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
Q9YF87
RL5_AERPE
50S ribosomal protein L5
Aeropyrum
MSAKAQSLPIPPERVSEILDEWKRSPMRRPRIVKVTVNISIGQSGERLQRAAEVLEELTGQKPVFRKAKRTIRAFGVRKGENIAVMVTLRGEKALNFLKRALDAVGHRIKTSSIDEHGNVSFGIEEHILIPGVKYDPRVGILGMDVAITIQRPGHRIVERRRQRRGHIPRRHRVTREETMVLLNQLFGVTFV
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Q9YF87
Q54TA5
TBC5B_DICDI
TBC1 domain family member 5 homolog B
Dictyostelium
MDTSGFLDLDINSGTTTPNIRNSVTTSNDIMSSIFDTIPTKEKKVDAAVESIFGTEAANSPLISSSIPPIPIEASTSTQQQQQQQQQQEEIIPSQPISVTKENTVTTTTTTTATTAVPTTTTTPTSTLINSEPIVVNPLEVNINTKVDDSDSDQDEQIKKENVVHEIFTPIVSIINNNNNNNNNEIDNNNNGNSNENTTTTTTNKDMNNSFSMGVTTASKDEHIISTTTVGTIEQEIHEKQEEPLISPLQSEFNKIFFSTIPLEKKPLEILKMNAFTGALKYSPLRGIAWKLFLGGLDINRVDKWERDITQQRKRYEKLKEEHCFDPRNSNSTYDPLSQNDDSPWNKFFKNLDTQKIIKIDLERTHPDNDFFSNPVIREMMATILFVYSKTNGIISYRQGMHELLAPIIYLYNQEYSSYKKLDENSSSTLVDFIYNIKYLEHDTFAIFERLMKFTSDWYAPAPTQQTNNSNNSNNTNNNNTTTSPSSSSSSSSSSTTTAAATTVSSSTSTSSSSSTITSSSSSTVSPPPPSSSSSPSPPPPPPLGSNSPTVASSSSSSVQDNEEEELSSKCNDVVLKCKYIHSILLKQKDFELYQHLDSLDIEPQIYLLRWIRLLFGREFHFDDVLNIWDALFAYGENLILIDYFCISMLTYIREHLLKSDSIYALKRIYKYPPVEDVYMLIKKALEIKDSNCSIAGMVKTAQPPTTLSSSGSRQIPNNNNNNNNNNNNNNNNNNNNNNSNNNINNNNNNSNNNITTPSTQANTLPFPETSTFESTTSSFQPYSSQLSSANTTPIDPLSNKTTPLISSTSNVSNTPNITSTSTLLSSSSSSSSSTTTPLQSHTPILTHNNNNSHFSPSPSSSSSSLNNSSHVSIPVKSNVKDIFANSKESDLFSLFSTATTPINNNTSSLSISNPTISIGQARTLNKHKSMTLPSSPLISQDSEALKQLKNTQIEFGNQLKEVLPFLEKGKNFLLGNEDELSKSEIDDFIKALEKVKQIQEILSNNNINNNNENKL
May act as a GTPase-activating protein for Rab family protein(s).
Q54TA5
A8EV74
ATPF_ALIB4
F-type ATPase subunit b
Aliarcobacter
MKRILLLGLALAPVALFASQGAVETDIVQRTVNFIIFAAILWYLLADKIKAFFANRTLSIQAELDKVQETLKASQDKVTDAQKKLEEARKLAAEIIESAKTDIDSVKQKVTTAVDADITNLNRNLEEMMKIETSKAKKQVVAEVLEELLSSENIKLTQQELVDVVLKKVA
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A8EV74
P61888
RMLA2_SHIFL
dTDP-glucose synthase 2
Shigella
MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPEDKGYFQRLLGDGSEFGIQLEYAEQPSPDGLAQAFIIGETFLNGEPSCLVLGDNIFFGQGFSPKLRHVAARTEGATVFGYQVMDPERFGVVEFDDNFRAISLEEKPKQPKSNWAVTGLYFYDSKVVEYAKQVKPSERGELEITSINQMYLEAGNLTVELLGRGFAWLDTGTHDSLIEASTFVQTVEKRQGFKIACLEEIAWRNGWLDDEGVKRAASSLAKTGYGQYLLELLRARPRQY
Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
P61888
B3PN30
GYRA_META1
DNA gyrase subunit A
Metamycoplasma
MSDDKKDEEKLKKSDENFDDDSKYYEFDDTIKKVFEEEKAKEEDEDEEEIPQEKEGYQVKSQLLETEQNGLQPADLAKVMKSSFIEYAMSVIVSRALPDARDGLKPVHRRILYGMSELGMFHTAPHKKSARIVGDVLGKYHPHGDSSVYEAMVRMAQDFSLRYPLIDGHGNFGSIDGDEAAAMRYTEARMSKIAGVMVDGIKKNTVDFIDNYDGTEKEPTVLPSRFPNLLVSGTSGIAVGMATNIPPHNLGEIIDAVCALAKNPEITIDGLMEFVLAPDFPTGATIFNKAGLIEAYKTGRGSITMRAKANIQELANGKSKIIITEIPYEVKKTEIMEKIADHLKNKRIEGISDFRDESNRDGIRVVIDVKKNAVPEVILNTLYKLTRLQTNFSFNMIALVNGEPKLLNLKECLQVYLDHQIDVTRRRLQFDLEKDLARAHILEGLKICVENIDRVIEIIKKSKTDVDAQAKLCQTFSLSEIQAKAIVDMRLGRLTGLAIEKMNDELDQVNARIAEYRAILSSHEKLIELIIKELQEVKEAYGDKRRSEIRWDVMSSINNEDLIPQKEIVITLSSNNYIKRIDLEEYREQRRGGVGVSTVKTYQDDDIQDVVVANTHADLLIFTDEAKIYRVRGHEIPSGTKQSKGTPIVNIVPTIQKNEKVVKIICVTDYEESQSLITVTERGVIKKTNLKEYELIRKNGKYALSLLEDDHLIDVRVVDQDEEIFIAASNSRINRFNVADVREMGRVARGVGGIRLSDDDKVVSVSSSKDGAYIFSLGAKGYGKLSLVESYRKTKRNAKGVITLNEDKAGKLVYAAAVHGVEDLIIMTQSGIAIRISLRDINVIGRNAKGVKIINLKGRSDQIVGVAKIYDEDATDRELTKEEYIEVTKEIDIDLANE
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
B3PN30
Q6GFF9
DAGK_STAAR
Diacylglycerol kinase
Staphylococcus
MRKRARIIYNPTSGKEQFKRELPDALIKLEKAGYETSAYATEKIGDATLEAERAMHENYDVLIAAGGDGTLNEVVNGIAEKPNRPKLGVIPMGTVNDFGRALHIPNDIMGALDVIIEGHSTKVDIGKMNNRYFINLAAGGQLTQVSYETPSKLKSIVGPFAYYIKGFEMLPQMKAVDLRIEYDGNVFQGEALLFFLGLTNSMAGFEKLVPDAKLDDGYFTLIIVEKSNLAELGHIMTLASRGEHTKHPKVIYEKAKAINISSFTDLQLNVDGEYGGKLPANFLNLERHIDVFAPNDIVNEELINNDHVDDNLIEE
Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway.
Q6GFF9
A1DI57
TPC1_NEOFI
Mitochondrial thiamine pyrophosphate carrier 1
Aspergillus subgen. Fumigati
MSAGGEHLKDEGTRRQVVLSGGIAGLVSRFCVAPLDVVKIRLQLQIHSLSDPASHRDVVGPIYKGTLSTMRAIIKQEGITGLWKGNIPAELMYVCYGALQFTAYRTTTQVLAQLDPHRLPPALESFVSGAVAGGLATASTYPLDLLRTRFAAQGTERIYTSLLASVQDIARNEGPAGFFRGCSAAVGQIVPYMGLFFATYESLRPVLSGLENMPFGSGDAAAGVIASVLAKTGVFPLDLVRKRLQVQGPTRTLYVHRNIPEYRGVFSTIAMIVRTQGVRGLYRGLTVSLIKAAPASAITMWTYERSLKLLHDFRVAE
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
A1DI57
Q9F7V5
MAZF_STAEP
mRNA interferase MazF
Staphylococcus
MIRRGDVYLADLSPVQGSEQGGVRPVVIIQNDTGNKYSPTVIVAAITDGINKAKIPTHVEIEKKKYKLDKDSVILLEQIRTLDKKRLKEKLTFLSESKMIEVDNALDISLGLNNFDHHKS
Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.
Q9F7V5
Q134V2
RS11_RHOPS
30S ribosomal protein S11
Rhodopseudomonas
MGKETTRIRRRERKNIASGIAHVNSSFNNTTITITDAQGNAIAWSSAGTMGFKGSRKSTPYAAQVAAEDVAKKAQEHGMRTLEVEVAGPGSGRESALRALQAAGFTVTSIRDVTTIPHNGCRPRKRRRV
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.
Q134V2
Q48LA4
RDGC_PSE14
Recombination-associated protein RdgC
Pseudomonas
MWFKNLLVYRLTQDVPFDAEALETALATKPARACASQEVATYGFVAPFGKGEDAPLVHISQDFLLIAARKEERILPGSVVRDALKEKVDEIEAEQMRKVYKKERDQLKDEIIQAFLPRAFIRRSATFAAIAPKQGLILVNASSPKRAEDLLSTLREVIGSLPVRPLTVKVSPSATMTDWVKTQKAADNFFVLDECELRDTHEDGGIVRCKRQDLTSDEIQLHLNTGKVVTQLSLAWQDKLSFVLDDKLVVKRLKFEDLLQDQAEQDGGDEALGQLDASFTLMMLTFGEFLPELFDALGGEEIPQGI
May be involved in recombination.
