPGKGSCSLVIRDAQREDEAWYFFRVERGSRVRHSFLSNAFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFKKCPAPSFSWTGAALSPRRTRPSTSHFSVLSFTPSPQDHDTDLTCHVDFSRKGVSAQRTVRLRVASLELQGNVIYLEVQKGQFLRLLCAADSQPPATLSWVLQDRVLSSSHPWGPRTLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLRNGTSLRVLEGQSLRLVCVTHSSPPARLSWTWGEQTVGPSQPSDPGVLQLPRVQMEHEGEFTCHARHPLGSQRVSLSFSVHCKSGPMTGVVLVAVGEVAMKILLLCLCLILLRVRSCRRKAARAALGMEAADAVTD | Putative adhesion molecule that mediates sialic-acid dependent binding to cells. | A6NMB1 |
A1DNL0 | CBHB_NEOFI | Exoglucanase B | Aspergillus subgen. Fumigati | MLASTFSYRMYKTALILAALLGSGQAQQVGTSQAEVHPSMTWQSCTAGGSCTTNNGKVVIDANWRWVHKVGDYTNCYTGNTWDKTLCPDDATCASNCALEGANYQSTYGATTSGDSLRLNFVTTSQQKNIGSRLYMMKDDTTYEMFKLLNQEFTFDVDVSNLPCGLNGALYFVAMDADGGMSKYPTNKAGAKYGTGYCDSQCPRDLKFINGQANVEGWQPSSNDANAGTGNHGSCCAEMDIWEANSISTAFTPHPCDTPGQVMCTGDACGGTYSSDRYGGTCDPDGCDFNSFRQGNKTFYGPGMTVDTKSKFTVVTQFITDDGTASGTLKEIKRFYVQNGKVIPNSESTWSGVGGNSITNDYCTAQKSLFKDQNVFAKHGGMEGMGAALAQGMVLVMSLWDDHAANMLWLDSNYPTTASSSTPGVARGTCDISSGVPADVEANHPDASVVYSNIKVGPIGSTFNSGGSNPGGGTTTTAKPTTTTTTAGSPGGTGVAQHYGQCGGNGWQGPTTCASPYTCQKLNDFYSQCL | The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. | A1DNL0 |
Q15QB4 | LPTD_PSEA6 | LPS-assembly protein LptD | Pseudoalteromonas | MKPLKLELNPRDFNHYQAAFLPYRMKIKQPLHVLCFSVCSLSAVAQETCPAPANTFVVEKRLPNGQIQVISNMTSIQQDNFAEFEGDVEITNKDSQIIANKAQIDRTTQQLIATGDVSYQNPQLSVTSQKVLLNTQNNRMEIADTQYELTTLNARGQAELLVVDQTQGLELNGVTFSTCPTGQEDWLVHADSITVKPDETRGVARNAFFYVQDIPIFYLPYYSFPVTDARETGLLFPQVGSSSSTGFAYEQPYYLNLDPQYDATITPRYMTKRGLQLKTEFRYLTENNSGQIDIEYLPNDSDSTTNEDRYFYRFTHKGALSDDWEVNVDFNGLSDDNYIVDLGSDYYNSADTHLFRTLGLHYYSDALNVSLQLRDFEILGDHDDTYRALPELKLDYVTDLPAGFKFDIHSELARFDNANGTSPKATRAHIAPTLSLPLENSWGEFLAETSIMHTVYRQEDIEGTDLSRDVSRTLGQAKLYGALVFERQAHWFGDNVTQTLEPRAQYLYTSYEDQSDIGLYDTTRLFNDFAGLFRGQEFTGLDRISDKNQVTLGVTSRIIDEDNREQFKLSLGQIFYLEDNKVTAASKEDDRSALAAELDWRIGSKWLAHSEVQVSTQTDKVERSSVGLEYRLARDKMLQINHRFVRDLSGEQISQLGLTASWPIAQDWYWVGRWYRDIDRHRTIESYTGLQYESCCWALRIVAQRQLTSRFDDDGLQSTDEFDSGIAIQFLFKGIGGDSSGRDMLRDGLFGYRQPYLLD | Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. | Q15QB4 |
C4QYF2 | LIPA_KOMPG | Lipoic acid synthase | Komagataella | MLSTRVVRLPKVISGGNKQLARGLASLSDEKSLNEANPTDLAGLKRKAKRRPTKLADELKTGPSFADFVTGKAKDMLVDPLELARNDPNARLPSWLKTQIPKGKSFHHLKSDLKELKLSTVCEEAKCPNIGECWGGKKSEATATIMLMGDTCTRGCRFCSVKTNRNPAPPDPNEPENTAEAISRWGLGYVVLTTVDRDDLPDGGAHHLASTVTKIKEKAPQILVECLSGDFRGNLEMAKVLASSPLDVFAHNLETVEDLTPHIRDRRATYRQSLSVLRAAKEANPRLVTKTSLMLGFGETDDQILQTLHDLRNISCDVVTFGQYMRPTKRHMKVVEYVTPSKFEYWRDKALEMGFLYCASGPLVRSSYKAGEAFIENVIKKRRTNVGAIEEQQHDKENNNLLLSKEDEKTTQEKANF | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | C4QYF2 |
Q0VP64 | RSMC_ALCBS | rRNA (guanine-N(2)-)-methyltransferase RsmC | Alcanivorax | MENTTQLLLRQSDALAGRNVLVVDANDPALKTLSVDATVHVHADDYTIGAQQWAPAPTVPAGTDLLVLPLSKSLDRLRFLLNWLAGEIAEPTELWLIGPTKGGIRGALKYLEAHVDGTMLEDSARHCKLYSGLLQPGEKQSLNAWGTVLEVADQEAVSYPGVFSHGRLDEGSALLLQAMEGHNLGKPGKVIDMGCGAGVISVWLARHGWQVQGVDVSASAVTASTESLARNGLQGRIMGGDLFSPIQGRVDMVVTNPPFHDRRQRTTDITRRLIAEAPTYLKPGGVLWLVANRELPYVQWLDDAFSHVQVASETTRFRVYRAVLS | Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. | Q0VP64 |
B0RZS5 | RL18_FINM2 | 50S ribosomal protein L18 | Finegoldia | MFKKIDKNANRVKRHLRIRKNLTGTSEKPRLCVFKSNTNIYAQLIDDVNHNTLVAASTLDKDFSGESKSNKEAAKLVGELIGKKAIDKGIEQCVFDRSGYLYHGKVKELAEGARSAGLKF | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | B0RZS5 |
Q43147 | C85A1_SOLLC | Protein DWARF | Solanum subgen. Lycopersicon | MAFFLIFLSSFFGLCIFCTALLRWNQVKYNQKNLPPGTMGWPLFGETTEFLKLGPSFMKNQRARYGSFFKSHILGCPTIVSMDSELNRYILVNEAKGLVPGYPQSMIDILGKCNIAAVNGSAHKYMRGALLSLISPTMIRDQLLPKIDEFMRSHLTNWDNKVIDIQEKTNKMAFLSSLKQIAGIESTSLAQEFMSEFFNLVLGTLSLPINLPNTNYHRGFQARKIIVNLLRTLIEERRASKEIQHDMLGYLMNEEATRFKLTDDEMIDLIITILYSGYETVSTTSMMAVKYLHDHPKVLEELRKEHMAIREKKKPEDPIDYNDYRSMRFTRAVILETSRLATIVNGVLRKTTQDMEINGYIIPKGWRIYVYTRELNYDPRLYPDPYSFNPWRWMDKSLEHQNSFLVFGGGTRQCPGKELGVAEISTFLHYFVTKYRWEEIGGDKLMKFPRVEAPNGLRIRVSAH | Catalyzes the C6-oxidation step in brassinosteroids biosynthesis . Converts 6-deoxocastasterone (6-deoxoCS) to castasterone (CS) . May also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3-dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY), but not castasterone (CS) to brassinolide (BL) . | Q43147 |
A5GI06 | IF3_SYNPW | Translation initiation factor IF-3 | unclassified Synechococcus | MPPRPRFDRRAPVRELPNINERINYPQLRVVDADGTQLGVIDREKALEVAQERELDLVLVSEKADPPVCRIMDYGKYKFEQEKKAKEAKKKSHQTEVKEVKMRYKIDQHDYDVRIGQAQRFLKAGDKVKCTVIFRGREIQHTALAETLLRRMAKDLEEPAEIQQPPKREGRNMIMFLTPRKTPLVKKDDKEEPATRAVRTITAPPRPTSARLASKPAGNG | IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. | A5GI06 |
B6HTQ4 | MAP22_PENRW | Peptidase M | Penicillium chrysogenum species complex | MAAQTTEKLDQLDLNVQAAPTADQVPAEAEEDSDDAQDEGAAEAGAAGAGSTLADKKKKKKKPKKKSKKKGGAKVQSEPPRVPVSNLFPNGQYPEGEIVEYLNDNAYRTTNEEKRYLDRMNNDFLQEYRQGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDSVRALTGHSGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLNEGDVMKVDFGAHLNGRIVDSAFTMTFDPVYDPLLAAVKDATNTGIREAGIDVRMSDIGAAIQEAMESYEVEINGTMHPVKCIRNLNGHNIDQHVIHGGKSVPIVKSTDQTKMEEGEVFAIETFGSTGKGYVREEMETSHYALAADAPNVPLRLSSAKNLLNLINKNFGTLPFCRRYIDRLGQDKYLLGLNNLVSSGIVQDYPPLCDIKGSYTAQYEHVCFYFGVFSTLIVY | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | B6HTQ4 |
Q97TX8 | DPHB_SACS2 | Diphthamide biosynthesis methyltransferase | Saccharolobus | MSILSLVGLGISKKFITDSAIETLSNSDIIIFDRYTSRSCDINVDVLRRLVKGEREFIEADRSLLENNSKAIIDYLDKGYNVSIASIGDALIATTHVSLLIEAKHRGHEVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKNEKAMTANEALQILLRLEERHKKSVLSKSDIIIVGARLGCDDERIIALKVEEATSFDFGNTPHIIIIPGNLHYMEADAIKWILRS | S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. | Q97TX8 |
