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2.75k
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5.51k
AlphaFoldDB
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O27093
HEM1_METTH
Glutamyl-tRNA reductase
Methanothermobacter
MLQVILNIRLDHKTSDVKTMESSHERMEAIVAELESSGTVMEKVPIRTCNRIEYYLSVQEIPPGFEFDGFTVEGDEDALRHILRLASGLESMIIGEDQILGQIKAARVQALREGTCGPVLDMVFTKAVHVGQTVRRKTQINRGSVSIGSAAVDLAESIHGDLKCRKVLAIGAGKMGTLVARALAEKHLSAIMVANRTYERAYQLACELGGDAIHFDRLNRALRDADVVISATGSPHYILTRERVRDAIPPERRSAVVMVDIANPRDIEESVRELGIRLFTIDDLRGVAEENRRRREAEAREAERIVEGELKLLLRSLKHMEVEPLLAEVRGNMESLRRREAERALNKIMNSSDPEGVIEALSRSIVDKIFHDIAISIRQAAERGDEEFLSMCAKLFNCKDLK
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
O27093
A5FW78
RNH2_ACICJ
Ribonuclease HII
Acidiphilium
MPDFSRELALGGVVAGVDEVGRGPLAGPVVAAAAILPADLPPEIAALIDDSKRLSPAQREAALAALIESGAAISAAAASVAEIARLNILQASLLAMRRAVARLAVRPDHVLVDGQVAPDLPMPCTPVVGGDGLSLSIAAASIAAKLVRDRAMSRLDRRYPGYGWARNSGYGTKTHRDAILGLGITPHHRRGFGPLLPPA
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A5FW78
A8FTT7
PDXB_SHESH
Erythronate-4-phosphate dehydrogenase
Shewanella
MKILADENMPYVEQLFGDLGTIEAVNGRTLTSEQVKDADVLLVRSVTKVNQALLSLNTNLKFVGSATIGTDHIDQSYLASQGIPFTNAPGCNATAVGEFAFIAMLELAKRFDTELKGKVVGIVGAGNTGSAVAKCLEAYGVEVLLNDPLIEADDPRTFVSLEALTERADVISLHVPLTKDGAHKTWYLFDEQRLQNLKPDTWLLNCCRGEVIDNRALIKIKAQRPDIKLVLDVWEGEPEPMLELVPFVELATPHIAGYSLEGKARGTYMLYQKLMAVLGIDADKSMTSLLPTLWSQQVSLDELPSEKALLQLSRFVYDLRDDDELFRKTLLDDSSIKAGENSANNNGFDLMRKNHKHRREFSALKLASAGQSDVDWLLNLGFSGVGR
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
A8FTT7
Q732C2
COXX_BACC1
Heme O synthase
Bacillus cereus group
MNHATSELHDESAVTSVPETTRLQDLKALVKMGIVNSNTLTVFTGFWLALHFNGLSVMDNLDKLFFTIVGSGLVMAGVCCLNNYIDRDIDPLMERTKTRPTVTGKYKPGFALTFGLVILLLGFVFLLLTTPMAVLMGFIGAFTYVVLYSLWTKRKYTLNTVVGSISGAVPPLIGWAAIDPSLGHPIAWMLFLIMFIWQIPHFLALAMKRVDEYRNAGIPMLPVVHGFEITKRQIMIWTVCLLPLPFYMSGLGITFMVIATLLNIGWIVLGFYGFRKKDDIKWSVQMFVYSLNYLTILFVSMIVVTFF
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Q732C2
Q9VPH8
RBBP5_DROME
Retinoblastoma-binding protein 5 homolog
Sophophora
MNLELLESFGQNYPEEFDGSLDCISLAVTCAFNKYGTLLAVGCNDGRIVIWDFLTRGIAKIISAHVHPVCSLSWTRNGHKLLSASTDNNVCIWDVLTGELEHKYRFPSPVLKVQFDPRNDNRLLVCPMRYAAVLVEVGGTHRCLPLDSDGDLNIVASFDRRGKHIYTGNAKGKILVLDVETFEVVASFRIIVGTSSATAVKSIEFARRGDAFLINTSDRVIRVYDSKEIITLGKDGEPEPIQKLQDLVNKTTWKKCCFSGDGEYICAGSARQHALYIWEKSIGNLVKILHGTKGELLLDVVWHPVRPIIASISSGLVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIADEDKSVDLNADAQQDEEIEVDVQKVEPVAAFCSSDEEGEDENALQFLPMAPEVEDPEDGWTGQDGLEPSAVMLGHMEPHDYEDDIMASKRRRMQLYDVSLPDAPTDETHPLISSKASKDKQQPVGGKKAAGRTKK
Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 and of the MLL3/4 complex which also methylates histone H3 'Lys-4'.
Q9VPH8
O75943
RAD17_HUMAN
RF-C/activator 1 homolog
Homo
MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLELLCQGCSGDIRSAINSLQFSSSKGENNLRPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKILYCKRASLTELDSPRLPSHLSEYERDTLLVEPEEVVEMSHMPGDLFNLYLHQNYIDFFMEIDDIVRASEFLSFADILSGDWNTRSLLREYSTSIATRGVMHSNKARGYAHCQGGGSSFRPLHKPQWFLINKKYRENCLAAKALFPDFCLPALCLQTQLLPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSAEESLGEPTQATVPETWSLPLSQNSASELPASQPQPFSAQGDMEENIIIEDYESDGT
Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.
O75943
Q9QZC7
PKHB2_MOUSE
Evectin-2
Mus
MAFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQSIEDKVHMPVDCINIRTGHECRDIQPPDGKPRDCLLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRTNTAYVGSAILSEETAVAASPPPYAAYATPTPEVYGYGPYSGAYPAGTQVVYAANGQAYAVPYQYPYAGVYGQQPANQVIIRERYRDNDSDLALGMLAGAATGMALGSLFWVF
Involved in retrograde transport of recycling endosomes.
Q9QZC7
Q5SLR5
RLMH_THET8
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Thermus
MRLRVVAVGRPRLAYARLGVEEYARRMRRYAPLDLVFVRKGEELLPKAEGHRKVVLDERGRLLTTEELYRRLLAWEGERVAFLVGGAEGHPEAVREEADLLLSLSPLTLQHELALLVLMEQLYRVLTLRAGHPYHRP
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Q5SLR5
F1RBN2
SPAG1_DANRE
Sperm-associated antigen 1A
Danio
MSQQEVCPLNLFQSAQGTGRVCMRVCVCERGRELAVLYRAAMGNAQKKGPGYREGGGPNSQPGTPGRRRSHGLNNAANSKEVPGSSPAANGSLPAGKSQDEPQGPGSAGESCNLDAPCGALPPPLARLKNQGNMLFKNGQFGDALEKYTQAIDGCIEAGIDSPEDLCVLYSNRAACFLKDGNSADCIQDCTRALELHPFSLKPLLRRAMAYESLERYRKAYVDYKTVLQIDISVQAAHDSVHRITKMLIEQDGPDWREKLPEIPAVPLSAQQHRKEEPSAELLQARAERAEQEKARKAEARFTILKQEGNELVKNSQFQGASEKYSECLAIKPNECAIYTNRALCFLKLERFAEAKQDCDSALQMEPKNKKAFYRRALAHKGLKDYLSASTDLQEVLQLDPNVQEAEQELEMVTNLLRESLLANAQG
May play a role in the cytoplasmic assembly and/or trafficking of the axonemal dynein arms.
F1RBN2
Q5UZR5
RPO1C_HALMA
DNA-directed RNA polymerase subunit A''
Haloarcula
MTAHDVSADIEAVVEDTELPRRLKDEVYSTIEERGVGVDDADRIAKAVETRYLDTRVDPLDPVGTVSAQSIGEPGTQMTMNTFHYAGVAEIDVTQGLPRLIELVDARKTPDTPMMTVHLDEEYATDRERAHEVVWKIEATRILALGDISTNVADMLVEIDLNEDTLLERWPTVNDTDAIAEEIAETIESNLGVSTRQAGTLIEFGPEEPSYRDLLQLVEELREIVFKGIEEITRVVIRKEETDNGEEFVLYTEGSDFGEVLDIEGVDASRTTCNNIHEIYRELGVEAARETLINETMNTLEEQGLDDVNVRHLMLVADIMTNEGTIESIGRHGISGSKDSVLARAAFEVTVNHLLDAAIHGEVDELDGVTENVIVGKPIKLGTGDVNLRMGTTQD
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Q5UZR5
B2XTF7
FTSH_HETA2
ATP-dependent zinc metalloprotease FtsH
Heterosigma
MNKKETNTSWWRIILISLGISIICILAAFLAMKDGFFVLENNTKNNNPDSPENKASSKMAYARLLNYIEKGWIKTIDFYENGQIAIVEASSSELSDRPQRLRVEIPAGSTSLIGKLKEANVDINAHPPKLDIFKTISDTLGSLIVPGLVVAVFYLFLERANNNNNNNSNGSPFGPGGGPNQNMRGLGEIKKEIQKEPDTGITFKDIAGIEEVKEEFEEIVTFLKDPSRFTAVGATIPKGVLLVGPPGTGKTLLAKAIAGEAKVPFINISGSEFVEMFVGVGAARVRNLFEKAKQDTPCIIFIDEIDAVGRQRGAGVGGGNDEREQTLNQLLTEMDGFEKNKGIVVIAATNRADILDNALLRPGRFDRQVTVNPPDRAGRVAILAVHARNKKLSPAISLETIAQRTTGFGGAELANLLNEAAIISAREEKAEIGSKEISLAIERVIAGLEGPSIADNKNKRLVAYHEAGHAMVGTLLRNHDNVQNVTLVPRGQARGLTWFMPNEDPSLVTRGQIVARIVGALGGRAAEQSVFGSTEITTGASGDLAQVTDLAKQMILRFGMSGIGPVSLSKPGGSFLFVGRGVRPSNEYSEALAIKIDEQIRTITELCYNEAVEIMDLNRISLDLAVTGLIQDEVLTGVSFEKVVADFSKLPTNKIYESKFPKK
Acts as a processive, ATP-dependent zinc metallopeptidase.
B2XTF7
F4HUK6
AAE1_ARATH
Pentanoate--CoA ligase CCL3
Arabidopsis
MKMEGTIKSPANYVPLTPISFLDRSAVVYADRVSIVYGSVKYTWRQTRDRCVRIASALSQLGISTGDVVSVLAPNVPAMVELHFGVPMAGALLCTLNIRHDSSLVAVLLRHSGTKVIFADHQFLQIAEGACEILSNKGDKVPILVLIPEPLTQSVSRKKRSEEMMEYEDVVAMGKSDFEVIRPTDECDAISVNYTSGTTSSPKGVVYSHRGAYLNSLAAVLLNEMHSSPTYLWTNPMFHCNGWCLLWGVTAIGGTNICLRNVTAKAIFDNISQHKVTHMGGAPTILNMIINAPESEQKPLPGKVSFITGAAPPPAHVIFKMEELGFSMFHSYGLTETYGPGTICTWKPEWDSLPREEQAKMKARQGVNHLGLEEIQVKDPVTMRTLPADGVTMGEVVFRGNTVMNGYLKNPEATKEAFKGGWFWSGDLGVKHPDGYIELKDRSKDIIISGGENISSIEVESTLFTHPCVLEAAVVARPDEYWGETACAFVKLKDGSKASAEELISYCRDRLPHYMAPRSIVFEDLPKTSTGKVQKFVLRTKAKALVSLSKKGRSKL
Catalyzes the ligation of CoA on butanoate to produce butanoyl-CoA . Can also use hexanoate, pentanoate and 4-methylpentanoate as substrates with a lower efficiency .
F4HUK6
P0DPA6
PSID_PSICU
Psilocybin biosynthesis decarboxylase
Psilocybe
MQVIPACNSAAIRSLCPTPESFRNMGWLSVSDAVYSEFIGELATRASNRNYSNEFGLMQPIQEFKAFIESDPVVHQEFIDMFEGIQDSPRNYQELCNMFNDIFRKAPVYGDLGPPVYMIMAKLMNTRAGFSAFTRQRLNLHFKKLFDTWGLFLSSKDSRNVLVADQFDDRHCGWLNERALSAMVKHYNGRAFDEVFLCDKNAPYYGFNSYDDFFNRRFRNRDIDRPVVGGVNNTTLISAACESLSYNVSYDVQSLDTLVFKGETYSLKHLLNNDPFTPQFEHGSILQGFLNVTAYHRWHAPVNGTIVKIINVPGTYFAQAPSTIGDPIPDNDYDPPPYLKSLVYFSNIAARQIMFIEADNKEIGLIFLVFIGMTEISTCEATVSEGQHVNRGDDLGMFHFGGSSFALGLRKDCRAEIVEKFTEPGTVIRINEVVAALKA
L-tryptophan decarboxylase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well . The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine . The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin . The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin . PsiK kinase can also turn psilocin into psilocybin . This activity may represent a protective mechanism to rephosphorylate the unstable psilocin to the stable psilocybin in case of intracellular ester cleavage .
