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 |
|---|---|---|---|---|---|---|
Q7VAW6 | OTC_PROMA | Ornithine carbamoyltransferase | Prochlorococcus | MNMNSLSVSRVLADLAGKDFISCSDFTSDQVKALLQLSSQLKNGDRRIDLGNRVLGLIFSKASTRTRVSFQVAMARLGGQTIDLSNQATQLARGEPLKDTARVLSRYCDALALRTFGNDELIEYAKWSSIPVINALTDLEHPCQALADFLTIKEAFGSLDGITLAYIGDGNNVLNSLMICGTLLGVNIQIASPKGFEPLPSIVERAKTLAHPTLKICVSNNPIDAVSGAHVIYTDVWASMGQESEQAQRKEIFEGYTVNKDLVDKAEKESIILHCLPAHRGEEITDDVLESSASRIFDQAENRLHVQQALLAALLGGL | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | Q7VAW6 |
Q5WJE6 | HTPG_ALKCK | High temperature protein G | Alkalihalobacillus | MEKKQFQAESKRLLEMMVNSIYSQKEIFLRELISNASDAIDKMYYRSLTDDSLSFEKDRYAIYVEADKDNRKLVMKDTGIGMTKEELEANLGTIAKSGSLAFKKETEIEDGHDIIGQFGVGFYAAFMVADKVTVITRSIDSDQAYKWESDGTDGYTIEPAEKEDVGTVITLHIKENTDDESYDEYLEEYRIKAIIKKYSDFIRYPIKMNVTVSKPKEDNEDEYAEYQEEQTINSMVPIWRKNKSELKDSDYEQFYQDKRYGFDKPLEHIHVSVDGAIRYNAILFIPEHTPFDYYSKEYEKGLELYANGVLIMEKCAELLPDYFSFVKGMVDSEDLSLNISREMLQHDRQLKLIAKNIKSKIKSQLKTMLKKEPDKYEKFYKAFGRQLKFGVYNDFGANKDDLQDLLLFYSSTEKKLVSLSDYVSRMKEGQTYIYYATGESNERIAKLPQTEMVADQGYEILYFTEDVDEFAIKMLRSYDEKEFMSVSSADLDIETDEKQEEETNSEENKKLFEKMKSILDGKVKDVRTSKRLKSHPVFLAADGEITLEMEKVLQAMPDNQNVKAEKVLEINPNHDVFHSLKQAYEEDEDKLKLYTNLLYNQALLIEGLPLEDPVEFSQNMCKVMV | Molecular chaperone. Has ATPase activity. | Q5WJE6 |
Q5NZH8 | GLND_AROAE | [Protein-PII]-UMP uridylyl-removing enzyme | Aromatoleum | MSTAAIPTDAAVQAAIAEARARLADGSMRIRMAYEGHPATSTVLKGRAHLVDETIHRLWRACAMPADVALLAVGGYGRGELFPCSDVDLMVLLPDTADDAMQARLSVLLGALWDVGLEIGHSARTVAEAIDAAEQDITVQTNLLESRLLEGNRPLFEEFCRRYRALLDVRVFFKAKQLEQEKRYARYNDTPYALEPNCKESPGGLRDLQMLGWIARAAGLGRNWRDLARRRLITGAEARDLRSIERFLQHVRIRLHYLTGRSEDRLLFDYQERLASALGIEATAAKRASEVFMQRYYVNAKKVTQTNTILLQNYGVEIFPRRAGAAIVINERFQAVRELLDMREDDTFARHPSALLECFLILQQRSELKGMTARTLRALWLNRKRINAAFRADPHNRELFVAILQQKRGIVHEFRRMNQYGILSGYLPSWRRIVGQMQHDLFHVYTVDQHIMMVLRNMRRFTMGEHAHEYPLMAQLIMAFDRHWLLYVAALFHDIAKGRGGDHSKLGTIDAREFCEHHHLAREDADLVVWLVEHHLTMSHVAQKEDTSDPAVIGRFADTVGTERRLTALYLLTHADIRGTSPKVWNGWKGKLLEDLFFATRRLLRGATPQEALGLDDRQENARALLRYHGLRPGVEDALWAQLDAVYFMRHSAEEIAWHSRTLYYRPDALEPVVKARVSDADQGVQVMVFTRDQKDLFVRLTGFFGRLGFSILDAKVHTTRHGYALDSFMLQDPGNAEHYRDVITLIEHELTERLKKSAPPDRPSAGRLSRQVKHFPITPRVSILPDESGRHYILSLTAADRRGLLFAVAEVLAQNGIVLHTAKIATLGERVEDTFLLSGNGLSQDARVVKIERELLQRLHI | Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | Q5NZH8 |
B6EN06 | IHFA_ALISL | Integration host factor subunit alpha | Aliivibrio | MALTKADLAETLFEKVGLSKRDAKETVEVFFEEIKQALESGEQVKLSGFGNFDLREKSERPGRNPKTGEDIPISARRVVTFKPGQKLKARVEDLPVEK | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. | B6EN06 |
Q02181 | PHEG_SYNPY | Phycoerythrin class II gamma chain, linker polypeptide | unclassified Synechococcus | MLGAETSLQALTSATRTGPAAFSTKSKAGKNTVPRTVAGAIAEYKRQHCAAMGIGIGPRLLSECPFAVTFDRYSPDSSAALERVIVAAYRQVLGNLPPTDNQRETSLEVRLMNGEITVRDFVNGLAKSDFYKDNFFHAVGAQRGIELNFKHLLGRAPLNQQEVQNHIKLQAEEGFDALIDTLTDSAEYTEVFGADIVPYDRTKDSYAGMNTRSFNLMRDLGGMKVAISDNAQGRQSKTVNALASASRESTKPQPFSYVSVTQIPVKLPQQQYTGHNVPAMSDYVPFRPFGIFF | This protein is a bile pigment-bearing rod linker polypeptide that associates with C-phycoerythrin. | Q02181 |
B8DG43 | LUXS_LISMH | Autoinducer-2 production protein LuxS | Listeria | MAEKMNVESFNLDHTKVKAPFVRLAGTKVGLHGDEIYKYDVRFKQPNKEHMEMPALHSLEHLMAELARNHTDKVVDISPMGCQTGFYMSFINFSDYDDALDVLAKTLADVLEAKEVPACNEVQCGWAASHSLEGAKELAEEFLAKRSEWKNVFGE | Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). | B8DG43 |
Q3B736 | ATGA1_DANRE | Autophagy-related protein 101 | Danio | MNCRSEVLEVSVEGRQVDEAMLGLLHTILLHRSTGKFHYKKEGTYSIGTVGTQDVDCDFIDFTFVRVSSDELDRVIRKAVAEFKDALGNSGSDGMGQISLEFYQKKKSRWPFSDECIPWEVWSIKVNVVNLANEQERQICREKVGEKLGEKVINIVEVINRHEYLPKMPTQSEVDNVFDTSLKDVQPYLYKITYQITDSLGTSVSTTMRRLIKDTLAL | Autophagy factor required for autophagosome formation. | Q3B736 |
Q746H2 | PARB_THET2 | Probable plasmid-partitioning protein ParB | Thermus | MSRLDEVLGTAILKGKKALGKEAPEVLRLPLDLLRVRGQPRRRFENLEALAESIREKGILQPLLVRRVGEAYEVVAGERRLRAAAMAGLKEVPARVLDLSEKEARLLALVENLQREDLNPYEETLGVLALLSEDLGKSVEEVVGLLRKMKNAKEGRVRDNVVPTAEAQRVEELFKALGRMSWESFVQHRLPLLSLPEDLKAALEEGAIPYTAALELKKVKDASLRKALLEEVKAGLSLRELKARVRGVLRKEKAPRPWPKEVAAKLARLDLEALPPERRARVEELLAELERVLEGPR | Probably involved in plasmid DNA partitioning. | Q746H2 |
Q3SJE0 | DAPE_THIDA | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Thiobacillus | MANETLEDAVLASETLALAVELLKRRSVTPDDAGCHDLIAARLQALGFHIERHRHNDVDNLWARRGTASPVVCFAGHTDVVPPGPLEQWLSDPFEPTLRDGKLYARGAADMKTSDAAFVTATERFLARRPDHPGSIAFLLTSDEEGPATDGTVRVVEALKARGELLDYCIVGEPTSAAEFGDTIKNGRRGSLSGTLRVKGVQGHIAYPHLAKNPIHLAAPAIAELAETMWDEGNSYFPPTTWQISNIHAGTGVTNVIPGMVEIQFNFRFSTASTAEGLMDAVNEILDSHGLDYEIDWNLSGKPFLTPRGALCDRLSEAVHEVTGLTPELSTTGGTSDGRFIADICREVVEFGPLNMSIHKLNEHVALENVEQLAAVYEKALEKLLGESDERV | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | Q3SJE0 |
B2GJ18 | RS13_KOCRD | 30S ribosomal protein S13 | Kocuria | MARLAGVDLPREKRLEVALTYIYGVGRTRALETLEATGISGDVRVKDLTDPQLVELRDYIEGNYKVEGDLRREVAADIRRKVEIGSYQGLRHRRGLPVHGQRTKTNARTRKGPKRTVAGKKK | 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. | B2GJ18 |
P07135 | RR7_SOYBN | 30S ribosomal protein S7, chloroplastic | Glycine subgen. Soja | MSRRGTAEEKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAMKKIQQKTETNPLSVLRQAIRGVTPDIAVKARRVGGSTHQVPVEIGSTQGKALAIRWLLGASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. | P07135 |
Q89AD0 | ENGB_BUCBP | Probable GTP-binding protein EngB | Buchnera | MYLVDTIDYQKICCIIKTFEDNILFQKNYHSTWFLKSIANIQKEKYNYGLEVAFVGYSNSGKSSIINALTNQKKLAKISRTPGRTRLINIFSVTSEIRLVDFPGYGYAQVSRSISKKWKEMIFQYLNIQKCLQGLVIITDIRCPIKEIDELVINLAVSLNIPILLLLNKMDKVTRSIQKSKLFSTREKMLNFSNNINVELFSSFKKIGIHKLQFVLNNWFSSDKKLCQ | Necessary for normal cell division and for the maintenance of normal septation. | Q89AD0 |
Q6NZQ8 | MARH1_MOUSE | RING-type E3 ubiquitin transferase MARCHF1 | Mus | MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAVTCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTANKLEKNFPCNVNTEIKDAVVVPVPQTGSNTLPTAEGAPPEVIPV | E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system. | Q6NZQ8 |
B8F3D3 | GMHA_GLAP5 | Sedoheptulose 7-phosphate isomerase | Glaesserella | MYQQQILIELQEAQQVLNDFINDQHNLKLIQEAALLITDSFKNGGKILSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDPSHLSCVSNDFGYEYVFSRYVEAIGQKGDILFCLSTSGNSKNVINAIIAAKAKGMKIIAMTGKDGGKIAELADIEIRVPHFRYADRIQEIHIKVIHILMMLIEFEMAK | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. | B8F3D3 |
