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
|
|---|---|---|---|---|---|---|
Q5GGR6
|
MATK_CUBDO
|
Intron maturase
|
Cubanola
|
MEEIQRYLQLDRSQQHDFLYPLIFQEYIYALAHDHSLNRSILLENPDYDNQLSFLIVKRLITRMYQQNHFIIFANDSNQNTFLGRNKNLYSQTISEGFSFIVEIPFYIRLIPSQAGKGILKSYNLRSIHSLFPFLENNFSHLNSVLDILIPHSVHLEILVQNLRYWVKDASSLHLLRFLFHEYWNCNPLSATKKRGFDFSPKRSQRLLFFLYNSHVCEYESIFVFLRNQSSHLRSTSFGVFLERIYFYVKMERLVEVFAKDFRASLWLFKDPFMHYVRYQGKSTLVSKGTPLLMNKWKYYLVNFWQCYFDLWVHSGRVYINQLPNHTLNFIGYLSSVRLNPSMVRSQMLENSFLINNAIKKLDTLVPIIPLIGSLAKAKFCNLLGHPISKPAWAGLSDSDIIDRFGQICRNLSHYHSGSSKKKSLYRIKYIIRLSCAKTLARKHKSTVRAFLKRLGSEFLEEFLTLEEEVLSLTFPRASSTFRGEYRSRIWYLDIIYINDLTNSQ
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q5GGR6
|
Q6BF87
|
LDRB_ECOLI
|
Small toxic polypeptide LdrB
|
Escherichia
|
MTLAQFAMTFWHDLAAPILAGIITAAIVGWWRNRK
|
Toxic component of a type I toxin-antitoxin (TA) system. Overexpression causes rapid cell killing, probably by disrupting the cell inner membrane and disruption of ATP synthesis.
|
Q6BF87
|
P94690
|
CYC3A_DESAF
|
Acidic cytochrome c3
|
Desulfocurvibacter
|
MFKHTLIALTLLAAATLFSLPAFSQEDMTHVPTDAFGKLERPAAVFNHDEHNEKAGIESCNACHHVWVNGVLAEDEDSVGTPCSDCHALEQDGDTPGLQDAYHQQCWGCHEKQAKGPVMCGECHVKN
|
Exchanges electrons specifically with the basic cytochrome c3.
|
P94690
|
Q03DS8
|
GLPK_PEDPA
|
Glycerokinase
|
Pediococcus
|
MADKYILAIDEGTTSTRTIIFDHAGNKMADAQREFPQYFPKPGWVEHNANEIWNAVLSTIANAFIESGIKPNQISGIGITNQRETTVIWDKKTGLPIYNAVVWQSRQTAEIAEQLVKDGYGDMIHQKTGLVTDAYFSATKIRWILDHVDGAQARAERGELLFGTIDTWLMWKLTDGDVHVTDYSNASRTMLYNIHKLEWDKEILALLNIPASMLPEVKPNSTIYGKTKDYHFYGSEVPISGMAGDQQAALFGQLAFEPGMVKNTYGTGAFTVMNTGEKPQLSDNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGMKLFKKASESEAAAVASQNDNEVYVVPAFTGLGAPYWDPNARGSVFGITRGTTREDFIKATLQSLAYQSRDVIDTMKKDSGIDIPSIRVDGGASNNDYLMQFQSDILGIEIDRASDLETTALGAAFLAGLAVGFWKDLEDLKKEYKPGKVFKPKMSTDEREDLYTGWQEAVAATRQFKHRPRQSK
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
Q03DS8
|
A1AS12
|
PYRC_PELPD
|
Dihydroorotase
|
Pelobacter
|
MNLLIQNGRVIDPSQGLDEELDLLVENGLVREMGRGLTAPAGVEIVDAAGCCVVPGLVDMHVHLREPGLEYKEDIESGSRAAVAGGFTSIACMPNTKPVIDNKALARYVIARGREAGLCNVFPVGCLTAGSKGERLAEMGELKEAGCVAVSDDGRPVVNAELMRRALEYARGMQIPVISHAEDLSLVGEGVMNEGFTSTELGLKGIPRVAEDIAIARDVMLAEYTNSPIHIAHVSTSGAVRIIRNAKLRGVRVTCETAPHYFTLTDDAVRGYNTNAKMNPPLREADDVAAIRAGLSDGTIDVIATDHAPHHLDEKDVEFNVAANGIIGLETSLPLSLALVEQGVLTMSQLVERMSCCPSLILGLERGTLAKGAVADITLIDPTLPWVVEADKLASKSTNTPWMGQEMKGAAVATIVAGRVVYRR
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
A1AS12
|
A1K4F0
|
PIMT_AZOSB
|
Protein-beta-aspartate methyltransferase
|
Azoarcus
|
MSGRQDASHAGRARARMVERLRAQGIQDEGALAAMMQVPRHLFVEEGLAYSAYDDTALPIGFQQTISQPYVVARMIELLRSGGRQLGRVLEIGAGCGYQAAVLSTLATEVYAVERIRPLLDKARANLRPLRLPNVRLKHADGTLGLPEAAPFESIIVAAAAGGVPNALKEQLAPGGRLIIPVGGGEQRLLLIERQGNVFRESGYEAVRFVPLLAGTE
|
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
|
A1K4F0
|
O51438
|
RL16_BORBU
|
50S ribosomal protein L16
|
Borreliella
|
MLSPKKVKYRKKQRGRLSGEAQKGNKISFGEYGLVSLETNFITARQIEAARIAMTRKIKRGGRVWIRIFPDIPYTKKPAETRMGKGKGGVDHWNAPVKLGTVMFEMSGVVEELAQEAMSLASSKLPVKTMFVVRRDLR
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
O51438
|
A6WY85
|
TILS_BRUA4
|
tRNA(Ile)-lysidine synthetase
|
Brucella
|
MGLSPSNISKLFEPFGFEQAKAVIAAVSGGSDSLGLLFLVRDYMAMLQNPPRLIAVTVDHQLRAESKAEAENVGLLCRQYGIEHRILVWDEAKPTSGLAAAARTARYRLLVQAARDVGGAFIVTGHTQDDQIETFLMRKERSAHAEARGLAAMSLRSLLDGLGLEGSVELDRPLLSVSRQTLRDELRGRGINWVDDPSNANTEYERPRIRHGIAAEADRQTVLDQIAEAGAARERDNAALIAALGNPASLRADANGALLVDPQLYAALPGNARRLFSGLLAAIAGGRRFLPGDSERSRIERVLSGDDDTHRLTVFGALIERGDSGSPHRFLREKRNLPKLHLEPGKPIVWDGRFRFLNEGMMDFELAAPGRQELADFLKSQNIEIESRKREALLVSPALYREGRLFALLFLQDGEFQQDIHIERHFAIFDHVLPGHDFDLARAVEARIGRICAEMS
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
A6WY85
|
A8FGB7
|
MURC_BACP2
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Bacillus
|
MTVYHFVGIKGTGMSPLAQILHDTGYTVQGSDIEKHIFTQKALEERNIKILPFDPDNIQPGMTVIAGNAFPDTHPEIERALSEGIPVIRYHKFLGEYMDSFTNVAITGAHGKTSTTGLLAHVMQSAKPTSYLIGDGSGMGKENSEYFVFEACEYRRHFLSYHPDYAIMTNIDFDHPDYFSDIDDVFDAFQNMALQVKKAIIACGDDEHLPKIQAKVPVVYYGFNEENDFQARNVVKNTEGTTFDVFVRNTFYDTFYIPAYGNHNVLNSLAVIALCHYESIDVELIKGALTTFGGVKRRFNEKVVGAQVLIDDYAHHPTEIEVTIEAARQKYPDREIVAVFQPHTFTRTQQFLSEFADSLKKADYVYLCDIFGSARENIGKLSIEDLREKIPQAQLIAEEDTSVLKAHKDGILIFMGAGDIQKYLRAYEKVAV
|
Cell wall formation.
|
A8FGB7
|
P00630
|
PA2_APIME
|
Phosphatidylcholine 2-acylhydrolase
|
Apis
|
MQVVLGSLFLLLLSTSHGWQIRDRIGDNELEERIIYPGTLWCGHGNKSSGPNELGRFKHTDACCRTHDMCPDVMSAGESKHGLTNTASHTRLSCDCDDKFYDCLKNSADTISSYFVGKMYFNLIDTKCYKLEHPVTGCGERTEGRCLHYTVDKSKPKVYQWFDLRKY
|
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P00630
|
Q5HPW3
|
FAPR_STAEQ
|
Fatty acid and phospholipid biosynthesis regulator
|
Staphylococcus
|
MKLKKNDRRVAIKEAIELNPFITDYELCEKFDVSIQTIRLDRTHLNIPELRKRIKLVAEQNYGRIKSIEANEIIGDLIQVNPDVSAQSLIEITIDSVFAKSEIARGHVLFAQANSLCVALIHKPIVLTHESQVEFKEKVKLNDTVRADARVIDITDKHYIIEVNSYVSDMLVFKGKFKMYYTSEDE
|
Transcriptional factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism.
|
Q5HPW3
|
C5BZZ8
|
ACPS_BEUC1
|
4'-phosphopantetheinyl transferase AcpS
|
Beutenbergia
|
MIVGVGIDVVDVARFLAALDRSPRLRDRLFTPEERDLVGGSLAARFAAKEAIAKALGAPGGMRWHDATVARVPGGAPAVSLRGTVLAVADGLGITSWHLSLSHDAGIASAIAVAER
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
C5BZZ8
|
Q5AJ71
|
CAN_CANAL
|
Non-classical export protein 103
|
Candida
|
MGRENILKYQLEHDHESDLVTEKDQSLLLDNNNNLNGMNNTIKTHPVRVSSGNHNNFPFTLSSESTLQDFLNNNKFFVDSIKHNHGNQIFDLNGQGQSPHTLWIGCSDSRAGDQCLATLPGEIFVHRNIANIVNANDISSQGVIQFAIDVLKVKKIIVCGHTDCGGIWASLSKKKIGGVLDLWLNPVRHIRAANLKLLEEYNQDPKLKAKKLAELNVISSVTALKRHPSASVALKKNEIEVWGMLYDVATGYLSQVEIPQDEFEDLFHVHDEHDEEEYNPH
|
Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in protection against oxidative damage. Acts as a CO(2) chemosensor and induces CO(2)-mediated filamentation. Essential for pathological growth in niches where sufficient CO(2) is not supplied by the host. Necessary for white-to-opaque switching at low CO(2) concentrations.
|
Q5AJ71
|
Q1C5H7
|
PEPB_YERPA
|
Aminopeptidase B
|
Yersinia
|
MTTEIMQISLSHNPADARWGEKALISTNDQGVTIHLTSHDQLGGIQRAARKIDGQGIKQVKLAGEGWGLEQSWAFWQGFRGPKGQRSVVWAELPANEKTELEQRLKIIDWVRDTINAPAEDLGPEQLAKNAIDLLCAVSCDAVSYRITKGEDLREQNYAGIYTVGRGSDRAPVLLALDYNPTGNPDAPVMACLVGKGITFDSGGYSLKQSAFMDSMKSDMGGAATLTGALALAAARGLKERVKLYLCCADNMVSGNAFKLGDIIRYRNGKTVEIMNTDAEGRLVLADGLIDASEQNAPLIIDAATLTGAAKTALGNDYHALFSFDDELAQALLNSAHSEHELFWRLPLAEFHRSQLPSNFAELNNVAGGAYSAGASTAAAFLSHFVKNYQQGWLHIDCSATYRKSAVDQWSAGATGLGVRTVANLLLAQAKQ
|
Probably plays an important role in intracellular peptide degradation.