Q48LA4
Q5M237
RECF_STRT2
DNA replication and repair protein RecF
Streptococcus
MWLEKIDIQHFRNYSEASVSFSPHLNIFLGRNAQGKTNILEAIYFLALTRSHRTHLDKELIQFQQNSLKLNGIVHRHSGNLPLEINLSNKGRVTKVNYLKQAKLSDYIGHMTVVLFAPEDLQLVKGSPSLRRKFIDIDLGQIKPVYLSDLSNYNHVLKQRNAYLKSTDKVDINFLSVLDEQLADFGARVIKHRLEFIKQLEEEADGHHSILSNQIERLKISYESNIPIQNSKDIREAFLTILNQNHKRDIFKKNTGVGPHRDDLKFYINDMNASFGSQGQQRSLILSLKMAEIALIKKVTEEFPILLLDDVMSELDNHRQLKLLESIDEEVQTFMTTTSLDHLSNLPPNLKTFLVKNGTIYEKQVD
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Q5M237
Q47HR1
LEU31_DECAR
Beta-IPM dehydrogenase 1
Dechloromonas
MKICVLPGDGIGPEITAQAVRVLNSLDLKFEMEEALLGGGAVDATGNPYPEATQKLARAADAVLLGAVGGPKWDSLPREQRPERGLLGIRKDLNLFANLRPAILYPELANASTLKPEVVAGLDILIIRELTGDIYFGQPRGVREENGERVGFNTMVYSESEIRRIGHVAFQAAQKRDKRLCSVDKMNVLECTQLWRDVMIEISRDYPDVELSHMLVDNAAMQLVKAPKQFDVMVTGNMFGDILSDEASMLTGSIGMLPSASLDDKNKGLYEPSHGSAPDIAGKGVANPLATILSAAMMLRYTFGLEEQALRVENAVKKVLAQGYRTGDIYERGTNKVGTREMGDAVLAAL
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Q47HR1
Q3J144
LHA2_CERS4
LH-2
Cereibacter
MTNGKIWLVVKPTVGVPLFLSAAVIASVVIHAAVLTTTTWLPAYYQGSAAVAAE
Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Q3J144
B0TCJ8
XPT_HELMI
Xanthine phosphoribosyltransferase
Heliomicrobium
MQELKDRILAEGEVIGTHILKVDTFLNHQIDPAFILRMGKELADRFAGAGITRVLTVEASGIAVASAVALSLNVPVVFAKKKQASTQSDVYTSQIYSFTRQESVNITVSKKFLPADDVVLIVDDFLAHGEALKGLVDIVRQSGAGLAGAGIVIEKLFQRGGAALRAEGMRIETLAAIERMEPGKIVFA
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
B0TCJ8
P79953
OVCH2_XENLA
Oviductin
Xenopus
MPTRNLLLGSILLSLAVKGDPGPHRGARCGVSPLGSATELNYLSRIVGGRESKKGQHPWTVSLKRNGKHFCGGTLVSHCHVLTAAHCLLDRNVKLYMRVYIGEYDQILKEETEQMFRVIEIFKHPNFNQSQPMNYDVAVLLLDGSVTFDENIQPACLPNPDDVFEPGDLCVTLGWGHLTENGILPVVLQEVYLPIVDLSSCLHVMSALKGTVVSSYIVCAGFPEGGKDACQGDSGGPLLCQRRHGSWVLHGLTSWGMGCGRSWKNNVFLPHNRKGSPGIFTDIQKLLGWVSSQLNTAVPNKNQESCSMQDGVLSGKSGELIFLKNPMSVTRTMSGAPGFSLSLKTCTSCLNFTHLDIESDFACNLDYLAIYTDSHRLIGKFCGDIPPRSLLISFSSIKLNFFSDFHENRTGFVLYYSAVEPNTYPDSGCGSFAVLFEEGEIQSMNYPENYLSNSRCHWIIHGPSGSYIKLQFEDFALEPSDDCRSDYLAVYQDLAAEDKIETFCGFSLPAPVYSTTAVMHIKFSTDERDNDKGFRATFTFVSPNSLVEDSRQGNMPSTNKKETTAQDSICGVSQVPPIFIYNSIAKVEEAVPHSWPWHTSLQYAGEHVCDGAIIAENWILTTASCVLNRKFNDVWLVDPGIHDLLRPGHNQKGLVKQIIPHPSFSSQTNDFDIALVELDESLQFNSDIFPICLPGKTSELAPASLCVVSGWSLRGKEAEKSTKLQQREVPILTDDACSAHYIQNPGGITDRMLCAGIGTGQDNDSCSEQSGSPLVCLLEKKGIYTIFGIASWGVNCKENSKPGIYTKVSPFIDWIRQIMSDTGQIHSNLGDPKPHPMGNIEPEETAGRDIIQGGFPTNDASSNQNLYIASSCEDVVLLQSPGEIKMETKSQMYPNGFSCQWRIIAPKFQIIKLVMKQVHMSAENGKCCNSLIIYEGISKNKTLKVRFPTDEMVPGTVWSEGSSVTIESPPHPVDPEFGFCLVYSFHSRTQSQDHVVPDSDSSEP
Converts the glycoprotein envelope surrounding the egg from an unfertilizable to a fertilizable form during its transit through the pars recta portion of the oviduct by selectively hydrolyzing the envelope glycoprotein gp43. The egg envelope is converted to a sperm-penetrable form, via an increase in sperm binding.
P79953
Q32A70
RHAS_SHIDS
L-rhamnose operon regulatory protein RhaS
Shigella
MTVLPSVDFFPSGNTSVAIEPRLPQADFPEHHHDFHEIVIVEHGTGIHVFNGQPYTITGGTVCFVRDHDRYLYEHTDNLCLTNVLYRSPDRFQFLAGLNQLLPQELDGQYPSHWRVNHSVLQQVRQLVAQMEQQEGENDLPSTASREILFMQLLLLLRKSSLQENLENSASRLNLLLAWLEDHFADEVNWDAVADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLMKARHLLRHSEASVTDIAYRCGFSDSNHFSTLFRREFNWSPRDIRQGRDGFLQ
Activates expression of the rhaBAD and rhaT operons.
Q32A70
B1ZFJ0
PROA_METPB
Glutamyl-gamma-semialdehyde dehydrogenase
Methylorubrum
MPVLNLKSGFADADDLDTLMAGIGRRARAAGRAMALAPAQTKDLALRAIAEQIRASAATILRENARDVSAAQAAGQTKAIIDRLTLDEGRVAAIAEAVEKVASLPDPVGRQLAAFERPNGLLIERISVPLGVVGVIFESRPNVTADAGALCLKAGNAAILRAGSDSHRTATAIAAAMSEGLARTGLPADAIQLVPTRDRAAVGLMLTGLGGCVDVIVPRGGRSLVERVQAEAKVPVFAHLDGICHVYIAEGADLGMARTVLLNSKMRRTGICGAAETLLVDAAVAKTHLKPLVEALLESGCAVRGDAATQGVDPRVTPADEADWRTEYLDAIISAKVVDGLDAAIAHIEANGSHHTDAIITDDTEAAARFLNEVDSAIVTHNASTQFADGGEFGFGAEIGIATGRMHARGPVGVEQLTTFKYRVHGSGQTRP
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
B1ZFJ0
B5XQ03
RUVC_KLEP3
Holliday junction resolvase RuvC
Klebsiella
MAIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAATNQSLPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHISQNVAQVSETRLNLARGRLR
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
B5XQ03
Q05373
ATPB_SYNP1
F-ATPase subunit beta
unclassified Synechococcus
MVTTAERTNVGFITQVIGPVIDIEFPSGKMPAIYNALRIQGKNAAGLDVAVTCEVQQLLGDNRVRAVAMSSTDGLVRGMEAVDTGAPISVPVGTATLGRIFNVLGEPVDEKGEVNISETLPIHRPAPSFTELETKPSVFETGIKVIDLLTPYRRGGKIGLFGGAGVGKTVIMMELINNIATQHGGVSVFAGVGERTREGNDLYNEMIESGVIDKDDPSKSKIALVYGQMNEPPGARMRVGLSGLTMAEYFRDVNKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTDVGALQERITSTMEGSITSIQAVYVPADDLTDPAPATTFAHLDGTTVLSRGLAAKGIYPAVDPLGSTSNMLQPDIVGSEHYQTARAVQATLQRYKELQDIIAILGLDELSEEDRLTVARARKVERFLSQPFFVAEVFTGAPGKYVTLEETIKGFQMILSGELDDLPEQAFYMVGNIEEAKAKAEKLKA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Q05373
A0LV34
ISPG_ACIC1
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Acidothermus
MTTINLGVPEVPAKSPLAPRRKSRQINVGGVLVGGGAPISVQSMTTTLTADVNATLQQIAELTAAGCDIVRVACPSQDDADALPIIAKKSPIPVIADIHFQPKYVFAAIEAGCAGVRVNPGNIKKFDDKVKEIAQAAKDHGTPIRIGVNAGSLDPRILQKYGKPTAEALVESALWEASLFEEHDFHDIKISVKHHDPMVMVQAYRLLAAQTDYPLHLGVTEAGPLLQGTIKSAVAFGILLSEGIGDTIRVSLSAPPVEEVKVGIGILESLGLRPRKLDIVSCPSCGRAQVDVYKLAEEVQAGLQGFPFPLRVAVMGCVVNGPGEAREADLGVASGNGKGQIFVRGEVIKTVPESQIVETLLEEAMRLAEEMQASGAFGDDQAVGAPIVTVQ
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
A0LV34
B0R4Y7
RPO6_HALS3
DNA-directed RNA polymerase subunit K
Halobacterium
MSDSQHFSRYEKARIIGARALQVAYGAPVLVDTDQTEPILIAAEEYDADALPFTVRREGT
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
B0R4Y7
Q72H91
SP0J_THET2
Chromosome-partitioning protein Spo0J
Thermus
MSRKPSGLGRGLEALLPKTGAGVVRLPLASIRPNPRQPRKRFAEESLKELADSIREKGLLQPLLVRPQGDGYELVAGERRYRAALMAGLQEVPAVVKDLTDREALELALVENLQREDLSPVEEARGYQALLEMGLTQEEVARRVGKARSTVANALRLLQLPPEALEALERGEITAGHARALLMLEPEDRLWGLKEILEKGLSVRQAEALRERLAMAPKRSAEPSPLSLELSRHLGLPVRVVGGKKGKVVIQYRSLEELEALLRRLGYQA
Probably involved in chromosome partitioning. Binds to a plasmid centromere-like site parS. Stimulates the ATPase activity 10-fold of Soj; the first 20 residues may be responsible.