Q21IX0 | HTPG_SACD2 | High temperature protein G | Saccharophagus | MTAEATVETRGFETEAKQLLHLMIHSLYSNKEIFLRELVSNASDAADKLRFEALKQPELLEQDSELKITIDFDKEAKTLSITDNGIGMNRDEVIANLGTIARSGTAQFMANLSGDQKKDSQLIGQFGVGFYSAFIVADKVEVLTRRAGSEPSEGVRWVSEGEAEYSIENIEKAARGTTIILHLKKDQEEFADGWRLRSIIKKYSDHISLPVEMPKEAAPGEDKEEKAEVEYEVINTAKALWARSRSDVTDEEYKEFYKHVSHDYTDPLSWSHNRVEGKLDYTSLIYIPSKAPFDMYNREKPRGVKLYVQRTFIMDDAEQFLPLYLRFIKGVVDSNDLSLNVSREILQQDPNIDSMRSALTKRVLDMLEKMAKKEPEKYATFWKEFGEVLKEGPAEDFANKEKIAKLLRFATTHKNTNEQDQSLDAYIERMKEGQDKIYYVVAENFNTAKNSPHLEVFRKKGIEVLLLSNRIDDWLMGHLMEYDGKQFQDVGKGSLDLGKLDSEEDKKEQEKVEEAMAPFVERMKAALAEQVEEVRITHRLTESPACLVVGEHDMGAQMRRLLEAAGQAVPESKPIIEINPTHPLVQKLDQEQDEDRFKDLSHILFDQASLAEGGSLKDPAAYVSRLNKLLLELSN | Molecular chaperone. Has ATPase activity. | Q21IX0 |
A0M6M4 | MURQ_GRAFK | N-acetylmuramic acid 6-phosphate lyase | Gramella | MNKKSPDTEKVSNYDYLEKMNTFELLSNINKEDHTIAENVKKQIPSIEKLVDEIIPRIDSGGRLFYIGAGTSGRLGVLDASECPPTFGVSPGIVIGLIAGGDTALRNAVENAEDDTNQAWKDLQEYDISEKDVLVGIAASGTTPYVIGGIKDARNNGIITGCITCSSGSPLAEASEYPIEVVTGPEFVTGSTRMKAGTAQKLVLNMISTSVMIKLGRVKGNKMVDMQLSNDKLVGRGIRMIMEDLNIEKEQAEKLLLEHKSVRKVLDAHKNERN | Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. | A0M6M4 |
P69883 | CH60_STRP1 | Chaperonin-60 | Streptococcus | MAKDIKFSADARAAMVRGVDMLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVHEGLKNVTAGANPIGIRRGIETATATAVEALKAIAQPVSGKEAIAQVAAVSSRSEKVGEYISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLENPFILITDKKVSNIQDILPLLEEVLKTNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATMTALGQAAKITVDKDSTVIVEGSGSSEAIANRIALIKSQLETTTSDFDREKLQERLAKLAGGVAVIKVGAPTETALKEMKLRIEDALNATRAAVEEGIVAGGGTALITVIEKVAALELEGDDATGRNIVLRALEEPVRQIALNAGYEGSVVIDKLKNSPAGTGFNAATGEWVDMIKTGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPATPAPAMPAGMDPGMMGGF | 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. | P69883 |
B6YT50 | RNZ_THEON | tRNase Z | Thermococcus | MLEVIFLGTGGIMPNRERNVPAIALRYKGEIILFDVGEGTMRQMSTAKLSPMKVEKIFITHFHGDHYLGLAALIQTMNLWNREKPLHIYGPKYTFRFIQNFLNSGFFRPGFDIHVHEIGEVRLKFGDYEIWSFKVEHGIPALGYVFKEKDKRGKFLPEKLAEYGLSEGPILGKLEKQGQIEWNGRIIRLEDVTGPRRKGVKVVYTGDTEPCERTRLFAENADLLIHEATYLRPEDRGDSYHTTVGEACEIAKKAKVKLLALFHRAFRYTYDEYMAKARELCDVPFVIPKDFDVLTFKSGRWEMRNLLEDWQ | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. | B6YT50 |
Q0UZ59 | DBP9_PHANO | ATP-dependent RNA helicase DBP9 | Parastagonospora | MAMKRKLNEHDVPEPESPQSPKRRASDASQSEPASPPAPTPAKEVVASFAELQLEPRLLRGIRDQKWGSPTAVQSKAIPLALQGRDILARSGTGTGKTGAYLLPILHNTLLRKGKTSLILVPTKELALQITKVAKALSAHCGQAVRIQNIAGKESEVVTKAKLADNPDIVIATPARASANINTGALAVTELAHLVVDEGDLVMGYGFKEDLDQIAQNIPKGVQMFLMSATLNTEVESLGSLLCNDPVVLKLDDLDKDSKRVKQYVIKCAEEEKFLLIYAMFKLGLIKGKTIVFVGDTDRSYRVKLFLEQFGIKSCVLNSELPLASRLHIVEEFNKNIYNILIASDETEILGSQKKADESRPKKKPKTDKEAKNDSGVSRGIDFLNVSCVLNFDFPATYKSYFHRIGRTARAGKSGTAISFIIPKDKYRKHKSTTFAGCENDEEVLKKVEKHQEAGQKLENYNFDMKRLEPFRYRFGDALRSVTRIAIREARIKEIRLELSKSQKLSRYFEENPEALAHLRHDQTLNHPARIQPHLKHVPDYLLPGGSRKPADVGFVGLNVPRVNKRQYVKGKGRKVVRRNGKVDPLKTFNARGKGKK | ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. | Q0UZ59 |
Q2JCI0 | WHIA_FRACC | Probable cell division protein WhiA | Frankia | MTATVKDELSRLRVAKPCCRRAEMAALLRFGGGLHIVGGRIVVEAELDTGATARRLRREVAEVFGFPSTVAVLAAGGLRRSVRYIVRVERDGEQLARSTGLLDQRGRPVRGLPPQVVTGSACDAAAAWRGAFLAHGSLTEPGRSCSLEVTSPGPEAALALVGAARRLGVQAKSRDVRGVDRVVIRDGDAIGALLTRIGAHDSLLAWEERRMRREVRATANRLANFDDANLRRSARAAVAAGARVQAAMRILGDDAPEHLLAAGRLRIEHAQASLEELGALADPPLTKDAVAGRIRRLLALADKRANALGIPNTEASVSPDLLENA | Involved in cell division and chromosome segregation. | Q2JCI0 |
B7V1R2 | PRMA_PSEA8 | Ribosomal protein L11 methyltransferase | Pseudomonas | MPWLQVRLAITPEQAETYEDALLEVGAVSVTFMDAEDQPIFEPDLGTTPLWSRTHLLALFEADTDETALLAHLALLTGGDLPEHHVEEIADQDWERSWMDNFQPMRFGRRLWIVPSWHAAPEPDAVNLLLDPGLAFGTGTHPTTALCLEWLDGQELAGRQVLDFGCGSGILAIAALLLGAERAVGTDIDPQALEASRDNASRNGIEPARFPVYLPADLPQRQADVLVANILAGPLVSLAPQLTGLVRPGGLLALSGILAEQAEEVRAAYSAHFDLDPTAEREGWIRISGRRRAD | Methylates ribosomal protein L11. | B7V1R2 |
O75379 | VAMP4_HUMAN | Vesicle-associated membrane protein 4 | Homo | MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALVAAILLLVIIILIVMKYRT | Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule. | O75379 |
Q6NFV3 | NDK_CORDI | Nucleoside-2-P kinase | Corynebacterium | MTERTLILIKPDGVERGLIGEIIARIERKGLKISALDLRVADRETAEKHYAEHADKPFFGELVNFITSAPLIAGVVEGPRAIEAWRQLAGGTDPVAKATPGTIRGDFALEVSTNVVHGSDSPESAEREISIWFPNL | 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. | Q6NFV3 |
Q5PHS1 | TTCA_SALPA | tRNA 2-thiocytidine biosynthesis protein TtcA | Salmonella | MQEIQKNTKKEQYNLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILRNLQQSAPINFSLVAVNLDQKQPGFPEHILPAYLEQLGVEYKIVEENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGATKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDGKHIVIRPLAYCREKDIIRFAEAKAFPIIPCNLCGSQPNLQRQVIADMLRDWDKRYPGRIETMFSAMQNVVPSHLCDTNLFDFKGITHGSEVVDGGDLAFDREEIPLQPAGWQPEEDDTSLEALRLDVIEVK | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q5PHS1 |
Q6N0K6 | NIKR_RHOPA | Putative nickel-responsive regulator | Rhodopseudomonas | MHRVTITLDDDLMEKLDAIIAARGYQNRSEAIRDLARIGIQQTAAETTSGHCVGAMVYTYDHSKRDLPRKLTQSFHHHHDLSRATMHVHLDHDQCLEVTILDGNATELQHFADHIFAERGVRYGRLVTIPAEPPAEGHEHHHEHDASS | Transcriptional regulator. | Q6N0K6 |
C1EQR2 | MTNX_BACC3 | 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase | Bacillus cereus group | MSIQVFCDFDGTITNNDNIMSIMEKFAPPEAEEVKNRILSQELSIQEGVSQLFQLIPTNLHDQIIQFLIETAEIRNGFHEFIQFVNENNISFYVISGGMDFFVYPLLQGLIPKEQIYCNETDFSNEYITVNWPHPCDRLCQNHCGLCKSSLIRKLSDTNDFHIVIGDSITDLQAAKQADKVFARDFLITKCEENHISYTPFETFHDVQTELKHLLEVKL | Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). | C1EQR2 |
Q6AQK0 | GATC_DESPS | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Desulfotalea | MKISEKEVQHVAHLSRLHLDQDELASMTEQLDGILSYMEKLAEVDTEGVLPTTHAFSKTNAFREDIVKDSLSQEESLANGPVQNGTAFQVPRVI | 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). | Q6AQK0 |
Q6XMH8 | DROS_DROSI | Drosocin | Sophophora | MKFTIVFLLLACVFAMAVATPGKPRPYSPRPTSHPRPIRVRREALAIEDHLAQAAIRPPPILPA | Antibacterial peptide with strong anti-Gram-negative bacteria activity. | Q6XMH8 |
Q8JZM6 | TIFAB_MOUSE | TIFA-like protein | Mus | MERPLTVLQVSLYHPTQGPVAFAHVPQQLQHDASRLLVGRGQNTHLQLQLPQLSRYHLSLEPYLEKGSSLLAFCLKVLTRKSCVWVNGLPLRYLEQVPLGTINRISFSGIQMLVRKEGGASLETFVCYFHLSPSPLIYRPKAQETDE | Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA. | Q8JZM6 |