P0DPA6
Q54PS7
PLBLD_DICDI
Phospholipase B-like protein D
Dictyostelium
MIIFKNLLKLLIILLTIKLYFCIEIKREEHLTILNELNENSDVIQYSILPGNNEEYEIVKGIQEDAIVYGYYMSNVEVNGWAYLSLVSNDKYNDSTQSRAFGYLEGYLTKDLIWNSKVNYYKNAFNSSEIPNKLDDWLTENIESIHTFIVNNRKSRYWNQITLVMDQINGMLDGYNEANTNSSETLSLHDFFVLNMFGDLFDLMPALNLDKEYKYFQKDLNDIQDWFKRSQHCSALIKVSSDYSELYSGHTTWSGYYTMLRIFKSYNQQFSSDVSGTLSKRNIFSSYPGALISVDDFYLLGDTRMVVIETTNSLVTNDLYHLIRPTTVLSWMRVIVSNRMSTNGKEWCENFQRYNSGTYNNQWMIVSYNLFVPYNELKDGALYVLEQIPGYIEFSDQTQALRQGWWNSYNIPFYETIYDASGYNNYTANNYSDSTIYYMSYQTCPRAEIFRNFAGYVESLEDFQSLLRYNDFEYDPLSHKLPFYAIASRYDLSKKNPSPFGATDTKVTCNSMIDQNTIVAISGPTTSNGQPIFEWNSKIDFMESTSHLGCPEKYNFPWVSFSDTTFRNL
Probable phospholipase.
Q54PS7
Q97YD2
RN393_SACS2
CRISPR system ring nuclease SSO1393
Saccharolobus
MEVHVCSVGTSLLKNSLDDDNVRKEIERLGLKDWDRLKFDDDRQNRIKENFDSLRKMLLKFIRSKGRRASAELDSLFSTFEKLKHNKSEIYVFLYSTNTSNSQLAGEVIRDYLIEEGIRSELVTVKTISSEENFYEGIVDLFDKVIYRILKFKEQDNEVYINATPGLKPESIFLTLAGLLAGADLIYYKYQEFNDVVILPSPPITIRPKYLDWLIRFAISGYTLSEKRAEELGIPVRLLEAKMLVERKGEDAYRLKDWVRKLLGIYLPIGAQNKYYRVIVEGEGERTFDNEVEAYNYMESKRKEGKNVRVEVPDRVYFLGL
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (Probable). A nuclease that degrades cyclic oligoadenylates (cOA), second messengers that induce an antiviral state important for defense against invading nucleic acids. Destruction of cOA deactivates the Csx1 ribonuclease, preventing uncontrolled degradation of cellular RNA. Slowly degrades cA4 (a tetraadenylate ring) into first a linear tetraadenylate product and secondly into a linear diadenylate product with 5'-OH and 2',3'-cyclic phosphate termini. Is 10-fold less active than SSO2081, suggesting it plays a minor role in cA4 degradation. There may be 2 active sites per homodimer .
Q97YD2
Q2RQX2
RL5_RHORT
50S ribosomal protein L5
Rhodospirillum
MARLQEHYQTVVKKALLEKFQYGNVMEIPRLEKIVINMGVGEASQDRKLIEGALTDMTAISGQKPIITRAKKSIAAFKLREQMIVGCKVTLRRDRMFEFLDRLVTIALPRVRDFRGVSAKSFDGRGNYNMGLKEQIVFPEIDYDRVDKVRGMDITICTSAKSDEEAKALLEGFAMPFMK
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. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Q2RQX2
Q2YYV8
HUTI_STAAB
Imidazolone-5-propionate hydrolase
Staphylococcus
MNDLIINHIAELILPRSTDKPLKGKELDELNVVKNGTVVIKDGKIVYAGQHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSREHEMSLKRQGKSYLEILEMGGGILSTVNATRETSEDDLFKKAEHDLLTMIKHGVLAVESKSGYGLDRENELKQLKVSNRLAEKHDLDMKHTFLGPHAVPKEASSNEAFLEEMIALLPEVKQYADFADIFCETGVFTIEQSQHYMQKAKEAGFKVKIHADEIDPLGGLELAIDEQAISADHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEDYADARGMLDNNGAIALATDYNPGSSVTNNLQLVMAIAALKLKLSPNEVWNAVTVNAAKAIDINAGTINTGDKANLVIWDAPNHEYIPYHFGINHAEKVIKDGKVIVDNTLSFKA
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.
Q2YYV8
Q5V385
CDC6I_HALMA
ORC1-type DNA replication protein 9
Haloarcula
MEQSEDGDLDAGDELFEEVDGDGKGEIFANRELLNIDHVPDENRIVGRDEHITELANEIGPAVTGSPPNSVILYGKTGSGKSLVANHVMERARREAQRRDRRLATVTVDCAQSRGEADTVQTIADKINRSTSGVTVPTRGISTNEYYNRLWQILGTEYDAALITLDEVDRLSDDDILMILSRAREAGKVDVPIGIISISNKVNFREQMTERVKSSLGHNEMIFDPYDGEQLRQILENRKDAFQEDILMPGVIPKTAALAAQRHGDARKAIRLLRHAGDYAKTNNIGTVKESHLELAQEQAEVERLKELISGLPPHSKYVLYALANLTDGTTNSNDWFRTTVIYDVYEEVCKTEATDTLTTDTIRGLLNELAFLEITESNQEHGGMGKGTYKEHRLLWDPNVVFKMNPGSAQVDTDR
Involved in regulation of DNA replication.
Q5V385
A7H029
OBG_CAMC5
GTP-binding protein Obg
Campylobacter
MFIDSVNLTLSSGHGGAGAVSFRREKHVILGGPDGGDGGDGGDVYLIADNNSHTLAAYKGKRALKAQNGEAGSGRRMTGKKGENLELIVPPGTAVYDAQTNELLADLTKESERVLFLKGGKGGLGNVHFKSSINQAPEYAQKGLPEETRDVRLELKLIADVGLVGFPNVGKSTLISTVSNAKPQIANYEFTTLTPKLGLVEVDEYSGFVMADIPGIIEGASDGRGLGLKFLKHIERTKILLYMLDLANHRSLKEQFVTLRGEVEKFSPELAKRDFAIALTRMDAAENLERKVGEFLQILGLSGERSNLIDEAGKAGKNLIYKQDIYEFDDSKPYFVMPISSATNQNITELKFSLLELLKKGKFQMIFAGNLTETRG
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.
A7H029
Q92L68
RLMN_RHIME
tRNA m2A37 methyltransferase
Sinorhizobium
MAATEILNRADIVKAPQVRLAPQPEKPSLIGLLRDDIAKLLAEKGVPERQVKMRVSQLWHWLYVRGVSDFDEMSNVSKDMREMLKEHFTIARPDIVEEQVSGDGTRKWLLRFPPRGAGRPVEIETVYIPEEGRGTLCISSQVGCTLTCSFCHTGTQKLVRNLTAEEILSQLLLARDRLGDFPERDTPQGAIVPAEGRKITNIVMMGMGEPLYNFENVKTALLIASDGDGLSLSKRRITLSTSGIVPEIYRTGEEIGVMLAISLHAVRDDLRDMLVPINKKYPLKQLMEACRAYPGLSNARRITFEYVMLKDVNDSLEDAKELVKLLKGIPAKINLIPFNPWPGTNYQCSDWEQIEKFADFINQAGYASPIRTPRGRDILAACGQLKSESERMRKVDRLAFEAMMIANHGED
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Q92L68
Q5HZE4
MTNA_RAT
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
Rattus
MRLEAIRYSPGSLQILDQLQLPEHCHYETLSSVQQAREAIRAMKVRGAPAIALVGCLSLAVELQAGAGGPGLAALVAFVRDQLSLLVAARPTAVNMARAARDLTHMAAREAELEGATEETVRERVIRFAEDMLEKDLKDNRSIGDLGARHLLEQTNPRGGKVTVLTHCNTGALATAGYGTALGVIRSLHEMGRLEHTFCTETRPYNQGARLTAFELVYEKIPATLITDSMAAAAMVHQGVSAVVVGADRVVANGDTANKIGTYQLAIVAKHHGIPFYVAAPSSSCDLRLETGKEIVIEERPSQELTDLNGVRIAAQGIRVWNPAFDVTPHELITGGIITELGVFAPEELRAALSATIFSEGQTLDSPQM
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Q5HZE4
Q9UXU2
VATI_PYRAB
V-ATPase subunit I
Pyrococcus
MFKPEEIVKVEIITLARFRDTLLTYLHEMGVAQLDEVPIEGIQRDTPNEFYRKATSYSITLSRLIDTVKHYLPPRKGGIKEFIFPEEKKKRKYKYRGIEELIKDVEKFLGEAEPKIREVESEVSRLNNEISALKDSLNALELLSSLNIEIENLRGRSFLSVEVGLVDREKVENLIKELEEIAEGRVFTLRKDLAAKSLLVVVSLRKDSGKVISLLAKYGFEKIEIPEGEGLPKDLIPKYIERIKGKEKELEDVKLKGREIAEKYYEDLVFYKELMDNEREKSNFLSYLVRTEMTFGLLAWVPKKDVEKVVEGVKRITNGIAYIEVREPSEEEIENVPVKLKNPEFISHFEMLTEMYGVPKYNEIDPTPILAFTYSFFFGFMLTDFVYGLLLGVISALLVKGHSKLKDGTWKFAKIMLWASAFTMVLGILFGSYCGNLLDMAGVKVPRLLDTMSEALTVLVMALAIGLGHLFTGYILGFIVNWKNGDKRAAILEQLPWVFIIIGITLFALSSKLGIPQIAFKAVFGVGLALFVVGEIVNNKGMAVLLTISDFFGFIGNWLSYARLMALALATSGIALVINIIANMVWGLKIGPIPLGILIGIVILIGGHIFSTAINALGAFVHALRLHYVEFFGTFYSGEGRKFEPFAAKREVSELEIES
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q9UXU2
Q2JNW5
PSAC_SYNJB
PsaC
unclassified Synechococcus
MAHSVKIYDTCIGCTQCVRACPTDVLEMVPWKGNNKAGMIAAAPRTEDCVGCKRCETACPTDFLSIRVYLGPETTRSMGLAY
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Q2JNW5
A2RN34
RPOZ_LACLM
Transcriptase subunit omega
Lactococcus cremoris subsp. cremoris
MMLEPSIDKLLDQVDSKYSLVVLEAKRAHELRDKERPTKEFKAVKRTLQALEEIADGTVKIHPAPELKRETLVEKRELERLQAKMKEQLIKEQIAKEEAEEEAKQKNSRAAKAAAAE
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
A2RN34
Q9UUZ6
RLA2_ASPFU
AfP2
Aspergillus subgen. Fumigati
MKHLAAYLLLALAGNTSPSSEDVKAVLSSVGIDADEERLNKLIAELEGKDLQELIAEGSTKLASVPSGGAAAAAPAAAGAAAGGAAAPAAEEKKEEEKEESDEDMGFGLFD
Plays an important role in the elongation step of protein synthesis.