Q4A6S7 | KGUA_MYCS5 | GMP kinase | Mycoplasmopsis | MNKKKKSIVIFTGPSGVGKGTVEQLVFNYDELNLSLSCSATTRSPRGGETNGIHYYFISKEEFKDRIKNKKFLEHSFHFDNYYGTLYSELDNIIARNKVPFLEIETNGAKIIAQKMQKLKNPPYNLITIFLSPPSITDIYKRIKNRGTENAQTIKNRVNKAKEELLEAGNFKYVVYNDRPERAAQEIREILHKELDID | Essential for recycling GMP and indirectly, cGMP. | Q4A6S7 |
A8EXA9 | RL9_RICCK | 50S ribosomal protein L9 | belli group | MEIILIKPVRKLGKIGDILKVADGFGRNYLLPQKLAIRATEPNKELIVKQKHEFEAKDKQIREEVEKINALIKEQKLVFIRQTSDDGKLFGSITNKEIADKLSENVSYNIFHSNIILDKKIKSTGIYTVEIRLHAELNAIVTVIVARSESEVQDYLREQKNESLETLAESA | Binds to the 23S rRNA. | A8EXA9 |
Q1J7I7 | EZRA_STRPF | Septation ring formation regulator EzrA | Streptococcus | MSSGIILLIVAIVLLVIIAYLVGVIIRKRNDSLITSLEERKQALFALPVNDEIEEVKSLHLIGQSQTSFREWNQKWVDLTVNSFADIENHIFEAENLNDTFNFIRAKHEINSVESQLNLVEEDIASIREALNILKEQEEKNSARVTHALDLYEKLQASISENEDNFGSTMPEIDKQMKNIETEFSQFVALNSSGDPVEASEVLDRAEEHTIALGQITEQIPAIVAKLEDDFPDQLDDLETGYRRLLEENYHFPEKNIEARFQEIRESIRANSSELVTLDLDRAREENTHIQERIDSLYEVFEREIAAYKVAAKNSKMLPRYLAHVKHNNEQLKDEIARLSRKYILSETESLTVKAFEKDIKEIEDSTLAVAEQFGLQEKPFSELQVTFERSIKTLTNVESGQMDVFAAVKDIEKIESQARHNLDVYVTQLHMIKRYMEKRHLPGIPQDFLSAFFTTSSQLEALMDELSRGRINIEAVSRLSEVATVAIANLEDLTYQVVQNATLTEQLLQYSNRYRSFEAGVQSSFEHALRLFEVENDYQASFDEISYALETVEPGVTDRFVNSYEKTREHIRF | Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. | Q1J7I7 |
B7L504 | MHPB_ECO55 | 3-carboxyethylcatechol 2,3-dioxygenase | Escherichia | MHAYLHCLSHSPLVGYVDPAQEVLDEVNGVIASARERIAAFSPELVVLFAPDHYNGFFYDVMPPFCLGVGATAIGDFGSAAGELPVPVELAEACAHAVMKSGIDLAVSYCMQVDHGFAQPLEFLLGGLYKVPVLPVFINGVATPLPGFQRTRMLGEAIGRFTSTLNKRVLFLGSGGLSHQPPVPELAKADAHMRDRLLGSGKDLPASERELRQQRVISAAEKFVEDQRTLHPLNPIWDNQFMTLLEQGRIQELDAVSNEELSAIAGKSTHEIKTWVAAFAAISTFGNWRSEGRYYRPIPEWIAGFGSLSARTEN | Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. | B7L504 |
Q67SL8 | SSRP_SYMTH | Small protein B | Symbiobacterium | MARAKAEIQPVAENRKARHDYFVEETYEAGIVLVGSEVKSCRAGRVNLRDAYAQIKDGEIFLLNCHISPFEQANRFNHEPLRPRKLLMHKSEIHRLYGKVREKGFTLVPLRLYFNQKGKVKVELALAKGKRAYDKRDDIAAREAKREMARALRGRYDD | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. | Q67SL8 |
P01968 | HBA2_BOSMU | Hemoglobin alpha-2 chain | Bos | VLSAADKGNVKAAWGKVGGHAAEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGAKVAAALTKAVGHLDDLPGALSELSDLHAHKLRVDPVNFKLLSHSLLVTLASHLPSDFTPAVHASLDKFLANVSTVLTSKYR | Involved in oxygen transport from the lung to the various peripheral tissues. | P01968 |
Q82F60 | SYM_STRAW | Methionyl-tRNA synthetase | Streptomyces | MARHLITSALPYINGIKHLGNMVGSMLPADVYSRYLRQRGHDVLYICATDEHGTPAELAAKERGLPVDEFCAQAHDAQKAVYDGFELAFDYFGRSSSEQNREITQHFARRLNENGFIEERAIRQVYSPADGRFLPDRYVEGTCPHCGYDKARGDQCENCTRVLDPTDLINPRSAISGSTDLEVRETKHLFLLQSKLQHEVEEWVARHEEEWPQLASSIARKWLNEGLHDRAITRDLDWGVPVPADTWPELAAEGKVFYVWFDAPIEYIGATKEWSDLDPENRDWKSWWYDADSGENPVRYTEFMAKDNVPFHTVMFPATELGVREPWKKVDYVKAFNWLTYYGGKFSTSQKRGVFTDHALEILPADYWRYFLIANAPESDDSSFTWEHFTATVNKDLADTLGNFVNRVLSFSKKRFGEEVPAGAPAGESETKLGEEIAALLAEYESHMETLQFRKAAAALRALWSAGNSYLEEKAPWLEIKTNPEGAALTLRTAMNLIHLYSVVSEPFIPASSKAMRSAFALSEDTATWVTQDEAKSLDSVPAGTPFTVPPVLFAKITDEDLESYKERFGGAPE | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | Q82F60 |
Q8NG76 | O2T33_HUMAN | Olfactory receptor OR1-56 | Homo | MEMRNTTPDFILLGLFNHTRAHQVLFMMVLSIVLTSLFGNSLMILLIHWDHRLHTPMYFLLSQLSLMDMMLVSTTVPKMAADYLTGSKAISRAGCGVQIFFLPTLGGGECFLLAAMAYDRYAAVCHPLRYPTLMSWQLCLRMTMSCWLLGAADGLLQAVVTLSFPYCGAHEIDHFFCETPVLVRLACADTSVFENAMYICCVLMLLVPFSLILSSYGLILAAVLHMRSTEARKKAFATCSSHVAVVGLFYGAAIFTYMRPKSHRSTNHDKVVSAFYTMFTPLLNPLIYSVKNSEVKGALKRWLGTCVNIKHQQNEAHRSR | Odorant receptor. | Q8NG76 |
Q2I3G8 | COX3_ELEMA | Cytochrome c oxidase polypeptide III | Elephas | MTHQMHAYHMVDPSPWPLTGALSALLMTSGLTMWFHYHSVILLLLGLTTNILTMFQWWRDVVREGTFQGHHTPIVQESLRYGMILFITSEVLFFTGFFWAFYHSSLAPTPELGSYWPPVGVYPLNPLEVPLLNTSVLLASGVTITWAHHSLMEGSRKNMLQALLITILLGVYFTLLQMFEYYEASFTISDGIYGSTFFVTTGFHGLHVIIGSTFLLICFIRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWGS | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | Q2I3G8 |
Q329V7 | GPPA_SHIDS | pppGpp-5'-phosphohydrolase | Shigella | MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPIADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQYMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQAQRVAKVAANFFDQVENEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVHWPLEVH | Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. | Q329V7 |
P57110 | ATS8_MOUSE | METH-2 | Mus | MLRDPTTTGWPPLLLLLLQLPPPPLVCGAPAGPGTGAQASELVVPTRLPGSASELAFHLSAFGQGFVLRLAPDASFLAPEFKIERLGGSSAAAGGEPGLRGCFFSGTVNGERESLAAMSCVAGWSGSFLLAGEEFTIQPQGAGDSLDQPHRLQRWGPGQRREDPGLAAAEVFPLPQGLEWEVEMGNGQGQERSDNEEDRKQDKEGLLKETEDSRKVPPPFGSKTRSKRFVSEARFVETLLVADASMAAFYGTDLQNHILTVMSMAARIYKHPSIRNSVNLVVVKVLIVEKERWGPEVSDNGGLTLRNFCSWQRRFNKPSDRHPEHYDTAILFTRQNFCGKGEQCDTLGMADVGTICDPDKSCSVIKDEGLQAAYTLAHELGHVLSMPHDDSKPCVRLFGPMGKYHMMAPFFIHVNKTLPWSPCSAVYLTELLDDGHGDCLLDAPTSVLPLPTGLPGHSTLYELDQQCKQIFGPDFRHCPNTSVEDICVQLCARHRDSDEPICHTKNGSLLWADGTPCGPGHLCLDGSCVLKEDVENPKAVVDGDWGPWRPWGQCSRTCGGGIQFSNRECDNPMPQNGGRFCLGERVKYQSCNTEECPPNGKSFREQQCEKYNAYNHTDLDGNFLQWVPKYSGVSPRDRCKLFCRARGRSEFKVFEAKVIDGTLCGPDTLSICVRGQCVKAGCDHVVNSPKKLDKCGVCGGKGTACRKISGSFTPFSYGYNDIVTIPAGATNIDVKQRSHPGVRNDGSYLALKTANGQYLLNGNLAISAIEQDILVKGTILKYSGSMATLERLQSFQALPEPLTVQLLTVSGEVFPPKVRYTFFVPNDMDFSVQNSKERATTNIIQSLPSAEWVLGDWSECPSTCRGSWQRRTVECRDPSGQASDTCDEALKPEDAKPCGSQPCPL | Has anti-angiogenic properties. | P57110 |
A6H7F2 | GPN2_BOVIN | ATP-binding domain 1 family member B | Bos | MAGAAPTTAFGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALQLGPNGGLLYCMEYLEANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMTQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPHVNLLSKMDLIEHYGKLAFNLDYYTEVLDLSYLLDHLASDPFFRHYRQLNEKLVQLIEDYSLVSFIPLNIQDKESIQQVLQAVDKANGYCFGVQEQRSLEAMMSAAMGADFHFSSTLGLQEKYLAPSEQSVEQEAMQL | Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. | A6H7F2 |