Q72H91
Q0VPI1
LEUD_ALCBS
Isopropylmalate isomerase
Alcanivorax
MEKFVRHDGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDEGFPGQDNAARLVNNDFVLNQPDYQGASILLTRRNFGCGSSREHAPWALMDFGFKAIIAPSFADIFYNNCFKNGLLPIVLSEDNVEALFQVVSSKGGYRITIDLEGQQVIPESGEPLPFEIDEFRKHCLLNGLDEIGLTLNEADAIRAYERSRIEREPWVFADH
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q0VPI1
Q59987
POR_SYNY3
NADPH-protochlorophyllide oxidoreductase
unclassified Synechocystis
MEQPMKPTVIITGASSGVGLYGAKALIDKGWHVIMACRNLDKTQKVADELGFPKDSYTIIKLDLGYLDSVRRFVAQFRELGRPLKALVCNAAVYFPLLDEPLWSADDYELSVATNHLGHFLLCNLLLEDLKACPDADKRLIILGTVTANSKELGGKIPIPAPPDLGNFEGFEAGFKKPIAMINNKKFKSGKAYKDSKLCNMLTTRELHRRFHQETGIVFNSLYPGCVADTPLFRNHYSLFRTIFPWFQKNVTKGYVSQELAGERVAMVVADDKFKDSGVHWSWGNRQQAGREAFVQELSEQGSDAQKAQRMWDLSEKLVGLV
Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Q59987
Q17YQ7
METK_HELAH
Methionine adenosyltransferase
Helicobacter
MKDSFLFTSESVTEGHPDKMADQISDAVLDYIIERDKKAKVACETLVSNGFCVITGELKTSIYAPMQEIAREVVKKIGYTDALYGFDYRSAAVLNGIGEQSPDINQGVDREDGEIGAGDQGLVFGYACKETQMLMPLPIHLAHQLTFALAQKRKDNTLPFLRPDGKSQVSVRYENNKPISIDTIVISTQHSPEVSQKHLKEAVIEEIVYKVLPKEYLHDNIKFFVNPTGKFVIGGPQGDAGLTGRKIIVDTYGGSCPHGGGAFSGKDPSKVDRSAAYAARYVAKNLVASGVCDRATVQLAYAIGVVEPVSIYVNTHNTSKYSSAELEKCVKLVFKLTPKGIIESLDLLRPIYSLTSSYGHFGRELEAFTWEKTNKAEEIKAFFKH
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.
Q17YQ7
Q13BU3
RNH2_RHOPS
Ribonuclease HII
Rhodopseudomonas
MIREPQKSAKAASKSSAPRARSSVAKATSTKATSSKAASSKAAPSKAGADAGAAKPRTKGLGKGVIAVAQPSFRRERALIKRGVWPVAGCDEAGRGPLAGPVVAAAVVLDPKRVPKGLDDSKRLTADRREELFEEICATAQVAVAYASPERINRDNILRASLWALTRAVHALPDLPQHVFVDGRDRLATRCESEAVVGGDGLIASIAAASIIAKVSRDRLMCRLAQECPGYGFESHKGYGVPEHLAALARLGPTVHHRRFFAPVAAAWRKIEGVPAEQTGVTGDLFETPVDAGIAATL
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q13BU3
Q58319
RELE2_METJA
Putative toxin RelE2
Methanocaldococcus
MKQWKYLLKKSFIKDLKELPKNIQEKIKKLVFEEIPNKNNPPEIPNVKKLKGADSYYRIRVGDYRIGFKYENGKIVFYRVLHRKQIYKRFP
Toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin is RelB2 (Potential).
Q58319
A8WUG4
KPC3_CAEBR
Atypical protein kinase C-3
Caenorhabditis
MSSPTSVEEDGDIKLKTRFHGQVVVLYARPPLILDDFFALLRDACKQHAKQDITVKWIDEDGDPISIDSQMELDEAVRCLNVSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQGKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQTPQGPNVPVAPSSGVGSLRGGRLDTSSSTTRSGGGIDNGAFHEHEIESPGSAKDMSRSTNGNGASKWAVSLNDFRLLTVIGRGSYAKVVQAEHIATRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRRLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENINAGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASNILKGFLNKDPSQRLGCKLDINDGLNDMKEHDFFRGFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDEPPQLSPDNSAVIARIDQSEFDGFEYVNPLQMSREDSV
Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphorylates serine residues of num-1. Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury.
A8WUG4
A9AWY7
COAD_HERA2
Pantetheine-phosphate adenylyltransferase
Herpetosiphon
MTIAVYPASFDPITNGHLDVAARASRLFDELVLAVAHRPYKKLLFTTEQRIAMIRESVAHLPNVRVDAFSSLVVEYALEIGATVLVRGLRAATDFEHEFQMAHINHHLAPTLDTVCLMADQRFTLLSSSAVREIAAYGGDVSSFVPAHIALALKQAYQTHEESRA
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A9AWY7
Q4WHD2
RIFK_ASPFU
Flavin mononucleotide kinase 1
Aspergillus subgen. Fumigati
MRPDGPRDPVAGPDSGPEPPYPVRLSGPVIKGFGRGSKELGIPTANIPAEGLEEYPDLQVGVYYGVVALDPAKFQYQEGQGSTSTSSTGGAEAAVLPAVLSIGYNPFYKNKTKSIEIHIMPPLSSPSPTADGAGEVKFHKLPDFYGTQLKLLILGYIRPEYDYVSLEALIEDIRVDCEVARKSLQRPAYACYIDGDEKECSDVVREQRRWLVTF
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Q4WHD2
Q2KV16
NRDR_BORA1
Transcriptional repressor NrdR
Bordetella
MRCPFCGHADTQVVDSRVSEEGDTIRRRRRCLSCDKRFTTYERVELAMPTVVKRDGSRSEYDAAKLRGSLALALRKRPVSTEEVDGAVARIEDTLLASGAREVASEHIGELVMNELKRLDKVAYVRFASVYKSFEDIGEFVEAIREMQGPRLGAGKLRKE
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Q2KV16
O81796
IDH3_ARATH
NAD(+)-specific ICDH 3
Arabidopsis
MARRSVSIFNRLLANPPSPFTSLSRSITYMPRPGDGAPRTVTLIPGDGIGPLVTGAVEQVMEAMHAPVHFERYEVLGNMRKVPEEVIESVKRNKVCLKGGLATPVGGGVSSLNMQLRKELDIFASLVNCINVPGLVTRHENVDIVVIRENTEGEYSGLEHEVVPGVVESLKVITKFCSERIARYAFEYAYLNNRKKVTAVHKANIMKLADGLFLESCREVAKHYSGITYNEIIVDNCCMQLVAKPEQFDVMVTPNLYGNLIANTAAGIAGGTGVMPGGNVGAEHAIFEQGASAGNVGNDKMVEQKKANPVALLLSSAMMLRHLRFPTFADRLETAVKQVIKEGKYRTKDLGGDCTTQEVVDAVIAALE
Performs an essential role in the oxidative function of the citric acid cycle.
O81796
Q9D2K4
IQCH_MOUSE
IQ domain-containing protein H
Mus
MAQAQEDSDPIGSILIQVHEDLHQLKEKLVKFSAEETRSTLDIQNLETAIQRTEMGLKIHIDKYLGVVNQEVLMAPVKKSLESPVTSKWSIPTVIDQKSFIFPMDSDFWRPQKHRGSLLHGLRRAKPKIQLTTKVMQDPENKHHRAAVTASYGISLPHINQRKAQDKVQRLIKGSTISNLTVLPPSHRTDPHFIPIPVLQKDASKGVLSMIERGLIPPTARITFQNPPIKPQALPLHSFDEHRKVPMEASFPLALKPRPVPEEVEEPSHQIEIPKGRAKRSRGPLRRKGMKIRTPSKTRKSPWDYIFSVYNGCVDRTAPDFLAFKSRFKLIWGSIFSFLEQIEKFLKDYAISEAKIKGKSLVSLLPEFELKNKLTRNDVLAVLENPVHIQMLLNLPGQRYKGQDGKAEAATKIQATWKSYKARSSFISYRQKKWASGVIALAWLLHCHRTRLKRIVKESRQRHLENFRIRAQHLAANWSRIRTSRRTIIHIPSLGYSQYVRKHIFDLDVEQNMQLGRLCDIIDANVNVIYICSHPMTDELKLYYRKLLSLQAAVKTGYYGDRTDLQNRFRIITPEAVNVFTKHHMCLATHLMYSPKAIKRIKNLIRGEEAYIVGGILHRDDLAVADMLNVPILGSEPELVHLYSAKSGSKRIFDNANVPMPPGIYDIYTYQQMIEQLSQLVTDNLGIRRWVFKMNTEFGGNGTAFCDIPSHLQCYNWVLKERNRFGHEDWKKKWAQESALVKISEELAGILAQHVQLVNEKRFPTWRKFLHMFLTQGGVIEAYPPADSVTNLTVDMLIEPDGEVRVLSMGDQLHADGPFISSGTTMPQTSVDPQVLNSLCLQIGNICKEKDVVGYFSIDLVTFIDPSTLEQQVWTTGLNLSYSDQLAMTQLTLYLTNGHLNCSLSTLEVPRFTEDSERERKRLSIQAELAPETSRYAVMSTQLKHDNLSLIFYYVFLQMCKAHGIGYDLEDRQGTVFILYESLKRYKLGMLTIGVDLQGVLMTFARNLFIIHQEISAPDMQGETNFKTTIDDIETILGVTEENKMIFVREKQSKEEEDNLYEPVEIHSEIV
May play a regulatory role in spermatogenesis.
Q9D2K4
Q8WI04
PSBE_PSINU
PSII reaction center subunit V
Psilotum
MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQEIPLITGRFNSLEQVDEFTRSF
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q8WI04
Q5QVQ6
GLUQ_IDILO
Glutamyl-Q tRNA(Asp) synthetase
Idiomarina
MYRGRFAPTPSGPLHLGSLVAAVGSYLDAKAHRGEWLVRIEDVDKPRAVPGAADTILTQLEAHGLEWDGSVLYQSQRDSVYQHQLNQLENAQRLYQCDCSRRAIRARSDHYDGYCRNRQPRSTPYALRFINNNPVDTFNDRAHGLLEDHSASVSEDFVLKRRDGLYAYQLAVVVDDIEQGITDIVRGSDLITPSFWQLTLWQYFTGKQPRMMHLPLIMNDDGLKLSKQNHAPSIESSQARNNLFTALDYLGIKPESELRHSPVSEILQQALQSWCKKWHIAGR
Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
Q5QVQ6
Q2S6K8
NUSB_SALRD
Antitermination factor NusB
Salinibacter
MSSRRDAREQVMKTLYANEQTDGDAEQALHALVRVPLDEDPSTRDFAEHLFRETLKTMEEADEIIEKHADNWEIHRIAAIDRSLLRMATTELLKFEEVPPKVSVDEAIEIAKRYSTPRSGTFVNGVIDAILLDLHDQGRLNKTGRGLIGMDTIQERAGSS
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Q2S6K8
A5GIT1
RL6_SYNPW
50S ribosomal protein L6
unclassified Synechococcus
MSRIGKSPIPIPDKVSVSLDGLAVTVKGPKGELKRTLPDGVTVNQVDNTIVVAPTSEKRQSRERHGLCRTLVANMIEGVSKGYSKKLEIVGVGSRAQVKGKTLVVSAGYSHPVEMLAPEGITFAVENNTNVTVSGTDKELVGNEAAKIRAIRPPEPYKGKGIKYAGERILRKAGKSGKK
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.