|
Q1C5H7
|
Q8KCZ6
|
FER1_CHLTE
|
Ferredoxin I
|
Chlorobaculum
|
MALYITEECTYCGACEPECPTNAISAGSEIYVIDAASCNECAGFADSPACVAVCPAECIVQG
|
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
|
Q8KCZ6
|
B8FGT6
|
ATPA_DESAL
|
F-ATPase subunit alpha
|
Desulfatibacillum
|
MEIRAEEISQIIKEQIKDYDKKVDLSETGTVLSVGDGIARVYGLEKAMALELVEFPGGILGLVLNLEEDNVGVAIMGEVTHIKEGDMVKRTGKIAQVPVGEAVLGRVVDGVGSPIDGKGPLDATETRMVEMVAPGVIARKSVHEPCYTGLKAVDAMTPVGRGQRELIIGDRQIGKTAVAVDAILAQKDTDIYCIYVACGQKKSTVAQVVATLEKYGAMEYTTVVSACASDPATLQYLAPYAGCAMGEYFRDKGQHALIIYDDLSKQAVAYRQISLLLRRPPGREAYPGDIFYNHSRLLERAAKVSDELGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIYLEPGLFFAGVRPAINVGLSVSRVGGAAQEKAMKQVAGTLRMDLAQFRELEAFAAFGSDLDAATQKQLKRGERLVQILKQPQYAPLPLEKQVAILFAGANGFLDAFPADSMAKYEAGMYSFLESKYPDAMGAIAKERKISDETDALLKKALEEYGKEFQDTIQ
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
B8FGT6
|
A5GPH4
|
GCSH_SYNPW
|
Glycine cleavage system H protein
|
unclassified Synechococcus
|
MAFDFPDSYRYADSHEYAWQDAAAVRIGLSAYAVDQLGDIVFVDLPEVGAELNRGSSFGTVESVKAVEEMYAPLSGVVLQRNEALLANPEELQNDPHGEGWLLVIQPGDPSQMDQLMDAATYAAKVAAT
|
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
|
A5GPH4
|
A6TQ96
|
THII_ALKMQ
|
tRNA 4-thiouridine synthase
|
Alkaliphilus
|
MENVLIIRYGEIMLKGDNKSFFEAKLTKHIRGAVKDLGDVKVYKMHSRVYIDVEDFNADEIIERVKKVFGVVCISPAVRFPVDFDVIKETALNQIKEEMAQRGVKTFKVESKRVDKKFPLKSPEMSREIGGYILENTEGLEVDVHNPEVRVYVEVRECSFVFTKKVYGFGGLPLGTNGKALLLLSGGIDSPVAGWLVAKRGVEIHGMHFHSYPFTSERAKEKVVDLAKILTTYCGRIKLYSVNLLAIQKEINEKCPEEEMTILSRRFMMKIAERVANKIGCDALVTGESIGQVASQTVKGLHVTNAAVELPVFRPLIAMDKVDIMDLARKIDTYETSILPFEDCCTVFLPKRPVTQPRLEKILRSEALLDVEGLIESAIGDMEVERISLDDE
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
A6TQ96
|
O25165
|
GUAA_HELPY
|
Glutamine amidotransferase
|
Helicobacter
|
MILVLDFGSQYTQLIARRLRERGIYTEIVPFFESIENIQKKAPKGLILSGGPASVYAKDAYKPSGKIFDLNVPILGICYGMQYLVDFFGGVVVGANEQEFGKAVLEITQNSVIFEGVKIKSLVWMSHMDKVIELPKGFTTLAKSPNSPHCAIENGKIFGLQFHPEVVQSEEGGKILENFALLVCGCEKTWGMQHFAQREIARLKEKIANAKVLCAVSGGVDSTVVATLLHRAIKDNLIAVFVDHGLLRKNEKERVQAMFKDLKIPLNTIDAKEVFLSKLKGVSEPELKRKIIGETFIEVFEKEAKKHHLKGKIEFLAQGTLYPDVIESVSVKGPSKVIKTHHNVGGLPEWMDFKLIEPLRELFKDEVRLLGKELGVSQDFLMRHPFPGPGLAVRILGEISESKIKRLQEADFIFIEELKKANLYDKVWQAFCVLLNVNSVGVMGDNRTYENAICLRAVNASDGMTASFSFLEHSFLEKVSNRITNEVSGINRVVYDITSKPPGTIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
O25165
|
Q6DEJ6
|
NLS1B_DANRE
|
Major facilitator superfamily domain-containing protein 2A-B
|
Danio
|
MAKGEGAEQYTNTSLLQKPSPDEVKLAKHETKSRLSVCSKLCYAIGGAPYQITGCAIGFFLQIYLLDVALLDPFYASIILFVGRAWDAVTDPTVGFLVSRTPWTRFGRMMPWIVLSTPFAVLCYFLIWYVPSVDQGKVVWYLIFYCCFQTLQTCFHVPYSALTMFISTEQKERDSATAYRMTVEVLGTLIGTAIQGQIVGMANAPCISTEIDLNSTGLEVAPDVNITDPHVSLQDLRNAYMIASGVICAIYVVCAVVLFLGVKEQKDTCRVRTEPMSFFQGICMVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCIYNLGFRNDFQNVLLVIMLSATLAIPFWQWFLTKFGKKTAVYIGTTSVVPFLISVVLVPSSLAVTYIASFAAGVSVAAAFLLPWSMLPDVVDDFKVQNPESQGHEAIFYSFYVFFTKFASGVSLGVSTLSLDFAGYVTRGCTQPGEVKLTLKILVSAAPIVLIIIGLLIFISYPINEEKRQGNRKLLNEQRENEMDSETDSTELNVV
|
Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function. Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid.
|
Q6DEJ6
|
A0KFR1
|
RNB_AERHH
|
Exoribonuclease II
|
Aeromonas
|
MFQDNPLLAQLKQQIRENIPKKEGVIRASDRGFGFLEVDEKTSYFVPPPYMKKVMHGDRVSALIRTEKEKEVAEPDALLEQSVTRFVARVKMFRDRLNVVADHPLIKDAIKARVKKGLDEKEFKEGDWVVATLKRHALVDGNFSAEITQTIASQEDHNVPWWVVLARHNLAQVEPADLPEWKVIEEEELPRTDLTATPFFTIDGAKTKDMDDALAIRKLDNGWELLVAIADPTAYVAEGSELDKEAAQRAFTVYMPGRNVPMIPRTLSDELCSLKEGEERNTLCARLLIAEDGLLLEETEFFAARISSHARLTYDDVSDWAEHGKQLDIDAGVLAQLPLMKAMTEARIAWRTEHALVFPDRPDYDFELGENGEVLAIHVEPRRIANRMVEESMIAANICAGRVLGKQVGYGIFNVHTGFDEESLDGAIDLLKSAEAPFEKEEIASLSGFCALRRWIDNLDTRWLDGKIRRFQSYALMSAEPGAHYGLGLDAYATWTSPIRKYGDMVNHRLLKAVIAGKTPGERPSLELTEHLTACRRLHRMVERDIGDWLYVRYLKADAGTDKVFNAEIIDVMRAGLKLRLRENGAVVFMPARHILDNKDRLECNWDNGRVYLDKTEVVYELGQIIEVKLTEAVEETRSLIAKPAVELVPGPAPVAPTSEADATPADEAPKAE
|
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
|
A0KFR1
|
Q9R0L1
|
HSF4_MOUSE
|
Heat shock transcription factor 4
|
Mus
|
MQEAPAALPTEPGPSPVPAFLGKLWALVGDPGTDHLIRWSPSGTSFLVSDQSRFAKEVLPQYFKHSNMASFVRQLNMYGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGREQLLERVRRKVPALRGDDSRWRPEDLSRLLGEVQALRGVQESTEARLQELRQQNEILWREVVTLRQSHSQQHRVIGKLIQCLFGPLQTGPSSTGAKRKLSLMLDEGSACSASAKFNACPVSGALLQDPYFIQSPLPETTLGLSPHRARGPIISDIPEDSPSPEGHRLSPSGGCRRVKGLALLKEEPASPGGDGEAGLALAPNECDFCVTAPPPLPVAVVQAILEGKGSYSPEGPRSVQQPEPRGPREVPDRGTLGLDRGNRSPESLLPPMLLRPAPETLEPVAPVDVLGPSLHGREWTLMDLDMELSLMQPLAPETDEAELTVKELNSSGVGKDHTLGTPLMLDVQADLEGAALSVPGALTLYNVTESNASYLDPGASPSSP
|
Transcriptional activator.
|
Q9R0L1
|
Q9FI22
|
DEF17_ARATH
|
Plant defensin 1.2c
|
Arabidopsis
|
MAKSATIITFLFAALVLFAAFEAPTMVEAQKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYVPC
|
Confers broad-spectrum resistance to pathogens.
|
Q9FI22
|
A0KVZ9
|
PSRP_SHESA
|
Pyruvate, water dikinase regulatory protein
|
Shewanella
|
MAPKVFYISDGTAITAEVFGHAVLSQFPLEFESLTIPFVETLAKAENVKRQINDCFITTGERPLVFHSIVKPEIRDIIYSSEGLDYDFLNTFVAPLEQHLGVSASPVLHRTHGKANHGYEARIDAINFAMDNDDGQTMKHMDQADLILLGVSRCGKTPSSLYLSMQFGIKAANYPFTEDDMDNLKLPEALKRNKKKLFGLTIDPVRLHEIRQSRMENSRYSSLKQCRLEVKEVEMMFKRERIPYIDTTNHSVEEIATKILDVTGLERHMF
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
|
A0KVZ9
|
A3QJR1
|
ATPG_SHELP
|
F-ATPase gamma subunit
|
Shewanella
|
MAGAKEIKTKIASVQNTQKITSAMEMVAASKMRKAQDRMAASRPYAENMRKVIGHVAQGSLEYKHPYLEVREAKRVGYIVVSTDRGLCGGLNVNLFKKVVADVKKQREAGAEVEFCPIGARSVQFFNSFGGKVSAHASGLGDAPKLADLIGTVRVMLKAYNEGTLDRLYVVFNKFVNTMSQTPVIEQLLPLPKSEEDEISHHWDYLYEPDPKELLETLLVRYVESQVYQGVVENIASEQAARMVAMKAATDNAGELIDDLQLVYNKARQAAITQELSEIVSGAAAV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
A3QJR1
|
A3LPW2
|
FYV10_PICST
|
Protein FYV10
|
Scheffersomyces
|
MSEPSLNFHIQSHSTQFRIPTELIKKNFKTIQKLVEKQKKQMTDDVAKIKKNPNIPTAMKLAMVRKSIKSFEGFQKKLQASIAKDEELRSRLIARIEHLALISEYCITQDKTKTQVEKPSQPQSQNEDTEEKEHSTKDDNDKYLDLHNPNLITWYRDQTNLLIIDYLIKSNTRTDHNIGLLLLKSLSESNPKYMKLIDYDLFESFNKVYVSIMEDHDLTLVIAWFNENRNFLKKANSNLEFEINYCRFLSLIEKGDVNEAIKFSSINLSPYGNVSNYQDTDRANHEHNLNRLKEIGGLLVYMAINEEKRTRNDKIAFSSNLLINSPRFHEYEKLLSDERWDSLSMCFVENFTKLYGISKNYPIFIYLSAGLASLKTKSCYHNTENTIFRENQEINVTDESIYKKDLTVLTDKKYRGSNQYYKLLNKINNCPVCSPELYKLSRNLPYAQLITSIFNNPFKLPNGNIYPFDKLLNPSEKYLSEKNTLLRMGKIKDPLTREIFLIDTCIRVYPA
|
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
|
A3LPW2
|
P50704
|
DEFA6_MOUSE
|
Defensin-related cryptdin-6/12
|
Mus
|
MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSVSFGDPEGTSLQEESLRDLVCYCRARGCKGRERMNGTCRKGHLLYMLCCR
|
Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
|
P50704
|
Q1I4M5
|
UBIC1_PSEE4
|
Probable chorismate pyruvate-lyase 1
|
Pseudomonas
|
MDNLWTSLPLPGLSDDQRHWLFAPGSLTLRLKALGRFSLEVTQQRIDFPEPGEAHALGCTTDSPAWIREVALKIDDQVMVCARSLTPMRERRPAWPELAGYGGEPLGSMLYNTPDIHRGAFECQRPQADDPLSRLATSLGQPSGKLLARRSRFLRDGQPLLIAECFVEGFWALLQERSAPLKLAI
|
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
|
Q1I4M5
|
B3PDM5
|
DER_CELJU
|
GTP-binding protein EngA
|
Cellvibrio
|
MIPVIALVGRPNVGKSTLFNRLTNSRDALVADYPGLTRDRKYGEARLENRRFIVIDTGGISGEEEGIDSAMAGQSLLAIQEADIVLFIVDSRVGLNPADELIARHLRVHNKKTYVVANKIDGMDPDIALAPFYELGMGEVHPTTATHGRGVRSLMEDVLAEYPEIPEEEQQGEATGIKIAIVGRPNVGKSTLVNRLLGEDRVVVYDQPGTTRDSIYINYTRFDKPYTLIDTAGVRRRKNIDLAVEKFSIVKTMQAIADANVVILVMDASEGIVEQDLHLMGTAIEAGRALVIALNKWDGLDESHKYYVKNELERRLRFVDFANIHFISALHGTGVGNLYKSIEQAYQSATDRFSTNYLTRILQDAVREHQPPMINGRRIKLRYAHPGGHNPPVIIVHGNQTDDVPGHYVKYLEKTYRRVLDLHGTPIRIEFRTTDNPYEARKKSMTRQQFIQKRRKEERDRNNPRR