P70773 | ARGP_AERSA | HTH-type transcriptional regulator ArgP | Aeromonas | MKALDYKLLLALDAVMQEQNFERAAQRLHITQSAISQRIKQLEQQFAEPLLIRSQPLQATPLGQKLLAHYRQVRQLELELAGEIAPDEPQAPIRVSIAVNADSLATWFLPALAPLLEQHPIELNLLVDDECRTLDRVREGQAFGAVSLHGQPLAGCCVDELGEMRYLLTASPAFVARHFPAGLTPAALAKTPAVAFDQRDDMHVSFMARHFGLEPGGYPCHTVRSSEAFVAMAEQGLAYCLIPELQIRQQLAQGILLDLSPSHHLIEPLYWHRWVLERGLHKQISQRLISEGRRALQPG | Controls the transcription of genes involved in arginine and lysine metabolism. | P70773 |
Q5E3N1 | FLGI_ALIF1 | Basal body P-ring protein | Aliivibrio | MTNRWSFDVNKNLVTVLFTWLCLSISTAHAARIKDVAEVAGVRSNQLIGYGLVSGLPGTGESTPFTDQSFNAMLQNFGIQLPPGTKPKTKNVAAVMVTATLPPFSKQGQVVDVTVSSVGSAKSLRGGTLLQTFLKGLDGKTYAIAQGNLIVSGFSATGADGSKIVGNNPTVGRISGGAMVEREVPSPFGRGDFITFNLLESDFTTAQRMADAVNNFLGPNMASAVDATSVRVRAPRDISQRVAFLSAVENVDFDPADGSAKIIVNSRTGTIVVGKHVKLKPAAVTHGGMTVAIKENLQVSQPGPFSDGQTVVTPDSDIEVTEEQGKMFKFEPGLTLDDLVRAVNEVGAAPSDLMAILQALKQAGAIEGQLIII | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q5E3N1 |
Q9CJU2 | PSD_PASMU | Phosphatidylserine decarboxylase beta chain | Pasteurella | MNILEKKAQLSYWQRIKIAFQYVMPQLYLTRLAGWFAKQQWGAVTHFVIKLFAKKYHVDMSEAAKPNFSDYASFNEFFIRPLADNARPINQNPTALCLPADGRISQLGHIEQDLLLQAKGHYFSLNDLLAGDEALAHHFKDGEFATTYLSPRDYHRVHMPCDATLCKMIYVPGDLFSVNPFLAEHVPNLFARNERVICVFDTEFGKMVQILVGATITASMSTVWAGVINPPRPEKITTWTYEGASAVKLTKGQEMGAFQLGSTVINLFEKDRVQLASHLQVDSPVRMGEILAHQK | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q9CJU2 |
B1I1K1 | RS14Z_DESAP | 30S ribosomal protein S14 type Z | Candidatus Desulforudis | MAKKSLIEKANRPPAFRVRQYNRCKLCGRPRAYMRKFGVCRICFRSLCYRGQIPGVRKASW | 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. | B1I1K1 |
P86970 | LECG_BOTPA | C-type lectin BpLec | Bothrops | NNCPQDWLPMNGLCYKIFDELKAWKDAEMFCRKYKPGCHLASIHLYGESPEIAEYISDYHKGQSEVWIGLWDEKKDFSWEWTDRSCTDYLSWDKNQPDHYKNKEFCVELVSYTGYRLWNDQVCESKNAFLCQCKF | This lectin displays hemagglutinating activity on dog (128'000 HU/mg) and cat erythrocytes, that is inhibited by beta-galactosides (D-galactose, D-lactose, and N-acetyl-D-galactosamine) and EDTA. In addition, has been shown to hemagglutinate promastigote forms of Leishmania amazonensis. Also inhibits Gram-positive (S.aureus ATCC 25923) (MIC is 31.25 ug/ml) but not Gram-negative (E.coli ATCC 25922) bacteria. Is a calcium-dependent lectin. | P86970 |
Q9Z275 | RLBP1_MOUSE | Cellular retinaldehyde-binding protein | Mus | MSDGVGTFRMVPEEEQELRAQLEQLTTKDHGPVFGPCSQLPRHTLQKAKDELNEKEETREEAVRELQELVQAQAASGEELALAVAERVQARDSAFLLRFIRARKFDVGRAYELLKGYVNFRLQYPELFDSLSMEALRCTIEAGYPGVLSSRDKYGRVVMLFNIENWHCEEVTFDEILQAYCFILEKLLENEETQINGFCIVENFKGFTMQQAAGLRPSDLKKMVDMLQDSFPARFKAIHFIHQPWYFTTTYNVVKPFLKNKLLQRVFVHGDDLDGFFQEIDENILPADFGGTLPKYDGKVVAEQLFGPRAEVENTAL | Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'. | Q9Z275 |
Q2H988 | SET2_CHAGB | SET domain-containing protein 2 | Chaetomium | MSPDDAKSAADGTSVPENGTAPKLSRKPSQKLPRGPPPLFDHLPDATADACDTFQVINDCLYGSKNMGSSDHDALDCDCAEEWHDGQNHACGEDSDCINRATKIECVSGDCNCGEGCENQRFQRKQYANVSVIKTEKKGFGLRTDADLQANDFVFEYVGEVINEPTFRNRTVKYDKEGIKHFYFMSLTKSEFVDATKKGNLGRFCNHSCNPNCYVDKWVVGDKLRMGIFATRAIRAGEELVFNYNVDRYGADPQPCYCGESNCVGFIGGKTQTERATKLPLATIEALGIDDGDSWDTAVAKKPRKKKAHEDDEDYVNSVQPRALDEDGVNKVMATLMQCKEKWIAVKLLSRLQATEDEHLRHRVVRMHGYQILKTTLNTFKDDTNVVLQILDILYQLPRITKNKISDSKVEGAVEPLASAAHEEVALAAKRLLDEWSKLETAYRIPRKKHDHAGPIPGNSFEEERRNKDREEPAKPTDPFANIVIPTGPRSTIPQRNANFFAGQQRPRKPPTNLPAGWFVNTDKTGRYYFYDATGRTQWQRPLTPAIETPKVSAKAQQDQKALQSIIDSLTKEPTPRHSAGHTPQRSTTPATEPKKDKWRSLPLEKQMKIYENTHVVDRFHGKLPKEELKKFAREVNKKLVSSDYKNNRVEDPTSIPPKQAKKVRKYAHDFFDRAVAKYTEHEKKKAHNPSKPTSGVPPGDVASSAATPAKDDVTMSDVEADTSPGSSAGRKRKRDGDDEHDDPAESPGAPPSETPSVKRIKEDDAEGEGEPTTIPPPPTPPPPPADTPPTEEDRSMREQEEALMRENEEAQRLEDEAQAEEGGKGSHEWNGRYHRTCAAGERAVEWRVGNGWCYGDDGHGRAAATTAAAAATAAAGSAGSLKTTLACFAFAPC | Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. | Q2H988 |
Q2T0H6 | DUT_BURTA | dUTP pyrophosphatase | pseudomallei group | MKLDLKILDARMRDYLPKYATTGSAGLDLRACLDAPVTLKPGDTALVPTGLAIHLADPGYAALILPRSGLGHKHGIVLGNLVGLIDSDYQGELMISTWNRGQTEFVLNPFERLAQLVIVPVVQATFNIVGDFAQSDRGAGGFGSTGRH | 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. | Q2T0H6 |
B4G9X6 | EIF3K_DROPE | eIF-3 p25 | Sophophora | MSHLVKMENGQSQTIQEMLGCIERYNPDHLKTLEAYIQDQAKNNTYDLEANLAVLKLYQFNPHMLNFEITYTILLKSLTNLPHTDFVMAKCLLLPQQMKDENIQTIIDLADILERADFTLFWQRAEVNRTMFRHISGFHDSIRKFVSHVVSITFQTIKKDLLKELLGGIEDSTLESWIKRNGWKHQGQDLIVVAMQDDKIKTKNITEKIEFENVGALMAQCL | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. | B4G9X6 |
O27197 | FKBPL_METTH | Rotamase | Methanothermobacter | MAVNKGDFIKIEFTGKVKETGEVFDTTYEEVAREAGLGIKKIFGPIPVVVGGGHLIKGLDEAVIGMEEGEEKHVEIEPEDAFGNRDPKLVQLIPMGEFKRQGIKPYPGMTLTVEGHEGRVLNVSGGRVRVDFNHELAGKTLEYDLKVKEIITDDAEKVKSMIQLHYPSQNMDIDKTEVKIEDGKVIIHMDEMTRFDNRSYMDVTLARFRIARDIWENIEGVEKVEFADVFEKRDMEAEEKEEEVEDAGED | Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding. Also exhibits chaperone-like activity . In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates. The PPIase activity is much lower than those of other FKBPs reported against oligopeptidyl substrates. As a chaperone, protects green fluorescent protein (GFP) and rhodanese from thermal denaturation or aggregation, and suppresses the aggregation of chemically unfolded rhodanese and elevates the yield of its refolding . | O27197 |