A5GIT1
Q2NCY7
DDL_ERYLH
D-alanylalanine synthetase
Erythrobacter
MSLDRKLHVVVLMGGWANEREVSLMSGEGVAKALEKRGHTVTRIDMDRQVAAKIAEAAPDVVFNALHGVPGEDGTVQGMLDLMGVPYTHSGLATSVIAIDKELTKQQLVPRGIPMPGGRIVQSEDLYQQDPLARPYVLKPVNEGSSVGVAIVTDESNYGNPIRRDAPGPWQEFRELLAEPFIRGRELTTAVVGGQALAVTELKPKSGFYDFDAKYTDGMTEHVCPADIPPEIEALCKKYALEAHRILGCRGTSRTDYRWDDEQGDDGLFVLETNTQPGMTPLSLVPEQAAYAGMSYEDLVEAIVEAALEHFAAKTGGNDGDQG
Cell wall formation.
Q2NCY7
Q96P47
AGAP3_HUMAN
MR1-interacting protein
Homo
MNFQAGGGQSPQQQQQLAGGPPQQFALSNSAAIRAEIQRFESVHPNIYAIYDLIERIEDLALQNQIREHVISIEDSFVNSQEWTLSRSVPELKVGIVGNLSSGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPELQFAAWVDAVVFVFSLEDEISFQTVYNYFLRLCSFRNASEVPMVLVGTQDAISAANPRVIDDSRARKLSTDLKRCTYYETCATYGLNVERVFQDVAQKVVALRKKQQLAIGPCKSLPNSPSHSAVSAASIPAVHINQATNGGGSAFSDYSSSVPSTPSISQRELRIETIAASSTPTPIRKQSKRRSNIFTSRKGADLDREKKAAECKVDSIGSGRAIPIKQGILLKRSGKSLNKEWKKKYVTLCDNGLLTYHPSLHDYMQNIHGKEIDLLRTTVKVPGKRLPRATPATAPGTSPRANGLSVERSNTQLGGGTGAPHSASSASLHSERPLSSSAWAGPRPEGLHQRSCSVSSADQWSEATTSLPPGMQHPASGPAEVLSSSPKLDPPPSPHSNRKKHRRKKSTGTPRPDGPSSATEEAEESFEFVVVSLTGQTWHFEASTAEERELWVQSVQAQILASLQGCRSAKDKTRLGNQNAALAVQAVRTVRGNSFCIDCDAPNPDWASLNLGALMCIECSGIHRHLGAHLSRVRSLDLDDWPPELLAVMTAMGNALANSVWEGALGGYSKPGPDACREEKERWIRAKYEQKLFLAPLPSSDVPLGQQLLRAVVEDDLRLLVMLLAHGSKEEVNETYGDGDGRTALHLSSAMANVVFTQLLIWYGVDVRSRDARGLTPLAYARRAGSQECADILIQHGCPGEGCGLAPTPNREPANGTNPSAELHRSPSLL
GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway.
Q96P47
O14027
PDX1_SCHPO
Probable pyridoxal 5'-phosphate synthase subunit PDX1
Schizosaccharomyces
MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.
O14027
B1YPZ0
DNAA_BURA4
Chromosomal replication initiator protein DnaA
Burkholderia cepacia complex
MNDFWQHCSALLERELTPQQYVTWIKPLAPVAFDASANTLSIAAPNRFKLDWVKSQFSGRISDLARDFWNAPIEVQFVLDPKAGMRSAAAHAAPAAQRAPLTPNGPAATVAAIAANLAANAGAAPSAPADVPMTASAAAAHHLNADDADIDLPSLPAHEAAAGRRTWRPGPGAAPANGGEADSMYERSKLNPVLTFDNFVTGKANQLARAAAIQVADNPGISYNPLFLYGGVGLGKTHLIHAIGNQLLLDKAGARIRYIHAEQYVSDVVKAYQRKAFDDFKRYYHSLDLLLIDDIQFFSGKSRTQEEFFYAFEALVANKAQVIITSDTYPKEISGIDDRLISRFDSGLTVAIEPPELEMRVAILMRKAQSEGVNLSEDVAFFVAKHLRSNVRELEGALRKILAYSKFHGREISIELTKEALKDLLTVQNRQISVENIQKTVADFYNIKVADMYSKKRPANIARPRQIAMYLAKELTQKSLPEIGELFGGRDHTTVLHAVRKIADERSKDAQLNHELHVLEQTLKG
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
B1YPZ0
O09101
PIGF_MOUSE
Phosphatidylinositol-glycan biosynthesis class F protein
Mus
MKDTDIKRLLYTNLLCVFSIFLSIFIPSFFVDNFSVLEAHLTWLCICSASVTTVNLLSYLVVKPNVSSKRSSLSHKVTRALKCCVCFLMSCFLLHIIFVLYGAPLIELVLETFLFAVVLSTFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFTGAWLGAFPIPLDWERPWQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI.
O09101
B0C1E2
RS17_ACAM1
30S ribosomal protein S17
Acaryochloris
MAIKERIGVVVSDKMDKTVVVAVSNRVPHKKYGKIVGQTRRYKAHDEENACHVGDRVRIRESRPLSRTKRWAVTDVLVAANRP
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
B0C1E2
O06430
DNAK_NITEU
Heat shock protein 70
Nitrosomonas
MAKIIGIDLGTTNSCVAVMEGNKPKVIENAEGARTTPSIVAYAEDNEILVGASAKRQAVTNPENTLFAIKRLIGRRFDEEVVQKDISVTPYKIVRADNNDAWIEARGRKIAPPEVSAQVLIKMKKTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAFGLDKKEGDRKIAVYDLGGGTFDISIIEIAEVEGEHQFEVLATNGDTFLGGEDFDSRVIEYLVDEFRKESGIDLKKDMLALQRLKDAAEKAKIELSSSQQTEVNLPYITADASGPKHLAVKITRAKLESLVEELIERTAGPCRTALKDAGLSVSDINDVILVGGQTRMPKVQEKVKEIFGKEPRKDVNPDEAVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMTKLIQKNTTIPTKAQQVFSTADDNQTAVTIHVLQGEREVASGNKSLGQFNLTDIPSAPRGMPQIEVIFDIDANGILHVSAKDKATGKENKIKIQASSGLSEDEIQKMVKDAEAHAEEDKKALDLVNSRNQCDAMIHSVRKSLAEYGDKLEGDEKSRIEAALKEAEEALKSGDKQTIDAKTQALTEASHKLAEKMYAQEQAQAGQQAGAGTASDQSQDKPVEGEVVDAEFEEVKDKK
Acts as a chaperone.
O06430
Q553R3
IF4G_DICDI
Eukaryotic translation initiation factor 4 gamma
Dictyostelium
MNFRYQPNQQPYQPPQHNNNSNNRGIPTNYQQYPPQNYQQYPPQQYYQAPINPQQFYPGPPQQPNFVSQQTGPIPQQPPGFNNQSPIPQQQPQQPQQPQPSQPSPIPQQPLSPQSSSPSSPQHVVIQPNQPNQQQQNANRKQSALKPSVQHNTIPNIPRTHSAPPSLEEQQQQHQHQNNIKGFTPEKRTPIQHSPQYVIPPQQFGKPIYPNPQQMYFQQQPPYPYYGQPPVVPVVNQMIPQTTVKKTLEIIDPKTNEKVIITSPPKSSTNSTVLPTSNTSSSSSSPTNANGSSTPSGSGYVTSFSSGNVNLRKNKQSGETTPIKQDAASTTTSTPATPSSKAESTTEAETTSKPSTPTTVDSVSSTTTPDKSNVVTAAATTTAAATTTTTTTDTTTTTTTPEAETSTTTPATEVQSPVETTKEEQPKEEVKPTEVQPPVEPTKEEPIKEEPTNEEPTKEEPAKVEPIKEEPSVVESTTTDTKEEPIIVAEEKKQEETPVTPVTEKKEEPIVKPETPVTDSTAASTTVEKESTDSTTTATVSTTAAATTTNGKVEEELEEWEKKGEEDFNIVQSSDSSTSITPATSLVFRNSGEKIVYSKELMMSLKPKSMEEPTGPLKDLKNQIETNTNQNQLNRSGNKIGGNQQNKNMGMGGMNMNPNYPPQMNMKYPPQMNMKYPPKNYNNQVQGQQQQQQGNPNFNKYAPGYQYQQQIQQGMPPPTLQPNPYQPQQATYGITFSRDPVQPSISSQPVNEKRWVPTKVNALDDSQKVLRKANFILNKITPEKFDVLTEELLELGIVDDEKVHKGTIDLIFDKALNESKFCTMYTNLCKKIFEFEKVKKEIAKRAVFEKIGVIETENYHKMSNKQRDEFDQEHNVKAVFRTLLLSTCQKEYEKIPFETVDKVPEDLKPEEKTDFEEGQFKERKRIFGLIKFIGELFKQQMLSEKIVHGIMVSLIGELQRPSEIKLECFCKLLSIVGKTLSQNEQASKYLTSYFQRMQQLVDNSQTLSQRIRFLIQNVMDLKNSNWTLKVDESAKTLKEVEATQNKQEDNRKSNPTGVKNTSNVKNMFNASFNFGGPNVKPMMAPPMNYNKNAPGIKPPAQFQPKPYPYNNNYNNQQQQQQHFGGGNNMMNNNNNNYNRGPMGNMNNNMNNNMNNNNMNNMNSNNSTSNNSANSEIQKKWDAVSTSITDSINEFLELKDEEEFMECVKSYVPSTDLYPHVISQLISTACSKQKDEPLIKKLIFASVFDKKLFTTAQFKSGYELFISSLPDLFEDRPSAFKSVASVFYSFVLNQEGLITITQFANAFTKVLDDCGSSIPKILFEFILQFEDPKKAAQLFVDNKVGVQGFFTEKDFSKITQTAISYNKDLQPFFDIVKL
Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
Q553R3
A6QBQ5
IF2_SULNB
Translation initiation factor IF-2
unclassified Sulfurovum
MDKVKIQEIAEEAGLSNGELIEKAKELGFNVKAANSAISMDDAGILVDFAISGTLPKGFKKPGEKPKLKVVKKKTVEKEPETIVEAPVIEKETAPEKTEVIPEETENTVEESTAAETVESEPETAVIEEIETPAETAKEETVEAAPVVKEVKQRKGISVVSKKAESEAEKGTEIEKPKRRTLSRTGIKIVRKAKPAPVRAATRISMGSGAPTPPSKKKVKKGPAEARETGKKIDIFNHDSMSGDIDSGFGEEEVVLLDFSDKNIYEDMMRQEQKRREEAKKREAANGGPAKGRQPFRPQQRRSLKRGGKRKKYTKEESSEVITSVEIPENVRVYEFAEKVNRSVGEVVKVLFALGMMVTKNDFLSKDEIEILAEEFGVEVSTMNPLDELDYVQAYDEVEDTHLEERPPVITIMGHVDHGKTSLLDKIRSAKVADKEAGGITQHVGAYQVEKNGKKITFVDTPGHEAFTEMRARGAQATDIVIIVVAADDGVMPQTKEAIAHTKAAGVPMIIAMNKMDKESANPDNIKSQLAEIDVMAADWGGEYEFVPVSAHTGLGIDDLLETILLQAEMMELKADPTRKAKAVVVESSVEKGFGPVANVIIKNGTLHVGDNVIVGTTYGRIKAIKLDDGSAVKEIGPSTPAAIVGLNEVPGAGEALVAMDTDKEVRELAEKRAEYDRAKQLSKSTKASLDDLSALIAEGQLKSLPVIIKADVQGSLEAIKGSLEKLRNEEVKVNIIHEGVGGVTESDVTLADASEHAVILGFNVRPTGSVKKKAKELGVEVRTYTIIYDLLDDVKALLGGMMSPVIKEEVTGQAEVRETFVVGKVGTIAGCKVSDGVITRNSKARLIRDGVVVYESKISSLKRFNEDAREVKNGYECGIMLENFNDIKEGDVIETFKDVEEQVTL
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
A6QBQ5
Q29137
CASK_TRAJA
Kappa-casein
Tragulus
VAQVQYQEQLTGCENDERFFNDKTIKYIPIPYLLNRYPSYGLNYYQQRPPALINNQFLPFSFYAKPMAVRSPAQILQWQVPLNAVSAKPCQAPPTTMARRPRPHLSFMAIPPKKDQDKTDTPTINTIVTVEPTTTPTTESIVNTVATLEASSESIASAPETTTVQVTSAEV
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Q29137
Q7NWC1
RECO_CHRVO
Recombination protein O
Chromobacterium
MSQPGRVDKQPGYILHTQPYRETSLLLEVLSRDHGRFSLVARSARRPRSDLRGVLLPFQPLTLSWFGKGELRTLHAADWDGGVRALTGLPLVCGFYLNELMMKLTARDDPEPRAFSVYDRAVRELAGGAPLSTALRRYELRLAQVLGYAPALSRDSRGEAIAADRHYLCRDAALPEPDEHPELAPVGRVVRLPGEALLALDADDYREPATRGHARLLSRVWLSALLGDEPLASRQLLQAIQSLSD
Involved in DNA repair and RecF pathway recombination.
