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2.75k
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5.51k
AlphaFoldDB
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P93471
COP1_PEA
RING-type E3 ubiquitin transferase COP1
Pisum
MEEHSVGPLVPAVVKPEPSKNFSTDTTAAGTFLLVPTMSDLDKDFLCPICMQIIKDAFLTACGHSFCYMCIITHLRNKSDCPCCGHYLTNSNLFPNFLLDKLLKKTSDRQISKTASPVEHFRQAVQKGCEVTMKELDTLLLLLTEKKRKMEQEEAERNMQILLDFLHCLRKQKVDELKEVQTDLQFIKEDIGAVEKHRMDLYRARDRYSVKLRMLDDSGGRKSRHSSMDLNSSGLASSPLNLRGGLSSGSHTKKNDGKSQISSHGHGIQRRDPITGSDSQYINQSGLALVRKKRVHTQFNDLQECYLQKRRQAADKPHGQQERDTNFISREGYSCGLDDFQSVLTTFTRYSRLRVIAEIRHGDIFHSANIVSSIEFDRDDDLFATAGVSRRIKVFDFSAVVNEPTDAHCPVVEMTTRSKLSCLSWNKYAKNQIASSDYEGIVTVWTMTTRKSLMEYEEHEKRAWSVDFSRTDPSMLVSGSDDCKVKVWCTNQEASVLNIDMKANICCVKYNPGSGNYIAVGSADHHIHYYDLRNISRPVHVFTGHKKAVSYVKFLSNDELASASTDSTLRLWDVKQNLPVRTFRGHANEKNFVGLTVRSEYIACGSETNEVFVYHKEISKPLTWHRFGTLDMEDAEDEAGSYFISAVCWKSDRPTILTANSQGTIKVLVLAA
E3 ubiquitin-protein ligase that acts as a repressor of photomorphogenesis and as an activator of etiolation in darkness. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Represses photomorphogenesis in darkness by mediating ubiquitination and subsequent proteasomal degradation of light-induced transcription factors. Light stimuli abrogate the repression of photomorphogenesis, possibly due to its localization to the cytoplasm. Could play a role in switching between skotomorphogenetic and photomorphogenetic pathways.
P93471
C3MG28
FLGH_SINFN
Basal body L-ring protein
Sinorhizobium
MRMQLTAVLAASLLAGCQNQAFREIGQAPSMSPIGSGLQYTQAPQLAAYPKQPHQMTAGYSLWNDQQAALFKDARAINVGDILTVDIQIDDKASFNNETDRSRTNSSGFNLGASGESQTSDFEWSGNLKYGSNIKTEGDGKTERSEKLRLLVAAVVTGVLENGNLLISGSQEVRVNHELRILNVAGIVRPRDVDADNIISYDRIAEARISYGGRGRLMEVQQPPWGQQVVDLVSPI
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
C3MG28
O25655
PYRD_HELPY
Dihydroorotate oxidase
Helicobacter
MLYSLVKKYLFSLDAEDAHEKVCKILRMLSSSPFLCNLIDSQWGYQNPKLENEILGLHFPNPLGLAAGFDKNASMLRALMAFGFGYLEAGTLTNEAQVGNERPRLFRHIEEESLQNAMGFNNYGAILGVRSFKRFAPYKTPIGINLGKNKHIEQAHALEDYKAVLSKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVHELFCMAKEMTHKPLFLKIAPDLETDDMLEIVNSAIGAGAHGIIATNTTIDKSLVFAPKEMGGLSGKCLTKKSREIFKELAKAFFNKSVLVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGPNLCQNILKDLVKLLQKDGFLSVKEAIGADLR
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
O25655
O22056
SIGB_ARATH
RNA polymerase sigma factor sigA
Arabidopsis
MSSCLLPQFKCPPDSFSIHFRTSFCAPKHNKGSVFFQPQCAVSTSPALLTSMLDVAKLRLPSFDTDSDSLISDRQWTYTRPDGPSTEAKYLEALASETLLTSDEAVVVAAAAEAVALARAAVKVAKDATLFKNSNNTNLLTSSTADKRSKWDQFTEKERAGILGHLAVSDNGIVSDKITASASNKESIGDLESEKQEEVELLEEQPSVSLAVRSTRQTERKARRAKGLEKTASGIPSVKTGSSPKKKRLVAQEVDHNDPLRYLRMTTSSSKLLTVREEHELSAGIQDLLKLERLQTELTERSGRQPTFAQWASAAGVDQKSLRQRIHHGTLCKDKMIKSNIRLVISIAKNYQGAGMNLQDLVQEGCRGLVRGAEKFDATKGFKFSTYAHWWIKQAVRKSLSDQSRMIRLPFHMVEATYRVKEARKQLYSETGKHPKNEEIAEATGLSMKRLMAVLLSPKPPRSLDQKIGMNQNLKPSEVIADPEAVTSEDILIKEFMRQDLDKVLDSLGTREKQVIRWRFGMEDGRMKTLQEIGEMMGVSRERVRQIESSAFRKLKNKKRNNHLQQYLVAQS
Required for the transition of plastids into chloroplasts by coordinating nuclear and chloroplastic genomes under light conditions. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Promotes the biosynthesis of plastid-encoded tRNAs (e.g. trnE-UUC and trnV-UAC).
O22056
Q8JZU0
NUD13_MOUSE
Nucleoside diphosphate-linked moiety X motif 13
Mus
MSLYCRTFFRRKSFGCYRLLSTYVTKARYLFELKEDEEACRKAQKTGVFYLFHDLDPLLQASGHRYLVPRLSRAELEGLLGKFGQDSQRIEDSVLVGCSEQQEAWFALDLGLKSASSSRASLPKSEMEAELGGSFIKLRQALFQLNSVDSSLLFTAQALLRWHDGHQFCSKSGQPTQKNVAGSKRVCPSSKIIYYPQMAPVVITLVSDGARCLLARQSSFPKGLYSALAGFCDIGESVEETVHREVAEEVGLEVENIQYSASQHWPFPNSSLMIACHATVKPGHTEIQVNLKELEAAAWFSLDEVTTALRRKGSLALQPSEASPLLLPPKLAIAHHLIKKWVETRSCSSLAA
NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP . Has a marked preference for the reduced pyridine nucleotides . Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-end of some RNAs .
Q8JZU0
Q6X9Z5
RLA2_HORSE
60S acidic ribosomal protein P2
Equus
MRYVASYLLAALGGNTSPSAKDIKKILDSVGIEADDDRLDKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEERKEEKKEESEESDDDMGFGLFD
Plays an important role in the elongation step of protein synthesis.
Q6X9Z5
P68253
1433G_SHEEP
Protein kinase C inhibitor protein 1
Ovis
AAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEITAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGG
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
P68253
Q2RJF1
END4_MOOTA
Endonuclease IV
Moorella
MRLGAHLSIAKGLPRTAAMATSIGANTFQYFTRNPRGGAARQIPGKEIQAWREARRRADLYPIAGHLPYTVNLGAAAERQQEFTRMVLHDDTLRVAAIDGEYLISHPGHYEGERQAGLDRIIQLIEEAYLSITPPGPMLLLETMAGQGKEVGTIDDLCYILEGLGWPDRVGVCLDSAHLFAAGWDLRTPAGCQQLVQELAAKIGLDRVKAMHLNDSAAPLGSHRDRHAGIGKGELGREGIAAVVNDPFLGELPLFLETPVANYEEYGEEIALIQKLKSV
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Q2RJF1
A6LD62
RNY_PARD8
Ribonuclease Y
Parabacteroides
MVGMYIIIPIVTFIIGGLLAWLGMRFLLKSKYDSVLQEAEKEAEVIKKNKMLEVKEKFLHLKADLEKQVSQRNAKIQSVETKLKQRELTMNQRQEELQRRNNEVEAVKENLSSQLELVEKKKQDLDKLHQKEVEHLEAISGLSAEEAKERLIESLKDEAKTQAASYINEIVEEAKMTANKEAKKIVIQSIQRVATETAIENSITVFHIESDEIKGRIIGREGRNIRALEAATGIEIVVDDTPEAIVLSGFDPVRREIARLALHQLVQDGRIHPARIEEVVTKVKKQVEDEVVETGKRTVIDLGVHGLHPELIRMIGKMKYRSSYGQNLLQHARETANLCAVMASELGLNPKKAKRAGLLHDIGKVPDDEPELPHAILGMKLCEKYKEKPDICNAVGAHHDEVEMQTLLAPIVQVCDAISGARPGARREIVEAYIKRLNDLEQLALSYPGVVKTYAIQAGRELRVIVGADKIDDKDTENLSAEIAKKIQDEMTYPGQVKITVIRETRAVSYAK
Endoribonuclease that initiates mRNA decay.
A6LD62
A4YW84
FABH_BRASO
3-oxoacyl-[acyl-carrier-protein] synthase III
unclassified Bradyrhizobium
MTIRSVVLGCGSYLPQRVVTNAELASRIETSDEWIVQRTGIRERHVAADGEFTSHLAINAARAALANADVDPQSIDLIVLGTSTPDNTFPATAVAVQNGLGIHHGAAFDLQAVCSGFVYALATADNFLRSGSFKRALVIGAETFSRILDWNDRTTCVLFGDGAGALVLDAQQQGGTAADRGVLSTHLRSDGRHKAKLYVDGGPSSTQTVGHLRMEGREVFKHAVGMITDVIVDAFEATGLSAETIDWFVPHQANKRIIDASAHKLHIAPEKVVLTVDRHGNTSAASIPLALDVAVKDGRIKKGDVVLLEAMGGGFTWGSALVRW
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
A4YW84
Q74IQ5
RIMM_LACJO
Ribosome maturation factor RimM
Lactobacillus
MTEYFEVGKILSPHGLKGEVKVNATTDFPEERLATGSRLFIKNNKQYEELIVENTRRHKQFYLVKFEKIDDIDQAEKICSKELYVAETDQQELPEGSYYFKDILNCPVYDAETGEKLGVLENIETPGANDIWEIKPEKGKSFWIPNIESVVKKVDLANKRIEVTLLEGLRDEN
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Q74IQ5
Q3SSV1
RL6_NITWN
50S ribosomal protein L6
Nitrobacter
MSRIGKRPVTVPSGVTATVEGQTVKMKGPKGELRFVVHDDVEVKLEDGAVKVAPRYETKRAQALYGTARAQVANLVAGVTKGFEKKLEIIGVGYRAALQGKSLQLALGYSHDVNYAVPEGITIAVPKPTEITITGNDAQRVGQVAAEIRGYRPPEPYKGKGVKYADETIFRKEGKKK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Q3SSV1
A6Q4I1
SYI_NITSB
Isoleucyl-tRNA synthetase
unclassified Nitratiruptor
MDYKETLLLPKTTFPMRGNLPQNEPKRFAKWFEKDVYEKMKKSREGKELFTLHDGPPYANGHIHIGHALNKILKDIIVKFNYFEGKAVRFTPGWDCHGLPIEQQVEKKLGTAKKEQLPKTKIRELCREHAAKFVGIQKEEFKNLGVIADWEKPYLTMDYAFEADIYRALCEIAKEGLLVERSKPVYWSWAAKTALAEAEVEYEDKVSPSIYVAFKLDKEAVQKIGKEASIIIWTTTPWTLPANTGIALNPDIEYVLTSDGYVVAADLLDELKEKGIVKGDVEKSISPKDLENLHAINPLNGRRSRIVLGEHVTTESGTGAVHTAPGHGEDDYRVGLKYDLEVLMPVDDAGRYDETIVREKLLPEEFVGMNVFEANDKICELLGDALLKKEDIKHSYPHCWRTHKPIIFRATKQWFIAVDKAPKDLQKTLRQIALEEVEKTTFYPEWGRNRLKSMIENRPDWCISRQRDWGVPIAFFRNKKTGEVIYDEKVLNYIAMIFERMGTDAWYSLSVEELLYPGSGYDPNDLEKVMDILDVWFDSGSTWYAVLKSRRYDAGNYPADLYLEGSDQHRGWFQSSLLVSGAIEKRAPFKAILTHGFTVDEKGEKMSKSKGNVVAPMDVAKKYGVEILRLWVAMSDYQSDLKISDNILKQIAEQYRKLRNTFRFMLANINDLETIQSDFGVLDRWILAKAKSVFEEVEKQFKNYQFAKGFSALNNFIVNEFSGIYLDVCKDRLYCDALNDSHRRASQSAMALIAKSMLGLIAPVLTYTADEIVEHAPSVLRNDAEDIFDFAIEPLPEIQSDFDEVYMIEARSKFNEIVDQLKKKKIIKSSLELVIETTSSKVLALDATEREDWFIVSGVEEEIGSKELGDFKVEGDQFIIKEAILHKCPRCWKYKAKEEGALCERCQKVVDGLEQAGS
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
A6Q4I1
Q65TN4
QUEF_MANSM
PreQ(0) reductase
Basfia
MDYKDNSLKTLKLGQKTDYIANYDRTLLQPVPRALNRDGLGITKQQPFSVGADIWTAYEISWLNIKGLPQVAIADVEIDYRSTNLIESKSFKLYLNSFNQTKFSDMSEVQRTISEDLSICAEGNVRVQLHSLSNYSHERIADFAGECLDELDIEISDYGFNAEILQNCTALSTEIVEETLVSHLLKSNCLITSQPDWGSVQIHYQGKRIDHEKLLRYLVSFRQHNEFHEQCVERIYCDIMKYARPEKLTVYARYTRRGGLDINPFRSNFEAIPQNLRLARQ
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Q65TN4
Q9SII6
PIX13_ARATH
Probable serine/threonine-protein kinase PIX13
Arabidopsis
MGLCWGSPSDSPPTTTPSSTGNISSVGTFKSSNNTTTTGTSRGSNISSNSGFSVASGEDAYPDGQILPIPNLRIFSLAELRASTRNFRSENVLGEGGFGKVFKGWLEDKTPGKQSNGTVIAVKKLNAESFQGFEEWQCEVNFLGRVSHPNLVKLLGYCLEGEELLLVYEYMQKGSLENHLFRKGSAVQPLSWEIRLKIAIGAAKGLAFLHASEKQVIYRDFKASNILLDGSYNAKISDFGLAKLGPSASQSHITTRVMGTHGYAAPEYVATGHLYVKSDVYGFGVVLAEILTGLHALDPTRPTGQHNLTEWIKPHLSERRKLRSIMDPRLEGKYPFKSAFRVAQLALKCLGPEPKNRPSMKEVVESLELIEAANEKPLERRTTRASPSIRQQQGHYRPQQLSSFRPRQNVSRAH
May be involved in plant defense signaling.