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
B3PDM5
|
Q5ZV64
|
RUVB_LEGPH
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Legionella
|
MLESDRLISSQSIVSEDAMDRAIRPLSLSEYVGQDSVSSQMQIFINAARKRNDPLDHVLIFGPPGLGKTTLANIIAHEMGVNIRQTSGPVIERAGDIAAILTNLQQNDVLFIDEIHRLSPVIEEILYPAMEDYKLDIMIGEGPAARSIKLELPPFTLIGATTRAGLLTSPLRDRFGIVQRLEYYSVDSLTQIVARSAHLLGVPTKPEGAREIALRSRGTPRIANRLLRRVRDYSEVKGNGIITVDMAQQALEMLEVDQHGFDLMDRKLLLAVIEHFNGGPVGIDSIAAAIGEEKGTIEDVLEPFLIQQGFLMRTPRGRIATSKAYQHFGFSAIEQE
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
Q5ZV64
|
Q39F73
|
GUAA_BURL3
|
Glutamine amidotransferase
|
Burkholderia cepacia complex
|
MHDKILILDFGSQVTQLIARRVREAHVYCEIHPNDVSDDFVREFAPKAVILSGSHASTYEDHQLRAPQAVWDLGVPVLGICYGMQTMAVQLGGKVEWSDHREFGYAEMRAHGHTRLLDGIEDFKTDEGHGMLKVWMSHGDKVAELPPGFALMASTPSCPIAGMADEARGYYAVQFHPEVTHTLKGRQIIERFVLQIAGAKPDWIMKNHIEEAVAKIREQVGDEEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDHGLLRLNEGKMVLDMFEGRLHAKVVHVDASEQFLGHLAGVTDPEAKRKIIGREFVEVFQAEAQKLSKAKWLAQGTIYPDVVESGGTKTKKATTIKSHHNVGGLPETLGLKLLEPLRDLFKDEVRELGVALGLPPEMVYRHPFPGPGLGVRILGEVKREFADLLRRADAIFIEELRNTTATAHDAAAGLCGEADVGKSWYDLTSQAFAVFLPVKSVGVMGDGRTYDYVTSLRAVQTTDFMTAHWAHLPYALLGRASNRIINEVRGINRVVYDISGKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q39F73
|
Q2N9V6
|
DNLJ_ERYLH
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Erythrobacter
|
MTTELENLSEAEAANELMRLARQIAKHDRLYHAEDAPEITDQEYDALVRRNAELEAAFPHLVREDSPSRKVGHAVAASPLSKVTHEVRMMSLDNAFADEEVAEFVARVRRYLNIGEDEAIAFTAEDKIDGLSCSLRYENGKLVRAATRGDGQVGEDVTPNVAHIGDIPQELTPLPLAGGAGGGPLDDSGSAPTPDPSRRREGKWNGPAVFEIRGEVYMATADFHALNARLMDEARAEADEKDNAFDTAKVRQFANPRNAAAGSLRQKDASVTATRPLRFWAHGWGAVEGDVPGETQVEVVEQIAAWGVPVSPLFRRCETLEEMLAHYEAIGAQRADLPYEIDGVVYKVDRLDYQQRLGFVAKAPRWAIARKFPAEQAETTLENIDIQVGRTGKLTPVGRLAPVLVGGVTVTNVTLHNRDEIERLGVRPGDRVVVQRAGDVIPQVVRNLTPDEKRDSFEFPDTCPECGSEAVSEEGGVDVRCTGGLICPAQRTERLKHFVSRAALDIDGLGEKTIDQFFALGWLESPADIFRLKDRRDEILALEGWMDKSVDNLLASVEARREPDTARLLLGLGIRHVGAVTARDLMKYFHELPALRETAEKARAGDEEAVVALTSIDGIGSAVVEALGDFFHEEHNRAVWDDLLSEVSPPRYEVETLDSPVAGKTVVFTGKLETMSRDEAKAQAERLGAKASGSVSAKTDLLVAGPGAGSKLKKAQDLGIEVIDEAGWAEIVAAAG
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
Q2N9V6
|
C3P7Z9
|
NAMA_BACAA
|
NADPH dehydrogenase
|
Bacillus cereus group
|
MNSELFSPYTIKDVTLKNRIVMSPMCMYSSENEDGQVTNFHLIHYGTRAAGQVGLVMIEATAVLPEGRISNKDLGIWDDSLIEGLHKTTTFIHDNGAKAAIQLAHAGRKAELETDALAPSAVPFNETMKIPVEMSIHQIKNTILAFQQAAIRSKQAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDSINEVWNGPLFVRISANDYHPDGLTVQDYVQYTKWMKEQGVDLIDCSSGAVVPARIDVYPGYQVQYAKHIKEHANIATGAVGLITTGAQAEQILNNNEADLIFIGRELLRNPYFPRIAANELGFELEEPHQYERAPGKISTNK
|
Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
|
C3P7Z9
|
P31514
|
FST_SHEEP
|
Activin-binding protein
|
Ovis
|
PGGVCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPTSSEQYLCGNDGVTYPSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCGELCPESKSEEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEDEEEDEDQDYSFPISSILEW
|
Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
|
P31514
|
Q2IQG8
|
ISPDF_ANADE
|
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
|
Anaeromyxobacter
|
MIRGERVIGILAAGGSGQRAGVAKQWLVLGGESVLRRSARVLAACDAVDGLVVVVPPGDEARGEAELAGLGKPVRAVAGGPARADSVRNGLAAADGAVVLVHDAARPFASAALAGRVAEAAARDGAALAALPATDTVKRAEAGAEVPRVLETLDRRTVWLAQTPQGFRRAVLEQAYAAAGPSASAATDECALVEAAGAPVTLVPGEPGNFKITGPDDVRRARALLEAPVATGVGYDTHRFAPGRRLVLGGVEFEGDGLLGHSDADVCAHAIGDAILGAAGLGDLGRHFPDTDPRWKGVSSLALLREIAAKAAERGWRVGNCDVTLAAKRPKIAPRAEEMRARLAGALGISPAQVNVKATTGEGMGFVGREEGVAAHAIALLVRAAG
|
Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
|
Q2IQG8
|
P22638
|
HEPA_NOSS1
|
Heterocyst differentiation ATP-binding protein HepA
|
Nostoc
|
MPKSPHKLFKANSFWKENNLILREIKHFRKIAILAVIFSFLAASFEGVSIGFLLSFLQKLTSPNDPIQTGISWVDMILAADAWPIPPIYRISLLILLSTWMRATFNYFGGVYTESAQLNLADRLHKQIFEQLQALRLSYFAQTRSGELINTITTEIERIKQGFSGLAFVLTRIMTVCVYFVVMFSISWQLSIISVLIFLLLAVGLSTLNKRVRETSFGISHANAQFTAVAVEFINGIRTIQAFGTQEFERQRFYKASTNQLNAAIKVVLAWTLVKPIAEGIATTVLISLIVISFATFTLPVASLLTFFFVLVRVIPNIQDINGTVAFLSTLQGSSENIKNILQTNNKPYLKNGKLHFQGLKRSIDLVSVDFGYTADNLVLNNITLTIERGKTTALVGASGAGKTTLADLIPRFYDPTEGQILVDGLDVQYFEINSLRRKMAVVSQDTFIFNTSIRDNIAYGTSGASEAEIREVARLANALQFIEEMPEGFDTKLGDRGVRLSGGQRQRIAIARALLRDPEILILDEATSALDSVSERLIQESIEKLSVGRTVIAIAHRLSTIAKADKVVVMEQGRIVEQGNYQELLEQRGKLWKYHQMQHESGQTNS
|
Acts early in the process of morphological differentiation of heterocysts.
|
P22638
|
A2BTV8
|
Y019_PROM5
|
Nucleoid-associated protein P9515_00191
|
Prochlorococcus
|
MAGFGLPNFGQLTEAFKKAKEIQQNAQKLQDELESMEIEGKSDDEMIKVWISGNQLPLRVEVKDTIAESNKEEIEKNILEAIKKAHETSTTTMKERMNDLTGGLNLNLPGLDNNDS
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A2BTV8
|
A1WGH3
|
ISPE_VEREI
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Verminephrobacter
|
MQALYDLPAPAKLNLFLHIIGRRADGYHLIESVFMLIDWCDTLHFECRADGAISRQDLGAPLPAADLSIRAAHALRAATGCRQGAHIGLLKRLPAQAGIGGGSSDAATTLLALNRLWGLGLSLSALEKIGVTLGADVPFFVRGRNARVAGIGEIITPLAHGQLPPACFAVVKPAAGLETKAIFSSPLLKRASGSATISGFAAADFGRDGDCYQDADFCRNDLQPVAQALCPEVTQAIEWLRARGLQGRMTGSGSAVFAQIPQAPDLGHVGDLGAAPEGWQVRVCENLMLHPLAGWAADED
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A1WGH3
|
O32130
|
LYTH_BACSU
|
Sporulation-specific endopeptidase
|
Bacillus
|
MKVLLSALLLLLFAFEPSASGKKLSDPVLSKRMELYHKIEAVTQIPWYALAAVDQYEENVRSNRKDLPEKAGIISIYIPDDIWSGPENPNPKDDAPLSIKVFDGIGMDGDGDGKAEVSNDEDILYTFSQYLLSYGTDEDNIRIGLWNYYRRDQTVGIISEFMKLFKAYGHIDLGEHAFPLPIRTDYSYRSTWGDARGFGGRRIHEGTDIFAHYGLPVKSTCYGVVEMKGWNRFGGWRIGIRDINNTYHYFAHLNGFAKGIKTGQIVEPGQVIGSVGSSGYGPPGTAGKFPPHLHYGMYKDNGRTEWSFDPYPHLRAWERYEYQKKK
|
L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.
|
O32130
|
Q52243
|
VAPD_AGGAC
|
Virulence-associated protein D homolog
|
Aggregatibacter
|
MYAIAFDLEISELKKHYGDPYNNAYFEVKSELEKIGFEWTQGSVYLSKDPRNNLATVYKAINLLSNIDWFKHSVRDIRAFKVEDWSDFTEIVKTS
|
Cleaves ssRNA, mostly between U:A.
|
Q52243
|
Q7MIT5
|
MNMC_VIBVY
|
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
|
Vibrio
|
MTSITHAELGWNEVGTPVSDQFDDVYFSNVNGLEETRYVFLKQNLIPERWQEFDRRRFVIGETGFGTGLNFLAVWQAFNDFRRANPDATLKELHFISFEKFPLSKQDLIKAHQAWPELAELAEKLHRHYPPAVPECHRIVLDNGAVTLDLWLGDIKDCLPSVPYGEEGIIDTWFLDGFAPSKNPEMWNQDLFNGMAKLARSECRVATFTSAGFVRRGLIEAGFAMKKVKGFGTKREMIAGCMETRQPQSRHAPYFNRTSASHLDSIAIIGGGIASAALAKALVQRGQKVTLYCKHAQAAEGASGNRQGAVYPLLNGSHDGVSRVFAPAFLFTRQFVEQAAQALTFDHDWCGVTQLMWDEKSTNKLDKMLSGNFAPELIQKLSAEETAAKIGLPIDMASVHYPLGGWLCPAELTQALFAQLDTLDNFTAKFEQSVEQLIWDERSQQWQVHTQGQHDTYSAVVIANGHEFQTFSQTADIPLGQVKGQVSHAPATETLSKLKSVLCYDGYMTPVNPNNQHLCIGASYDRRHLDTEFDVNAQQENAEKLTQCVPNQAWAKEVDTSGNLSRQGIRCVSRDHLPFVGNVGDFSAIKRQYADLPHTQAEEIEVISQFPNLFCLLGLGSRGLSSAPLMAELLASQICNDPLPLPVDVLEELHPSRMWVRKLRKGKAITEL
|
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
|
Q7MIT5
|
B8CU43
|
METK_SHEPW
|
Methionine adenosyltransferase
|
Shewanella
|
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVMVGGEVTTSAWVDIEEITRKTVREIGYTHSDMGFDADSCAILNAIGKQSPDINQGVDRADPKEQGAGDQGLMFGYANNETDVLMPAPITYSHKLVKRQSEVRKDKTLPWLRPDAKSQVTFAYNNDGSIAGIDAVVLSTQHREDVSQADLIEGVMETIIKPVLPAKWLSKDTKYFINPTGRFVIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSISIETFGTAKVAEELLIDLVRRHFDLRPYGLTEMLNLARPIYQATAAYGHFGRNEFPWEATDKAEALRADAGL
|
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.