A8ACJ9 | IBPB_CITK8 | 16 kDa heat shock protein B | Citrobacter | MRNYDLSPLLRQWIGFDKLANALQNTGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPAQPEKEIKWLHQGLVTQPFSLSFTLAENMEVSGATFTNGLLHIDLTRNEPETIAPQRIAISERPALNS | Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | A8ACJ9 |
Q5ATZ7 | SFH5_EMENI | Phosphatidylinositol transfer protein sfh5 | Aspergillus subgen. Nidulantes | MAEQAKLPDQAQPVPETQVPDNGKPEQQPTATESAPAPEPATTEPTTAATAPSAVDGTGETAPAAPEPAAAPVAAAAAAPAPEPTKSEPQPAVGEQSEPAKKDEPAKPEYFTKTPALEQFFDRLPTILSNTGHQEMWGVPLKHEVTDIPTINVLIKFLRANAGDLKAAEDQLSKALTWRKENDPIALADASKNSYDASKFKGLGYLTTYQREGKGDLVVTWNIYGAVKKFDETFGDITEFIKWRAALMELAVQELKLDQATSVIDYDGEDPYQMIQVHDYLNVSFLRMNPNVKAATKKTIDVFSTAYPELLREKFFVNVPAIMGWMFAVMKVFVNQNTARKFHPISNGANLAKEFPAGVAEKFPKAYGGSAPDLESSARTVALKEVKEEKKEEPKEGSKEEQKGEQKGE | Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses. | Q5ATZ7 |
Q07154 | EXPB9_MAIZE | ZmEXPB9 | Zea | MGSLANNIMVVGAVLAALVVGGSCGPPKVPPGPNITTNYNGKWLTARATWYGQPNGAGAPDNGGACGIKNVNLPPYSGMTACGNVPIFKDGKGCGSCYEVRCKEKPECSGNPVTVFITDMNYEPIAPYHFDLSGKAFGSLAKPGLNDKLRHCGIMDVEFRRVRCKYPAGQKIVFHIEKGCNPNYVAVLVKFVADDGDIVLMEIQDKLSAEWKPMKLSWGAIWRMDTAKALKGPFSIRLTSESGKKVIAKDIIPANWRPDAVYTSNVQFY | May aid fertilization by loosening the cell wall of the stigma and style, thereby facilitating penetration of the pollen tube. Acts selectively on grass cell walls, which are relatively poor in pectins and xyloglucans and rich in glucuronoarabinoxylans and (1-3),(1-4)-beta-D-glucans, when compared with cell walls of other angiosperms, including other monocots. | Q07154 |
Q46I07 | ARGJ_PROMT | Arginine biosynthesis bifunctional protein ArgJ beta chain | Prochlorococcus | MKNALLNLSLLTSSVWSPISGGITAPDGFLAAGISAGLKPSGKKDLALLYAPDGACCSGTFTQSVTRAYCVDLCIDRIKASEGKIRAVVINSGHANACTGSRGKIDSEMITHKLAQLLRLSSEEVLICSTGVIGEAIPVEKVNSHLDQLINSLDKEAYLDAANAILTTDLQVKQIAYQAVLGGRRISIGGMAKGSGMIHPSMATMLSYLTCDVGVDHVLWSDMIKRVAESSFNSITVDGDTSTNDTFLAFASGAELDPRYLSILEEGLHLTAQHLAKSIARDGEGANCLLEIKVEGASSDLDARAIARTIASSSLVKTAVHGSDPNWGRIIAALGRAGTSFNLNDVKLWIGPYEIFSNGTPLDFDRQIVSNFMKARLTGKYLIDDLISIRLRIGIGTGSATAWGCDLSDQYVRINADYTT | Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. | Q46I07 |
Q03VA1 | RF1_LEUMM | Peptide chain release factor 1 | Leuconostoc | MDPIFQSLQTVIDHYDELNEQLADPEVMNNGQHYMKLSKEAGEIRQTVEVYTRYKQVIQDIQDAEELLGDAEMAPLAKEDLSALKPEKEQLEEQLKILMLPKDPNDDKNIIMEIRGAAGGDESSLFAADLLDMYRRYAERQNWSMSIIDESTTEVGGYKEVAVMITGDNVYSKLKFESGAHRVQRVPATETQGRVHTSTATVGVMPEFEEIDFELNESDLEEEFFRSGGAGGQNVNKVSTAVRLIHKPTGIMVKMQEERTQIKNRDKARKLLASRVYDFYAQQNESEYAAQRKSAVGTGDRSERIRTYNYPQNRVTDHRIGLTLNKLDRIMNGELGEVIDALVIADQTAKLAELNK | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | Q03VA1 |
Q8NH57 | O52P1_HUMAN | Olfactory receptor 52P1 | Homo | MESPNHTDVDPSVFFLLGIPGLEQFHLWLSLPVCGLGTATIVGNITILVVVATEPVLHKPVYLFLCMLSTIDLAASVSTVPKLLAIFWCGAGHISASACLAQMFFIHAFCMMESTVLLAMAFDRYVAICHPLRYATILTDTIIAHIGVAAVVRGSLLMLPCPFLIGRLNFCQSHVILHTYCEHMAVVKLACGDTRPNRVYGLTAALLVIGVDLFCIGLSYALSAQAVLRLSSHEARSKALGTCGSHVCVILISYTPALFSFFTHRFGHHVPVHIHILLANVYLLLPPALNPVVYGVKTKQIRKRVVRVFQSGQGMGIKASE | Odorant receptor. | Q8NH57 |
Q22235 | ENPL1_CAEEL | Endoplasmin homolog | Caenorhabditis | MRFLLVGFVALLAVSAFIPNVYAEDEIEDAPKETKEETREEDSIKLDGLSVSQIKELRSKAEKHEFQAEVNRMMKLIINSLYRNKEIFLRELISNASDALDKIRLLSLTDPEQLRETEEMSVKIKADRENRLLHITDTGVGMTRQDLINNLGTIARSGTSEFLSKLMDTATSSDQQQDLIGQFGVGFYAAFLVADRVVVTTKNNDDDQYIWESDSASFTISKDPRGNTLKRGTQITLYLKEEAADFLEPDTLKNLVHKYSQFINFDIFLWQSKTEMVEEAVEEEPATTEDGAVEEEKEEKKTKKVEKTTWDWEKVNNVKPIWMRKPNQVEEDEYKQFYKSITKDSEEPLSHVHFSAEGEVSFRSILYVPKKSPNDMFQNYGKVIENIKLYVRRVFITDDFADMLPKYLSFIRGIVDSDDLPLNVSRENLQQHKLLKVIKKKLVRKVLDMLKKLDGAQFDDFWSEFSTNIKLGVMEDPSNRMRLAKLLRFQSSNDADKTTTLAAYVERMKEKQDAIYYMAGTSRKEVETSPFVERLIAKGYEVLFLTEAVDEYCIQAMPEYESKKFQNVAKEGVTIDDGEKAKEAHKGLEEEFKPLTDWLKETALKDLIEKAVVSQRLVKSPSALVASSYGWSGNMERIMKSQAYAKAKDPTQDFYATQKKTFEINPRHPVIKELLKRVTASEEDTTAASTAKLLFETATLRSGFSLQDQVGFADRIEAVLRQSLDVSQDAQVETEQHIEEAEPEPEAAEETTIEEEHSEL | Molecular chaperone that functions in the processing and transport of secreted proteins. | Q22235 |
Q5X4X1 | RS18_LEGPA | 30S ribosomal protein S18 | Legionella | MSAYFRRKKMCRFSAEGGNEIDYKDINLLKNYITETGKIVPSRITGTQTRFQRQLAKAIKHARFIGLLPYCDSHR | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | Q5X4X1 |
A4IJ94 | PDXS_GEOTN | Pdx1 | Geobacillus | MALTGTDRVKRGMAEMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPADIRAAGGVARMADPTVVEEVMNAVSIPVMAKVRIGHYVEARVLEALGVDYIDESEVLTPADEEFHIDKRQFTVPFVCGCRDLGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQIRKVVSMSEDELVAEAKQLGAPVEVLREIKRIGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKSENPEKYARAIVEATTHYEDYELIAHLSKGLGGAMRGIDVATLLPEHRMQERGW | Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. | A4IJ94 |
Q99020 | ROAA_MOUSE | CArG-binding factor-A | Mus | MSDAAEEQPMETTGATENGHEAAPEGEAPVEPSAAAAAPAASAGSGGGTTTAPSGNQNGAEGDQINASKNEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDSSSVEKVLDQKEHRLDGRVIDPKKAMAMKKDPVKKIFVGGLNPEATEEKIREYFGQFGEIEAIELPIDPKLNKRRGFVFITFKEEDPVKKVLEKKFHTVSGSKCEIKVAQPKEVYQQQQYGSGGRGNRNRGNRGSGGGQGSTNYGKSQRRGGHQNNYKPY | Transcriptional repressor. Binds to CArG box motifs, single-stranded and double-stranded DNA, and RNA. It may be that repression by CBF-A is a result of competitive binding of CBF, a putative positive factor, and CBF-A to the same or overlapping motifs around the CArG boxes. | Q99020 |
B0RB59 | KAD_CLAMS | Adenylate monophosphate kinase | Clavibacter | MTRLLIVGPPGAGKGTQAKRIAADRGIPDVSTGDIFRQNIKDRTELGQQVQALVDAGNYVPDELTNRLVTVRLQEEDAQAGFLLDGYPRTLAQVAYLEELLQGWGQELDAVIQLVADEDEVVARLTRRAAEQGRADDGEDEIRHRQEVYVRETSPLIDVYREHGLLVEVDGLGEVDEVAERIRTALAARGVRPSSDAGRA | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | B0RB59 |
B1LW28 | CLPP_METRJ | Endopeptidase Clp | Methylobacterium | MRDPIDVYNNALVPMVVEQSSRGERAFDIYSRLLRERIIFLTGPVEDYGASLIVAQLLFLEAENPKKEISFYINSPGGVVTSGLSIYDTMQFIRCPVTTLCVGQAASMGSLLLTAGEPGHRFALPNARIMVHQPSGGFQGQATDILIHAREIEALKRRLNEIYVKHTGRDYDTIHTALERDNFMTADAAKEFGLIDEVIEKRPEPAAA | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | B1LW28 |
Q82XI7 | THIG_NITEU | Thiazole synthase | Nitrosomonas | MEPLVIAGKSYSSRLLLGTGKYRDFAETRAAVDASGAQIITVAIRRTNIGQNPDEPNLLDILPPSQFTLLPNTAGCYTAEDAVRTLRLARELLDGHALVKLEVLGDQKTLFPDVVATIEAAKILVKEGFQVMVYTSDDPIVARQLEDIGCAAIMPLASLIGSGMGILNPWNLQIIIDKATVPVIVDAGVGTASDAAIAMELGCDGVLMNTAVASARNPILMASAMRKAVEAGREAYLAGRMPRKIYQASPSSPAEGMFTGTQHPAANS | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q82XI7 |