O75154 | RFIP3_HUMAN | MU-MB-17.148 | Homo | MASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYLDPSGLGVISFEDFYQGITAIRNGDPDGQCYGGVASAQDEEPLACPDEFDDFVTYEANEVTDSAYMGSESTYSECETFTDEDTSTLVHPELQPEGDADSAGGSAVPSECLDAMEEPDHGALLLLPGRPHPHGQSVITVIGGEEHFEDYGEGSEAELSPETLCNGQLGCSDPAFLTPSPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK | Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. Also required for the structural integrity of the endosomal recycling compartment during interphase. May play a role in breast cancer cell motility by regulating actin cytoskeleton. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) . | O75154 |
P51685 | CCR8_HUMAN | TER1 | Homo | MDYTLDLSVTTVTDYYYPDIFSSPCDAELIQTNGKLLLAVFYCLLFVFSLLGNSLVILVLVVCKKLRSITDVYLLNLALSDLLFVFSFPFQTYYLLDQWVFGTVMCKVVSGFYYIGFYSSMFFITLMSVDRYLAVVHAVYALKVRTIRMGTTLCLAVWLTAIMATIPLLVFYQVASEDGVLQCYSFYNQQTLKWKIFTNFKMNILGLLIPFTIFMFCYIKILHQLKRCQNHNKTKAIRLVLIVVIASLLFWVPFNVVLFLTSLHSMHILDGCSISQQLTYATHVTEIISFTHCCVNPVIYAFVGEKFKKHLSEIFQKSCSQIFNYLGRQMPRESCEKSSSCQQHSSRSSSVDYIL | Receptor for the chemokine CCL1/SCYA1/I-309. May regulate monocyte chemotaxis and thymic cell line apoptosis. Alternative coreceptor with CD4 for HIV-1 infection. | P51685 |
Q44685 | TRPB_BUCAI | Tryptophan synthase beta chain | Buchnera | MTLLNPYFGEFGGMYVPQILMPALFELEKNFVSAQKDAEFQKKFFYLLQNYAGRPTPLTLCKNLTKGTKTKIYLKREDLLHGGAHKTNQVLGQAMLAIRMKKKEIIAETGAGQHGVASAIACALFNLKCRIYMGIKDIKRQNTNVFRMKLMGAEVISVKNGSGTLKDACNEALRDWSSSYKKSHYMIGTAAGPHPYPTIVREFQKMIGEETKKQILEKENKLPDSIIACIGGGSNAIGIFSDFINDKVNLIGVEPAGYGIHTGKHGAPLKHGRTGIYFGMKSHLMQNKQGQIQESWSISAGLDFPSVGPEHAWLNSINRAKYVSITDEEAISAFQVLSRKEGIIPALESSHALAYALKLMKKDPTIEQILIANLSVVEIKIFLQYMMF | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q44685 |
Q54465 | MERA_SHEPU | Hg(II) reductase | Shewanella | MILLSIEGMTCPSCVAHVKEALDAIEGVNKVEISYENARATITTNGGVSVTVLIGAIEALGYIAKESTGTAKEITSPNDCCDNENASNTESNQTQHVAIIGTGSGAFACAIKAAEGGAKVTLIEGADVIGGCCVNVGCVPSKILIRAAQLAQQQRNNPFTGLENHAPQLSRALLTQQQTARVEELRAAKYQNILETNPALSLLKGWAQFKNANTLIVRKNDGTEQAVHADKILIATGSTPTIPPIDGLTETPYWTSTEALFAQELPQHLVVIGSSVVALEIAQAYRRLGSEVTILARHTLLYREDPLLGEKLTGCFEKEGIRVLNSTQATKVTHDGSQFTLETNAGDLRCDRLLVSTGRHANTCQLNLGAVGVTTNKKGEIVVNERMETNVPGIYAAGDCCNMPQFVYVAAAAGSRSGINMTGGYAKLDLSTMPAVIFTDPQVATVGLTEEQANAQDIETDSRVLEMENVPRALANFETDGFIKLVTEKATGRLIGAQILAHEGGELIQSAALAIRNRMTVTELADQLFPYLTMVEGLKLCAQTFNKDVKELSCCAG | Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). | Q54465 |
A9B5N1 | LON1_HERA2 | ATP-dependent protease La 1 | Herpetosiphon | MSEVERTTTIPDEIAILPLLGTVAYPQTIMPLAIGQPESIRLIDDLMAGQRIVGLMALKNEDERPNPVLPEDFYQLGSAAVVHKLMKLPDGTLRAAMQVLERIEIVEIIQTEPYYRAKIRVMPDALAESEQLEVTALMRSIGTIASQIAPLIPQFPTELLNSVLSEEDPRRLAYLVASYARMSVTDRQAVLAEPSIKQKLLKLNEVLTRELNVLQIGQQIQSQVQDEMSKTQREYVLREQLKAIRKELGENNEQEVEVDRLAEQIEAAGMSAEAHQQAMRELDRLRQMPTAAAEYSVIRGYLETLIALPWQKRSDDTIDVAQATEVLDADHYGLDEIKERILDYLAVRELRRKRSPERDPGRGAILCFVGPPGVGKTSLGRSIAKAMNREFVRLSLGGVHDEAEIRGHRRTYIGAMPGSLIQAIRRSGVNNPVVLLDEIDKLSSDHRGDPTSAMLEVLDPAQNTNFRDHYLDVAWDLSPVMFIATANTLQTIPAPLRDRLEIIQLGSYTMREKYEIASRYLVPEQREQHSLAPNEVEIDHEALLVAIEEYTREAGVRNLEQQIGTLMRKAARQVALGSATPIVLDPAKTREYLGKRRYFSEIHERTDRPGIVTGLVWTPVGGDIIFIEATKMTGRGNFALSGQLGDVMKESARAALSWVRAEGEAYGIDPNFAQHYDLHVHVPAGAQPKDGPSAGIAMATALVSLLTGRVLRDDVAMTGEITLRGKVLPIGGVREKVLAAHRAGIRTIILPQRNLADLDEIPADVLAEVQFHGVEHVGQVIELALRAEASEAPVSVPESAVMPNLFQSDVEVLVH | ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | A9B5N1 |
P63638 | MURI_STAAN | Glutamate racemase | Staphylococcus | MNKPIGVIDSGVGGLTVAKEIMRQLPNETIYYLGDIGRCPYGPRPGEQVKQYTVEIARKLMEFDIKMLVIACNTATAVALEYLQKTLSIPVIGVIEPGARTAIMTTRNQNVLVLGTEGTIKSEAYRTHIKRINPHVEVHGVACPGFVPLVEQMRYSDPTITSIVIHQTLKRWRNSESDTVILGCTHYPLLYKPIYDYFGGKKTVISSGLETAREVSALLTFSNEHASYTEHPDHRFFATGDPTHITNIIKEWLNLSVNVERISVND | Provides the (R)-glutamate required for cell wall biosynthesis. | P63638 |
C1DLI3 | RIBA_AZOVD | GTP cyclohydrolase II | Azotobacter | MSVVFVAASKLPTPFGVFTMHGFLDEATGKEHVALTLGTVDDGAPVLGRLHSECLTGDALFSLRCDCGFQLEAALRAIAAEGRGVLLYLRQEGRGIGLLNKIRAYKLQDAGADTVEANERLGFRADQRDYGICKPMLEHLGITAIKLMTNNPRKVKALEGAGIQVTERVPLQTGLNPHNQKYLATKAGKLGHLLGSLHQGEVETPTGS | Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. | C1DLI3 |
Q9C5W3 | NADK2_ARATH | NAD kinase 2, chloroplastic | Arabidopsis | MFLCFCPCHVPIMSRLSPATGISSRLRFSIGLSSDGRLIPFGFRFRRNDVPFKRRLRFVIRAQLSEAFSPDLGLDSQAVKSRDTSNLPWIGPVPGDIAEVEAYCRIFRSAERLHGALMETLCNPVTGECRVPYDFSPEEKPLLEDKIVSVLGCILSLLNKGRKEILSGRSSSMNSFNLDDVGVAEESLPPLAVFRGEMKRCCESLHIALENYLTPDDERSGIVWRKLQKLKNVCYDAGFPRSDNYPCQTLFANWDPIYSSNTKEDIDSYESEIAFWRGGQVTQEGLKWLIENGFKTIVDLRAEIVKDTFYQTALDDAISLGKITVVQIPIDVRMAPKAEQVELFASIVSDSSKRPIYVHSKEGVWRTSAMVSRWKQYMTRPITKEIPVSEESKRREVSETKLGSNAVVSGKGVPDEQTDKVSEINEVDSRSASSQSKESGRFEGDTSASEFNMVSDPLKSQVPPGNIFSRKEMSKFLKSKSIAPAGYLTNPSKILGTVPTPQFSYTGVTNGNQIVDKDSIRRLAETGNSNGTLLPTSSQSLDFGNGKFSNGNVHASDNTNKSISDNRGNGFSAAPIAVPPSDNLSRAVGSHSVRESQTQRNNSGSSSDSSDDEAGAIEGNMCASATGVVRVQSRKKAEMFLVRTDGVSCTREKVTESSLAFTHPSTQQQMLLWKTTPKTVLLLKKLGQELMEEAKEAASFLYHQENMNVLVEPEVHDVFARIPGFGFVQTFYIQDTSDLHERVDFVACLGGDGVILHASNLFKGAVPPVVSFNLGSLGFLTSHPFEDFRQDLKRVIHGNNTLDGVYITLRMRLRCEIYRKGKAMPGKVFDVLNEIVVDRGSNPYLSKIECYEHDRLITKVQGDGVIVATPTGSTAYSTAAGGSMVHPNVPCMLFTPICPHSLSFRPVILPDSAKLELKIPDDARSNAWVSFDGKRRQQLSRGDSVRIYMSQHPLPTVNKSDQTGDWFRSLIRCLNWNERLDQKAL | Involved in chlorophyll synthesis and chloroplast protection against oxidative damage. | Q9C5W3 |
Q93JG0 | SEPF3_STRCO | Cell division protein SepF 3 | Streptomyces albidoflavus group | MKSGEPVNSHDVTDEQWEGLAQVVPLRGRDAWPSAVGHRAMPEAETERRRRFVVLRINVFADAREVAETLMAGIPVLLDLTSAEGEVAKRVLDFSTGVVFGLASGMHRVDRNVFLLTPAGTEVNGLMESAAGVPGV | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. | Q93JG0 |
A1U2Y6 | RL19_MARN8 | 50S ribosomal protein L19 | Marinobacter | MSGKNNIISQLEAEQMTKEIPAFAPGDTVVVQVRVTEGNRERLQAFEGVVIGKRNRGMNSSFTVRKISYGVGVERTFQTYSKLIDSVSVKRRGDVRQAKLYYLRDLSGKAARIKEKLN | 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. | A1U2Y6 |
