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2.75k
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AlphaFoldDB
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10
Q2GG24
GATB_EHRCR
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Ehrlichia
MTIIKGNRCDWEVVIGLEVHAQVISNSKLFSGASTKTYDALPNTQVALFDVAMPGMLPVLNEYCVYQAIKTGIALSCKINKYSAFDRKNYFYPDLPSGYQITQFYYPIATEGKIVLEDHDMKEIRIARIHLEQDAGKSIHEFDKTYIDFNRAGVALMEIVSEPDFRSIEEVAEYLKKLRMILRFIETCDGDMEKGSLRCDANVSVKPVGSSELGIRSEIKNLNSIRYVMQAIEYEANRQVNALENGEIVTQNTLLFDVTSGQTRVIRTKEDAHDYRYFPDPDLFPLKIDDQYIDHVRSSLPELPMQKRERYTNDFSLSKYDADILSSDKDVAIYFEKVAEKHDGKLAASWITGELFGRLNRLGITIGESSVTAEDLIQLLDLIVNNTISGKIAKQVFDMMFESGKSPALIVSEHGLKQVSDENALSVIVERVLKNNASKVVEYKQGKEKLFGYFVGQVMKETQGKANPDMVNSIIKQQLEN
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).
Q2GG24
F4JYE9
DHFS_ARATH
Protein GLOBULAR ARREST 1
Arabidopsis
MRTLWNHFSTISYIKISPRMRRISAANLISNRNLSTISSTEDPELRDFVGFLESLKNYEKSGVPKGAGTDSDDGFDLGRMKRLMLRLRNPHYKYKVVHVAGTKGKGSTSAFLSNILRAGGYSVGCYSSPHILSIKERISCNGEPVSASTLNDLFYSVKPILEQSIQEENGSLSHFEILTGIAFSLFEKENVDIAVIEAGLGGARDATNVIESSNLAASVITTIGEEHMAALGGSLESIAEAKSGIIKHGRPVVLGGPFLPHIEGILRSKAASVSSSVILASNIGSSSSIKGIINKNGIGLCQSCDIVIQNEKDDQPIVELSDVNLRMLGHHQLQNAVTATCVSLCLRDQGCGRVTDEAIRIGLENTRLLGRSQFLTPKEAETLLLPGATVLLDGAHTKESARALKEMIKKDFPEKRLVFVVAMASDKDHVSFAKELLSGLKPEAVILTEADIGGGKIRSTESSVLKESWIKAADELGSRSMEASENKTVLGSLKLAYKILSDDTTSSDSGMVIVTGSLHIVSSVLASLQH
Conversion of folates to polyglutamate derivatives, including tetrahydrofolate . Required during embryogenesis; from maternal tissues until the globular stage, and from the embryo after the globular stage .
F4JYE9
B4RZN1
RS10_ALTMD
30S ribosomal protein S10
Alteromonas
MPNQRIRIRLKAFDHKLIDQSTAEIVETAKRTGAQVSGPIPLPTRKERYTVLISPHVNKDARDQYEIRTHKRLVDIIEPTDKTVDALMRLDLAAGVDVQISLG
Involved in the binding of tRNA to the ribosomes.
B4RZN1
Q9I2H6
RIMJ_PSEAE
[Ribosomal protein S5]-alanine N-acetyltransferase
Pseudomonas
MPGNRRQVPILHRDADFLLRALQPDDFVRTSRYENANREHLAPWEPLRDPGYFSVDNARARTLLQVASMDEGEALLLLLLDPDDGEVLGRCSYTNIVRGVFQACHLGFSLAAAAQGRGLMARALRVANRYCFEQLGLHRIMASHLPRNARSERLLESLGFEKEGYARAYLKIAGVWEDHVLRALVDAPR
Acetylates the N-terminal alanine of ribosomal protein S5.
Q9I2H6
B0JU07
RIMM_MICAN
Ribosome maturation factor RimM
Microcystis
MEENWLEIGTIVAPQGLEGELRVLSVSDFPERFQKRGMRGIQGPQGGEIREITLLRGRELPGKNVYVIKLEGVENREQAEALRGYKLWANKLEKPRLKADEYHVSELVNLEVYHHLTGEKIGVVVDIFWAGNDILAVQLEANLASVKKKSPSSDSEARALVPFVKEIVPLVDLKAARIEIAPPPGLLEINLS
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
B0JU07
Q18FC0
RF1_HALWD
Translation termination factor aRF1
Haloquadratum
MSTDAEDVSNDRRKYEFRKVIEELREYEGSGTQLVTIYIPPDRQVSDVVAHITQEHSEASNIKSKQTRTNVQDALTSIKDRLRYYDTYPPDNGIVLFSGAVSTGGGQTTMVTRSLESPPEPVQSFRYHCDSDFLTDPLEDMLADKGLFGLIVLDRREANVGWLKGKRVEPVKSASSLVPGKQRKGGQSAQRFARLRLEAIDNFYQEVAGMANDLFVPKRHEIDGVLVGGPSPTKDEFLDGDYLHHELGDVVVGKFDVSYTDESGLHDLVDSAQDVLADQEVMKDKAEMEEFFEKLHGGEEATYGFEPTRKNLMMGAVDRLLLSEDLRSDVVVYECPDGHEEYEVIDRRHDDPEHTCSDCGSASEKTEREDVIEYLMSIAEQRGTETKFISTDFEKGEQLHNAFGGIAGILRYATGI
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Q18FC0
Q49ZE3
RS11_STAS1
30S ribosomal protein S11
Staphylococcus
MARKQVSRKRRVKKNIENGVAHIRSTFNNTIVTITDEFGNALSWSSAGALGFKGSKKSTPFAAQMASETASKTAMEHGLKSVEVTVKGPGPGRESAIRALQSAGLEVTAIRDVTPVPHNGCRPPKRRRV
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.
Q49ZE3
Q57JR8
DSBI_SALCH
Protein-disulfide oxidoreductase DsbI
Salmonella
MDFIKGLWRDLRARPVDTLVRWQEQRFLWLLMAIAMGGLIILAHSFFQIYLYMAPCEQCVYIRYAMFVMVIGGVIAAINPKNIVLKLIGCIAAFYGSIMGIKFSIKLNGIHHAVHNADPDSLFGVQGCSTDPTFPFNLPLAEWAPEWFKPTGDCGYDAPIVPDGVTLSSVQQWFVDLYQQSEGWYLLPPWHFMNMAQACMLAFGLCLILLLVMSGAWALKLARGK
Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.
Q57JR8
B8ZSB7
RL23_MYCLB
50S ribosomal protein L23
Mycobacterium
MATIADSRDIILAPVISEKSYGLLDDNVYTFVVHPDSNKTQIKIAIEKIFSVKVASVNTSNRKGKCKRTRTGFGRRKNTKRAIVTLAPGSKSIDLFGTPA
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
B8ZSB7
P41384
CKS1_PATVU
SUC1 homolog
Patella
MSARQIYYSDKYFDEDFEYRHVMLPKDIAKMVPKNHLMSEAEWRSIGVQQSHGWIHYMKHEPEPHILLFRRKVTGQ
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
P41384
P17025
ZN182_HUMAN
Zinc finger protein KOX14
Homo
MTPASASGEDSGSFYSWQKAKREQGLVTFEDVAVDFTQEEWQYLNPPQRTLYRDVMLETYSNLVFVGQQVTKPNLILKLEVEECPAEGKIPFWNFPEVCQVDEQIERQHQDDQDKCLLMQVGFSDKKTIITKSARDCHEFGNILHLSTNLVASIQRPDKHESFGNNMVDNLDLFSRSSAENKYDNGCAKLFFHTEYEKTNPGMKPYGYKECGKGLRRKKGLSLHQRIKNGEKPFECTACRKTFSKKSHLIVHWRTHTGEKPFGCTECGKAFSQKSQLIIHLRTHTGERPFECPECGKAFREKSTVIIHYRTHTGEKPYECNECGKAFTQKSNLIVHQKTHTGEKTYECTKCGESFIQKLDLIIHHSTHTGKKPHECNECKKTFSDKSTLIIHQRTHTGEKPHKCTECGKSFNEKSTLIVHQRTHTGEKPYECDVCGKTFTQKSNLGVHQRTHSGEKPFECNECEKAFSQKSYLMLHQRGHTGEKPYECNECEKAFSQKSYLIIHQRTHTEEKPYKCNECGKAFREKSKLIIHQRIHTGEKPYECPVCWKAFSQKSQLIIHQRTHTGEKPYACTECGKAFREKSTFTVHQRTHTGEKPYKCTECGKAFTQKSNLIVHQRTHAGKKAHGRGHTRKSKFMAH
May be involved in transcriptional regulation.
P17025
Q1MB43
ACCA_RHIL3
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Rhizobium
MHNYLDFEKPISDLEGKIIELKKLATEDESIDTTDEIGRLEVRVREAIVEIYSKLNPWQKTQVARHPQRPHFVDYAKTLFQEFTPLAGDRKFSEDAAIQAGLARFRGQPVAVIGQEKGNDTKSRLKHNFGSPRPEGYRKAIRILEMADRFGLPVISLVDTAGAYPGVGAEERGQAEAIARSTEMCLGVKVPLVSVVIGEGGSGGAIAIATGNKVYMLEHSIYSVISPEGAASILWRDSTRAREAATNMKITAEDLKSLGVIDGIISEPLGGAHRDPDSVIAATGDVIASALAEMAPRSGEQLRNDRRQKFLAMGRNL
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.
Q1MB43
Q9TUM6
PLIN2_BOVIN
Adipose differentiation-related protein
Bos
MASVAVEPQLSVVTRVANLPLVSSTYDLVSSAYISRKDQYPYLKSLCEMAEKGMKTITSVAVTSALPIIQKLEPQIAVANTYACKGLDRIEEKLPILNQPTNQVVANAKGAMTGAKDAVTTTVTGAKDSVASTITGVVDRTKGAVTGSVEKTKSVVSGSINTVLRSRVMQLMSSGVENALTKSELLVDQYLPLTKDELEKEAKKVEGFDMVQKPSYYVRLGSLSTKLRSRAYQQALCRVEEAKRKGQETISQLHSAFNLSELARKNVHNANQKIQDAQDKLYLSWLEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTMCHTLLSNIQGLPQNIQDRANHLGVMAGDIYSVFRNAASFKEVSDGLLASSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQVTESESAQAPGTTRRPGRWSRKHPKPVPVSNAEGSQPDDSSS
Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets.
