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.
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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
|
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