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2.75k
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5.51k
AlphaFoldDB
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10
B7UI87
FIXA_ECO27
Protein FixA
Escherichia
MKIITCYKCVPDEQDIAVNNADGSLDFSKADAKISQYDLNAIEAACQLKQQAAEAQVTALSVGGKALTNAKGRKDVLSRGPDELIVVIDDQFEQALPQQTASVLAAAAQKAGFDLILCGDGSSDLYAQQVGLLVGEILNIPAVNGVSKIISLTADTLTVERELEDETETLSIPLPAVVAVSTDINSPQIPSMKAILGAAKKPVQVWSAADIGFNAEAAWSEQQVAAPKQRERQRIVIEGDGEEQIAAFAENLRKVI
Required for anaerobic carnitine reduction. May bring reductant to CaiA.
B7UI87
B0CDM2
DNAA_ACAM1
Chromosomal replication initiator protein DnaA
Acaryochloris
METSLETLWSQVLERLQLQLSRPTFETWIKTANAEQLDENRLVIRTPNPFARNWLQKYYVKTIRDVVHEILGHPVEIQIEIAQGDSNATISAPEVASPPPTASPVENTNTSQRQQASLNPKYVFSRYVVGPNNRMAHAACLAVAESPGREFNPLFLCGGVGLGKTHLMQAIGHYRLEISPNSRIFYISTEQFTNDLIAAIRKDGMQKFREHYRAVDVMLVDDIQFIEGKEYTQEEFFHTFNTLHEAGKQVVLASDRPPSQIPRLQERLCSRFSMGLIADIQPPDLETRMAILQKKAEYENIRLPREVIEYIASSYTSNIRELEGALIRAVAYISISGLPMNVENIAPVLNPPTAKISASPESIINAVADTYGISIDDLKGNSRRREISMARQIGMYLMRQHTDLSLPKIGEEFGGKDHTTVMYSCDKVSDLQKKNPELAQSLRQLGDRIKLANQP
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.
B0CDM2
O25688
RBFA_HELPY
Ribosome-binding factor A
Helicobacter
MNAHKERLESNLLELLQEALASLNDSELNSLSVTKVECSKGKHHAYVFVLSSDHKILSKLKKAEGLIRQFVLQASGWFKCPKLSFVSDNSLEKQLRLDAIFNEIAKGKDND
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.
O25688
B4SEU9
DAPB_PELPB
4-hydroxy-tetrahydrodipicolinate reductase
Pelodictyon
MRFTLVGNGRMGQQVALVIAQSGCHETAAVLDINTAITPDLFQGSDAIIDFTVREAFFANLPAMLESGVPIVVGTTGWDDLRDEIEVKVSDAGASLLYSANFSLGVNIFLRTVREAARLIAPFGQFDIAFAEQHHTAKADFPSGTALRAADMILSANSRKKSVVRQLSDDKKLAPDELQVASLRLGSVFGKHSAFIDSDADEIVISHTAKSRSGFAAGAVEAAIWLARRHTTAPGFYTMDDFLNETFS
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
B4SEU9
B3LT72
LCL2_YEAS1
Long chronological lifespan protein 2
Saccharomyces
MSQSRWSIVLIFALFIFGSTGVNAFFNFGHHQQQQQQQQQSYEDQVLNNPCDGYLCPDTLTCVAQQKDCPCPFPKSQLKCVLPDNKFVCISKPATHNEKFRAIYDDPVKGPKAKNKGFRDCGWVSDAYKNH
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
B3LT72
Q9VG97
GSTD3_DROME
Inactive glutathione S-transferase D3
Sophophora
MVGKALGLEFNKKIINTLKGEQMNPDFIKINPQHSIPTLVDNGFTIWESRAILVYLVEKYGKDDALYPKDIQKQAVINQRLYFDMALMYPTLANYYYKAFTTGQFGSEEDYKKVQETFDFLNTFLEGQDYVAGDQYTVADIAILANVSNFDVVGFDISKYPNVARWYDHVKKITPGWEENWAGALDVKKRIEEKQNAAK
Has no glutathione S-transferase activity.
Q9VG97
Q1KVX3
PSBF_TETOB
PSII reaction center subunit VI
Tetradesmus
MTTRKSAEAITYPIFTVRWLSIHALAVPTIFFLGSITAMQFIQR
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q1KVX3
O15204
ADEC1_HUMAN
A disintegrin and metalloproteinase domain-like protein decysin-1
Homo
MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVGLAASNSLCSPSSVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAPIPTNIMTTPVCGNHLLEVGEDCDCGSPKECTNLCCEALTCKLKPGTDCGGDAPNHTTE
May play an important role in the control of the immune response and during pregnancy.
O15204
Q8ZAX7
DUSB_YERPE
tRNA-dihydrouridine synthase B
Yersinia
MRIGHFQLTNCLIAAPMAGITDRPFRALCHGMGAGMAVSEMLSSNPEVWRTDKSRLRMVHVDEPGIRNVQIAGNDPDEMAAAARINVASGAQIIDINMGCPAKKVNRKLAGSALLQHPDLVKQILSAVVNAVDVPVTLKIRTGWSPEHRNCIEIAQLAENCGIQALTIHGRTRSCLFNGEAEYDSIRAVKQTVSIPVIANGDITDPHKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPMPLGEVQRLLDGHIRELHDFYGPGKGFRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENLA
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Q8ZAX7
Q9ZMB7
KGUA_HELPJ
GMP kinase
Helicobacter
MNNDFNLLILSGPSGAGKSTLTKYLQEKIPKTHFSLSTTTRKPREGEVDGLHYNFVSEEEFKQGIEKGQFLEWAIVHNHYYGTSKIPVEKALKEGKIVIFDIDVQGHEILKKHYPNACSVFISTKNQEILKERLLLRGTDSKETIEKRLINAYKEMQCLESFDYLIINEDLEKSKEIILSIAKTLVHRLKAFNFEKICKAWKNESL
Essential for recycling GMP and indirectly, cGMP.
Q9ZMB7
C6HRP6
GET3_AJECH
Guided entry of tail-anchored proteins 3
Histoplasma
MSSTAMVSGDDSLEPTLQSLLDQKTLRWVFVGGKGGVGKTTTSCSLAIQLAKVRKSVLLISTDPAHNLSDAFGQKFGKEARLVDGFDNLSAMEIDPNGSIQDLLATGGDQADDPMAGLGLGGMMQDLAFSIPGVDEAMSFAEVLKQVKSLSYEVIVFDTAPTGHTLRFLQFPTVLEKALAKLSQLSSQFGPMLNSILGARGGLPGGQNLDEILSKMESLRETIGEVNAQFKDADLTTFVCVCIAEFLSLYETERMIQELTSYQIDTHCIVVNQLLFPGKDSSCEQCKARRKMQKKYLNEIEDLYEDFNVVRMPMLVEEVRGKEKLEKFSNMLVNPYVPPEE
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
C6HRP6
A7FPZ7
EFTS_CLOB1
Elongation factor Ts
Clostridium
MISAKMVKDLREKTGAGMMDCKKALTECDGDLEKAVEVLREKGLAAAAKKSGRVAAEGIVSTYISEDMKNGSIVEFNCETDFVSVNELFVELANNLSKQAAFSNVSTAEELLEEKYIADESKLVKDVITELIAKLGENMNLRRIAKLSVDKGVITSYIHGGGRIGVLVKLACEKEDAKLAEIAKDVAMQVAATNPLFLNRDGVDTDTLEKEKEIYRVQALNEGKPEKVVEKMVMGRINKYYKENCLVEQLWVKNGDYTITKYLQEQSKEIGADITVEAFVRYEKGEGIEKKEEDFAEEVQRQMNQGK
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
A7FPZ7
A4JB96
DDL_BURVG
D-alanylalanine synthetase
Burkholderia cepacia complex
MSGIDPKRFGKVAVLFGGESAEREVSLTSGRLVLQGLRDAGIDAHLFDPAERPLSALKDEGFVRAFNALHGGYGENGQIQGALDFYGIRYTGSGVLGSALGLDKFRTKLVWQQTGVPTPPFETVLRGDDYAARATEIVAKLGLPLFVKPASEGSSVAVLKVKTADALPAALSEAATHDKIVIVEKSIEGGGEYTACIAGDLDLPLIKIVPAGEFYDYHAKYVADDTQYLIPCGLPAAQEAELKRIARRAFDVLGCTDWGRADFMLDAAGNAYFLEVNTAPGMTDHSLPPKAARSIGISYSELVVKVLSLTLND
Cell wall formation.
A4JB96
A0A0B4J2D9
KVD13_HUMAN
Immunoglobulin kappa variable 1D-13
Homo
MDMRVPAQLLGLLLLWLPGARCAIQLTQSPSSLSASVGDRVTITCRASQGISSALAWYQQKPGKAPKLLIYDASSLESGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQFNSYP
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
A0A0B4J2D9
Q9PP99
ISPT_CAMJE
Isoprenyl transferase
Campylobacter
MNELKHLAVVMDGNRRWARAKGFLAKLGYSQGVKTMQKLMEVCMEENISNLSLFAFSTENWKRPKDEIDFIFELLDRCLDEALEKFEKNNVRLRAIGDLSRLEDKVREKITLVEEKTKHCDALCVNLAISYGARDEIIRAAKRVIEKKLELNEENLTQNLDLPLDVDLMLRVGNAKRLSNFLLWQCSYAEIYFSETLFPSLTKREFKRIIKEFRNRERTFGK
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Q9PP99
Q5FLL0
GATB_LACAC
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Lactobacillus
MNFKSTIGLEVHFELKTKSKIFSPSPVTYGAEQNTETNVIDWAMPGTLPMVNKNVYRLGIMVALATHSHILPTTHFDRKNYFYPDNPKAYQITQFFQPLARDGYIEVEVRGKKKRIGIHEMHIEEDAGKNTHGTNGYSYVDLNRQGVPLLEVVSEPDMEDPEEAYAYLEKLRKIVQFTGASDVKMEEGSMRVDTNISIRPAGQKELGTKVEMKNLNSFDHVRRSLAYEEKRQEQVLLAGGHIQLSTRRFDEATGKTVLERVKEGASDYRYFPEPDIAPDHISQEWIDQIAKELPKSPFDRYDDYVNKFGLKPYDANVLLQTKESSDFFDAAVAAGADPTLAANWMNTQVNGYLNDNRVSLEDIKLTPENLAKMIKLIQDGTISSKIAKKVFAETVANGTDPKKYVEDNGMVQLSDTSVLEPMVKKVVDDNPQSVEDFKNGKDRAIGFLVGQIMKQTRGKANPKMVNKLLNQELQSR
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).