Q9TUM6
Q2G341
ARGB_NOVAD
NAG kinase
Novosphingobium
MSQNHDPAMLAKAETLTEALPYLQRYAGKTFVVKYGGHAMGDPELAQDFAEDIVLLKAVGINPVVVHGGGPQIGRMLKALGIESRFVDGLRVTDKQTAEVAEMVLAGAINKELVSWIARAGGKAIGISGKDGGMVIARKVEAKKAPKAVADAESGDPIVVDLGFVGEPDRIDTTVIDTICKAGMIPVIAPIGVGEDGETYNINADTMAGSIAAALGAARLFLLTDVPGVLDKDKNLLTDLRPADIARLAEDGTISGGMIPKLETCVHAVEAGCEATVVLDGRVPHAMLLEIFTARGAGTLIRA
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Q2G341
A6VIG8
PURQ_METM7
Phosphoribosylformylglycinamidine synthase subunit I
Methanococcus
MIKVVPKVLVMSGYGINCETETAHTFQKAGAKTDIVHINDLIAGKKKMADYEIIMFPGGFSYGDDTGSGNAFANKIKNNLFDDLKEFINSGKLILGICNGFQVMTNLGLFALPSTDYGERISALEANTNNRYECRWVHIKENESICVFTKGIDIIHVPIAHGEGRFYCDEKTYLELKENKQIVFTYCDSEGNPANKEYPLNPNGAYYDIAGICDKSGRIMGLMPHPERSLYSISEPEYQLKKEIAKRNGEIIPEFIESNIQIFKNAVEYFNK
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.
A6VIG8
P31721
C1QB_RAT
Complement C1q subcomponent subunit B
Rattus
MKTQWSEILTPLLLLLLGLLHVSWAQSSCTGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPPGPRGPKGGSGDYKATQKVAFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNIVRGRDRDRMQKVLTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEGANSIFTGFLLFPDMDV
C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
P31721
P0CV44
RL111_PLAVT
Secreted RxLR effector protein 111
Plasmopara
MRGTLATALLLVASCRIAAESNQINPQQASHHVGTTLNKLFTKSSPRRFLRDNREQRVALALTAANESRTIENAVTSAVHGITDASTTTAATRDAARDILNQHAFPKEGIRPQFDLNLPPSETSALLTGASNIPQRNHAFSSITSGIAVSSSRTSNQRTAKTQANLDMSHQGTVRKTLSKTQFKNPAASKSTKRRKKARIIPPFVVNKVDTLYREHLTAKSLEFDPTIKETEAMLKLYVESTVDPLPVSTVHFNHFRYFKDQDLTLLKEKLGTTLESALSTLAALNLPPGMLKAIERPFVWYASLARWRAMYCDFFEFLNANSNKIATSLPNVEFFGGETSSTVRDQLLATLKEEMKTRTKTRRNGKIMNDLKVVLAKYNVEEEIKAAIRGLGEQFLKRDHEIIPLQRHSRRSPASQSRSNNQRTGLTPYGLQIPGPERDSFRHIESNKHA
Secreted effector that acts as an elicitor that induces cell death in host plant cells.
P0CV44
C3P778
TRHO_BACAA
tRNA hydroxylation protein O
Bacillus cereus group
MATTKPYRVLLYYMYTTIENPEEFAAEHLEFCNSLELKGRILVAKEGINGTCSGTVEQTEKYMEAMNNDPRFDGIVFKIDEADGHAFKKMHVRPRPELVTLRLEDDINPHEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKEVLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAVPVNQKEHVIVGKDHFTGEPCERYVNCANPECNKKILCSEENEAKYLRACSHECRVSPRNRYVIQHELTEEQVAAALEKIEAGK
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
C3P778
Q03ED1
RL6_PEDPA
50S ribosomal protein L6
Pediococcus
MSRIGRKPVEIPAGVEIKQDGNVVTVKGPKGELTRTMSSDITMSVDGNVVSFDRPNDNNKMRALHGTTRANFNNMVEGVVNGFEKKLELIGVGYRAQLKGKTLILNLGYSNPVEMETPEDLKVEVPDNTHINISGISKQRVGDLAAEIRAVRSPEPYKGKGVRYVGEYVRRKEGKTGK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Q03ED1
P11094
RK14_CHLRE
50S ribosomal protein L14, chloroplastic
Chlamydomonas
MIKPLSYLNVADNSGARELMCIRALGGSYRESANIGDVIIAVVKDALPNMPVKRSDIVRAVIVRTRKGIRRENGMAIRFDDNAAVIINKEGNPRGTRVFGPIARELRDKNFTKIVSLAPEVL
Binds to 23S rRNA.
P11094
B5XJZ7
UPP_STRPZ
UPRTase
Streptococcus
MGKCQVISHPLIQHKLSILRRQTTSTKDFRELVNEIAMLMGYEVSRDLPLEDVDIQTPVSKTVQKQLAGKKLAIVPILRAGIGMVDGLLSLVPAAKVGHIGMYRNEETLEPVEYLVKLPEDINQRQIFLVDPMLATGGSAILAVDSLKKRGAANIKFVCLVAAPEGVKKLQEAHPDIDIFTAALDDHLNDHGYIVPGLGDAGDRLFGPK
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
B5XJZ7
Q91VD1
LEG12_MOUSE
Galectin-12
Mus
MSTDEHLDPIPDSFILQPPVFHPVIPYGTTIFGGLYAGKMVTLQGVVPLHARRFQVDFQCGCCLHPQPDVAFRFSPRFYTVKPHVICNTHQGGLWQKEIRWPGVALQRGDSFLILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAVGFLNINPFVEGSREYPVGYPFLLYSPRLEVPCSRALPRGLWPGQVIVVRGLVLKEPKDFTLSLKDGTTHVPVTLRASFTDRTLAWVSSWGRKKLISAPFLFHPQRFFEVLLLCQEGGLKLALNGQGLGATSLDQKALEQLRELRISGNVHLYCVHC
Binds lactose. May participate in the apoptosis of adipocytes.
Q91VD1
Q2NU52
TRHO_SODGM
tRNA hydroxylation protein O
Sodalis
MPVLHNRVSNQELRARMLAESEPRTTVSFYRYFTLSDPQGFRDDLYRTLTALQVFGRVYIAAEGINAQISVLQSRFDAMREALYAAHPQLDGLRLNVALDDDGKSFWVLRMKVRPRIVADGIDDPTFNPANVGHYLKAEEVNALADDPQALFVDMRNHYEYEVGHFDQAIEIPSDTFREQLPMVVEMLQHDKDKKIVMYCTGGIRCEKASAWMRHNGFKNVYHVEGGIIEYARRAREQGLPLKFTGKNFVFDERLGERITPDIIAHCHQCGAPCDSHTNCRNQGCHLLFIQCPVCAEHYVGCCSVTCQEELSLPLSEQRSHRAGRENGMKIFNKSRERLQLSLTGEDSAQK
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q2NU52
Q9NR56
MBNL1_HUMAN
Triplet-expansion RNA-binding protein
Homo
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues.
Q9NR56
Q84LH3
WEX_ARATH
Werner Syndrome-like exonuclease
Arabidopsis
MSSSNWIDDAFTEEELLAIDAIEASYNFSRSSSSSSSAAPTVQATTSVHGHEEDPNQIPNNIRRQLPRSITSSTSYKRFPLSRCRARNFPAMRFGGRILYSKTATEVDKRAMQLIKVLDTKRDESGIAFVGLDIEWRPSFRKGVLPGKVATVQICVDSNYCDVMHIFHSGIPQSLQHLIEDSTLVKVGIGIDGDSVKLFHDYGVSIKDVEDLSDLANQKIGGDKKWGLASLTETLVCKELLKPNRIRLGNWEFYPLSKQQLQYAATDAYASWHLYKVLKDLPDAVSGS
Exonuclease that digests recessed strands of DNA duplexes in the 3' to 5' direction but hardly single-stranded DNA or blunt-ended duplexes. Also able to digest 3'-protruding strands and 3'-recessed strand termini of duplexes containing mismatched bases.
Q84LH3
Q3SSV7
RS17_NITWN
30S ribosomal protein S17
Nitrobacter
MPKRTLQGVVVSDKQAKTVVVRVDRRFTHPIYKKTIRRSKNYHAHDENNEFKPGDMVWIEESKPISKLKRWTVVRGEQRKTA
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Q3SSV7
Q4FNQ0
DNAJ_PELUB
Chaperone protein DnaJ
Candidatus Pelagibacter
MAKRDFYDVLGVSKSASPEELKSAYRKLAVKYHPDKNPGDKASEDKFKEAGEAYGVLSDKEKKQNYDNFGHAAFEGGGGRQGGGFGGGFGGADFSDIFEDFFGDFGGGQSRGRRKTNNRGSDLRYDLSITLEEAYEGKKQDIKFSTTEKCNTCNGNGSKPGHSPDRCTVCGGNGKVRSNQGFFTVQQTCPQCAGSGEEITNPCTDCNGQGNKQASKKISVTIPKGVDDGTRIRLAGKGEAGSKGGANGDLYLFVNVHSHDLFKRSDENLFFEFPISIADAALGTTIEIPTIDGGKAKIKIPDGTQNGKQFRLKGKGMPYMRGSGNGDLYVQVNTEVPISLNKEQKALLEKFREIENEKSNPSIKQFFQKAKSFWKN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q4FNQ0
A9M4F8
SUCC_NEIM0
Succinyl-CoA synthetase subunit beta
Neisseria
MNLHEYQAKELLAGYGLPVQGGILARNGEEAAAAYDKLGGKFAVVKAQVHAGGRGKAGGVKVVKSREEAKEVAESLIGTNLVTYQTDANGQPVNSVLVCEDMYPVQTELYLGAVVDRSTRRITFMASTEGGVEIEKVAAETPEKIFKVTVDPLVGLQPCQAREVAFQLGLKDKQINEFVKLMTGAYKAFVDNDFALFEVNPLAVRENGALACVDGKIGIDSNALYRLPKIAELRDKSQENERELKASEFDLNYVALEGNIGCMVNGAGLAMATMDIIKLKGGQPANFLDVGGGATKDRVVEAFKLILEDKSVKGVLINIFGGIVRCDMIAEAIVAAVKEINVNVPVVVRLEGNNAELGAKILNESGLKLTSADGLNDAAEKIVAAVNA
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
A9M4F8
P77875
NIFK_HERSE
Nitrogenase component I
Herbaspirillum
MPQNADSVLDHENLFRQPEYRELFARKKEEFEFAVPLDKVQDVAEWTKTKEYQQKNFAREALTINPAKACQPLGAVYAAVGFQNTLPFVHGSQGCVAYYRSHFSRHFKEPTSCVSSSMTEDAAVFGGLNNMIDGLANALSLYKPEMIAVSTTCMAEVIGDDLDSFIKNAKDKGSVPAEYDVPFAHTPAFVGSHVTGYDNALKGILTHFWDGKAGTVPALERKPNERINFIGGFDGFVVGNLPEVKRIFKLMGVDGTIVCDPSEVWNTPTDGQFRMYSGGTTKQEVIEALDAKATVVFQEFSTLKTAKYIAEKGQEVVTLNHPMGVAGTDQFLMELSRLSGQPIPAELELERGRLVD
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
P77875
B3QZF1
ATPD_CHLT3
F-type ATPase subunit delta
Chloroherpeton
MHSISIVGRRYALALMEVAVDQNIVGQVMADFELIEQTMVEAKQLRLAIQSPLIQAYKKAALLKEVFGGKVSQQVATFLFLLASKNRAEYLPEVIQEYRALLDEQNGVISVDIKTAVDLDDKQTKQLKDKLEAYTSKKVRVHLATDKQLIGGLTIQIGDTVLDGSIRHQLAMLKNNLAAGALN
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
B3QZF1
A1VKP2
FPG_POLNA
DNA-(apurinic or apyrimidinic site) lyase MutM
Polaromonas
MPELPEVEVTRLSFAERIAGARIEAVLVGKPLRWPLGCETQQLQGQRVLAVRRRGKYLLLDLSEGLLLMHLGMSGSVSFGLNLPVTGKHDHFDMVTSLGTLRLHDPRRFGAVVYASGEDDAVAKKLLGRLGVEPLSDAFDALVFHQWLKGRKTAIKPLLLAGQAVVGVGNIYASEALFLAGIRPTTKASLISKPRAARLHRAIQDVLTNAVAKGGSTLRDFSNADGEAGHFQLDAMVYDRAGLPCRVCAAPIKSIRQGQRSSFYCATCQKP
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
A1VKP2
P21793
PGS2_BOVIN
PG-S2
Bos
MKATIIFLLVAQVSWAGPFQQKGLFDFMLEDEASGIGPEEHFPEVPEIEPMGPVCPFRCQCHLRVVQCSDLGLEKVPKDLPPDTALLDLQNNKITEIKDGDFKNLKNLHTLILINNKISKISPGAFAPLVKLERLYLSKNQLKELPEKMPKTLQELRVHENEITKVRKSVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITTIPQGLPPSLTELHLDGNKITKVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLNNNKLVKVPGGLADHKYIQVVYLHNNNISAIGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRAAVQLGNYK
May affect the rate of fibrils formation.