Q7NWC1
B4TQJ5
RPOB_SALSV
Transcriptase subunit beta
Salmonella
MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVVFEIRDNKLQMELIPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDIKHIEVPVEYIAGKVVSKDYVDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETVRVDPTNDRLSALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLRDEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRRVVDGVVTDEIHYLSAIEEGNYVIAQANSNLDDEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGTVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQILEAGLFSRIRAVLVSGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDDEVLRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTSGQITLFDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLLKEIRSLGINIELEDE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
B4TQJ5
Q9LMA1
FMO1_ARATH
Probable flavin-containing monooxygenase 1
Arabidopsis
MASNYDKLTSSRVAIIGAGVSGLAAAKNLVHHNPTVFEASDSVGGVWRSCTYETTKLQSARVDYEFSDFPWPNNRDDTTFPPYLEILDYLESYAKHFDLLKFMKFGSKVIEVRFIGDGETPQMVDLGAYGNLLPGKPVWEVAVQIGDSGDIQWHAFEFVVVCTGKYGDVPRIPAFPAKKGPEMFQGKVMHSMDYCKLEKEEASTLLSGKKVAVIGFKKSAIDLALESALANQGEGGKACTMVVRTTHWGIPHYWVWGLPFFLFYSSRASQFLHDRPNQSFLRTLFCLLFSLLRAVVSKFIESYVLWKLPLEKYGLKPNHSFEEDYASCQMAIIPENFFEEADKGMIRFKKSSKWWFYEEGIVFEDGTTLEADVVILATGYDGKKKLKAIVPEPFRTWLEFPSGVMPLYRGTIHPLIPNMGFVGYVQSSSNLHTSELRSMWLSRLVDEKFRLPSKEKMLDQFLKEMEVTRNSSRFYKRHCISTFSIQHADDMCNDMGLNPWRKSNFLLEAFSPYGSQDYRLGQEEKEDMTA
Required for the establishment of systemic acquired resistance (SAR). Not involved in local defense mechanisms. Confers a salicylic acid-dependent (SA) resistance to virulent pathogens such as P.syringae pv tomato and H.parasitica.
Q9LMA1
Q99Y73
MUTS2_STRP1
Endonuclease MutS2
Streptococcus
MNNKILEQLEFNKVKELLLPYLKTEQSQEELLELEPMTEAPKIEKSFNEISDMEQIFVEHHSFGIVSLSSISESLKRLELSTDLNIQELLAIKKVLQSSSDMIHFYSDLDNVSFQSLDRLFENLEQFPNLQGSFQAINDGGFLEHFASPELERIRRQLTNSERRVRQILQDMLKEKAELLSENLIASRSGRSVLPVKNTYRNRISGVVHDISSSGSTVYIEPRAVVTLNEEITQLRADERHEEGRILHAFSDLLRPHVATIRNNAWILGHLDFVRAKYLFMSDNKATIPKISNDSTLALINVRHPLLSNPVANDLHFDHDLTAIVITGPNTGGKTIMLKTLGLAQLMGQSGLPVLADKGSKIAVFNNIFADIGDEQSIEQSLSTFSSHMTHIVSILNEADHNSLVLFDELGAGTDPQEGASLAMAILEHLRLSHIKTMATTHYPELKAYGIETNFVENASMEFDAETLSPTYRFMQGVPGRSNAFEIASRLGLAPFIVKQAKQMTDSDSDVNRIIEQLEAQTLETRRRLDHIKEVEQENLKFNRAVKKLYNEFSHERDKELEKIYQEAQEIVDMALNESDTILKKLNDKSQLKPHEIIDAKAQIKKLAPQVDLSKNKVLNKAKKIKAARAPRIGDDIIVTSYGQRGTLTSQLKDGRWEAQVGIIKMTLTQDEFSLVRVQEEQKVKNKQINVVKKADGSGPRARLDLRGKRYEEAMQELDHFIDQALLNNMGQVDIIHGIGTGVIREGVTKYLRRNKHVKHFAYAPQNAGGSGATIVTLG
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Q99Y73
Q0HXP1
TORD_SHESR
Chaperone protein TorD
Shewanella
MSNVDINHARALVYQLLSSLFAREIDEQRLKQLTSEQAQLFWTQLGYASEFSAPVANIQKVLNGLTSDEALLELAADYCGLFLVGTKHSASPYASLYLSPEEEPLLFGQQHQQMSEFLHQSQLQVQSHFPEPADHLAVILAYMGHLTCHSEDAAQLSFLNACIDSWLAKFVAKVVECDSKHSNGFYSALATLTLAWVQQDKQQLEQAIN
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
Q0HXP1
Q5X5W9
HISX_LEGPA
Histidinol dehydrogenase
Legionella
MLTIKNWQLLSDNDKRRCLSRPRDNSAIKENVLEIINQVQLSGDKALYDLTKRFDRVNLQYLQISQEKIRQASIPQNALIAIKQAIETISSYHQFLLPENTEISTASGITIRNVYRPIQKVGLYVPGGNKTPLVSSLLMQAIPAKVAGCPIKVLCTPPDAEGEINEHILVAARLCGIDTIYAIGGAQAIAAMAYGTESVIKVDKIFGPGNSYVTQAKTLVAIDADGAAIDMPAGPSEVMILADTEANPEFIAADLLAQAEHGPDSQVILICDECELANQVNQQLEIQMSYLSRIEFIKQSLTNSRIIICSNQSEQLDIINSYAPEHLIINRKNPEPWVEKIVAAGTVFLGSWAAETMGDYVTGSNHVLPTSGFARNHSGLSTLDFMTRFTVQAINQEAIRNLGPAAMTLAELEGLDAHANAVQIRLNTLGD
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Q5X5W9
A5W907
FABV_PSEP1
Enoyl-[acyl-carrier-protein] reductase [NADH]
Pseudomonas
MAIIHPKVRGFICTTTHPKGCELNVRDQIEATRKLGVREDGPKKVLVIGASSGYGLAARITAAFGFKADTLGVFFEKPGTETKAGTAGWYNAAAFDKFAKAEGLYSKSINGDAFSDEARAKVIELIKNEMGGKVDLVIYSLASPVRKLPQTGEVIRSALKPIGQPYKSTAIDTNKDTIIEASIEPATEQEIADTVTVMGGQDWQLWIDALAGANVLAEGARTVAFSYIGSDITWPIYWHGALGQAKQDLDETALRLNQKLAGEVKGGANVAVLKSVVTQASSAIPVMPLYLSMVFKIMQEKGVHEGTQDQLDRMYRDRMYRTDGAPAEVDEKGRLRLDDWELRDDVQNACKALWPQVTTENLFELTDYAGYKKQFLNLFGFERADVNYDEDVATDVKFDCVEL
Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
A5W907
Q24134
NELFD_DROME
Negative elongation factor D
Sophophora
MEVEYDDSGWQGRAKGQTNPEETLEDNPQKTIQECLEKFLTPDYIMEPGIFTQLKRYFQSGGSPEEVISMLSENYKAVAQMANLLAEWLILAGVKVTEVQAMVENHLKEMILKSFDPKKADTIFTEEGETPDWLTEMIDHYTWRSLIYRLAEEYPDCLMLNFTIKLISDAGFQSEITSISTAAQQIEVFSRVLKTSIVKFLNNPDDVHGAIQECARMVCHGQHTYVYSQVLIQVLSQEQKGGFNMKRLSQEIIKYALQNNQNVTPITMALNGSAVYPQACQALTSMLTRNTLNPADITVLFRNYSGSDPPPIDLIRNPQFLELLVDALFRSGVKINPEHKPKYMFLLAYASAVIDQPAKKRPMTERMLNKEELKSTIQAIEKAHTICNVDQGSTELIAELQTLYNCIKYPVVGVGVIRWIENVVMEPSYFKLSTDSCPTHLAVLDEVAAVHPTLQQQILFLLIRLFESKQDELEILVQLEMKKMILDRMVNLLTRGCVVPVLRYIKQCCAIEDTDISLIRYFVTEVLETITHPYSPEFVQLFLPMVENEEITGTMRGEGDNDPVSEFIVHCKAHYTTV
Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex, causes transcriptional pausing.