Q5ZT17 | SODC_LEGPH | Superoxide dismutase [Cu-Zn] | Legionella | MNKSGIILIGTILFSSMAIADDLTAPIYTTGPKPVAIGKVTFTQTPYGVLITPDLTNLPEGPHGFHLHKTADCGNHGMHAEGHYDPQNTNSHQGPYGNGHLGDLPVLYVTSNGKAMIPTLAPRLKLSDMHNLAVMIHANGDTYSDNPPQGGGGDRIACGVIK | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Q5ZT17 |
O46262 | HUNB_DRODA | Protein hunchback | split tarsi subgroup | WYSSMFAANIKQEPISHHHHHHHAHHSHHAHDSNSNSNASSPHQSPLPSPNPPSHTNLQLEQYLKQQQQQQQQHQHQQQQQPMDTLCAAAMTPSPSNNDQNSLGWLVGLPNPMQTIMPANMRPSPTATTATAAAAAPTTTAAAIALQANDKLQALTPPMDVTPPKSPAKSQQSCAEPEKEHDLMSNSSEDMKYMA | Gap class segmentation protein that controls development of head structures. | O46262 |
Q5LWL4 | IF2_RUEPO | Translation initiation factor IF-2 | Ruegeria | MSDTDGKKTLGLRGSRPGNVKQSFSHGRTKNVVVETKRKRVVVPKPGAGKPSAGGSSPAGDPSRRPAGISDAEMERRLNALKAAKARESEEAAQREAEEKARAEERERRRAEQEAKEREQREAEQRAREKAEEEERQRREAEEEAKRAAVRAAAEQEAPKAERSAERAPAAARPEGGDNARRTTDRDREREQRQTRGKGRQDGRRSGKLTLSQVTDGEGGRQKSLAAMKRKQERARQKAMGGAAEREKVIREVQLPEAIVVSELANRMAERVADVVKELMKMGMMVTQNQTIDADTAELIIEEFGHKVVRVSDSDVEDVISDIEDAEEDLKPRPPVITIMGHVDHGKTSLLDAIRDAKVVAGEAGGITQHIGAYQVKTDGGATLSFLDTPGHAAFTSMRSRGAQVTDIVVLVVAADDAVMPQTVEAINHAKAAGVPMIVAINKIDKPEANPTKVRTDLLQHEVVVEAMSGEVQDVEVSAKTGEGLDELLEAIALQAEILELKANPDRPAQGAVIEAQLDVGRGPVATVLIQKGTLRQGDIFVVGEQYGKVRALINDKGERVSEAGPSVPVEVLGLNGTPEAGDVLNVTSTEAQAREIAEYRAQVAKDKRAAAGAATTLEQLMAKAKADENVAELPILVKADVQGSAEAIVQAMEKIGNDEVRVRVLHSGVGAITETDVGLAEASGAPIMGFNVRANASARNTANQKGVEIRYYSVIYDLVDDVKAAASGLLSAEIRENFIGYANIKEVFKVSNVGKVAGCLVTEGVARRSAGVRLLRDNVVIHEGTLKTLKRFKDEVAEVQSGQECGMAFENYDDIRPGDVIEIFEREEVTRTLT | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. | Q5LWL4 |
Q9JYS8 | DPO4_NEIMB | DNA polymerase IV | Neisseria | MSSRKIIHIDMDAFYASVELREQPHLKGRPVVVAWEGARSVICAASYEARQFGLHSAMSVATAKRLCPQAVYVPPHFDLYRQVSAQIHAVFRRYTDLIEPLSLDEAYLDVTRNFKNIPYAGDVAKEIRAAIFAETGLTASAGIAPNKFLAKIASDWRKPNGQFVLPPHKVMAFLETLPLGKIPGVGKVTLKKMQSLGMRTAGDLRRFERGELLNHFGRYGYRLYDLVRGTDERPVKAERERLQISTEITLPEDLPLEQAAGHLPHLAEDLWRQITRKNVEAQSVTLKLKTYDFRIITRTLTYSSVLPDCALCCRLRKC | Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Q9JYS8 |
Q1GGM0 | PURQ_RUEST | Phosphoribosylformylglycinamidine synthase subunit I | unclassified Ruegeria | MKAAVVVFPGSNCDRDLAVAFEQAGFDVSMVWHKDSELPEGVDIVGVPGGFSYGDYLRCGAIAAQSPICKAVVAHAERGGYALGVCNGFQILTETGVLPGALLRNAGLKYICKTVDLAVATSDSAFTQGYNAGDVIGVPIAHHDGNYYADDATVQMLKDQDRVAFTYVDNPNGSVADIAGILSENRRVLGMMPHPERAADEGHGGTDGVAMFRALSGLLTDA | Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. | Q1GGM0 |
Q9QXF8 | GNMT_MOUSE | Glycine N-methyltransferase | Mus | MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVMSVDASDKMLKYALKERWNRRKEPSFDNWVIEEANWLTLDKDVLSGDGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGTGRDGSPGFSKFRLSYYPHCLASFTELVRAAFGGRCQHSVLGDFKPYKPGQAYVPCYFIHVLKKTD | Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate . Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine . | Q9QXF8 |
A1USR6 | RS13_BARBK | 30S ribosomal protein S13 | Bartonella | MARIAGVNIPTNKRLVIALQYIHGIGEKFAHKIIEKVGIPAERRVHELSDSEILQIRETIDRDYQVEGDLRREVAMSVKRLMDLGCYRGLRHRRSLPVRGQRTHTNARTRKGPARAIAGKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | A1USR6 |
Q6LWN2 | DGGGP_METMP | Geranylgeranylglycerol-phosphate geranylgeranyltransferase | Methanococcus | MDIKAYFELIRLKNCLTASFGAFIGGLIASYFNLAMVDNLILASIVVFLVCGFGNALNDIYDLKIDRINKPKRPIPSKRITLNNAKVFSYSLVVMGLFISLFNISCFLMAVLNSIVLQQYASTYKKNKIIGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDLKEKVISIPIKCGERSIYIAAFLLIFAIFLSPLPYLFGFFGIYYMISVVFCDLLFLFGIYKLVFNPSKMEAKKASRNIKIVTNLVLIAFLIGSLFK | Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | Q6LWN2 |
Q31PU7 | COFG_SYNE7 | FO synthase subunit 1 | Synechococcus | MKHFSDQTWRSPQQSAVITYSPAYTLVPTYECFNRCTYCNFRRDPGMDEWLSLSTAQQRLLTVRDRGVCEVLILSGEVHPQSPRRAAWRQRLIELAELALDMGFLPHTNAGPLNRAEMIALQNVNVSLGLMLEQLTPQLQRTVHRAAPSKDPQLRLQQLEQAGELGIPFTTGLLLGIGETSRDRLETLEAIAACHDRWGHIQEVILQPHSPGRQQAIQHPPLAPDELIDCVAIARQVLPTSIAIQVPPNLLTQPQQLADCLGAGARDLGGIVPYDEVNPDYQHHDLDELREALAQQGWQLQPRLPVYPHLVDRLPQRLQTHVAAWLNRFNSQSRSS | Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil. | Q31PU7 |
Q9M5P3 | CCDA_ARATH | Cytochrome b6f biogenesis protein CCDA | Arabidopsis | MNLSVNRCITGGFVGGFSSCRLNHEKRWVRAGKHCELERERSLVSDAVSLERLESKSIKLAMLASGLGVANLVTLSSAKAADLKMIVLDQATSIYILAEGSLGDSVGNFLYSANQQANEAVQDQLSALSVTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKSRGQVIGDTVAFALGLATTLALLGIVASFAGKAYGQIGQGLPVAASGLAIVMGLNLLEIIELQLPSFFNNFDPRAAAANFPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPVIGGSLLLTYTTGYVAPLIVAASFAGALQSLLSLRKVSAWINPISGALLLGGGLYTFLDRLFPAATMVM | Required for the transfer of reducing equivalents from stroma to thylakoid lumen. Involved in the biogenesis of the plastid cytochrome b6f complex by probably transferring reducing equivalents from stromal m-type thioredoxin (Trx-m) to the lumenal thioredoxin HCF164. | Q9M5P3 |
B1KHY4 | ALR_SHEWM | Alanine racemase | Shewanella | MKPFPRAEISAQALKNNLSRLRQIAPNSSVMAVVKANGYGHGLLNVASCLTEADGFGLARLEEALALRAGGVKAKLVLLEGFFRQVDLTTLVEHGIDTVIHNEVQLDMLENASLSKPVTVWLKLDSGMHRLGFTPEQFAQVYARLEACPQVAKPINIMSHFACADEPDNPMTQEQLQVFEALTKNSKGYRTLANSAGTLYWPDSQADWIRPGIALYGVSPVIGDLGRNHGLEPAMKLVSQLIAVREHKAGQPVGYGCFWHAKADTRLGVVAIGYGDGYPRNAPEGTPVWVNGRRVPVVGRVSMDMLTVDLGIDAKDSIGDDVVLWGKELPVEEVAEHIGTIAYELVTKLTPRVAVCLD | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | B1KHY4 |