Q9SII6
A4QKE4
RK22_BARVE
50S ribosomal protein L22, chloroplastic
Barbarea
MIKNRKKKSYTSVYALGQYISMSAHKARRVIDQIRGRSYEEALMILELMPYRGCYPIFKLVYSAAANASHNKGFKETNLVISKAEVNQGNTVKKLKPRARGRSYPIKRSTCHITIVLEDISFYQQYEEYFMYLKKPGCSNENRNLTCYDTYSSGGLWDKK
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.
A4QKE4
Q5SIY0
ILVD_THET8
Dihydroxy-acid dehydratase
Thermus
MRSDQIKKGLKQAPARAMLRAVGVGDEDFGRPFVGVVNTFTDGMPCNFHLRELAQHLKAGLKEAGLFPFEFGAPAISDGISMGTPGMRASLVSREVIADSVELIAQGYLYDGMVGLSACDKTIPGTAMGVIRSGVPGMILYGGTIAPGEWQGRKLTIVEVFEAVGQRAAGKISEEELLEIERRAIPGPGACGGQYTANTMAMALEALGLSPVGYNAIPAVHPEKERATKEAGKILAWAIAHDWKPKDFLTRKSFLNAIAAVAATGGSTNAVLHLLALAKEAGVELSLDDFDQISRKTPVIADLRPWGTYTAWELYEAGGTALVFKRLLEAGLLFGEEKTLTGRTLAEEVERAYREQEGQKVVFPVEKALKPHGGLVVLKGNLAPKGAVLKLAGTERTYFEGPARVFDSEEAAMEKVLKGEIRPGDVVVIRYVGPKGAPGMPEMLSVTSAIVGEGLGPEVALLTDGRFSGGTRGLMIGHIAPEAFVGGPIALLEEGDRIRIDVEGRRLEVLLPEEELERRRARWRPRPPAFTHGLFARYAALVRQADEGAVLEDPL
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Q5SIY0
A5TY85
PKNA_MYCTA
Serine/threonine-protein kinase PknA
Mycobacterium tuberculosis complex
MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTFSSGQRALLWAAGVLGALAIIIAVLLVIKAPGDNSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTPHSRASLARYEIAQ
Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ and MurD. Shows a strong preference for Thr versus Ser as the phosphoacceptor.
A5TY85
B8CVU6
ATPG_SHEPW
F-ATPase gamma subunit
Shewanella
MANAKEIKTKIASVQNTQKITSAMEMVAASKMRKAQDRMASSRPYAENMRKVIGHVAQGSLEYKHPYLEVREAKRVGYIVVSTDRGLCGGLNVNLFKKVVADVKKQREAGAEVEFCPIGARSVQFFNSFGGQVSAHASGLGDAPSLTDLIGTVRVMLEAYNEGKLDRLYVVFNKFVNTMTQTPVIEQLLPLPKSEEDEISHHWDYLYEPDPKELLDTLLVRYVESQVYQGVVENIASEQAARMVAMKAATDNAGELISDLELVYNKARQAAITQELSEIVSGAAAV
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.
B8CVU6
P49425
MANA_RHOM4
Endo-(1,4)-beta-mannanase
Rhodothermus
MTLLLVWLIFTGVAGEIRLEAEDGELLGVAVDSTLTGYSGRGYVTGFDAPEDSVRFSFEAPRGVYRVVFGVSFSSRFASYALRVDDWHQTGSLIKRGGGFFEASIGEIWLDEGAHTMAFQLMNGALDYVRLEPVSYGPPARPPAQLSDSQATASAQALFAFLLSEYGRHILAGQQQNPYRRDFDAINYVRNVTGKEPALVSFDLIDYSPTREAHGVVHYQTPEDWIAWAGRDGIVSLMWHWNAPTDLIEDPSQDCYWWYGFYTRCTTFDVAAALADTSSERYRLLLRDIDVIAAQLQKFQQADIPVLWRPLHEAAGGWFWWGAKGPEPFKQLWRLLYERLVHHHGLHNLIWVYTHEPGAAEWYPGDAYVDIVGRDVYADDPDALMRSDWNELQTLFGGRKLVALTETGTLPDVEVITDYGIWWSWFSIWTDPFLRDVDPDRLTRVYHSERVLTRDELPDWRSYVLHATTVQPAGDLALAVYPNPGAGRLHVEVGLPVAAPVVVEVFNLLGQRVFQYQAGMQPAGLWRRAFELALAPGVYLVQVRAGNLVARRRWVSVR
Acts as endo-acting enzyme with a requirement for at least five sugar moieties for effective catalytic activity. Hydrolyzes carob-galactomannan (locust bean gum) effectively and to a smaller extent guar gum, but not yeast mannan.
P49425
Q96M95
CCD42_HUMAN
Coiled-coil domain-containing protein 42
Homo
MSLGIMEEEDLAEYFRLQYGERLLQMLQKLPNVEGASESPSIWLLEKKKETEIMHQTMVQKKKMFQRRMETLNLRWEELGVKEAQLKAHIQKSEQFIQENDQKRIRAMKKANKERELKCQHMQELTKRKQEMVALRLEHQRLSAKLKDYYIFNKYLEKVVENSEFEEIHEVIARYKTLVSMRHDLMQSAQEGQEKIERAKARLARYMEEKDDEILQQNNELARLQMRFDRARSNVIFWESRWAHIQNTAAKKTLLLGTIKMATLNLFQIVSKHLKEVTEVALEDTHKQLDMIQQFIQDRSDIWAEVKKKEQQRVRI
Required for sperm development.
Q96M95
Q09LL3
BBD_ORYMI
Bifunctional nuclease
Oryza
MEIINGPVLPRYAAPATGALTSDAKISGQLLRRVHLRRRACGLQGDHYRAARRFFGFPSERHARSGWVWPVYCSYGSSSDGDGAAAADYDASGEEFVNSSVMEAVELRSVSDGFVIKMRDGKNLRCVQNNPRVLRLRDSAPHHAIVLKMEDGSDLLLPIIVMETPSIMLLAALRNIRIPRPTIYNVVKEMTERMGYAVRLVRITEMVHDAYYSRLYLAKIGNEEETISLDLKPSDAINIAFRCKVPIQVNRRIAYNNGLKVVQPTPSESYVSSDQFQYTRLDRPDDQPCFEAQEFDLVRNMLVAAVEERYKDAAQYRDQLFMFRAKKKNMI
Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid-derived callose deposition following infection by a necrotrophic pathogen.
Q09LL3
Q92GL2
COAE_RICCN
Dephosphocoenzyme A kinase
spotted fever group
MLAIGITGSYASGKTFMLDYLTEKGYKTFCADRCIKELYQDVVLQTQILKLLPELESFNIRKISNLIYNNDLAREKLQNFIYPLLIDKLILFKKENANSKFGFAEIPLLYEAKFEKYFDFVVTIYCSEAIRMQRAITRSSFDIEIYNKIKEIQLSQESKIAKADFAINSGVDMLDLEKQIAKLIKDLECRV
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Q92GL2
Q1DC68
NFI_MYXXD
Deoxyribonuclease V
Myxococcus
MCMALQPEVSRWDVTPSEAVELQRRLREQLVLRPPPGLKVERIAGADISTEKGKDTGFGGFVVLDVETLAPVAQSEAVVTLHFPYVPGLLSFRELPTIAAAWERLTVRPDVVIFDGQGTAHPRRMGIACHGGLLFGVPSIGCAKSLLVGTHGPLGEARGSTAPLMHRGEVVGMAVRTRKGVQPVYVSPGHLMDLPTAVEWVLKVSPKYREPETTRHAHRLVNALRRADGEAAELE
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Q1DC68
O67353
PYRG_AQUAE
UTP--ammonia ligase
Aquifex
MAKYIFITGGVLSSLGKGITSASIASILEEMGYRVTLQKLDPYLNVDAGTMSPYQHGEVYVTEDGAETDLDLGHYERFTNAVMTRDNNVTAGRIYYNVISKERKGDYLGATVQVIPHITEEIKESIKRVEKDNDIVIVEIGGTVGDIEGLPFLEAVRQLSLELGRKNSMFIHLTYVPYIKAAGELKTKPTQHSVKELRAIGIQPDMIICRADRELPKGIKSKIALFTNVKEEAVISAPDLEFSYEVPLKLKEQGIDRIITERLNLEHREVNLGKWKKIVNVLRNPEEEVNVALVGKYVELKDSYKSVIEALIHGGIANKVKVNVILKNSEQLDISELQEDIHGIMVPGGFGERGIRGKIEALNFGRENNIPTFGICLGMQLMAIEFARNVLGFSNANSTEFDPDTPFPVIDIMEEQKKVDKLGGTMRLGAYPCKVKENTLAHRIYQKDLIYERHRHRYEFNNRYRKDFESKGVVFSGTSPDDKLVEIMELKNHMWYLGCQFHPEFKSKPFAPHPLFRDFIRACLEYKRKFT
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
O67353
Q9KPG9
FTSQ_VIBCH
Cell division protein FtsQ
Vibrio
MINKVLLEGQRITRSPQVKQHACGASFFLVVLLLIGGLLYSTISWMWDEQRLPLSKLVLQGDLHYVSALDVQRVLARLDHIGTFMSQDINVLQESVQSIPWVSHASIRKQWPDTIKVYLTEYQVEALWNANALLDKNGTVFYGDIARVNGEYVKLYGPDGTAPQVLKAWRDYNPKFAQLGLNISSLVLNDRRAWQIILDNGIRLELGKESLEERISRFFLLYKQLGNKAEQVSYIDLRYDTGAAVGWFPEQELTQEKNDD
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Q9KPG9
Q9ST43
PH1_ARATH
Pleckstrin homology domain-containing protein 1
Arabidopsis
MESIWRIATGQDPSREDYEGIEFWSNPERSGWLTKQGDYIKTWRRRWFVLKRGKLLWFKDQAAAGIRGSTPRGVISVGDCLTVKGAEDVVNKPFAFELSSGSYTMFFIADNEKEKEEWINSIGRSIVQHSRSVTDSEVLDYDHRR
Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides.