Q9UUZ6
Q819H7
METE_BACCR
Methionine synthase, vitamin-B12 independent isozyme
Bacillus cereus group
MAIQTSNLGYPRIGLQREWKKTLEAFWSNKIDEEQFLTTMKEIRLQHVKVQQEKGIELIPIGDFTYYDHVLDTAYMLGFIPSRFSEFTSYLDVYFAMARGSKDHVASEMTKWFNTNYHYIVPEYEEGLQISLKDNRPLRLYEEAKQELGVDGKPVILGPYTFLKLAKGYTQEQFPTILKQLVAPYVQLLSELHAAGAPAIQVDEPIFASLTKKEVQQAKEIYEAIRKEVPNATLLLQTYFDSVEENYEEIITFPVSGIGLDFIHGKEGNLNAISKYGFPADKTLAVGCIDGRNIWRADLDEVLELFTTLQKQVQTKDIIVQPSCSLLHTPIDKTEETHLSTELFDALAFANQKLEELVLIHSALTQGTESISNELETYRNVHHTIRSSAARNREDVKAARTALKEEDFSRPLPFEKRYELQQVALELPLLPTTTIGSFPQTTEVRQTRKEWRNGVISNEQYEQFIEKETEKWIRYQEEIGLDVLVHGEFERTDMVEYFGERLAGFSFTKNGWVQSYGSRCVKPPVIYGDVAFINGMTIKETVYAQSLTEKVVKGMLTGPVTILNWSFVRNDIPRKEVSYQIALALRHEIELLESSGIRVIQVDEPALREGMPLKEKDWDAYITWAVQSFLLATSSVANETQIHTHMCYSNFEDIVDAIRALDADVISIETSRSHGEFIDTLKHTTYEKGIGLGVYDIHSPRVPSKDEMYKIVEQSLEVCDPKYFWINPDCGLKTRRTEEVIPALEHMVQAAKDARSLLKTNA
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Q819H7
B4KCG1
CRBN_DROMO
Protein ohgata
Drosophila
MDDEETAEIDETSSSSTNTNTNATAMATATETAAEMHVELEQDEEIPQGSENGAGTGAGDGTRAEAGASAIHAETTAHVSSRARLENMIEEVDNMFEEVSELMVDVTELMRRANQLREDAGTGAVPQNPTVATNTTPPAEIEEEEEGPEQQAEQALVNNDSPSQASISSRHSGSDMSLDSPGSEDDSDAEAVPRWMIPANRVRSAVDMLVSQARNRDGGIATLLRRENFLQRVRSMVFSQDRIRGRASDDANNADVINTVPDDTSEASPPPPLDVDMEEGVRFDTNLPAEHSYFGTNLNRVPGVDYLEVGSTHRMLIFMHQHILFPGEVLPFMIDGNIIDEEIEDTGRDGVIFGVGFPLMQPPDDNPHKLYGVTCQIYEKGESGRQHVFYKSRALQRIVINCDDIQGPPQYIARNPTMKCYSKVKILPEYFLPEPLKCIDMGSLNRFRDIPSMQEKFRRFQLTTTPWPVEACGEYSFEHIVEKARQKLEIHKIDTMPKCPIQLSFWLVRNLHLTEKMMRLTFLTDSVNIRLQIIGTTLKHESLFYCRYCNSSLAYCSDLFAMSKHGVQTQYCNSAGYIHETNTVYRVIAHAIGYSGEPSTEFSWFPGYQWHIIICKFCAQHVGWEFKAVEPNLAPKVFFGLAGSSVRIGKTSERTPTHGSRFVVRNLLRLVSRELE
Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae.
B4KCG1
B8DUE9
RUVC_BIFA0
Holliday junction resolvase RuvC
Bifidobacterium
MIVLGVDPGLTRCGVGVIEAGAYRRLSFIHVDVVRSDPHESQDLRLLKIYDGLCAKMDEFIPDTVSIERVFAQENRNTVLGTAQAAGMAMLAAAQRGIPVALHTPTESKMAITGNGKAEKIQMERMVARILNLNALPTPADAADALAIAICHALRPSGALEGGEREQHLTPAQRQWAQATQHATRRRGVRRGM
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.
B8DUE9
B7L0Y4
CYSI_METC4
Sulfite reductase [NADPH] hemoprotein beta-component
Methylorubrum
MDDHKPIETPDGPAVDTPGIGARRYETPPTELPITEAEAARAAGLAHNEHLKIASGYLRGGLADGLLKHATGAISEDDGQLVKFHGMYMQDDRDIRAERTKKKLEKAYSFMIRLRIAGGVVTPKQWLILDNIATTYAGSALRATTRQTFQYHGVIKSNLKRTMAAIDSALLDTIAACGDVNRNVMAATNPAQAGAHKIALQLAKDISDTLLPKTGAWREIWLDGERVVGGEDAAEVEPVYGKTYLPRKFKTVVAVPPSNEVDIFAHDLGFIAILDKKNRVTGWNVTVGGGMGMTHGEADTFPRTADVLGFVQPEDALKAAEAVMTVQRDWGNRKNRKNARLKYTIERFGLDAFRAEVEKRIGKKLGAPKPFTFDGNGDRYGWVEGDDGRHHLTLYVPSGRIKDIEGGPQFLSGLRRIAEVHEGDFRLTGNQNVIIANVPAGKRAEIDALVDEYGLTRGASALRRNSMACVALPTCGLALAESERYLPDLLSELEESLARHGLQDEPITIRSTGCPNGCARPFISEIGLVGRGPERYHLYLGAAFDGSRLSKLYREDVTASEITGTLDPLFAAYAKDRQPGEHFGDFVIRAGFVAKTSNGPDFHERTGPLRAA
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
B7L0Y4
B3PK42
RL22_CELJU
50S ribosomal protein L22
Cellvibrio
MEVAAKLSGARLSAQKARLVADQIRGKGVEDALDILAFSTKKGAQIIKKVLESAIANAEHNEGADVDELKVKTIFVDEGVSLKRIKPRAKGRADRITKRTCHITVKVADK
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
B3PK42
D2Y2N2
H8M01_CYRHA
Hainantoxin-VIII-13
Haplopelma
MVNMKASMFLTFAGLVLLFVVCYASESEEKEFPKGMLSSIFAVDNDFKQEERDCAGYMRECKEELCCSGYVCSSRWKWCVLPAPWRR
Ion channel inhibitor.
D2Y2N2
B2U3Z3
PPNP_SHIB3
Xanthosine phosphorylase
Shigella
MLQSNEYFSGKVKSIGFSSSSTGRASVGVMVEGEYTFSTAEPEEMTVISGALNVLLPDATDWQVYEAGSVFNVPGHSEFHLQVAEPTSYLCRYL
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
B2U3Z3
Q0D3N0
PER2_ORYSJ
Peroxidase 2
Oryza sativa
MASASSVSLMLLVAAAMASAASAQLSATFYDTSCPNALSTIKSAVTAAVNSEPRMGASLVRLHFHDCFVQGCDASVLLSGQEQNAGPNAGSLRGFNVVDNIKTQVEAICSQTVSCADILAVAARDSVVALGGPSWTVLLGRRDSTTANESQANTDLPAPSSSLAELIGNFSRKGLDVTDMVALSGAHTIGQAQCQNFRDRLYNETNIDSSFATALKANCPRPTGSGDSNLAPLDTTTPNAFDSAYYTNLLSNKGLLHSDQVLFNGGSTDNTVRNFSSNTAAFNSAFTAAMVKMGNISPLTGTQGQIRLNCSKVN
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Q0D3N0
A1RT13
SYA_PYRIL
Alanyl-tRNA synthetase
Pyrobaculum
MLSAKVLLNSNFLRKQCPLCKSYFWTRRADQIYCGDQPCVPYGFIGNPPTKTSIESPAELRERFLRFFERNGHVRIKRYPVVARWRDDVYLVGASIYDFQPWVTSGAVPPPANPLVISQPSIRLTDVDKVGRSGRHLTGFEMMAHHAFNYPDKYVYWIDETTQYAYEFFTKELGIPQDEITFKESMWEGGGNAGECFEVLVRGLEVATLVFMHYEVKDGKYVELPLKIVDTGYGLERIYWLLKGTPTIYDAVFSHYLAKVRQKVGIPEPPADIMGRASIYFGQMDPEVIGLDKAYDIIAEKIGVDPKWLREVVRPQEALYVLADHSRTVSWMIADGVIPSNTGAGYLARLLIRRILKNLRVVGIDAPLVELFDMHLAELKREYPEIWAARDLILELVDLEEKKYREVLKSAPAAVKKALEEARRRGRAGLDTDDLVALYDSQGIPPEIVAEVAKSLGAEVKVPDDFYTKLAARHAKREKKPESPLVEMSKVADLPRTRELFYEDSYMRSFKARVLRVIDGRYVVLDQTAFYPEGGGQPADRGVLKFQGGEAKVVDVQRVGHVVVHVVEGQLPPEGAEVVGEIDWERRYSLMKMHTGTHVLIQSIRRVLGPHIWQAGAQKDIPSSRLDVTHYKLPTAEEIAKIEELANKVVQENLPVYVKIMPRNEAEAKYGFILYQGGVVPTREIRVLQIGPDEEPFDIQACGGTHLRSTGEIGLIKIQKVERIADGVVRFVFTTGMHALAYIQELERKLAEAAHIIGGSREEFVESVKKLLQRAEEAERRAKHYAELYAAVVAENLRAEQIGKYRVAVVELNDDELAKHIALAATRRDKDLVLVFVGGDRVTIYTGGVDVTPVVKTLREAGFRGGGSKTFAQGLYKGDIQTLKEALKKALS
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
A1RT13
B7VJ08
LPXC_VIBA3
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Vibrio
MIRQRTLKEIVKTTGVGLHSGRKVTLTLRPAAANTGIVYRRTDVNPPVDFPADPASVRDTMLCTALVNDEGVRISTVEHLNAALAGMGIDNIIVEVDAPEIPIMDGSASPFVYLLQQAGVETLNAAKRFIRIKKPIRFEDGDKWAEFVPFNGFRMDFEIEFNHPAIESDEQHLLFDFSSQGFVKEISRARTFGFMRDIEYLQSQNLCLGGSFDCAIVLDEYRILNEEGLRFENEFVTHKVLDAIGDLYMCGHAIIGEFRAYKSGHGLNNQLLRAVLADAEAWEWATFEEEVGSPVAFAEPGMVLA
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.
B7VJ08
Q5FWT5
GATA_RAT
Glutaminyl-tRNA synthase-like protein 1
Rattus
MLGRTLREVSSALKQGHITPTELCKKCLSLIKKTKYLNAYITVSEEVALKQAEESEKRYKQGQSLGDLDGIPVAVKDNFSTSGIETTCASNMLKGYLPPYNATVVQRLLDQGALLMGKTNLDEFAMGSGSTDGVFGPVKNPWTYSKQYRERSRQDAQEDSHWLITGGSSGGSAAAVAAFTCFAALGSDTGGSTRNPAAHCGTVGFKPSYGLVSRHGLIPLVNSMDVPGIFTRCVDDTAIVLGVLAGHDPKDSTTVNDPVKPTTLPSVPDVSGLCIGIPKEYLVPELSSEIRSLWSQAADLFEAEGARVIEVCLPHTCYSIVCYHVLCTSEVASNMARFDGLQYGHRSAVDMSSTEALYAATRQEGFNDVVKGRILSGNFFLLKENYENYFVKAQKVRRLIVNDFVNVFGSGVDVLLTPTTLTQAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVNVPVALSSQGLPIGLQLIGRAFCDQQLLTVAKWFEKQVQFPVIQLQDLMDDGSLVPENGKLTSGSLTQ
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q5FWT5
Q6FU40
KAR5_CANGA
Karyogamy protein 5
Nakaseomyces/Candida clade
MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVGLSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVSETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKKTIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKLPTLEQQYLGNFAQALSNIDKQVLSASLQWQYDYDVVFANLYAALDLLNSNLNSSVKKIEQIEHVIDTIIVDTSFLNDQLANLILIPSTILRAFSFIGVKRVIIAIIVLYFKSTLLCLVHYGQSFRIAALLMSATAGIFCSKLLMSYIYN
Required for nuclear membrane fusion during karyogamy.