Q01674 | FOXA_YEREN | Ferrioxamine receptor | Yersinia | MFSAFIIKRSAILCSLAMFIPLASIADDTIEVTAKAGHEADLPTSGYTATTTKGATKTDQPLILTAQSVSVVTRQQMDDQNVATVNQALNYTPGVFTGFSGGATRYDTVALRGFHGGDVNNTFLDGLRLLSDGGSYNVLQVDPWFLERIDVIKGPSSALYGQSIPGGVVMMTSKRPQFTSEGHFRLTAGNNNTQVAAFDYTDAISEHWAFRLTGITRNSDTMYDHQREERYAIAPSLLWQPDENTSLLLRANLQKDPSGGYHSAVPADGSIYGQKLSRGFFDGESNHNVFKRWQQIYSYEFSHKFDDVWSFRQNASYTHSNTQLEQVYQGGWNSDRTLMNRYYSGEDSSLNAFAVDNQLEADLRTAAVKHKVLLGVDFQKFRNNLRSDSAYATPLNPYTGVSGGSTLYSDYLLTTPGINTSYLSRRYEQSGVYLQDEMTLDNWHLNLSGRYDRMKTENINNTANSTDERTDNHASGRASLLYSFDSGISPYVSYSQAITPSLFPDAQQKLLKPMTSEQYEVGIIYQPPGSTSLYSAALYDLTQNDVANRAVPATYYVPAGKVNSQGLELEARSQISDRLSVIAGYTYNRVKFKDAIDGNDGNTPVLAPSNMASLWAQYEAGYGINVGAGIRYIGKQWADDANTLRVPSYTLGDASVRADLGTWAASLKGAFVQLNVNNIADKKYVAACYSTSYCYWGAERSVQATVGYDF | Ferrioxamine binding and uptake, in association with the TonB protein. | Q01674 |
Q48MF3 | RLMF_PSE14 | rRNA adenine N-6-methyltransferase | Pseudomonas | MTDTRKPPRKKPQRPAKPAAPREKATLHPRNRHQGHYDFAKLIKSSPELAAFVILNPYGKESIDFADPQAVRVFNRALLKAFYGIAHWDIPADYLCPPIPGRADYLHFLADLLAEDNEGVIPRGASIKALDIGTGANCIYPLLGHSDYGWQFVGSDIDSTAIAAATTIIKANGLSKAISVRQQDNRKQILLGLLDSSERFHVSLCNPPFHASLDEAQRGSQRKWRALGKADPKRKLPVLNFGGQSQELWCEGGEIGFVTRLIQESATLPSQVVWFSTLVSKASNLPPIQNALKKAGALEVKVIEMGQGQKQSRFVAWTFLDKAQRTPH | Specifically methylates the adenine in position 1618 of 23S rRNA. | Q48MF3 |
O26900 | MOAC_METTH | Molybdenum cofactor biosynthesis protein C | Methanothermobacter | MMIMKEFTHTDEKGVRMVDVGSKPVVRRTATAEGHILLREDTINLIREKKIEKGNVLATAQIAAIVAVKRTWEIIPLCHPLPLTGVDVEFDLDDDRITARVTVRCDGKTGVEMEAVTGVSVALLTIWDMVKSVEKDDDGQYPETAISNIRVIKKEKLEL | Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). | O26900 |
P58426 | TXHP2_HETVE | Toxin KJ6 | Heteropoda | DDCGKLFSGCDTNADCCEGYVCRLWCKLDW | Inhibitor of voltage-gated potassium channels of the Kv4/KCND family. Inhibition of Kv4.3/KCND3 and Kv4.2/KCND2 is strongly voltage-dependent, while inhibition of Kv4.1/KCND1 shows less voltage-dependence. Its binding site may be near the potassium channel voltage sensor. Also blocks calcium channels. | P58426 |
Q6F6Z6 | PYRE_ACIAD | Orotate phosphoribosyltransferase | Acinetobacter | MTTPSSFNPQAFIELALSRGVLKFGEFTLKSGRVSPYFFNAGLLNDGEALSLLAQGYADQLMQCQHVDVIFGPAYKGIPFVAATAVALSQLHAKSVPWGFNRKEAKDHGEGGVLVGASVEGKKVWIIDDVITAGTAIREVVTILKNAGATIAGVLVALDRQERGQGQLSAIQEVQQELEIPVHALITMKDLMNYLDAKGETQALAKMEDYRLKYGI | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | Q6F6Z6 |
Q30Y32 | NADK_OLEA2 | ATP-dependent NAD kinase | Oleidesulfovibrio | MHRELKRVFIVTKQAHAGAAALAADMQAWFAARGIEAATEENDTASALPDFARSASCIMVLGGDGTMLSVSRRAVGLDVPLLGVNLGKVGFLAEVSAAGWQQAFTRLAENGLTCSERLALHFAVSREGRCVFEGTAVNDVVLHRGVLARVINLGLGVDGEWLGDLRADGLIVSTPTGATGYAVSAGGPLVHPDMSVYAITPICPFLNNFHPMVLAGSMRFEIRILEGPQEVYVTQDGQECFALQAGDLVTVTQASRGLLFVAVEGSTYFTRLRAKGFVRDPRGRGRAVPASS | 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. | Q30Y32 |
Q8TQR1 | DNAJ_METAC | Chaperone protein DnaJ | Methanosarcina | MATKRDYYEILGLPKDASVEDIKKTYRKLALQYHPDRNKDPGAEDKFKEISEAYAVLSDTEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYITFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPTCGGTGQVRTTRSTLGMQFISTTTCSTCHGRGQIIESPCPVCGGAGRVRNKRTITVNVPAGADSGMSLRLSGEGDSGEPGAPSGDLYIIIHVMEHRHFKRVDYDVISELSITFTQAALGADVMVDTLYGKVKMNIPAGTQTHSVFRLRDKGIQRLHGHGKGDQLVRVIIKTPTKLNQEQKELLRQFENLSKGKKPQEEEKSKAEKHKKGIFEKVKDAFES | 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. | Q8TQR1 |
A8Z673 | RL22_SULMW | 50S ribosomal protein L22 | Candidatus Sulcia | MESNNYINFFFKKKKYTKSVADVRNIYCSPRKLRLVADIIRNKKVEYSLFILKNIKNKGGGIIYKILLSVISNWKNYENNINNYNIYIEKVLINQGYQLKKIRPGPQGRGNKVRKRYSNLKIIINSKFNNYYGT | 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. | A8Z673 |
P60742 | RL24_MYCPA | 50S ribosomal protein L24 | Mycobacterium avium complex (MAC) | MKVRKGDTVLVIAGKDKGAKGKVLKAYPDRERVLVEGVNRIKKHTAISTNQRGAQSGGIVTQEAPIHVSNVMVVDSDGKPARVGYRLDEETGKRVRISKRNGKDI | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | P60742 |
Q3YUX6 | METAS_SHISS | Homoserine transsuccinylase | Shigella | MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQEQNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTDKLSGVYEHHILHPHALLTRGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDAQTLAQEYFRDVEAGLDPDVPYNYFPHNDPQNKPRASWRSHGNLLFTNWLNYYVYQITPYDLRHMNPTLD | Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. | Q3YUX6 |
A8YWU7 | METK_LACH4 | Methionine adenosyltransferase | Lactobacillus | MERRLFTSESVSEGHPDKVADQISDAILDAMLEKDPNSHVACETIVTTGMVFVFGEISTNAYVDIQDVVRKTILRIGYDRPELGFDGNNCAVMVDIDEQSPDIAGGVDHSLETRENESDQDELDQIGAGDQGLMFGFAIKETPELMPLPISLAHRLMRRVASLRKDHTLDWLRPDAKAQVTVEYDENNNPLRVDTVVISTQTDAEVSNKEIRRAMIDLVIKEVIPARYLDEKTKFLINPSGRFVIGGPKGDSGLTGRKIIVDTYGGYARHGGGAFSGKDSTKVDRSASYAARYVAKNIVAAGLAYRCEVQLAYAIGVAHPVSIMIDTAGTGKVDDDLLTEAVRHVFDLRPAGIIKMLDLRRPIYEQTAAYGHFGRTDVDLSWEKTDKTQDLLDYIKNNK | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | A8YWU7 |
Q16AK0 | RNH_ROSDO | Ribonuclease H | Roseobacter | MPELFAYTDGACSGNPGPGGWGVLLQAKEGDRLVKERALKGGEAHTTNNRMELLAAINALESLSRASTITVVTDSNYVKNGITGWIHGWKRNGWKNAAKKPVANAELWQRLDEANARHDVTWKWVKGHAGHAENERADELARAGMAPFKP | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q16AK0 |
Q09313 | DCT6_CAEEL | Daf-16/foxo controlled, germline tumor-affecting protein 6 | Caenorhabditis | MIESTTSHQDFQQRSMTGYALEHPSYRIRGALFRHQDDGRLLSGCGGDIEVIHALELERSQHTCLPVRVTNVVVFGSNDVVRLIQPIEGTEDVIVNGDYHVSIVQSVELFESSTVSKSRILKLPGKIIAVNAEKHSNTELLLVFLLETGIFHYSFCAHTSTHFQCIQAFRCNRPITSGLLWRDSGLLHVAYYDGFVRVGVVHEQYDDMLLVKRVAVNRNNLSVLLDVVFEEIGRIQKFEDTEKQRREDMLTTSKSLSDKLVAEEEVVEGDTTNDDFAKLKIEFKNQSIRCERVSQRLTSLRKLITIIKSALDMNDQIEQMISLLVDELSELEKLEQLCKEVERTGNQNLIGKSWIAVEEKQMVVEELIAKVNSDQIKKHSDVWEQKIDQIIDQLNGCSEAAKDMRLIISQNIFEHRGDKKDVFTHFVLDAQSRDITLYCLSGLTTMAIYPRKGKRVASISLDASFATCLTAACAMKSAEGVYVADQNNVFPTYFYRNRPKAGKGEKRYLDAGNQLQLPTFDSISSILVEPHQMILGSVTGGLLHLSFDFASNYEHFVVASSILAHPISSGSVNCIKLLATGESLLALHCTDTEIVVSEKDQERWHRVTHHTGGAHAIAVTPFSVDERGAFAVVASDTFVRLKVLQYAEESLIGLHDLGESRAEDENGHPIEVLNVSLDPSMQYRQLPCKLRYAVGFADKAIRTYVALLTGQHDFNVQEKFIAQIEPLFNVQNMICFHGRPMGCYVSCAKTLQIWNDLDRHQQKKLKSERMQLLKLSSSVTSMERAEGYLLLGFADDRLSIYEEKGNGAVDLVGTVDDWHKGLNDRIVMSLRTRASKTSCGTRLFIHSLTAHHIVIHTVLVTASKIEQHDFIVAHEHSMSQPIGFEFVSYKYFEFLVYGRGISNEKLSIEDRKRMDNFRDFEFN | May have a role in tumor suppression. | Q09313 |