|
B8CU43
|
Q6MAS9
|
GLGA_PARUW
|
Starch [bacterial glycogen] synthase
|
Candidatus Protochlamydia
|
MHIIHIASELAPLAKVGGLADVVLGLCRELSWKGHDVDIIIPKYDCMDSEQIRDLTVDYFELPSFYNGEWFFNTVWMGWVENLKVYFIEPHHPRFFFNRGCFYGCEDDLERFLYFSRTALEFLYKKSILPDIIHLHDWQTAVIAPLYKDMYQKLGYTKPKILFTIHNMEYQGKCAAHDLNYIGLDGNRYQQHSFMQDNLYPHLINLLKGGIVYSDFVTTVSPNYAKEVLTPKEGRGLEATLVEYQHKFKGILNGIDYSYWNPEIDRFLPAHYSLREMPKNKKDRNTVDKKGFIKKILREKLYLAEEHRPIIGCITRLVPQKGIDLIKHTIRHIVEKKGQFILLGSSPIPSINDEFHRLKHQYTDHPHIHLILHHSEELAHLIYAGSDMFIVPSLFEPCGLTQIIALKYGTVPIVRRTGGLADTIIDVDHTDQQPDKKNGYVFDDPDANGIDSAIDRAIHCWFEEPEKWRQLMLNGMKMDFSWNQSSDCYLKIYQAISAKN
|
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
|
Q6MAS9
|
Q0ARM2
|
UVRC_MARMM
|
Excinuclease ABC subunit C
|
Maricaulis
|
MTSQTPQSGEIDDASAAPAQSLAGAKLIADYVRNLPPKPGVYRMFGEDGAVLYVGKARNLKNRVSNYANGRGHSNRIALMIGLTRKMEFVVTQTETEALLLEANLIKSLKPRFNILLRDDKSFPYILIRKDHPAAQLTKHRGARKAKGDYFGPFASVGAVNQTLNTLQKAFLVRTCSDSVYEGRSRACMLHQIKRCAGPCVDLIDPAAYDELVGQATDFLRGRSNALREDLQTRMAQASEAMDFETAAKLRDRIRAIAAVTTDQGINPDGVEEADVVAVHSDGGKSCVQVFFFRAGQNWGNQSFFPRHDMEAEPAEVLAAFIAQFYDDKPAPALILLSHEIEEAELLGEALSLRTERKVSLHTPRRGEKRKLVDRTLTNAREALARRMAESASQTQLLKGVQRVFDLTDLPQRIEVYDNSHIQGTNALGAMIVAGPEGFEKNHYRRFNMKGDDAATNDDFAMMKAMLKRRFSRLLKERDDGAPVPDLVLIDGGKGQLSSVMEIAEELGITDETGITIAAIAKGPERDAGREAFYLPGKPPFKLPMKDPVLYYLQRLRDEAHRFAIGGHRAKRKKQMTDNPLDGIDGIGPSRKKALLAHFGSAKAVRNAALADLEAVDGISRAMARKIHDWFQK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q0ARM2
|
A6WV84
|
GLND_BRUA4
|
[Protein-PII]-UMP uridylyl-removing enzyme
|
Brucella
|
MSAHDLKLEEIVNPETLRRKLNELADSTDENYTSPTVRKVVLQALKDALVRGRANAEGMLMKDGGGTLCAKRLSFLMDTLIEALFEFATTKAYPMINPSKAENMAIVAVGGYGRGGLAPGSDIDLLFLLPYKQTPWGEQVVEYMLYMLWDMGLKVGHSTRNIDECIRLSREDMTIRTAILDARFLTGNRELFKTLVTRFDEEIVKDTGPEFIQAKLAERDQRHRKAGETRYLVEPNVKEGKGGQRDLHTLFWITKYFYRVKTKEELVKLGVLSRAELKLFNKAEDFLWAVRCHMHFATLKAEERLSFDIQPEIAQRLGYTAHPGQNYVERFMKHYFLVAKDVGDLTRIISAALEEQQAKHVPGFNRIFLTFSRRKRKLSADGDFVSENHRINIARPEVFKEDPVNIIRLFHLADKHGLEFHPEAMQSLTRSLKLINSDLRENPEANKLFLEILTSPRNPELILRRMNESGVLGKFIPDFGKIVAMMQFNMYHHYTVDEHLLRCIAVLSEIEHGELENEHPLSNHLITTVKRDRNLLYVALLLHDIAKGRPEDHSVAGARIARRLGPRLGLTPTETETVEWLVREHLTMSMVAQSRDLNDRKTIIDFADTVQTMERLKLLLILTVCDIKAVGPGVWNGWKGQLLRTLFYETELVLTGGFSELSRADRDHQAREALADRLSDWPKDKRDAYLALHYTNYFLTVSLEDQVRHAHFIREADRNERALATMAKPHTFEAVTEITVLAPDHPRLLSIITGACAAAGANIVDAQIFTTGDGRALDTILISREFDTDDDERRRAERVGKVIEDVLSGKAHLPDVLAKRTKPKRAAKAFKVEPRVEINNTLSNKFTVIEVEGLDRPGLLSELTGLISDLSLDIASAHITTFGEKVIDSFYVTDLVGHKISNATRQGNIRRKLLGVLSGENGSKTNGRSSQAAA
|
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
|
A6WV84
|
Q6YQA6
|
SYY_ONYPE
|
Tyrosyl-tRNA synthetase
|
Candidatus Phytoplasma asteris
|
MSFYEELKWRNLIKDCSNETQVKELLDNNQVKFYCGFDPTSHSLTVGHLVQITMILLMQRQGHLPVILVGGATGLIGDPKETEERKLLSLENSLQNAKSIECQLKNILLNKQVEFVNNYQWLSQIDIISFLRNYGKLFNINYMLSKHAVAKRLASGISFTEFSYMILQSLDFHHLYKNHKVRLQLGGSDQWGNITSGLELIRKLEKKSDALGISTPLLLNSDGTKFGKSEKGVLWVNPSMTSPYEIYQYFLNVSDKEVINYLKMLTLIPKQEILELEKNTLENPQQRLAQKALTQNIITLIHSSDILQECIKTNQILFSNAKKESFQEKDFILLQKTLFCHSTKEDILLVDALVQTKLATSKSEAREFIKDNTIKLFNQKIKSLDFAITKKNTLFDKYVLLKKGKKNNALIVF
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
Q6YQA6
|
P24279
|
MCM3_YEAST
|
Minichromosome maintenance protein 3
|
Saccharomyces
|
MEGSTGFDGDATTFFAPDAVFGDRVRRFQEFLDTFTSYRDSVRSIQVYNSNNAANYNDDQDDADERDLLGDDDGDDLEKEKKAASSTSLNILPHRIIISLDDLREFDRSFWSGILVEPAYFIPPAEKALTDLADSMDDVPHPNASAVSSRHPWKLSFKGSFGAHALSPRTLTAQHLNKLVSVEGIVTKTSLVRPKLIRSVHYAAKTGRFHYRDYTDATTTLTTRIPTPAIYPTEDTEGNKLTTEYGYSTFIDHQRITVQEMPEMAPAGQLPRSIDVILDDDLVDKTKPGDRVNVVGVFKSLGAGGMNQSNSNTLIGFKTLILGNTVYPLHARSTGVAARQMLTDFDIRNINKLSKKKDIFDILSQSLAPSIYGHDHIKKAILLMLMGGVEKNLENGSHLRGDINILMVGDPSTAKSQLLRFVLNTASLAIATTGRGSSGVGLTAAVTTDRETGERRLEAGAMVLADRGVVCIDEFDKMTDVDRVAIHEVMEQQTVTIAKAGIHTTLNARCSVIAAANPVFGQYDVNRDPHQNIALPDSLLSRFDLLFVVTDDINEIRDRSISEHVLRTHRYLPPGYLEGEPVRERLNLSLAVGEDADINPEEHSNSGAGVENEGEDDEDHVFEKFNPLLQAGAKLAKNKGNYNGTEIPKLVTIPFLRKYVQYAKERVIPQLTQEAINVIVKNYTDLRNDDNTKKSPITARTLETLIRLATAHAKVRLSKTVNKVDAKVAANLLRFALLGEDIGNDIDEEESEYEEALSKRSPQKSPKKRQRVRQPASNSGSPIKSTPRRSTASSVNATPSSARRILRFQDDEQNAGEDDNDIMSPLPADEEAELQRRLQLGLRVSPRRREHLHAPEEGSSGPLTEVGTPRLPNVSSAGQDDEQQQSVISFDNVEPGTISTGRLSLISGIIARLMQTEIFEEESYPVASLFERINEELPEEEKFSAQEYLAGLKIMSDRNNLMVADDKVWRV
|
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.
|
P24279
|
A9N026
|
RSXD_SALPB
|
Rsx electron transport complex subunit D
|
Salmonella
|
MVFRIASSPYTHNQRQTSRIMLLVLIAALPGIAAQTWFFGWGTLFQIVLAAITALVAEAIVLRLRKQSVASHLQDYSALLTGLLLAVSIPPLAPWWMVVLGTGFAIIIAKQLYGGLGQNPFNPAMIGYVVLLISFPVQMTSWLPPYEIAATTPDMLDTLRMIFSGHTASGGDMTLLRIGIDGISQATPLDTFKTSLRAGHSVEQIMQYPIYSGALAGVGWQWVNLAWLVGGVFLLWQKAIRWHIPVSFLLTLALCAALGWLFSPATLASPQLHLLSGATMLGAFFILTDPVTASTTNRGRLIFGALAGVLVWLIRSFGGYPDGVAFAVLLANITVPLIDYYTRPRVYGHRKG
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
|
A9N026
|
Q5RC79
|
ZFP1_PONAB
|
Zinc finger protein 1 homolog
|
Pongo
|
MNKSQGSVSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSVEVWKADDQMERDHRNPDEQARQFLILKNQTPIEERGDLFGRALNLNTDFVSLRQVPYKYDLYEKTLKYNSDLLNSNRSYAGKQTDECNEFGKALLYLKQEKTHGGVEYSEYNKGGKALSHKAAIFKHQKIKNLVQPFICTYCDKAFSFKSLLISHKRIHTGEKPYECNVCKKTFSHKANLIKHQRIHTGEKPFECPECGKAFTHQSNLIVHQRAHMEKKPYECSECGKTFAQKFELTTHQRIHTGERPYECNECAKTFFKKSNLIIHQKIHTGEKRYECSECGKSFIQNSQLIIHMRTHTGEKPYECTECGKTFSQRSTLRLHLRIHTGEKPYECSECGKAFSRKSRLSVHQRVHIGEKP
|
May be involved in transcriptional regulation.
|
Q5RC79
|
Q8R7V5
|
RL4_CALS4
|
50S ribosomal protein L4
|
Caldanaerobacter
|
MPKVPVYNVKGEQVGEIELKDSVFGVPVNVAVMHQAVVNYLANQRQGTHSTKTRGEVRGGGRKPWRQKGTGRARQGSIRAPQWIKGGVVFGPKPRDYSYKLPKKVKRLALKSALSSKVRDNEIIVLDEFKLEQPKTKKVAELLKNFNAKSALIVVPQGEKNVELSARNMPNAKALYANLLNTYDVLKYEKFIITKDAVAIVEEVFA
|
Forms part of the polypeptide exit tunnel.