Q9ST43
B5VS52
SEY1_YEAS6
Synthetic enhancer of YOP1 protein
Saccharomyces
MADRSAIQLIDEEKEFHQSALQYFQQCIGNRDVGLDYHVISVFGSQSSGKSTLLNVLFNTNFDTMDAQVKRQQTTKGIWLAHTKQVNTTIEIDNDRPDIFVLDVEGSDGSERGEDQDFERKAALFAIAVSEVLIVNMWEQQIGLYQGNNMALLKTVFEVNLSLFGKNDNDHKVLLLFVIRDHVGVTPLSSLSDSVTRELEKIWTELSKPAGCEGSSLYDYFDLKFVGLAHKLLQEDKFTQDVKKLGDSFVMKGTENYYFKPQYHHRLPLDGWTMYAENCWDQIERNKDLDLPTQQILVARFKTEEISNEALEEFISKYDESIAPLKGNLGSLTSQLVKLKEECLTKYDEQASRYARNVYMEKREALNTKLNSHISGTINEFLESLMEKLWDDLKLEVSSRDKATTSFVESVAAGKSKIEKEFNESMETFKKLGLLISNEEITCKFSDDIEERIKQLRDAELKAKIGRIKKNLVPELKDHVIHLLSHPSKKVWDDIMNDFESTIKDNISAYQVEKDKYDFKIGLSESENAKIYKNIRILAWRTLDTTVHDYLKIDTIVSILRDRFEDVFRYDAEGSPRLWKTEEEIDGAFRVAKEHALEVFEVLSLAVTSDNVEIIPDVPMAEEESGEDNEIYRDNEGVFHSRRFAHILTELQKENVLDQFRRQINITVLDSKRSIITTRTHIPPWIYVLLAVLGWNEFVAVIRNPLFVTLTLILGATFFVIHKFGLWGPVVNVVQSAVGETRTAIKDKLRQFVVEDHEVKESFEMKDFSKNEQKEK
Cooperates with the reticulon proteins RTN1 and RTN2 and the tubule-shaping DP1 family protein YOP1 to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
B5VS52
A8YXI3
ALR_LACH4
Alanine racemase
Lactobacillus
MVPGYYRPAVVKVNLGAIRRNIKNEMQHLEPNQKMLAVVKANGYGHGAVEVAKVAEEEGAAGFCVAILDEALELRRADIVKPILVLGVVSPEYAPIAAVNNVSLTVPNLEWLKDAEKYLAKENLQLKIHLGIDSGMGRIGFNEDDEFVAANKFLENNNNFFIEGMFAHFASADSDDETYFKHQCEKFKHMKSLLTVKPKWIHVDNTAASIFHSGIKSDLVRFGIGIYGLNPSSNPSSPDLTSAIELEPALSFESELTHVKTIHKGDGVGYGSTFMAEEDTIIGTVPVGYADGWIRKYQGFKVKVGDEYCSIVGRICMDQFMVKMPKKMLVGTKVVIISNNPSDPNNIKAAADYVDTIHYEVACLLNDRLPRVYYEK
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
A8YXI3
O23731
CHS8_BROFI
Naringenin-chalcone synthase 8
Bromheadia
MAPAMEEIRQAQRAEGPAAVLAIGTSTPPNALYQADYPDYYFRITKSEHLTELKEKFKRMCDKSMIKKRYMYLTEEILKENPNICAFMAPSLDARQDIVVTEVPKLAKEAAARAIKEWGHPKSRITHLIFCTTSGIDMPGADYQLTRLLGLRPSVNRFMLYQQGCFAGGTVLRLAKDLAENNAGARVLVVCSEITAVTFRGPSESHLDSLVGQALFGDGAAAIIVGSDPDSATERPLFQLVSASQTILPESEGAIDGHLREIGLTFHLLKDVPGLISKNIQKCLLDAFKPLGVHDWNSIFWIAHPGGPAILDQVEIKLGLKAEKLAASRNVLAEYGNMSSACVLFILDEMRRRSAEAGQATTGEGLEWGVLFGFGPGLTVETIVLRSVPIAGAE
The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
O23731
A8AGR7
SOTB_CITK8
Probable sugar efflux transporter
Citrobacter
MTTNTVSRKVAWLRVVTLAIAAFIFNTTEFVPVGLLSDIARSFAMPTAQVGIMLTIYAWVVALMSLPFMLLTSQVERRKLLICLFVLFIASHVLSFLAWNFTVLVISRIGIAFAHAVFWSITASLAIRLAPPGKRAQALSLIATGTALAMVLGLPIGRIVGQYFGWRTTFFAIGIGALITLVCLIKLLPKLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQTVAGLSANFATVLLLILGGAGIIGSVVFGKLGNQYASPLISIAIMLLVICLMLLLPAADSESHLAVLSIFWGIAIMVIGLGMQVKVLALAPDATDVAMALFSGIFNIGIGAGALVGNQVSLHWSMSTIGYVGAVPALAALVWSIIIFRRWPVSLEEQPQH
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
A8AGR7
P33775
PMT1_YEAST
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Saccharomyces
MSEEKTYKRVEQDDPVPELDIKQGPVRPFIVTDPSAELASLRTMVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIGDSFPSTTPYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPANSLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIHFQSLTLDGDGASFFSPEFRSTLKNNKIPQNVVADVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRLHSHDHKPPVSESSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHDLTLWYVENNSNPLLPEDTKRISYKPASFISKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRNVYLLGNAIVWWAVTAFIGIFGLIVITELFSWQLGKPILKDSKVVNFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGWDYNCNTYFSSLEEYKNQTLTKRESQPAATSTVEEITIEGDGPSYEDLMNEDGKKIFKDTEGNELDPEVVKKMLEEEGANILKVEKRAVLE
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.
P33775
A9WAN7
MINE_CHLAA
Cell division topological specificity factor
Chloroflexus
MSFLNGLFGRKRDSSAELAKQRLLTVLIDDRYKLTPEMMAQMKADLAEVLKRYLPAIDAEQIEVTLSRGEAHDLLKADVPLRRATDHPPNR
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
A9WAN7
Q49939
PAPA5_MYCLE
Polyketide synthase-associated protein A5
Mycobacterium
MFAGSVIRKLSHSEEVFARYEVFTSMTIQLRGVLDIDALSEAFDALVQAHPVLASHLETSSDGGWNLVADDLLHPGICVVDANNGAQSGCGGIQSETRLDQSVSLLNLRLTPREGGGELVLYIHHSMADGHHGAVLVDELFSRYTDVVTTGDPGPIIPQATPLSMEAVLQQRGVKKHALSGAERFMSVMYAYDLPATGTPAVLAEPGLPQAVPVTRLWLTKQETSDLAAFGREHRLSINAVVAAAILMTEWRLRETPHVPIPYVYPVDLRYVLAPPVAPTESTNLLGAAGYLAEIGQDTDIVDLATDIVATLRADLANGVVQQSGLHFGTAFEGTPPGLPPLVFCTDATAFPTMRTPPDLAIEDIQGRFYCSISVPLDLYSCGVYEGQLIIEHHGHIEEPAKALEAIRSLLCTVPSEYGWIME
Catalyzes diesterification of phthiocerol, phthiodiolone, and phenolphthiocerol with mycocerosic acids, the final step in the phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters (PDIM) synthesis. Can directly transfer the mycocerosate bound to the mycocerosic acid synthase (mas) onto the substrate alcohols.
Q49939
P47533
P69_MYCGE
ABC transport system permease protein p69
Mycoplasma
MITKLFFHQVGDNKKRLIWYWKLLIIIAVLAIVIYSWIDNFSSFNQFGLNVFINNITSLFTPNLNHEYTLVRFLAQTAFFVTGGSFLGFIFAILFSYWTAFKIQPFYIALPIRLITIVLRAFPVLLFGFLFSNLFNKQLAATLTISWFSFLWNTKYITTFFENSNLKYFFNKKIREGSGFKAFWTTIFLSENERLWLFFLYSLEANFRWTTLLSIFGIGGIGQLIVDPLSIRVQFDLVLIPLVVLITFLIFIEVVVFLLSSFVFEKNSEDLRPILKTTVIEKRKWKRIIFILFIVVLISLSLANLVTIDYRINDAEFLQDFFNQFFQLKSNLFSSNDPNINPILMLVKLTTQAISLISLVVIFSILFGFISCNLFKKRFSISFKILLLFVRVVPSILLFRLLDPLFLEAKTTIILVLLINHGSSYGQLMSINFNKANQNIINNYKNHGMTKGFILWNYLLVENKPNLINITSDAYDSVIRDLILFGSFGGSIIGSRITNFFERAQFDNLGSVTIPLMVYLIAIEIIFLSVRLTRISVFKNYLY
Probably part of a high-affinity transport system.
P47533
B9MS73
ATPL_CALBD
Lipid-binding protein
Caldicellulosiruptor
MTALAAGIAMLAGLGVGIGIGIATGKASESIGRQPEAFGRIFPLFLIGAALAEAVAIYSLVIAFMLISKI
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
B9MS73
B4SW31
PPNP_SALNS
Xanthosine phosphorylase
Salmonella
MLQSNEYFSGKVKSIGFTSSSIGRASVGVMAEGEYTFGTAEPEEMTVVSGALKVLLPGTVEWKVYTAGEVFNVPGHSEFHLQVAEPTSYLCRYL
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.
B4SW31
P9WJ40
VPB24_MYCTO
Putative antitoxin VapB24
Mycobacterium tuberculosis complex
MIRTQVQLPDELYRDAKRVAHEHEMTLAEVVRRGLEHMVRIYPRRDAASDTWQPPTPRRLGPFRASEETWRELANEA
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC24 (Potential).
P9WJ40
Q90W58
DUS1B_XENLA
XCL100-beta
Xenopus
MVNMEICAMDCCVFKGLLAERAHKCLILDCRSFFAFSSSSIIGSSNVRLSTIVKRRAKGSMGLEHIIPNEEQRGRLVAGMYEAVVLLDERTSELDMLRKDSTMMLAVNALSRDPRGSRIYFLKGGYETFSSQCPEFCNKNSPPVALSLPLSPNNVPGSADSNCTPCGTPLYDQGGPVEILPFLYLGSAYHASRKDMLEALGITALINVSANCPNHFEGHFQYKSIPVEDSHKADISSWFNEAIDFIDSIKTCGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPSCSAEAGSPTISVLDRGTSTTTVFNFPVSIPVHSGANSLSYLQNPITTSPSC
Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity during the meiotic cell cycle.