B1J2D7 | ILVC_PSEPW | Ketol-acid reductoisomerase type I | Pseudomonas | MKVFYDKDCDLSIIQGKKVAIIGYGSQGHAQACNLKDSGVDVTVGLRKGSATVAKAEAHGLKVADVATAVAAADLVMILTPDEFQGALYKNEIEPNIKKGATLAFSHGFSIHYNQVVPRADLDVIMIAPKAPGHTVRSEFVKGGGIPDLIAIYQDASGNAKNVALSYASGVGGGRTGIIETTFKDETETDLFGEQAVLCGGTVELVKAGFETLVEAGYAPEMAYFECLHELKLIVDLMYEGGIANMNYSISNNAEYGEYVTGPEVINEESRKAMRNALKRIQDGEYAKMFISEGATNYPSMTAKRRNNAAHGIEVIGEQLRSMMPWISANKIVDKTKN | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | B1J2D7 |
Q6CAC9 | UTP25_YARLI | U three protein 25 | Yarrowia | MARSHKVTKPKRQQVDTSGSYNALMVLMGDNVKKAEKRVEEEEPVEQELEEDDIEGAGEEEEEVDEEQEEEEDADDAEEDAEDDSETDKYDPYKLHFEAEEAKYVSVIKSEEWKTSSEKTKIGSQPVRITYTNLEDADELLDFSEAQKTEFSKYTVRPRIKDGFKQLNGSLTSVQKAIYPSLMAYRDLCYATSSLSDTEEFSRLVAMHIAQHVVRTAEEVAYNTRILKRNAEEGIHDVEFRDQGYTKPRVLVLVPTKNACFEFMQLLVGASGVDREDNKARFNKAFHEAGAVLDTKPEDFQKAFKGNTDDMFCLGVKLRNKSIRYYSYFYQADIVFASPLGLKTLVGSEGDSKREFDFLSSIEIAYLHETNHMEMQSWDNVLTVLGQTNLLPNESHGCDFSRVKSFYLDGLAKHFRQTIVACQFVTPTINSVFSNTVNFAGKTKITPIYNGELAVAGMKIRQIFTRFKALSVSDEIDARFKAFVQITLEGMIRSGDYSGTLIYVPTYVELVRLRNYMDEKNISFGAISEYSSITEVKRHRTLFRDGREKILLYTGRLHHYRRYFVKGVKSVVIYKLPENPAFYRELLLFLTHSVDEGTLEQSMAKCRALFTIYDLLALERIVGTKRVKTMAKSGESSYEFY | DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2. | Q6CAC9 |
Q4WAX0 | FTMG_ASPFU | Fumitremorgin biosynthesis protein G | Aspergillus subgen. Fumigati | METLDAIQLPYLGVVGASLIVILGIILLFPLGSDPFITINQHPRDLFQTKAKQQFEYNAAALLNEGLQTGHSAFRLVTNMVTYLILKDQYAEEIKNDSRFGAHEAVDPVLLVDLPGLESMFQGSLHNQVPPMAVRALNKELVHLTPSLSEEAMNCLQTRWTDSTEWHGVSIPETVLALIAQMTTRALLGPELCRNPEWLDIAKSFTTNRAIAVAAVQSWPSFLQPVIHWFLPPCRALRRQIQCARNIILPALERERRAYCSDQPTKREFSNLVFIDQYAKGARYDATMAQLRIIAVAFQTTSDLVEKVIARLCKHPELIEPLREEVVSVVGNHGLHRHSLRKLTLMESVMKETQRLEPAVIIGMFRLAKEKVTLKDGTVVPKGTNIAFANDLRFDPEMYLEPETFDGYRFQRMREDPAKIDLAPFTKTRMSHLAFGHGKHACPGRFLACDEAKLILCHILLNYDIRAVEGSPPELPGSWGNDVGEKTAGD | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA . Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B . The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively . The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B . Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties . In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable). | Q4WAX0 |
Q9HUX4 | NASLL_PSEAE | Nicotianamine synthase-like enzyme | Pseudomonas | MQGRTPLLETLRELECEIRLLTVYARECCGCYEILRRKLDRLSGLIGEDCSRAQWQADSDDPALQALGLRLRDAAVQALCELEKHLCQGVLHEPGEMGRYLGSLLESIRGELDSAGIDADARVLFVGSGALPTSALVLAREVGAHLCCLDIDEEALGCAREIARCQGLEARMQFSSLPPAELAFSRDATHFLIASLVQQKSAVLAQIRQVMRADAKVLLRHGSGIKGLFNYPVEPAELDGWRVCAERVSQPLYDTLILEKAGR | Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto L-histidine to produce the intermediate (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to Pseudomonas virulence. Appears to be specific for L-histidine as substrate. | Q9HUX4 |
Q32IR3 | YBEY_SHIDS | Endoribonuclease YbeY | Shigella | MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTILVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q32IR3 |
A8Z6D9 | END4_CAMC1 | Endonuclease IV | Campylobacter | MRYIGAHVSAAGGVSNAPINAAKIGANAFALFTKNQRQWSAKELSEGEIEQFKANLKASGISADHVLPHASYLINLGHPEKEARAKSLEAFIDEIERASKLGLKLLNFHPGSHLKQISQNECLDNIARCINEALKRTSGVKLVIENTAAQGSNLGFDFAQLAYLIERVDDESRVGVCIDTCHAFAAGYDLRSKEAYAKTMGEFDAVIGYKFLSGMHLNDAKFGLGSKKDRHESLGKGELGLGAFENIINDDKIGEIPLILETIDESIWEDEIKILRNLEKEKL | Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | A8Z6D9 |
P93394 | UPP_TOBAC | UMP pyrophosphorylase | Nicotiana | MAAQNKAMSGNRMLVFVPPHPLIKHWVSVLRNEQTPCPIFRNAMSELGRLLMYEASRDWLPIITGEIQSPMGVASVEFVDPREPVAIVPILRAGLALAEHASSILPATKTYHLGISRNEETLQPSVYLNKLPDKFPEGSRVIVVDPMLATGGTIVAAIDLIKERGVDNSQIKVICAVGAPPALQKLSEKFPGLHVYAGILDPTVNDKGFIIPGLGDAGDRSFGT | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | P93394 |
Q1LQS4 | CH60_CUPMC | Chaperonin-60 | Cupriavidus | MAAKDVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVREGMKFVAAGMNPMDLKRGIDKAVGAAVEELKKLSKPTTTSKEIAQVGAISANSDASIGERIAEAMDKVGKEGVITVEDGKSLADELEVVEGMQFDRGYLSPYFINNPEKQVVQLDSPFVLLFDKKVSNIRDLLPVLEQVAKAGRPLLIIAEDVEGEALATLVVNNIRGILKTAAVKAPGFGDRRKAMLEDIAILTGGTVIAEEIGLTLEKATLQDLGQAKRIEIGKENTIIIDGAGDASAIEGRVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGIVPGGGVALLRARAAIAGLHGENPDQNAGIKIVLRAMEEPLRQIVLNAGEEASVVVAKVIEGKGNYGYNAASGEYGDLVEMGVLDPTKVTRTALQNAASVASLMLTTDCAVAESPKEESAPAMPGGMGGMGGMEGMM | 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. | Q1LQS4 |
Q824U5 | PYRH_CHLCV | Uridine monophosphate kinase | Chlamydia | MSKRITRVLFKISGESLSTDSGNRIDEVRLSRLVSELRAVRNSDIETALVIGGGNILRGLAQQKELQINRVSADQMGMLATLINGMAVADALKADDIPCLLTSTLSCPQLADLYTPQKSEEALSQGKVLICTTGAGSPYLTTDTGAALRACELKADILLKATMHVDGVYDKDPLMFTDAVKYDRISYKDFVAQGLGVMDVSAVSLCMDSNIPIRVFSFVKHSLEQAIFDENIGTLICGDA | Catalyzes the reversible phosphorylation of UMP to UDP. | Q824U5 |
A9KSC2 | HEM12_LACP7 | Glutamyl-tRNA reductase 2 | Lachnospiraceae | MNISMVGIDYNTASIEDREHFTLTSDKQLEIAKIIKETYHASGCIILSTCNRTEIWFSELGTSEAECFHQLVLGENAKETMRSICVCRQGDEAVTYLMELGCGIHSQIFGEDQILTQLKQALQQARDYQYVDSVLECLFRTAITAAKKVKTSIQIAKGNTSLPQTIVEQLEKEQGDLLGKSCLVIGNGEMGRLMTEKLLEKKCKVWMTLRQYKKSKAIIPEGSGVVLYDERYEHIAVMDYIFSATKSHHFTINKSMFENIRLKGKTYCLIDLAIPRDIEPSVEELSDVTVYNMDYFCQEVNDREKELEETRELLSEYVNEFKQWYQFRNLVSTVDDISNIVSDITDAKLTKVYKSIDLSREQQELLQSNVQMAAKKAVSKIIFGLRDVLQIDQCEEVLQALEQSAMNCTDSVK | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | A9KSC2 |
Q9ERQ3 | ZN704_MOUSE | Glucocorticoid-induced gene 1 protein | Mus | MQARRLAKRPSLGSRRGGAAPAPAPEAAALGLPPPGPSPAAAPGSWRPPLPPPRGTGPSRAAAASSPVLLLLGEEDEDEEGAGRRRRTRGRVTEKPRGVAEEEDDDEEEDEEVVVEVVDGDEDDEDAEERFVPLGPGRALPKGPARGAVKVGSFKREMTFTFQSEDFRRDSSKKPSHHLFPLAMEEDVRTADTKKTSRVLDQEKETRSVCLLEQKRKVVSSNIDVPPARKSSEELDMDKVTAAMVLTSLSTSPLVRSPPVRPNEGLSGSWKEGAPSSSSSSGYWSWSAPSDQSNPSTPSPPLSADSFKPFRSPAPPDDGIDEADASNLLFDEPIPRKRKNSMKVMFKCLWKSCGKVLNTAAGIQKHIRAVHLGRVGESDCSDGEEDFYYTEIKLNTDATAEGLNTVAPVSPSQSLASAPAFPIPDSSRTETPCAKTDTKLVTPLSRSAPTTLYLVHTDHAYQATPPVTIPGSAKFTPNGSSFSISWQSPPVTFTGVPVSPPHHPTAGSGEQRQHAHTALSSPPRGTVTLRKPRGEGKKCRKVYGMENRDMWCTACRWKKACQRFID | Transcription factor which binds to RE2 sequence elements in the MYOD1 enhancer. | Q9ERQ3 |
A9YTQ3 | AHRR_HUMAN | Class E basic helix-loop-helix protein 77 | Homo | MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELHGKPNYSAGRSSRESGVLVLREQTDAGRWAQVPARAPCLCLRGGPDLVLDPKGGSGDREEEQHRMLSRASGVTGRRETPGPTKPLPWTAGKHSEDGARPRLQPSKNDPPSLRPMPRGSCLPCPCVQGTFRNSPISHPPSPSPSAYSSRTSRPMRDVGEDQVHPPLCHFPQRSLQHQLPQPGAQRFATRGYPMEDMKLQGVPMPPGDLCGPTLLLDVSIKMEKDSGCEGAADGCVPSQVWLGASDRSHPATFPTRMHLKTEPDSRQQVYISHLGHGVRGAQPHGRATAGRSRELTPFHPAHCACLEPTDGLPQSEPPHQLCARGRGEQSCTCRAAEAAPVVKREPLDSPQWATHSQGMVPGMLPKSALATLVPPQASGCTFLP | Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site. | A9YTQ3 |