P21793
C4JTH6
UTP25_UNCRE
U three protein 25
Uncinocarpus
MAVKGAAKGRGPPRRKQPRFETSRVQDLDDREPLNGEQVVSEDALNEASDAEYSVSSSDNEEEEKSTDKPYNVLLQLLNASEDSIGPAKKKRKLKHKEKNVKQQTEATKEASPGKGDLDLQDDLDVKEAENTESDNEQVENDEAEGSEDEADSGSDPFEIHFSQPDEAQLSKRIEATSQKWRTSRQTLPAGMRFTAVYPDVGEEQNLHRASLHSPKDLTLKRKLSEAASVHLPQFDAPNTSVAPYLFGYYDMIYGGRTTGNAAKLRDMYCLHALNHIIKTRDRVIKNNARVPKEGEDIEIRDQGFTRPKVLIILPTRQACVRVVDSISKFYQAEQQENRKRFMETFSTADDDTWEDKTEDFRELFGGNDDDMFRLGLKFTRKTVKFFSQFYSSDIILASPLGLRTAIEKEDGKKIEYDFLSSIELVIVDHADALLMQNWDHVEYIFSHLNLQPKEAHGCDFGRVRTWYLDGNAKYLRQTLILTSFITPEINSLFSHHAYNVFGKIKIDSTYPGAILDVPVPVPVRQTFSRFDSLSPVKDPDARFKYFTSTVLSSLAKNWSSSGKSSAAGTLIFIPSYLDFVRIRNYFATSSQTTNLSFGAISEYSSPRDVARARSHFMNGRHTVMLYTERLHHFRRYKIRGVKRVVMYGVPENPVFYKEIAGFLGIDPAAVGEAAEKGVRALFSKWDALKLERIAGTKRMGSMMLEKGGDTFTFT
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
C4JTH6
Q2S320
UPP_SALRD
UPRTase
Salinibacter
MENVTVVDHPLLKRDLTLLRREETPHGQFRKTVSDAAAILAYEAMRDIELEETSIETPLEQTTGYEIAEEVMVVPIMRAGLGMVDGFVRYVPEARVGHLGMQRDEETYRPVDYYSNIPSTIGHAHVFVVDPMLATGGSASFAIDHLKEEGGQDFTFACLVAAPEGVQKLREEHPDVPVVTAVLDRELDDNAFIRPGLGDAGDRIFGTRES
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Q2S320
B2VC79
AROA_ERWT9
5-enolpyruvylshikimate-3-phosphate synthase
Erwinia
MQDSLTLQPIALVDGTVNLPGSKSVSNRALLLAALAEGTTRLTNLLDSDDVRHMLDALKAIGVKYSLSADRTCCEIVGQGGPLNAKEPLELFLGNAGTAMRPLAAALCIGNGDVVLTGEPRMKERPIGHLVDALRQGGAEVEYLEQENYPPLRVKGGFSGGEVTVNGSVSSQFLTALLMAAPLAPNDTRIVIKGDLVSKPYIDITLKLMATFGVVVENNDYDTFHISGQQQYQATREYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIHFADVLEKMGASVEWGDDYIACTRGDLNAVDLDMNHIPDAAMTIATTALFAQGTTVMRNIYNWRVKETDRLTAMATELRKVGAEVEEGHDFISITPPAKIVFAEIGTYNDHRMAMCFSLVALSSSPVTILDPKCTAKTFPDYFEQLARLSHLA
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
B2VC79
O28126
CCA_ARCFU
tRNA-NT
Archaeoglobus
MKVEEILEKALELVIPDEEEVRKGREAEEELRRRLDELGVEYVFVGSYARNTWLKGSLEIDVFLLFPEEFSKEELRERGLEIGKAVLDSYEIRYAEHPYVHGVVKGVEVDVVPCYKLKEPKNIKSAVDRTPFHHKWLEGRIKGKENEVRLLKGFLKANGIYGAEYKVRGFSGYLCELLIVFYGSFLETVKNARRWTRRTVIDVAKGEVRKGEEFFVVDPVDEKRNVAANLSLDNLARFVHLCREFMEAPSLGFFKPKHPLEIEPERLRKIVEERGTAVFAVKFRKPDIVDDNLYPQLERASRKIFEFLERENFMPLRSAFKASEEFCYLLFECQIKEISRVFRRMGPQFEDERNVKKFLSRNRAFRPFIENGRWWAFEMRKFTTPEEGVRSYASTHWHTLGKNVGESIREYFEIISGEKLFKEPVTAELCEMMGVKD
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
O28126
Q4H3K6
FGFR_CIOIN
Fibroblast growth factor receptor
Ciona
MIQLQNTFIFIALTIFTSASTTSLKNETKPLNTISTLAAQTNISNPEEDLFDTNGAPKSDTVNASTTTDRHKIPRWVNEQKMQKRLHAEPAGNTVQFRCAVQGARPITVDWYKDGEPIKKNGRLGGYKFRQRNQQISLESVIMSDRAKYMCVAHNKYGSINHTYELDVVARIPIPPVLSADGMKNQTVKVGSTVTFRCRIVYSDAHPHVEWLKYNVNVTVLKRAGINTTDAEMEKLTLKNVSFADAGEYTCLAGNSIGVSHVSAWLTVLPVVDENDVWTEEIPQDTHYLIYIFGVVCFIILLAFIVYMCNSRYQNKDPPRLIPIENPDNIPPMSKMEEPVMLFGNEQAWRRMCLPHADHIEINIQPDLQWELKREDILLHERIDEGFFGQVFRADLIRCAGGRKEKVDAAVKMLKSTRTEKDMLDLLTEMDQMKRVGKHKNIVNLLGVCTQNGILWLVTEYAQKGNLRDYLRRNRPSELQYELSTPDSPAPPRDEPLTLRALMSASHQVARGMEYLSQKKCIHRDLAARNVLVANDFVMKIADFGLARDIRSNDYYRKETRGHLPYKWMALEAMTDNMFTHATDVWSFGILLWEIFSLGGSPYPGVKTHDLVRFLRNGDRLEQPQFASSELYRLMRDCWEESPRRRPQFRQLVEDLDRMLASSSSLEYIDLNSPCEADYLPSDVDSNEDTESRDSANATGEDSDSVFEPIDGHGAHAYEVDEAGPLLNPQPDANIVCNGHARMQSDV
Receptor for basic fibroblast growth factor.
