accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
B2Y1X2 | CYF_WELMI | Cytochrome f | Welwitschia | MEKRNTYDWVTRWVIASFSILTISYMITWTSISNAYPIFAQKSYESPREATGRIVCANCHLAKKSVEIEVPQSVLPNSVFEAIVKIPYDTQIKQVLANGKKGGLNVGAVLILPEGFELAPSDRISPEIKQKIGNLNFQNYSPSQKNILVIGPIPGQKYREIVFPILSPDPATKKEVNFRKYPIYVGGNRGRGQVYPDGSKSNNTVYNASATGRVSQILRKDKGGYEVTIENISQGRSVVDIIPPGPELLVSEGDFVKVDQPLTNNPNVGGFGQVNAEIVLQDPFRIQGLLVFLASVVLAQIFLVLKKKQFEKVQLAEMNF | 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. | B2Y1X2 |
Q9EV79 | 6PGL_PSEPU | 6-phosphogluconolactonase | Pseudomonas | MGGRGMGISELKLPAAVKVHELADAKTLAATLAHDVAERLRAAIAAKGQACVVLSGGRSPVPFLEKLASEPLDWAKVTVSLADERWVPVEHADSNAGLLARHLLTGAAAKARFVGLYQQAENLDAAALKADQALTGLPPIDVLVLGMGDDGHTASLFPASPNLEAGLDLASTRRCLPLLAPSVPHQRLSMTRSLLASAAFIALSVQGPGKLATLRAALAGNDLTEMPIRAFLHDPLDIYWCP | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. | Q9EV79 |
Q8DEK8 | MURD_VIBVU | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Vibrio | MDRWQDIKQVVVVGLGITGLSVVRHLRKTQPQLQVKVIDTRPTPPGVEQLPPDIALHVGSWNDAWLAEADLVVTNPGIALATPQIQTVLARGVAVVGDIELFAWAADKPVIAITGSNGKSTVTDLTGVMANACGVKCAIGGNIGVPALDLLEQEVELYVLELSSFQLETTSSLHLVAAAFLNLSEDHMDRYQGMDDYRQAKLRIFQHAKHGVVNRDDRQTYPETSHGQQSLALVTFGSDDKEFGVISHQGESWLSYNQQPILASRELKLVGQHNVANVLVVLALLTCAGIDYRKGLSALKSYTGLTHRCQVVADNRGIKW... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | Q8DEK8 |
A0PXW1 | RL6_CLONN | 50S ribosomal protein L6 | Clostridium | MSRVGRLPIEIPNGVNVTVTPENVVTVKGPKGELTKAMHEDMNIAVEENNIVVTRPSENVQHKALHGLTRALINNMVVGVTQGYEKTLELVGVGYRAQLKGKDLTLNLGYSHPVEIKAVKGVEYKVPEPTKVVVSGIDKELVGSVAANIRVWRKPEPYKGKGIKYAGEVIRRKEGKTGK | 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. | A0PXW1 |
P61411 | THIE_GEOSL | Thiamine-phosphate pyrophosphorylase | Geobacter | MAKVDFSLYLITDRHQAGGRDLLAVVEGALAGGVRCVQLREKDLPARTLLELARAMRRLTDRFGARLLINDRVDIALAAGADGVHLGEEGMPAAVARELLGSGRLIGVSCHGRGGAAAAVAQGADFITFGPVYPTPSKAAYGEPVGIDQLAATTKEIHIPVFALGGIKEANIPEALAAGAAGVALISAIIADPDPRERARALLALLPPRTRDE | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | P61411 |
B1L838 | LEXA_THESQ | LexA repressor | unclassified Thermotoga | MKDLTERQRKVLLFIEEFIEKNGYPPSVREIARRFRITPRGALLHLIALEKKGYIERKNGKPRALRVSKSIRNKIPLIGEIRAGEKREAIEYLEDYIEIPESFLSSGYDHFLLKVKGESMIEEHICDGDLVLVRRQDWAQNGDIVAAMVDGEVTLKKFYQRGDTVELRPANREMSSMFFKAEKVKILGKVVGVFRKL | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair... | B1L838 |
Q4ZWQ0 | SURE_PSEU2 | Nucleoside 5'-monophosphate phosphohydrolase | Pseudomonas syringae | MRILISNDDGVNAPGLVALHAALADYADCVVIAPDQDKSGASSSLTLDRPLHPHTLENGFISVNGTPTDCVHLGIHGLLERQPDMVVSGINLGANLGDDVLYSGTVAAALEGRFLQRPSFAFSFLSRQPDNLATAAHYARLLVEAHEQLDLPPRTVLNVNIPNLPLEHIRGIQLTRLGHRARAAAPIRVVDPRGRAGYWIAAAGDVEDGGAGTDFHAVVQGYVSITPLQLDRTCQDGFSSLNTWLEGLR | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | Q4ZWQ0 |
Q0I6K7 | RL11_SYNS3 | 50S ribosomal protein L11 | unclassified Synechococcus | MAKKVVAVIKLALQAGKANPAPPVGPALGQHGVNIMAFCKEYNARTQDKAGYVIPVEISVFEDRSFTFITKTPPASVLITKAAGIQKGSGESAKGSVGSINRSQLEEIAKTKLPDLNCTSVESAMRVIEGTARNMGVAISD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q0I6K7 |
Q3B6W8 | ATPB1_CHLL3 | F-ATPase subunit beta 1 | Pelodictyon | MQEGKISQIIGPVVDVDFPEGQLPSILDALTITRPDGSRLVLETQQHLGEERVRTVAMESTDGLIRGLSVANTGRPIQAPVGEGVLGRMLNVVGDPIDGRGPVNATKTYSIHRSAPKFEDLSTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINNIAKQQSGYSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARARVALTGLSIAEYFRDEEHRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQDRITSTKNGSVTSVQAIYVPADDLTDPAPATAFAHLDA... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q3B6W8 |