|
Q8R7V5
|
Q6MB27
|
GRPE_PARUW
|
HSP-70 cofactor
|
Candidatus Protochlamydia
|
MVDKDEEQIKQNVEEDLSSTVEQTGEENIEFPSAPNHPKQVLVTDEELKALKKEATEYKDKYLRLLADSENARKRLQKERQEISRYALENMVVDFLKPLDNLENALKFAQGMSDEVKNWAFGFQMILTQFKDVLASNGITALESQGTFFDPHLHEAIEMVETDSYAPGIIVEENVRGYKMGDRMIRPARVKVAKAISAIDPQDKSELNENN
|
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.
|
Q6MB27
|
P28448
|
RBL_RORGO
|
Ribulose bisphosphate carboxylase large chain
|
Roridula
|
VGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIESVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYCKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQDETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIIMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYIEKDRARGIYFSQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIRRAGKWSPELAAACEVWKEIKFEF
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P28448
|
Q8U7Y5
|
GLYA2_AGRFC
|
Serine hydroxymethyltransferase 2
|
Agrobacterium tumefaciens complex
|
MLNRLSHNTVSDTVIADAIAEELDRQKTQIELIASENIVSADVLAAQGSVLTNKYAEGYPGKRYYGGCEFVDKVEQVAIDRLKQLFGAEFANVQPHSGAQANQAVFLALLQPGDRIMGLSLAHGGHLTHGSPVTMSGKWFDVVSYEVDPETHLIDMEKVREKALETKPKLIVAGASAYPRQIDFAGFREIADEVGAYLMVDMAHYAGLIAGGHYPNAVPHAHVTTSTTHKTLRGPRGGVILTNDADLAKKLNSAVFPGNQGGPLMHVIAAKAVAFGEALRPEFSDYAGQVIANAQALAKVLIQGGLGIVSGGTDSHMVLVDLRPKGVTGKIAEIALERAGLTCNKNSIPNDPEKPFVTSGIRLGSSAGTTRGFGVLEFEKIGALILRVIDALATNAEGDSAVEAEVREEVAALCEAFPIYVS
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
Q8U7Y5
|
Q88I82
|
DNAE2_PSEPK
|
Error-prone DNA polymerase
|
Pseudomonas
|
MAAGLVRMNTPGYAELHCLSNFSFQRGASSADELFRRAREQGYQALAITDECTLAGIVRAWQAAKVHQLRLIVGSEVQLCDGPKLVLLVENLTGYQNLCALITRARRRAEKGAYQLFRDDLLLHHQGLLALWVAADSGDTATGAWLRSVFAERLWLAVHLHRGSDDAVRLQRLRALAADVGIRAVACGDVHMHVRGRRALQDCMTAIRQHCQVSEAGRFLFANGERHLRSQAQLAELYPLDLLAETLVIARRCQFDLSELNYQYPRELVPEGHTPASWLRELCEQGMPLRWPDGPSGKVRDVLAKELGLIEELGYESYFLTVHDIVAFARSQRILCQGRGSAANSVVCFVLGITELDPMKHHLLFERFLSRERNEPPDIDVDFEHDRREEVIQYVFRRYGRHRAALTAVVNTYHAAGAVRDVARALGLPADQVDALAKCCGRWSDRIPDDQRLAEAGFEAGSPSLRRVLVLAGELIGFPRHLSQHPGGFVISQQPLDQLVPVENAAMPERTVIQWDKDDLDMVGLLKVDVLALGMLSALRRCFDQLQHHRGRHLTLATIPSEDPATYAMISRAETMGVFQIESRAQMAMLPRLRPQKFYDLVIEVAIVRPGPIQGDMVHPYLRRRLKQEPVTYPSPQLKEVFERTLGVPLFQEQVMELAMVAADYTPGEADQLRRSMAAWKRHGGLEPHRERLVQGMLRNGYTLAFAERIFEQIKGFGSYGFPESHAASFALLCYASSWLKCHEPAIFTCALVNSWPMGFYSPDQLLQEARRQGIEVRPVDVCHSDWDCTLEPDAEGTLAIRMGLRLVRGLAEADAKRVQQARSQRPWRNVEDLCLRAGLDARARARLADGGALRALASDRHQARWQVAAVQPQLPLFADVQALPEEPVQLPVPTVGEDLMADYQTLGTTLGPHPLALLRARLRALGCRSSSELQGVEHGDNIAVAGLVVGRQRPQTASGVTFVTLEDEHGMVNVVVWRALAERQRRALVGSQLLKVSGRLEQENGVRHLIARRLEDVSPLLQGLDVRSRDFH
|
DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
|
Q88I82
|
O67365
|
SPEE2_AQUAE
|
Spermidine synthase 2
|
Aquifex
|
MSVSTALKLCIFFTGFAGIVAEYSLATLATYLLGNAVLQWSVVISIFLLSMGLGSHASRYIPDDKTPLAFVLAELFLSLLVPFSVPIAYHFANNFLHLQTVIYGLSFVIGSLIGLEIPLAVRINNMYEELKVNISSVLEKDYLGSVPAGLLYAYLFLPKLGLPLTAILAGFFNLISAFLLVKVLKPKKFLKFLAIFTFFLLATYAVGHKRITLYEEQKFYGEEIIHFEQTPYQKIVLTRFGKHYSLYLDGHLQFSTLDEKRYHETLVHVPASFLKRYEKALILGGGDGLALRELRKYPFGEIHLVDLDPKMIEFSKKNLVMRKINENSFYDTRLKVFSEDAFNFVKKTKEKYDFVIVDLIDPRTPSSARVYSLEFYMSLKNKLKEDGIFITQAGDTFYKREVFCSILKTIKKAGFYAYPLVVYIPTFGEWGMVIGSKEPLNFENFELKEKTEFLNRERALAFYTLGKSLECPNVEVNTLLKPVLIYYYYKIQN
|
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
|
O67365
|
Q9K165
|
SLAM1_NEIMB
|
TPR repeat-containing protein NMB0313
|
Neisseria
|
MVIFYFCGKTFMPARNRWMLLLPLLASAAYAEETPREPDLRSRPEFRLHEAEVKPIDREKVPGQVREKGKVLQIDGETLLKNPELLSRAMYSAVVSNNIAGIRVILPIYLQQAQQDKMLALYAQGILAQADGRVKEAISHYRELIAAQPDAPAVRMRLAAALFENRQNEAAADQFDRLKAENLPPQLMEQVELYRKALRERDAWKVNGGFSVTREHNINQAPKRQQYGKWTFPKQVDGTAVNYRLGAEKKWSLKNGWYTTAGGDVSGRVYPGNKKFNDMTAGVSGGIGFADRRKDAGLAVFHERRTYGNDAYSYTNGARLYFNRWQTPKWQTLSSAEWGRLKNTRRARSDNTHLQISNSLVFYRNARQYWMGGLDFYRERNPADRGDNFNRYGLRFAWGQEWGGSGLSSLLRLGAAKRHYEKPGFFSGFKGERRRDKELNTSLSLWHRALHFKGITPRLTLSHRETRSNDVFNEYEKNRAFVEFNKTF
|
Required for correct export to the cell surface of some cell outer membrane lipoproteins both in Neisseria and heterologously in E.coli.
|
Q9K165
|
P31460
|
DGOR_ECOLI
|
HTH-type transcriptional repressor DgoR
|
Escherichia
|
MTLNKTDRIVITLGKQIVHGKYVPGSPLPAEAELCEEFATSRNIIREVFRSLMAKRLIEMKRYRGAFVAPRNQWNYLDTDVLQWVLENDYDPRLISAMSEVRNLVEPAIARWAAERATSSDLAQIESALNEMIANNQDREAFNEADIRYHEAVLQSVHNPVLQQLSIAISSLQRAVFERTWMGDEANMPQTLQEHKALFDAIRHQDGDAAEQAALTMIASSTRRLKEIT
|
Involved in the regulation of D-galactonate metabolism . Represses the expression of the dgoRKADT operon by binding to two closely spaced inverted repeats in the cis-acting element, which overlap with the D-galactonate responsive dgo promoter . Employs a derepression mechanism using D-galactonate as a specific effector molecule .
|
P31460
|
A2SH39
|
RBFA_METPP
|
Ribosome-binding factor A
|
Methylibium
|
MKHKRAIPNRGLRVADQIQRDVAGLIRELKDPRIGMVTIQAVEVTPDYAHAKVFFSVLIGDPAECAAALNEAAGYLRNSLFKRLQIHTVPTLHFQFDRTTERAADLNALIHQANATRAKDADDQPGATEA
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
A2SH39
|
B2SSQ1
|
GCST_XANOP
|
Glycine cleavage system T protein
|
Xanthomonas
|
MTQKTILNDTHRALGAKMVDFGGWDMPIHYGSQLDEHHQVRRDAGMFDVSHMTVVDLHGARVRAFLRDLLANSVDKLKVCGKALYTCMLNPQGGVIDDLIVYYMSEDFFRLVVNAATREKDLQWIGEQAVRFDVRVEERSDFAMIAVQGPNARANVIDLLDPADTAAASKLGRFAALQTRSRDGIELFLARTGYTGEDGFEIVLPQEAAVAFWNALLAQGVKPAGLGARDTLRLEAGMHLYGQDMDDAVTPYEAALAWTIALDEGRDFIGRRVLESQKAQGAPCQLIGVVMDDKGVLRHGQAVFTASGEGEILSGTFSPTLGKAIAFARVPAGSIDQLRVDIRGKQVPLRAVKFPFVRDGQAQPGVLGD
|
The glycine cleavage system catalyzes the degradation of glycine.
|
B2SSQ1
|
P0C917
|
RBL1B_ACIFR
|
Ribulose bisphosphate carboxylase large chain 2
|
Acidithiobacillus
|
MAVKTYNAGVKDYRNTYWEPDYSVKDTDILAVFKITPQAGVDREEAPAAVAAESSTGTWTTVWTDLLTDLDYYKGRAYRIEDVPGDDTCFYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRALRLEDVRFPIAYVKTCGGPPHGIQVERDIMNKYGRPLLGCTIKPKLGLSAKNYGRACYEGLRGGLDFTKDDENVNSQPFMRWRQRFDFVMEAIQKAEAETGERKGHYLNVTAPTPEEMYKRAEYAKEIGAPIIMHDYITGGFCANTGLANWCRDNGMLLHIHRAMHRVLDRNPHHGIHFRVLTKILRLSGGDHLHSGTVVGKLEGDREATLGWIDIMRDRFIKEDRSRGIFFDQDWGSMPGVMPVASGGIHVWHMPALVTIFGDDSVLQFGGGTLGHPWGNAKGAAANRVALEACVEARNRGVAIEKEGKAVLTEAAKHSPELKIAMETWKEIKSEFDTVDKLDVAHK
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
|
P0C917
|
Q52978
|
PHAAB_RHIME
|
pH adaptation potassium efflux system protein A/B
|
Sinorhizobium
|
MTRPASVLAGPKSRPPIHSQGDKTIEYAEKLLSVFILVPFAGSLIAIFFPSDQRGAISWFAGAIALVCFLVTAGLYPYVASGGVLHYRIDWVPELGLNFTLRMDGFAWLFSALITAIGVLVALYARYYMAEEDPVPRFFALFLAFMGSMLGVVLSGNLILLAVFWELTSIVSFLLIGYWHHNAHARDGARMALTITGTGGLAMFVGLIIIGKIVGSYELDAVLASGDAIRNHPLYGTVLVLVLLGALTKSAQFPFHFWLPHAMAAPTPVSAYLHSATMVKAGVFLLVRFWPVMAGTEAWFWIVGLAGLTTLLLGAYFAIFQQDLKGLLAYSTISHLGLITVLLSLGSPLAAVAAVFHIVNHATFKASLFMAAGIIDHESGTRDIRRLGGLFHFMPITATLAMVASAAMAGVPLLNGFLSKEMFFAEAIETHLVNPLDTVTPYVATIAGMFAVTYSLRFIHGVFFGRPPADLPRKPHEPPRWMRAPLDFLVLACLVVGIIPAQTIGPFLHTAVLSVLREGTPDYSLSVWHGWNIPLIMSFVALSGGIGLYFLMRSYLATAVEGPPVFRLLQGQRIFERVLVTLSWKWARWLEQRLGTRRLQPQMRLLVFLALAAGASPLLLGNFELPPLVIRGIDPAFALLWAIGIACAIGSAYQAKFHRLASLVLLGGAGLVTCITFVWLSAPDLAVTQLLVEIVTTVLILLGLRWLPKRIEEPVAAEDISIRVRLRRLRDLLLAIGAGGGMMLIAYTVMTRPLPETIASYFLERAYREGGGTNVVNVILVDFRGFDTLGEIAVLCIVALTVFALLLRFRPQSDSLEAPEQQKVQNAFDDDHPDRAAGDSVAEYLFIPAVIMRWMFPVTGMLAAFLFLRGHDLPGGGFAAGIAMSIGFILQYMSGGTRWVEERLRIHPLRWMSIGLLVATATGVGSWFFGYPFLTSHAQYASLPVVGKFPLASAILFDLGVFSLVLGATVLILIALAHQSVRAPRAHAKAARSDKEAVR
|
Part of a K(+) efflux system which is required for the adaptation of R.meliloti to alkaline pH as well as for the infection process during symbiotic nodule development.