Q4H3K6
Q5JIR3
VATA_THEKO
V-ATPase subunit A
Thermococcus
MGRIIRVTGPLVVADGMKGAKMYEVVRVGEIGLIGEIIRLEGDKAVIQVYEETAGIRPGEPVEGTGSSLSVELGPGLLTAMYDGIQRPLEVLRQLSGDFIARGLTAPALPRDKKWHFTPKVKVGDKVVGGDVLGVVPETSIIEHKILVPPWVEGEIVEIAEEGDYTVEEVIAKVKKPDGTIEELKMYHRWPVRVKRPYKQKLPPEVPLITGQRTIDTFFSQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVVYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDQGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKIAEFYERAGRVITLGSDERVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLRSYSLYIDAIQDWWHKNVDPEWRKMRDTAMALLQKEAELQEIVRIVGPDALPDREKAILIVTRMLREDYLQQDAFDEVDTYCPPKKQVTMMRVILNFYEKTMQAVDRGVPVDEIAKLPVREKIGRMKFEPDVEKVRALIDETNQQFEELFKKYGA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
Q5JIR3
C4XMR7
DTD_SOLM1
Gly-tRNA(Ala) deacylase
Solidesulfovibrio
MRLVVQRVREASVAVDGQAVASIEAGLLVLVGFGAADGSDFAAGKPCRATLEKLLDLRIFPDEAGKLNLSLRETGGGLLLVSQFTLYASCRKGRRPSFSEAAPPQVALGLYNALVEMAGQALPGRVGSGVFGADMDVSLVNWGPVTILLDSADLGGAT
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
C4XMR7
Q4UU98
CHED_XANC8
Probable chemoreceptor glutamine deamidase CheD
Xanthomonas
MSTAVQVDDVMRYRDSRFQTIAAKLLPTQYLVVDDDTALTTTLGSCVAACLRDPVLKIGGMNHFLLPEGQVGDGAPARYGSYAMELLINDMLKRGAHRKRIEAKVFGGANVLKGFTSNPVGTRNAEFVRQYLQAEHIPIIAEDLCGIHPRKVWFFPTTGRVVVQRLPHAHEAEVAAAESAVRARLSKAPVTGGVELFE
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Q4UU98
Q4QML8
SURE_HAEI8
Nucleoside 5'-monophosphate phosphohydrolase
Haemophilus
MRILVSNDDGFHAEGIQVLAMELRKIAEVIIVAPDRNRSAASSSLTLVEPLRPRHLDNGDYCVNGTPADCVHLALNGFLSGQVDLVVSGINAGCNMGDDTIYSGTLAAALEGRHLGLPAIAVSLDGRQHYETAARVVCDLIPKLHHQLLNPREIININVPDLLFEELKGYKVCRLGYRASSAEVIKQKDPRDETIYWIGPSALPEDESEGTDFYAVKNGYVSITPIQADLTAYHSLLSLQNWLEQEFTK
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q4QML8
Q31655
RBL_AJUCH
Ribulose bisphosphate carboxylase large chain
Ajuga
MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVLGEKDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFVEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAAEGNTIIREACKWSPELAAACEVWKEIKFEFPAMD
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Q31655
A6LN85
NADK_THEM4
null
Thermosipho
MKVLGIFHKPSLKSVAEKFSEILFDENFHVEYVGSEIPSIEVDLTLVLGGDGTFLKAAHKVRNPLVGFKGGRLGFLSSYTLGDFDKFLEDLKNENFERDIRYFLKAGDFYTLNEVLLIRDPVQKMVDIQIFFQDGDFYFHADGLIISTPTGSTGYSLSLGGPIMLPNVNSFVITPVAPQFLASRSIIVPDDEEIIVRIDQEINLILDGMDFGKVREVNLKKSRRRIVILRPKDYNFSKSIKEKLGYGKRFL
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
A6LN85
Q4UK24
NUOI_RICFE
NDH-1 subunit I
spotted fever group
MINYLKSFFLYEIVRGMALTLKYFFKPKVTINYPYEKSPVSPRFKGEHALRRYENGEERCIACKLCEAICPAQAIVIEADERDDGSRRTTRYDIDMTKCIYCGLCQEACPVDAIVEGPNFEFASLTHTALIYDKERLLQNGDRWEQALASKLHKDYEYR
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.
Q4UK24
A6W3T1
ATPD_MARMS
F-type ATPase subunit delta
Marinomonas
MAELKTVARPYAKAVFEVAREQGHIVEWADMLNVLASVTVEPKLKKALGNPAFSAEEKANALADVCAEVTTEQGKAFLLALAVNKRLSLLPAISELFLQFKLNFEKAVNVQFTSAFELTAEQTQALAASLAKKLDRTVNLTSETDASLIGGVVIRTGDLIIDGSVRGKLAKLAEAINS
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
A6W3T1
Q2YDJ8
KMT5A_BOVIN
SET domain-containing protein 8
Bos
MARGRKMSKPRAVEAAAAAAAVAATAPGPEMVERRGPGRPRTNGENVFTGQSKIYTYMSPNKCSGMRSPLQEENSVAQYEVKCQGKPLAGIYRKRDEKRNSGNAIRSSMKAEEQKIKDARRGPLAPFPNQKSEAAEPPKTPTSSCDTPNAAAAKQGLKKPVRGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGEFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIEAGEELLYDYGDRSRASIEAYPWLKH
Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.
Q2YDJ8
Q8CHZ9
MTF1A_MOUSE
Mitochondrial transcription termination factor 1a
Mus
MASRNIWCVRRNFLFDLRDWMLQYSAEVFLKSISFRPFSAECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKLFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKRDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEEKISASQIIENPRILDSSINTLKTRIRELSHAGYDLSTSSIALLSWSQRRYEAKLKRLCG
Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand.
Q8CHZ9
Q8BLC3
LYPD1_MOUSE
Ly-6/neurotoxin-like protein 2
Mus
MWVLGIAATFCGLFWLPGLALQIQCYQCEEFQLNNDCSSPEFIVNCTVNVQDMCQKEVMEQSAGIMYRKSCASSAACLIASAGYQSFCSPGKLNSVCISCCNTPLCNGPRPKKRGSSASAIRPGLLTTLLFFHLALCLAHC
Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro increases receptor desensitization and decreases affinity for ACh of alpha-4:beta-2-containing nAChRs . May play a role in the intracellular trafficking of alpha-4:beta-2 and alpha-7-containing nAChRs and may inhibit their expression at the cell surface . May be involved in the control of anxiety .
Q8BLC3
B3FIS0
TXLC_CYRSC
Lectin SHL-Ia1
Cyriopagopus
MKTSMFLTLTGLVLLFVVCYASESEEKEFPKELLSSIFAADSDFKVEERGCLGDKCDYNNGCCSGYVCSRTWKWCVLAGPWCR
Agglutinates erythrocytes.
B3FIS0
A1SBC7
LEXA_SHEAM
LexA repressor
Shewanella
MRPLTPRQAEILDLIKRNIAETGMPPTRAEIASRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLAGDELEDQPDPGLPLIGQVAAGEPILAQEHVEQYYQVDPAMFRPHADFLLRVRGDSMKDIGILDGDLLAVHKMNQARNGQVVVARVEDDVTVKRFEKQGNVVYLHAENEAFAPIRVDLANQSLTIEGLAVGVIRNGDWL
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.
A1SBC7
Q755C8
PUS1_ASHGO
tRNA-uridine isomerase 1
Eremothecium
MPSDASTGYVDDQPGDEAYKRGALYKQTKARRADYDSDKEAKRPCTEDSDVALAGTSEEKEARLPKRKVAVMVGYCGTGYHGMQYNPPNRTIEAELFEAFVKAGAISRANSTDLKKNGFMRAARTDKGVHAGGNVISLKLIIEDPAIKDKINEHLPPGIRVWGISRVNKAFDCRKLCGSRWYEYLLPTYSFIGPKPNTYLARTIEQCGEAASEKPDRDQESLDFWEAFRKAVDEKFTQEEQDAIVNYVAPSKEDFDENSGLYQKVKQYKQMENAHRRSYRVSSAKLARFREAMKQYLGPHNFHNYTLGKDFKDPSTVRFMKDITVSDPFVIGEMKTEWVSIKIHGQSFMLHQIRKMISMATLVARCNCSPERIAQSYGPQKINIPKAPALGLLLESPVYEGYNKRLLEFGYEPIDFRNYQKEMDTFKMVHIYDKIYKEEVDENVFNAFFNYIDAFNQVTGAQGEPTKSHDPAKIQLSIIDFLLPCSSSPQENASPEAQKAPETPAGDNTISAEQPKTATEVPTTQSDA
Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs.
Q755C8
B2VFU8
LGT_ERWT9
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Erwinia
MNNGYLAFPQFDPVIFSIGPVSLHWYGLMYLVGFVFAMWLAVRRANKPGSGWKKEEVENLLYAGFLGVFLGGRIGYVLFYNMPLFLENPLYLFKVWDGGMSFHGGLIGVIVVMLVFAHRTKRHFFQVADFIAPLIPFGLGAGRLGNFINGELWGRVDPNLPWAMLFPGSRSEDIALVAAHPQWQQLLSTYGVLPRHPSQLYELILEGVVLFIILNLFIRKSRPMGAVSGLFLIGYGAFRIIVEFFRQPDQQLGLFGGISMGQILSLPMILAGVIMMIWAYRRRPQQRIREAK
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
B2VFU8
Q3B3N9
MIAA_CHLL3
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Pelodictyon
MTVPVITGPTASGKSALAHRLALETGAEILSADSRQVYRELTIGSAKPSREMLREVAYHFINERAITEPFSAGAFALEATARIREIKRRGKRVIVAGGSALYLEGLISPFAELPPQNAEIRRKLSEQLADLGGELLYERLKQLDPEQAETLDPTKTHRLLRSLEIIEITGRTVTELQAKKSGEPSPPSSLHFKTFAIDIPREELYRQINRRTESMMEEGLLIEAEQLWKRYRIEIENKSLPALLTVGYQELFDHFRGRTTLDEAVTLIQQHTRNYAKRQLTFMRNRLTVQWMPADTDWTAHFTG
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Q3B3N9
A6KZL8
SYY_PHOV8
Tyrosyl-tRNA synthetase
Phocaeicola
MNFVEELTWRGMVHTMMPGTEELLAKEQVTAYLGIDPTADSLHIGHLCGVMMLRHFQRCGHKPLALVGGATGMIGDPSGKSQERNLLTEETLRHNVACIKKQLAKFLDFESDAPNKAELVNNYDWMKDFTFLDFAREVGKHITVNYMMAKDSVQKRLNGEARDGLSFTEFTYQLLQGYDFLHLYETKGCKLQMGGSDQWGNITTGAELIRRTNGGEVFALTCPLITKADGGKFGKTESGNIWLDPRYTSPYKFYQFWLNVSDEDAARYIKIFTSLSQEEVEALTAEHAEAPHLRVLQKRLAKEVTVMVHSEEDYNAAVEASGILFGNATSEALKKLDEDTLLAVFEGVPQFEVSRDALAEGVKAVDLFVDNAAVFASKGEMRKLVQGGGVSLNKEKLSAFDQVITTADLLDEKYLLVQRGKKNYYLVIAK
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
A6KZL8
Q6DGF9
ACBD4_RAT
Acyl-CoA-binding domain-containing protein 4
Rattus
MGTEKEEPDCQKQFQAAVSVIQNLPKNGSYRPSYEEMLRFYSYYKQATAGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEMKLVAQKVIDTVPLGEVAEDMFGYFEPLYQVIPDMPRPPETFLRRVTGWQEPAVNRDVQAAPEPSHPPKEPAPPSPESRLPRDLDLEVFCDSVEQLEPELVRVPVLSPVPAESELPHLHTGTGDSAQRVWAEQKEAAGRELTTRSSPESPEGFGGSLMGPQELDRWLVGTVQAMQESMKDVHRRLQILESKPQPLEQQRSPRTRPWPLGLSTPTLLFFILWPFVVQWLFRQFRTQRR
Binds medium- and long-chain acyl-CoA esters and may function as an intracellular carrier of acyl-CoA esters.
Q6DGF9
P43862
DPRA_HAEIN
Protein Smf
Haemophilus
MNDITYTLLRLMQVPKLGGVGIDKILSNITLNELLNYDDVAFRQMGWGAIQIRRWFKPEAKFIEPALVWSQKEGNHLVNYFSPFYPFLLKQTASFPPLLFVKGNLTALSQRQMAMVGSRYCTTYGEYWAKHFATELSLAGFTITSGLALGIDGHCHQAVVNIQGQTIAVLGSGLEQIYPSKHQRLSAQIIENNGALVSEFLPNQAPIAANFPRRNRIISGLSVGTLVVEATEKSGSLITARYALEQNREVFAVPGNIQNKSSQGCHRLIKQGAMLVENAKDILETLYQHSIHSQTEIDFDQIAVPNYTPPPDPRRLVEAPSHPKLYSRIGYTPVSIDDLAEEFNLSVDVLLVQLLDLELQDLIISENGLYKRV
Essential for efficient chromosomal DNA transformation but not required for plasmid transformation . Its disruption can be partially complemented by the smf gene of E.coli .