Q5FLL0
Q135P8
AMPA_RHOPS
Leucyl aminopeptidase
Rhodopseudomonas
MPDAVKVGFVPFSAAARGTLVVFCDDTLKFGSVTGKALGAAASTVKRAVAASQFKGKSGSALDLLAPEGLKVGRLIVIGTGKAAALKDNDIVKLGGAVAGKLSTGDSAVTVIAELPGGAMRPEQAAAVASGIRLRAYKFDRYKTKKKDDDADAANANVSIAVADVAAAKKAFAPDSHVVDGVILARELVNEPPNVLYPEEFAKRAAQLRKLGVQVEILDVKAMTRLKMGALLGVSQGSAHPGRTVIMRWNGGKRGAQPVAFVGKGVCFDTGGISIKPSASMEDMKGDMGGAACVVGLMHALAARKAKINVIGAIGLVENMPDGNAQRPGDIVTSMSGQTIEIINTDAEGRLVLADVLWYVAQKHKPKFMVDLATLTGAIMVALGTDHAGLFSNNDELAERLTAAGLSTGERVWRMPLGPEYDKQIDSQFADMKNTGSRNGGSITAAQFLQRFVDNTPWAHLDIAGTAMGAPKSDINHSWGSGYGVRLLNALVAEHYEAKK
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q135P8
P0C1F5
NA13_BUNGR
Neurotoxin Bg-3
Bunodosoma
GASCRCDSDGPTSRGDTLTGTLWLIGRCPSGWHNCRGSGPFIGYCCKQ
Binds voltage-dependently at site 3 of sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. Has effect on SCN4A/SCN1B, and SCN5A/SCN1B, has no effect on SCN2A/SCN1B, and SCN10A/SCN1B. Possesses the highest efficacy for the insect sodium channel para/tipE. Also interacts with sodium channels in cardiac cells. Shows lethality to crabs .
P0C1F5
B6J9H9
PANC_COXB1
Pantoate-activating enzyme
Coxiella
MTKVIEALSDWQSIRKTINDLSVGFVPTMGNLHAGHLSLLERSKCENTITVLSLFINPTQFNDKNDFKNYPRTLAQDIAMAEENGIDYVLAPTDDALYPDQYAYKITNSTINNQEAEFRPRHFDGVLTVVMKLLLLVKPTRAYFGEKDYQQLQLVKGLAEAFFLDTEIIGCKIVRNEFGLPLSSRNRRLTEDQYQLAQRFSEIFHSDLSCDEIKNALIQEGIIVDYIEDYNERRFAAVHVGDIRLIDNIPFAKDKKC
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
B6J9H9
O52791
HMAS_AMYOR
4-hydroxyphenylpyruvate dioxygenase II
Amycolatopsis
MQNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKGDVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTGQSEFGAARR
Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.
O52791
Q679B3
NU4LM_MIRAN
NADH dehydrogenase subunit 4L
Mirounga
MTMVYANIFLAFIMSLMGLLMYRSHLMSSLLCLEGMMLSLFVMMTVTILNNHFTLASMTPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Q679B3
Q9CGY9
GRPE_LACLA
HSP-70 cofactor
Lactococcus
MSEETKEEIKNEKVDEEVTEELTEEALEDIVEEEINELDEAQKLATEWENKFLRVSAEMQNVQRRGNEERLQLIKYRSQDLAKKILSSLDNLERALAVEGLTDDVKKGLEMVQESLISALKEEGVEEVSYESFDHNIHMAVQTVPADDEHPADSIVQVFQKGYQLHERLLRPAMVVVAQ
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Q9CGY9
Q91918
RA51A_XENLA
DNA repair protein RAD51 homolog A
Xenopus
MAMQAHYEAEATEEEHFGPQAISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELLNIKGISEAKAEKILAEAAKLVPMGFTTATEFHQRRSEIIQISTGSKELDKLLQGGVETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMAESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Also involved in interstrand cross-link repair.
Q91918
B7LRJ2
NANT_ESCF3
Sialic acid/H(+) symporter
Escherichia
MSTTTQNIPWYRHLNRAQWRAFSAAWLGYLLDGFDFVLIALVLTEVQGEFGLTTVQAASLISAAFISRWFGGLMLGAMGDRYGRRLAMVTSIVLFSVGTLACGFAPGYITMFIARLVIGMGMAGEYGSSATYVIESWPKHLRNKASGFLISGFSVGAVVAAQVYSLVVPLWGWRALFFIGILPIIFALWLRKNIPEAEDWKEKHAGKAPVRTMVDILYRGEHRIANIVMTLAAATALWFCFAGNLQNAAIVAVLGLLCAAIFISFMVQSTGKRWPTGVMLMVVVLFAFLYSWPIQALLPTYLKTELAYNPHTVANVLFFSGFGAAVGCCVGGFLGDWLGTRKAYVCSLLASQLLIIPVFAIGGANVWVLGLLLFFQQMLGQGISGILPKLIGGYFDTDQRAAGLGFTYNVGALGGALAPILGALIAQRLDLGTALGSLSFSLTFVVILLIGLDMPSRVQRWLRPEALRTHDAIDGKPFSGAVPFGSAKNDLVKTKS
Catalyzes the proton-dependent transport of sialic acid.
B7LRJ2
B2GD65
EX7S_LIMF3
Exodeoxyribonuclease VII small subunit
Limosilactobacillus
MASQPKSFEEQLAKLQEIVTKLQQGNVSLNDSIELFKEGMTLSNDLKGQLNEAETTLAQMMDENGQLHPAEEKGDDVSNNGVQNQGYKSQFLDGDVF
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
B2GD65
P0CT87
GCE1_PHACR
Glucuronoyl esterase 1
Phanerodontia chrysosporium
MKSAAYLAALAAVLPAYVNAQAQEWGQCGGIGWTGATTCVSGTVCTVLNPYYSQCLPGTATTAPPPPPPPPTSVSSSSSSSTSSAPPSGPSGTSPTCSVASTIPGFSNAALPNPFVFNDGSPVQSKADFTCRQQQILALIQGYEAGALPGPPQSVTASFSKSGSTGTLSITVTDNGKSISFAPTISIPSGTPPANGWPLVIAFEGGSIPIPAGIAKLTYSNSDMAQQTDTSSRGKGLFYNLYGSGATASAMTAWAWGVSRIIDALEKTPSAQINTQRIAVTGCSRDGKGALMAGALEPRIALTIPQESGSGGDTCWRLSKAESDQGHQVQTATEIVTENVWFSTNFNNYVNNLNVLPYDHHMLMALVAPRALVSFENTDYTWLSPMSAWGCVNAAHTVFSALGVADHHGFAQVGGHAHCAWPDSLTPSLNAFFNRFLLDQNVDTNVFTTNNQFGGATWTQSSWINWSTPTLS
Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin . Can hydrolyze benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree methyl glucuronic acid (MeGlcA) in vitro .
P0CT87
Q9X405
MSMB_METHY
Methanesulfonic acid monooxygenase hydroxylase subunit beta
Methylosulfonomonas
MDIQTEMTAPPLSGGLDPAQARDAADAVRNAIYRATILLDSQKWDEWLALCADNFVYDIKAWSPEINYDMTYLHGSRKDLEALIRLLPKHNTDHSPLTRHTTIYTVDVADEGATAKGVSAFIVFQHLLDGTNSHIDAGESRLFLVGKYYDTFRIENGQALFTSRETRLENRRLDKGSHWPI
Methanesulfonate monooxygenase (MSAMO) mediates the primary degradation of methanesulfonic acid (MSA) to produce formaldehyd and inorganic sulfite by initial hydroxylation of the carbon atom prior to spontaneous cleavage of the unstable hydroxymethanesulfonic acid. MSAMO has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methane- to butanesulfonate) and excludes all larger molecules, such as arylsulfonates and aromatic sulfonates. All MSAMO components are required for enzyme activity.
Q9X405
C3KW94
PRSA_CLOB6
Foldase protein PrsA
Clostridium
MKSAKKLLSVLCLGIFILTFTACDMVEKTPEAKAKSTIAKVNGEKIQRKDLDENPRFKQVVSQMKMQYGEEFEKSEQGKEVIKEQKSQILDELITEKILLQKGKELKVIPKDEELNKEADKKVNEIKAVYNNDEKKFEETLKSTGFTKETLKEYLKDQIVIEKVINEATKDVKVEDKDAQKYYNENQSMFTEKPNTMNVSHILVKTEDEAKKVKKRLDAKEDFAKVAKEVSQDTGSKDKGGLLGDINYNDANFDPTFMKAAMALKEGAISNPVHTQFGYHIIKINSKKEYPVKKFDAVKEDIKKQLKQEKQQEAYTKKIEEWKKASKIKTYEKNLL
Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
C3KW94
Q08353
IKBA_PIG
I-kappa-B-alpha
Sus
MFQPAEPGQEWAMEGPRDALKKERLLDDRHDSGLDSMKDEEYEQMVKELREIRLEPQEAPRGAEPWKQQLTEDGDSFLHLAIIHEEKALTMEVVRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLEAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQPRGTQHLHSILQATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEDELPYDDCVLGGQRLTL
Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.
Q08353
B5RR32
EFP_BORRA
Elongation factor P
Borrelia
MSTIKSGDIDKGSFLLFKGMPHIVLEREFSKMGRGGSIVRLKLKNLKNKSVIKETLKGSDTVEEIEVLEVNSQYLYKDNESLIFMDLETYDQFSVNLRDVVNLEDKVLFLQEAEVYSLIKWGNEVIDLKLPPKVAFEVVDAEIAVKGDTVTNAMKNVTLHTDLVVKAPLFINIGDKILVNSETKEYAERVKV
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
B5RR32
P07603
PHFS_DESVH
Fe hydrogenlyase small chain
Desulfovibrio
MQIASITRRGFLKVACVTTGAALIGIRMTGKAVAAVKQIKDYMLDRINGVYGADAKFPVRASQDNTQVKALYKSYLEKPLGHKSHDLLHTHWFDKSKGVKELTTAGKLPNPRASEFEGPYPYE
May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
P07603
Q31W45
TRUB_SHIBS
tRNA-uridine isomerase
Shigella
MSRPRRRGRDINGVLLLDKPQGMSSNDALQKVKRIYNANRAGHTGALDPLATGMLPICFGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVEERPVTFSAEQLAAALDTFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITIYELLFIRHEGNELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIYLRRLAVSKYPVERMVTLEHLRELVEQAEQQDIPAAELLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTSGAPLEGLVRVTEGENGKFIGMGEIDDEGRVAPRRLVVEYPA
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Q31W45
Q8EP32
OAT_OCEIH
Ornithine--oxo-acid aminotransferase
Oceanobacillus
MTITSTNIIEETNYYGAHNYHPLPIVVSEANGVWVKDPEGNSYMDMLSAYSAVNQGHRHPKIIEALKNQADKVTLTSRAFHNELLGPWTKRMAKLTKKDKVLPMNTGVEAVETAIKAARRWAYQVKGVTENQAEIIAADGNFHGRTLNAISLSNDPDATKNYGPFVPGINKVSYGDINAIEKAITENTAAIILEPIQGEAGIIIPPEGYLKKVRELCSEKNILFIADEVQTGFARTGKMFACEWENVEPDIYVMGKALGGGVFPVSAIAANNEIMDVFTPGSHGSTFGGNPLACAVSMAAIDVIEEENLVNKSLESGKYFADKLRAVNFEGIKEVRARGLFIGMEFHQPVREICEKLKDKGILCKETHVNTIRFAPPLVITKDEMDWAIQRIEEVLTN
Catalyzes the interconversion of ornithine to glutamate semialdehyde.