Q24134
P26401
RFBV_SALTY
O antigen biosynthesis abequosyltransferase RfbV
Salmonella
MLISFCIPTYNRKEYLEELLNSINNQEKFNLDIEICISDNASTDGTEEMIDVWRNNYNFPIIYRRNSVNLGPDRNFLASVSLANGDYCWIFGSDDALAKDSLAILQTYLDSQADIYLCDRKETGCDLVEIRNPHRSWLRTDDELYVFNNNLDREIYLSRCLSIGGVFSYLSSLIVKKERWDAIDFDASYIGTSYPHVFIMMSVFNTPGCLLHYISKPLVICRGDNDSFEKKGKARRILIDFIAYLKLANDFYSKNISLKRAFENVLLKERPWLYTTLAMACYGNSDEKRDLSEFYAKLGCNKNMINTVLRFGKLAYAVKNITVLKNFTKRIIK
Catalyzes the transfer of CDP-abequose on D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid to yield D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid.
P26401
A6TWF3
RPOA_ALKMQ
Transcriptase subunit alpha
Alkaliphilus
MIEMEKPKVEVFEISDDSTYGKFVVEPLERGYGTTLGNSLRRIMLSSLPGAAVTSVKIEGILHEFSTIPGVKEDVTEIILNLKDLSIGIDGNEPKTLRIEMEGPGTVTAGDIIADADVEVLNPDMYIATLDDNSKLNMEINIAKGRGYVSAENNKTAGMPIGVIPVDSIFTPVRKVSYFVGNTRVGQVTDYDKLEIEVFTDGSIKPDEAISLAAKVMSEHLNLFITLKEDVSDVEIMVQKEEDKKEKVLEMTIEELDLSVRSYNCLKRAGINTVEELSLKSEEDMMKVRNLGKKSLEEVDKKLEELGLGLRPSDE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A6TWF3
B8E2D4
VATE_DICTD
V-ATPase subunit E
Dictyoglomus
MALEKIIEKLENEKKVKIEELRKKREKEYEDFVAKKEKELEEWKEQQRKNLKESLNREESTLLSQLRLKYNTEKARIEAETVNRVKLLLLEKIKSLSNELYNGIWDGFVEKESVKGGEIILAKGEDKIDVDHFCKKYGLVLGKDRVEGKGGFVIQKDNLVIDLTIDTIVEELVNKNILEIAQILRGEK
Produces ATP from ADP in the presence of a proton gradient across the membrane.
B8E2D4
Q2JDP1
PROB_FRACC
Gamma-glutamyl kinase
Frankia
MRPFVTDARRVVVKVGSSSLTTAAGGLDVDRLEALVAAVLPRAGQQLVLVSSGAIAAGLAPLGLARRPRDLATQQAAASVGQSSLVHSYAAAFGRAGHQVGQVLLTATDVIRRTHYRNARTALDRLLELDVIPIINENDAVATQEIRVGDNDRLAAIVAHLVSADLLVLLSDVDGLYDANPRLGPATMVREVRSDTDLDGLTARGTGTAGVGVGGMATKIEAARMAASGGVTAIITSAANAAPVLRGEEVGTVFHPTGSRRASRLLWLAHATAPEGRLHLDSGAVAAVVRRRASLLPAGITGVEGDFAAGDPVDLVDPDGRSVARGLVAFDAAELPVMLGRSTADLAMELGPSYEREIVHRDDLVLLLPAR
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Q2JDP1
Q5FSN7
APT_GLUOX
Adenine phosphoribosyltransferase
Gluconobacter
MSFQDPQPLDLKNYIREIPDFPKRGILFYDISTLIRSPDAWQVATARLARVIAAWQPDILAGIESRGFLTAAPLALRLGCGFTMLRKPGKLPGKTISLKYGLEYGEDELHIQADAIKPGQRVVVLDDLLATGGTLAASIDLLRKVGAEVVGASVLIELADLKGREKLDVPLNALMTYDE
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Q5FSN7
Q0AJ92
PLSY_NITEC
Lysophosphatidic acid synthase
Nitrosomonas
MITVILIFSAYLLGSISFAVVASWLFKLPDPRSYGSGNPGATNVLRTGKKVAAAVTLLGDAGKGWVAVVVAKYLGNVLGLGDEVIASAALAVFLGHLFPIFLAFKGGKGVATSAGILLGLNLWLGILAILTWIIVALVSRISSLSALLSALLAPLYTYFLLQKEMLTITVLIISILLILKHQSNIANLIAGKETRIGKSS
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Q0AJ92
A7ML63
RHAT_CROS8
L-rhamnose-H(+) transport protein
Cronobacter
MSNAITMGILWHLIGAASAACFYAPFKKVRHWSWETMWSVGGVVSWLILPWVVSALLLPDFWAYYRSFSAATLLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIVGTLMTPLLNGKFGVLVGTAGGRMTLLGVFVALVGVAIVTRAGQLKERQMGIKAEEFNLKKGLVLAVLCGVFSAGMSFAMDAAKPMHEAAAALGVDPLYVALPSYVVIMGGGALINLGFCFIRLAKVKNLSIKADFSLAKPLLISNVLLSALGGLMWYLQFFFYAWGHARIPAQYDYISWMLHMSFYVLCGGIVGLLLREWKTAGRRPVSVLSLGCVVIIVAANIVGLGMATN
Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system).
A7ML63
B1XJP0
DEF_SYNP2
Polypeptide deformylase
unclassified Synechococcus
MTVGISVEKGKQDTPPLELHYLGDKVLRQKAKRIAKVDDEIRTLAKEMLQTMYSSQGIGLAAPQVGVNKRLIVIDTDPENPANAPLVLINPEIKKFGQQLCPFEEGCLSIPGVHLDVIRPDEIEVSYRDEQGKPKRIKASGLLSRVIQHEIDHLDGVMFVDRVENEIALSSQLKQRGFALKSVQRIA
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
B1XJP0
Q59YT1
QDR2_CANAL
MFS antiporter QDR2
Candida
MLSTTQSVTEPTEVTSKKVEDIEKENDEETPYSIFTSYDRLVLIVILSLIGFWSTISSPIYFPALPTLTSYFHTSSSIMNISVVAYLIFQGIAPTISSNLADTFGRRPVILASIIVFCASCVAISQTNVYWLLAVLRCIQAAGIAAVISISSGVAGDVCTRANRGSMVGAVAGLQLVGNGIGGLVGAALISSFNSWRSIFIFLTIGGGVTFILAIFILPETSRKLVGNGSVVPKNILNKSPYIYLPHFKKRMNNDITTIVPATRFDLLGPLKIFFQKNVFCTLLPVGIHFAAWTMVLTSLSTELESRYHYSVMHVGLIYLPQGIACIAGSLVVGKSLDWYYRYRKTIYDQEVECLPLDERPQFNIVATRLTLSVVPALLMIIGLVIFGWCIQYKRHIISIIISTILVSFSASVFIAICTTMLVDLYPNNGSGSTSCLNLMRCWLAALGAGVLDSMINAMNVGGTYTVVAGFCILFDLALIYVLHNAKKKFSNSGPTTTKSPPKQ
MFS antiporter that does not display functional linkage as drug transporter and performs functions that significantly affect biofilm development and virulence. No substrate for transport has been identified yet, but plays an important role in the growth in the host.
Q59YT1
B3QRD8
OBG_CHLP8
GTP-binding protein Obg
Chlorobaculum
MKFVDSAKISVKAGDGGRGCVSFRREKFVPKGGPDGGDGGRGGHVYLRANRQLSTLLDFKYRKSYIAGRGEHGMGARKSGKNGNDVVIGVPCGTVVRNAETGEVLCDMVEDGQEIMIAKGGRGGQGNQHFATATRQAPRFAQPGEKGDEIELEMELKLMADVGLVGFPNAGKSTLISVFSAARPKIADYPFTTLVPNLGIVRYDDYKSFVMADIPGIIEGAAEGRGLGIQFLRHIQRTKTLLVMVPSDSADIAAEYATLLRELEKFDASLLSKPRLAVITKMDIAPEDFAIPELEPGIKVIAISSVAGQGLKALKDELWRQISTSTQITVDDAGN
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
B3QRD8
Q96474
ALB1_LUPAN
Albumin-1 chain a
Lupinus
IPPSRSSDCRCVPITLIVGFCIHPTGLSSVAKMIDEHPNLCQSDDECMKKGSGNFCARYPNNYIDYGWCFGSDSEALKGFL
A1b binds to basic 7S globulin (BG) and stimulates its phosphorylation activity.
Q96474
Q4X265
LKHA4_ASPFU
Leukotriene A-4 hydrolase homolog
Aspergillus subgen. Fumigati
MTTVVNLPRDPNTLSNYNNWVSTHITANFDILFDQRKLAGNVIHRFRSTTDGESNHIILDTNHLDIGSVKVNGQPSEWEYLPRLEPYGTPLKIKLDQGVKLNETIEVDISVQTTEKCTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKCTLDFNITSPLPVIASGLPVRGSSEAPKSDGKTLYKFHQKVPIPSYLFALASGDISEAPIGPRSVVATSPDKLGECQWELEADTEKFINAIEKIVYPYVWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENIDVIAHELAHSWSGNLVTNASWEHFWLNEGWTTYLERRLRHGEPYRHFSAIIGWKALTDSVEHFGPEHDFTKLITNLKGMDPDDAFSSIPYEKGFNFLFHLENLVGKSKFDRFIPHYFNKYKGKSLDSYEFKSTILDFFKDDSDASTALNELDWDSWFYAPGLPPKPDFDTSLVDVVYDLAKKWLSLPKSSFKPQPEDIRGLTANQVVVFLEQILVSERQLTPELSKLMGEIYGLAASQNIEVANLYFQVGLQAGDASVVEPTADLLGKIGRMKFVRPLYRKLAKFDRKRALDTFEKHKGFYHPICRAMVEKDLFGKKDE
Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Q4X265
P83525
FER_SCOJA
Ferredoxin
Scopolia
ATYKVKLVTPDGPVEFDCPDDVYILDQAEEEGHELPYSCRAGSCSSCAGKVSAGTVDQSDGNFLDDDQMADGFVLTCVAYPQSDVIIETHKEEELTG
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
P83525
B1KJM2
T23O_SHEWM
Tryptophanase
Shewanella
MVCPHNNPKQGNTREMEDSIHTDFNNDMSYGDYLCLEQVLSAQHPQSEVHDEMLFIIIHQTSELWLKLAGNELDTMIHNVQQGDFSHAFKVISRVKQILNQLTQSWNILSTLTPVDYLKFRDALGRSSGFQSYGYRKIEFLLGNKNADLIQVHESNEQVHSELQGILERPSLYDEVIRVLHKQGLPIDDSALNRDFTQPYQANESVLNAWLSVYRNADEHFELYELAEKLIDIEDAFQQWRFKHMYAVQRIIGNKMGTGGSSGVSFLKKALDISFFPELFELRTHL
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
B1KJM2
Q2L284
RL14_BORA1
50S ribosomal protein L14
Bordetella
MIQMQTTLDVADNTGARAVMCIKVLGGSKRRYAGIGDIIKVSVKDAAPRGRVKKGEIYNAVVVRTAKGVRRKDGSLIRFGGNAAVLLNAKLEPIGTRIFGPVTRELRTEKFMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Q2L284
Q8X9H0
NANK_ECO57
N-acetyl-D-mannosamine kinase
Escherichia
MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNLGGLLHFPLVKTLGQLTDLPTIAINDAQAAAWAEYQALEGDITDMVFITVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFMRAGQGDEQAQQLIHRSAHVLARLIADIKATTDCQCVVVGGSVGLAEGYLALVETYLAQEPAAFHVDLLAAHYRHDAGLLGAALLAQGEKL
Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
Q8X9H0
P57340
GRPE1_BUCAI
HSP-70 cofactor 1
Buchnera
MIHNEEEQLEKKIEKNQDPKINHKKYDSDNLIKKNLIQFLEIQLKESEEKIIEKEEIVEKEIVLIHNRFNKEIEKSIKFSLEKIIIDFLPIIDNIERALNLIETINLKQEKYTEILKKLQFICNLLEKFFYLFNIKKINDTNVLFNPSIHQAMSIHYTNDIISNQIVTVMQSGYILHKSRLLRPAMVVVSKEKI
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.