P43862
C5B9K5
PANC_EDWI9
Pantoate-activating enzyme
Edwardsiella
MLILETVPLLRREVRRWRQEGKRIALVPTMGNLHDGHMALVNEAHARADVVIVSVFVNPMQFDRPDDLARYPRTLQEDCEQLNRHGVDLVFAPAAEEIYPQGVSQQTYVDVPALSSILEGASRPGHFRGVATIVSKLFNLVQPDLACFGEKDYQQLQLIRKLVADMGYGTEIVGVPIVRGEDGLALSSRNGYLDSDERRLAPRLYNIMMQLASQLENGERDLEALLEQTASRLRQAGFCPDELFIRDADTLGDVNVDTRTAIVLMAAWLGQARLIDNVRIAFNADA
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
C5B9K5
O84375
ARODE_CHLTR
Shikimate dehydrogenase (NADP(+))
Chlamydia
MLCTTISGPSFLEAKKQILRSLKECHCFEMRVDLLSVSCLELKKLMELAPISILAWKKPESCSQADWIDKMQSLAELNPNYLDLEKDFPEEDMIRIRQLHPQIKIIRSLHTSEHTDIIQLYAHMRSSAADYYKFAVSSSSTTDLLDICHQKRSLPENTTVVCLGGMGRPSRILSPILQNPFTYARSTGSSPVAPGQFSLKHHYFYNFASLSAQSPICALIGDTSRSIGHLTHNPFFSQLGVACPYIKLPLTPQELPKFFSTIRTQPFLGVSVTSPLKTAVLPFLDKQAPSVKASGSCNTLVIRQGEIEGHDTDGEGLFSVLMQHQIPLNNQRVAIIGAGGAAQSIATRLSRANCELLIFNRTKAHAEDLASRCQAKAFSLEELPLHRVSLIINCLPPSCTIPKAVAPCVVDINTIPKHSTFTQYARSQGSSIIYGHEMFTQQALLQFRLWFPTLSFKHLEKTFIRRAAVLASLFSIAP
Bifunctional enzyme that catalyzes two sequential steps of the aromatic amino acids biosynthetic pathway. In the first reaction, the AroD domain catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate; in the second reaction, the AroE domain catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
O84375
Q5KUK3
NUOK_GEOKA
NDH-1 subunit K
Geobacillus thermoleovorans group
MTLSAYLALALILFCIGLYGALTKRNTVIVLICIELMLNAVNINFVAFAKYGAHPSVHGHVFALFAIAVAAAEAAVGLAALIAFYRSRKTVQVDEANSLKH
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 a menaquinone. 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.
Q5KUK3
A4J151
TRUA_DESRM
tRNA-uridine isomerase I
Desulforamulus
MKNIKLTLAYDGTNYHGFQEQRGTGLATIQEALEKALSTIAQTPIQVIGAGRTDAGVHAQGQVVNFRSEKWPVPAEKAPLALNVLLPGDIKVVKAEEVPMDFHARFSAVAKTYRYSIYHHRVMSPFHRYYCYHEPRRLDVNAMQEGAAYLLGTYDFKSFQAQGTPVKDTIRTIYRADIIEDAPVINLYLRGNGFLYNMVRIITGTLLNIGFGKIKPEDMVKIIESKNRTLAGTTAPPQGLCLMEVEY
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
A4J151
A9KQC8
Y047_LACP7
Nucleoid-associated protein Cphy_0047
Lachnospiraceae
MAKRGGFPGGNMPGNMNNLMKQAQRMQKQMEDKTKEMEEKQWEATAGGGAVTVTVSGKKEVVSVKLSKEVVDPDDIEMLEDLIVAATNEALRKMEEESASAMNSIAGGLGNFGGLGGLF
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
A9KQC8
P77737
OPPF_ECOLI
Oligopeptide transport ATP-binding protein OppF
Escherichia
MNAVTEGRKVLLEIADLKVHFEIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHSVSCLKVDPL
Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system.
P77737
Q7TU18
GCST_PROMP
Glycine cleavage system T protein
Prochlorococcus
MDLLKSPLYSKYIESNAKLVNFAGWEMPISFSGLINEHESVRTSAGFFDISHMGVISLRGINPKEYIQKFFPTNLYSFSEGQGLYTLMLNEKGGIIDDLIIYDLGQQEEDISEIFLIVNASRYQTDFSWIKNNLNTNNISISNAKKDKVLFALQGKNSFKLFEEWIKSSISHIPYFGCEYKIFKHISSKEKIFFSKTGYTGENGLEILLSAKAAINLWDFLVSKNIKPCGLGARDTLRLEAGMHLYGQDLNETTTPYEAGLGWLVHLENNHDFFGREFLEKQSRFGINKKLVGLNIEGRAIGRKGCEVFKDGENIGTITSGSWSPTKQKAIAFAYIQNSYATLNNVVEILIRGKTFKGTITKRAFYKKDI
The glycine cleavage system catalyzes the degradation of glycine.
Q7TU18
Q5ANA3
CDR1_CANAL
Pleiotropic drug resistance protein CDR1
Candida
MSDSKMSSQDESKLEKAISQDSSSENHSINEYHGFDAHTSENIQNLARTFTHDSFKDDSSAGLLKYLTHMSEVPGVNPYEHEEINNDQLNPDSENFNAKFWVKNLRKLFESDPEYYKPSKLGIGYRNLRAYGVANDSDYQPTVTNALWKLATEGFRHFQKDDDSRYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFAARLRTPQNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSAVILDTTPLIAIYQCSQDAYDLFDKVVVLYEGYQIFFGKATKAKEYFEKMGWKCPQRQTTADFLTSLTNPAEREPLPGYEDKVPRTAQEFETYWKNSPEYAELTKEIDEYFVECERSNTRETYRESHVAKQSNNTRPASPYTVSFFMQVRYGVARNFLRMKGDPSIPIFSVFGQLVMGLILSSVFYNLSQTTGSFYYRGAAMFFAVLFNAFSSLLEIMSLFEARPIVEKHKKYALYRPSADALASIISELPVKLAMSMSFNFVFYFMVNFRRNPGRFFFYWLMCIWCTFVMSHLFRSIGAVSTSISGAMTPATVLLLAMVIYTGFVIPTPSMLGWSRWINYINPVGYVFESLMVNEFHGREFQCAQYVPSGPGYENISRSNQVCTAVGSVPGNEMVSGTNYLAGAYQYYNSHKWRNLGITIGFAVFFLAIYIALTEFNKGAMQKGEIVLFLKGSLKKHKRKTAASNKGDIEAGPVAGKLDYQDEAEAVNNEKFTEKGSTGSVDFPENREIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDRLLFLQKGGRTAYFGELGENCQTMINYFEKYGADPCPKEANPAEWMLQVVGAAPGSHAKQDYFEVWRNSSEYQAVREEINRMEAELSKLPRDNDPEALLKYAAPLWKQYLLVSWRTIVQDWRSPGYIYSKIFLVVSAALFNGFSFFKAKNNMQGLQNQMFSVFMFFIPFNTLVQQMLPYFVKQRDVYEVREAPSRTFSWFAFIAGQITSEIPYQVAVGTIAFFCWYYPLGLYNNATPTDSVNPRGVLMWMLVTAFYVYTATMGQLCMSFSELADNAANLATLLFTMCLNFCGVLAGPDVLPGFWIFMYRCNPFTYLVQAMLSTGLANTFVKCAEREYVSVKPPNGESCSTYLDPYIKFAGGYFETRNDGSCAFCQMSSTNTFLKSVNSLYSERWRNFGIFIAFIAINIILTVIFYWLARVPKGNREKKNKK
Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including anisomycin, cycloheximide, fluconazole, miconazole, ketoconazole, itriconazole, nystatin, terbinafine, amorolfine, brefeldin A, amphotericin B, fluphenazine, as well as estrogen. Plays a role in farnesol-induced apoptotic process through glutathione efflux activity. Mediates in-to-out translocation of membrane phospholipids including aminophospholipids and thus regulates asymmetric distribution of phosphatidylethanolamine. Exhibits nucleoside triphosphatase activity.
Q5ANA3
G5EFW7
IF122_CAEEL
Abnormal dauer formation protein 10
Caenorhabditis
MRPNLLWVDKILDENNEAGVCIYDLAFKPDGSELLLAADNKVYLFDVNEGGQMQTLKGHKDLVYTVAWSHNGELFASGGADKLVILWNEKHEGTLRYSHTDVIQCMMFNPCNQILLTCALNEFGLWSTADKNVIKQRSVVRCCSCAWNTDGTIFAIGHGDGTITLRKGTNATEEPSIIIQRDNEPIWGIAFSSNRTFASRDSQGNPMGIDEIMAVIDWNKTLSFYSLDGTFIESKNLEFEPHCISYCLNGEYLLIGGSDKILKIYTRKGVLLGTVAQMDHWIWSVTVRPNSQTVAMGCVDGTIACYNLVFSTVHCVDHARYANRKSMTDVFVQNLEYRTSSNICCHDLVKKMSLYDTKLAVQLSDKIQIYKQTGGVSKNERRKQLKYTLQDTIRKDLSFSLMVVTHGHLVVCNDEKLECYDFKGIKKRSWNMKSIVRYLRVLGGPAHRETLVLGTTDGGVYKVFIDNDYPILLDSRKTAIKCIDINANRTVLASIEDTLVCKWSDIATGETLLQEPGCYSVVFNTVNENLFAFTTNNMLHVRTLAAPGHTTRGVGYVLGFVKNRTFCLVQYNLIPLEVPYTIHLYQYIERGDFKEALRIACLGVVKNDWKYLANKALDALEFDVARKAYKRVRDRKMLRMVWELKKMKSNGEPDAILRATILAYTKKFREAAKIFKENGFENRAMELFTDMRMFDDVQEVMTTASGETKKMLMRKRASWARDANQPKIAAEMLISSGDLDKAALLIIDNDWLELAIEISHKIDRSDLETMKKLSAYFIRKHEFGLASRIFQSINDMKSIVDMHVNAGHWTDAFAIADRHPKYVEDVYLPYARFLAERDRFEEAQKAFHRAGKEQEAMHVLEQLTSNSVNENRFADAGFYYWLLSQQYLDRSQTEENLTLLNKAKEAASLADAYYAYYPVFIFCSQPFSFERNENILNMARYLTFTPYIDNISKVFVYFTIAKIANEMGAYKSARTALDQLTNLRVLPQFELDGQIEVMTLNIRAKPFTDVESMQPMCYRCGLNNPLLGGMSCIHCETPFIISFVSFDILPLIEFKIENDISFDEAKELIESEPPLSDDDYNPLRGLKKGIKEIILNRESLSKLEQGHVIIQTFPPPLAPKFLFNVMPSITIAQCKGCNKVFDLDDFEMACLRKGHCPFCRTSYDRNEAFFVDEEEDEDNTNIPSFGQFSRFS
Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs) . Plays a role in chemotaxis and sensory perception . Required for entry into and exit from the dauer larval stage and this may be mediated by daf-12, daf-16 and daf-41 . Controls the behavioral response, namely the avoidance response, and pathogen-responsive gene expression in the response to pathogenic bacteria such as E.coli and P. aeruginosa .