Q8EP32
Q9TEZ5
CYB_GEOPI
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
null
MAIMRKSHPLMKIVNHAFIDLPTPPNISGWWNFGSLLGLCLILQISTGLFLAMHYTSDTLTAFSSVTHICRDVNYGWLIRYMHANGASLFFICLYIHIGRGIYYGSYLYTETWNIGILLLFLTMATAFTGYILPWGQMSFWGATVITNLLSAIPYIGQDLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMVHLLFLHETGSNNPLGIPSDCGKVPFHPYYSTKDFLGVIMLLMLFLTLVLFFPDKLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSVPNKLGGVVALVMSILVLALLPYLHTSKQRSLMFRPLSQTLFWMLVSDLFLLTWIGGQPVEPPFIIIGQVASIMYFSIILLLMPMAGLIENKLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q9TEZ5
Q8CWG1
PYRDB_OCEIH
Orotate reductase (NADH)
Oceanobacillus
MNLSVKLPGLNLKNPIMPASGCFGFGKEYSEYYDLSLLGGVMMKAATQFERLGNPTPRVAETSAGMLNAIGLQNPGVQQIIDHEVPRLAKYDTSIIANIAGSSIEEYEFVAASFNQTTDVDALELNISCPNVKEGGIQFGTDPFMAKKVTEVVKKASNKPVYVKLSPNVHNIVEMAKAVEEAGADGLSMINTLTGMKIHLPSRKPLIANKTGGLSGPAIKPVAIRMIYEVRQQVSIPIIGMGGITSAEDVLEYLIAGADAVAVGTANFQNPFVCVDIINELPEVLEQYGFNSIEDVIEKRGITV
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Q8CWG1
Q3YZD6
SYE_SHISS
Glutamyl-tRNA synthetase
Shigella
MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGRSPALDVTVHAIGKTRSIERINKALDFIAERENQQ
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).
Q3YZD6
C3P5L5
IF2_BACAA
Translation initiation factor IF-2
Bacillus cereus group
MSKIRVHEYAKKHNISSKDLMTKLKEMNIEVSNHMTMLDDEVVNKLDNEYQAEKPSVADEFEVEEKVVRSKKNSNKKKKKGKGNEDKRQENFAGRQQTQTVETPDKITFSGSLTVGDLAKKLSKEPSEIIKKLFMLGIMATINQDLDKDTIELIANDYGIEVEEEVIVSETEFETFIDEQDDEENLKERPAVVTIMGHVDHGKTTLLDSIRNSKVTAGEAGGITQHIGAYQVELNDKKITFLDTPGHAAFTTMRARGAQVTDITIIVVAADDGVMPQTVEAINHAKAAGVPIIVAVNKMDKPAANPDRVMQELTEYELVPEAWGGDTIFVPISAIQGEGIDNLLEMILLISEVEEYKANPNRYATGTVIEAQLDKGKGTIATLLVQNGTLRVGDPIVVGTSFGRVRAMVSDIGRRVKVAGPSTPVEITGLNEVPQAGDRFMAFADEKKARQIGESRAQEALLAQRGEKSKLSLEDLFQQIQEGDVKEINLIVKADVQGSVEAMAASLRKIDVEGVKVKIIHTGVGAITESDIILASASNAIVIGFNVRPDVNAKRTAELENVDIRLHRIIYKVIEEIEAAMQGMLDPEFEEKVIGQAEVRQTFKVTKVGTIAGCYVTDGKITRDSGVRIIRDGVVIFEGQLDTLKRFKDDVKEVAQNYECGITIERYNDLKEGDIIEAYIMEEVKR
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
C3P5L5
Q85X12
PSBB_PINKO
Protein CP-47
Pinus subgen. Strobus
MGLPWYRVHTVVLNDPGRLISVHIMHTALVAGWAGSMTLYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGIKDSWSGWNITGETVINPGIWSYEGVAGAHIMFSGLMFLAAIWHWVYWDLEIFYDERTGKLCLDLPKVFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKIQPVDPAWGAEGFDPFVPGGIASHHIAAGILGILAGLFHLSVRPPQRLYVGLRMGNIETVLSSSIAAVFFAAFIVAGTMWYGSATTPVELFGPTRYQWDQGYFQQEIDRRVRAGLAENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHPIFKDKEGNELFVRRMPTFFETFPVVLVDKEGIVKADVPFRRAESKYSVEQVGVTVEFYGGGLDRVSFGDPAIVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFSGHIWHGARTLFRDVFAGIDPDLDSRIEFGAFQKLGDPTTKRQVV
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Q85X12
Q1J904
RL14_STRPF
50S ribosomal protein L14
Streptococcus
MIQQETRLKVADNSGAREILTIKVLGGSGRKFANIGDVIVASVKQATPGGAVKKGDVVKAVIVRTKTGARRPDGSYIKFDDNAAVIIRDDKTPRGTRIFGPVARELREGGYMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Q1J904
C1CCH0
RNH3_STRZJ
Ribonuclease HIII
Streptococcus
MASITLTPSEKDIQAFLEHYQTSLAPSKNPYIRYFLKLPQATVSIYTSGKILLQGEGAEKYASFFGYQAVEQTSGQNLPLIGTDEVGNGSYFGGLAVVAAFVTPDQHDFLRKLGVGDSKTLTDQKIRQIAPILKEKIQHQALLLSPSKYNEVIGDRYNAVSVKVALHNQAIYLLLQKGVQPEKIVIDAFTSAKNYDKYLAQEANRFSNPISLEEKAEGKYLAVAVSSVIARDLFLENLENLGRELGYQLPSGAGTASDKVASQILQAYGMQGLSFCAKLHFKNTEKAKKRLER
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
C1CCH0
Q885W6
COBT_PSESM
N(1)-alpha-phosphoribosyltransferase
Pseudomonas
MSNSWWLKPAQAIDVPMREAALARQQQLTKPAGSLAQLERLAVQLSGLQGRERPAADKLWIAIFAGDHGVVAEGVSAYPQEVTGQMLHNFVNGGAAISVLARQLSAQLDVVDLGTVSPMDLPGVRHLRIGAGTANFVDGPAMTVEQGLAALQAGRDSVLRAKAVGTELFIGGEMGIGNTAAASAVACSVLECAAPLLVGPGTGLNAEGIVHKTRVIERALALHAEHAGDPLQSLFCLGGFEIAALTGAYLACAQEGIVAMVDGFICSVAALVAVRLNPSCRDWLLFGHRGAEPGHRHLLETLQAEPLLDLGLRLGEGSGAALAVPLVRLACELHNGMATFAEAAVADRPA
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Q885W6
Q06H16
MATK_DRIGR
Intron maturase
Drimys
MEELQGYLEIDGSRQQCFLYPLFFQEYIYALAHDHGLNGSILYKPMEIFGYDNKFSSLIGKRLITRMHQQNHLILSVKDSKQNLFVVPNKYFDSQMMSEVFAVIVEIPFSLRLVSSLEEKKIAKSHIRSIQSIHSIFLFFEDKFSHLNHVSDILIPHPIHLEILVQTLRCWIQDAPSLHLLRFFLYESRNSNSLIIPKKSISFFSKRNQRFFLFLYNSHIYGCESIFVFLRKQSSHLRSTSSRTLLERTHLYGKIEHFLVVLRNDFQRTLWLFKDPFMHYVRYQGKAIMASKGTHFLMKKWKYHLVNLWQCHFYLWSQPDSIHINQLYNHSFYFLGYLSRVQLNPSVVRSQMLENLFIIDTAINKFETIVPMIPLIRSLAKAKFCNVSGHPISKPARADSSDSDIIDRFGRICRNLFHYHSGSLKKQSLYRIKYILRLSCARTLARKHKSKVRAFLKRLGSGFFQEFLTEEEQVLSLIFPRTYSTSHRSHSERIWYLDIIRINDLANHE
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q06H16
A7MV12
KDSB_VIBC1
CMP-2-keto-3-deoxyoctulosonic acid synthase
Vibrio
MSFTVVIPARYASSRLPGKPLADIGGKPMIQWVYEQALQAGAEDVIIATDDKRVSAAAEQFGGKVCMTSPNHESGTERLAEVVEKMAIPADHIVVNVQGDEPLIPPSIIRQVADNLAGCDAPMATLAVEIESEEEVFNPNAVKVVADERGYAMYFSRATIPWDRDNFAKQDKTIANPLMLHIGIYAYRAGFINTYVNWQPSALEQIECLEQLRVLWYGEKIHVEVAKEAPAAGVDTPEDLESVRAIVAKQAQ
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
A7MV12
Q03749
CR7AA_BACTU
Insecticidal delta-endotoxin CryVIIA(a)
Bacillus cereus group
MNLNNLDGYEDSNRTLNNSLNYPTQKALSPSLKNMNYQDFLSITEREQPEALASGNTAINTVVSVTGATLSALGVPGASFITNFYLKIAGLLWPENGKIWDEFMTEVEALIDQKIEEYVRNKAIAELDGLGSALDKYQKALADWLGKQDDPEAILSVATEFRIIDSLFEFSMPSFKVTGYEIPLLTVYAQAANLHLALLRDSTLYGDKWGFTQNNIEENYNRQKKRISEYSDHCTKWYNSGLSRLNGSTYEQWINYNRFRREMILMALDLVAVFPFHDPRRYSMETSTQLTREVYTDPVSLSISNPDIGPSFSQMENTAIRTPHLVDYLDELYIYTSKYKAFSHEIQPDLFYWSAHKVSFKKSEQSNLYTTGIYGKTSGYISSGAYSFHGNDIYRTLAAPSVVVYPYTQNYGVEQVEFYGVKGHVHYRGDNKYDLTYDSIDQLPPDGEPIHEKYTHRLCHATAIFKSTPDYDNATIPIFSWTHRSAEYYNRIYPNKITKIPAVKMYKLDDPSTVVKGPGFTGGDLVKRGSTGYIGDIKATVNSPLSQKYRVRVRYATNVSGQFNVYINDKITLQTKFQNTVETIGEGKDLTYGSFGYIEYSTTIQFPDEHPKITLHLSDLSNNSSFYVDSIEFIPVDVNYAEKEKLEKAQKAVNTLFTEGRNALQKDVTDYKVDQVSILVDCISGDLYPNEKRELQNLVKYAKRLSYSRNLLLDPTFDSINSSEENGWYGSNGIVIGNGDFVFKGNYLIFSGTNDTQYPTYLYQKIDESKLKEYTRYKLKGFIESSQDLEAYVIRYDAKHRTLDVSDNLLPDILPENTCGEPNRCAAQQYLDENPSPECSSMQDGILSDSHSFSLNIDTGSINHNENLGIWVLFKISTLEGYAKFGNLEVIEDGPVIGEALARVKRQETKWRNKLAQLTTETQAIYTRAKQALDNLFANAQDSHLKRDVTFAEIAAARKIVQSIREAYMSWLSVVPGVNHPIFTELSGRVQRAFQLYDVRNVVRNGRFLNGLSDWIVTSDVKVQEENGNNVLVLNNWDAQVLQNVKLYQDRGYILHVTARKIGIGEGYITITDEEGHTDQLRFTACEEIDASNAFISGYITKELEFFPDTEKVHIEIGETEGIFLVESIELFLMEELC
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. This protein is not toxic in its natural form. It is highly toxic to Colorado potato beetle larvae after an in vitro solubilization and trypsin activation step.