Q90W58
B0WAU6
LIAS_CULQU
Lipoic acid synthase
Culex
MKYFFSLPFPKVHTTCKHTAAATASQPLQKIRERLESGPGFQEFVQNPSYNREDWSAYEGKLKREKGEQDRLRLPPWLKTKIPMGKNFSRIKDQLRELKLATVCEEAKCPNIGECWGGGEHGTQTATIMLMGDTCTRGCRFCSVKTARAPPPLDPDEPKKTASAIASWGLDYIVLTSVDRDDLPDGGSNHIAETIREIKRQNPRIFVECLAPDFRGNLDCIRTVATSGLDVYAHNIETVESLTPFVRDRRAEYRQSLKCLASVKEINPNMVTKTSIMLGLGETDEQVEQTMKDLRAVGVDCLTLGQYMQPTKRHLKVIEYVTPEKFKHWETRGNELGFLYTASGPLVRSSYKAGEFFITSILKNRAAAAAEEATATKPSE
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
B0WAU6
B7VGI4
DNAA_VIBA3
Chromosomal replication initiator protein DnaA
Vibrio
MSSSLWLQCLQQLQEELPATEFSMWVRPLQAELNGNTLTLFAPNRFVLDWVRDKYLNSINRLLQEYCGNDIPHLHFEIGNKRVTAPKSETIAPARTRTAADVAAESSAPAQLQARKPVHNIWRDEEPVAVDLNHRSNVNPKHKFNNFVEGKSNQLGLAAARQVSDNPGTAYNPLFLYGGTGLGKTHLLHAVGNAIVDNKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKAEDHQIHLADEVAFFIAKRLRSNVRELEGALNRVIANANFTGRPITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQLAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIAQLREESHDIKEDYSNLIRTLSS
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
B7VGI4
P20247
HBB2_TORMA
Hemoglobin beta-2 chain
Torpedo
VSLTDEEKHLIQHIWSNVNVVEITAKALERVFYVYPWTTRLFTSFNHNFKASDKGVHDHAVNVSKALSAAIGDLHNVNKNFSALSTKHQKKLGVDTSNFMLLGQAFLVELAAFEKDKFTPQYHKAALKLFEVVTEALSCQYH
Involved in oxygen transport from the lung to the various peripheral tissues.
P20247
Q6A6A0
NANE_CUTAK
ManNAc-6-P epimerase
Cutibacterium
MSGFTDRIIASMAGGLVVSCQAYPGEPLRHPETMAQMAAAVEAGGAVAVRAQGLSDVSAVKGRVSVPVVGIWKEGDEGIYITPTLRHARCVSAAGADVVALDGTRRERADGLSLAETIERLKREYDVVVMADCGSVDDGLFAAEAGADLIGTTLCGYTGERPKTDGPDYEVIEALVKKLDGDRPVIAEGRIHTPDQARRAMDLGAHAVVVGTAITHPTSITGWFRDALR
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Q6A6A0
B9JXN7
PDXJ_AGRVS
Pyridoxine 5'-phosphate synthase
Agrobacterium
MPAKLSVNLNAIAMLRNRRDLPWPDVRHFGRLALQAGAQGLTVHPRPDQRHVRFSDLPLLRALIDDEFPKAEFNIEGYPSEDFLQLCEEAQPEQVTLVPDDPSQATSDHGWDFAAHQVFLTDVVARLKAAGMRVSLFADGDGNAQAVATAKATGADRIELYTGPYGSCYDAPEKAARELALLGATADAAHALGMGVNGGHDLTIANLPALAERIPFLAEVSIGHALTADALEFGMAETVRRFRRACGELA
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
B9JXN7
A0A5C1RD96
ASC5_DIDFA
Ascochitine biosynthesis cluster protein 5
Ascochyta
MPHRLPSHGASLGLIFGPQAMNFDSNTFTTLRAKLVKDRHSQWAIDAIAALPAEWSAVSGNVAIFKQYDAGKALQNLNEWLKTGHVPPADIPFCNVLLAPMVVIDHVISYLEFLQSAFPDLDDDEELPASAKESLETLGLSLGTLSAFAVSSSSTLSEVKKHGATAIRLAMLVGAVGDAEDLAREPEEGALSFSAFWKSTELHDLLHTSLDAIPEAYISVAVDEKRSTITTSRSKASSHMQDLRSSGLYIAEVSIRGRFHWDGHESTLQELIQYCDRNLQFQFPDTSRIVLPSHSVTGGEYITQEDGSLHAIALRAILVDLSQWLETITGAYGSESSKGIKSVVCFGPERCVPSALVRRLGSKLTHVLDVDLPTSALPKQLLQSADVSSTNGVKIPASIKGQSPARQHPIDIDANDDKIAVIGMACNVPGGEDMDEFWKILVAGKSQHEELPRGTGRFEFETPWREPYTKTKWYGNFIKDYDVFDHKFFKKGPREMLNTEPQHRLLLHAAYQTLEQSGYFSKPDYDKHIACFLGPGHVDYASSVNCYAPNAYTATGNLKSMCAGKISHHFGWTGPILTLDTACSSSCVAIHYACRSILSGEVSAALAGGSNVLSSVEWYENLSGAQFLSPTGQCKPFDAKADGYCRGDGIGLVFLKKLSTALADGDQVYGVIAGSKVYQNVGSTTITVPNADSLATLFKDITKQARIDPAKVSVVEAHGTGTPVGDPAEYEAICRIFGGSQRTDVLSLSSVKGLFGHTEGASGVCSLLKVLLMMHENAIPPQASFGSMNPGLKATTQDNIEVPTRLTPWKPNTQIALINNYGASGSNSSLVVTEPPAFETFDHEALQYRAFPFWIPGLDDKSIQRYATRLRAWFQRHHSSSKDLSMRNMSFQLAFQSNRTLPQALVFKAASVSDLESKLKAFENGTLNSISSAATSQRPVILCFGGQISTYIGLDREVYENVAVLRQFLDQCDETSVSLGFPSVFPHIFQKEPIYDLIKLQLALFAMQYSCAQAWIACGVEVAAVVGHSFGELTASCVSGTVSLQDAITMIAGRARLIQKKWGTDSGAMIAVDTELSGVNDLLAKTREGSGADDNPSIACYNGHRSFTLAGTTKSIEQAESILKQDATFSSTRWKRLNVTNAFHSVLVDSLHHDLQSLGKRIVFNEPKLHFERSTKERMSGKPNSDYIAHHMRNPVYFDHAVQRLAKDFPAAIWLEAGSNSTITSMANRALSSSAASSTSSFHAVSITTDKSFDLLVDSTLKLWKEQLNVSFWAHHRSQTHQYTPMILPPYQFEKSRHWLETKPPPKPEPIPVEKSTTQAVETSKGFTSFAGYIDGNQRSLRYRINSNHETFQRHVNGHICAKLAAVWPSSIQIDMVLDALMNLRAEFKDLSYQPQISNIVHHRPLLLDNSKDYWLELVAKDDKGLTWDWNFSSSSGLGSKSTICTSGVCSFCSATDPNRLAEFQTLERLSSRRRCVELLEARDVENIMQGTANIYRAFSEVIEYTDDYRYVKKLVGHNNESAARVVKKHYGKTWLDYLLFDGLGQTAGMYVNLMADKANVSEKGIFMCETINRWLRSPTIRSHESLPTDWEVYAVHHPISDKKYVSDIFSFDARDGSLVEVVLGASYNKVPLPVMRGILGSQSSTTRLDAITANAEIPSQAGIGSQQPHLNFKPLSALPALSNGTTGTENPQIKSKTNKVKKVPTRKSGGSDLETPAKTRNILENLTGVEASSINDDSNLIDLGLDSLLSMELIRDVEDIFKVDLDAEQMLDLTDFASLVKYIREIRGVLEEQNVDDSESESEELQQQATPIDSATRQNHEKLTMNGTGLLTNGESVPEVPLDSTLVLDAFRYIKEASDDFIVKNKFETYCAEFMPRSEEVSIAIFCNAFEELGCPIRTATAGTRLERVQHLPKHKKVVDYIYKALEKNAGLIEISGEEIIRTSVPCPSEQTEAMLESLLHDRPAQDAEIQLMRITGAAFGKCLAGKADVLPLLFGSIEGRALLTKLYATSTLSNTILQQLEVFVEKIGSSWPKDGGPLRILEVGAGTGGTTTKIVPVLARLGIPVEYTMTDVSSFFTATGRTKFKEYPFMKFKTVDIEKEPDAKLLKTQHIVLGSNVIHATRVLSVSLSNIHKMLRPDGLIIYHELTSQLLWADIIFGLVEGWWLFEDGRDHALQSPQHWEKILRSVGYGHVDWTDGTRPEAKIQNLIFAMASDPTYDREPLPTASIMTDVADQVATVNAYVCQYSSNFQFRRNSASRATGLSSGRCVLITGATGSLGAHLVAYCAERLDVSKVICFNRTSQTAGVARQAKAFKSKGISLEVNTNPKLEVIETDASKDQLGLSPSEYAALVDSVTDIVHNAWPMSINRGVRSYEGQFRVMRNLVDLARDATMQRPEPFKFGFQFISSIGVVGMYPLLTNNFLVPEHRMPVESVVPSGYGYAKLVCERMLDETLHLYPQAFHPSAVRINQIAGSTRSGYWNRNEHLVFLIKSSQTLNALPDLQGHLTWCPVDTVAATLGELLLDNANSVASAHPIYHIENPSRQSYSEMIRVLADSLFIDHANIIPFYDWVQRVRDFEGPVTENPAKQVVDFFDEHFLRMSCGDLVLDTVKSREISATLRARGVITSDLVNKYVEAWRRAGVLR
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the selective antifungal agent ascochitine, an o-quinone methide that plays a possible protective role against other microbial competitors in nature and is considered to be important for pathogenicity of legume-associated Didymella species . The pathway probably begins with the synthesis of a keto-aldehyde intermediate by the ascochitine non-reducing polyketide synthase pksAC from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (Probable). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (Probable). The HR-PKS (orf7) probably makes a diketide starter unit which is passed to the non-reducing polyketide synthase pksAC for further extension, producing ascochital and ascochitine (Probable). The aldehyde dehydrogenase (orf1), the 2-oxoglutarate-dependent dioxygenase (orf3) and the dehydrogenase (orf9) are probably involved in subsequent oxidations of methyl groups to the carboxylic acid of the heterocyclic ring (Probable). The ascochitine gene cluster also includes a gene encoding a short peptide (orf2) that is often found in secondary metabolite gene clusters and which function has still to be determined (Probable).