G5EFW7
B7GJ99
TRUA_ANOFW
tRNA-uridine isomerase I
Anoxybacillus
MRRIKCTIAYDGTNFAGYQIQQQKRTVQGELERALSIIHKGQFVRVYASGRTDATVHAYGQVIHFDTPLTIPDERWPKALNALLPDDVIVKEASEVPSSFHARFSVKKKEYRYRVWIGEKNVFLRHYVYHHPYDVSVPAMNEALRYLIGTHDFTSFCSAKTEVDDKVRTIYEAEVVQEGEELIFRLVGNGFLYNMVRIIVGTVLEVGRGERCAEEIKTILEQKNRSVAGKTAPGHGLYLWHVSYDN
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
B7GJ99
B1YIM4
TRMD_EXIS2
null
Exiguobacterium
MNITVLTLFPEMFTALNHSIVARAQEEKRIELNYVNFRDYSTNRHGRVDDSPYGGGAGMLLMPQPIFDAIADLPEAKRRIIALTPTGRRFDQRLAEEWSKETDLVFLCGHYEGFDQRVHDELVTDEVSLGDFVLTGGELAAMTMIDATVRLLPDVLGKAASHEDDSFSTGLLEYPHYTRPADFRGLTVPEVLLSGNHARIETWRREQALRRTLERRPDLLETADLSETDRRYLQSISGLSND
Specifically methylates guanosine-37 in various tRNAs.
B1YIM4
A6L8D1
NADD_PARD8
Nicotinate mononucleotide adenylyltransferase
Parabacteroides
MGLKTGIYSGSFNPIHIGHLALANWLCEFEGLDEVWFVVTPHNPLKKKDDLLDDSLRLEMAQAAIDGYPKFRVCDIEFYLPKPSYSIDTLRTLSRNYPNRDFYFIMGADNWQLFPRWKEHEKILQDYKLLIYPRLGFDISIPAIYPNVKKVDAPLMEISSTFIRNAYQADKDIRFFLPEGVRPYYYKI
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
A6L8D1
Q8EFG1
APT_SHEON
Adenine phosphoribosyltransferase
Shewanella
MAMNTETLSLIKQSIKTIPNYPKEGILFRDVTSLLENATAYKATIDLLVEHYRSKGFTKIVGTEARGFLFGAPLALGLGIGFVPVRKPGKLPRATISQSYELEYGHDSLEIHTDAITANDKVLVVDDLLATGGTIEATVKLIRQLGGEVQDAAFVISLPDLGGEARLTALGLELVKLCEFEGE
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Q8EFG1
C3MC58
RECR_SINFN
Recombination protein RecR
Sinorhizobium
MAKRVTGPEIEKLIQLLAKVPGLGPRSARRAALHLVKKKEQLLGPLAEAMGEAHRKVKICSCCGNVDTIDPCTVCTDERRDRSVIIVVEDVADLWALERAAALNAAYHVLGGTLSPLDGIGPDDLNIKGLVDRVAKGGVRELVIAVNATVEGQTTAHYITDQLEGMEVKITRLAHGVPVGGELDYLDEGTLTAALRARTTI
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.
C3MC58
C5CJ68
HPRK_VARPS
HPr(Ser) kinase/phosphorylase
Variovorax
MKPTVISADAMFEEFRGSLRWEWLAGLGASERQFDPEVISRAQSAADLVGYLNYIHPYRVQILGAREVAYLTRGSQEDCARRIARIVTLEPPMLVLADGQAAPDELLSICERAQLPLFATRESSAFVIDLLRAYLSKHFAERTSMHGVFMDILGMGVMITGESGLGKSELGLELISRGNGLVADDAVDLFRINQNTIEGRCPDLLLNLLEVRGIGLLDIRAIFGETAVRRKMRLKLIVHLVRRDSFERDYERMPSAPLTQDVLGIPVRKVIIQVVAGRNIAVLVEAAVRNSILQLRGIDTYADFVARHHKAMESGRDGD
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
C5CJ68
P40176
VDH_STRFR
Valine dehydrogenase
Streptomyces
MTDASHPTAADDLGALSTLFRSEQGGHERVLLCQDRESGLKAVIALHSTALGPALGGTRFHAYASDEEAVLDALNLARGMSYKNALAGLPHGGGKAVIIGSPAPVSEGGLKSEALLRAYGRFVASLDGRYVTACDVGTYVADMDVVARECRWTTGRSPENGGAGDSSVLTAFGVFQGMRASAQALWGEPTLRGRTVGVAGVGKVGHHLVDHLVEDGARVVVTDVRPESVERVRARHPRVVAVPDTESLIRADLDVYAPCALGGALNDDTVPALTARVVCGAANNQLAHPGVEKDLAGRGILYAPDYVVNAGGVIQVADELLGFDFDRAKAKAAQIFDTTLAIFDRARTDGVPPAVAADRIAEQRMAEARTV
Oxidative deamination of branched-chain amino acids. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors.
P40176
Q63553
SNRK_RAT
SNF1-related kinase
Rattus
MAGFKRGYDGKIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYNIPLVSYKNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAERILREKQEKEIQTRSASPSNIKAQFRQSWPTKIDVPQDLEDDLTATPLSHATVPQSPARAGDSVLNGHRSKGLCDPAKKDELPELAGPALSTVPPASLKPAASGRKCLFRVEEDEEEDEEDKKPVSLSTQVVLRRKPSVTNRLTSRKSAPVLNQIFEEGESDDEFDMDENLPPKLSRLKMNIASPGTVHKRYHRRKSQGRGSSCSSSETSDDDSESRRRLDKDSGLAYSWHRRDSSEGPPGSEGDGGGQSKPSGGGGVDKASPGEQGTGGSGQGGSGGTPSGTAGSSRRCAGPDSSSSSPASAAPRGAELVQSLKLVSLCLGSQLHGAKYILDPQKALLSSVKVQERSTWKMCISAPGPGPSADLDPVRTKKLRNNVLQLPLCEKTISVNIQRSRKEGLLCASSPASCCHVI
May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.
Q63553
B7MBE3
DGTP_ECO45
Deoxyguanosinetriphosphate triphosphohydrolase
Escherichia
MAQIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKTQVFPLERNAAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDELTGPFESIVEMSCLMHDIGNPPFGHFGEAAINDWFRQRLYPEDAESQPLTDDRCSVAALRLRDGEEPLNALRRKIRQDLCHFEGNAQGIRLVHTLMRMNLTWAQVGGILKYTRPAWWRGETPETHHYLMKKPGYYLSEEAYIARLRKELNLALYSRFPLTWIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWGQHEKGSLFSLVVENAWEKSRSNSLSRSTEDQFFMYLRVNTLNKLVPYAAQRFIDNLPAIFAGTFNHALLEDASECSDLLKLYKNVAVKHVFSHPDVEQLELQGYRVISGLLEIYRPLLNLPLSDFTELVEKERVKRFPIETRLFHKLSTRHRLAYVEAVSKLPSDSPEFPLWEYYYRCRLLQDYISGMTDLYAWDEYRRLMAVEQ
dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.
B7MBE3
B3QXJ5
RL19_CHLT3
50S ribosomal protein L19
Chloroherpeton
MNEKIKLVEAAQMRADIPEIHPGDTLKVHVKVVEGDKERLQLFQGILISIRGVGMSKTITVRKISHGVGVERIIPLHSPIIEKIEVVKRGKVRRAKLFYMRNRTGKAAMKIKEKTTNSEMA
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.
B3QXJ5
P53944
MTQ1_YEAST
Mitochondrial MRF1 N(5)-glutamine methyltransferase MTQ1
Saccharomyces
MPRISTSLIRKASRIRPGLHLLLPECRTLEQAKLEYKWLTEELPPDKSIRWACLQRYKHVPLQYILRSQPFGALDIVCKPGVLIPRWETEEWVMAIIRALNNSMLSRHTIPLHICDTFTGTGCIALALSHGIANCTFTAIDVSTRAIKLVKENMLKNKVSGGKLVQHNILSSKASDEYPSHIDILTGNPPYIRKRDFNRDVKTSVKLFEPRLALVGELECYINLVNYWLPKTDSFFYEIGDVEQFNYVERRIKEDSYLSRIWSIGLKYDSNGKARVVYGFKATPKGRILHQIFASFGTIRHLATALSGHKANCN
Methylates MRF1 on 'Gln-287' using S-adenosyl L-methionine as methyl donor.