Q6FU40
Q8U477
ENO_PYRFU
2-phosphoglycerate dehydratase
Pyrococcus
MENPYEIVGVVAREILDSRGNPTVEVDVYTHVGMGRAAVPSGASTGTHEALELRDGGKRYHGKGVRRAVENVNKIIAPELIGMDVRWQREIDALLLELDGTENKSNVGANAILAVSLAVAKAAANSLELPLYQYLGGVNAYVLPVPLSNVINGGVHAGNDLDFQEFMIMPIGADSFREAIRWVSETYHVLKKVIMEKYGKNAVNVGDEGGFAPPMKEVTEPLDVLIKAIEEAGYKPGDEIALALDVASSELFNEETGKYVVGGKEYDRGELLELYKDLTSTYPIVSIEDPFHEEDWEGFVMITKELGHKVQIVGDDLFVTNPKRLRKGIELGAANALLLKVNQIGTLSEAMDAAFTAFRAGYGVIVSHRSGETEDATIADLAVALNAGQIKTGAPARSDRNAKYNQLIRIEEELEGVAVYAGKRFRKVFF
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q8U477
Q0CXB1
DAPB_ASPTN
Probable dipeptidyl-aminopeptidase B
Aspergillus subgen. Circumdati
MGKSEADEDAQFLPMNRPRSSSAASQTSSDSGLSVESALIRNSTYGKTPDEAYNPAGDPRYRDIEDGEAESDQPFLPSRKGSGARARRVFWGLLLLCLAGWVLAFVLFLIQGRSGYSATSEELQQHEADSSAGVTSDGKPVTLKQVLSGDWLPRSHGIAWIAGPDGEDGLLVEAGEDGGEGFLRVKDIRARHGDDAGTLKSRVLMKKSTFYAGQRSILTRLTWPSPDLKKVLVLSDYEKNWRHSYTGLYWIFDVDSQTAEPLDPDVPEGRVQLASWSPNSDAVVFVRDNNMFLRKLSSDKVVPITKDGGKDLFYGVPDWVYEEEVLSGNSATWWSNDAKYVAFLRTNESTVPEYPVQYFLSRPSGKKPLPGLEDYPDVRQIKYPKAGAPNPVVNLQFYNVEKNEVFSVEVPDDFADDDRIIIEVLWAAESNVLVRATNRESDVLKIFLIDTESRTGKMVRLEDIVGLDGGWVEPSQSTRFIPADPAAGRPNDGYIDTVIHDGYDHLAYFTPLDNPEPIMLTTGEWEVVEAPTAVDLRRGLVYFVATKEAPTQRHVYQVQLDGSNLKPLTDTSKPGYYHVSFSDGTAYALLSYQGPSIPWQAIINTEGDDVVFEETIEENPELARMVETYAIPSKVFSNITIDGFTLQMVERRPPHFNPHKKYPVLFFLYGGPGSQTVDRKFTIDFQSYVASNLGYIVVTLDGRGTGFIGREARCIIRGNLGYYEAHDQITAAKMFAEKSYVDESRMAIWGWSYGGFMTLKTLEQDAGQTFQYGMAVAPVTDWRFYDSIYTERYMHTPQHNPSGYDNSSITDMAALEENVRFLVMHGASDDNVHLQNTLTLIDKLDLSNVQNYDVHFYPDSDHSIFFHNAHYMVYERLSNWLVNAFNGEWHRIAAPVPDNSMWQRFKRALPVFVH
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Q0CXB1
P20072
ANXA7_BOVIN
Synexin
Bos
MSYPGYPPTGYPPFPGYPPTGQESSFPPPGQYPYPSGFPPMGGGAYPPAPSSGYPGAGGYPAPGGYPAPGGYPGAPQPGGAPSYPGGQGFGAPPGGAGFPGYPQPPTQSYGGGPAQVPLPGGFPGGAMPSQYPGGQSPYPSQPAPMTQGTHGTIRPAANFDAMRDAEVLRKAMKGFGTDEQAIIDVVANRSNDQRQKIKAAFKTMYGKDLIKDLKSELSGNMEELILALFMPSTYYDAWSLRNAMKGAGTQERVLIEILCTRTNQEIREIVRCYQSEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDENQNVNHQLAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLKATMEAYSRMANRDLLNSVSREFSGNVESGLKTILQCALNRPAFFAERLYYSMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFSQMYQKTLGTMIASDTSGDYRKLLLAIVGQ
Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
P20072
A3QBX3
LSPA_SHELP
Signal peptidase II
Shewanella
MPSSWKESGLRWYWVVVLVFVADQLSKQWVLANFDLRESINLLPFFNFTYVRNYGAAFSFLNDAGGWQRWLFTLVAVGFSTLLTVWLRKQPKGLWRLNLAYTLVIGGALGNLIDRLQHGFVVDFLDFYWKTSHFPAFNIADSAICVGAGLIILDSFISERKPNGEDVAKG
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
A3QBX3
C3PA65
ANMK_BACAA
AnhMurNAc kinase
Bacillus cereus group
MYIAGVMSGTSLDGIDVALVRIEGSGVESKVELIHFTTVPFCNDIKSEIQQALSIENSNVQLICSLNFKLGLCFANAVKEVCKEANFSLEQLDLIGSHGQTIYHQPKQDGNRIPSTLQIGEPAVIAYETNTTVISNFRTMDMAAGGQGAPLVPYSEVILYRDPSKNRLLQNIGGISNVTVIPNQQSDQNVIAFDTGPGNMIIDEVCQRLFQLSYDQNGEIAKQGRVVDEILTYCMSHPFLKMNPPKSTGREQFGEKFASELLKRFEKHSKENILTTVTMFTANSIVHHYKKFILPYYEIDEVILGGGGSYNSTLVEMLRNGLKDENCAIFIQEDIGYSSEAKEAIAFAILANETHHCNPSNVPSATGAKQSVVFGNITFPPV
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
C3PA65
Q8ZMF6
ISPD_SALTY
MEP cytidylyltransferase
Salmonella
MAATLLDVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLANHPQITVVDGGNERADSVLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRDTMKRGEPGKNAIAHTVERADLWHALTPQFFPRELLYDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIHQEKA
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q8ZMF6
Q8ZLG5
GLGB_SALTY
Glycogen branching enzyme
Salmonella
MSSRIDRDVINALIAGHFADPFSVLGMHQTQAGLEVRALLPDATDVWVIEPKTGRKVGKLECLDARGFFCGVLPRRKNFFRYQLAVTWHGQQNLIDDPYRFGPLIQEMDAWLLSEGTHLRPYETLGAHADTMDGVTGTRFSVWAPNARRVSVVGQFNYWDGRRHPMRLRKESGIWELFIPGAHNGQLYKFELLDANGNLRIKADPYAFEAQMRPETASMICGLPEKVTPGEERQKANQFDAPISIYEVHLGSWRRHTDNNFWLSYRELADQLVPYAKWMGFTHLELLPVNEHPFDGSWGYQPTGLYAPTRRFGTRDDFRYFINAAHAAGLNVILDWVPGHFPSDEFSLAEFDGTHLYEHSDPREGYHQDWNTLIYNYGRREVSNYLVGNALYWMERFGIDALRVDAVASMIYRDYSRKEGEWIPNEFGGRENLEAIEFLRNTNRIIGEQVPGAVSMAEESTDFSGVTRPPETGGLGFWYKWNLGWMHDTLDYMKLDPVYRQYHHDKLTFGMLYNHTENFVLPLSHDEVVHGKKSILDRMPGDAWQKFANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASLDWHLLEGGDNWHHGVQRLVRDLNHTYRHHKALHELDFDAYGFEWLVVDDNERSVLIFVRRDKAGNEIIVASNFTPVPRHDYRFGINQPGRWREILNTDSMHYHGSNTGNGGVVHSDEIESHGRQHSLNLTLPPLATIWLMREGE
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Q8ZLG5
Q3A949
MURA2_CARHZ
UDP-N-acetylglucosamine enolpyruvyl transferase 2
Carboxydothermus
MEKFVIEGKQRLTGRVKISGAKNAALPILAGALLTGGTVRLTEVPELTDIYTMLEVLKALGAKVTFSEGEVVLHTPEITSAEAPYEQVRKMRASFLVMGPLLARTGRARISLPGGCAIGARPIDLHLKGFEALGAKIEMGHGFIEATAPRLKGTTVYLDFPSVGATENIMMAAVLAEGQTIIENAAEEPEIVDLANFLNNMGAKIKGAGTKVIRITGVKDLDGVNHTVIPDRIEAGTFMIGAVATQGEVIVENVITDHLTPLIAKLIEAGAEVIEDEDQNALLVRSNGKLKPLDIKTLPYPGFPTDLQAQMMALLATVPGISVVTETVFENRFMHVTELNRMGAKIRIEGRSAFIEGVESLTGARVKATDLRAGAALVIAGLVADGVTEVGHIFHIDRGYERFEEKLRGLGAKIERVSD
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Q3A949
P38250
IST2_YEAST
Increased sodium tolerance protein 2
Saccharomyces
MSQTITSLDPNCVIVFNKTSSANEKSLNVEFKRLNIHSIIEPGHDLQTSYAFIRIHQDNAKPLFSFLQNLDFIESIIPYHDTELSDDLHKLISISKSKILEAPKQYELYNLSNLTNNPKQSLYFAFLQNYIKWLIPFSFFGLSIRFLSNFTYEFNSTYSLFAILWTLSFTAFWLYKYEPFWSDRLSKYSSFSTIEFLQDKQKAQKKASSVIMLKKCCFIPVALLFGAILLSFQLYCFALEIFIKQIYNGPMISILSFLPTILICTFTPVLTVIYNKYFVEPMTKWENHSSVVNAKKSKEAKNFVIIFLSSYVPLLITLFLYLPMGHLLTAEIRTKVFNAFSILARLPTHDSDFIIDTKRYEDQFFYFIVINQLIQFSMENFVPSLVSIAQQKINGPNPNFVKAESEIGKAQLSSSDMKIWSKVKSYQTDPWGATFDLDANFKKLLLQFGYLVMFSTIWPLAPFICLIVNLIVYQVDLRKAVLYSKPEYFPFPIYDKPSSVSNTQKLTVGLWNSVLVMFSILGCVITATLTYMYQSCNIPGVGAHTSIHTNKAWYLANPINHSWINIVLYAVFIEHVSVAIFFLFSSILKSSHDDVANGIVPKHVVNVQNPPKQEVFEKIPSPEFNSNNEKELVQRKGSANEKLHQELGEKQPASSANGYEAHAATHANNDPSSLSSASSPSLSSSSSSSKTGVVKAVDNDTAGSAGKKPLATESTEKRNSLVKVPTVGSYGVAGATLPETIPTSKNYYLRFDEDGKSIRDAKSSAESSNATNNNTLGTESKLLPDGDAVDALSRKIDQIPKIAVTGGENNENTQAKDDAATKTPLIKDANIKPVVNAAVNDNQSKVSVATEQTKKTEVSTKNGPSRSISTKETKDSARPSNNNTTTTTTTDATQPHHHHHHHRHRDAGVKNVTNNSKTTESSSSSSAAKEKPKHKKGLLHKLKKKL
May be involved in ion homeostasis together with BTN1 or BTN2.
P38250
B5RLN1
RUVA_BORDL
Holliday junction ATP-dependent DNA helicase RuvA
Borrelia
MINKIYGKIVDKKESSIIILAFPFEFEILVSSFCKMELRLLEDVEILTYFHFRDDDVKLFGFLNISEREVFEDLIGVDGIGPKAALKILSGIKYDAFRLAIAKEDINLISKVKGIGNKIAGKIFLKLRGKLVKGDESSSYMLKFKELEQSIVNMGFDRKLVVVAFREIMLSDKFLILKEAEQEQFLFTETLKRLSV
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
B5RLN1
Q7NSG1
GUAA_CHRVO
Glutamine amidotransferase
Chromobacterium
MDKILILDFGSQVTQLIARRVREAHVYCELHSFDMPIEEIQAFAPKAIILSGGPNSVYESDYQADPKLFELGVPVLGICYGMQFMAQTLGGKVESGDKREFGYAQIKARHHSKLLEGLQDQIDDAGNGFLDVWMSHGDKVTQLPAGFQVIAETPSCPYAAMADEARGFYGVQFHPEVTHTKRGTEMIHRFVLHVAGCKPSWTMPNYIDEAVKKIREQVGDEEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDHGLLRLNEGKMVMEMFAQNLGVKVVHVQAEADFMAKLAGETDPEKKRKIIGAEFIEVFDRESGKLTNAKWLAQGTIYPDVIESAGAKTKKAHTIKSHHNVGGLPEDMNLKLLEPLRELFKDEVRQLGVALGLPHDMVYRHPFPGPGLGVRILGEVKKEYADLLRQADAIFIEELRNTVDEKTGKNWYELTSQAFAVFLPVKSVGVMGDGRTYDYVVALRAVVTSDFMTAHWAELPYSLLGRASNRIINEVRGINRVVYDVSGKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
Q7NSG1
Q9KNG8
ATPZ_VIBCH
ATP synthase protein I
Vibrio
MVAVLARQGRELAKRLLLIQFSAVMVAAAVFAVAVNGDWGLSALVGGGIFVIANAVFAGCAFLFAGARALKMVAISFYTGEALKILITIVLFSVAYMYMQLELVPLKLTYLLALGINICAPVLFINNKK
A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex.