C0HLJ6 | CO1A2_MEGAE | Alpha-2 type I collagen | Megatherium | SGGFDFSFLPQPPQEKDGGRYYGVGLGPGPMGLMGPRGPPGASGAPGPQGFGPAGEPGEPGQTGPAGARGPPGAPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNTGPSGPAGPRGEQGLPGVSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGASGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGSSGEEGKRGPNGESGSTGPTGPPGLRGNPGSRGLPGADGRAGVIGPAGARGASGPAGVRGPSGDTGRPGEPGLMGARGLPGSPGNVGPAGKEGPAGLPGIDGRPGPIGPAGARGEAGNIGFPGPKGPAGDPGKAGEKGHAGLAGNRGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPAGTTGEAGKPGERGIPGEFGLPGPAGPRGERGPPGESGAVGPSGAIGSRGPSGPPGPDGNKGEPGVVTAGPAGSGGLPGERGAAGIPGGKGEKGETGLRGEVGTTGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGIVGPTGPVGSAGPAGPNGPAGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGLRGPRGDQGPVGRTGETGAGGPPGFTGEKGPSGEPGTAGPPGTAGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPSGAVGPGVNGAPGETGRDGNPGSDGPPGRDGLPGHKGERGYAGNAGPVGAAGAPGPHGTVGPAGKHGNRGEPGPVGSVGPVGALGPRGPSGPQGIRGDKGEPGDKGPRGLPGLKGHNGLQGLPGLAGQHGDQGSPGPVGPAGPRGPAGPSGPAGKDGRTGHPGAVGPAGIRGSQGSQGPSGPPGPPGPPGPPGASGGGYDFGYEGDFYRA | Type I collagen is a member of group I collagen (fibrillar forming collagen). | C0HLJ6 |
C3P9L3 | HSLO_BACAA | Heat shock protein 33 homolog | Bacillus cereus group | MKDYLVKALAFDGEVRAYSVRTTNTVSEAQRRHDTWRTASAALGRSLTAGTMMGAMLKGDQKLTIKVEGNGPIGPILVDAHANGDVRGYVTNPHVDFEGTEQGKLRVYQAVGTEGFVTVIKDIGMREPFIGQSPIVSGELGEDFTYYFAVSEQTPSSVGVGVLVNGDDSILAAGGFILQIMPGAQEETISFIEERLQKIPPVSTLIEQGLSPEELLYAVLGEDKVKVLETMDVQFNCTCSRERIESVLISLGKTELEQVREEEEETEVHCHFCNERYKFSKEDITNLIENL | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | C3P9L3 |
Q089W9 | MOAC_SHEFN | Molybdenum cofactor biosynthesis protein C | Shewanella | MSNCFTHINADGNAHMVDVTEKAVTEREARAEAFIDMAPDTLAMIMNGSHHKGDVFATARIAGIQAAKKTSDLIPLCHPLMLTKVEVELEAQPEHNRVRITSLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDMIISQVRLLEKRGGKSGHFKA | Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). | Q089W9 |
Q2NQP5 | RS11_SODGM | 30S ribosomal protein S11 | Sodalis | MAKAPIRARKRVKKQVSDGVAHIHASFNNTIVTITDRQGNALGWATAGGSGFRGSRKSTPFAAQVAAERCAEAVKEYGIKNLEVVVKGPGPGRESTVRALNAAGFRITNITDVTPIPHNGCRPPKKRRV | 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. | Q2NQP5 |
Q2KAC2 | PSD_RHIEC | Phosphatidylserine decarboxylase beta chain | Rhizobium | MSLFNTVRNTIVPVHKEGYPFVAAFFVASLVLGWIFKPLFWIGMIFTLWCAYFFRDPERVTPQDDDLVISPADGKVSAIQMVTPPAELDLGSEPMLRISVFMNVFNCHVNRAPMRGRIVSINYRSGSFVNAELDKASEDNERNGLVIETRHGQIGVVQIAGLVARRILCWANTNEPLDAGERFGLIRFGSRLDVFLPAGAAPRVSLGQTAIAGETVIAEFASAKGPVISRHS | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q2KAC2 |
Q8Z8T2 | HEMH_SALTI | Protoheme ferro-lyase | Salmonella | MRQTKTGILLANLGTPDAPTPEAVKRYLKQFLSDRRVVDTPRLLWWPLLRGVILPLRSPRVAKLYQSIWMDGGSPLMVYSREQQQALAARLPDTPVALGMSYGSPSLESAVDELLASDVDHIVVLPLYPQYSCSTVGAVWDELGRILARKRRIPGISFIRDYADDGAYIDALAKSARESFARHGEPDLLLLSYHGIPQRYADEGDDYPQRCRDTTRELVSALGLPPEKVMMTFQSRFGREPWLTPYTDETLKMLGEKGTGHIQVMCPGFAADCLETLEEIAEQNREIFLEAGGKKYAYIQALNATPEHIDMILKLTAPYR | Catalyzes the ferrous insertion into protoporphyrin IX. | Q8Z8T2 |
Q93DA2 | METN_STRMU | Methionine import ATP-binding protein MetN | Streptococcus | MSKAIIKLDHIDITFHQKKRTIEAVKGVTVHINQGDIYGIVGYSGAGKSTLVRVINLLQTPTKGKITVDQDVIFENGEKRLSSQELRKKRHEIGMIFQHFNLMAQKTARQNVAFALRHSNLSAAQKESKVTELLELVGLTDRAENYPSQLSGGQKQRVAIARALANDPKILISDEATSALDPKTTKQILALLQDLNKKLGLTVVMITHEMQIVKDICNRVAVMQEGSLIEEGSVLDIFSNPREDLTKDFIKTATGIEEALIKIKQQEIVKNLPANAALVQLKYAGKTTDEPILNNLYKKYQVTANILYGNIEILEKTPVGEMIVILEGAATNIDQALNDLTHSDLTVTVLKRGV | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. | Q93DA2 |
A6V7W8 | RECR_PSEA7 | Recombination protein RecR | Pseudomonas | MSFSPLIRQLIESLRILPGVGQKSAQRMALMLLERDRSGGLKLAQALTAAMEGVGHCRQCRTLSEEELCPQCADPRRDDSLLCVVEGPLDVFAVEQTGYRGRYFVLKGHLSPLDGLGPEAIGIPELDARIRDGAFSEVILATNPTVEGEATAHYIAQLLADRGLTLSRIAHGVPLGGELELVDGGTLAHALAGRRPIS | 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. | A6V7W8 |
Q2YDG0 | GPC5C_BOVIN | G-protein coupled receptor family C group 5 member C | Bos | MAIHRTVLMCLGLPLFLLPGARAQEQAPPGCSPDLNPLYYNLCDRSEAWGIILEAVAGAGVVTTFVLTIILVASLPFVQDTKKRSLLGTQVFFLLGTLGLFCLVFACVVKPSFSTCASRRFLFGVLFAICFSCLVAHVLALHFLVRKNHGPRGWVIFLVALLLSLVEVIINTEWLIITLVRGAGTEGDALGNGSAGWVAVSPCAIANADFVMALIYVMLLLLCAFSGAWSALCGRFKRWRKHGVFILLTTTASIAVWVVWIVMYTYGNRQHNSPTWDDPTLAIALATNAWAFVLFYVIPEVSQVTRSSPEQSYQGDLYPTRGVGYETILKEQKGQSMFVENKAFSMDEPASAKRPVSPYSGYNGQLLTSMYQPTEMTLMHKAPSDGAYDVILPRATANSQVTGSANSTLRAEDIYAAQGRQEATLPKEGKNSQVFRNPYVWD | This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways. | Q2YDG0 |
Q99063 | PRA1_USTHO | Pheromone receptor 1 | Ustilago | MLDHVTPFFALFACILVLFALGWHIRSRNVGTITLSLYLFFGNLDNFVNSVAWWSTAEDKAPGFCEVSIRLRHALYIAIPASNLVIARKLESIASTRQVRASASEHKKSIIIDLLISVGLPVLYVSLMIVNQTNRYGIIEQVGCWPFLSLSWVWVLLVAAPVLIVSFASAVYSVLAFRWFWIRRRQFQAVLASSASTLNKARYIRLLVLTAIDMLLFFPIYVGSVSDTIRGAITTSYVSWSYVHTGFSYIPQFSAEVMEMQPSFKARLILSRLVCPISAYIFFAMFGLGQEARQGYKHAVLKALVFCKLRKERQKPIQNHIVANIEVVTFQSRETSGGIDGSPHSEKFSINTPTKYEEA | Receptor for the A2 pheromone, a prenylated mating factor. | Q99063 |
Q53138 | COBM_RHOER | Precorrin-3 methylase | Rhodococcus erythropolis group | MTVYFIGAGPGAADLITVRAQRIIAASPVCLYAGSLVPQELLAECPEGARVIDTARLSLDEIVALLIEADAAGQDVARLHSGDPSIFSAVAEQVRRLESAGVAYQVVPGVPAFTAAAASLGRELTVPGVSQSIVLTRVSTLSTAMPEGEDLRSLGRSGATMVVHLGAHRIDQIAEELIEDYGRDCPAAVVAFASRPDEIVLRGTLATIADQVKAAGVTKTAVVIVGRVLAAEGFPDSYLYSATRERTTH | Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5. | Q53138 |
B8E088 | RSMH_DICTD | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Dictyoglomus | MEEIEIIHKPVMLKEVIHYLKLSPGKIVVDATLGLGGHSSEILRELKGEGLLIGIDRDEEVLNLARERLRKIANNFVLFNTTYDKVQEILKELKLSFIDAILFDLGFSSFHIEKSERGFSFMRPEEPLDMRYSKDTTLTAADILNSFNELELSNLFWEYGEEPLSRKLAKKIVERRKEKKFVYVKDLLEVVEEVIPKRKRHEATKVFQALRIVVNDEVNILKRALDQIPFILAPRGRIVVLTYHSIEDRVVKNFFKSHSDKIFPVNKKVIRPSVNEIRENRRARSAKLRVGERRE | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | B8E088 |