P53944
Q0SQN0
ISPF_CLOPS
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Clostridium
MRIGMGYDVHKLVENRDLILGGVKIPYEKGLLGHSDADVLLHAIMDSLLGAAALGDIGKYFPDTDPKYKGADSIKLLEFVGELLNKNNYKISNIDATIIAQRPKMAPHIPTMRENIAKALNIDLDKINVKATTEEGLGFTGTGEGISSQSICLLIK
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q0SQN0
Q2LR05
ATPB_SYNAS
F-ATPase subunit beta
Syntrophus
MNIGRIVQVIGPVIDVVFEEGQLPAILNAITITNPVINDEEDNLIVEVAQHLGDNNVRCIAMDVTDGLVRGMPAKDTGAPITVPVGKECLGRILNVVGKPVDGLGPIEAKNTMPIHREAPSFLEQDTSVHVLETGVKVIDLLVPFPRGGKMGLFGGAGCGKTVVMMEMIHNIAMHHGGISVFAGVGERTREGNDLYREMLESGVIKQAALIYGQMTEPPGARARVSLTALAAAEYFRDVEGQDVLLFVDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATDLGELQERITSTDKGSITAVQCVYVPADDLTDPAPATTFAHLDGTVVLSRPIAELGIYPAVDPLDSTSRILDPIVLGEEHYKVARAVQVTLQKYKDLQDIIAILGMDELSEEDKLTVNRARKIQRFLSQPFFVAAQFTGVDGKFVSVPDTVRGFKEILEGKYDDLPEQAFYMVGGIEEAVEKAKKYQEQ
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Q2LR05
P23291
KC11_YEAST
Casein kinase I homolog 1
Saccharomyces
MSMPIASTTLAVNNLTNINGNANFNVQANKQLHHQAVDSPARSSMTATTAANSNSNSSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGVPVAIKFEPRKTEAPQLRDEYKTYKILNGTPNIPYAYYFGQEGLHNILVIDLLGPSLEDLFDWCGRKFSVKTVVQVAVQMITLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANNIHLIDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDMEALGHVFFYFLRGHLPWQGLKAPNNKQKYEKIGEKKRSTNVYDLAQGLPVQFGRYLEIVRSLSFEECPDYEGYRKLLLSVLDDLGETADGQYDWMKLNDGRGWDLNINKKPNLHGYGHPNPPNEKSRKHRNKQLQMQQLQMQQLQQQQQQQQYAQKTEADMRNSQYKPKLDPTSYEAYQHQTQQKYLQEQQKRQQQQKLQEQQLQEQQLQQQQQQQQQLRATGQPPSQPQAQTQSQQFGARYQPQQQPSAALRTPEQHPNDDNSSLAASHKGFFQKLGCC
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
P23291
Q9SWX9
ILL5_ARATH
IAA-amino acid hydrolase ILR1-like 5
Arabidopsis
MSFCKLVSFVLILHLLNSCLISCSSNDLSQIPKNFLSLAKREDFFDWMVGIRRRIHENPELGYEEVETSKLVKTELDKMGVSYKNPVAVTGVIGYVGTGHAPFVALRADMDALPIQEMVEWEHKSKIPGKMHACGHDAHTTMLLGAAKLLKEHQEELQGTVILVFQPAEEGGAGAKKIVEAGVLENVGAIFGLHVSNLLGLGQLSSREGLLMAGSGRFKATISGKGGHAALPQFAIDPVLAASNVILSLQHLVSREADPLDSQVVTVATFEGSDAFNVIPDSVTIGGTFRALLPKSFEQLKQRIVQVITTQASVNMCNATVDFLEDETPPFPPTVNNKTLHLFYKNVSVDMLGIENYVETLPVMVSEDFAFYQQAIPGHFSFVGMQNKSHSPMANPHSPFFEVNEELLPYGASLLASLATRYLLDSSSSPNKDEL
Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA).
Q9SWX9
Q9BQI0
AIF1L_HUMAN
Ionized calcium-binding adapter molecule 2
Homo
MSGELSNRFQGGKAFGLLKARQERRLAEINREFLCDQKYSDEENLPEKLTAFKEKYMEFDLNNEGEIDLMSLKRMMEKLGVPKTHLEMKKMISEVTGGVSDTISYRDFVNMMLGKRSAVLKLVMMFEGKANESSPKPVGPPPERDIASLP
Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function.
Q9BQI0
A0A3B6KF13
BZP1A_WHEAT
bZIP transcription factor 1-A
Triticum
MGSSEAETPAKANKASAPQEQQPPATSSIATPTVYPDWTSFQGYPPIPPHGFFPSPVVSNPQGHPYMWGPQPMMPPYGTPPYVIYPPGGIYAHPSMRPGAHPFAPYTMTSPNGNPDAAGTTTTAATAGGETNGKSSEGKEKSPIKRSKGSLGSLNMITGKNCVEHGKTSGASVNGTISQSGESGSESSSEGSEANSQNDSQHKESGQEQDGDVRSSQNGVSPSPSQAQLKQTLAIMQMPSSGPVPGPTTNLNIGMDYWANTASSSPALHGKVTPTAIPGAVAPTEPWMQDERELKRQKRKQSNRDSARRSRLRKQAECEELAQRAEVLKQENASLKDEVSRIRKEYDELLSKNSSLKDNVGDKQHKTDEAGLDNKLQHSGDDSQKDTN
Probable transcription factor that may be involved in responses to fungal pathogen infection and abiotic stresses.
A0A3B6KF13
B5Y1U1
LPXC_KLEP3
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Klebsiella
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIIVEVDAPEIPIMDGSAAPFVYLLLDAGINELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDASTQRYTLNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFEDDAKLPMAFRAPSMVLA
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
B5Y1U1
P39104
PIK1_YEAST
Phosphatidylinositol 4-kinase PIK1
Saccharomyces
MHKASSSKKSFDDTIELKKNEQLLKLINSSEFTLHNCVELLCKHSENIGIHYYLCQKLATFPHSELQFYIPQLVQVLVTMETESMALEDLLLRLRAENPHFALLTFWQLQALLTDLSTDPASYGFQVARRVLNNLQTNLFNTSSGSDKNVKIHENVAPALVLSSMIMSAIAFPQLSEVTKPLVESQGRRQKAFVFKLARSAMKDFTKNMTLKNTLLNKKTSRSKRVSSNRSSTPTSPIDLIDPIKTKEDASFRKSRHSEVKLDFDIVDDIGNQVFEERISSSIKLPKRKPKYLDNSYVHRTYDGKNINRDGSISNTAKALDGNKGDYISPKGRNDENNEIGNNEDETGGETEEDADALNSDHFTSSMPDLHNIQPRTSSASSASLEGTPKLNRTNSQPLSRQAFKNSKKANSSLSQEIDLSQLSTTSKIKMLKANYFRCETQFAIALETISQRLARVPTEARLSALRAELFLLNRDLPAEVDIPTLLPPNKKGKLHKLVTITANEAQVLNSAEKVPYLLLIEYLRDEFDFDPTSETNERLLKKISGNQGGLIFDLNYMNRKENNENRNESTLTSNNTRSSVYDSNSFNNGASRNEGLSSTSRSDSASTAHVRTEVNKEEDLGDMSMVKVRNRTDDEAYRNALVIQSAANVPILPDDSQDRSPELNFGSNLDEVLIENGINSKNIHSQTDALADQMRVSAVMLAQLDKSPQQLSESTKQIRAQIISSMKEVQDKFGYHDLEALHGMAGERKLENDLMTGGIDTSYLGEDWATKKERIRKTSEYGHFENWDLCSVIAKTGDDLRQEAFAYQMIQAMANIWVKEKVDVWVKRMKILITSANTGLVETITNAMSVHSIKKALTKKMIEDAELDDKGGIASLNDHFLRAFGNPNGFKYRRAQDNFASSLAAYSVICYLLQVKDRHNGNIMIDNEGHVSHIDFGFMLSNSPGSVGFEAAPFKLTYEYIELLGGVEGEAFKKFVELTKSSFKALRKYADQIVSMCEIMQKDNMQPCFDAGEQTSVQLRQRFQLDLSEKEVDDFVENFLIGKSLGSIYTRIYDQFQLITQGIYS
Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate . PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton . Involved in the response to mating pheromone .
P39104
Q9KQ06
CHER1_VIBCH
Chemotaxis protein methyltransferase 1
Vibrio
MTAITISDQEYRDFCRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLSSLSDLLRDVVTGRNRDLRVAAVDAMTTNETLWFRDSYPFTVLADKLLPEMAANKRPIKIWSAASSSGQEPYSMAMTILEVQQKRPGLLPSVSITATDISASMLDMCRAGIYDNLALGRGLSPERRRVFFEDAGDGRMKVKDNVKRLVNFRPQNLMESYSLLGKFDIIFCRNVLIYFSPDMKSKVLNQMAASLNPGGYLLLGASESLTGLTDKFEMVRCNPGIIYKLK
Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Q9KQ06
D3UMA1
CBIM_LISSS
Energy-coupling factor transporter probable substrate-capture protein CbiM
Listeria
MKKLWKFIPFVLMGVIYFTLTNPESAHAMHIMEGFLPVKWAVFWLIVFIPFLVLGLIRIRKLIAIDKNNKLLLALCAAFIFVLSALKIPSVTGSCSHPTGVGLATVMFGPLVVSVLGVIVLLFQALLLAHGGITTLGANAMSMAVIGPMVGFVVYKLARKLNCNKSVSIFLCAMTADLATYFTTSVQLGVVFPDPASGMMASILKFMAIFCVTQVPIAIAEGLLTVVMYNLISKNLPEKVAQLR
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
D3UMA1
P43703
PARE_HAEIN
Topoisomerase IV subunit B
Haemophilus
MTTNYSAQEITVLKDLEPVQIRPGMYTDTTRPNHLAQEVIDNSVDEALAGFATKIEVILHPDQSIEVTDNGRGMPVDIHPTEGVSGVEVILTKLHAGGKFSNKNYEFAGGLHGVGISVVNALSERVDIQVKRNGEIYKIAFENGSKVEELEIIGTCGRRTTGTIVHFKPNPKYFDSAKFSVSRLRHLLRAKAVLCSGLEIKFIDKVNNTQDIWLYEDGLSDYLIEAVNGFETLPKKPFVGEFKGANEAVSWALLWLPEGGELIGESYVNLIPTIQGGTHVNGLRQGLLDAIREFCEFRNLLPRGVKLTADDIWDRCSYILSLKMQDAQFAGQTKERLSSRQSAVFVSGVLKDAFSLWLNQNVQDAEKLAEIAISSAQRRLRAAKKVVRKKLVSGPALPGKLADCGSQDLEKTELFLVEGDSAGGSAKQARDREYQAILPLRGKILNTWEVSPDQVLGSTEIHDIAVALGIDPDSNDLSQLRYGKVCILADADSDGLHIATLLCALFLRHFPKLVQDGHVYVAMPPLYRIDLNKEVFYALDENEKEAILDRLKNKKGKPNVQRFKGLGEMNPSQLRETTMDPNTRRLVQLTYDLGEDQGSDTLELMDMLLAKKRSEDRKNWLQAKGDQVDLSV
Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
P43703
P18182
HRDA_STRCO
RNA polymerase principal sigma factor HrdA
Streptomyces albidoflavus group
MRGGQRRASRLRPPTYRRRPPPAASILEVAPVQTQTLTQTDTAAGGAEPDAERGVLLAMPAQPGAGAALPHPGAPVDVPEHPEPPPPTRTESGGPSSDLFRQYLREIGRIPLLSAAEEVDLARRVEAGLFAEEKLRCSPGLDDRLALDLDRLVVLGRLAKRRLIEANLRLVVSVAKRYVGRGLTMLDLVQEGNLGLIRAVEKFDYARGYKFSTYATWWIRQAMSRALADQARTIRVPVHVVELINRVVRVQRRMLQERGCEPTPQEVAAHLDLAPERVGEVLRLAQEPVSLHAPVGEEDDVALGDLIEDGDAASPVESAAFLLLRQHLEAVLSTLGERERKVVQLRYGLADGRPRTLEEIGRLFGVTRERIRQIESKTLSKLRDHAYADQLRGYLD
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
P18182
Q321Y0
RSMF_SHIBS
rRNA (cytosine-C(5)-)-methyltransferase RsmF
Shigella
MAQHTVYFPDAFLTQMREAMPSTLSFDDFLAACQRPLRRSIRVNTLKISVADFLQLTAPYGWTLTPIPWCEEGFWIERDNEDALPLGSTAEHLSGLFYIQEASSMLPVAALFADGNAPQRVMDVAAAPGSKTTQIAARMNNEGAILANEFSASRVKVLHANISRCGISNVALTHFDGRVFGAAVPEMFDAILLDAPCSGEGVVRKDPDALKNWSPESNQEIAATQRELIDSAFHALRPGGTLVYSTCTLNQEENEAVCLWLKETYPDAVEFLPLGDLFPGANKALTEEGFLHVFPQIYDCEGFFVARLRKTQAIPALPAPKYKVGNFPFSPVKDREAGQIRQAAAGVGLNWDENLRLWQRDKELWLFPVDIEALIGKVRFSRLGIKLAETHNKGYRWQHEAVIALATPDNVNAFELTPQEAEEWYRGRDVYPQAAPVADDVLVTFQHQPIGLAKRIGSRLKNSYPRELVRDGKLFTGNA
Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
Q321Y0
A8MKJ7
RL9_ALKOO
50S ribosomal protein L9
Alkaliphilus
MKVILLQDVKGLGKKGEVVNASDGYARNFLFPKKLAAEATQGNVKTLNEQKTSQELKKQQEVEEAKELAKKIENSPIEIIAKAGDGGRLFGSVTSKDLAETLEKQHHIKIDKRKITLPEPIRELGVRHVEIKLHVGVVGKLTVNIKEA
Binds to the 23S rRNA.