Q9KNG8
B5ZSV9
ISPH_RHILW
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Rhizobium
MNIAAKPPLTIRLCGPRGFCAGVDRAIQIVVLALKSYGAPVYVRHEIVHNRYVVEGLEAKGAVFVEELDEIPAEHRAQPVVFSAHGVPKSVPEDAVSRNLFYLDATCPLVSKVHKQAMRHNRLGRHVVLIGHAGHPEVIGTMGQLPEGSVSLIETIEDADAYIPVDADNLGYVTQTTLSVDDTAGVIARLQERFPNLTAPAADSICYATTNRQEVVKQAAPGCDLFIIVGAPNSSNSKRLVEVALRAGAKKSILVQRAAELDWDEIGAISTLGLSAGASAPEVIVNEIIEAFRARFDARVELAETVQETENFLVNRELRSIELTAADMAFVNG
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
B5ZSV9
Q8MZM3
PPO8_ANOGA
Prophenoloxidase 8
Anopheles
MATLTQKFHGLLQHPLEPLFLPKNDGTLFYDLPERFLTSRYSPIGQNLANRFGPNSPASSQVSNDTGVPPTVVTIKDLDELPDLTFATWIKRRDSFSLFNPEHRKAAGKLTKLFLDQPNADRLVDVAAYARDRLNAPLFQYALSVALLHRPDTKSVSVPSLLHLFPDQFIDPAAQVRMMEEGSIVLDENRMPIPIPMNYTATDAEPEQRMAFFREDIGVNLHHWHWHLVYPASGPPDVVRKDRRGELFYYMHQQLLARYQIDRYAQGLGRIEPLANLREPVREAYYPKLLRTSNNRTFCPRYPGMTISDVARSADRLEVRIADIESWLPRVLEAIDAGFAVSDDGVRVPLDETRGIDVLGNILERSAISINRNLYGDVHNMGHVLLAFIHDPRGTYLESSGVMGGVATAMRDPIFYRWHKFIDNIFLRNKARLAPYTMAELSNSNVTLEALETQLDRAGGAVNSFVTFWQRSQVDLRAGIDFSAAGSAFVSFTHLQCAPFVYRLRINSTARSNRQDTVRIFLLPRQNEQGRPLSFEDRRLLAIELDSFRVNLRPGMNNIVRQSSNSSVTIPFERTFGNVEQANAGNAQSRFCGCGWPAHMLLPKGNANGVEFDLFAMVSRFEDDNANVNYDENAGCDDSYAFCGLRDRVYPSRRAMGFPFDRRASNGVRSVADFVAPYKNMRLATVTLRFMNTIIDRPTN
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (Probable). Catalyzes the oxidation of o-diphenols such as dopamine . Also oxidizes monophenols such as tyramine .
Q8MZM3
Q89ZL5
SECA_BACTN
Protein translocase subunit SecA
Bacteroides
MGFNEFLSSIFGNKSTRDMKEIKPWVEKIKAAYPEIEALDNDALRAKTEELKKYIRESATDERAKVEELKASIESTELEDREEVFAQIDKIEKEILEKYEKALEEVLPVAFSIVKATAKRFTENEEIVVTATEFDRHLAATKDFVRIEGDKAIYQNHWNAGGNDTVWNMIHYDVQLFGGVVLHKGKIAEMATGEGKTLVATLPVFLNALTGNGVHVVTVNDYLAKRDSEWMGPLYMFHGLSVDCIDRHQPNSDARRQAYLADITFGTNNEFGFDYLRDNMAISPKDLVQRQHNYAIVDEVDSVLIDDARTPLIISGPVPKGDDQLFEQLRPLVERLVEAQKALATKYLSEAKRLIASNDKKEVEEGFLALYRSHKCLPKNKALIKFLSEQGIKAGMLKTEEIYMEQNNKRMHEVTEPLYFVIEEKLNSVDLTDKGIDLITGNSEDPTLFVLPDIAAQLSELENQNLTNEQLLEKKDELLTNYAIKSERVHTINQLLKAYTMFEKDDEYVVIDGQVKIVDEQTGRIMEGRRYSDGLHQAIEAKERVKVEAATQTFATITLQNYFRMYHKLSGMTGTAETEAGELWDIYKLDVVVIPTNRPIARKDMNDRVYKTKREKYKAVIEEIEKLVQAGRPVLVGTTSVEISEMLSKMLTMRKIEHSVLNAKLHQKEAEIVAKAGFSCAVTIATNMAGRGTDIKLSPEVKAAGGLAIIGTERHESRRVDRQLRGRAGRQGDPGSSVFFVSLEDDLMRLFSSDRIASVMDKLGFQEGEMIEHKMISNSIERAQKKVEENNFGIRKRLLEYDDVMNKQRTVVYTKRRHALMGERIGMDIVNMIWDRCANAIENNDYEGCQMELLQTLAMETPFTEEEFRNEKKDTLAEKTFNIAMENFKRKTERLAQIANPVIKQVYENQGHMYENILIPITDGKRMYNISCNLKAAYESESKEVVKAFEKSILLHVIDEAWKENLRELDELKHSVQNASYEQKDPLLIYKLESVTLFDAMVNKINNQTISILMRGQIPVQEAPADEQQPRRVEVRQAAPEQRQDMSKYREQKQDLSDPNQQAAASQDTREQQKREPIRAEKTVGRNDPCPCGSGKKYKNCHGQNA
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q89ZL5
Q3SRY8
RS18_NITWN
30S ribosomal protein S18
Nitrobacter
MADAGARRPFFRRRKTCPFTGANAPKIDYKDSKLLMRYVSERGKIVPSRITAVSAKKQRELARAVKRARFLGLLPYVIR
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.
Q3SRY8
A2SAS9
HSCA_BURM9
Chaperone protein HscA homolog
pseudomallei group
MALLQISEPGMAPAPHQRRLAVGIDLGTTNSLVAAVRNSIPEALPDDAGRVLLPSVVRYLDKGGRRIGHAAKEEAAIDPRNTIVSVKRFMGRGKAEVEGAANAPYEFVDAPGMVQIRTVDGVKSPVEVSAEILATLRQRAEDTLGDDLVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDNGAEGLYAVYDLGGGTFDLSILKLTKGVFEVLAAGGDSALGGDDFDHLLFEHVLAQAGLEVAALAPEDVRLLLDRVRGAKEALSAAPQARVDVKLSTGEKLAQTITRDTFAALVEPLVQRTLGPTRKALRDAQVSAADIKGVVLVGGATRMPVIRDAVAKYFGQPPLVNLDPDQVVALGAAIQADLLAGNRSGGDDWLLLDVIPLSLGVETMGGLVEKIIPRNSTIPVARAQEFTTFKDGQTAMAIHVVQGERELVSDCRSLARFELRGIPPMTAGAARIRVTYQVDADGLLSVFAREQHSGVEASVVVKPSYGLGDDDIARMLEDSFKTAEVDMRARALREAQVEAQRLVEATEAALVADGDLLDASERATVDALVASLRALAPGDDADAIDTATKALAEGTDEFAARRMDKSIKRALAGRKLDEI
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
A2SAS9
Q755F7
CET1_ASHGO
mRNA 5'-triphosphate monophosphatase
Eremothecium
MSSEKQEGSPRRVLSLSDLVNREDSKDASGNTAGAALKPLSNDEVRRRLAHEDYSSNTASQVDDETDTDDGLGEVAFDRADFRFDFEGQERSGGRASGEAEAESGGPGHEKATQQPSDAIATSPDRESTEPRAMDIFEERASLESKKNNLRKDLRVLNEIASTARPGRYKVAPIWAQKWKPTVRALQNVNSKDLMKIDVSFTQVIPDDDLTKSVQDWVYATLLSIPPEQRQYVEVEMKFGILMDRSSDSQRVTPPVSSQTVYMEADARMKPDVDERVFVELNRYVKGISELTENTGKFNIIESHNKDEMYRAGINTQRPRFLRMSKDVKTGRVGEFIEKRRISQLLLFSPKDSYDVKISINVELPVPENDPPEKYMGQAPLNSRTKERISYIHNDSCTRIDITKVTNHNKGKRDDAEVTHEIELELNSQALLAAFDKIAQDSKDYATIVRTFLNNGTIIRRKLTSLSYEIFEGGKKVV
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Q755F7
B5QXJ3
ARGO_SALEP
Arginine exporter protein ArgO
Salmonella
MISYYFQGFALGAAMILPLGPQNAFVMNQGIRRQYHLMIALLCALSDLVLISAGIFGGSALLMQSPWLLALVTWGGVAFLLWYGLGALKTAMSSNLELASAEVMKQGRWKIIATMLAVTWLNPHVYLDTFVVLGSLGGQLAMEPKRWFALGTISASFLWFFGLALLAAWLAPRLRTAKAQRIINILVGVVMWLIAFQLAREGVAHMHALFN
Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine.
B5QXJ3
Q7VK73
UVRC_HELHP
Excinuclease ABC subunit C
Helicobacter
MSNKESTSYNLLVHLADLPTQSGIYQFFDNEDTLLYVGKAKNLKNRIKSYLSIENKHIVPKNNLSPRIALMVSQITRIHTLLTNNEQDALILENSLIKSLKPKYNILLRDDKTYPYIYIDKSLPYPRFELTRQVLKSNQIQYFGPFVSGARELLDSLYDNLPLVQKKSCVKGKKACIFHQIHKCPAPCENKVSIQTYAQTIAQGIALIEDKKALLKILESKMHTLSHNLQFEEAAIMRDRIQKITQMKNQSIIDMMSGDYDVFVLQEQDCGKNSQDSHKKSHTALHTHILMMLFIRNGRIISSDFILLHDDIQSHNLPQLYTQALLNHYKTQIPLLPQEILIPPFDFPDLLHLQQLLREQTRSSLKIVQPQRGAKKDLLQLAHKNALEIRRLHTQQNNTFSTLVSIKELCVLSQIPYSIEVFDTSHHSGTHNVGGMIVYENDDFIRSKYRRYELHTSDEYSQMHEMLLRRAQSFDSNPPPALWLLDGGRAQINLALDILKSVGANVEVLAIAKMKHNAKAYRAKGNAFDILRSKNAEFKLKPNDKRLQFLQKLRDEVHRYAITYHRYKKQKDIQKAQMMGKNYTQAQIKKLLDYFGSFESLKTASQEQINSVLSRRNRSDT
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.
Q7VK73
B8I2Z7
RPOZ_RUMCH
Transcriptase subunit omega
Ruminiclostridium
MIYPSINELMKKVDSRYTLAVEAAKRARQLVDGATKMAKCDSDKEVTIAINEIAEDKITYVRTKSGIK
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
B8I2Z7
P65570
NUOD_MYCBO
NDH-1 subunit D
Mycobacterium tuberculosis complex
MTAIADSAGGAGETVLVAGGQDWQQVVDAARSADPGERIVVNMGPQHPSTHGVLRLILEIEGETVVEARCGIGYLHTGIEKNLEYRYWTQGVTFVTRMDYLSPFFNETAYCLGVEKLLGITDEIPERVNVIRVLMMELNRISSHLVALATGGMELGAMTPMFVGFRAREIVLTLFEKITGLRMNSAYIRPGGVAQDLPPNAATEIAEALKQLRQPLREMGELLNENAIWKARTQGVGYLDLTGCMALGITGPILRSTGLPHDLRKSEPYCGYQHYEFDVITDDSCDAYGRYMIRVKEMWESMKIVEQCLDKLRPGPTMISDRKLAWPADLQVGPDGLGNSPKHIAKIMGSSMEALIHHFKLVTEGIRVPAGQVYVAVESPRGELGVHMVSDGGTRPYRVHYRDPSFTNLQSVAAMCEGGMVADLIAAVASIDPVMGGVDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
P65570
A4W070
AROK_STRS2
Shikimate kinase
Streptococcus
MPIVLLGFMGVGKTTTAHLLNLPVYDMDHIIEERIGMPIADYFSLEGEASFRQLETEVLKGLLDLPSNCIVSTGGGVIKSEVNRELLLANREDNVLLTASFEVSYQRIRKDRQSQRPLFLQCSKEEFEALYRERMALYQGLADTVIDTDKLIPEQVARKILCK
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
A4W070
Q8X166
PPIB_ASPNG
Rotamase B
Aspergillus subgen. Circumdati
MNFKNIFLSFFFVLAVGLALVHAEDAQPRGPKITSKVFFDIEHGDKPLGRVVLGLYGKTVPKTAENFRALATGEKGFGYEGSTFHRVIKDFMIQGGDFTRGDGTGGKSIYGEKFADENFKLRHTRKGLLSMANAGKDTNGSQFFITTVPTPWLDGRHVVFGEVLEGYEIVAQIENVPKGRSDRPVETVKIVKSGELESEDKAGEKGSSHEEL
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Q8X166
Q7NZ10
RPPH_CHRVO
(Di)nucleoside polyphosphate hydrolase
Chromobacterium
MLDRDGYRPNVGIILTNAKNEVFWGKRVREHSWQFPQGGIKPGESPEAAMYRELLEEVGLLPQHVKILGRTRDWLRYEVPTNWVRREWRGSYKGQKQIWFLLRLVGRDSDVCLRATNHPEFDGWRWNDYWAPVDAVIEFKRDVYERALSELARFMRGVESHHAYLARTSTQSEQ
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Q7NZ10
B8ZS15
LEU3_MYCLB
Beta-IPM dehydrogenase
Mycobacterium
MKLAIIGGDGIGPEVVAQAVKILDVVLPGVQKTTYDLGARRYHTTGELLPESVLAELREHDAILLGAVGDPSVPSGVLERGLLLRLRFELDHHINLRPARLYPGVNSLLAGKPDIDFVVVREGTEGPYTGTGGAIRVGTPNEVATEVSVNTAFGVRRVVQDAFERARQRRKHLTLVHKNNVLTYAGTLWCRIVQEVGEKYPDVEVVYQHIDAATIYLVTEPSRFDVIVTDNLFGDIITDLAAAVCGGIALAASGNIDATRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSLALLLAHLGEDEPAARLDQAVASYLATRGNGRFSTGEVGERIAAAL
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.