Q03749
P10987
ACT1_DROME
Actin-5C
Sophophora
MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
P10987
Q678S2
CYB_OTABY
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Otaria
MTNIRKVHPLAKIINNLLIDLPAPSNISAWWNFGSLLAVCLALQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTLTETWNIGIILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFVVSALVMVHLLFLHETGSNNPSGISSDSDKIPFHPYYTIKDILGTLLLILILMLLVMFSPDLLGDPDNYIPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILAIIPLLHTSKQRGMMFRPISQCLFWLLAADLLTLTWIGGQPVEHPFITIGQLASILYFTILLVLMPIAGIIENNILKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q678S2
A8W3K2
PETG_CUSOB
Cytochrome b6-f complex subunit V
Cuscuta sect. Cleistogrammica
MIEPFLLGIILGLIPITLIGLFVTAYLQYRRGDQLDF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
A8W3K2
Q17423
CREC_CAEEL
Crescerin-like protein che-12
Caenorhabditis
MTSLFDALSRSNDRLPSPNFLPEDFLELLKSNDFDTKLTTLIRAATIAKREEDWFHKFQKKGELFKCIDKIICDDRWELQHQCIKFLVEAMPTFGSATEYCMCFVMPNLIPKLVSNKVTVRKITHQAIATFLRLKPEALQSFLKMLSNFMPNCNSKSELITELHHILIPELVKSNWTCLVENFTTESNIQGCEDQAGVLMKKLHYFIGNEFWQKIITNLSPEKREVLEQITANVQVEHTESKAGSGVLRASAKPQSGGERRLRFGIVPSLVCALIAEDTDANQRISGLEKMKQVVDQITPEEIARLVPHLHSYLLMLSNVLEDLNFKVVVLALDIVRATGHHLKGHMEAHIQQFVNLVAKHFGNQKSVIKQIIMMTFMELFQNINPKTVGGCLRVFLENKNSRVREEVINIYTASLMTISPSKFNLQPLVNILVPMFHDVKKRVRLAAFEQLSVLAYLLNGKTEIIMKPVRDFEQDQNSRGLTEAVTARIRRQVLPRIRYDGLIEYSTPPMMDSFDLAEAEMSLPSNADLSWIVSNGGVEPDPFERTMSPISLAGNLATIRRNRVIQQQGQAEKPSFSLPQQPAQQASHQAQRLPNGIEKSHETSENSSLDIGQRIVMTRMKSDDSFVRRQGSAASNPNSSTSSWEAPKRPPISPSEKSSISATKKEVNNNHIVKKGNLKSMRARSDTNLSEDHGEEEMENDPPRSFDDRPAKASGQYSFQDFDAAIVPSSMGKKSISHHSLPITSHPPLKHAISQPQKRINNNGTFLRSGQGQRTKSVSKPHRELTAVSKTYSLLDTSNMSVNQALKKMSSDEWADKVDGLNMISTLSETQPRMVADNLKEVIIAILNECKNLRSSVSRVAIVTIGTVAQNLNSKIDSEMEKICAVLLSKSGDVSNAFIRDDATDSLNKLVKAATAGKALQGIILAGAKSKNNTIRSSCANFVYDIITIQGSSAILNNQNALSNVLPVLLQFSRDQSPQVRNPGKQSLCFLSKDPNFDRLMRKNALESEIKAVKDVLANVEKRGGVDSLESTANLSGSLSRIGSTRRVQKKLPDSLQLDLDEIRTELLAAGWERRLTGLQRFEEMCGHASKAVASDTRLIEAFISRLGDTNGKVASCAMETYISTMGSMAKLYSTESNLKAVMNQLAHALTAHLSSKSEEHKHLARTCIQHTIRSIEPVSLLPAMTSATKKSNVKQRPFILTQYCELSKLAYKSKPKQVEVMALPLLWDSVKNSAPDVDNKKATQYLAKTLAKLIGEKQLLDLATSELDPNRKKQLDALIR
Required for normal structure and function of sensory cilia on amphid neurons, especially for the formation of distal ciliary structures, but is less important for normal assembly of middle and basal ciliary structures. Plays a role in the organization of axoneme microtubule bundles in sensory cilia. Required for normal structure and function of the ASER neuron that mediates attraction to NaCl. Required for normal chemotaxis to NaCl . Required for normal avoidance response to high osmolarity. In contrast, is not required for normal chemotaxis to isoamyl alcohol. Does not play a role in intraflagella transport (IFT) . Promotes dauer formation in response to pheromones such as the ascarosides ascr#2, ascr#3, ascr#5, ascr#8 and icas#9 .
Q17423
Q8PYZ1
SYP_METMA
Prolyl-tRNA synthetase
Methanosarcina
MAESEKEAALPPKEAFSDWYNELLWMAEIMDVRYPVKGLYVWYPFGFAIRRNTYSIIREILDNSGHQETLFPLLIPENEFMKEAEHIKGFENEVYWVTHGGKDPLDIPLALRPTSETAIYPMYKKWVRSHADFPLKLYQIVNTFRYETKHTRPLIRLREITSFKEAHTVHATWEDAEAQVKEAIGLYTEIYRRLAVPVLRSRRPDWDKFPGADYTDALDAVMPDGKTLQIGTVHHLGDNFAKTFDIKYEAPDGEQRYAHQTCYGISERSIAATISIHGDDKGLVLPPEIAPVQVVIIPIIFKKGAEEVFAACKDVQERLKKAGIRVEVDASDLRPGAKYYKWEMKGVPLRLEIGPRDLQNNVAVAVRRDTGEKDQITLLEIEAGVRLKFEAIQKSLYEKAGSELESRIFDCVDLDEVKEKIQEGVATIPWCGKRECGLAMEDHIGAGILGIPLTPRSKGKEKCPACGEETETRVYVARTY
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Q8PYZ1
Q9FR95
PEN1_ARATH
Pentacyclic triterpene synthase 1
Arabidopsis
MWRLRIGAKAGNDTHLFTTNNYVGRQIWEFDANAGSPQELAEVEEARRNFSNNRSHYKASADLLWRMQFLREKGFEQKIPRVRVEDAAKIRYEDAKTALKRGLHYFTALQADDGHWPADNSGPNFFIAPLVICLYITGHLEKIFTVEHRIELIRYMYNHQNEDGGWGLHVESPSIMFCTVINYICLRIVGVEAGHDDDQGSTCTKARKWILDHGGATYTPLIGKACLSVLGVYDWSGCKPMPPEFWFLPSSFPINGGTLWIYLRDIFMGLSYLYGKKFVATPTPLILQLQEELYPEPYTKINWRLTRNRCAKEDLCYPSSFLQDLFWKGVHIFSESILNRWPFNKLIRQAALRTTMKLLHYQDEANRYITGGSVPKAFHMLACWVEDPEGEYFKKHLARVSDFIWIGEDGLKIQSFGSQLWDTVMSLHFLLDGVEDDVDDEIRSTLVKGYDYLKKSQVTENPPSDHIKMFRHISKGGWTFSDKDQGWPVSDCTAESLKCCLLFERMPSEFVGQKMDVEKLFDAVDFLLYLQSDNGGITAWEPADGKTWLEWFSPVEFVQDTVIEHEYVECTGSAIVALTQFSKQFPEFRKKEVERFITNGVKYIEDLQMKDGSWCGNWGVCFIYGTLFAVRGLVAAGKTFHNCEPIRRAVRFLLDTQNQEGGWGESYLSCLRKKYTPLAGNKTNIVSTGQALMVLIMGGQMERDPLPVHRAAKVVINLQLDNGDFPQQEVMGVFNMNVLLHYPTYRNIYSLWALTLYTQALRRLQP
Converts oxidosqualene to arabidiol. Minor production of arabidiol 20,21-epoxide.
Q9FR95
O54942
CLD5_MOUSE
Lung-specific membrane protein
Mus
MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
O54942
Q6BPY6
QCR2_DEBHA
Ubiquinol-cytochrome-c reductase complex core protein 2
Debaryomyces
MLSRVSARSYSSAAQSIKLTAREAPGNLSTLSVVVNNAGSKAGKSGVAHLLSKYNFLNNEAKSALRFTRESELLGGIVSSDVTRDSIVLKTQFLKQDLPYFVEALGNVLTKTSFRDHELPETVLPAAKAQNAEAQGSNAFKAFESLHEISFRKGLGNPLYYDGTSPISVDEIKQFASEAYNTSNVSVFGSGVNEGDLKKFIGESAFSALPAGSSKTTPVELHNGKESRIRAAGGSVALIGVPIKTADFAKYEVLSAAIGSTYLPGSSAPLSQIPGAISKVLKYQDAGLFVICVCNSDAAVVAQGVKAAKKAVDSVSASDLSSATKAAELAVALQSRFESPVDVKIDASAAKSPAKLSEFNYVAVGNVDLLPYANEL
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Q6BPY6
Q1PG58
CYB_CYNSP
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Cynopterus
MTNIRKSHALFKLINDALIDLPAPSNISSWWNFGSLLGICLLIQILTGLFLAMHYTSDTATAFQSVTHICRDVNYGWILRYLHANGASMFFICLFLHVGRGLYYGSYIYTETWNVGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFLLPFIISALVVVHLLFLHETGSNNPTGIPSDMDMIPFHPYYTIKDMLGALIMILALLLLVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILALMPLLHTSKQRSMMFRPLSQCMFWLLVADLLTLTWIGGQPVEHPFIIIGQLASILYFLLILVLMPLVSIVENHLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q1PG58
A7MH65
TRUA_CROS8
tRNA-uridine isomerase I
Cronobacter
MSESLEKPVVKIALGIEYDGSKYYGWQRQQEVRSVQEKLEKALSQVANEPINVFCAGRTDAGVHATGQVVHFETTAIRKDAAWTLGVNANLPGDIAVRWVKDVPAEFHARFSATARRYRYVIYNHRLRPAVLSQGVTHYHLPLDAERMHRAAQCLIGENDFTSFRAVQCQSRTPWRNLMHINVERFGAYIVVDIKANAFVHHMVRNIVGSLMEIGCGNQPESWMAELLAAKDRTLAAATAKAEGLYLVSVDYPAQFELPKPPMGPLFLAD
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
A7MH65
A5U372
DER_MYCTA
GTP-binding protein EngA
Mycobacterium tuberculosis complex
MTQDGTWVDESDWQLDDSEIAESGAAPVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRAGKRR
GTPase that plays an essential role in the late steps of ribosome biogenesis.