Q9SSM4 | CHM1B_ARATH | Vacuolar protein-sorting-associated protein 46.2 | Arabidopsis | MGNTDKLMNQIFDLKFTSKSLQRQSRKCEKEEKAEKLKVKKAIEKGNMDGARIYAENAIRKRSEQMNYLRLASRLDAVVARLDTQAKMTTITKSMTNIVKSLESSLATGNLQKMSETMDSFEKQFVNMEVQAEFMENAMAGSTSLSTPEGEVNSLMQQVADDYGLEVSVGLPQPAGHAIPTKTEEKVDEDDLSRRLAELKARG | Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. Mediates the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for embryonic axis establishment and seedling growth . Required for autophagic degradation of plastid proteins. Promotes the efficient sequestration of cargo from plastids into autophagosomes. Mediates the efficient delivery of autophagic plastid bodies to the vacuole, but not into the cytoplasm . | Q9SSM4 |
Q2RSU7 | RLP_RHORT | 5-methylthioribulose-1-phosphate isomerase | Rhodospirillum | MTDRLRATYRVKATAASIEARAKGIAVEQSVEMPLSAIDDPAVLDGIVGVVEEITERGEDCFEVRLALSTATIGGDAGQLFNMLFGNTSLQDDTVLLDIDLPDDLLASFGGPNIGAAGLRARVGASADRALTCSALKPQGLPPDRLADLARRMALGGLDFIKDDHGMADQAYAPFASRVGAVAAAVDEVNRQTGGQTRYLPSLSGHLDQLRSQVRTGLDHGIDTFLIAPMIVGPSTFHAVVREFPGAAFFAHPTLAGPSRIAPPAHFGKLFRLLGADAVIFPNSGGRFGYSRDTCQAVAEAALGPWGGLHASLPVPAGGMSLARVPEMIATYGPDVIVLIGGNLLEARDRLTEETAAFVASVAGAASRGCGLAP | Catalyzes the conversion of 5-methylthio-D-ribulose 1-phosphate (MTRu-1P) to a 3:1 mixture of 1-methylthioxylulose 5-phosphate (MTXu-5P) and 1-methylthioribulose 5-phosphate (MTRu-5P) . Involved in the MTA-isoprenoid shunt of the methionine salvage pathway . | Q2RSU7 |
Q23588 | UTPP_CAEEL | Pyrimidine-nucleoside phosphorylase | Caenorhabditis | MNGLVKNGNVEKPNKYFDIKDKRDFLYHFGFGVDTLDIPAVFGDTKFVCTGGSPGRFKLYAEWFAKEANIPCSENLSRSDRFVIYKTGPVCWINHGMGTPSLSIMLVESFKLMHHAGVKNPTFIRLGTSGGVGVPPGTVVVSTEAMNAELGDTYVQIIAGKRIERPTQLDAALREALCEVGKEKSIPVETGKTMCADDFYEGQMRLDGYFCDYEEEDKYAFLRKLNALGVRNIEMESTCFASFTCRAGFQSAIVCVTLLNRMDGDQVQIAKEQYIEYEERPFRLVTAYIRKQTGI | Catalyzes the reversible phosphorylytic cleavage of uridine and thymidine to uracil and ribose-phosphate or thymine and deoxyribose-1-phosphate . The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable). Required for normal lifespan . | Q23588 |
Q2YU70 | DNLJ_STAAB | Polydeoxyribonucleotide synthase [NAD(+)] | Staphylococcus | MADLSSRVNELHDLLNQYSYEYYVEDNPSVPDSEYDKLLHELIKIEEEHPEYKTVDSPTVRVGGEAQASFNKVNHDTPMLSLGNAFNEDDLRKFDQRIREQIGNVEYMCELKIDGLAVSLKYVDGYFVQGLTRGDGTTGEDITENLKTIHAIPLKMKEPLNVEVRGEAYMPRRSFLRLNEEKEKNDEQLFANPRNAAAGSLRQLDSKLTAKRKLSVFIYSVNDFTDFNARSQSEALDELDKLGFTTNKNRARVNNIDGVLEYIEKWTSQRESLPYDIDGIVIKVNDLDQQDEMGFTQKSPRWAIAYKFPAEEVVTKLLDIELSIGRTGVVTPTAILEPVKVAGTTVSRASLHNEDLIHDRDIRIGDSVVVKKAGDIIPEVVRSIPERRPEGAVTYHMPTHCPSCGHELVRIEGEVALRCINPKCQAQLVEGLIHFVSRQAMNIDGLGTKIIQQLYQSELIKDVADIFYLTEEDLLPLDRMGQKKVDNLLAAIQQAKDNSLENLLFGLGIRHLGVKASQVLAEKYETIDRLLTVTEAELVEIHDIGDKVAQSVVTYLENEDIRALIQKLKDKHVNMIYKGIKTSDIEGHPEFSGKTIVLTGKLHQMTRNEASKWLASQGAKVTSSVTKNTDVVIAGEDAGSKLTKAQSLGIEIWTEQQFVDKQNELNS | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Q2YU70 |
C0SVZ6 | CURS1_CURLO | Curcumin synthase 1 | Curcuma | MANLHALRREQRAQGPATIMAIGTATPPNLYEQSTFPDFYFRVTNSDDKQELKKKFRRMCEKTMVKKRYLHLTEEILKERPKLCSYKEASFDDRQDIVVEEIPRLAKEAAEKAIKEWGRPKSEITHLVFCSISGIDMPGADYRLATLLGLPLTVNRLMIYSQACHMGAAMLRIAKDLAENNRGARVLVVACEITVLSFRGPNEGDFEALAGQAGFGDGAGAVVVGADPLEGIEKPIYEIAAAMQETVAESQGAVGGHLRAFGWTFYFLNQLPAIIADNLGRSLERALAPLGVREWNDVFWVAHPGNWAIIDAIEAKLQLSPDKLSTARHVFTEYGNMQSATVYFVMDELRKRSAVEGRSTTGDGLQWGVLLGFGPGLSIETVVLRSMPL | Catalyzes the synthesis of curcumin by condensing feruloyl-CoA with a diketide-CoA in the curcuminoid biosynthesis. | C0SVZ6 |
B3H2N1 | GTF_ACTP7 | Polymerizing glucosyltransferase | Actinobacillus | MENNIDLNVYFCFVNRPCTGGDFVNLDHVRTLRKLGINASILLAGNQSEEIVNSFGSLPVVILNEEIEFSSQDIFIVPEVMQVLYDLASKMTVFPRMIMHNQNPFYTGYGFLSAQHINEHRLERIIVPSSYTKYKLQEIGVTKPIDIIHPYIPDYFKPAEKQREVIQIAFSRRKRSAEFDIFKFYFLSLYSHKHSVNFVNIQGLTREEVAKVMSEAAIFISFAERESLGLMTLEAMASGCHVIGFSGYTDIYNNEVIDDSVGDWIGEGEYTLFAQKVCQAIDDFVNGKMNPKIENGLRLIEQRFRIRHFEQEVKRVYGNIFDYDLENSRS | Catalyzes the transfer of a glucose moiety from UDP-glucose to another glucose that is N-linked to an asparagine within a peptide or protein. Can act in a repetitive manner, and this way it elongates the N-linked glucose by a glycan chain consisting of several alpha-1->6 linked glucose residues. Is able to add up to six glucose units in vitro. Cannot use UDP-Gal, UDP-GlcNAc or UDP-GalNAc as a substrate donor. | B3H2N1 |
A8ZU48 | CH60_DESOH | Chaperonin-60 | Desulfosudis | MAGKEIKYSTKAREAMLAGVRTLADAVAVTLGPRGRNVVIEKSWGSPTVTKDGVTVAKEIELEDKFENMGAQMVKEVASKTSDTAGDGTTTATVLARAIYEEGQKLVAAGNNPMAIKRGIDKACEVAVKELAGMSKPTKNQREIAQVGTISANSDETIGNIIAEAMEKVGKEGVITVEEAKSMDTTLDVVEGMQFDRGYLSPYFVTDAEKMVVSLENAYILINEKKLSNMKELLPILEQTAKAGRPLLIIAEDIEGEALATLVVNKLRGTLNVAAVKAPGFGDRRKAMLEDIATLTGGQVVSEDVGINLEGITLGDLGHAKRITIDKDNTTIVDGAGKKADIEGRVKQIRAQIEDTTSDYDREKLQERLAKLVGGVAVINVGAATETEMKEKKARVEDALNATRAAVEEGVLPGGGVALVRCLDALSKIKIKSEEKLGVKVVMRAIEEPLRRIANNAGVEGSVVIEKVKNETGSFGYNAATGDYGDLIAAGVIDPTKVVRFALQNACSVASVMLTTEAMIAEKPSKEEPAAMPGGGMGGMGGMGGMGGMM | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | A8ZU48 |
A1SQV9 | RNPA_NOCSJ | Protein C5 | Nocardioides | MLSAAHRLRDGATFREAIRRGRRAGRQTLVVHLLVGEPVASQPARVGFVVSRAVGNAVIRNQVKRRLRHLAREHVSSLPGSAVLVVRALPPAANASAAELARDLERCLLRVGAEVTG | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | A1SQV9 |
Q39D07 | QUEF_BURL3 | PreQ(0) reductase | Burkholderia cepacia complex | MNPEHSPLGKATVYAAQYDASLLFPIPRAGAREQLGITSALPFFGTDIWNAYELSWLNARGKPQIAVATFYVPAESPNIVESKSFKLYLGSFAQTTFDSIDAVRDTLKRDVSAACGATVSVQLVSPHDFGKLEMEELDGLSLDRLDLDTDVYEPDPSLLKAAEDEAPVEETLVSDLLRSNCPVTGQPDWGSVQIHYVGPQIDHAGLLRYIISFRNHTGFHEQCVERIFLDILHACKPVKLAVYARYTRRGGLDINPFRTNYNQPMPDNARNARQ | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | Q39D07 |