B8ZS15
B8DS03
NUOB_DESVM
NDH-1 subunit B
Desulfovibrio
MAAQDCPVRPPVIAPATGGVDAPIVNVAPVQKILDVCRAMSLWPMTFGLACCAIEMMAVGMARFDISRFGAEVFRPSPRQSDLMIVAGTVTRKMAPALVRLYEQMPAPRYVMALGNCAISGGPFNFEGQYAIVEGVDNLVPVDVYVPGCPPRPEALLEGLFQIQHKITGRRWWPVPAEISGSMGGGA
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B8DS03
Q02C42
ALLB_SOLUE
Allantoin-utilizing enzyme
Candidatus Solibacter
MSECVVRGGQVVQAGGVVSADVAIEDGRISAIGPELPGAKREINARGLTVFPGVIDDHLHFNEPGRTEWEGAATGSRALAAGGGTAFFDMPLNSTPCTVDRAAFAGKRAALERASIADFALWGGIVPGNLSELAPLAESGVIGFKAFLSDSGLPEFPRADDLTLYEGMREAARLGLPVAVHAESEEITSRLTRRARDAGRTSARDYLDSRPVIAEVEAIHRAALLAREAGCKLHIVHISSGRGVAAALEARTMGTDIAIETCAHYLFFTEDDLLRLGAIAKCAPPLRDRQEFDRLWAHVLGGIVDVVASDHSPAPPAMKTGDDFFAIWGGIAGVQSTLAVLLEAGHFQRGLRLERIAELTAGYPARRFALHNKGSIAVGNDADLTLVDMDGQENLEPESLWQKHPVNPYTGNSFRGSIRRTMLRGTTIFNHDEITVKSGGQLLRPKANTYATSGIHP
Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
Q02C42
O14107
DNI1_SCHPO
Delayed minus-nitrogen induction protein 1
Schizosaccharomyces
MLFLHSVVQGTGTLCTLAAWILLALVMTGCQSSTTSKFQLFSLATNVAQINVGYFNMCVLSANATLICKPQFTGCPGLTSISLTDVRSKFLINEVHPWMIVFSFCVCGVSFLMGVVSSLPLIGRLEFLRNIRISLSFFSFFSILVTALFAHVAVSSFVMAVGNGTQNRVTASLGKKAMIFLWCSMGLVTLTGITDSIILLVTSRTKKIRKTILEKSKVLTPSSSFSSKSSTTKY
Cell membrane protein which plays a relevant role in coordinating membrane organization and cell wall remodeling during mating.
O14107
Q49XM7
ARLR_STAS1
Response regulator ArlR
Staphylococcus
MTKILIVEDEQNLARFIELELEHENYDVDIEYDGKPGLEKALSNTYDLILLDLMLPNINGLEICRQIRQNQTTPIIIITAKSDTYDKVAGLDYGADDYIVKPFDIEELLARIRAMLRRQPQKNLIDIKGIIIDKDAFKVTVDGQPLDLTKTEYDLLFLLVENRNHVLQREQIITDVWGYDTEVETNVVDVYIRYLRNKLKPFGKDKCIETVRGVGYVVRQ
Member of the two-component regulatory system ArlS/ArlR.
Q49XM7
Q089N1
RS11_SHEFN
30S ribosomal protein S11
Shewanella
MAKVPSRSPRKRVRKQVADGMAHIHASFNNTIVTITDRQGNALSWATSGGSGFRGSRKSTPFAAQVAAERAGIAAQDYGVKNLEVFVKGPGPGRESAIRALNAVGYKITNITDVTPIPHNGCRPPKKRRV
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.
Q089N1
B6EKN1
LEPA_ALISL
Ribosomal back-translocase LepA
Aliivibrio
MKHIRNFSIIAHIDHGKSTLSDRLIQVCGGLSDREMAAQVLDSMDLERERGITIKAQSVTLNYTANDGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTALEMDLEVVPILNKIDLPAADPDRVAEEIEDIVGIEAMEATRCSAKTGLGVDAVLETIVKCIPAPEGNPEGPTQALIIDSWFDNYLGVVSLVRVKHGSLKKNDKIKVMSTGQAWNVDRIGIFTPKQVDTDGLNTGEVGWVVCGIKDILGAPVGDTLTHAKGGCEERLPGFQKVKPQVYAGLFPISSDDYENFRDALGKLSLNDASLFYEPESSSALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAPTVVYEVVLNNGDLLYVDSPAKLPAVNDLDEIREPIARCNILVPAEYLGNVISLCIEKRGTQVDMIYHGNQVALTYDIPMSEVVLDFFDRLKSTSRGYASLDYNFQRYELSNMVRVDVLINAERVDALAIITHHDNAQGRGRLLVEKMKEFIPRQMFDIAIQAAIGGHIIARSTVKQLRKNVIAKCYGGDISRKKKLLKKQKDGKKRMKQIGNVELPQEAFLAILHVGKD
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
B6EKN1
A9H0U2
AROC_GLUDA
5-enolpyruvylshikimate-3-phosphate phospholyase
Gluconacetobacter
MSHNSFGHLFRVTTWGESHGPAIGCVVDGCPPRLPLSEADIQPWLDRRRPGQSKFTTQRQEPDAVEILSGVFEGQTTGTPISLLIRNTDQRSRDYGDIAERYRPGHADVAYDLKYGIRDYRGGGRSSARETAMRVAAGAVARRVLGEGVRIRGALTQIGAHRVDRARWDWDAVDTNPFFCPDPAMVPVWEEYLGAVRKAGSSIGAVIEIVAEGVPAGWGAPVYGKLDSDLAMALMSINAVKGIEIGDGFAAAELTGEENADPMRMVDGRLTFGANHAGGVLGGISTGQPLVARFAVKPTSSILAPVDSVTRGGENVEVSTRGRHDPCVGIRAVPVGEAMMACVLADHFLRHRAQVGP
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
A9H0U2
B4EC23
ISPD_BURCJ
MEP cytidylyltransferase
Burkholderia cepacia complex
MTPRLFALIPCAGTGSRSGSAVPKQYRTLAGRALLHYTLAAFDACTEFAQTLVVLAPDDSHFDARRFAGLRFAVRRCGGGSRQASVLNGLLELAEFGATDHDWVLVHDAARPGITPELIRTLVATLKDDPVGGIVALPVADTLKRVPAGGDAIARTESRDALWQAQTPQMFRIGMLREAILRAQREGHDLTDEASAIEWAGHTPRVVQGSLRNFKVTYPEDFALAEAILARPANAS
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
B4EC23
Q3JC02
SYT_NITOC
Threonyl-tRNA synthetase
Nitrosococcus
MPVITLPDGSQRSFDHPVTVYDVAADIGPGLAKAALGGKIEGRLVDSSYPLEKDTKLTIITERDMDGLEIIRHSCAHLLAQAVKALYPEAQVTIGPVIEDGFYYDFAYPKGFTPEDLEAIEAKMRELVEQDLSVHRELKSREEAVSLFRRMGEEYKAEIIASIPSEEEISLYRQGDFVDLCRGPHVPSTARLKAFKLTKVAGAYWRGDANNEMLQRIYGTAWPDKKALKAYLHRLEEAEKRDHRRIGADLDLFSIQEEAGGGLVFWHPMGARIRRVIEDFWQERHTAAGYEMLYTPHIAHEELWQTSGHTDFYRESMYQPMEDDHQLYQLKPMNCPFHVLIYQGRLRSYRELPIRWAELGTVYRHEMSGALHGLMRVRGFTQDDAHIFCREEQIENEILGILDLTLEMLAAFGFDRYEIDLSTRPEKSVGPEAIWEQATQALRSALDKKGLDYAVDEGGGAFYGPKIDIKIEDAIGRKWQCSTVQLDFNLPERFAMEYVAEDGARHRPIMIHRAVLGSLERFFGVLIEHYEGKFPPWLAPVQVVVMSITDRQEGYARQVEEAMRNKGFRSLLDLRNEKIGFKIREHILRRIPYLLVIGDREVANQTVAVRTRYSQDLGAMSLDAFMEHLSVDVARLGHNISEED
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Q3JC02
B1ZQ93
RNY_OPITP
Ribonuclease Y
Opitutus
MSAADFAFLIAESDLFDWSLTVALVIGGALGFLVVWAFTRHTRRMAHEQAAELEEVARREAAVAAEEIRQKAEAEIQEKRAELNRDFDRREIESEVRLREIRAHEESLALLDYQLEQRQERLNRETAAMRQARDAIRALSKSVRQRLEGVSQMDAESIRQALREEVQLECQDELRALRREIMEKSEQDLQTEGRRIMIAAMQRLASKPNNDLTSTIVSLPNEDMKGRIIGREGRNIKAFEAATGVTVLIDESPQTVLISSFDPIRREVARGALEALIKDGRIHPATIEEFVKRAHEEIELSAMQAGEDAVTRLNINGLHPEIIKLLGKLKFRFSYNQNVLDHSVETASLASMIASEVGLDPNVAKRAGLLHDIGKAVNADYEGSHAHIGAEFIRRYGETPIVVNSVAAHHEEVKPETVYAGLVILADTISATRPGARAESMAGYIQRLGRLEKLAMAIDGVQQAFAIQAGREIRVVVSPQTVTDDRAREIAKELRKRIEAELQYPSTIKITVIREQRFTETAT
Endoribonuclease that initiates mRNA decay.
B1ZQ93
B4ETP0
CMOB_PROMH
tRNA U34 carboxymethyltransferase
Proteus
MINFSSFYQHIAQDERLFHWLDTLPAQLSEWRAHALHGHFASWERMLENLPEITPTELNLKQGVIANKTPALSTGEQLGLTNILKALMPWRKGPFSLYGVNIDTEWRSDWKWDRVLPHLSPLKGRLVLDVGCGSGYHMWRMLGEGADFVVGIDPTQLFLCQFEAVRKLLGNDQRAHLIPVGIEQMPELNAFDTVFSMGVLYHRRSPLDHLWQLKNQLVSGGELVLESLVIDGDEFQCLIPGERYAQMRNVYFIPSAKMLKVWLEKCGFKDVRIVDENVTSLEEQRKTDWMVTDSLEAFLDPLDHTKTVEGYPAPKRAILIATKP
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
B4ETP0
D8VPP5
AL11A_OLEEU
Pollen allergen Ole e 11.0101
Olea
MSCIAVEAVLLGILLYIPIVLSDDRAPIPSNSAQLNSWFDGIIQPVAVRKATMDPALVTAEGQTKVIKLKSDGSGDFKSINEAIKSIPDDNTKRVILSLAPGNYSEKVKIGMYKHYITFYGEDPNNMPILVFGGTAAEYGTVDSATLIVESNYFSAVNLKIVNSAPRPDGKRVGAQAAALRISGDKASFYNVKIYGFQDTLCDDKGKHFYKDCYIEGTVDFIFGSGKSIFLNTELHAVPGDQPAIITAQARKTDSEDTGYYFVNCRVTGGGAFLGRSWMPAAKVVFAYTEMVDAIHPEGWILVKPEHESTVRFSEYNNKGPGANMEKRAKFVKRLSDAEAKQSISLGSIEASKWLLPPRVVGLP
Catalyzes the demethylesterification of homogalacturonan components of pectin. May be involved in pollen tube development.