P57340
A1K7K2
RS20_AZOSB
30S ribosomal protein S20
Azoarcus
MANSAQARKRARQATKARAHNASLRSRLRTAIKAVRKAIVGGDKAAAQAVFRTSMSTIDSVADKKIIHKNKAARHKSRLSAAVKAMAA
Binds directly to 16S ribosomal RNA.
A1K7K2
A9IW08
RS8_BART1
30S ribosomal protein S8
Bartonella
MSMSDPLGDMLTRIRNALGRKKDKVVTPASKLRAHVLDVLQSEGYIRGYNQVDLGDGKAELEIELKYFEGMAAIRDISRVSKPGRRVYVSAKSLPQVANGLGISVLSTPKGVMADHEAREQNVGGELLCRVF
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.
A9IW08
Q6BV42
NPC2_DEBHA
Phosphatidylglycerol/phosphatidylinositol transfer protein
Debaryomyces
MVAYKNIALLALTFTIASVESLSIVGARPYIDKALSVFDIKTPNSQSEKPEIILTFAGPDDKPVPGDSPIVQCEASVPQLLNLQSVVIDPNPPLRGENLTFVAKGVLSQDIEDGAYVEVDVRYGFIKLLHQTFDLCEEITKIDLECPISKGQQVIEKKVEIPAEVPPGKYIVSARAYTKDDIFITCLSAMVEFPPL
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Q6BV42
Q9PCE8
UBIB_XYLFA
Ubiquinone biosynthesis protein UbiB
Xylella
MKALFRACRIGKVMLRYRLDTLLDGTAAERWLRLAKPFVPRISAEIVEQSRGRRLRLALQELGPIFVKFGQILSTRRDLVPQDIGDELVMLQDRVEPFEGQTARIIIETALGKSVESAFAHFDTVPLASASISQVHAATLHDGREVVVKVLRPDIEHQISDDIALLKSLATLVEHTHPNADKIRPCEIVAEIETTLAAELDLQREGANASVLRRFWEASDDIYVPEVIWSHTAEQVLTLERMYGIPSDDIALLDASGIDRKALSSKGIRVFYTQVFRDNFFHADAHSGNIWVDSDPARKSNPRFIALDFGIMGQLSQKDQYYLAENFMAIFHKDYRRIAELHVEAGWIPPHVRIEELEAAARSVCEPYFTRPLSQISLAEVLMKLFHVARRYQLTLQPQLILLQKTLLNIEGVGRQLDPELDIWVVARPVLERILRARYSPRHALKELNKRLPEIMTHAPDTPRLIHTWLVQQVESRKQNDVYLQQIRALAMTLQGLQRRVVNAIVGSGLLVAAAVLYGLHPDGLYLGAIPVWSLISGCVGALALFSAWWRS
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
Q9PCE8
Q48259
HAP_HELPX
Zinc metalloprotease
Helicobacter
NSGLVYRDMSGGINEAFSDIAGEAAEYFMRGNVDWIVGADIFKSSGGLRYFDQPSRDGRSIDHASQYYSGIDVHSSGVFNRAFYLLANKSGWNVRKGFEVFAVANQLYWTPNSTFDQGGCGVVKAAQDLNYNTADVVAAFNTVGVNASCGTTPPPVGKVLEKGKPITGLSGSRGGEDFYTFTVTNSGSVVVSISGGTGDADLYVKAGSKPTTSSWDCRPYRSGNAEQCSISAVVGTTYHVMLRGYSNYSGVTLRLD
May play a role in ulcer formation. Proteolytic digestion of gastric mucus has been suggested as an important mechanism by which its pathogenicity is at least partly exerted.
Q48259
Q19958
STO2_CAEEL
Stomatin-2
Caenorhabditis
MKTQPSEESASPAPVNPGNSGNSGNRRASSTRISFSDQLDGGDSGDSSSNESERLMESDDEGNIQIPVPTGQPRGRMGRRFTLNPLIFAKEEREARRQSLAQLKLSYYPKHMNPEHYDTGLGFCGWFLMGLSWIMVISTFPVSIYFCMKVVQEYERAVIFRLGRLIGGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRALRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLPMELVRHLIN
May be involved in cilia-related function.
Q19958
Q1D801
HSLU_MYXXD
Unfoldase HslU
Myxococcus
MSAFTPREVVSELDRYIVGQNAAKRAVAIALRNRWRRQQVDDDLRDEIHPKNIIMIGPTGVGKTEIARRLAKLAQAPFVKVEASKFTEVGYVGRDVESMIRDLVEAAIALVREEETEKVGPRAEELAEDRLIELMQGGGVKSSSATPPFGFAPPPPPPVQRVSDSAREKFRAQLRAGTLDDVEVEVETAESSPTFMRGFSGQGMEEIGVNLQDLFKNVPGMNKTRRRRVRVPEALQLLRKEEAAKLVDPDRVQREAVARAEMNGIIFIDEIDKIASREGGKGGGGPDVSREGVQRDILPIVEGSTINTKYGVVKTDHMLFIAAGAFHVSKPSDLIPELQGRFPIRVELEPLTGEDLVRILREPKNSLLRQYTALLSTEGVRLSFTDDAVTELARIAQQANESTANIGARRLHTILERLLDEVSFSASEMGPRDFQVDAAYVRERLAAIVQDEDLSRYIL
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Q1D801
Q5WTJ3
LPXC_LEGPL
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Legionella
MIKQRTPKKVIQATGVGLHSGEKVLLTLRPAPVNTGIVFRRVDLSPVVEIPASYEYVGDTMLCTTLHHGKVKIATVEHLLSALAGLGIDNAYIDVNAPEIPIMDGSAAPFVFLIQSAGIREQNAAKRYIRILKPIRVEENGKYVQFLPHKGYKITFTIGFEHPVFNDRPQTVSFDFSGTSYVKEVCRARTFGFLSDYEKLRECDLAKGGSLDNAIVVDDYRVLNEDGLRFESEFVTHKVLDAIGDLYLLGSSLIGAFEGYKSGHELNNRLLRELMIRQDAWEYTYFDTENYLPAVHPEYYPVEA
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.
Q5WTJ3
Q0SUV5
AZOR_CLOPS
FMN-dependent NADH-azoreductase
Clostridium
MSKVLYIKANIKNEGESRTFKVSDSFVEEYKKNNPEDQIITLDLYKENIDFLRADDLGKLFGPKDEESKNNSILKYAYQFADADKYIIAAPMWNLSFPAILKAYIDYVSVSGITFKYTAEGPVGLLNNKKAVHIVSRGGGYDNSPYEMGDRYLRTILGFFGIKDIETIDIDNLDVIGVNVKEKVKEGIEKAISLAKKF
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Q0SUV5
A8GGX8
UBIG_SERP5
3-demethylubiquinone 3-O-methyltransferase
Serratia
MNAESSSQAQNVDHHEIAKFEAVASRWWDLEGEFKPLHRINPLRLNYILQRAGGIFDKTVLDVGCGGGILAESMAREGAQVTGLDMGAEPLQVARLHALESGVNVAYIQETVESHAQANPQRYDVVTCMEMLEHVPDPASVVRACAHLVKPGGHVFFSTINRNTKAWLMAVVGAEYILKMVPQGTHDHKKFIRPSELIGWVDGTPLREKHMIGLHYNPITDHFKLGRNVDVNYMVHTQHEG
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
A8GGX8
A8MKS3
RNPA_ALKOO
Protein C5
Alkaliphilus
MKAINRLRKNEDFRKVYKKRKSMANKLLIIYILENGYNFNRVGFTVSKKVGKSVIRSRVKRLLNESYRLNNEKVKQGYDIIFVARNTCVDASYKEIESAILHLLKKMNLINSAV
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
A8MKS3
Q47G52
URED_DECAR
Urease accessory protein UreD
Dechloromonas
MTSRLPISQPEHSPSWHAELHLGFARAGERTVLRENRHRGPLRVQKALYPEGEAVCQTIVLHPPSGIAGGDHLAISAEVGEGSHAQLTTPGAGKWYRSGGAEASQRVAFTVGEGATLEWLPQETIVFDGARARMETQVDLAADSRYIGWDILCLGRVAAGERFEKGRFDLFLQVNRDQRPIWIERGGFDGSDPMLISPAGWAGATVCGTLLCAFPEWPMQASALLEACRKIVPADGAQHGLSALPGVLIARYLGNSSEAARLWFAELWTILRPACCGRPAVIPRIWNT
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q47G52
O32157
FRLB_BACSU
Fructosamine deglycase FrlB
Bacillus
MSQATAKVNREVQAFLQDLKGKTIDHVFFVACGGSSAIMYPSKYVFDRESKSINSDLYSANEFIQRNPVQLGEKSLVILCSHSGNTPETVKAAAFARGKGALTIAMTFKPESPLAQEAQYVAQYDWGDEALAINTNYGVLYQIVFGTLQVLENNTKFEQAIEGLDQLQAVYEKALKQEADNAKQFAKAHEKESIIYTMASGANYGVAYSYSICILMEMQWIHSHAIHAGEYFHGPFEIIDESVPFIILLGLDETRPLEERALTFSKKYGKKLTVLDAASYDFTAIDDSVKGYLAPLVLNRVLRSYADELAEERNHPLSHRRYMWKVEY
Catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid.