|
Q52978
|
P00472
|
MTE1_ECOLX
|
Modification methylase EcoRI
|
Escherichia
|
MARNATNKLLHKAKKSKSDEFYTQYCDIENELQYYREHFSDKVVYCNCDDPRVSNFFKYFAVNFDNLGLKKLIASCYVENKEGFSSSEAAKNGFYYEYHKENGKKLVFDDISVSSFCGDGDFRSSESIDLLKKSDIVVTNPPFSLFREYLDQLIKYDKKFLIIANVNSITYKEVFNLIKENKIWLGVHLGRGVSGFIVPEHYELYGTEARIDSNGNRIISPNNCLWLTNLDVFIRHKDLPLTRKYFGNESSYPKYDNYDAINVNKTKDIPLDYNGVMGVPITFLHKFNPEQFELIKFRKGVDEKDLSINGKCPYFRILIKNKRLQK
|
A methylase that recognizes the double-stranded sequence 5'-GAATTC-3', methylates A-3 on both strands, and protects the DNA from cleavage by the EcoRI endonuclease.
|
P00472
|
Q3Z4S5
|
KAD_SHISS
|
Adenylate monophosphate kinase
|
Shigella
|
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYFKEAEAGNTKYAKVDGTKSVAEVRADLEKILG
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
Q3Z4S5
|
Q8HYJ3
|
FUT5_HYLLA
|
Galactoside 3-L-fucosyltransferase
|
Hylobates
|
MDLLGAAKPQWPWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPRLMAVEPVTGAPNGSRCQDSMAAPARPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSNVYPQADAVIVHHWDIMRTPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWEPGSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLAPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTVRSIAAWFN
|
Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosaccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens. Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate. Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an alpha (1,4) linkage. Preferentially catalyzes sialylated type 2 oligosaccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide acceptors. Lactose-based structures are also acceptor substrates.
|
Q8HYJ3
|
Q5F8T1
|
LEUC_NEIG1
|
Isopropylmalate isomerase
|
Neisseria
|
MTAQTLYDKLWNSHVVREEGDGTVLLYIDRHLVHEVTSPQAFEGLKMAGRKLWRIDSVVSTADHNTPTGDWDKGIQDPISKLQVDTLDQNIKEFGALAYFPFMDKGQGIVHVMGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHTMATQCITAKKSKSMLIAADGKLKAGVTAKDVALYIIGQIGTAGGTGYAVEFGGEAIRSLSMEGRMTLCNMAIEAGARSGMVAVDQTTIDYVKGKPFAPEGEAWDKAVEYWRTLVSDEGAVFDKEYRFNAEDIEPQVTWGTSPEMVLNIGGKVPNPAEETDPVKRSGIERALEYMGLKAGTPLNEIPVDIVFIGSCTNSRIEDLREAAAIAKGHKKAGNVQRVLIVPGSGLVKEQAEKEGLDKIFIEAGFEWREPGCSMCLAMNADRLAPRQRCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAVTGHFTDIRTMA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q5F8T1
|
C1DAU3
|
RPOA_LARHH
|
Transcriptase subunit alpha
|
Laribacter
|
MQNSASEFLKPRLIDVQPVSATQARVAMEPFERGYAYTLGNALRRILLSSMPGFAPTEVSIAGVLHEYSALDGVREDVVDILLNLKGVVFKLHGRDSVLLTLKKEGEGAVRASDIDLPHDVEVVNPDHVICHLAAGGKIDMEIKVEKGRGYQPAPARVKQDDNRQIGTILLDASFSPLRRVSFSVESARVEQRTDLDRLVMDIETNGVIEPEEAVRSAARILIDQLSIFADLQGTTVEVVEERAPQVDPILLRPVDDLELTVRSANCLKAENIYYIGDLIQRTETELLKTPNLGRKSLNEIKEVLASKGLTLGMKLENWPPAGLEKP
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
C1DAU3
|
P46044
|
NIFB_FRAAL
|
Radical SAM assemblase NifB
|
Frankia
|
MTGEPAFAAAPAGGLPRRSAQAPASAGGCKTTTSCGTSAPVQDPEIAEKIANHPCYTAEAHQYYARMHVAVAPGCNIQCNFCNRKFDCANESRPGVTSTLLTPEDALAKVNVVASEIKQMSVLGIAGPGDPLANPKPTFRTIELVARDCPDIKLCLSTNGLRLPEFVDRIADLNVDHVTITINMIDPEVGERIYPWVAWRGKRYTGREASKILSEQQLAGLAALTERKILCKVNSVMIPGINDEHLVEVSRTVKGLGAFLHNVMPLVSAPEHGTVFGLTGQRGPTPQELKALQDRCEQDDGAEMNMMRHCRQCRADAVGLLGEDRGDDFLPETFQGREIVYDLAGRQQAHEEIERWRTEVAATRQTLNIATGARTPDVPAAEPVRPAEVVLVAVATKGSGVVNQHFGHAGEFWIYEAGPGWARLVQTRDVDRYCNGPSDCDEDASKLDRTIEMLSDCAAVLCSKIGLGPREALEEAGIEPVEIYDLIDKAVAEIGARLVTDRAPAEVGTP
|
Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
|
P46044
|
B9E7A4
|
PFKA_MACCJ
|
Phosphohexokinase
|
Macrococcus
|
MKKIAVLTSGGDAPGMNAAVRAVVRKAMYYDIEVYGVYQGYQGLINNNIKKMERGTVGDKIQRGGTFLQSARCPEFKDPEVRKQAIANLNNLGIEGLVVIGGDGSYRGAQRLNEEGIKTIGIPGTIDNDINGTDFTIGFDTALNTIVEAIDKIRDTASSHERTFIVEVMGRDAGDLALWSGLAGGAETVLCPEHRKDVKVIADKIQQGIERGKKHSIIVVAEGVMTGEECGQELKKYINVDTRISVLGHMQRGGSPSGMDRVLASRLGGYAVELLMNDETGLAVGIQNNSLSKTKFEDIFTSVHHLDEKMYELSNELSI
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
B9E7A4
|
P52405
|
CHI3_SOLTU
|
Endochitinase 3
|
Solanum
|
EFTIFSLLFSLLLLNASAEQCGSQAGGALCAPGLCCSKFGWCGNTNDYCGPGNCQSQCPGGPGPSGDLGGVISNSMFDQMLNHRNDNACQGKNNFYSYNAFISAAGSFPGFGTTGDITARKREIAAFLAQTSHETTGGWPSAPDGPYAWGYCFLREQGSPGDYCTPSSQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDSVISFKSAIWFWMTPQSPKPSCHDVITGRWQPSGADQAANRVPGFGVITNIINGGLECGHGSDSRVQDRIGFYRRYCGILGVSPGDNLDCGNQRSFGNGLLVDTV
|
Defense against chitin-containing fungal pathogens.
|
P52405
|
P34539
|
ATP5E_CAEEL
|
Putative ATP synthase subunit epsilon, mitochondrial
|
Caenorhabditis
|
MVAWRAAGLNYVRYSQIAAQVVRQCTKGGANVKKPQATLKTTAWENGKMVSKSQ
|
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
|
P34539
|
B9WYE6
|
VRDA_ASPPA
|
VHA reductase
|
Aspergillus
|
MEYARLGDSGLKVSKVILGCMGYGSPEWQGWVLNEEESLPLIEHAYNKGIRTWDTADMYSHGKSEEIVGKALKKYNIPRSRVVILTKCYFGVDDQGNFPSPLSTGRQNEGDYLNRVGLSRRHILEAVDASVERLGTYIDVLQIHRLDRETPREEIMRALNDVVESGKARYIGASSMAAWEFQTLQNIAIRNGWHKFISMQNYHNLIAREEEREMIPYCLDSGVSLIPWSPVARGALARPWASRSTLRENTDAGISILVRARESESDKAIIDRVEELADKKGISMAQVAIAWSLSHPSEYPIVGLNTKDRIDEAVASVQVKLTPEEIQYLEEPYVPKAIHPGER
|
Catalyzes 3 reactions: from hydroxyversicolorone (HVN) to versicolorone (VONE), from versiconal hemiacetal acetate (VHA) to versiconol acetate (VOAc) and from versiconal (VHOH) to versiconol (VOH). Probably not an aflatoxin biosynthesis gene: may be involved in the vertical branching steps connecting the main pathway from HVN to VHOH with the side pathway from VONE to VOH.
|
B9WYE6
|
Q57L31
|
TRMD_SALCH
|
tRNA [GM37] methyltransferase
|
Salmonella
|
MFIGIVSLFPEMFRAITDYGVTGRAVKNGLLNIQSWSPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGVDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHEASAIEDSFADGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q57L31
|
A3N2R0
|
UREG_ACTP2
|
Urease accessory protein UreG
|
Actinobacillus
|
MRKYIKIGVAGPVGAGKTALIERLTREIASKYSVAVITNDIYTQEDAEFLTKNSLLPPERIMGVETGGCPHTAIREDASMNLEAVDEMVARFPEVELIFIESGGDNLSATFSPDLADVTIFVIDVAQGEKIPRKGGPGITRSDLLVINKTDLAPFVGADLSVMERDARRMRNGQPFIFTNLMKNENLDGVIGWIEKYALLKNIEDPASLVR
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
A3N2R0
|
P35540
|
RPOS_SHIFL
|
Sigma-38
|
Shigella
|
MSQNTLKVHDLNEDAEFDENGVEVFDEKALVEEEPSDNDLAEEELLSQGATQRVLDATQLYLGEIGYSPLLTAEEEVYFARRALRGDVASRRRMIESNLRLVVKIARRYGNRGLALLDLIEEGNLGLIRAVEKFDPERGFRFSTYATWWIRQTIERAIMNQTRTIRLPIHIVKELNVYLRTARELSHKLDHEPSAEEIAEQLDKPVDDVSRMLRLNERITSVDTPLGGDSEKALLDILADEKENGPEDTTQDDDMKQSIVKWLFELNAKQREVLARRFGLLGYEAATLEDVGREIGLTRERVRQIQVEGLRRLREILQTQGLNIEALFRK
|
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response.
|
P35540
|
P53251
|
SLX9_YEAST
|
Ribosome biogenesis protein SLX9
|
Saccharomyces
|
MVAKKRNTLRSKVSARNSQNFGPDVANNGILDESYDIESDPRAFLHQPKETKKEKLLNRQNTFLSNLKGKSTLNDGIAANFDGISKSSIRRRKRKLREELKPRMQDLLTSLEQEKDLRGIIENSSKDMNNDDDIDMDSKIRFVDTKEMNLKKIEPGSVRIKKNQPNIRNQKGAKALAANETARFNQVLTNQDFQKNPFGALREVIKLQKQ
|
Involved in ribosome biogenesis. Required for normal pre-rRNA processing in internal transcribed spacer 1 (ITS1). May be involved in the movements of the replication forks.