A0A5C1RD96
Q65DY4
FDHD_BACLD
Sulfur carrier protein FdhD
Bacillus
MGKNITTSRKIFRYDNGELVQQEDQMATEFPLTVMVNGEEFVTLVCSPDSLEELVIGFLASEGVIRFKNEIKRFTIDESLGFAYVDLVSTKKLQLKDYTKRVIGSCCGKGRHFYFQQDVKTAKTAIDGVTITPENCLKLMRDMQKSSKLFHHTGGVHNAALCSTDKLIAVRSDIGRHNALDKLYGYCLLHQVPVRDKLIVFSGRISSEVLLKAAKIGVSAVISKSAPTELAIQMAEELNIMTIGFARNRSFNVYTHHERIQFS
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Q65DY4
Q8YP62
EFG_NOSS1
Elongation factor G
Nostoc
MARINPLEKVRNIGIAAHIDAGKTTTTERILFYSGIIHKIGEVHEGTAVTDWMDQERERGITITAAAISTSWKDYQINIIDTPGHVDFTIEVERSMRVLDGVIAVFCSVGGVQPQSETVWRQADRYKVPRIAFINKMDRTGANFYRVHEQMRDRLRANAIAIQLPIGSENDFKGIVDLVRKRAYMYNNDQGTDIEETDIPADLQDQVEEYYTKLVEAVAETDDDLMSKYFDGEPLTEEEIRSALRKGTIAGTIVPVLCGSAFKNKGVQLMLDAVVDYLPAPTEVPPIQGTLPNGDAIERRADDNEPLAALAFKIMADPYGRLTFVRVYSGVLKKGSYVLNATKNKKERISRLVLMKADDRQDVEELRAGDLGAALGLKDTLTGDTITDEGAPVILESLFIPEPVISVAVEPKTKNDMDKLSKALQSLSEEDPTFRVNVDPETNQTVIAGMGELHLEILVDRMLREFKVEANVGAPQVAYRETIRKPVTNVEGKFIRQSGGKGQYGHVVINLEPGEPGTGFEFVSKIVGGVVPKEYIGPAEQGMKESCESGILAGYPLIDVKATLVHGSYHDVDSSEMAFKIAGSMALKEAVLKASPVLLEPMMKVEVEVPEDYIGNVIGDLISRRGQIESQSTEQGLAKVASKVPLATMFGYATDIRSKTQGRGIFTMEFSHYEEVPRSVAETIIAKSKGNA
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q8YP62
Q5GSI3
SYE2_WOLTR
Glutamyl-tRNA synthetase 2
unclassified Wolbachia
MPNIVTRFAPSPTGFLHIGGARTALFNWLYAKHHGGRFLLRIEDTDRKRSTQEAIDAIINGLKWLGVSYDGEIVYQSKRIERHIEVANLLVEKGKAYCCCCPEDKVAEKKAKAREERKIYKHKCTSVIPDAKPVVRFNVPDSQEIIVDDKIYGHIKVNSDQLDDMVILRSDNTPTYIFAVVVDDHDAGITDIIRGSDHLTNTFKQVLIYQALDFDIPRFAHVPLIHGRDGNKLSKRHGATSVCDYEKMGILPKAMRNYLLRLGWSHGNDEIISNEQAVKWFNLESIGRSPARLNFKKLEHLNNHYINNMSNEDILTLMLGESTLTNKKKNYLLQGLTELKKRANYLTELLDLAQFYIKDPPFDLSEEAEQVVKSNLDIIKLLASFLSNIGDKNWNKGFLSSQVKEFSKLHSAKISDIYHSLRAPITGVMDAPGIIDIMIILGKDECIRRLQAV
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Q5GSI3
Q6NMR8
FAF3_ARATH
Protein FANTASTIC FOUR 3
Arabidopsis
MGTVVYQQGFQSQLNEPRALRLRLSSPNPHFSQPFGLALKSHLLDSSHAEDTRNRNDDKAAASPVSDSSGWSSLQSLSSGSSSSTKTTTSSEKESSYYVQRPSSCRALSDQSLALCTENLGSESGSDVTDIDELFSLDVQTKNLGETTTETRTLKSRKRSVSPSDLPPPLTTMRGFQCIQMRPHRENGRLVMTATNAPPRNGCFQADRSNGRLRLSILKDSNEFVENEEETIEPEETEEYEEEEEEEEDEDEDEVMGIENVQVSRRCVQGDRENRGLLNWESFCVATS
Able to repress WUS when constitutively overexpressed, but have no effect on CLV3.
Q6NMR8
Q6YR94
CH60_ONYPE
Chaperonin-60
Candidatus Phytoplasma asteris
MSKKILYGKEARKALLQGVDAIANTVKVTLGPKGRNVILEKAYDSPAIVNDGVSIAKEIELKNPYQNMGAKLVYEVASKTNDKAGDGTTTATVLAQSMIHRGFDAIDAGANPVLVKEGIELAALTVAKKLLAKSKKVDAQEDIQNVAAVSSGSQEIGKIIAQAMQKVGKDGVINVDESKGFETELEVVEGLQYDKGYASPYFVSDRESMTVQLENALVLVTDHKISTVQEIVPILEEVVKASRPLLIVAEAVENEVLGVLVANKLRGTFNVVVTNAPGFGDNQKEMLQDIAVLTKANFVSKELNMKLADLKMDDLGNINKAIIKKDNTTLISNSKSPELEKRIQVLKTQIKNATSDYETKNLQERLAKLSGGVALIKVGAATDTELKDKKLRIEDALNATKAAITEGIVVGGGKALVEVYQELKDTLVSDNKEVQQGIDVVVQSLLVPTYQIAYNAGFSGKDVVKQQLLQPLNFGFNAKEGKYVCLLKEGIIDPTKVTRQAVLNAASISALMITTEAAVVSLKENKDNNFDLGTQE
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.
Q6YR94
O22666
RGP3_ARATH
UDP-L-arabinose mutase 3
Arabidopsis
MAQLYSSVKPTPMLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVINIPVGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGKEINALEQHIKNLLSPSTPHFFNTLYDPYRDGADFVRGYPFSMREGAITAVSHGLWLNIPDYDAPTQLVKPLEKNSRYVDAVMTIPKGTLFPMCGMNLAFDRELIGPAMYFGLMGDGQPIGRYDDMWAGWCVKVICDHMGWGVKTGLPYIWHSKASNPFVNLKKEYNGIFWQEEAIPFFQSVTLPKECTSVQQCYLELAKLVREKLGKVDPYFITLATGMVTWIEAWEELNSAEGTEAEAPKGKN
UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf). Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose form over the furanose form is 95:5. Is not active on other UDP-sugars (UDP-Gal, UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc). Is probably active as heteromer in vivo.
O22666
B0T2B5
EFTU2_CAUSK
Elongation factor Tu 2
unclassified Caulobacter
MAKEKFERNKPHCNIGTIGHVDHGKTTLTAAITIILAKSGGATAKNYADIDAAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPALVVYMNKVDLVDDEELLELVEMEVRELLSSYDFPGDDIPITKGSAKVAIDGGDPVIGEQSILALMTTVDAYIPQPDRPIDLPFLMPVEDVFSISGRGTVVTGRIEKGVVKVGEEVEIVGIRAVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQFYFRTTDVTGIIKLREGVEMIMPGDNAELDVELITPIAMDQGLRFAIREGGRTVGAGVVAKIVE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
B0T2B5
Q1R1C8
DCUP_CHRSD
Uroporphyrinogen decarboxylase
Chromohalobacter
MPLQNDRLLRALARQPVDRTPVWMMRQAGRYLPEYRETRGQAGSFMDLCRNAELACEVTMQPLRRYALDAAILFSDILTIPDAMDLGLYFETGEGPKFRKTVRSAEAVDALPVPDAERDLDYVMNAVRTIRHELADSVPLIGFSGSPWTLATYMIEGGSSKDFRHAKALMYGDPAAMHALLDKLARSVTDYLNAQIRAGAQIVQIFDTWGGVLSTPAYREFSLAYMARIVEGLIREHEGRHVPVILFTKQGGQWLETIADSGADAVGLDWTTELSDARARVGDRVALQGNLDPNVLFASPQAIRDEVARILASYGSGPGHVFNLGHGVSQFTDPDHVAAFIEALHELSPRYHG
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Q1R1C8
A0KT03
MURA_SHESA
UDP-N-acetylglucosamine enolpyruvyl transferase
Shewanella
MDKLAIQASPPLAGDVIISGAKNAALPILMAGVLAETDFIVSNVPNLRDVSTSCKLLRCLGADVDELGNGQIRISTKNLNEFCAPYDLVKTMRASILILGPLLARYGTADVSLPGGCAIGARPVNLHLHGLEMMGAKIEVKEGYIKARVDGRLKGAHIFMDMVSVGATENLLMAAALADGETVIENAAREPEVIDLANCLIAMGAKITGVGSATLRIQGVERLQGCEYRVMPDRIETGSFLVAAAVTRGRIRCLKADPASLESVIAKLEDAGAKITTGEDWIELDMEGKRPKAVNIKTAPYPGFPTDMQAQFCVLNVLAQGTATITETIFENRFMHVPELIRMGANMELEGNTCIIQGIESLSGAQVMATDLRASASLVIAGLVADGKTIVDRIYHLDRGYEHIEQKFQGLGAHVERVQ
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
A0KT03
B1ZDT1
DAPF_METPB
PLP-independent amino acid racemase
Methylorubrum
MSPLANRRFLKMHGAGNAIVVLDLRGTSIRVAPAEARAIAADAHSRFDQLMVVHDPVTPGTDAFMRIYNTDGSESGACGNGTRCVGYALLDDPAMARPAENGCLTLETKAGLVAVKRVTDRSFTVDMGQPRLRWDEIPLAEPFPDTRRIELQVGPIDDPILHSPAAVSMGNPHAIFFVERDPDTFDLGRIGPLLEAHPIFPERANISIAQVTSRDTIKLRVWERGAGLTLACGTAACATVVAAARLRMIGRAARVALPGGELSIEWRADDHVLMTGPVFLEGEGSLSPDLFAGLDG
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
B1ZDT1
A3CNV3
AROA_STRSV
5-enolpyruvylshikimate-3-phosphate synthase
Streptococcus
MKLSTNVKGLKGRIRVPGDKSISHRSIIFGSLAKGVTTVRDILRGEDVLSTMQVFRDLGVQIEDDGNLVKIHGVGFEGLQAPKNKLDMGNSGTSIRLISGVLAGQDFEAEMFGDDSLSKRPMDRVTIPLRQMGVEIAGRTERDLPPLKMKGSRELQPIHYQLPVASAQVKSALIFAALQAQGESVIIEKEITRNHTEDMIAQFGGQIEVEGKEIRIQGGQEFTAQEVTVPGDISSAAFWLVAGLIVPDSKIVLENVGINETRTGILEVIEAMGGRMTLSDVDPVAKSATITVETSELKGTEIGGEIIPRLIDELPIIALLATQAQGRTVIRDAEELKVKETDRIQVVADALNSMGAAITPTEDGMIIEGKTPLHGAQVNTLGDHRIGMMTAIAALLAQSSQVELERSEAIKTSYPNFFNDLEGLMHG
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
A3CNV3
Q2GGA2
TRUB_EHRCR
tRNA-uridine isomerase
Ehrlichia
MYGWINLDKPCGISSASAVNLVKKILNVKKVGHAGTLDPLASGVLPIAIGEATKVMPYAVDVVKSYLFTVQWGEQRTTDDIEGKIVAKSDIVPSSEDIKKAIPNFIGLLRQVPPNFSAVHVNGVRAFKLARNGQDVSLTSRDVNVLKLKLLSADQENNKADFYLLCKKGVYVRSIARDLGIELGCLGYVRKLQRVRVGCFRKKNAITLEMLKMLYNNSRKCSYLLPLWYVLQDMKHLNDVFSDIQIKKIKNGQNIELNNLYVVRNCGICYVSTGNVPVAICSIVNSVVRPVRIFNV
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Q2GGA2
Q4UKF2
GATC_RICFE
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
spotted fever group
MITKEEAQKIAKLARLKFEEDTVEKFSAQLSTIMNMIDILNEIDCKDIEPLTSVSNMNVRMREDVVTSSDLSNKLFDNVSGNSAQLAKEVKYFITPKVIE
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Q4UKF2
Q9H5I1
SUV92_HUMAN
Suppressor of variegation 3-9 homolog 2
Homo
MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKDMEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLKPAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPGISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCPNRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
Q9H5I1
P45584
CU63_LOCMI
LM-ACP 63
Locusta
GLLGLGYGGYSGYGGYGGYGHGLALAAAPAAIAAPAVVAAPAIAHAPAVAVAPAVAHAPAAVSTVSQVSYGTTHYAPAVAKVAAAPVAVAAPAIAAAPAIAAAPAVGLGYGQGLSLGYGHGLGYGHGLSLGYAAAAPALSLGYGGYGHGLSLGYGHH
Component of the cuticle of migratory locust which contains more than 100 different structural proteins.