O32157
Q0SY12
RPOC_SHIF8
Transcriptase subunit beta'
Shigella
MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELFKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERLYRTGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGRAILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKPTVIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISEAEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAMMDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTHEGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADILVPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCAHCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTFHIGGAASRAAAESSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLIDEFGRTKESYKVPYGAVLAKGDGEQVAGGETVANWDPHTMPVITEVSGFVRFTDMIDGQTITRQTDELTGLSSLVVLDSAERTAGGKDLRPALKIVDAQGNDVLIPGTDMPAQYFLPGKAIVQLEDGVQISSGDTLARIPQESGGTKDITGGLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLVITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEAPHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVIVRQMLRKATIVNAGSSDFLEGEQVEYSRVKIANRELEANGKVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAGEAPAAPQVTAEDASASLAELLNAGLGGSDNE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q0SY12
Q49VV9
LGT_STAS1
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Staphylococcus
MMTLSYIDPIAFELGPISVRWYGIIIAMGILLGYFIAQASVKRIGFHQDTLVDIIFWSAIFGFIIARIYFVIFQWPYYVQHPIEIPMIWQGGIAIHGGLIGGFVTGIIICKQKNINPFQIGDVIAPSMILGQGIGRWGNFMNHEAHGGTVSKSFLENLHIPDFIINNMYIDGKYYQPTFLYESIWDVLGFVILILLRKHLRIGDTFCLYLIWYSIGRFFVEGMRTDSLMLAGDIRIAQLMSIILIIIGVVIMIVRRVKYDAPRYKAVGPLSWPSKEVK
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.
Q49VV9
Q33824
COX3_PATPE
Cytochrome c oxidase polypeptide III
Patiria
MTHQHPYHLVDQSPWPLTGAISALMMTSGLILWFHTNSNHLLLAGTILLLLTVINWWRDVIREATFQGSHTLPVNTGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVELGVSWPPTGISPINPFLVPLLNTAVLLSSGVTVTWAHHSILTQNRTEAIQGLFLTVILGIYFTGLQAWEYYDSPFTIADSVYGSSFFVATGFHGLHVLIGTTFLFICFLRLITFHFSNNHHFGFEAAAWYWHFVDVVWLFLYICICWWGS
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Q33824
Q0VRI8
QUEC_ALCBS
Queuosine biosynthesis protein QueC
Alcanivorax
MKKAVVLLSGGLDSATCLAIARDQGYACHTIAFDYGQRTRSELDAAERVSGVLGALSHRVIELGMGNIGGSALTDHSIEVPENGGDGIPVTYVPARNTVFLSLALGLAEVIDAQAIFIGVNAVDYSGYPDCRPAFIEAFQSMATLATKAGVEGRPMQIETPLMHLSKAQIIQRGVALGLDYGLTVSCYQADDHGNACGKCDSCRLRSQGFEDALVKDPTNYQ
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Q0VRI8
Q1LIL8
RSMH_CUPMC
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Cupriavidus
MSPTESPGTTTLRHRTVLLDEAVDALVWRPDGAYVDGTFGRGGHSRAVLARLGPAGTLVAFDKDPAAIAEAGTIKDARFSIEHASFAEMGDRLAGRGPVAGVLLDLGISSPQIDEAARGFSFRFEGPLDMRMDTTRGITAAEWLAQADEQDIARVIRDYGEERFALQIAKAIVARRRESGDGGALATTSDLAALVAKAVKTREKGQDPATRTFQALRIYINQELEDLERGLKAAYELLQVGGRLVVISFHSLEDRIVKRFMQAHARPERDADPALRRAPLRAADLPQPTMKLLGRFKPGAEEVAGNPRARSAVMRVAEKLGEQSA
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q1LIL8
A5I4S1
COAD_CLOBH
Pantetheine-phosphate adenylyltransferase
Clostridium
MKTAVYPGSFDPITKGHLNIIKRASKVCDKLIVAVLVNPEKKGLFSVDERVEMIKRVTKKHSNVEVQCFSGLLIDFMKEKKSKVIIKGLRTMSDFEYEFKMALMNNKLDPNIETVFMMTNAKYSYLSSSSVKQVAMFGGCIKDLVPDEIIPDIKKKINHKKECI
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A5I4S1
P83640
DRS3_PHYDS
Dermadistinctin-M
Phyllomedusa
ALWKTMLKKLGTMALHAGKAAFGAAADTISQ
Antibacterial activity against Gram-positive bacteria S.aureus and E.faecalis, and Gram-negative bacteria P.aeruginosa and E.coli.
P83640
Q8Y0M0
HSCB_RALSO
Co-chaperone protein HscB homolog
Ralstonia
MNSASDTHFSLFGLPEHFEVDDGALNAAYRTVQSRAHPDRHAHASDAERRVAMQWATRANEAYQTLRDPLKRATYLLHLRGVDVQAENNTAMPPAFLMQQLEWRESLADAKAAGDLDALDDLLAMLRGEKRARYQTLAGLLNGGGHDAAAADAVRQLMFIEKIERDTAEAIDRLDD
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
Q8Y0M0
Q1D778
RS7_MYXXD
30S ribosomal protein S7
Myxococcus
MPRRRVVAKRKILPDPKFQDRLVTKFVNDLMRKGKKSIAEGVCYGAFALIEERAKEDPLKTFKKALDNVKPVLEVKSRRVGGATYQVPVEVRQDRRVALGMRWIITYSKARGEKTMQEKLAGEIMDAANNRGNAVKKREDTHKMAEANKAFAHYRW
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. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Q1D778
C1D7C0
COQ7_LARHH
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
Laribacter
MLDKLIIEFDKGLRTVFAPAQTLRPHPDTGLEEAGLSDLEKRHALGLMRVNHCGEVCAQALYQGQALTARDPATREALKEAAWEETEHLAWTEKRIAELGGRKSLLNPLWYGGSLAMGITAGLLGDRWNLAFLEETEYQVEAHLNEHLATLPEQDAKSRAIVTQMRDDEHRHAETAHALGAAAMPAPVKGLMHLTSQLMKKTSYHI
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
C1D7C0
Q2GNR9
GET1_CHAGB
Guided entry of tail-anchored proteins 1
Chaetomium
MPSLLVVVFVIELVVQLVNTIGATTINNLIWRAYLSIPTSLAKQFTEQRQKQKEYLAVRLELNATSSQDEFAKWAKLRRQHDKLLDELEKKKSAVEASRTKFDRYITAVRFISTRGVQWLLPMWYGKLPMFWLPYGWFPYYVEWFVSFPRAPLGSVSIVTWQAACTAILTLVMNAVVGILAFISASRQSGKQKQKQPVPAAGARNGETKKEL
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol.
Q2GNR9
A4XYB8
GLUQ_PSEMY
Glutamyl-Q tRNA(Asp) synthetase
Pseudomonas
MNTAYIGRFAPTPSGYLHFGSLVAALASYLDARAVGGRWLLRMEDLDPPREIPGAQDAILRTLETYGFEWDGELVRQSERHAEYAAVIARLLSQGLAYACTCSRKQLEGYAGIYPGFCRNACHPDHDAAIRLRVPELDYHFIDRVQGEFRQHLGREVGDFVIRRRDGLFAYQLAVVLDDAWQGVTDVVRGADLLDSTPRQLYLQELLGLPQPRYLHVPLIIQPDGHKLGKSYRSPPLPADQAGPLLLRALRALGQQPPTELQGAAPAELLSWGRANWDAMRIPRSRTLAEAQLR
Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
A4XYB8
B9DYB5
RS3_CLOK1
30S ribosomal protein S3
Clostridium
MGQKVHPHGLRVGIIKEWDAKWYADKKNFADNLVEDNKIRKFVKKKGAIAGISKIQIERAAKRIKLNIFTAKPGMIIGKGGQGIEALKTELKKIVPDKVILINIVEVKVAEADAQLMAENIALQLEKRISFRRAMKQTIQRAMKSGIKGVKTTCSGRLGGAEIARSESYHEGTIPLQTLRADIDYGFAEADTTYGKIGVKVWVYKGEVLPVKKPVENKEEAKA
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
B9DYB5
Q9V6B9
NUP54_DROME
Probable nucleoporin Nup54
Sophophora
MSFFGSNTSLGATSTPAKTTGGLFGSPFGGTAATSQPAPAFGAQATSTPAFGAQPATSAFGAGSAFGATAAAPAFGAATGTSAFGGSAFGSTPAFGAATTTTAGTGLGGGGFGGFGAAPATSQAGLFGAPATSAAPPAFSGFGQQAAASTAPASGFSGFGTTTTSAPAFGGFGTSQSTGFGGGAFGSTFGKPANTTVTPGFGGFGGTSFMLGQPQQQPAPISADEAFAQSILNVSIFGDERDKIVAKWNYLQATWGTGKMFYSQSAAPVDITPENVMCRFKAIGYSRMPGKDNKLGLVALNFCRELSAVKPHQQQVIQTLHSLFGSKPNMLVHIDSIKELENKKCQIVIYVEEKLQHAPNESKRILATELSNYLNQATLKPQLNNLGVVEALALVLPDEDQLREYLENPPRGVDPRMWRQANSDNPDPTLYIPVPMVGFNDLKWRVKCQEQETDTHALYIKKVESELTELKKRHATATAKILEHKRKLAELSHRILRIIVKQECTRKVGTSLTPEEEALRTKLQNMLAVVSAPTQFKGRLSELLSQMRMQRNQFAANGGAEYALDKEAEDEMKTFLTMQQRAMEVLSDTVNKDLRALDVIIKGLPELRQS
Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope . Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner . Together with Nup58, required for transposable element silencing regulation in ovarian follicle cells . By interacting with the nuclear (Nxf1/Nxt1) and cytosolic (fs(1)Yb) components of the flamenco (flam) transcripts processing pathway, enables export and subsequent piRNA production .
Q9V6B9
A6QCE8
MIAA_SULNB
Isopentenyl-diphosphate:tRNA isopentenyltransferase
unclassified Sulfurovum
MNQPIRQLALIGPTASGKTALAIKAAQALDAHILSIDSLSIYKEIDIVSAKPTKEEQKGIKHFGIDFIAPNEDFDVTTFIRLYEDVHVRAVADNKNLVIVGGTSFYLKMLMEGISKLPKISETTKRRTTEALRDLQKSHEWLSTLDPDYMQKISSSDPYRIEKALDIYFETGTCPTEYFKAFPPKPTIQSELPIYQIETDRELLRKRISLRTQMMLEDGLIDEICMLEEKYTRAPNCMKAIGIKETLAYLDGIYEREMLKEKITVNTARLAKRQTTFNHSQFDNVIKGSVSELEKILLQGA
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).
A6QCE8