|
P53251
|
Q661H9
|
YIDC_BORGP
|
Membrane protein YidC
|
Borreliella
|
MNQSKKILRTVYLSLFLIGLFMLINDIFSSIMLSFKSSDKEVQFDLNKSFDDNEIFLSKSNGFDLINKSQNIVVETEIYFATFSTFRGNLVSLKLKNHLNLEKDPTDLINVDYKNETFFDVSLDYLVEDLFLYKKIDNLNHEFKAYFKNHGKIYEYVKKYTFSEKNEYLMKFTVIVNSLNDYDLFDIDSYKIVFSSEIERLSDKAKLQYNNYLSQIIYYDNKLKYGKDGLSINNPRWIGSSTKYFEVLISRENMEVEFKKERGVLKSFIVNNVGNKKNISDEFFIYAGPKDNRYLDIFDKSGDNTFGLSDIAFGMSVEKSLWYLIQVPMQMVMQVFYDVIPNWGLSIIFLTIVVRILIFPLTFKGFRATAELSKLQPKMKELQVKFKHDPKKLNEEMGRLYKEEGVNPLGGCFPVILQLPIFFALYSLVNNLFLLRGASFIPGWIDDLSIGDSVYNFGYRLYFVSWTDIRILPFIMMFTQLGSTIVSSNLDLKNLGAQQKFLYFGMPIMFFFILYNMPSGLLIYWITTNIFTILQQYYIKMHLS
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
Q661H9
|
A1YFW6
|
ZN449_PANPA
|
Zinc finger protein 449
|
Pan
|
MAVALGCAIQASLNQGSVFQEYDTDCEVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIEDLQRELDIPEQQVDMHDMLLEELAPVGTAHIPPTMHLESPALQVMGPAQEAPVAEAWIPQAGPPELNYSATGECQNFLDPGYPLPKLDMNFSLENREEPWVKELQDSKEMKQLLDSKIGFEIGIENEEDTSKQKKMETMYPFIVTLEGNALQGPILQKDYVQLENQWETPPEDLQRDLAKLVDQQNPTLGETPENSNLEEPLNPKPHKKKSPGEKPHRCPQCGKCFARKSQLTGHQRIHSGEEPHKCPECGKRFLRSSDLYRHQRLHTGERPYECTVCKKRFTRRSHLIGHQRTHSEEETYKCLECGKSFCHGSSLKRHLKTHTGEKPHRCHNCGKSFSRLTALTLHQRTHTEERPFKCNYCGKSFRQRPSLVIHLRIHTGEKPYKCTHCSKSFRQRAGLIMHQVTHFRGLI
|
May be involved in transcriptional regulation.
|
A1YFW6
|
Q73RN8
|
HUTI_TREDE
|
Imidazolone-5-propionate hydrolase
|
Treponema
|
MTLFISDSIFSSTEKKGVDFDKAFAGYIVVENGLIQKVGKGDAPESLKSQAEKIIDARGKTITAGLVDAHTHLVHGGSREHELAMKLAGKTYLEIHASGGGIFSTVRATRAASKEELTQKALTSLDRMLIHGTTTAESKSGYGLDMETEIKCLEINSYLNKNHPIDIVSTYMGAHATPPEFKDNKEGYIKFMIEEVMPEVKKRGLAEFSDAFCEDKIFSVEETERIMKAAADLGFKLKLHADEIIPLKGAELAAKMNAHSAEHLMAISDEGITALAKSGTVAVLLPATSFFLMSPIYAPAKKMIEEGVRVALATDYNPGSSPTENLQMAMWAACYKMKLLPAQILRGVTINAAYAIDREKTIGSIEEGKQADLVIFDAPNIDFLVYHFGVNSVDQVWKKGKLVAEKGRLVYKN
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
Q73RN8
|
Q8GU92
|
AB35G_ORYSJ
|
Pleiotropic drug resistance protein 11
|
Oryza sativa
|
MDAAAEMQKVVSLRRGGGGSSSRGAASMWWSADNGVFSRSRASSSGEDGEDDEEALRWAALEKLPTYDRVRRAVLPVVEEGGGGGEAGKKVVDVLSLGPQERRALLERLVRVAEDDNERFLLKLKERIDRVGIDIPTIEVRFEHLEAEAEVRVGNSGLPTVLNSMTNKLEGAANALGILPNKKQTMPILHDVSGIVKPRRMTLLLGPPGSGKTTLLLALAGRLGKDIKFSGQVTYNGHQMEDFVPQRTAAYISQHDLHIGEMTVRETLSFSARCQGVGSRFDMLTELSRREKAANIKPDADIDAFMKASAMEGQETNLITDYILKILGLDICADTMVGDDMVRGISGGQRKRVTTGEMLVGPANALFMDEISTGLDSSTTFQIVKSLRQAIHILGGTAVISLLQPAPETYDLFDDIILLSDGQIVYQGPREGVLEFFELMGFKCPERKGVADFLQEVTSRKDQKQYWMQHDKPYRYVPVKDFASAFQSFHTGKSIANELATPFDKSKNHPAALTTSRYGVSAMELLKANIDREFLLMKRNSFVYIFRACQLMVVSAIAMTVFFRTKMHRDSVTDGVIFMGALFFSVMMIMFNGLSELPLTIFKLPVFFKQRDLLFFPAWTYTIPSWILKIPMSFIEVGGFVFMSYYVIGFDPSAGRFFKQYLLMLAINQMAAALFRFVGGAARNMIVANVFGSFMLLIFMVLGGFILVREKVKKWWIWGYWISPMMYAQNAISVNEFLGHSWDKVLNNSLSNETLGVQALRSRGVFPEAKWYWIGFGALLGFIMLFNGLFTLALTYLKPYGKSQPSVSEEELKEKQANINGNVLDVDTMASSTNLAIVDNTETSSEIADNSQPTQRGMVLPFAPLSLTFDNIKYSVDMPQEMKAHGIVEDRLELLKGVSGSFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGNITISGYPKKQETFARVSGYCEQNDIHSPQVTVSESLLFSAWLRLPKDVDSNTRKMFIEEVMELVELKPLRDALVGLPGVNGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLMKRGGEEIYVGPLGHQSSELIKYFEGIKGVSRIKDGYNPATWMLEVSTISQEQALGVDFCDIYRKSELFQRNKALIQELSTPPPGSSELYFPTKYSLSFLNQCLACLWKMHLSYWRNPPYNAIRLFFTTVIALLFGTIFWDLGGKTGKSQDLFNAMGSMYSAVLFIGVLNSQSVQPVVSVERTVFYRERAAGMYSAFPYAFGQVAIEFPYTLVQSIIYGIIVYSMIGFKWTAAKFFWYLFFMFFTFLYFTFYGMMAVGLTPSYHVASIVSSAFYGIWNLFSGFIIPRPKVPIWWRWYCWICPVAWTLYGLVASQFGDIMTPMDDGTPVKIFVENYFDFKHSWLGVVAVVIVAFTMLFAFLFGFAIMKLNFQKR
|
May be a general defense protein.
|
Q8GU92
|
Q9NDV2
|
RNKA_CERCA
|
Ribonuclease kappa-A
|
Ceratitis
|
MVLYFSPVLTFFLANFFNSKSTTTENLQVFLVENQHRDSKRKINPTFSKKGIEVRQQNENLWSKIVALRFDYSVWGIIQLVLMMGLFFYINSVALIEDLPIDEEFNSVEEFYTAATSAYNQNAYTVGLPVHLCAYASI
|
Endoribonuclease.
|
Q9NDV2
|
P24153
|
HAPT_VIBCH
|
Vibriolysin
|
Vibrio
|
MKMIQRPLNWLVLAGAATGFPLYAAQMVTIDDASMVEQALAQQQYSMMPAASGFKAVNTVQLPNGKVKVRYQQMYNGVPVYGTVVVATESSKGISQVYGQMAQQLEADLPTVTPDIESQQAIALAVSHFGEQHAGESLPVENESVQLMVRLDDNQQAQLVYLVDFFVASETPSRPFYFISAETGEVLDQWDGINHAQATGTGPGGNQKTGRYEYGSNGLPGFTIDKTGTTCTMNNSAVKTVNLNGGTSGSTAFSYACNNSTNYNSVKTVNGAYSPLNDAHFFGKVVFDMYQQWLNTSPLTFQLTMRVHYGNNYENAFWDGRAMTFGDGYTRFYPLVDINVSAHEVSHGFTEQNSGLVYRDMSGGINEAFSDIAGEAAEYFMRGNVDWIVGADIFKSSGGLRYFDQPSRDGRSIDHASQYYSGIDVHHSSGVFNRAFYLLANKSGWNVRKGFEVFAVANQLYWTPNSTFDQGGCGVVKAAQDLNYNTADVVAAFNTVGVNASCGTTPPPVGKVLEKGKPITGLSGSRGGEDFYTFTVTNSGSVVVSISGGTGDADLYVKAGSKPTTSSWDCRPYRSGNAEQCSISAVVGTTYHVMLRGYSNYSGVTLRLD
|
May play a role in the pathogenesis of cholera. Hap nicks and activates the A subunit of cholera enterotoxin and related enterotoxins.
|
P24153
|
P56577
|
MALF2_MALFU
|
Thioredoxin-dependent peroxiredoxin
|
Malassezia
|
MPGDPTATAKGNEIPDTLMGYIPWTPELDSGEVCGIPTTFKTRDEWKGKKVVIVSIPGAYTPICHQQHIPPLVKRVDELKAKGVDAVYVIASNDPFVMAAWGNFNNAKDKVVFATDIDLAFSKALGATIDLSAKHFGERTARYALIIDDNKIVDFASDEGDTGKLQNASIDTILTKV
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
|
P56577
|
P16127
|
CHLI1_ARATH
|
Protein CHLORINA 42
|
Arabidopsis
|
MASLLGTSSSAIWASPSLSSPSSKPSSSPICFRPGKLFGSKLNAGIQIRPKKNRSRYHVSVMNVATEINSTEQVVGKFDSKKSARPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPEINVVAGDPYNSDPIDPEFMGVEVRERVEKGEQVPVIATKINMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDADLRVKIVEERARFDSNPKDFRDTYKTEQDKLQDQISTARANLSSVQIDRELKVKISRVCSELNVDGLRGDIVTNRAAKALAALKGKDRVTPDDVATVIPNCLRHRLRKDPLESIDSGVLVSEKFAEIFS
|
Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. Possesses high affinity for ATP and may play a major role in chlorophyll biosynthesis. Does not bind abscisic acid (ABA), but is a positive regulator of ABA signaling.
|
P16127
|
Q9UYS8
|
TOP1_PYRAB
|
Untwisting enzyme
|
Pyrococcus
|
MILVIAEKPNVARKIAGALSERRPIRKTIFGVPYYEVFRDGKKLIVASAVGHLYGLAPKQDFFGYPIFDIEWVPVYIAEKNKDYAKDYIKALSVLAKRVKEFIVACDYDTEGEVIGYTALKYACGVDPSRAKRMKFSALTKRDLLNAWRNLEPTINFGMANAGIARHVLDWYWGVNLSRALTHAIKRASGKWVVLSTGRVQGPTLKFLVEREREIQSFVPKPYWVIKLVIEKNGQKLVANYEKDKIWSEEEAKKIVTEVKKSKARVSNIEVKRQKRNPPVPFDLGTLQREAYSAFGFSPKKTLDIAQSLYEKGFTSYPRTESQKLPKNLNFRLIIQNISRMPQYRPYAHLLLGMPELKPVEGKKEDPAHPAIYPTGEIPGPGDLSKDEEKLYDMIVRRFLALFMEPAVRESVKVTILAGPHKFMLSGARTVKQGWLSVYGKYIKFDEVTLPEFFIGERVRVLQVRREKKKTKPPARYSPAAVIKKMEDLGIGTKATRAQILETLYQRGYIEGKKSIKVTPLGMKVIETLEKYVPEIISVELTREFERKMDLIMQGKLTKEEVIEEAKVKLTKILEEFKKRELEIGLELARIVVGDVKDEIKEEKPIVVGKCPKCGGDLIVKYNKKTGKRFVGCSNWPKCDVTYPILQRGEIIPTNKTCCNGAPVVIIRDKGRDIEICLDIKCKKW
|
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
|
Q9UYS8
|
P33915
|
YEJE_ECOLI
|
Inner membrane ABC transporter permease protein YejE
|
Escherichia
|
MSRLSPVNQARWARFRHNRRGYWSLWIFLVLFGLSLCSELIANDKPLLVRYDGSWYFPLLKNYSESDFGGPLASQADYQDPWLKQRLENNGWVLWAPIRFGATSINFATNKPFPSPPSRQNWLGTDANGGDVLARILYGTRISVLFGLMLTLCSSVMGVLAGALQGYYGGKVDLWGQRFIEVWSGMPTLFLIILLSSVVQPNFWWLLAITVLFGWMSLVGVVRAEFLRTRNFDYIRAAQALGVSDRSIILRHMLPNAMVATLTFLPFILCSSITTLTSLDFLGFGLPLGSPSLGELLLQGKNNLQAPWLGITAFLSVAILLSLLIFIGEAVRDAFDPNKAV
|
Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane.