P45584
A8GKQ1
CYSG2_SERP5
Sirohydrochlorin ferrochelatase 2
Serratia
MDYLPIFCQLQHKACLLVGGGEIAERKARLLLDAGAALTVNACSFTPQFHEWAALGRLTLAAGEFSAELLAEKWLVIAATDRVEVNALVYQCANQQRVFCNVVDDPKRASFIMPSIIDRSPIMVAVSSGGKAPVLARLLREKLEAVLPQHLGKLAQLGGSLRQRVKKHFSDIGSRRRFWEKLFAHDRLAQSLANNDVALAERQIEQLFSHQPQECGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDEIMTLVRRDAERIFVGKRAGHHCVPQEQINQILLQQAQLGKRVVRLKGGDPFIFGRGGEELETLADANIPFSVVPGITAASGCSAYSGIPLTHRDHAQSVRLVTGHAKSDGGLDWSTLAAGQQTLVFYMGLTQAADIQRQLIAHGMPAATPVALVENGTSCRQRVIEGELSQLGTLALQAASPSLIIVGSVVSLRSKLNWFSSQEPSQPLAQMA
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
A8GKQ1
P00430
COX7C_BOVIN
Cytochrome c oxidase polypeptide VIIc
Bos
MLGQSIRRFTTSVVRRSHYEEGPGKNIPFSVENKWRLLAMMTLFFGSGFAAPFFIVRHQLLKK
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
P00430
B4SKH7
DEF_STRM5
Polypeptide deformylase
Stenotrophomonas maltophilia group
MALLPILEFPDPRLRTKAALIDAAEVTTPAFQELVDNMFQTMYDAPGIGLAATQVDVHKRFMVIDVSEEKNEPHVFINPEIVAKDGGRVYQEGCLSVPGIFADVTRADTITVKYLDRDGQQQELEAGEVLATCIQHEMDHLDGKLFIDYLSPLKREMVRKKLAKQRKHVA
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
B4SKH7
O31041
PDUD_SALTY
Propanediol utilization protein PduD
Salmonella
MEINEKLLRQIIEDVLRDMKGSDKPVSFNAPAASTAPQTAAPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGLPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL
The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
O31041
B2FN89
RBFA_STRMK
Ribosome-binding factor A
Stenotrophomonas maltophilia group
MPKTFHRTDRVSAQLRRELGTLVHNAVREHGLPSVSVSDVEITRDMAHAKVFVTALMPERSAEAVAGLKELGYRLRMDLARAMKLRHVPELHFHYDDSVDRGEHIDNILRDLPDTLAAEKRRESDEE
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.
B2FN89
A1SRP9
CYSG_PSYIN
Sirohydrochlorin ferrochelatase
Psychromonas
MDYLPIFTKLENRPCLVVGGGSIACRKIHLLLKAGADVTVCALEFNPSLLKQAANKELKILEQAFTEELLENKWLVIAATNKKQVNEHIATAAHAKQLLVNVVGQADISSFILPSIVDRSPLVVAISSGGKAPVLARLIRERLETLLPMHLGRLAAISAQFRHRVKEVIKVAPLRRRYWEKLFGNGMLANLLQKGQTEKAIALMETSLSEDITQGDVALVGAGPGDPSLLTLKALQLMQQADVVLYDRLVSSDILDLVRRDADLISVGKAAGNHEVEQSRTNQMLVEFAREGKKVVRLKGGDSFIFGRGGEELEELVEAGIAFQVVPGITAASGCSAYAGIPLTHRDFAQSVTFVTGHRKTDGEELNWQALAAPNQTLVVYMGLIQSQEIQTQLLSHGRAPETPVALVNKGTTSDQHVVIGQLSELEQLGGGLQGPTLMIIGEVVNLADKLAWYQSDNKPPLSRDPFLVNLA
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
A1SRP9
B0JS46
UREF_MICAN
Urease accessory protein UreF
Microcystis
MLDQKELLCLLQLASPILPVGAYSYSEGLETLVEKGIISNSASLNDWLERSLCQGSIRLETAVLLRVYRCFCQEDFTKLNYWDNWLSATRETAELRQQSWQMGRSLLNLLRELAPARDNLPEQANYATAFAIGASHWQIGEELAVLGYLHSWASNLINAGLRLIPLGQTLGQSLLIGLQPSLLTATADIISLADENLSSWSWGLSFASMNHETQYSRLFRS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
B0JS46
B1J5D6
TUSA_PSEPW
Sulfur carrier protein TusA
Pseudomonas
MTDFTPDAILDATGLNCPEPVMMLHTHVRNLAAGGLLKVIATDPSTRRDIPKFCNFLGHELLQQQEEAGTYLYWIRKKAD
Sulfur carrier protein which probably makes part of a sulfur-relay system.
B1J5D6
Q89A13
YFGM_BUCBP
Chaperone YfgM
Buchnera
MIKNSYINEKLNFYQKSFLTCMLLIVIVIVYFFSKNYLDKPKNSYVHTKMMTFLTNSNELNISKNLIWTKKTISGNLMSLKLAKVYVINNQLEKALKILEKSKNNSVDLNFFNLISFKIAQIYFQKNNIKKAITTIKDILGDSWDSIRNNFIGDVYFKLDNQKRAVTLWKRSIIQNKKIEFEKIIQMKINNYN
May mediate protein transfer from the Sec translocon to the chaperone network via its extracellular C-terminal region.
Q89A13
B2SHB9
ALR_FRATM
Alanine racemase
Francisella
MNILKISKQTLRNNIKIIREYIGNAKMCFPVKANAYGHGIEDIVENTHDLVDFFAVANSLEAFRVTAVAKNPVLVFGVIYYEYIEKMISENIRVSIQDYEDIEKLEQIAKELDKKVYAHININTGMNRMGVNYNDACRTIQRAYESDWLILEGVYSHLACADNRDHPTNIKQKNRFDSIVKFTKGLSQDIICHLSNSYGFLGQKGICYDMVRPGILSYGFLPEFYVDRVIREIKPIARLLSKVVKIITLQEGEGVGYSLIYRGFEGEQLAVIPIGYGDGFPRELGDRGFVNINDVMYPMAGRMSMDGLTVSLGINEYDVKVGDTVELISAIPRNRNSAFSIAKQTNTIEYDIMSTLNDRIIRKII
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
B2SHB9
A7ZTI5
COAD_ECO24
Pantetheine-phosphate adenylyltransferase
Escherichia
MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A7ZTI5
Q5WCP7
HUTU_ALKCK
Imidazolonepropionate hydrolase
Alkalihalobacillus
MNLNNEPIRAKRGTALTAKGWVQEAALRMLMNNLDEEVAEHPDQLVVYGGIGKAARNWPSYHSIVSSLTTLDNDETLLIQSGKPVAVFKTHEDAPRVLLANSNLVPAWANWETFHELDKKGLTMYGQMTAGSWIYIGSQGIVQGTYETFAECARQHFGGSLKGTITVTAGLGGMGGAQPLAVTMANGVAICVDVDRSRIDKRMETNYLDIVAHTLTEAIEEAELAKKEGIPLSIGLVGNAAEVLPEMLDRGFVPDIVTDQTSAHDPLNGYLPKGFTNEQGQVLRREDPQAYISLAKKSMAEQVEAMLELKKRGAIVFDYGNNIRQVAFDEGIRDAFSFPGFVPAYIRPQFCEGKGPFRWVALSGDPADIDKTDEVILQEFADNEPLCQWIRMARRHISFQGLPARICWLGYGERARFGKRINEMVASGELSAPIVIGRDHLDAGSVASPNRETEAMKDGSDAVADWPILNALVNTAAGASWVSVHHGGGVGMGYSLHAGMVVVADGTAEAARRLERVLTTDPGLGVVRHADAGYQKAIETAKATGIVIPALAREGKENG
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Q5WCP7
Q9Y3R5
DOP2_HUMAN
Protein dopey-2
Homo
MDPEEQELLNDYRYRSYSSVIEKALRNFESSSEWADLISSLGKLNKALQSNLRYSLLPRRLLISKRLAQCLHPALPSGVHLKALETYEIIFKIVGTKWLAKDLFLYSCGLFPLLAHAAVSVRPVLLTLYEKYFLPLQKLLLPSLQAFIVGLLPGLEEGSEISDRTDALLLRLSLVVGKEVFYTALWGSVLASPSIRLPASVFVVGHINRDAPGREQKYMLGTNHQLTVKSLRASLLDSNVLVQRNNLEIVLFFFPFYTCLDSNERAIPLLRSDIVRILSAATQTLLRRDMSLNRRLYAWLLGSDIKGNTVVPESEISNSYEDQSSYFFEKYSKDLLVEGLAEILHQKFIDADVEERHHAYLKPFRVLISLLDKPEIGPQVVGNLFLEVIRAFYSYCRDALGSDLKLSYTQSGNSLISAIKENRNASEIVKTVNLLITSLSTDFLWDYMTRCFEECFRPVKQRYSVRNSVSPPPTVSELCALLVFLLDVIPLELYSEVQTQYLPQVLGCLVQPLAEDMEALSLPELTHALKTCFKVLSKVQMPPSYLDTESTSGTSSPVKGENGKIILETKAVIPGDEDASFPPLKSEDSGIGLSASSPELSEHLRVPRVSLERDDVWKKGGSMQRTFLCIQELIANFASKNIFGVQLTASGEESKSEEPAGKRDRDGTQSLAANDSSRKNSWEPKPITVPQFKQMLSDLFTARGSPFKTKSSESPSSSPSSPARKNGGEWDVEKVVIDLGGSREERREAFAAACHLLLDCATFPVYLSEEETEQLCATLFQLPGAGDSSFPSWLKSLMTICCCVTDCYLQNVAISTLLEVINHSQSLALVIEDKMKRYKSSGHNPFFGKLQMVTVPPIAPGILKVIAEKTDFYQRVARVLWNQLNKETREHHVTCVELFYRLHCLAPTANICEDIICHALLDPDKGTRLEALFRFSVIWHLTREIQGSRVTSHNRSFDRSLFVVLDSLACTDGAIGAAAQGWLVRALSLGDVARILEPVLLLLLQPKTQRTSIHCLKQENSADDLHRWFNRKKTSFREACAVPEPQESGSEEHLPLSQFTTVDREAIWAEVEKEPEKYPLRGELSEEELPYYVELPDRTAHGAPDSSEHTESADTSSCHTDSENTSSFSSPSHDLQELSNEENCCAPIPMGGRAYPKRSALLAAFQSESFKAGAKLSLVRVDSDKTQASESFSSDEEADLELQALTTSRLLKQQRERQEAVEALFKHILLYLQPYDSRRVLYAFSVLEAVLKTNPKEFIEAVSRTSMDTSSTAHLNLISNLLARHQEALIGQSFYGKLQTQVPNVCPHSLLLELLTYLCLSFLRSYYPCYLKVSHRDILGNRDVQVKSVEVLIRIMMQLVSVAKSSEGKNVEFIHSLLQRCKVQEFVLLSLSASMYTSQKRYGLATAHHGRALPEDSLFEESLINLGQDQIWSEHPLQIELLKLLQVLIVLEHHLGRAHEEAENQPDLSREWQRALNFQQAISALQYVQPHPLTSQGLLVSAVVRGLQPAYGYGMHPAWVSLVTHSLPYFGKSLGWTVTPFVVQICKNLDDLVKQYESESVKLSVSTTSKRENISPDYPLTLLEGLTTISHFCLLEQANQNKKTMAAGDPANLRNARNAILEELPRTVNTMALLWNVLRKEETQKRPVDLLGATKGSSSVYFKTTKTIRQKILDFLNPLTAHLGVQLTAAVAAVWSRKKAQRHSKMKIIPTASASQLTLVDLVCALSTLQTDTLLHLVKEVVKRPPQVKGGDEKSPLVDIPVLQFCYAFLQRLPVPALQENFSSLLGVLKESVQLNLAPPGYFLLLSMLNDFVTRTPNLENKKDQKDLQEITQKILEAVGNIAGSSLEQTSWLSRNLEVKAQPQASLEESDAEEDLYDAAAASAMVSSSAPSVYSVQALSLLAEVLASLLDMVYRSDEKEKAVPLISRLLYYVFPYLRNHSAYNAPSFRAGAQLLSSLSGYAYTKRAWRKEVLELFLDPAFFQMDTSCVHWKSIIDHLLTHEKTMFKDLMNMQSSSLKLFSSFEQKAMLLKRQAFAVFSGELDQYHLYLPLIQERLTDNLRVGQTSIVAAQMFLFFRVLLLRISPQHLTSLWPIMVSELIQTFTQLEEDLKDEDESLRSTNKVNRTKVSVPDANGPSVGEIPQSELILYLSACKFLDTALSFPPDKMPLFQIYRWAFIPEVDTEGPAFLSDVEENHQECKPHTVRILELLKLKFGEISSSDEITMKSEFPLLRQHSVSSIRQLMPFFMTLNGAFKTQRQLPADSPGTPFLDFPVTDSPRILKQLEECIEYDFLEHPEC
May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation.