A1CYJ1 | NOP16_NEOFI | Nucleolar protein 16 | Aspergillus subgen. Fumigati | MGRVLQKKKNRSSTPKQKPKRTGQLKSGKKKINVLGNAIIAQNWDRKLTLTQNYRRLGLVHKLNAPTGGSEKRPTKDGRIEELPEDPLHIRGSAKASAKQAAMGETRVERDPETGKIIRVIRDEEEIEIGGRKVKPSNPLNDPLNELSEDEAAQQPASQRANAKSAIVQQLERQADQEGQAVKAKKPRHQSKREEEWIMRLIERHGENYSAMARDRKLNPMQQSEGDLKRRIRKWKANHSS | Involved in the biogenesis of the 60S ribosomal subunit. | A1CYJ1 |
Q47C26 | RLMF_DECAR | rRNA adenine N-6-methyltransferase | Dechloromonas | MHPRNKNAEGYDFAALAATSAALAKHIKTTQAGTASIDFANPAAVKMLNRAILMHHYGVKGWDIPAGYLCPPIPGRADYIHSVADLLATCNKKNIPSGPGVRVLDIGVGANMVYPLIGHAEYGWSFLGVDIDEAALANAQSIIGKNPELASDIELRHQPVWDNIFTGLLRSGEVFDLSICNPPFHNSPDDVHAVSQRKWNNLNKPGAKRGAAEPRLNFGGGGSELWCNGGERAFVKRMIEQSCNIPKRVMWFTSLLSQGDNLPHIEAALKKAKVVESRIIPMAQGQKQSRLVAWTFCGNGEREKWRRERWTAAPSYAVPAFAEQTAPLTAEATPPAADPV | Specifically methylates the adenine in position 1618 of 23S rRNA. | Q47C26 |
P39040 | TYTR_CRIFA | N(1),N(8)-bis(glutathionyl)spermidine reductase | Crithidia | MSRAYDLVVIGAGSGGLEAGWNAASLHKKRVAVIDLQKHHGPPHYAALGGTCVNVGCVPKKLMVTGANYMDTIRESAGFGWELDRESVRPNWKALIAAKNKAVSGINDSYEGMFADTEGLTFHQGFGALQDNHTVLVRESADPNSAVLETLDTEYILLATGSWPQHLGIEGDDLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTHENPAKVTKNADGTRHVVFESGAEADYDVVMLAIGRVPRSQTLQLDKAGVEVAKNGAIKVDAYSKTNVDNIYAIGDVTDRVMLTPVAINEGAAFVDTVFANKPRATDHTKVACAVFSIPPMGVCGYVEEDAAKKYDQVAVYESSFTPLMHNISGSTYKKFMVRIVTNHADGEVLGVHMLGDSSPEIIQSVAICLKMGAKISDFYNTIGVHPTSAEELCSMRTPAYFYQKGKRVEKIDSNL | Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase. | P39040 |
B7XHR6 | KIN1_ENTBH | Probable serine/threonine-protein kinase KIN1 homolog | Enterocytozoon | MQSTSKYNCDSDYIAGRNYNTKRTNGREELSTGLTNEETGVVNISDENNIFFKKNIDYVKGSRIGKYKLIKTLGKGSCAKVVQAEDCETGEYVAIKIIERTPKQLSDIRIYREALICSLFNHPHIIKLLDFFHTTEYFFLIFEYVDGQQLYDIILNKGYLDEDEARKYFRQIISAVDYSHRNSVVHRDLKIENILIDRNDNIKLIDFGLSNFYDADDLLGTFCGSLYFAAPELLLGTRYTGPEIDVWSLGVILYVMLVGKVPFDDENIHALQNKIKSCKFKFEKTISPEAQDLITNMILSSDARINLENVKKSKWTNLGYKNLTNNFMTLRKPIIEINKNILRALQAAMFFQFTDMERVLMQYLQICKGDKHSLEQTYWCKKPVVILYYLTMEKFNELNYKSIPIDIDTGMNTKSLIDITIEKQPIIIYNFVRFTNAKKNNNPYNLFFSRSVFEPEMEFLNMTKDVSLDSCNISEDENKKHNFPKIKQSIIKGLFKGIKIKNGDKDYVKNAIIKILLDLDITYEANEKSYFCSYSHSGVECHFKIDLYFNILLLEHYVVLNCLNRKKDNFKLVTELIKEKLEEIGDTSNYPENAI | Serine/threonine protein kinase involved in regulation of exocytosis. | B7XHR6 |
Q7Y1W1 | TIC56_ARATH | Translocon at the inner envelope membrane of chloroplasts 56 | Arabidopsis | MSSMNFNPFQNWFEKPPNPVPSINFVSLADSFFPKSQSPNFASIGLPKFSKKSPKPETAGTDEPGPYKQIAEQFLWECENIPDYRHTPEVDKLLNEDPVFEKKENPSTEEIEAEQKWWESFRASPVVQFMTRAEEIADDMNKMELEDNDTPYRKEDKDYWRAIPHVPGFDGRPMPRKAIKSKEESDDKFWDFMKQFLFGLWGFRQRPYPPGRPIDVAQAIGYKRLEKRYYDFIMKTGGWWYKDRLGRSRGPCEIITLKTAYGAGIIDRDTFIWGEDMDEWAPIHMVYGLEPAIATWEVRLGAAATAFLHKLQKGIPPWVPLKGREPKTYKQLQKEAIESKKRDMAVLEANGGVWPGVRTPSHALFLWASGSELTTVLESDHMPNKFIPKQLRLELAKVIPGLRPWEVISIEQAMDQISYGGEWYREPLGTYTTGPPYIREWNRSVMRLFRIFYNLSVRVGQKLERTVPGFDTIMDKVQKDYDKRIARRMKRREEELREEDLKHYSGRTDEDEEEEEEEDDDSNSKKD | Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope. | Q7Y1W1 |
B2BS84 | VKT_AUSLA | Putative Kunitz-type serine protease inhibitor | Austrelaps | MTREKSLALLITLAAALAAAESPPGRCHSPKTVGPCRASFHRWRYNATSQMCQEFIFGGCKGNANNFVSKQDCFQTCIRGGAAEATVVPSGPATEVATPRAGHLPEAYENRPGFREFCAAPRVVGPCRASFLRWYFDLESRMCKMFIYGGCRGNKNNYLFEEHCWSQCTGDGEITEEPGDAGAQPPLPSEPFSFSTRAVVLAVLPAILVTILLGSMGVFFVKICRKNPELSVGTVWSTLDDKEYLMSNAYTL | Serine protease inhibitor. | B2BS84 |
Q6A7K8 | DXR_CUTAK | 2-C-methyl-D-erythritol 4-phosphate synthase | Cutibacterium | MKKVIILGSTGSIGTQTLEVISSRRDQFEVAGISAGGSDVGSLAQQIIDFSIPVVAVAREDAAEELQRALAVQAGSRGRIVPNPRILTGPDASTELAAMPADVVCNAITGAAGLRPTLATLAAGTTLALANKESLVIGGRLVTQAAASGQIVPVDSEHSAFAQCLRGGGRNEVRRLVLTASGGPFRGRDRASLADVSAAEAMKHPTWNMGRVITINSSTLVNKGLELLEAALLYDVDLDDITVVVHPQSIVHSMVEFWDGATIAQASPPDMRLPIALGLSWPDRLPDAAAGCDWSTATQWTFEPLDNDTFGAVELARRAGHAAGTAPAVFNAANESCVDAFCAGSIGFLDITDTIAAVLDEHLSGDENDTLGARHVGDEALTLDAVLAADAWGRRRAAEVCARGIRR | Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | Q6A7K8 |
A1U3L1 | PYRC_MARN8 | Dihydroorotase | Marinobacter | MTRQITITRPDDWHLHVRDGDILNDVVPATAACFGRAIIMPNLVPPVTDASAAMAYRDRILAAARGTDFQPLMTLYLTESTTAETIREAKAAGVVAAKLYPAGATTNSASGVTDIRNIYPVLEAMADCGMLLLVHGEVTDSDIDIFDREKVFLERVLAPTLTAFPSLRVVLEHITTAESAEFVRNHQGNNLGATLTPQHLMYNRNHMLVGGIRPHLYCLPILKRNKHQEALREAVASGDPRFFLGTDSAPHAKDKKEAACGCAGCYSAYGAIGLYADIFEELGILDKLEAFASFNGADFYGLPRNTDTVTLVREPWTMPENLPLAGGGIVPLKAGETVNWRLA | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | A1U3L1 |
B0XYC4 | PGXC_ASPFC | Poly(1,4-alpha-D-galacturonide)galacturonohydrolase C | Aspergillus subgen. Fumigati | MLITNPALLGILASLVPLALGAPNQPIQARSRKCVIPSSYASSHGTADDSPAVASAFAQCAENSVIVFQEGVDYNIFHPIKATNLSNVEIRVLGNLHLPQDITAVQNIVKSGQSTWFTFQGPRVDWTGADDIKNGWINSYGQAWWDANPANSSSFPNRPHLMSYKTSQASIKNFRSRKPIAWNVKLQGDDITVSHAIVDATSTGGFPFNTDGFDVEGTNISITDSVMFNGDDAIAVNTPSHNIVFARNTIGYQSHGMSIGSLGKDPTDFANITNLRFEDVTVIDALYAARFKSWSGGRGLVKNVVWKNIRTFNVTFPIFVTQSYSDQSASRPGTIDPFSSVMMEDFTWSDFSGTINTYHPGDGSCVTDPCWYNVGLPNLKHTEAIVLECNTESSCKNFRTEGIRLHPQSKDSPSVICMKATAELNPKLGFECKNGTFVPH | Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates. | B0XYC4 |
B1XS66 | PTH_POLNS | Peptidyl-tRNA hydrolase | Polynucleobacter | MTKLIVGLGNPGEEHEEDRHNAGFWFVDALAKQLGVRFESEKRFHGKVAKAKWEGEDLFLLKPSTYMNLSGQSVGALCRFHKIMPADILVVQDELDIKPGSARLKLGGGTGGHNGLKDIQAHLSTPNYWRLRLGIGHPRDIAGDGRPMDVADYVLRRPQLTEQKLINTSIENGLNILSLFLKGDTQTAMMELHSKG | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | B1XS66 |
A4WD96 | NDK_ENT38 | Nucleoside-2-P kinase | Enterobacter | MTIERTFSIIKPNAVAKNVIGSIFARFESAGFKIVGTKMLHLTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLESENAVQRHRDLLGATNPANALAGTLRADYADSFTENGTHGSDSVESAAREIAYFFAEGEVCPRTR | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | A4WD96 |
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