Q9V2X0 | FLAB2_THEKO | Flagellin B2 | Thermococcus | MFRGLKKRGAVGIGTLIVFIAMVLVAAVAAAVLINTSGYLQQKASSTGRETTQEVASGLKIMKVIGYDPADPPASGKIERLAVYVSPNAGSSGIDMKKVRVILSNGDKQAIYNYYVPESGTFVSETTTTLKLAFATSEPDWTSGGTGLDFSAGLKIVFDASGSLTIADGNGNSVSINRFTITTDTSNNYYGDSGTNDYKETFTTDSASNYYLYSQYDAVIVLFDQNGNVVGKLPLKAGANTIVVEAYDIDASSLSNIDYLVIYNKDFPDSKITWGVPQNLDKAGTTVTVVDVTTNNQVTLDSDGDFSLGAINVADYNDPNSGTGDVMFEIDYSLGSETTPKLGGDDTVTLKFLQDNSGTPTPVSLDLSVVDDQTSSGTDYYIYTGHAVFYASENATIVLGDTKIPIKAGPNVVDIYAEDKGNSADGTDVDYIKVTINGVSFEWGTQGQENNAFSGTVAQIKDVNIDVIDSTDGLYGAAFTGFDNVNGGIFGDANGAWAALRANTNFGIIALQDADGSLKATTPTLTEGDIAVLTLDVKGIFGGFAPRTHITGKVVPEFGAPGVIDFTTPTSFNSNVIELQ | Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. | Q9V2X0 |
P0A2E9 | FLIA_SALTI | Sigma-28 | Salmonella | MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVDRYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAMGQLEQELGRNATETEVAERLGIPVAEYRQMLLDTNNSQLFSYDEWREEHGDSIELVTEEHQQENPLHQLLEGDLRQRVMDAIESLPEREQLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL | Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | P0A2E9 |
Q1QEM6 | THIC_PSYCK | Thiamine biosynthesis protein ThiC | Psychrobacter | MTISDIGSQATTHTPVKASKADALKTPAHRSETDARFEEDARDLHRILPASRKVYIEGSRPDIQVPMREITLDPTPIQGVSESEWEQNPPFYVYDTSGVYTDPNAAIDLTKGLPKLREGWIDERGDTEQLAGLSSSYGLARARDISTANLRFAHIDKPRRAKAVDGKVGNVTQLHYARRGIITPEMEYIAIRETQKQHELTDMRQHEGETFGAHTPAIITPEFVRSEVAAGRAIIPNNINHPESEPMIIGRNFLVKINANIGNSALGSSIDEEVSKMTWATRWGADNIMDLSTGNHIHETREWLIRNSPVPIGTVPIYQALEKVDGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLEYVPLTAGRLTGIVSRGGSIMAQWCMFHNKESFLYTHFEDICEIMKQYDVAFSLGDGLRPGCLQDANDEAQFGELRTLGELTQVAWKHDVQVMIEGPGHVAMNRIKENMDLQLEVCADAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPNKKDVKDGIITYKIAAHAADLAKGHPGAQARDNALSKARFEFRWDDQFNLALDPDTAREFHDETLPKDAHKTAHFCSMCGPKFCSMKITQNVREYAKGLNAQ | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | Q1QEM6 |
A1WVA8 | RS8_HALHL | 30S ribosomal protein S8 | Halorhodospira | MSMTDPIADMLTRVRNAHHAEKADVRMPSSKLKRAIAAVLQEEGYIEGYREVGEEKKPVLEVTLRYHEGQPAIREIQRYSRPGLRVYRGRDELPRVRNGLGTAIISTSKGVMSDGQARAQGHGGEVLCWVF | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | A1WVA8 |
P57893 | RUVA_PASMU | Holliday junction ATP-dependent DNA helicase RuvA | Pasteurella | MIGHLTGRLVEKHPPEILLDVQGVGYELLLPMTSFYQLPDIGQQTALFTHLVVREDAHLLFGFSQKTDRTLFRELIKTNGVGPKLALAILSAMSVEEFAYAIEREELSKLVKIPGVGKKTAERLLVELKGKFKGIQQEDFFIESQHLKQPEHALNEQDIPASEAISALIALGYKAAEAEKLVKKISKPALSSEQLIREALKAAL | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | P57893 |
Q09MG7 | YCF4_CITSI | Photosystem I assembly protein Ycf4 | Citrus | MSWRSEYIWVEFIAGSRKPGNFFWAFILFLGSLGFLVVGISSYLDRNLLSLFPSQQINFFPQGIVMSFYGIAGLFISSYLWCTIIWNVGSGYDRFDTKEGIVCIFRWGFPGKNRRIFLRFLMKDIQSIRIEVKEGIYARRVLYIESRGLGAIPLNRTDENLTPREIEQKAAELAYFLRVPIEGF | Seems to be required for the assembly of the photosystem I complex. | Q09MG7 |
B2T744 | RL16_PARPJ | 50S ribosomal protein L16 | Paraburkholderia | MLQPKRRKYRKEQKGRNTGIATRGNAVSFGEFGLKAIGRGRLTARQIEAARRAMTRHIKRGGRIWIRIFPDKPISHKPAEVRMGNGKGNPEYYVAEIQPGKMLYEMDGVTEELAREAFRLAAAKLPLKTTFIVRQLGA | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | B2T744 |
A3PIB9 | ATPB1_CERS1 | F-ATPase subunit beta 1 | Cereibacter | MATASQGKVTQVIGAVVDVQFDGGLPPILNALETENNGKRLVLEVAQHLGESTVRTIAMDATEGLVRGARVTDTGSPISVPVGDATLGRILNVIGEPIDEKGDLGEASTRAIHQPAPTFAEQSTTSEILVTGIKVIDLLAPYSKGGKIGLFGGAGVGKTVLIMELINNIAKVHSGYSVFAGVGERTREGNDLYHEMIESGVIKIDNLSESKVALVYGQMNEPPGARARVALTGLTLAEQFRDQSGTDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITSTKAGSITSVQAIYVPADDLTDPAPATSFAHLDATTVLSRAISELGIYPAVDPLDSTSRILDPQIVGEEHYNVARAVQGILQRYKSLQDIIAILGMDELSEEDKLSVARARKIQRFLSQPFDVAKVFTGSDGVQVPLEKTIASFKAVVNGEYDHLPEAAFYMVGDIEDVIAKAQRLAAQAA | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | A3PIB9 |
Q2U9B5 | KAE1_ASPOR | tRNA threonylcarbamoyladenosine biosynthesis protein kae1 | Aspergillus subgen. Circumdati | MIAIGLEGSANKLGVGIMLHPDNGNPPQVLANIRHTYVSPPGEGFLPKDTARHHRAWVVKLVKKALKEAHVSVQDVDCICFTKGPGMGAPLQSVAVAARMLSLLWGKELVGVNHCVGHIEMGRLITGSTNPVVLYVSGGNTQVIAYSSQRYRIFGETLDIAVGNCLDRFARTLHISNDPAPGYNIEQLAKKGKQLVDLPYTVKGMDCSFSGILAAVDGLATTYGLGGEGKDDETDTPIPDADGNGKPTRADLCFSLQETIFSMLVETTERAMAHVGSKEVLIVGGVGCNERLQEMMGIMARDRGGSVHATDERFCIDNGIMIAQAGLLAYSTGFRTPLKDSTCTQRFRTDDVFVKWRD | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. | Q2U9B5 |
Q9PK65 | EX7L_CHLMU | Exodeoxyribonuclease VII large subunit | Chlamydia | MSITSPPVEVSVLTDSIKNLLEKNFLRVVVKGELSNVSLQTSGHLYFAIKDSKAVLNGAFFHFRSKYFDRRPKDGDYVILHGKLTVYAPRGQYQIVAYALTFSGEGNLLQQFEERKQRLAAEGYFDPKRKRQIPSEARTIGVITSPTGAVIQDILRVLSRRCHQFQVILYPVTVQGPTAAQEISRAIQVFNQENIKIDTLIVARGGGSIEDLWAFNEEILVKAIAASSIPIISAVGHETDFTLCDFAADVRAPTPSAAAEIVCKSSEQYHQELQNLLRHLSSHSRQFIAAKKNLLSHWKKHLATADFYHTAQQTLDYTRLSLERTLDAKLEHYKQHLAQYKRWLKSDILIRVEKHLSNLNQALESAIKNKLYSNKVSLHQLYTSRFKNELPNLQHRTQHAKHLLNQLSRRLHFVMANSQETKLQRFARLQEEFSFMIQHLLTKAKERCQSVQEQMASLNPKNVLKRGFAQLFDFNKHSVIISAESLKQSDLVRVCLQDGEAVLSVKEVWLNNDKKG | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q9PK65 |
P14083 | LOV_DROME | Tyrosine kinase-related | Sophophora | MLKDAHQKLIKHRQSTKLSMTDFACQAAPVKQPLPLELPLPLSVQLQLLAKTPTSDHAPMHSTPPTTPPTPPPLPLNMSQSASAVTEAATPENSLPATPPSEGALAVPSAPQDHYSLRWNNHQNHILRAFDALLKTKTLVDVTLVCAETSIRAHKMVLSACSPFFQRVFAETPCKHPVIVLKDFRGWVVQAIVDFMYRGEISVPQQRLQTLIQAGESLQVRGLVESSVPEHTPTPAASPDDFGMLDTSMLSSTFEDECPTMVRPSKGGKLLMPSARLFGNASSAIAALGLRRKREQESDRDLESDQELGGSSPMPRRKQARPRRRSGDVPHDFTLNKTDAESLQTVIKHELLERAERDQEEAPDQDNSQGEAEKISSSPAKTLVERAKEQKSMKEEGSDQPRSLNENHHQLELDDEDDDDQDHEEEEEQDIEELIHTTNELRRQAAAAAANAAAMSPNPSPCLSDGPEDLCTTKKGKELISGPSSSADCESNNNNSSKLQDNNQRIMLSLKDIRQLNANPNPTAIHTPTSCSGGNNGLLTFPPPGLRPPGLPDSPPCHMEALEAQMHAAAAAAVAAAGSGEHPFHHMEHQMEMSLAAAAAAAAMHQREPRDPRDGRDHNAFASNLLGPMGMPPFGGHNGGHPGNSGPGNGCPGQAAHERLEESMNRLSKELGKEFGKEFGKEFGKEFGPASPMSLQGPFNAPDGPPHPPSPLPFPGMSSAMTLTPPHMFGLDSPLGLFPPGIDPGKLYNPLMEMSDPRDMPGGPPPFLKKKMPRPKGQHSAPRGGPPRSWTNTELTEALQHVWNKKMTTSQASRIFGIPYNSLLMYVRGKYGKSLKLEQLRKDCISGPPIEMLQMGIGGGSGGSTKNEKSKERKEKEKDKNSMSSNGSGGSANSQGGAPTSGSGPMQHSGELGPMGQLDLDLGLPLGPPGGPRSNSSEPDLLSAPNALFNPFNPQGFYPDFSGGFPGLPLSMLNLLPPAERHHAAAAMHHLGVSMDEDCKSVGSKQSSSVDEDYSGPGIPLSLEHRREISATGPPLTPSNGGTGHD | Has a regulatory role during midline cell development. | P14083 |