Q9Y3R5
Q11HP8
RS7_CHESB
30S ribosomal protein S7
unclassified Chelativorans
MSRRHRAEKREINPDPKFGDTVVTKFMNAIMFEGKKSVAERIVYGALDQVQEKTKQEPVAVFHQALDNVAPHVEVRSRRVGGATYQVPVDVRPERRQALAIRWLISAARGRNEKTMVERLSGELLDASSNRGTAVKKREDTHKMAEANRAFSHYRW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Q11HP8
Q3J7X9
HLDD_NITOC
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Nitrosococcus
MIIVTGGAGFIGSNIIKALNQGGREDILVVDDLTQGEKFSNLIDCEIWDYWDKQPFLQAIKAGEEFPHPVDAFIHQGACSATTEWNGRYMMENNFYYSKRLLHYCLERRIPFLYASSAAVYGCGLTFQEHREFEAPRNVYGYSKWLFDQYVRRYLPTASSQIVGLRYFNIYGPREAHKGAMASVAYHAHCQLKETGRIKLFEGCDGYEHGEQRRDFVSVADAAAVNLWFLEHPNQSGIFNVGTGQAQTFNEVAQAVLAFHGHGEIEYIPFPDHLRGRYQSFTQADIHALREAGYAEPFALVEKGVKTYLDWLGKNQD
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Q3J7X9
B7LVJ5
COAD_ESCF3
Pantetheine-phosphate adenylyltransferase
Escherichia
MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQHATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
B7LVJ5
Q49UQ0
RS6_STAS1
30S ribosomal protein S6
Staphylococcus
MRTYEVMYIIRPNIEEDAKKAVVERFNGILASHGSEVLEAKDWGKRRLAYEINDFSEGYYNIVRIQTADNEATDEFQRLAKISDDVIRYIVIREDEDKTRK
Binds together with S18 to 16S ribosomal RNA.
Q49UQ0
Q0I178
HEM3_HAES1
Pre-uroporphyrinogen synthase
Histophilus
MSINKTLKIATRQSPLALWQANYVKNRLQQRYSHLSVELVPIITKGDVILDTPLAKIGGKGLFVKELENALLNGEADIAVHSMKDVPMQFPKGLELSVICPREDPRDAFVSNKYRTLDELPQGAIVGTSSLRRQCQLKNWRADLDIRSLRGNVGTRLNKLDQGDYDAIILASAGLIRLGLTERIRSFIEIDTILPACGQGAVGIECRVDDRDVQSLLMPLADQTTTYCVLAERAMNFHLQGGCQVPIGAYAILENNQLYLRGLVGDVHGSQILSAEGQFELSLDFESSQSAVQKAEELGVSIAEQLLQQGADKILQAVYQS
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Q0I178
P62659
RS18_THET2
30S ribosomal protein S18
Thermus
MSTKNAKPKKEAQRRPSRKAKVKATLGEFDLRDYRNVEVLKRFLSETGKILPRRRTGLSAKEQRILAKTIKRARILGLLPFTEKLVRK
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.
P62659
Q75I94
BGL08_ORYSJ
Beta-glucosidase 8
Oryza sativa
MGCAPAAHYLPGGGWRRLLVVVVALVVLDRAGARVRAADDDTGGLSRAAFPKGFVFGTATSAFQVEGMAASGGRGPSIWDPFVHTPGNIAGNGNADVTTDEYHRYKEDVDLLKSLNFDAYRFSISWSRIFPDGEGKVNTEGVAYYNNLIDYVIKQGLIPYVNLNHYDLPLALQKKYEGWLSPKIVGVFSDYAEFCFKTYGDRVKNWFTFNEPRIVAALGHDTGTDPPNRCTKCAAGGNSATEPYIVAHNIILSHATAVDRYRNKFQASQKGKIGIVLDFNWYEPLTNSTEDQAAAQRARDFHVGWFLDPLINGQYPKNMRDIVKERLPTFTPEQAKLVKGSADYFGINQYTANYMADQPAPQQAATSYSSDWHVSFIFQRNGVPIGQQANSNWLYIVPTGMYGAVNYIKEKYNNPTIIISENGMDQSGNLTREEFLHDTERIEFYKNYLTELKKAIDDGANVVAYFAWSLLDNFEWLSGYTSKFGIVYVDFTTLKRYPKDSANWFKNMLQASGPGSKSGSGTSDSQVGSATSASHPVGSAISSSHRLLLPLLVSLHFLFPSFFMFLSL
Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides, laminari-oligosaccharides, sophorose and gentiobiose.
Q75I94
Q740T9
TRHBN_MYCPA
Hemoglobin-like protein HbN
Mycobacterium avium complex (MAC)
MKILARFRKAEPASIYDRIGGHEALEVVVENFYVRVLADEQLSGFFTGTNMNRLKGKQVEFFAAALGGPHPYTGAPMKQVHQGRGITMHHFGLVAGHLADALTAAGVPSETVSEILGAIAPLAPEIATGEAGKVTV
Binds oxygen cooperatively with very high affinity because of a fast combination and a slow dissociation rate.
Q740T9
Q9V2V6
PSA1_HALVD
Proteasome subunit alpha 1, N-terminally processed
Haloferax
MQGQAQQQAYDRGITIFSPDGRLYQVEYAREAVKRGTASIGVRTPEGVVLAADKRSRSPLMEPTSVEKIHKADDHIGIASAGHVADARQLIDFARRQSQVNRLRYGEPIGIETLTKEVTDHIQQYTQVGGARPFGVALLIGGVENGTPRLYETDPSGTPYEWKAVSIGADRGDHQEHLEENFRDDLTLDEGIELALEAIASTSDEGTAPDGVDVATVSAETERFVELSNDEIESYLEANDLLATEDDEQTEE
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity.
Q9V2V6
B0TM02
RL14_SHEHH
50S ribosomal protein L14
Shewanella
MIQMQSTLEVACNSGARRVQCIKVLGGSHRRYAGIGDVIKVSVKEAIPRGKAKKGDVYNAVVVRTKKGVRRPDGSVIRFDRNAAVLLNANLAPIGTRIFGPVTRELRTERFMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
B0TM02
B3QCH9
ARGB_RHOPT
NAG kinase
Rhodopseudomonas
MTDAPVISPLDQARILSEALPHMQRYDEETIVIKYGGHAMGAEDTAKAFARDIVLLEQTAVNPVVVHGGGPQIAQMLKRLGIKSEFAAGLRITDAATIEIVEMVLAGSINKQLVGYINEAGGKAVGLCGKDGNMVSATKATRTMVDPDSRIEEVIDLGFVGEPEKVDLTLLNQLIGHELIPVLAPLATSASGQTFNVNADTFAGAVAGALRAKRLLLLTDVPGVLDQNKKLIPELSIKDARKLIADGTISGGMIPKVETCIYALEQGVEGVVILDGKVPHAVLLELFTNQGTGTLIHK
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
B3QCH9
Q7WMS0
FDHD_BORBR
Sulfur carrier protein FdhD
Bordetella
MDRLHTSSADWPDHLATQVVRVRGGVLQAAGQSDHVAEETPVALEFNGISHATMLVTPTHLDDFALGFALTEGIVGGMADVRGVELETRCDGIVVQVEIATSCEVRLKERRRAMAGRTGCGLCGVETLPEVVRDVAPVADSDALPVHNVLRAMQSLRSRQTLHDATGATHAAGWADASGEVVLAREDVGRHNALDKLIGALARQGIAPLPGMAVVSSRASFEMVQKTASAGIPILAAVSAPTALAIRLARQTNVTLLGFVRNTDATIYSHPQRIAA
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Q7WMS0
Q1X6Z5
BDNF_RAMSP
Brain-derived neurotrophic factor
unclassified Ramphotyphlops
SCMKAAPMKEVSLRGQGNLAYPGLRTQANLENLGGPNDATRGLTSLADTFEQVIEELLDEQQAIQPSKENKDADLYSSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCESTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCSSKGYTKEGCRGIDKRYWNSQCRTTQSYVRALTMDNKKRVGWRFIRIDTSC
Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it.
Q1X6Z5
Q629K1
TRIQK_HUMAN
Triple repetitive-sequence of QXXK/R protein homolog
Homo
MGRKDAATIKLPVDQYRKQIGKQDYKKTKPILRATKLKAEAKKTAIGIKEVGLVLAAILALLLAFYAFFYLRLTTDVDPDLDQDED
May play a role in cell growth and maintenance of cell morphology.
Q629K1
P51475
OPSP_CHICK
Pineal gland-specific opsin
Gallus
MSSNSSQAPPNGTPGPFDGPQWPYQAPQSTYVGVAVLMGTVVACASVVNGLVIVVSICYKKLRSPLNYILVNLAVADLLVTLCGSSVSLSNNINGFFVFGRRMCELEGFMVSLTGIVGLWSLAILALERYVVVCKPLGDFQFQRRHAVSGCAFTWGWALLWSAPPLLGWSSYVPEGLRTSCGPNWYTGGSNNNSYILSLFVTCFVLPLSLILFSYTNLLLTLRAAAAQQKEADTTQRAEREVTRMVIVMVMAFLLCWLPYSTFALVVATHKGIIIQPVLASLPSYFSKTATVYNPIIYVFMNKQFQSCLLEMLCCGYQPQRTGKASPGTPGPHADVTAAGLRNKVMPAHPV
Produces a slow and prolonged phototransduction response consistent with the non-visual function of pineal photoreception.