|
P33915
|
B0T1Q2
|
SURE_CAUSK
|
Nucleoside 5'-monophosphate phosphohydrolase
|
unclassified Caulobacter
|
MRILLTNDDGIHAPGLGSLERIARMLSDDIWIVAPEYEQSGAGRALTLSDPIRVRRIDPRRFAVEGTPTDCVAMAMQQLIEGPAPDLVLSGVNRGQNLAEDVTLSGTVAGAIEGMAFGIRSIALSQAMTYFHDEVVAHWETAEHFGPGIVQRLLEVGWPKDVIINVNFPAVAPEMVTEVEVTRQGFRDSHMRSMEKRTDLRGRDYYWTGFVVKPSNPAEGTDLKAVYQGRISVTPLHIDLTHNQTVAAMKGALGGTPPRFDQPGLETAS
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
B0T1Q2
|
Q2J4C6
|
RS18_FRACC
|
30S ribosomal protein S18
|
Frankia
|
MAKAAVRKPKKKVCVFCKDKVDYIDFKDTSLLRKYISDRGKIRARRVSGNCSQHQRDVATAVKNSREMALLPYTASAR
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
Q2J4C6
|
A6X391
|
DEACT_BRUA4
|
Deacetylase Oant_2987
|
Brucella
|
MISGEQAKPLLITNVKPVAFGVEHSDATTDILVGKDGSISAIGKSLNAPADVERVDGKGAWISPGWVDLHVHIWHGGTDISIRPSECGAERGVTTLVDAGSAGEANFHGFREYIIEPSKERIKAFLNLGSIGLVACNRVPELRDIKDIDLDRILECYAANSEHIVGIKVRASHVITGSWGVTPVKLGKKIAKILKVPMMVHVGEPPALYDEVLEILGPGDVVTHCFNGKSGSSIMEDEDLFNLAERCSGEGIRLDIGHGGASFSFKVAEAAIERGLLPFSISTDLHGHSMNFPVWDLATTMSKLLSVNMPFENVIEAVTHNPASVIKLSMENRLSVGQRADFTIFDLVDADLEATDSNGDVSRLNRLFEPRYAVIGAEAITASRYIPRARKLVRHSHGYSWR
|
Esterase that catalyzes the deacetylation of acetyl-(R)-mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates.
|
A6X391
|
Q8TVJ1
|
RIFK_METKA
|
Flavokinase
|
Methanopyrus
|
MFTGPIVAVGEYVEGLGEGRRYVSIPYYRREIERVIGARPFPGTFNVRVEREERESLRELASSYGYRIEPHGEYGGAWLYPCLVNGRPAWLVFPDLTEHRDQVELISETELRRELNVIHGDMVKIEVWGPSTWKLARRLTCGPSGGR
|
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
|
Q8TVJ1
|
C3PKG1
|
HEM1_CORA7
|
Glutamyl-tRNA reductase
|
Corynebacterium
|
MSVLVVGMSHQSAPVALLEKLSMDETVQNDTCRAMVSAGSLSEAMIISTCNRLEVYTVTNSFHSGVQDVVHNLAEVSGVEEEKLRSYLYVRYADAAAEHLMMVTSGLDSMVVGEQQIIGQVRTAYQFASEQGTVGPRIHALAQSALRTGKRVHSETEIDEAGSSMVSFAFDQALSRMGREDLAGKRVLILGAGAMASLAATHAGRLGAHLIIANRTIARAERVAQHAHEAGVYADVIDFSERAQALRDVDVAISATGAQGFTITAADVERYHVADRELMLVDLSLPRDIDDAVAEAEGVDLINIERLNNSLQAADTDLAAGTSPHAQARRIVSEELESYASEQRVRDVVPAVSALRKRAANLVQCEVARMEQKHPELDERQMGDINRALKRVADKLLHEPTVRAKQLAANSGTVSHETALQELFGLQLEGSGVAVDMAELPDAAQMEAAENTKEEKDA
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
C3PKG1
|
Q2SHA6
|
KATG_HAHCH
|
Peroxidase/catalase
|
Hahella
|
MSDSKCPFHHAPAEGTSNRDWWPNQLRLEILHQRSALSNPLGEEFNYAEAFKSLDLAAIKQDLTALMTDSQDWWPADFGHYGPLFIRMAWHSAGTYRTGDGRGGGGTGNQRFAPLNSWPDNVNLDKARRLLWPIKQKYGQKISWADLMILAGNVALESMGFKTFGFGGGRADIWEPEQDIYWGAEKTWLDDNRYSGDRDLENPLAAVQMGLIYVNPEGPNGNPDPVAAAKDIRETFARMAMDDEETVALIAGGHTFGKTHGAGDAANVGPEPEAAGLEEQGLGWRSSYGSGKAGDAITSGLEVTWTETPTQWSNNFFENLFGYEWELTKSPAGAHQWVPKGGAGADKIPDAHDPSKRHVPTMLTTDLSLRFDPAYEKISRRFYENPDQLADAFARAWFKLTHRDMGPRARYLGPEVPAEELIWQDPIPAVDHPLINDQDISALKSKILTSGLSVAQMVSTAWASASTFRGSDMRGGANGARIRLAPQNEWEVNQPDQLAQVLKTLEGVQAEFNSAQSDGKKVSLADIIVLAGCAGVEKAAQNAGHTIKVPFSPGRMDASQEQTDIEAFEVLEPIADGFRNYMKGKYAVSPEELLVDRAQLLTLTAPEMTVLIGGMRVLNANVGQSKHGVFTQRPESLTNDFFVNLLDMGTVWKATSKEEDLFEGRDRVTGDLKWTGTRIDLVFGSNSQLRALAEVYASSDAQERFLKDFVAAWTKVMNLDRFDLA
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
Q2SHA6
|
B2TY47
|
HFQ_SHIB3
|
RNA-binding protein Hfq
|
Shigella
|
MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNASGGTSSNYHHGSSAQNTSAQQDSEETE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
B2TY47
|
Q21RW2
|
RS19_ALBFT
|
30S ribosomal protein S19
|
Rhodoferax
|
MTRSLKKGPFVDHHLVAKADKAVATKDKKPIKTWSRRSMVLPDFIGLTIAVHNGKQHVPVYITDQMVGHKLGEFALTRTFKGHPADKKVQKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q21RW2
|
Q8LBI1
|
RL51_ARATH
|
Protein PIGGYBACK 3
|
Arabidopsis
|
MVFVKSTKSNAYFKRYQVKFRRRRDGKTDYRARIRLINQDKNKYNTPKYRFVVRFTNKDIVAQIVSASIAGDIVKASAYAHELPQYGLTVGLTNYAAAYCTGLLLARRVLKMLEMDDEYEGNVEATGEDFSVEPTDSRRPFRALLDVGLIRTTTGNRVFGALKGALDGGLDIPHSDKRFAGFHKENKQLDAEIHRNYIYGGHVSNYMKLLGEDEPEKLQTHFSAYIKKGVEAESIEELYKKVHAAIRADPNPKKTVKPAPKQHKRYNLKKLTYEERKNKLIERVKALNGAGGDDDDEDDEE
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Seems involved in the regulation of cell proliferation . Essential in leaf polarity establishment, probably having a role for translation in leaf dorsoventral patterning to specify leaf adaxial identity .
|
Q8LBI1
|
Q8NGA0
|
OR7G1_HUMAN
|
Olfactory receptor OR19-8
|
Homo
|
MGPRNQTAVSEFLLMKVTEDPELKLIPFSLFLSMYLVTILGNLLILLAVISDSHLHTPMYFLLFNLSFTDICLTTTTVPKILVNIQAQNQSITYTGCLTQICLVLVFAGLESCFLAVMAYDRYVAICHPLRYTVLMNVHFWGLLILLSMFMSTMDALVQSLMVLQLSFCKNVEIPLFFCEVVQVIKLACSDTLINNILIYFASSVFGAIPLSGIIFSYSQIVTSVLRMPSARGKYKAFSTCGCHLSVFSLFYGTAFGVYISSAVAESSRITAVASVMYTVVPQMMNPFIYSLRNKEMKKALRKLIGRLFPF
|
Odorant receptor.
|
Q8NGA0
|
Q1I6F8
|
QUEC_PSEE4
|
Queuosine biosynthesis protein QueC
|
Pseudomonas
|
MTDKRAVILLSGGLDSATVVAMAKAEGYACYTMSFDYGQRHRAELDAAARVARDLGVVEHKVIGLNLNGIGGSALTDNSIDVPEAPGEGIPVTYVPARNTVFLSLALGWAEVLEARDIFIGVNAVDYSGYPDCRPEFVEAFERMANLATKAGVEGQGFRIQAPLQNLSKAQIVQAGIAQGVDYSLTVSCYQADDEGRACGKCDSCRLRADGFKAAGVEDPTRYF
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
Q1I6F8
|
Q9C0K3
|
ARP3C_HUMAN
|
Actin-related protein 11
|
Homo
|
MFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKYDVDPQKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDSMESISDVVDEVIQNCPIDVRRPLYKMEQIPLSYPQGHGFHPLSPPFH
|
May play a role in the suppression of metastatic potential in lung adenoma carcinoma cells.
|
Q9C0K3
|
A9KD01
|
FABV_COXBN
|
Enoyl-[acyl-carrier-protein] reductase [NADH]
|
Coxiella
|
MIVQPKVRGFICTTAHPEGCARHVGEWINYAKQQPSLTGGPQKVLIIGASTGFGLASRIVAAFGAGAKTIGVFFERPASGKRTASPGWYNTAAFEKTALAAGLYAKSISGDAFSDEIKQQTIDLIQKDWQGGVDLVIYSIASPRRVHPRTGEIFNSVLKPIGQTYHNKTVDVMTGEVSPVSIEPATEKEIRDTEAVMGGDDWALWINALFKYNCLAEGVKTVAFTYIGPELTHAVYRNGTIGRAKLHLEKTARELDTQLESALSGQALISVNKALVTQASAAIPVVPLYISLLYKIMKEKNIHEGCIEQMWRLFKERLYSNQNIPTDSEGRIRIDDWEMREDVQAEIKRLWESINTGNVETLSDIAGYREDFYKLFGFGLNGIDYERGVEIEKAIPSITVTPENPE
|
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).
|
A9KD01
|
P85184
|
CYO21_VIOOD
|
Cycloviolacin-O21
|
Viola
|
GLPVCGETCVTGSCYTPGCTCSWPVCTRN
|
Probably participates in a plant defense mechanism.
|
P85184
|
F9XLC1
|
GGS3_ZYMTI
|
Geranyltranstransferase
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Zymoseptoria
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MHISTIKTAGSSGMSHMNEAYSSTTATEMVARGAGSEIIHTEIDSNGSKELAPNGAQSRVQKPSEDAVRAPYDYIRTLPSKRIRETFIDALDSWLAVPAGSSTSIKSIIGMLHQSSLMLDDIEDDSTLRRGKPTAHTLFGTAQTINSANWVFVCAFEELRQLRGVDAATVFVEELKNLHCGQALDLHWKHHTYIPSVDEYLNMVDHKTGGLFRLCVRLMQGESSTSCHHIDAERFITLLGRYFQIRDDYQNLVSDEYTNQKGFCEDLDEGKISLPLIYCLAGSDPTQIMIKGILQHKRTGEMPLSMKKLILEKMRSGGALNATISLLKDLQDDILEELKSLELAFGSGNPMLELVLRRLWI
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Geranylgeranyl pyrophosphate synthase; part of the gene cluster 25 that mediates the biosynthesis of an isoprenoid secondary metabolite.
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F9XLC1
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