B1LF98 | LSRF_ECOSM | 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase | Escherichia | MADLDDIKDGKDFRTDQPQQNIPFTLKGCGALDWGMQSRLSRIFNSKTGKTVMLAFDHGYFQGPTTGLERIDISIAPLFEHADVLMCTRGILRSVVPPATNKPVVLRASGANSILAELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMVRDQRYFSLATRIAAEMGAQIIKTYYVDKGFERIVAGCPVPIVIAGGKKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMKAVQAVVHHNETADRAYELYLSEKQ | Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA. | B1LF98 |
Q72PK6 | SYT_LEPIC | Threonyl-tRNA synthetase | Leptospira | MYQLTLPDKSIKEVASGFTYRDFIEKELPFLKNKALAVRLNGEEILDLSRTVEKNSNIEVLTYSEKLGWETFQHSAAHLLGMAVQNLYKNANLTVGPVIDNGPGFFYYDIDFQGAIVTPEDFPKIEAEMEKIVKADHPVWRKVVSKKQAIETFQKLGEKYKIEIIDGIPSEEVSIYGMGEWFDLCRGPHVPNSGVLKSFKLTAISGAYWKADKNNSMLTRIYGVAFPTKKELDQYLFQIEEAKKRDHRKIGKEMDLFSFQKEGPGFPFWHPKGTILWNSLAEYLRSECNKRGYQEIKTPAVLSSELWKKSGHWDNFHENMYFTDIDEEDYALKPMNCPGCSLIYKHHLHSYRELPLRFAEFGSVHRHELHGVLHGLFRVRAFTQDDSHIYAPLDYLESEVMDIIDFTFTVYKKFGFSEFKTFIATRPEKSQGKDEDWEFATSTLKQSLEKKGIPYGIKEGEGAFYGPKIEFNIKDSIGRLWQCGTIQVDFSMPERFDLDYTDSDGQKKRPVMIHRAIYGSLERFIGILIEHYEGKFPLWISPNQIRILTVTEKVTDYAKNVYRELLDSGFRVELDTRNEKIGAKIRDSILKKANYLLILGEKEMESNTLAVRMRGQEDTKILTRTGFISNLQDEIKSS | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q72PK6 |
B4E8E6 | PAND_BURCJ | Aspartate 1-decarboxylase alpha chain | Burkholderia cepacia complex | MQRHMLKSKIHRAAVTHCELHYEGSCAIDEDLLEAAGLIENERIDIWNINNGERFSTYAIKGERGSGMISLNGSAARRAQLGDLVIIAAFAMVDEAELQAGWKPKLVFIDEGNKIKGHRDHVPTQNWT | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | B4E8E6 |
B3PXB0 | UREE_RHIE6 | Urease accessory protein UreE | Rhizobium | MQRVTSYLPAGTPSSHPTAQVKLPHDLRHLRRKLLHLENGEMVMLDLKDPVLFANGDLLVREDGELIEILAADEKLFEIRGRDRTHLVELAWHLGNRHLAAQIEEDRIVILRDHVIRNMLQGLGATVLEINEPFQPARGAYHSHGGHSHDHGHAAHDHGHAAHDHGHNHDHDHGHAHGHDHQHDHNCDHDHDHGHHHGHKHD | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B3PXB0 |
Q7Z3Y8 | K1C27_HUMAN | Type I inner root sheath-specific keratin-K25irs3 | Homo | MSVRFSSTSRRLGSCGGTGSVRLSSGGAGFGAGNTCGVPGIGSGFSCAFGGSSSAGGYGGGLGGGSASCAAFTGNEHGLLSGNEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELIEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIDGEDGSCSKSKGYGGPGNQTKDSSKTTIVKTVVEEIDPRGKVLSSRVHTVEEKSTKVNNKNEQRVSS | Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs). | Q7Z3Y8 |
Q9AMS6 | PAND_BRADU | Aspartate 1-decarboxylase alpha chain | Bradyrhizobium | MQITLMKGKIHRASVTEADLHYEGSISIDRTLLEAAGMVINERVEIYNVETGTRFATYVIEAPPMSGTMSLNGAAARLVMPGDKIIIVAYASFDEAEAKKFKPHVVRVDRDNRILAS | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | Q9AMS6 |
Q033H5 | PTH_LACLS | Peptidyl-tRNA hydrolase | Lactococcus cremoris subsp. cremoris | MTKMIVGLGNPGDKYEKTKHNMGFMALDLLANELNVDFKEEKPFMSLVASTFVNGEKLFLVKPLTFMNESGRAVAPLLKYYNIDEADLTVMHDDLDSPVGRVRLRQKGSSGGQNGIKSVITHVGSQTFNRVKIGIGRPKHGMTVVNHVLSGFDNEDKEIAQDGIFKAVDAMKFYLENGDFQKTMNKFN | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q033H5 |
Q311P4 | THIG_OLEA2 | Thiazole synthase | Oleidesulfovibrio | MEHTTTHNNDPLVLGGRALESRLFIGTGKYGSDSLIPRVAEASGAQVITVALRRVDMQAAAGNVMQHIPQHMQLLPNTSGARTAEEAVRIARLARAAGCGDWIKIEVISDSRYLLPDGYETAKATEILARDGFVVLPYMNPDLYVARDLVSAGAAAVMPLGAPIGTNRGLRTQEMIGILIEEIELPVIVDAGIGRPSQACEAMEMGAAACLVNTAIASAGDPVLMASAFGAAVRAGRRAWLAGTGAVLEGQAQASSPLLGFLDS | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q311P4 |
A3PEX6 | RS20_PROM0 | 30S ribosomal protein S20 | Prochlorococcus | MANNKSAKKRIQIAERNRLINKSYKSTVRTLTKKTLENCEKYKKEPNDENKNLVTTSLNKAFSLIDKAVKKNVLHKNNGANRKSKINNFVKTTLTTK | Binds directly to 16S ribosomal RNA. | A3PEX6 |
P33919 | RADD_ECOLI | Putative DNA repair helicase RadD | Escherichia | MIFTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRVLVLAHVKELVAQNHAKYQALGLEADIFAAGLKRKESHGKVVFGSVQSVARNLDAFQGEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGKGWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIFAATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAGNPHDLYAPEVGTPKGKSDNVPVQVFCPACGFANTFWGKTTADGTLIEHFGRRCQGWFEDDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDTVLVDPDDMLKAALRLKDALVLRCSGMSLQHGHDEKGEWLKITYYDEDGADVSERFRLQTPAQRTAFEQLFIRPHTRTPGIPLRWITAADILAQQALLRHPDFVVARMKGQYWQVREKVFDYEGRFRLAHELRG | RadD contains helicase motifs, suggesting it may be a helicase, although that activity has not been observed (Probable). In combination with RadA is important in repair of double-strand DNA breaks (DSB) . Has DNA-independent ATPase activity that is stimulated by single-stranded DNA-binding protein SSB. ATPase is stimulated by a peptide with the last 10 residues of SSB, but not when the peptide's last Phe residue is missing. Binds ssDNA; binding is slightly better in the presence of nucleotides . May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds to DNA structures with 3 branches that resemble replication forks . | P33919 |
Q8X878 | KEFB_ECO57 | K(+)/H(+) antiporter | Escherichia | MEGSDFLLAGVLFLFAAVAAVPLASRLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSKLWQLRRSIFGVGAAQVLLSAALLAGLLMLTDFAWQAAVVGGIGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALVPLLAGSADEHFDWMKIGMKVLAFVGMLIGGRYLLRPVFRFIAASGVREVFTAATLLLVLGSALFMDALGLSMALGTFIAGVLLAESEYRHELETAIDPFKGLLLGLFFISVGMSLNLGVLYTHLLWVVISVVVLVAVKILVLYLLARLYGVRSSERMQFAGVLSQGGEFAFVLFSTASSQRLFQGDQMALLLVTVTLSMMTTPLLMKLVDKWLSRQFNGPEEEDEKPWVNDDKPQVIVVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMRKYGYKVYYGDATQVDLLRSAGAEAAESIVITCNEPEDTMKLVEICQQHFPHLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKTLVTLGMHPHQAQRAQLHFRRLDMRMLRELIPMHADTVQISRAREARRELEEIFQREMQQERR | Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. | Q8X878 |
A7NAH6 | GCST_FRATF | Glycine cleavage system T protein | Francisella | MLKTPLYESHIAANAKMIDFSGWSMPINYGSQIQEHNNVREDCGIFDVSHMLAVDIQGSEAEKFLRYLLANDVAKLQENKAQYGCMLNHDAGIVDDLITYKVTDEHFRIVVNAGNRESDVAWFNQNAQNFDVAITPQTDLAIVAVQGPKAVAVIKRVVTKEIAAEIEALLPFSFKFFSKWMVARTGYTGEDGFEVILPATQVKKFWDSLLENGAQPAGLGARDTLRLEAGMHLYGADMDTSTTPLERGLGWSVDLSDEHRDFIGKKAYLAKKAQGVDTKWVGVVLKTKGVLRAGQEIDFDNGEKGYITSGSFSPTLKVAIGLAYVPKQADNPVVNIRGKELEVELVKPKFVKNGKSLI | The glycine cleavage system catalyzes the degradation of glycine. | A7NAH6 |