P51475
B1ZWG7
COAD_OPITP
Pantetheine-phosphate adenylyltransferase
Opitutus
MRHCIYPGTFDPVTYGHLDVLARAVKLFDHVTVAVAENTPKGPLFTSAQRIAMLQPNVTRFPNVSVTSFNSLLVEFAMAQKAIAVIRGLRAFSDFEFEFHMALMNRHLESQIETIFVMPNEQFSYTSSSLVKDVAKHGGDVSHFVPPNVAAALEAVFGTK
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
B1ZWG7
B3LTX4
RRT14_YEAS1
Regulator of rDNA transcription 14
Saccharomyces
MSSSLSQTSKYQATSVVNGLLSNLLPGVPKIRANNGKTSVNNGSKAQLIDRNLKKRVQLQNRDVHKIKKKCKLVKKKQVKKHKLDKEQLEQLAKHQVLKKHQQEGTLTDHERKYLNKLIKRNSQNLRSWDLEEEVRDELEDIQQSILKDTVSTANTDRSKRRRFKRKQFKEDIKGSDFVKDHRYPGLTPGLAPVGLSDEEDSSEED
Involved in ribosome biogenesis, probably through modulation of rDNA transcription.
B3LTX4
P38604
ERG7_YEAST
Oxidosqualene--lanosterol cyclase ERG7
Saccharomyces
MTEFYSDTIGLPKTDPRLWRLRTDELGRESWEYLTPQQAANDPPSTFTQWLLQDPKFPQPHPERNKHSPDFSAFDACHNGASFFKLLQEPDSGIFPCQYKGPMFMTIGYVAVNYIAGIEIPEHERIELIRYIVNTAHPVDGGWGLHSVDKSTVFGTVLNYVILRLLGLPKDHPVCAKARSTLLRLGGAIGSPHWGKIWLSALNLYKWEGVNPAPPETWLLPYSLPMHPGRWWVHTRGVYIPVSYLSLVKFSCPMTPLLEELRNEIYTKPFDKINFSKNRNTVCGVDLYYPHSTTLNIANSLVVFYEKYLRNRFIYSLSKKKVYDLIKTELQNTDSLCIAPVNQAFCALVTLIEEGVDSEAFQRLQYRFKDALFHGPQGMTIMGTNGVQTWDCAFAIQYFFVAGLAERPEFYNTIVSAYKFLCHAQFDTECVPGSYRDKRKGAWGFSTKTQGYTVADCTAEAIKAIIMVKNSPVFSEVHHMISSERLFEGIDVLLNLQNIGSFEYGSFATYEKIKAPLAMETLNPAEVFGNIMVEYPYVECTDSSVLGLTYFHKYFDYRKEEIRTRIRIAIEFIKKSQLPDGSWYGSWGICFTYAGMFALEALHTVGETYENSSTVRKGCDFLVSKQMKDGGWGESMKSSELHSYVDSEKSLVVQTAWALIALLFAEYPNKEVIDRGIDLLKNRQEESGEWKFESVEGVFNHSCAIEYPSYRFLFPIKALGMYSRAYETHTL
Lanosterol synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol .
P38604
Q6N5R2
LPXB_RHOPA
Lipid-A-disaccharide synthase
Rhodopseudomonas
MSGAAKTGDRVRTVYLIATEESGDRLGAALMRELRARLGSKVRFAGVGGHCMAGEGLASLFPIEELSIIGFAAVVQRLPMILKLIRRAVDAVLTAKPDILVIIDSPDFTHRVARRVRQRDPSIPIVDYVSPTVWAWRPGRARAMLGYVDHVLALLPFEPAEYRRLQGPPCSYVGHPLTEQFGSLRPDAAEQARREASPPVLLVLPGSRRSEVRHHAAAFGDTLARLKHEGVAFEAVLPTTPHLEGLVRAAVASWEVQPRIVVGEQDKRAAFRIAHAALAKSGTVTLELAIAGVPMVTAYRAGSVEIWIARRVVRPGTVILANLVMGDDVIPEFIQEDCVPDKLVPAVRDLLGNTPARRRQLAGFAKIDDILSTGEQTPSGRAADIVLDVMRHA
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q6N5R2
Q7WL81
NADD_BORBR
Nicotinate mononucleotide adenylyltransferase
Bordetella
MTRIGLLGGSFDPVHVAHIALADTARQFLGLDQVQLIPAANPWQRQPLKASAPHRLRMLELAIAGHPALAINPVEIERGGATYTADTVRALPGGPQYFWLLGTDQLQNFCTWRDWQDIAARIELAVATRPGASIAPPAELATWLAAHRRQLHELPFAPMAVSASDIRQRLAAGAATDGLLPEPVAAYIATHHLYR
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Q7WL81
Q3SRD1
TIG_NITWN
PPIase
Nitrobacter
MQVNETLAEGLRHEFQVSIPAAEIAAKADERLDDLKDKVKINGFRPGKVPVSHLKKLYGRSVMVETIEDTIRDTNMQIVNDRGLKLAGNPKVTMPSEPKEIEDILAGNSDLSYSVAIEVVPPIELADFKSFTIEKPVVDVSDADVDEAVERIAEQNRTYTTRAEGAKAENGDRITISFKGTIDGELFEGGSSEDILVVLGSNALIPGFEEQLVGAGVGETRTVKASFPGNYADSELAGKDAEFETTVSLIEAPEELKIDDEFAKLLGLEELDQLRQVVREQLSAEFARAMRQHVKRALFDRLDETHKFDAPPTLVEEEFEQVWKTIMAEMEKEKKTFADENTTEEEARAEYRRIADRRVRLSLVLSEIGEKNGITVADDEINRALISRARQTPGREKEIWDYYQRNPQALAQIRAPLFENKVVDFILELATITEKSVTREDLFKEHEAHSAEM
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Q3SRD1
A7HY09
LPXD_PARL1
UDP-3-O-acylglucosamine N-acyltransferase
Parvibaculum
MADKRFFEAKEPLSLGEIAGRIGAALADADDGSRIVTGVAPLDTAGSNDLSFLDNPKYAEAFYATAAGACIVHPRFAERAPDNVALILSDQPYRAYALVAQIFHPDEAHGADTFGARGEIHPRATVHPTAKLGTGVTLEPGVTIGAGVEIGNNTVIGTNTSVGKGCTVGKDCFIGPNVTLSHAHLGDRVMVHPGVRIGQDGFGFAMGLPRHEKVPQLGRVIVQDDVEIGANSTVDRGAGPDTVIGEGTKIDNLVQIGHNVEIGRGCIIVSQTGIAGSTKLGDFVVLAAQVGVTGHLTINSGAQIAARGAVVHDVPAGQQYGGVPAKPIAEWRREVVELRKLGRRRRSGTKADD
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A7HY09
P87314
HIR1_SCHPO
Histone transcription regulator 1 homolog
Schizosaccharomyces
MKIKKIPWLGHFDDRGHRLSIFSIHIHPDGSRIATGGLDGTIRIWSTEAINRENENENENEDLPKQLCCMSTHTGTVTSVRFSPNGQYLASGSDDRVVIIWHKEEAIPGLGSTFGSGEKHTENWRSYRRLLGHDNDIQDLCWSYDSQLVVSVGLDSSIIVWNGTTFERLKRIEAHQSHVKGITFDPAGKYFATESDDRTIKVWRVSDFSIEKTITGPFNNSPLSTYFRRPSWSPDGKHIAAPNAMNGPVSCVSIIERGTWTSEINLIGHEGPVEVTAFNPKLFRDKNDKLVCILACGGQDRSLSIWSSALPRPLLSCQNVFQKSIGDVCWSPDGLSLFLCSYDGNVLVCTFEKEEFGDMVSDEEISKALAKYGHGRHGIVLPESAKQLELEETAYAILKKPSSLSTTDPTLVPQSSSTPKSAQKTPQKLPAFLPNRLTAETVDTNKLTASKEQIASPKRPGPSDNGNEIPTKFVQKVTITKEGKKRVAPQLLTTLSATPSTSRLASTQLQHTGSSQLPPQQFSQPINSLPKGGVPILIVGNKTKVNHENDESDQALQEEKIEEGLLKNYYSSLIDSSTSISNINFEAPRYKTNIVHSLNNEQKYVLEVKNGTSEKNPTRIVALENGNTKWMDYLPRPVILVTGSIHFWSIACDDGSLHLYSLTGSRLLPPIMIESKASFLHCNNAYLLCISSSGMVYAWNVVNKTALFTANSLAPILSRVSNNVTIENNSTDIPHVVIASISKEGVPSVTLSTGETYVYSSTMLCWQRITEPWWAIGSREWDSSGLLQSNTQTESQPLKIYEHRTNNVLMDSGRGKLLQKMVADAITEEGYDDFETIVTINHLENKIASARLLKLDDEFLVTSEVYVRLLMHHGLWQKLEEFLGELRTQTKCSIKLSGREVVAKMLVVLRQAVQTDNEFDRANKLIEKYAST
Probably required for replication-independent chromatin assembly. Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. Repressor of histone gene transcription in G1 arrested cells. Required for repression of htb1 gene expression outside of S phase.
P87314
B1LXF3
ILVC_METRJ
Ketol-acid reductoisomerase type I
Methylobacterium
MRVYYDRDADLNLIKGKKVAIVGYGSQGHAHALNLRDSGVKDIVIALREGSATAKKAEHEGFKVLSVAEAAKWADVVMMLTPDELQGDIYRESLEGNMKQGAALLFAHGLNVHFNLIEPRKDLDVLMVAPKGPGHTVRSEYLRGGGVPTLIAIAQDASGNAHDLGLSYASANGGGRAGIIETTFKEECETDLFGEQAVLCGGLVELIKAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVTGPRIVTPETKAEMKRVLNDIQSGTFTRNWMLENKVNQTSFKATRAKLAAHPIEEVGAKLRGMMPWISEKALVDKTRN
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
B1LXF3
P0A5X5
RS19_MYCBO
30S ribosomal protein S19
Mycobacterium tuberculosis complex
MPRSLKKGPFVDEHLLKKVDVQNEKNTKQVIKTWSRRSTIIPDFIGHTFAVHDGRKHVPVFVTESMVGHKLGEFAPTRTFKGHIKDDRKSKRR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
P0A5X5
Q9CJ30
DUT_LACLA
dUTP pyrophosphatase
Lactococcus
MKIRGFEVVTKYKNAGINIPKRSTEHSAGYDIEAAETVSFAPGEIKLIPTGLKAYMQAGEVLYMYDRSSNPRKKGLVLINSVGVIDKDYYNNPDNEGHMFMQMRNFTDEEVVIEKGERVVQGVFMPFLVADGDENQEKEERTGGFGSTGA
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Q9CJ30
A0LI00
LEPA_SYNFM
Ribosomal back-translocase LepA
Syntrophobacter
MTKIRNFSIIAHIDHGKSTLADRLIQRAGLVTDRQFRDQILDNMDIERERGITIKSQTVTLPYRSRNGEEVELNLIDTPGHVDFSYEVSRALASCEGVLLLVDASQGVQAQTLANLYAAMEHDLTIIPVINKIDLLSADIENTRAQIESELGLDSSQAVLCSAKEGRGIDDVLEAVVDRIPPPSGKLDAPLSALIFDAHYDSFRGTIVACRVFDGSVRPGDVIRFMSNGATYKVEEVGVFRLSREPKKELRAGMVGYVISGVKTVSDTRVGDTITLDSNPVPAPLPGFKEVKPVVFSSIYPISSDDYLSLADSLEKYKLNDAALIYQKDSSVALGQGFRCGFLGLLHLEIVQERLEREYDQSIIMTFPSVQYVLTLEDGSTTMVDNPQYYPDPIRIRTSAEPFIKASIIIPERYMGAVMKLCLDKRGVNPRFNYPTPGRIEISMEMPLAEVVFDFYDKLKTVTQGYGSFDYDLIEHRVSDLVKLDILVNSEKVDALSLIVHRERAREWAVQVCDRLKEEIPRHQFKIAIQGAIGGKIIARSTVNAFRKDVTAKCYGGDISRKRKLLEKQKKGKKRMKMVGSVMIPQSAFVAVLKADNE
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.
A0LI00