D8VPP5
Q73K78
DXR_TREDE
2-C-methyl-D-erythritol 4-phosphate synthase
Treponema
MGRKRVVVLGAGGSIGKNSLEIIRRFPDRFELAGFSVHSNSGFAKTLLAEFTDAQFVSTKKKNSNLKHEIDEEAVRRLIEKSKADIVINGIAGSAGLKASVEVIKSGLDLALANKETIVEAGELIFQDAEKSGSTIIPVDSEHAAIFQLINAHKKGNIEKIIITASGGPFLNTPREKLSTIKLEDALKHPTWKMGGKISIDSASLANKALEVIEAVKLFSFPPEKIEVTVHPQSIIHSMVQCKNGEIFAQASPPDMKNPILNALSFPKMPESFLKPLDFSQIIKLEFMPPRTDDFPMLALGFEAAGKGGAYPIAFNVANEEAVDAFIKGKIGFTDLADITQEVLNSDWTMKPSSYEEVYDYENRARAIALARILDRVNGLQ
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q73K78
Q5R514
UMPS_PONAB
OMPdecase
Pongo
MAAVGAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADTLFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETAEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKIDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFSARAELPRIHPVASKLLRLMQKKETNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKRHEFLIFEDRKFADIGNTVKKQYEGGVFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADCLEAAEMYRKAAWEAYLSRLGV
Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
Q5R514
Q47NX7
ARC_THEFY
Proteasomal ATPase
Thermobifida
MADRDDERHAERDRDELVAQVSYLEKELSVLRRKLADSPRHVRLLEDRLQEAQTALAAANAKNERLVSALKEARDQIVALKEEVDRLSQPPSGFGVFLRARDDGTVEIFTNGRKMRVNVSPSVNVDELRPGQEVMLNEAFNVVEASSYETVGEVVMLKEILEDGERVLVISNHDEERIVRIAEPLRDEPLRAGDSLLLEPRSGYVYERIPKAEVEELILEEVPDISYSDIGGLNGQIEMIRDAVELPYLHKELFREHKLRPPKGVLLYGPPGCGKTLIAKAVANSLAKQVAEKTGRDVGKSFFLNIKGPELLNKYVGETERHIRLVFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVENTIVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAARDIFSKYITPDLPLHPDDLAEHGGSPTATVNAMIQRVVERMYAETEENRFLEVTYANGDKEVLYFKDFNSGAMIQNIVDRAKKMAIKDYLENGSKGLRVSHLLQACVDEFSENEDLPNTTNPDDWARISGKKGERIVYIRTLVSGKKGADAGRSIDTVANTGQYL
ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
Q47NX7
A4VP82
CH60_PSEU5
Chaperonin-60
Pseudomonas
MAAKEVKFGDSARKKMLVGVNVLADAVKATLGPKGRNVVLEKSFGAPTITKDGVSVAKEIELKDRFENMGAQLVKDVASKANDEAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKATIAIVAELKQLAKPCTDSKAIAQVGTISANSDESIGQIIAEAMERVGKEGVITVEEGSGFENELSVVEGMQFDRGYLSPYFINKPDTMVAELDNPLLLLVDKKISNIRELLPVLEGVAKAGRPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLSLETATLEHLGNAKRVVLNKENTTIIDGAGAQADIEARVAQIRKQIEDTTSDYDKEKLQERLAKLAGGVAVIKVGAGTEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRALQAISELKGDNEDQNVGIALLRRAVEAPLRQIVANAGGEPSVVVDKVKQGSGNYGFNAASDTYGDMIEMGILDPAKVTRSALQAAASIGGLMVTTEAMVAEVVEDKPAPAMPDMGGMGGMGGMM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
A4VP82
A0A1U8QHE3
PBCA_EMENI
Pimaradiene biosynthesis cluster protein A
Aspergillus subgen. Nidulantes
MTCADVTDLCTQASQLVQQLRTKDGELGFMSAAVYDTAWVSMVQKTTPEGRQWLLPKCFEYILRTQLEDGSWETYASDVDGILNTAASLLALETHAESRIASTDPPVEEMKERIGRARAALSRQLQAWSVKDTVHVGFEIILPALLRLLREKGHEFEFDGRAELDRLNRIKLSKFRPEYLYSARTTALHSLEAFVGMIDFDKVAHQKVNGSFMFSPSSTAAFLMFSSSWDDECEQYLRLVLQNGAGGGTGGMPSAYPSKYFEVSWVRGQLARLESKLTELQALTTLLDNGYSTGDLGIEDTDSLGEMLRDALVKGGGIVGFAPSIQADADDTAKSLIAVSLLDKPVSAQGLIDAFEGPMHFRTYHGERDPSFTANSNVLLALLNTPDAATVSPQIEKAAAFLCDVWWTADSEIGDKWNLSPYYPSMLMAEAFGKLLQVWSDGGLKSISSQFIRDRVSVCLYQALVRTLQTQNENGSWGSHSHEETAYAILTIAHACQLPVVNQLWTNVQLAVSRGRKFLQNSAGDKAEYLWVEKVTYSSILLSKSYVLAALKVSFERSYPACLANLFIVSKKRVIEFARFHSMLPLFSSMELWKVRAAIVEGYLLLPQLRDRRLAVFSRTGMEEDKYFEYIPFTWTLCNNRRNTFLSTKTLVEMMVISFLNYQADEFMEAVVGRLNSSQRSMTRSCIDEIFRDLKDKPELNDAIQAQSGPRNADANGHRILPQAKRIKMGSQLPSDVSRVLSAFVHHVMDHPSVKAAAPLEYERVKNELQVFLLSHIEQADDNGRFAAQLESTRDDFETARSSFYRWVSSTSSDHTSCPYSFAFYQCLLGFEQASHNAACFQTCEEKYVAEAMCRHLAVMCRMYNDYGSLARDRDEKNLNCVNFPEFAQAGPKSDAVRQKQLFSLAEFERSNMKRGLEVLTEMAAQDRAKMRMLEKVQMFCDVTDVYGQIYALEILRVGCDLAHDCFMLELPAQWSNST
Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
A0A1U8QHE3
B2UPT6
NUOB_AKKM8
NDH-1 subunit B
Akkermansia
MVTTNEPNIYETGVLDSNAEGNFVYTTLDAAINWIRKNSLWPMPMGLSCCAIEFMAVACSRYDLSRFGSEVTRFSPRQADVMIVAGTVTYKMALAVRRIWDQMPEPKWCIAMGACASTGGMFRSYSVLQGVDKILPVDVYISGCPPRPEAILEALLTLRKKLDTQQPARTFFKKEEPREANAPVPVNTEMPLE
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B2UPT6
Q06067
ATOS_ECOLI
Signal transduction histidine-protein kinase AtoS
Escherichia
MHYMKWIYPRRLRNQMILMAILMVIVPTLTIGYIVETEGRSAVLSEKEKKLSAVVNLLNQALGDRYDLYIDLPREERIRALNAELAPITENITHAFPGIGAGYYNKMLDAIITYAPSALYQNNVGVTIAADHPGREVMRTNTPLVYSGRQVRGDILNSMLPIERNGEILGYIWANELTEDIRRQAWKMDVRIIIVLTAGLLISLLLIVLFSRRLSANIDIITDGLSTLAQNIPTRLPQLPGEMGQISQSVNNLAQALRETRTLNDLIIENAADGVIAIDRQGDVTTMNPAAEVITGYQRHELVGQPYSMLFDNTQFYSPVLDTLEHGTEHVALEISFPGRDRTIELSVTTSRIHNTHGEMIGALVIFSDLTARKETQRRMAQAERLATLGELMAGVAHEVRNPLTAIRGYVQILRQQTSDPIHQEYLSVVLKEIDSINKVIQQLLEFSRPRHSQWQQVSLNALVEETLVLVQTAGVQARVDFISELDNELSPINADRELLKQVLLNILINAVQAISARGKIRIQTWQYSDSQQAISIEDNGCGIDLSLQKKIFDPFFTTKASGTGLGLALSQRIINAHQGDIRVASLPGYGATFTLILPINPQGNQTV
Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine . Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon . AtoS is a membrane-associated kinase that phosphorylates and activates AtoC in response to environmental signals .
Q06067
Q8A7G0
QUEF_BACTN
PreQ(0) reductase
Bacteroides
MAELKDQLSLLGRKTEYKQDYAPEVLEAFDNKHPENDYWVRFNCPEFTSLCPITGQPDFAEIRISYIPDIKMVESKSLKLYLFSFRNHGAFHEDCVNIIMKDLIKLMNPKYIEVTGIFTPRGGISIYPYANYGRPGTKFEQMAEHRLMNRE
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Q8A7G0
Q4AAF8
RL15_MESHJ
50S ribosomal protein L15
Mesomycoplasma
MSIRLENLSYTPGARKEKHRKGRGHAAGKGKQAGRGQSGQKKRSTVRLGFEGGQNPWFRRVPKRGFRNFNKKEYEIFNISDLESRYQDGDTVSLESLYLKKVLKKRNMKAKLLANGDLTKKLTVTTNAFSIAAQKKIEEKGGKIEVR
Binds to the 23S rRNA.
Q4AAF8
H9TB19
AOXB_CAVPO
Azaheterocycle hydroxylase 2
Cavia
MPHPPGSDVLVFFVNGRKVTERDVDPEVTLLTYLRRNLGLTGTKSACGGGSCGTCTVMLSRFDLASRKPRHIAVTACLVPLCSLHGAAVTTVEGVGSIRTRVHPVQERIAKSHGTQCGFCTPGMVMSLYALLRSHPQPSEEQLLEALAGNLCRCTGYRPILESGRTFCLDSASCGQHGARQCCLDQPGDGTCPPGRNGPQAHMCSELIPRTEFQPWDPTQEPIFPPELMRMAESPVQPSLTFRGDRVTWVSPGSLQELLALRARHPEAPLVLGNTALGPAQRSQGRVHPLLISPARIPELSTVTETSDGLTIGASCSLAQLQDILAKSISQLPVEKTQTLRALAKALRSVAGLQVRNLASLGGHVMSLHSYSDLNPILAVGQAALHLRSEGGARLISLDEHFLAGVVSASLQPGEILESVHIPHSQKWEFVFSFRQAQAPQNASPHVSAGMRVRFTEGTDTIEDLSIAYGGVGTTTVMAPQACQRLLGRHWTEETLDEACRLVLGEVTIPGAAPGGRVEFRRTLLVSFLFRFYLQVLQELKAHRFLKPPCTPRTLSDTWKYPQLPDQTLGALEDVPIMVPRGVQMYERVDPQQPPQDPVGRSIMHLSGLKHATGEAVFCDDLPRVDKELFMALVTSTRPHAKIVSVDPAEALRLPGVVAIVTAEDIPGTNGTEDDKLLAVDKVLCVGQVICAVVAETDVQARQATGSVRVTYEDLEPVVLSIQDAIGHSSFLCPEKKLELGNTEEAFEDVDHILEGEVHVGGQEHFYMETQRVLVIPKVEDQELDIYASTQDPAHMQKTVSSTLNVPLNRVTCHVKRVGGGFGGKQGRSAMLGAIAAVGAIKTGRPVRLVLDRDEDMLITGGRHPLFGKYKVGFMDSGRIKALDIQCYINGGCVLDYSELVIEFLILKLENAYKIRNLRFRGRACRTNLPSNTAFRGFGFPQGALVIESCITAVAAKCGLLPEKVREKNMYRTVDKTIYKQAFSPEPLHRCWAECLEQADVPGRRALADAFNRQSPWRKRGIAVVPMKFSVGFAATSYHQAAALVHIYTDGSVLVTHGGNELGQGIHTKMLQVASRELRVPLCRLHIQETSTATVPNTVTTAASVGADVNGRAVQNACQTLLKRLEPIMKKNPEGTWEAWVEAAFEQRISLSATGYFRGYKAFMDWEKGEGEPFPYCVFGAACSEVEIDCLTGAHRKLRTDIVMDAGCSLNPALDIGQVEGAFLQGAGLYTTEELHYSPEGALLSGGPEEYKIPTAADVPEKLNVTLLPSAQAQTGLTIYSSKGLGESGMFLGSSVFFAIQDAVAAARRDRGLAEDFTVPREDPGTCKPWSISVA
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal.
H9TB19
A6W3D6
METK_MARMS
Methionine adenosyltransferase
Marinomonas
MSEYSLFTSESVSEGHPDKIADQVSDAILDAILAEDPEARVACETLVKTGMVLVAGEVRTNAWVDIEEIARGVIREIGYNSSDMGFDWESCAVMNAIGKQSADIAVGVDEAGEHEQGAGDQGLMFGFATNETDVLMPAPITYAHRLVQRQAEVRKNGTLDFLRPDAKSQVTFRYDENGKPCAIDAVVLSTQHSASVKQADLREAVMEEIIKPVLPAEWLSKETKYFINPTGQFIIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLADKCEIQISYAIGVAEPTSISINTFGTGKVSDAVISQLVREHFELRPAGLIKMLDLKRPIYLPTAAYGHFGREGENFTWEKTDKADALRKAAGL
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.