Q2SWD4 | HISZ_BURTA | ATP phosphoribosyltransferase regulatory subunit | pseudomallei group | MSTWLLPENIADVLPSEARKIEELRRRLLDRFRSYGYEMVMPPLLEYLESLLTSGGNELRLRTFKLVDQVSGRTLGLRADMTPQVARIDAHLLNRQGVTRLCYAGPVLHTRPRGLHASREQLQIGAEIYGHAGLEADQEIQQLMLDALHLAGLKKIRLDLCHAGVLAALFARDAAAAGRGEALYEALAGKDVPRLNELTDDLGADTRAALRALPRLYGDASVLDEARRQLPALPEIARALDDLAHLASQVKDAEVAIDLADLRGYAYHSGAMFAAYVDGVPNAVAHGGRYDHVGQAYGRARPATGFSLDLREIARISPVEARGAAILAPWKQDDALRAAVGALRDAGEVVIQALPGHDHVLDEFACDRALVERDGAWVVEPR | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | Q2SWD4 |
Q9C1B5 | TRI10_FUSSP | Core trichothecene cluster (CTC) protein 10 | Fusarium | MEFPKPRQFRETSLLMYYLDVVFPLQYISPNNNCLGKREWLLTILTSARPTYYATLCLALLYKESLSTSCRSEQTLVWKREKTYYYILALQESQKLLGGLNKTFGITRLKGTVVALACMLQLIGFESSHLSRGDWRVHLLAANTLIPVLAEGWSTALQSGPPATSIWCELDESDFDSIDDQTSLSFEYLGALRFLSNSLAKIGILSCISVGPAAPFEDYGHLLDQPGLIQLEEVLGCKNWAMLTILEVGKLDRWKRQEQEHNRLSLKTLAMRAMIIEDMLTDELQKLPTSETLPDLITHIYAASIATYLHTVVSGLNPNLSEVQDSVCATILLLERLPDLQAVASVTWPLAVTGCMASESHKDFFRSTLRSYEATFSSLKKYDGVLEVLEDAWKKREVDTESPMRWEDLMDHHGLPVLLF | Transcriptional activator of all of the trichothecene biosynthesis genes . Acts upstream of the cluster-encoded transcription factor TRI6 and is necessary for full expression of both the other trichothecene genes and the genes for the primary metabolic pathway that precedes the trichothecene biosynthetic pathway . | Q9C1B5 |
A6UYJ0 | THIG_PSEA7 | Thiazole synthase | Pseudomonas | MSQASSTDTPFVIAGRTYGSRLLVGTGKYKDLDETRRAIEASGAEIVTVAVRRTNIGQNPGEPNLLDVIPPDRYTILPNTAGCYDAVEAVRTCRLARELLDGHNLVKLEVLADQKTLFPNVVETLKAAEQLVKDGFDVMVYTSDDPIIARQLAEIGCIAVMPLAGLIGSGLGICNPYNLRIILEEAKVPVLVDAGVGTASDAAIAMELGCEAVLMNTAIAHARDPVMMAEAMKHAIVAGRLAYLAGRMPRKLYASASSPLDGLID | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | A6UYJ0 |
P0A2C6 | RBSB_SALTI | Ribose import binding protein RbsB | Salmonella | MNMKKLATLVSAVALSATVSANAMAKDTIALVISTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAKIPVITLDRQATKGDVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKADVMVVGFDGTPDGEKAVKDGKLAATIAQLPDQIGAKGVEVADKVLKGEKVQAKYPVDLKLVIKQ | Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. | P0A2C6 |
E7D082 | SCX5B_MESEU | MeuNaTxalpha-5b | Mesobuthus | MNYLILISFALLVITGVESARDAYIAKPHNCVYECFDAFSSYCNGVCTKNGAKSGYCQILGTYGNGCWCIALPDNVPIRIPGKCHRR | Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin inhibits inactivation of Nav1.6/SCN8A (EC(50)=790 nM) and drosophila DmNav1 (EC(50)=280 nM) . The toxin (1 uM) does not significantly shift the midpoint of activation at the two channels, but induces a significant depolarizing shift in the V(1/2) of inactivation of the channels . Has antimicrobial activity (Ref.2). | E7D082 |
Q7VEJ7 | GRPE_PROMA | HSP-70 cofactor | Prochlorococcus | MKEEVSTSNQEDLVADQEVIASEESDLSPKEEKVSESTIDDDDSLNDAELQSNKQTLDNEARLEQLEKEHETLRSQYVRIAADFDNFRKRQSRDQDDLKLQLTCNTLSEILPVVDNFERARQQINPEGEEALTIHRNYQNLYKQLVDVLKKLGVAPMRVVGQSFDPTLHEALLREPSELMVEDMILEELVRGYHLNGRVLRHAQVKVSMGPGPKVDEEDKQIDEDSQADKRDEATTASNELD | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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. | Q7VEJ7 |
Q4JXU4 | GCSH_CORJK | Glycine cleavage system H protein | Corynebacterium | MTALPTDFLYSEEHEWVNTSAVVEGETVRVGITHIAAEALGDIVFVELPEVGSEVEAGEAFGEVESTKSVSDIYAPVSGEVVAVNEALEDNAGLINEDPYGEGWLYEVKVTEAGELMEAEAYQAANE | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Q4JXU4 |
A0A3Q7HRZ6 | MYC2_SOLLC | bHLH transcription factor bHLH147 | Solanum subgen. Lycopersicon | MTEYSLPTMNLWNNSTSDDNVSMMEAFMSSDLSFWATNNSTSAAVVGVNSNLPHASSNTPSVFAPSSSTSASTLSAAATVDASKSMPFFNQETLQQRLQALIDGARETWTYAIFWQSSVVDFSSPSVLGWGDGYYKGEEDKAKRKLSVSSPAYIAEQEHRKKVLRELNSLISGAPPGTDDAVDEEVTDTEWFFLISMTQSFVNGSGLPGQALYSSSPIWVAGTEKLAASHCERVRQAQGFGLQTIVCIPSANGVVELGSTELIVQSSDLMNKVRVLFNFSNDLGSGSWAVQPESDPSALWLTDPSSSGMEVRESLNTVQTNSVPSSNSNKQIAYGNENNHPSGNGQSCYNQQQQKNPPQQQTQGFFTRELNFSEFGFDGSSNRNGNSSVSCKPESGEILNFGDSTKKSASSANVNLFTGQSQFGAGEENNNKNKKRSATSRGSNEEGMLSFVSGTVLPSSGMKSGGGGGEDSEHSDLEASVVKEADSSRVVEPEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELKSKLQNTESDKEDLKSQIEDLKKESRRPGPPPPPNQDLKMSSHTGGKIVDVDIDVKIIGWDAMIRIQCNKKNHPAARLMAALMELDLDVHHASVSVVNDLMIQQATVKMGSRHYTEEQLRVALTSKIAETH | Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in the promoter of the jasmonate-induced gene LAPA1 . Acts as negative regulator of blue light-mediated photomorphogenesis and positively regulates root growth . Promotes growth in response to the phytohormones abscisic acid (ABA) and jasmonate (JA) . Binds to the G-box motif (5'-CACGTG-3') of the RBCS-3A gene promoter . Acts downstream of the jasmonate (JA) receptor to orchestrate JA-mediated activation of plant responses . Positively regulates both wound-responsive and pathogen-responsive genes through MYC2-targeted transcription factors (MTFs) involved in early response to JA . With JA2L forms a transcription module that regulates wounding-responsive genes . With ERF.C3 forms a transcription module that regulates pathogen-responsive genes . Plays a critical role in orchestrating JA-mediated defense gene expression during Botrytis cinerea infection . Regulates negatively defense responses to root-knot nematodes, potentially by mediating crosstalk among the hormones strigolactones, abscisic acid (ABA) and jasmonate (JA) . Regulates the termination of JA-mediated defense responses by specifically binding the G-box (5'-CACATG-3') motifs in the promoters of MTB1, MTB2 and MTB3, which are transcription factors that negatively regulates JA signaling . May be involved in JA-induced chilling tolerance, possibly by ameliorating the antioxidant enzyme system of fruit and increasing proline and lycopene levels . | A0A3Q7HRZ6 |
O32143 | XDHE_BACSU | Probable xanthine dehydrogenase subunit E | Bacillus | MDIKEAGPFPVKKEQFRMTVNGQAWEVAAVPTTHLSDLLRKEFQLTGTKVSCGIGRCGACSILIDGKLANACMTMAYQADGHSITTIEGLQKEELDMCQTAFLEEGGFQCGYCTPGMIIALKALFRETPQPSDKDIEEGLAGNLCRCTGYGGIMRSACRIRRELNGGRRESGF | Oxidizes hypoxanthine and xanthine to uric acid. | O32143 |
Q88M07 | SERC_PSEPK | Phosphohydroxythreonine aminotransferase | Pseudomonas | MSKRAFNFCAGPAALPDAVLQRAQAEMLDWRGKGLSVMEMSHRSDDYVAIAEKAEQDLRDLLSVPSNYKVLFLQGGASQQFAEIPLNLLPENGTADYIETGIWSKKAIEEARRFGNVNVAATAKPYDYLAIPGQNEWNLTKNAAYVHYASNETIGGLQFDWVPQTGDVPLVVDMSSDILSRPIDVSQFGLIYAGAQKNIGPSGLVVVIVREDLLGHARSSCPTMLDYKVSADNGSMYNTPATYSWYLSGLVFEWLKEQGGVEAMEQRNRAKKDRLYGFIDRSEFYTNPISVNARSWMNVPFRLADERLDKAFLAGADARGLLNLKGHRSVGGMRASIYNALGLEAVEALVGYMAEFEKEHG | Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. | Q88M07 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.