A5U372
B4XT64
NAL1_ORYSJ
Protein SPIKELET NUMBER
Oryza sativa
MKPSDDKAQLSGLAQSEESSLDVDHQSFPCSPSIQPVASGCTHTENSAAYFLWPTSNLQHCAAEGRANYFGNLQKGLLPRHPGRLPKGQQANSLLDLMTIRAFHSKILRRFSLGTAVGFRIRKGDLTDIPAILVFVARKVHKKWLNPAQCLPAILEGPGGVWCDVDVVEFSYYGAPAQTPKEQMFSELVDKLCGSDECIGSGSQVASHETFGTLGAIVKRRTGNKQVGFLTNHHVAVDLDYPNQKMFHPLPPNLGPGVYLGAVERATSFITDDVWYGIYAGTNPETFVRADGAFIPFADDFDISTVTTVVRGVGDIGDVKVIDLQCPLNSLIGRQVCKVGRSSGHTTGTVMAYALEYNDEKGICFFTDILVVGENRQTFDLEGDSGSLIILTSQDGEKPRPIGIIWGGTANRGRLKLTSDHGPENWTSGVDLGRLLDRLELDIIITNESLQDAVQQQRFALVAAVTSAVGESSGVPVAIPEEKIEEIFEPLGIQIQQLPRHDVAASGTEGEEASNTVVNVEEHQFISNFVGMSPVRDDQDAPRSITNLNNPSEEELAMSLHLGDREPKRLRSDSGSSLDLEK
Involved in the regulation of lateral leaf growth . May be involved in the regulation of basipetal polar auxin transport (PAT) and vascular patterning in leaves . Controls photosynthesis rate by regulating carboxylation efficiency and consequently photosynthesis rate . Controls panicle and spikelet numbers, and grain yield .
B4XT64
A7ZP28
NAPA_ECO24
Periplasmic nitrate reductase
Escherichia
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQNVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSDTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEELLAKKPELRGKTLYEVLYATPEVSKYPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
A7ZP28
A5IY65
RS6_MYCAP
30S ribosomal protein S6
Mycoplasmopsis
MNKYEIMLIIDPAIDMAMANEIVESVFDKKNINKVVKLENSTLAYPINKSSKAQYVVYTLEAKSELIAEFTRRANIAKFIWRQMVINLDTEKGFQRSKKAFKHRIAKDAKVANKGTGVKQLIENLEKTMSHKAKPSFKKEVKKSN
Binds together with S18 to 16S ribosomal RNA.
A5IY65
Q03VI4
METK_LEUMM
Methionine adenosyltransferase
Leuconostoc
MAKYFTSESVSAGHPDKIADQIADAILDAVLEQDPKARSAVEVTTSTGDVSIFGELSTNAYVNIRKIATDTIREIGYNHAELGFTADSVNVSNKIVEQSGDIAQAVDNAEDDPDQLGAGDQGMVFGYATNETDSYLPLTLALSHRLMRKIRDARENEILPYLRPDAKGEVTVELDDNDKVKRIAAVVLSTQHDDEVTLEQLRADIRKHVIDEVLPQDLVDEDTIYYINPSGRFVLGGPQADSGLTGRKIIVDTYGGAAHHGGGAFSGKDATKVDRSAAYYARYVAKNMVAAGVADKLELQVSYAIGVARPVSLNVDSFGTAKVSEEKINEIITKLFDFRPLAIINNLNLRRPIYKQTAAFGHFGRTDIDLPWESLDKVKEIKNLL
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.
Q03VI4
Q24MP2
ATPE_DESHY
F-ATPase epsilon subunit
Desulfitobacterium
MAGTFTLRVVSPEGNVLKEEAEFVVLPGGNGEIGILPNHAPLISSIEIGVIRYTVNGKVEKIATSGGFVEVSDNKVTILADTAEPGEKVDLDRALAAKERAEKRLTQREGIDVRRAELALMRAVARINAARN
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q24MP2
P9WQE8
PHAS_MYCTO
Polyketide synthase pks2
Mycobacterium tuberculosis complex
MGLGSAASGTGADRGAWTLAEPRVTPVAVIGMACRLPGGIDSPELLWKALLRGDDLITEVPPDRWDCDEFYDPQPGVPGRTVCKWGGFLDNPADFDCEFFGIGEREAIAIDPQQRLLLETSWEAMEHAGLTQQTLAGSATGVFAGVTHGDYTMVAADAKQLEEPYGYLGNSFSMASGRVAYAMRLHGPAITVDTACSSGLTAVHMACRSLHEGESDVALAGGVALMLEPRKAAAGSALGMLSPTGRCRAFDVAADGFVSGEGCAVVVLKRLPDALADGDRILAVIRGTSANQDGHTVNIATPSQPAQVAAYRAALAAGGVDAATVGMVEAHGPGTPIGDPIEYASVSEVYGVDGPCALASVKTNFGHTQSTAGVLGLIKVVLALKHGVVPRNLHFTRLPDEIAGITTNLFVPEVTTPWPTNGRQVPRRAAVSSYGFSGTNVHAVVEQAPQTEAQPHAASTPPTGTPALFTLSASSADALRQTAQRLTDWIQQHADSLVLSDLAYTLARRRTHRSVRTAVIASSVDELIAGLGEVADGDTVYQPAVGQDDRGPVWLFSGQGSQWAAMGADLLTNESVFAATVAELEPLIAAESGFSVTEAMTAPETVTGIDRVQPTIFAMQVALAATMAAYGVRPGAVIGHSMGESAAAVVAGVLSAEDGVRVICRRSKLMATIAGSAAMASVELPALAVQSELTALGIDDVVVAVVTAPQSTVIAGGTESVRKLVDIWERRDVLARAVAVDVASHSPQVDPILDELIAALADLNPKAPEIPYYSATLFDPREAPACDARYWADNLRHTVRFSAAVRSALDDGYRVFAELSPHPLLTHAVDQIAGSVGMPVAALAGMRREQPLPLGLRRLLTDLHNAGAAVDFSVLCPQGRLVDAPLPAWSHRFLFYDREGVDNRSPGGSTVAVHPLLGAHVRLPEEPERHAWQADVGTATLPWLGDHRIHNVAALPGAAYCEMALSAARAVLGEQSEVRDMRFEAMLLLDDQTPVSTVATVTSPGVVDFAVEALQEGVGHHLRRASAVLQQVSGECEPPAYDMASLLEAHPCRVDGEDLRRQFDKHGVQYGPAFTGLAVAYVAEDATATMLAEVALPGSIRSQQGLYAIHPALLDACFQSVGAHPDSQSVGSGLLVPLGVRRVRAYAPVRTARYCYTRVTKVELVGVEADIDVLDAHGTVLLAVCGLRIGTGVSERDKHNRVLNERLLTIEWHQRELPEMDPSGAGKWLLISDCAASDVTATRLADAFREHSAACTTMRWPLHDDQLAAADQLRDQVGSDEFSGVVVLTGSNTGTPHQGSADRGAEYVRRLVGIARELSDLPGAVPRMYVVTRGAQRVLADDCVNLEQGGLRGLLRTIGAEHPHLRATQIDVDEQTGVEQLARQLLATSEEDETAWRDNEWYVARLCPTPLRPQERRTIVADHQQSGMRLQIRTPGDMQTIELAAFHRVPPGPGQIEVAVRASSVNFADVLIAFGRYPSFEGHLPQLGTDFAGVVTAVGPGVTDHKVGDHVGGMSPNGCWGTFVTCDARLAATLPPGLGDAQAAAVTTAHATAWYGLHELARIRAGDTVLIHSGTGGVGQAAIAIARAAGAEIFATAGTPQRRELLRNMGIEHVYDSRSIEFAEQIRRDTNGRGVDVVLNSVTGAAQLAGLKLLAFRGRFVEIGKRDIYGDTKLGLFPFRRNLSFYAVDLGLLSATHPEELRDLLGTVYRLTAAGELPMPQSTHYPLVEAATAIRVMGNAEHTGKLVLHIPQTGKSLVTLPPEQAQVFRPDGSYIITGGLGGLGLFLAEKMAAAGCGRIVLNSRTQPTQKMRETIEAIAAMGSEVVVECGDIAQPGTAERLVATAVATGLPVRGVLHAAAVVEDATLANITDELLARDWAPKVHGAWELHEATSGQPLDWFCLFSSAAALTGSPGQSAYSAANSWLDAFAHWRQAQGLPATAIAWGAWSDIGQLGWWSASPARASALEESNYTAITPDEGAYAFEALLRHNRVYTGYAPVIGAPWLVAFAERSRFFEVFSSSNGSGTSKFRVELNELPRDEWPARLRQLVAEQVSLILRRTVDPDRPLPEYGLDSLGALELRTRIETETGIRLAPKNVSATVRGLADHLYEQLAPDDAPAAALSSQ
Involved in sulfolipid-1 biosynthesis. Catalyzes the synthesis of the hepta- and octamethyl phthioceranic and hydroxyphthioceranic acids, the methyl-branched acyl constituents of sulfolipids.
P9WQE8
Q1MPS7
MNMG_LAWIP
Glucose-inhibited division protein A
Lawsonia
MRTTFDCIVVGGGHAGCEASMALARLGQKVLLITGNVDRIGHLSCNPAVGGIAKGHIVREIDALGGMMGLWADKAGIQFRTLNRSKGPAVRATRAQVDRDLYMQAVKQDIFSQPNLSVWQDTVEAIIVKDGHTGGVKTALGQLFNSQYVILTTGTFLSGLMHIGQKNFSGGRLGDVGTSKLSSSLHSIGLHLGRLKTGTTPRLLKTSIDFTSMEMQLGDTPIPSFSFHGPKPSQPQVPCYITWTNEYTHDVIRSGMDRSPMFTGVITGTGARYCPSIEDKVARFADRDRHQIFVEPEGLTSQECYINGISTSLPLDIQLALIATIPGLENAHMVRPGYAIEYDYVDPMQLHPTLETKVLPGLWLAGQINGTSGYEEAAGQGLWAALNVFCKITRQEPFILGRDNAYLAVLVDDLVTQGTKEPYRMFTSRAEYRLLLREANADIRLTPLGRKIGLVGDYQWNLFQKKISDIDTLVNRLQNIRIKPDTLDPSIFLELGESIPNRAYTLEELLKRPSITFQTLRKIYSDLPITSEDVYLETETIIKYAGYLDRQEELVQRSAKLEHSYLPKEIDYTKVAGLSSEVIEKLQIVRPQTLGQAGRISGVTPAAITCLEIYLKKIHAFR
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.
Q1MPS7
B3R1I3
RPIA_CUPTR
Phosphoriboisomerase A
Cupriavidus
MTQDELKALVAQAAADYVKQEVPEGAVLGVGTGSTANLFIDAVAAFKDRFAGAVSSSEASTRRLQQHGFKVLDLNEVDEIPVYVDGADEIDASGAMVKGGGGALTREKIVASVARRFVCIADGSKLVQTMGAFPLPVEVVPMARAAVARKLQALGGQPRLRMTKEGGIYKTDNGNVILDVAGLKIDDPRGLEQTINQVPGVVTVGLFALRGADVLLLGTGDGVQRTDY
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
B3R1I3
Q9H6Z4
RANB3_HUMAN
Ran-binding protein 3
Homo
MADLANEEKPAIAPPVFVFQKDKGQKSPAEQKNLSDSGEEPRGEAEAPHHGTGHPESAGEHALEPPAPAGASASTPPPPAPEAQLPPFPRELAGRSAGGSSPEGGEDSDREDGNYCPPVKRERTSSLTQFPPSQSEERSSGFRLKPPTLIHGQAPSAGLPSQKPKEQQRSVLRPAVLQAPQPKALSQTVPSSGTNGVSLPADCTGAVPAASPDTAAWRSPSEAADEVCALEEKEPQKNESSNASEEEACEKKDPATQQAFVFGQNLRDRVKLINESVDEADMENAGHPSADTPTATNYFLQYISSSLENSTNSADASSNKFVFGQNMSERVLSPPKLNEVSSDANRENAAAESGSESSSQEATPEKESLAESAAAYTKATARKCLLEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDTEDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSDDDDVLAPSGATAAGAGDEGDGQTTGST
Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.