A8MKJ7
Q0JKI9
ARFB_ORYSJ
OsETTIN2
Oryza sativa
MVGIDLNTVEEEEDEEEGGATGTVTAPAEARAGGAVCLELWHACAGPVAPLPRKGSAVVYLPQGHLEHLGAAPGSGPGAAVPPHVFCRVVDVSLHADAATDEVYAQVSLVADNEEVERRMREGEDGAACDGEGEDAVKRPARIPHMFCKTLTASDTSTHGGFSVPRRAAEDCFPPLDYSLQRPFQELVAKDLHGTEWRFRHIYRGQPRRHLLTTGWSGFINKKKLVSGDAVLFLRGEDGELRLGVRRAAQLKNASPFPALHNQISNTSSLSEVAHAVAVKSIFHIYYNPRLSQSEFIIPYWKFMRSFSQPFSVGMRFKLRYESEDASERRRTGIIIGSREADPMWHGSKWKCLVVKWDDDVECRRPNGVSPWEIELSGSVSGSHLSTPHSKRLKSCFPQVNPDIVLPNGSVSSDFAESARFHKVLQGQELLGLKTRDGTVNTASQATEARNFQYTDERSCSINMSNNILGVPRLGVKTPSGNPGFSYHCSGFGESQRFQEVLQGQEVFRPYRGGTLSDACIRGSGFRQPDGNHAPGAAFKWLAPQGCDHHGITTSVLPQASSPSSVLMFPQTSSKMPGLEYIYGCLDRNENSRHFKIGPTQDMTRTDQTLRLWPHLISGKVLDECTRNEKLHSPVSGAEHESNNKCLNTNGCKIFGISLTEKAQAGDEVDCGNASYHSRLQSLKPQMPKSLGSSCATVHEQRPVVGRVVDISAVNTMI
Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Q0JKI9
Q5F9N1
DCUP_NEIG1
Uroporphyrinogen decarboxylase
Neisseria
MTLLKNDTFLRALLKQPVEYTPIWMMRQAGRYLPEYKATRTKAGSFLDLCKNTGLATEVTIQPLERFDLDAAILFSDILTVPDAMGLGLYFAEGEGPKFKRALQHESDIAKLHVPDMEKLQYVFDAVTSIRKALDGRVPLIGFSGSPFTLACYMVEGGGSKEFRTIKTMMYSRPDLLYKILDTNAQAVTAYLNAQIDAGAQAVQIFDTWGGVLSDAAFKEFSLKYIRQIVAGLKRESEGRRVPVIVFAKGGGLWLESMAQIGADALGLDWTCNIGEARRRVGNQVALQGNFDPSALFGTPESIRTEVARILTGYGHGSGHVFNLGHGINQHADPEHAKILVDTVHELSRQYHGG
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Q5F9N1
Q8DCF5
OTC_VIBVU
Ornithine carbamoyltransferase
Vibrio
MAFNLRNRNFLKLLDFSTKEIQFLIDLSADLKKAKYAGTEQKKLLGKNIALIFEKASTRTRCAFEVAAFDQGAQVTYIGPSGSQIGDKESMKDTARVLGRMYDGIQYRGFGQAIVEELGAFAGVPVWNGLTDEFHPTQILADFLTMLEHSQGKALADIQFAYLGDARNNVGNSLMVGAAKMGMDIRLVGPQAYWPDEELVAACQAIAKQTGGKITLTENVAEGVQGCDFLYTDVWVSMGESPEAWDERVALMKPYQVNMNVLKQTGNPNVKFMHCLPAFHNDETTIGKQVADKFGMKGLEVTEEVFESEHSIVFDEAENRMHTIKAVMVATLGS
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q8DCF5
P14141
CAH3_RAT
Carbonic anhydrase III
Rattus
MAKEWGYASHNGPEHWHELYPIAKGDNQSPIELHTKDIRHDPSLQPWSVSYDPGSAKTILNNGKTCRVVFDDTFDRSMLRGGPLSGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFGEALKQPDGIAVVGIFLKIGREKGEFQILLDALDKIKTKGKEAPFNHFDPSCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLFASAENEPPVPLVGNWRPPQPIKGRVVRASFK
Reversible hydration of carbon dioxide.
P14141
A0QL13
RL22_MYCA1
50S ribosomal protein L22
Mycobacterium avium complex (MAC)
MTTTEFPSAVAKARFVRVSPRKARRVIDLVRGRSVTDALDILRWAPQAASEPVAKVIASAAANAQNNNGLDPATLVVATVYADEGPTAKRIRPRAQGRAFRIRKRTSHITVVVESRPAKDQRSAKSSRTRRAEASKAAAKAPAKKAPAKKAPAKKAPAKTAAKKTPAKTSETSDAKGGSD
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.
A0QL13
A2SGT2
DNLJ_METPP
Polydeoxyribonucleotide synthase [NAD(+)]
Methylibium
MSDRAEDPAARAAQLREQLEYHAHRYYVLDAPEIPDAEYDRLFTELQALEAAHPGLRTPDSPTQRVIGAVLEGLSAVRHAVPMLSIKTETDTTPTGALKFDAAVRNALKLPPDAPPLRYAAELKFDGLAINLRYQAGRLVQAATRGDGETGEDVTHTVGTIESVPKQLRGITAPVLEVRGEVFMRRDDFEALNERQREAGLKTFVNPRNAAAGIVRQLDASIARQRPLSFFAYGLGDVQGWDVPPTHAGLLDALAALGLPVDAHRTVVEGGEALAAFHAGIAAERDALPFDIDGVVYKVDERALQQQLGFKSREPRWAVAHKYPAQEQSTQLAGIEIQVGRTGKLTPVAKLQPVFVGGTTVSNATLHNRFELRRKGIRIGDTVIVRRAGDVIPEVVGRVPVPRTAYIPNFRMPRACPVCGSQALRERGSVDYRCSGGLFCAAQRKQALLHFAGRRMMDIEGLGDKLVEQLVDGGIIRTLPELYRLGVAKLVALERMGDKSAANLVAALEASKATTLARFLFSLGIRHIGEATAKDLARHFGALDRVMDASVEQLLEVNDVGPVVAQSLRTFFDQPHNREVVEQLRAAGVHWDEHSGEADLTPRPLAGKTFVLTGTLPSLGREAAKELIEAAGGKVAGSVSKKTDYVVAGEEAGSKLEKAQALGVAVIDEAALRALLD
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.
A2SGT2
Q6AFQ4
RS15_LEIXX
30S ribosomal protein S15
Leifsonia
MALDAETKKSIIDEYATHPGDTGSPEVQVAILTQRIRDLTEHLKEHKHDHHSRRGLLLLVGQRRRLLGYLADIDISRYRALIERLGLRR
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Q6AFQ4
A6VHE8
MTRE_METM7
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E
Methanococcus
MDPTLISLGALALAGAAATVSGCAEDLESDVGSQSNPNSQVQLGPQMGNIHRYFNKAISGEPVSYGLYVAVAGTIAWALINAGLNAVLAIIVGSGVAAIVHGAYSVSAFLGRIVGQSKKFGQPVYMDVLTSHIGPIVGHGFIAVFTMTLAAYLATTALGNPFPLPLVALIFGITVGAIGSSTGDVHYGAEREYQKYPFGGGIPVANQGDIDIYAEYGVRNGLDSSYFCSRFGGPLTGLCFGLIIFLDGWRSILGNIVGGDLVTKTSIALLVGLLVVAVAAVINRKLEVYARNKYGPYRN
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
A6VHE8
O51337
LGT_BORBU
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Borreliella
MPNYINYPSWLHPEVIQGIPITWYSLSYILIILISYKFIWYQIQSDNVDIKKEDYEIFMFSLVLGAILGGRLASTLVYDKSGIYYSNPWLILLPFDQHWNFTGFRGMAIHGGFLGAIIAPLITINTNLKNTNVQKYFLKLTDYGSIAFSSGYILGRLANFANAELYGRVMKGGIIFPNAEPFDTNIPGVKEFASSVGLEISPHDLLINLPRIPSQLIEGFFEGPVTFLLLWFLFKKIKKYDGFIFGVYVMLYAFFRFFIEYLREPDKELGFIITYKPITSLSEFSFLNISMGQILSLTLMLSGLIWIIVTKKIADKKIKNNTNLAYKN
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
O51337
B2TIR0
LEUD_CLOBB
Isopropylmalate isomerase
Clostridium
MNVKGRVFKYGDNVDTDVIIPARYLNTSNHKELASHCMEDIDKEFVNNVKDGDIIVANKNFGCGSSREHAPIAIKAAGISCVIASTFARIFYRNSINIGLPILECDEAVKNINHGDELEVDFSTGIIKNLSKNEQYQGEAFPEFMQKIIDNDGLIGYIRNK
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
B2TIR0