A6W3D6
P29599
SUBB_LEDLE
Alkaline protease
Lederbergia
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATSLGSTNLYGSGLVNAEAATR
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
P29599
Q1BR97
MNMG_BURCA
Glucose-inhibited division protein A
Burkholderia cepacia complex
MLFPTEFDVIVVGGGHAGTEAALASARMGAKTLLLTHNIETLGQMSCNPSIGGIGKGHLVKEVDALGGAMAAATDESGIQFRILNSSKGPAVRATRAQADRILYKAAIRHRLENQPNLWLFQQAVDDLMVEGDRVVGAVTQIGIRFRARAVVLTAGTFLDGKIHVGLNNYTGGRAGDPAAVSLSSRLKELKLPQGRLKTGTPPRIDGRTIDFSKLDEQPGDLDPIPVFSFLGRADQHPQQLPCWVTHTNERTHDIIRGGLDRSPMYTGVIEGVGPRYCPSIEDKIHRFASKESHQIFLEPEGLTTHEFYPNGISTSLPFDVQLELVHSMRGLENAHILRPGYAIEYDYFDPRALKASLETKAINGLFFAGQINGTTGYEEAAAQGLLAGLNAGRYVQEKDAWCPRRDQAYLGVLVDDLVTRGVAEPYRMFTSRAEYRLSLREDNADMRLTEIGRELGLVDDARWDAFSRKRDAVSRETERLKSTWVTPKTLPVEEATALLGKAIDHEYSLAELLRRPGVSYDGVCGLKGGECGPAEPLADDPVLLEQIKEQVEIGIKYQGYIERQASEIERNDANENTRLPDGIDYREVRGLSFEVSQKLNEFRPETIGQASRISGVTPAAISLLMVHLKRRGLGRRNGTAAEAAEQGDGAVPTQQ
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q1BR97
B8N9H4
LIS1_ASPFN
Lissencephaly-1 homolog
Aspergillus subgen. Circumdati
MPPLLTNRQAEELHKSMIAYLVASDLPDTAAALRREVNLSEDVFDPTTAKRYEGMLEKKWTSIARLQKKIMDLESRNATLQSELDNSTPASRLKRNQDPASWLPSTVRYSLESHRDKVNCVAFHPTFSSIASGSDDCTIKIWDWELGELERTLKGHTRAVRDVDYGGPRDNVLLASCSSDLSIKLWKPTDNYKNIRTLQGHDHIVSAVRFIPSRNLLVSASRDNDMRIWDVTTGYCVKTINGHTDWVRDVSISFDGRFLFSTGQDMTARLWDISTVSNIEHKRTMLGHENFIECCAFAPPTSYQFLAPLAGLGKRPSSTNGADFMATGSRDNTIKIWDSRGTCLMTLVGHDSWVQALVFHPGGKYLLSVSDDKTLRCWDLNQQGKCVKTLDAHESFVTSLRWAPGVAKNVPGGDGAAEGEGNDKNGAGSENPANIQMRCVVATGGWDQKLKIFAG
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
B8N9H4
P42305
DBPA_BACSU
ATP-dependent RNA helicase DbpA
Bacillus
MSHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAALERKDLVVKSQTGSGKTASFGIPLCELANWDENKPQALILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISFVTAFEKRFLADIEEYIGFEIQKIEAPSQEEVARKKPEFLAKLNDRPESKKDKSEELNKDIMKLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNKANK
DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes (Probable).
P42305
Q5FUJ8
MRAY_GLUOX
UDP-MurNAc-pentapeptide phosphotransferase
Gluconobacter
MLFNLIAAHDTSHGGFFNLFHYLTFRSGCACLTALVISLALGNPFIAQLKRIQREGQPIRTVGPERHILEKAGTPTMGGMLILIALFSATLLWADLTNGFVWAVMLTTAAFGAVGFADDYLKLSKRNTTGVSKRTRLGCEFLASLIAGIWLQSLTPPELRNMVAFPFVKDVLLPLGYAFPIFAMITITGFGNAVNFTDGLDGLAIVPVVIAALVFALISYLVGNHVFADYLQLHPVPGTGELAVFCAALIGAGLGFLWFNAPPAAVFMGDTGSLSLGGALGAVAVATKHELVLCIVGGVFVAETLSVVIQIFWFKRTGRRVFLMAPLHHHFEKKGWQEPKIVIRFWIVSIVLGLCGLATLKLR
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Q5FUJ8
Q48LX4
MLTF_PSE14
Murein lyase F
null
MFFRPDFRPRCAKWLIATGLFLMLGACVEKPTTLERVKEDGVLRMITRNSPATYFQDRNGETGFEYELVKRFADDLGVELKIETADNLDDLFDQMNKPGGPVLGAAGLIETPKRKQQARFSHSYLEVTPQVVYRNGQSRPTDPGDLVGKRIVVLKGSAHAEQLAALKAQNPGLEYEESDAVEVVDLLRMVDEGQIDLTLVDSNELAMNQVYFPNVRVAFDLGEAREQRWVVAPGEDNSLLNEINAYLDKVEKNGTLQRLKDRYYGHVDVLGYVGAYTFAQHLQERLPKYEKHFQTSAKKEQVDWRLLAAIGYQESMWQPAVTSKTGVRGLMMLTQNTAQAMGVTNRLDARQSIQGGAKYFAYVKDQLDDSIKEPDRTWLALASYNIGSGHLEDARKLAQNEGLNPDKWLDVKKMLPRLAQKKWYSKTRYGYARGGEPVHFVANIRRYYDILTWVTQPQLEGSQVADGNLHVPGVDKTQPPAPPAPASGSSPDKPAL
Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Q48LX4
P0C7A4
SEMG2_PONAB
Semenogelin II
Pongo
MKSIILFVLSLLLILEKQAAVMGQKGGSKGQSPSGSSQFPHGQKGQHYFGQKDQQHTKSKGSFSIQHTYHVDVNDHDRTRESQQYDLNALHKTRKSKQHLGGSQELLNYKQEGRDHDKSKGHFHMIVIHHKGGKAHRGTQNPSQDQGNSPSGRGISSQYSNTEKRLWVHGLSKEQASASGAQKGRTQGRSQSSYVLQTEELVANKQRETQNSHQNKGHYQNVVEVREKHSSKLQTSLRPAYQDRLQHGPKDIFTTQGELLVYDKNQHQTKNLNQDQEHGRKAHKISYQSSHTEERQLNHGEKSVQKDISKGRISIQTEEKIHGKSQNQVTIHSQDQEHGHKENKMSYQSSSTEERHLNCGEKGIQKSVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSGEKDIQKGVSKGSISIQTEEKIHGKSQDQVTIPSQDQEHGHKENKMSYQSSSTEERRLNYGGKNTQKDVSQSSISFQTEKLVEGKSQIQTPNPNQDQWSGQNAKGKSGQSADREQDLLSHEQKGRYQQESSAARNIVITEHEVARDDHLTQQYNEDRNPIST
Participates in the formation of a gel matrix (sperm coagulum) entrapping the accessory gland secretions and ejaculated spermatozoa.
P0C7A4
P54734
PKNA_NOSS1
Serine/threonine-protein kinase PknA
Nostoc
MEQLLDNRYRVIKTLGSGGFGETFLAEDSQMPSNRRCVVKQLRPIHNNPQIYQLVQERFQREAAILEDLGSYSGQIPTLYAYFQSNTQFYVVQEWVEGDTLTAKLKQQGVLSESAVRDILINLLPVLEYVHSKRIIHRDIKPDNIILRHRDGKPVLIDFGAVRESMGTVINSQGNPTSSIVIGTPGYMPSEQAAGRPVYSSDLYSLGLTAIYLLTGKQPQELETEPHSGEIIWHRYALNISPTLAAVIDRAIAYHPRERFTTAREMLEALQLGVVSYPPTVPYQQPQSSPTVPYQQPPVVTTPPFATQTNTVAVSPGTAPTPQPINHNNSNKGILMGSLIAGGLIGASVVIGFALTRPNQPVTQTTSLPSETTISNNDTPTVEPSPTDTPETPISQTVTQDPTPQASVRFPINSRPFTTPIDSKPRNTTEPTTSVPQPTTPSEPQITTPVEATDRPSPEQAVQNYYETINQGEYSTAWNLLASSFQNNRKLHPRGYDSYLDWWGGQVENVDVEQVSLLKANADTATVNARLRYFMKSGRQSSSSVRFSLVWDADNNRWVVSGAR
Probably required for both normal cellular growth and differentiation. Inactivation of pknA leads to colonies that appear light green and rough in the absence of combined nitrogen.
P54734
Q6D3T7
CLPS_PECAS
ATP-dependent Clp protease adapter protein ClpS
Pectobacterium
MGNNRTWSQSESLTADQQKEKLQPPSMYNVVLNNDDYTPMEFVIDVLQKFFSYDIERATQLMLTVHYQGKAICGVFSAEVAETKVVQVNRYARENEQPLLCTLEKA
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Q6D3T7
Q09316
CK5P1_CAEEL
CDK5RAP1-like protein
Caenorhabditis
MLRQWWLRSVGSCSTVYRAHSGCSTSAAVKPKRAIPTDGLQLSDFIKESTKKQRQKAIIPSIEDTKEYLNPEDLQGNGRTVCYVTYGCQMNVSDMEIVRSIMTKYGFVESDKKENADIVLLMTCSIRDGAEKKVWNQLKLIRSNSVNKGQIVGVLGCMAERVRHDLLEKRNLVNIVAGPDSYRDLPRLVAVAAGGSNGINVQLSLDETYADVQPIRVDSASKTAFISIMRGCDNMCTYCVVPFTRGRERSRPIESIVEEVQRLRDQGYKQVTLLGQNVNSYRDMTSMDFSMAPSTSQEDRVPGFKTVYKPKSGGLTFTTLLEKVADAAPDIRFRFTSPHPKDFPMQLIELIASRPNLCKQLHLPAQSGDDETLERMERGYTRDLYLRLVDDIRHVLPSVSLTSDFIAGFCGETEQAHQNTLSLIRAVRYSFCFVFPYSMRGKTRAHHRLTDDVPEDVKARRHLDLTTVFREEALKLNQALIGSEQTVLLEGKSKRDASFSHGRIDGGVKAVFDNSKLCLEPGQYAKILITDANSQTLKAQLIGQSSI
Potential regulator of CDK5 activity.
Q09316
Q6CZF2
WECG_PECAS
UDP-N-acetyl-D-mannosaminuronic acid transferase
Pectobacterium
MTALKTTETIPLYTIRGLPIHGFRNMGTFVDYLFAGERVETGTLVAINAEKVLTAEKEVALRTLLDRAEYKYADGISIVRSIRRKYPQADVTRIAGADLWEALMERAGKQETPVFLVGGKPDVLAQTEAKLRAQWDVNIVGSQDGYFTPEQRDALFERIRASGAQIVTVAMGSPRQEILMRDCRHHYPDALYMGIGGTYDVFTGHVKRAPLVWQNLGLEWLYRLLSQPSRIFRQLRLLKYVAYHYSGRL
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis.
Q6CZF2
Q88XS8
CITD_LACPL
Citrate lyase gamma chain
Lactiplantibacillus
MEIKTTAVAGTLESSDIQIMLMAGDNGIQIDLESDVIKQFGAQIKHVITTTLQQLNIDNVKVRAVDKGALDCVIKARTITAAQRALETTTPAWEVL
Covalent carrier of the coenzyme of citrate lyase.
Q88XS8
A7ZK04
LPXK_ECO24
Lipid A 4'-kinase
Escherichia
MIEKIWSGESPLWRLLLPLSWLYGLVSGAIRLCYKLKLKRAWRAPVPVVVVGNLTAGGNGKTPVVVWLVEQLQQRGIRVGVVSRGYGGKAESYPLLLSADTTTAQAGDEPVLIYQRTDAPVAVSPVRSDAVKAILAQHPDVQIIVTDDGLQHYRLARDVEIVVIDGVRRFGNGWWLPAGPMRERAGRLKSVDAVIVNGGVPRSGEIPMHLLPGQAVNLRTGTRCDVAQLEHVVAMAGIGHPPRFFATLKMCGVQPEKCVPLADHQSLNHADVSALVSTGQTLVMTEKDAVKCRAFAEENWWYLPVDAQLSGDEPAKLLTQLTSLASGN
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
A7ZK04
P52754
HYP1_HYPJE
Hydrophobin I
Trichoderma
MKFFAIAALFAAAAVAQPLEDRSNGNGNVCPPGLFSNPQCCATQVLGLIGLDCKVPSQNVYDGTDFRNVCAKTGAQPLCCVAPVAGQALLCQTAVGA
Contributes to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures.
P52754