Q9H6Z4
P50719
TBA_HAECO
Tubulin alpha chain
Haemonchus
MREVISIHIGQAGVQIGNACWELYCLEHGIQPDGQMPSDKSLGGCDDSFSTFFSETGSGRHVPRAVMIDLEPTVIDEIRTGTYRSLFHPEQLITGKEDAANNYARGHYTIGKEIIDLTLDRIRRLADNCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKAKLEFSVYPAPQVSTAVVEPYNSILTTHTTLEHSDCSFMVDNEAIYDICRRNLDIERPSYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATFSPVISAEKAYHEQLSVAEITNMCFEPHNQMVKCDPRHGKYMAVCLLFRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVPRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSLEDNGEEGDEY
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P50719
Q3J8Q6
RL7_NITOC
50S ribosomal protein L7/L12
Nitrosococcus
MAVAKEEILETISNMTVMDVVELIEAMEEKFGVSAAAPIAAAAPAAGAEAGAAAEEKTEFDVVLVSFGSNKVQVIKAVRSITSLGLKEAKDLVEGAPSPVKEGISKDEADEIKKQLEEAGASIEVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q3J8Q6
P83411
SDMI_SPOLI
Spodomicin
Spodoptera
VHVGPCDQVCSRIDPEKDECCRAHGYRGHSSCYYGRMECY
Fungicide.
P83411
O17907
CTG1_CAEEL
Protein ctg-1
Caenorhabditis
MLVSPTAAATSIEQQTIRDLRSIVPQIDNLNDGYVLRWLRAKEGRFDETAESLKKHVTFRNAWHLDKIEQWTPPECLEKYCGYGLLGDTEGRPILMSLLGNVDVEGLLRSVASLDYIKFSLAAIEKGMKLCEEKAKESGRPFEQMTLVFDLENITSAHFSCKQFASSFTTLVSLFQDHYPLFLRKILIIRAPEMARIAYASITAILQDPITRLVEMPSESDWKWSLAQIVNLDAWPMYWGGNLVENGDPKCPSRIKYGGGAVDESYFVDPKKAMADYDQLTTVYAGDKHLIQIKVKRPSRISWTYMTDEDDIGFEIHYDKTGSCDKLTEMETVYPYIRLECTNVPITGHLDVTDVGNYVLEFDNYYSWFSAKQLRYNIEIEDL
Vesicle trafficking protein (Probable). Functions in uterine cells to promote basement membrane (BM) mobility and BM gap formation during tissue remodeling .
O17907
C0HLS6
IBBA4_HYAOR
Bowman-Birk type proteinase inhibitor A4
Hyacinthus
WPPVEGRPSCKRCGACTRMWPPEANRCVCDDIVPQCHEGCSKCEKVDTRSGKPLYQCQSFEYYNCAA
Serine protease inhibitor . Inhibits trypsin (Ki=12nM) and weakly inhibits chymotrypsin with (Ki=460nm) . Does not inhibit bacterial subtilisin .
C0HLS6
B4HXA6
GATC_DROSE
Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial
Sophophora
MLRLLSKRFYCKIATKSNEKATKLYFKQLTHPTKVPQTPVDAEFPDTSASEIQIDTKTIQLLERLSLVDLDSERALATLKSSIQFADKIAHINTDHVRPLYTVLEHQQLQLRNDQVTEGDCRAEVLQNAKVTDEDYYVSPPGNIPLEQ
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).
B4HXA6
A4F6D0
Y254_SACEN
Nucleoid-associated protein SACE_0254
Saccharopolyspora
MQPGGQPNMQQIMEQAQKMQQQLMTAQQELAEAEVSGSAGGGLVTAVVSGSGELKSVAIDPKAVDPDDTDTLSDLVVAAVRDANRAAQELQQEKMGPVTGALGGGQGLGGLGLPGL
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
A4F6D0
Q5ATJ7
AUSA_EMENI
Methylorcinaldehyde synthase ausA
Aspergillus subgen. Nidulantes
MGSLDDNTLQQVSVLFGPKYPEVELPAGHIRRYLSNQRNANWLHDAIRDLPSVWHDILRLWPAAEKLHGDARLRQLSAFLGGGTLRPDMAEPMNFLLVPATVLRHLVDFLELKEDKNYDVCDIQGFCVGFLAAIAAACWSDNEDEFGKVVSTVLRLAVYIGAAVDLDELCEQPARSIAVRWRTAQEHKLLTEVLTRYQGAYISCVTDENAVTVTVWDSQSVSFAKELEKHGLSVKTTTLRGRFHHSNHTQAVEDILQSCERNSRLCLPSKCHKRSLPRSNINGRVCEADSLFTVAVESILTTQANWKITVTATLDNMGQSDARSIIPIGAGQFVPRHARCRMLNIVEFNKGEHINGRRKMQSATALDVGVNVTAPETTAVPIAVTGMACRYPQADSVEELWRILDLGQCTVSPMPNSRLKSGSLQREPKGPFFGNYLARPDAFDHRFFGISAREAESMDPQQRVLLQVAYEAMESAGYCGLRRSKLPDDIGCYVGVGCDDYSENVGSRNATAFSATGTLQAFNSGRISHYFGWSGPSVTVDTACSSAAVAIHLACQAIRTNDCAIAVAGGVNIMTDPRWSQNLAGASFLSPTGASKAFDADANGYCRGEGAGLLVLRPLEAALRDGDPIHAVITGTSVNQGANCSPITVPDSNSQRSLYLKALSLSGLTPDVVGYVEAHGTGTQVGDPIEFESIRKTFSGPNRATKLYVGSIKDNIGHTETSSGVAGMLKTILMIQKRRIPKQANFRRLNPRITLNERNHIEIPTQSIDWEAEKRVAMVTNYGAAGSNAAIVLREPASTPATSNSAHRETLPSHVPFYVSARTEESLRSYCEALQSTIREVAQSGTNTVQHIAYNLARKQNRDMEHFVTFPAAAGEPSELMTRLGSIASAHTQVERRSQSFHPVIICFGGQTGDTASISRNLFESCELLRFHVDECENACNALDLPSLFPAIVSPFPNKDIVNLHCVLFSIQYATAKAWLDSGLQVTRMIGHSFGQLTALCVAGGLSLIDGMRLVATRAQLIQKHWGPHTGVMLSLRASKEKVQALLDAASGHADLACLNGPDNFVVAGDEESIRRIEIIATEKGMHVELKRLKNTHAFHSRLVDAILPGLSEVANTLTFRQLDIPVEACAEQEDDWLWVTGDKIVQHSRKPVFFHDAVERTLSRVDGPCVWLEAGTASPVINMVRRVVEASRPLKSHVYLPTDLSGAQAQANLAKVTCTLWSKAVPVQFWPFHPSETGYRWINLPPYQFAKTSHWIEYNPDAFRSPPQVPDQENVQEASLVRLLRQDGKEALFTINNKDNVFRMCTAGHAVANQNLCPASLYFELVVQAALLVSSTATKPTMYHIESLNICSPLVLGMPGAVLLQLTQQDESHGQWSFVLSTRDGLQDAVTHATGRVSLQAAGSNTGICARLSSLQRLLNLASWNSIATSPSSSGLKRSTVYQAFARAVNYADYYRGVEEVYAVGHEATGRVILPSSPTKCNPCDPILIDNFIQVAGIHVNCLSETHDDEVFVCSSVGDVLIGESFVRRDTAATVPWAVYSNYEPESKKKIVCDVFVLDHTTGALAVCMLSATFTGVSIQSLKRTLNRLSNHTARPTEAEQVSINVAAEATALSSTPVAHVSSSDGDLLAVQTMLGELLGISADELSAAAALGDIGVDSLMSTEVLTEINKRFGVAISNAELTQIPDVGGLVQRIFPGHSVVRIKTHSQGAVETEITITDREPKSISVDLAPVCDTSPTAFVDKASKLFATTRTSAEFSRKTRFAGFCDTVFPQQMELVTSYVVEAFHALGADLASLTPGQVVPPVKILPQHGKVMNQLVAVLEYSDLIERRESEIIRSQQPVGTVPSLILYKKILNKHAQHASEHKLLHTTGSRLAECLSGKADPLSLLFQNAEARALMTDVYSNAPMFKSATIQLAQYLKDLLFNLGTQREIKVLEIGAGTGGTTNYLVQELAAVPGLRFQYTFTDISSSLVTLARKRFKAYDFMRYTTLDIENDPSPELQGQYDIIISTNCIHATRNLITSCTNIRRLLRPEGILCLIELTRNLFWFDLVFGLLEGWWLFNDGRSHALAHERLWDHNLRQAGFNWVDWTDNDSAESDILRLIVASSTQPFYALEGDDECEADCNTVQEQTVLYNTRDGLELFADIYYPEKTDRSGAKRPIALLIHGGGHIMLSRKEIHHEQVRMLFDMGFLPVSIDYRLCPEVSLLDGPMQDACDALAWARNKLPQLQLQRRDILPDGNNVVAVGWSTGGHLAMTLAWTAPARGVSAPEAILSFYSPTDYTDPFWSKPNFPYRVDVSTSDIQTGNPLDALQDAPISGYNPPPSKRALGGWMAPSDPRSRIALYMNWTGQTLPVLFYGCNYRARAAESGQDYEVVLPEPILSEVQKVCPFSQISAGSYRAPTFLIHGTLDDLIPVQQAQRTHDKMQACGVDSDLRIVRDGLHLFDLEANFAGNQHAFQAVVDGYEFLRRHVGL
Non-reducing polyketide synthase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN . Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A . Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE . Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 . The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide . Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol . Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation . Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional .
Q5ATJ7
Q9UXT1
GCSPB_PYRAB
Glycine dehydrogenase (aminomethyl-transferring) subunit 2
Pyrococcus
MYRQAKWDEPLIFELSRPGRVGYTLPKPIEDVDVEIPEKLKRKSPLNLPEVSEPEVVKHYTRLSEMNYGVDSGIYPLGSCTMKYNPKINEELAGHPKVAYIHPYQDERTVQGALRIMWELEQWLKEITGMDRFTLQPAAGANGEFTGVMIIKAYHLDRGETQRNEMLVPDSAHGTNPASAAMAGFKVIEIPSNENGTVDLEALENAVSERTAGLMLTNPNTLGIFEDEIEEIAKIVHKAGGLLYYDGANLNGILGKVRPGDMGFDIVHLNLHKTFSTPHGGGGPGAGPVGVKEFLKDYLPVPLVSYDEENDRYYLDYDVPKSIGKVKELFGNFAVLVRALTYLKVMGKDGLREVSEVAVLNANYLARKLKGTRGYELPHKELRKHEVVFSAEPMKRETGVRTLDVAKRLLDFGMHAPTIYFPLIVHEALMIEPTETVSKEELDAYVEAMKKISEEAYTNPEVVKSAPHNTAVRRVDDVLASKKPIITWKMYKELKEKGEVDY
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Q9UXT1
Q18B66
EX7L_CLOD6
Exodeoxyribonuclease VII large subunit
Clostridioides
MKLRALDISEANSYIKRILINDPILSNLKVKGEISNFKVHSSGNVYLSLKDETSKLNCVIFKSNFNRNLKLDNGVKIIANGYISVYERDGAYQLYINEIEIEGIGNLHIEFNRLKEKLNKEGLFDPKYKIPIPKMPNSIGVITSPTGAVIRDIINVIKRRYPKVNIKLYPVTVQGDKSAEEICEAIRFFNHMKNVDTLIVGRGGGSIEELWSFNDEMVAREVFNSQIPIISAVGHETDFTICDFVSDMRAPTPSAAAEIATPSLDDINYKLGNIKSRMSKSLTNQIELDQYRLETVFNKINNYLDSYTIKDKVIQLDKIYDKIIFGIENNLKLEDEKLVKIGALLHNLSPLATMDRGYSITQKNGKVINSIKGLKIKDSIDIVLKDGNLECMIDKIENKEG
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q18B66
B1YK70
GLGA_EXIS2
Starch [bacterial glycogen] synthase
Exiguobacterium
MKVWFAATEATPFIKTGGLADVVGSLPLALAEEGAEVSVILPNYGQIKEQYKLEMEFLFDFIVPVGWRQQFGAVLRLKQDGVTFYFIDNEYYFKRDGVIYGHYDDAERFAYFSRAVLEMIQRVDAEEVPDVIHCHDWQTGVLPAFLRIHYQHLNRYQEIKTVFTIHNLQYQGVFPEEVLGDLLGLSHEHFTAEGIAHNGLVNYMKAGLVHANQITTVSPSYRDEIMDPYYGETLEPVLQHRAVDVRGILNGIDYRQFSPETDEHLVENYDVKTVEEGKAANKAALQQELGLPVNPDVPLFGFVSRLVDQKGIDLLAHILPDLFELDAQFIILGSGEAEYEGLFQHASTIRPDKVASYIGFDVGLAQRIYAGSDAFLMPSRFEPCGLSQLISMKYGSLPIVRETGGLRDTVQPFNQFTLEGNGFSFSNYNAQEFLDAIKRTIETYHDKPVFKHLIETAMQEDFSWIRSADEYLALYRLIAPSAD
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
B1YK70
B0VX69
SETD3_CALJA
SET domain-containing protein 3
Callithrix
MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEEEVRYLQSTQAVHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDNAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNQDLSVRAKMAIKLRLGEKEILEKAVKSAAVNREYYRQQMEEKAPLPKYEESNLGLLESSMGDSRLPLVLRNLEEEAGVQDALSIREAISKATATENGLVNGENSIPNGTRSEDENLNQEESKRAVEDAKGSSSDRADAVKE
Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin.
B0VX69
D5BW25
FTSW_NITHN
Peptidoglycan polymerase
Nitrosococcus
MSRFFSTRQAVGGSTPQPDLYLLGAAVALMGLGWVMVGSASVAIADSRFGQPTYYLWRQGLFLLLGLVTAFGVWRIRLAFWEKLGPVMLLLGLGLLLLTLIPGIGVEVNGSRRWLALGPIRLQPSELAKLFMVIYLSGYLVRRSAEVRTIRGFLFPVGVFAMAGLLLLLEPDFGAVVVLFATLLGMLFLGGARLWHFLLLAALGGASLAALAWYSPYRMQRLTSFLDPWADPLNSGYQLTQALIAFGRGEWLGVGLGNSIQKLFYLPEAHTDFLYAVLAEELGLMGSLAVIALFVVFIYRVLLIGRAAERAGRTFGAHLAYGLGIWIGLQAFINLGVNMGVLPTKGLTLPLMSAGGSSSIVTCVAVALILRVDLETRFPKVARRSVK
Peptidoglycan polymerase that is essential for cell division.
D5BW25
Q0BPG3
RBFA_GRABC
Ribosome-binding factor A
Granulibacter
MSSRPPSSSGPAGIPKGAPSQRQLRVAEEIRHVLAGVFARQEFRDPELATTTFTINEVRISPDLKHATVFISRLGSSEIEPLLPNLKRVATYLRGEVAKVMRLRYAPELHFQPDSALEYAMHVDSLLRRPEVKRDLDE
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.
Q0BPG3
Q8A1A2
RHAA_BACTN
L-rhamnose isomerase
Bacteroides
MKKEEMIQKAYEIAVERYAAVGVDTEKVLKTMQDFHLSLHCWQADDVTGFEVQAGALSGGIQATGNYPGKARNIDELRADILKAASYIPGTHRLNLHEIYGDFQGKVVDRDQVEPEHFKSWIEWGKEHNMKLDFNSTSFSHPKSGDLSLSNPDEGIRQFWIEHTKRCRAVAEEMGKAQGDPCIMNLWVHDGSKDITVNRMKYRALLKDSLDQIFATEYKNMKDCIESKVFGIGLESYTVGSNDFYIGYGASRNKMVTLDTGHFHPTESVADKVSSLLLYVPELMLHVSRPVRWDSDHVTIMDDPTMELFSEIVRCGALERVHYGLDYFDASINRIGAYVIGSRAAQKCMTRALLEPIAKLREYEANGQGFQRLALLEEEKALPWNAVWDMFCLKNNVPVGEDFIAEIEKYEAEVTSKR
Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
Q8A1A2
B7IPS5
PPAX_BACC2
Pyrophosphatase PpaX
Bacillus cereus group
MRINTVLFDLDGTLINTNELIISSFLHTLNTYYPNQYKREDVLPFIGPSLHDTFSKIDESKVEEMITSYREFNHDHHDELVEEYETVYETVRELKKQGYKVGIVTTKARQTVEMGLQLSKLDEFFDVVVTIDDVEHVKPHPEPLQKALELLDAKPEEALMVGDNHHDIVGGQNAGTKTAAVSWTLKGRAYLEAYKPDFMLDKMSDLLPILSNMNRS
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
B7IPS5
Q4QN63
ATPG_HAEI8
F-ATPase gamma subunit
Haemophilus
MAGAKEIKTKIASVQSTQKITKAMEMVATSKMRKTQDRMAASRPYSETIRNVISHVSKASIGYKHPFLVECEVKKIGILVISTDRGMCGGLNVNLFKTTLNQIKNWKEQNISTDLGLIGSKGISFFRSFGFNIKGQLSGLGDTPALEELIGVANTMFDAYRNGEIDAVYIAYNKFVNTMSQKPVVQQLVPLPESKDDHLNERQQTWDYLYEPEPKALLDSLLVRYLESQIYQAVVDNLASEQAARMVAMKAATDNAGNLINDLRLVYNKARQASITNELNEIVAGAAAI
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.
Q4QN63
A4SIZ9
RL9_AERS4
50S ribosomal protein L9
Aeromonas
MQVILLDKIAKLGGLGDQVAVKAGYARNYLIPQGKAVMATKANIETFDARRAELEAKLAAGKAAAEERAAKLGELAAVVIASKAGDEGKLFGSIGTRDVADAITAAGVAVAKSEVRMGNVLRNTGEYEVVVQLHADVKATVQVQVVAL
Binds to the 23S rRNA.
A4SIZ9
Q2S0U5
PDXJ_SALRD
Pyridoxine 5'-phosphate synthase
Salinibacter
MTNLLINVDHVGTLRNAREETFPDPVHAAARCEQAGADGIVFHLREDRRHITERDVRLLAETVNGKLDFELSTEEEVVSICCDVVPDLATLVPERREEVTTEGGLDVTASRPRLNAVTDRLYDAGVDQVSLFVDPVPAQIEATAAVGANCVELHTGDFAEASTEAARREEAERLAAAADAAHEAGLRVHAGHGLDYNNFSLFRETVPHVAEVSIGFAVMARAILVGMDQAVRDMRATVANAQP
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.
Q2S0U5
Q6LVB2
RS19_PHOPR
30S ribosomal protein S19
Photobacterium
MPRSLKKGPFIDLHLLKKVEKAVESGDKKPVKTWSRRSMIIPQMIGLTIAVHNGRQHVPVFVSEEMIGHKLGEFAPTRTYRGHAADKKAKKR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q6LVB2
Q46HR0
RBFA_PROMT
Ribosome-binding factor A
Prochlorococcus
MANSRRVEKLAALLKREVSELLVNGIRDERIHQAMITITSVEVSGDLQHAKIFISLFGEEKKKDEVLVGLEEAKGFIRAELAQRLQMRRSPELVFKIDKGMTKGPAVLDLLNALELERKSKDL
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.
Q46HR0
Q6AFJ7
COAD_LEIXX
Pantetheine-phosphate adenylyltransferase
Leifsonia
MHRIAVVPGSFDPVTLGHLDVIERAARMWDEVHVLVVHNPDKSALLPIAQRVALLDRSIEDAGIAGNIVASWSVGLLVDYCTDIGAHVLVKGIRSQVDVAYETPMAIVNRHLAEVETVFLLPNPANAHVSSSLVRQVASLGGDVSPYVPAAVSELLSSS
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Q6AFJ7
Q5SHT5
MUTS2_THET8
Endonuclease MutS2
Thermus
MRDVLEVLEFPRVRALLAERAKTPLGRELALALAPLPREEAEKRHELTGEALSYPYALPEAGTLREAYGRALAGARLSGPELLKAAKALEEAMALKEELLPLKNALSQVAEGIGDHTPFLERVRKALDEEGAVKDEASPRLAQIRRELRPLRQQILDRLYALMDRHREAFQDRFVTLRRERYCVPVRAGMAQKVPGILLDESESGATLFIEPFSVVKLNNRLQALRLKEEEEVNRILRDLSERLAKDEGVPKTLEALGLLDLVQAQAALARDLGLSRPAFGERYELYRAFHPLIPDAVRNSFALDEKNRILLISGPNMGGKTALLKTLGLAVLMAQSGLFVAAEKALLAWPDRVYADIGDEQSLQENLSTFAGHLRRLREMLEEATSHSLVLIDELGSGTDPEEGAALSQAILEALLERGVKGMVTTHLSPLKAFAQGREGIQNASMRFDLEALRPTYELVLGVPGRSYALAIARRLALPEEVLKRAEALLPEGGRLEALLERLEAERLALEAERERLRRELSQVERLRKALAEREARFEEERAERLKALEEEVRAELLKVEAELKALKEKARTEGKRDALRELMALRERYAKKAPPPPPPPGLAPGVLVEVPSLGKRGRVVELRGEEVLVQVGPLKMSLKPQEVKPLPEAEPGKPLLAKPRREVKEVDLRGLTVAEALLEVDQALEEARALGLSTLRLLHGKGTGALRQAIREALRRDKRVESFADAPPGEGGHGVTVVALRP
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. Cleaves the phosphate backbone of oligodeoxynucleotides non-sequence-specifically at the 3' side of the phosphates. Preferably incises the branched DNA structures, especially the D-loop structure over the Holliday junction. Has ATPase activity. Binds to dsDNA but not to ssDNA.
Q5SHT5
B1VAE7
RL4_PHYAS
50S ribosomal protein L4
16SrXII (Stolbur group)
MPKYNVINQLGDLISTKDLKSNVFDIQPHQQALYDVINAQRAAMRQGTHATKTRAFVSGGGKKPWRQKGTGRARHGSIRSPLWRGGGVVFGPSPRNYSVKVNQKVSHLALKSALSSHFRQNQLILVDDFNLDTHKSKDFQKTLQKLNVTSKALIIVTNSNRNLTLASRNLPYVTLETAAHASVYQILNCKNLILTLDAVAYFEEVLK
Forms part of the polypeptide exit tunnel.
B1VAE7
Q54XW7
GACB_DICDI
GTPase activating factor for raC protein B
Dictyostelium
MTDQTLRLENVSPYLLLILDYFEKNCINKTDLFSIQGNQENVNRIISNIKNFTPTKQFEKDLNRGLYSRHDLSFSIINILNSLNHPLLLENYNEAYIVNAYYEDIERIKQTLLELPHSNLEIILKLFSTFNLLCNQEEHKSFLLLSPEMLGETFAFVLMRFKKTKDEVDQFGNKIFATNVISYLISHFNEIFDSTILDFEQKEKKSRENAILFMEYAMRKYTSLDNHFKSIYNKYIPHKRDLSQEDVQTIKTEFNLRKYSGKSKIRPPIPIYM
Rho GTPase-activating protein involved in the signal transduction pathway.
Q54XW7
A7H8E6
SECA_ANADF
Protein translocase subunit SecA
unclassified Anaeromyxobacter
MVNYVLRKMLGTKNERELKRLRPLVARVSELEPRMKALSDADFPRLTAEWKQQVRNGRPLDDLMPEAFALVREAGVRALGMRHFDVQLIGGAVLHSGRIAEMKTGEGKTLVATLPSVLNALSGRGVHVVTVNDYLARRDSEWMGRLYRFCGLTTGVIVHGLTDRERQDAYHSDITYGQNNEFGFDYLRDNMKFRLQDYVQGELNFAIVDEVDSILIDEARTPLIISGPSDESSDLYYRVNQVIPSMIRDQDFTVDEKSRTIVMSDSGVEKMEKKLGVQNLYDPNAIETLHHVEQALRAHHLYRNEVDYVVKNGEVLIVDEFTGRLMPGRRWSDGLHQAVEAKEGVKIEAENQTLATISFQNYFRMYSKLAGMTGTADTEAEEFAKTYNLDVVVVPTNKKNVRKDSEDVVYKTEREKFGALCDEIETRHKKGQPVLVGTVSVAKSEVVSSLLKRRGVPHDVLNAKHHQREAEIVAQAGRKGSVTISTNMAGRGTDIILGGNAEMMAKHEVGPEPDLPMEGEAEESFLARKQEWARRLEETRERLRGQTATEHDEVVALGGLHIVGTERHESRRIDNQLRGRAGRQGDPGSSIFYLSLEDELMRIFGSERIQGLMSRMGMKEGEQIEHPWLTKAIEGAQKKVEGHNFDIRKNLLEYDDVMNQQRRSVYRLRRMVLGFGAGVPVVEYDEEPKTRKKTRREQVFTWGDQREHVLDLIEDLVFDMVGASCPNRLSDWNLDGLSSMVKEQFGVEMKFAPPSGKAADARREIEEQVYAVVEKAYRQKEEELGIGPDGEPVLRRYEQWLYLQAIDQQWKDHLLSMDHLRQGIGLRGYGQKDPKQEYKKEGYEMFVQMTWRVKSAVIGNLLRLQLVRQETAEEIEQKRLAAQRRAMQRITETHAAAAGDGEEKPRPKQETVVRTQPKVGRNDPCPCGSGKKYKKCHGATEAAV
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.
A7H8E6
Q9FJ17
DI197_ARATH
Protein HYPERSENSITIVE TO RED AND BLUE 1
Arabidopsis
MDSNSWINCPPVFSSSPSSRRYQSRSDLYLGDVEGEDDLKAEFMCPFCADEFDIVGLCCHIDVNHPVEAKNGVCPVCTKKVGLDIVGHITTQHGNVFKVQRRRRLRKGGYSSTYLTLKKELREANLQSLGGSSTFIPSSNIDSDPLLSSFMFKPPSAIPITEGDSVAQVSPKDTSKSKIQQESFSNEDQEKAKKSKFVRGLLWSTMLEDKF
Involved in both red and blue light signaling.
Q9FJ17
Q8PPY3
GLNE_XANAC
Adenylyl transferase
Xanthomonas
MPMPTVSMSPALTALIERAVARVRQSLPVEQAWPGGEFDRQLAQVALASEFALDTLARQPALLQHLAQPDPPPLPLPQFDPAQPQLWPAQLRRYRSAESTRLVWRDVLGLDSVEATLAGATQLAEHCLQCGLQALEQQFHTRHGKVVAADGSVQRLVVFGLGKLGGGELNFSSDVDLVYAYPQGGQSDGARPLAAEEYFARLGQQLARLLDETTADGFSHRVDLRLRPFGTAGRVALSFAGMDQYFQREGRDWERYAWLKARAVAGDIDAGEAWLETLRPFVYRRYLDFTALDGLREMKAAITAEVARHDRLDDIKRGPGGIREIEFLAQSLQLIRGGREPSLRERRLLPALQALVAAGQIDQENGQALSTAYRFLRRLENRLQMLRDAQTHALPQAPLDRERIALGLGYAQWSALLDALAPQRARVAAEFAELLAPRVRATAPDALADYWRALPDGDAAPLAGIGLNDPDGAHRALADFAQSSGVRALSDSARARLDRVMPALLHAATRASQPDAAVRRMLGLLQATLRRTSYLALLDEQPSALARLVDVLSRSALLAERLAAYPLLLDELLDTRISGPLPDRAALHAACAHTLHIDDTEAALRELNERRLALSFRIALATLDGRQQAVESTRQLAWLAEAVVQTVLHLARSDMLAAHGHVPGGSFAIVGYGSLGGLELGFGSDLDLVFLYDHPREVDASDGKRPLDAGRWFARLAQKVMALLAAETGAGRLYDIDVRLRPDGGKGALVSSLASYREYQRDRAWTWEHQALVRARAVAGDAALCDAFAQVRRDTLMRVRDTAQLHEDVRKMRARMRAELDRSDAGRLDLKQGAGGLVDLEFVLQAGVLGLAAQQPQLLDACDTPALIDALARTHWLPDESAAPLHQAHATLVDAGLSCTLDRRPRLIAPTPAIQQARGIIFNAARGQGLTFPLGKDETAL
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Q8PPY3
P17180
PER3_ARMRU
Peroxidase C3
Armoracia
MGFSPLISCSAMGALILSCLLLQASNSNAQLRPDFYFRTCPSVFNIIGDIIVDELRTDPRIAASLLRLHFHDCFVRGCDASILLDNSTSFRTEKDAAPNANSARGFGVIDRMKTSLERACPRTVSCADVLTIASQISVLLSGGPWWPVPLGRRDSVEAFFDLANTALPSPFFTLAQLKKAFADVGLNRPSDLVALSGGHTFGRAQCQFVTPRLYNFNGTNRPDPTLDPTYLVQLRALCPQNGNGTVLVNFDVVTPNTFDRQYYTNLRNGKGLIQSDQELFSTPGADTIPLVNLYSSNTFAFFGAFVDAMIRMGNLRPLTGTQGEIRQNCRVVNSRIRGMENDDGVVSSI
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.
P17180
Q2S9Y9
MRAY_HAHCH
UDP-MurNAc-pentapeptide phosphotransferase
Hahella
MLVWVADFLAQYFSIFSVFQYLTLRAILGVLTALLISLLVGPVMIRKLSYYQIGQAVRDDGPESHFSKAGTPTMGGALILVAIAVSTLLWADLTNRYVLITLGVTLLFGAIGWVDDWRKVVERNPKGLPARWKYFWQSVFGFGAAVLLFKTAHLPQETTLIVPFFKDITLALGVGFVLLTYFVIVGGSNAVNLTDGLDGLAIMPTVMVGGALAVFAYLSGHVKFAEYLHIPYLPGTGELVIFLGALVGAGLGFLWFNTYPAQVFMGDVGALALGAALGVVAVIVRQELVFFVMGGVFVMETVSVILQVASYKLTGRRIFRMAPLHHHFELKGWPEPRVIVRFWVITVVLVLVGLATLKIR
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.
Q2S9Y9
A6MMW2
PETL_ILLOL
Cytochrome b6-f complex subunit VI
Illicium
MPTITSYFGFLLAASTITPALLIGLSKIRLI
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
A6MMW2
Q32L48
H2B1N_BOVIN
Histone H2B type 1-N
Bos
MPEPSKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGNMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Q32L48
P22322
GPR_BACSU
Spore protease
Bacillus
MKKSELDVNQYLIRTDLAVETKEAMANQQAVPTKEIKGFIEKERDHGGIKIRTVDVTKEGAELSGKKEGRYLTLEAQGIRENDSEMQEKVSAVFAEEFSAFLENLNISKDASCLIVGLGNWNVTPDALGPMAVENLLVTRHLFKLQPENVQEGYRPVSAFAPGVMGITGIETSDIIKGVIEQSKPDFVIAIDALAARAVERVNTTIQISDTGIHPGSGVGNKRKDLSKDTLGVPVIAIGVPTVVDAVTIASDTVDYILKHFGREMKDNRPSRSLVPAGMTFGKKKVLTEDDLPDQKQRQSFLGIVGTLQEDEKRQLIHEVLSPLGHNLMVTPKEVDSFIDDMANVLANGLNTALHEKVSQENKGSYNH
Initiates the degradation of small, acid-soluble proteins during spore germination.
P22322
Q5CB04
B3GA1_PANTR
UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
Pan
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCMSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSSQPGVVYFADDDNPYSLELFQKVTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group.
Q5CB04
Q92QG3
RL16_RHIME
50S ribosomal protein L16
Sinorhizobium
MLQPKRTKYRKQFKGRIKGVAKGGSDLAFGEFGLKAQEPNRVNAREIEAARRAITRHMKRAGRVWIRVFPDVPVTAKPTEVRMGKGKGSVEYWACKVKPGRMMFEIDGVNEELAREALRLGAAKLSVKTRFVQRIAE
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Q92QG3
Q30WB0
ACKA_OLEA2
Acetokinase
Oleidesulfovibrio
MNVLVINAGSSSCKYQLINMESEGVLCAGLVERIGEATGKLAHKIAPDTDSEEKIVLEQPFPNHVEAMKKVVELITDPEKGVIKDKSEIYAIGHRVLLGGEEIKESVKIDEWAKGVIRDYIPLGPLHNPANLAGIEVAEELFPGVPSVGVFDTEFHQTMPAKAYLYPLPLELYEEMKIRRYGFHGTSHRYVTKKTAEFLGKPLDEVNIITCHLGNGCSMAAVKNGKCVDTTMGITPLEGLMMGTRCGDIDPAIVPFLMEKKGLTTAEADTLMNKQSGLKGVCGMNDMRDIHAAVEKGDEKAKLALDMFVYRIKKYIGAFYAALGRVDAVVFTAGIGENDDIVRAEVCENMDVFGIALDAEKNKIRSGEPRNIAAENSKVAVLVVPTNEELEIAQAAVNVLKG
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Q30WB0