Q2IJA7 | IHFA_ANADE | Integration host factor subunit alpha | Anaeromyxobacter | MTKADIIESVYEKVGFSKKEAAEIVEMVFDTIKETLERGEKIKISGFGNFIVRDKKSRVGRNPQTGEEIEISARRVLTFRPSQVLKNALNGGVSDETEGADDDDDDEEGEGDE | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. | Q2IJA7 |
P00782 | SUBT_BACAM | Subtilisin Novo | Bacillus amyloliquefaciens group | MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNK... | Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin. | P00782 |
P07367 | LHA2_RHOCA | LH-2 | Rhodobacter | MNNAKIWTVVKPSTGIPLILGAVAVAALIVHAGLLTNTTWFANYWNGNPMATVVAVAPAQ | Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. | P07367 |
Q08478 | PIT1_ONCMY | Growth hormone factor 1 | Oncorhynchus | MSCQAFSADSFTTLAGDSLPLLMHHASAADCLPSSASTHTHNMVSAVPSGLSLLQSSKRSHMHLSTSTLGNALSNGPPGLHYPVTPCHYSNQQTTYGMMAAQEMLSASISQTRILQTCSVPHPNMVNGANTLQGSLAPCLYKFPEHGLGGGSCSLSHSFPPLPPAVLSEEPPLGGTKDLRLRSRPPDDPPDMDSPQIRELEKFANDFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACTLKAILAKWLDEAEQAGALFNEKMGMNERKRKRRTTISLGAKEALERSFGEKIKPSSQEIVRMAEGLH... | Transcription factor that activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'. | Q08478 |
Q1IIY8 | ARGR_KORVE | Arginine repressor | Candidatus Koribacter | MSKLSRHAAIRDAITSHPVQNQDELRRLLFKRGHRVTQATLSRDIHELGLVKTGEGYQFPSSEDDSNAAWLPSVERLIREFVYDVKIAQNTVVVKTSAGSAQPVAAALDAEGWPEVVGTVGGDDTIFVVTPSNKDAEKLQSRIKELIA | Regulates arginine biosynthesis genes. | Q1IIY8 |
P31339 | ASPA_AERSA | Microbial serine proteinase | Aeromonas | MRKTSLALAISALLSALPIASVQANESCTPLTGKEAGLDTGRSSAVRCLPGINPLQDLLNSGQNAFSPRGGMAGNDLNLWWAHRTEVLGQGINVAVVDDGLAIAHPDLADNVRPGSKNVVTGGSDPTPTDPDRCPRHSVSGIIAAVDNSIGTLGVAPRVQLQGFNLLDDNIQQLQKDWLYALGQRRHRRQPGLQPELRMSLVDPEGANGLDQVQLDRLFEQRTQHASAAYIKAAGTAFSRIAAGNYVAQPHRNLPKLPFENSNIDPSNSNFWNLVVRAINADGVRSSYSSVGSNVFLSAPGGEYGTDAPAMVTTDLPGCD... | Agent of furonculosis. | P31339 |
A7MQK4 | CYAY_CROS8 | Iron-sulfur cluster assembly protein CyaY | Cronobacter | MNDSEFHRLADGLWMTIEERLDAWDGDSDIDCEINGGVLTLSFENGSKIIINRQEPLHQVWLATKQGGYHFDYKNDEWICDRSGERFWDLLETAATQQAGEAVSFR | Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | A7MQK4 |
Q6D4E2 | POTA_PECAS | Spermidine/putrescine import ATP-binding protein PotA | Pectobacterium | MICQIRKQSYTLMKENSLTVPVVELLNVHKGFDGKDIISHFNLTINNGEFLTILGPSGCGKTTVLRLIAGLETVDSGNIMLEKQDITHQPAEQRHVNTVFQSYALFPHLSVFENVAFGLRMQKTPAVEMTPRVIEALKMVQLDELAQRRPHQLSGGQQQRVAIARAVVNQPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFIFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDAIVLDLLDEQRVRALVEGHECVITVSFLVNIGQHLNVLLRPEDLRVEELGDGMQAEGMVG... | Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. | Q6D4E2 |
Q89ZG0 | RNY_BACTN | Ribonuclease Y | Bacteroides | MIAIIATAIACFVVGGILSYVLFRYVLKSKYDSVLKDAETEAEVIKKNKLLEVKEKFLNKKADLEKEVALRNQKIQQAENKLKQREMVLSQRQEEIQRKKLEAEAVKENLEAQLVIVDKKKEELDKLQHQEIEKLEAISGLSADEAKERLVESLKEEAKTQAQSFINDIMDDAKLTASKEAKRIVIQSIQRVATETAIENSVTVFHIESDEIKGRIIGREGRNIRALEAATGVEIVVDDTPEAIVLSAFDPVRREIARLALHQLVTDGRIHPARIEEVVSKVRKQVEEEIIETGKRTTIDLGIHGLHPELIRIIGKMKYR... | Endoribonuclease that initiates mRNA decay. | Q89ZG0 |
Q06106 | MRD1_YEAST | Multiple RNA-binding domain-containing protein 1 | Saccharomyces | MSRIIVKGLPVYLTDDNLREHFTKRLRQKHSHQAVNGSGPDLITDVKILRDRNGESRRFGFIGYRNEEDAFDAVEYFNGSFINTSKIEVSMAKSFADPRVPQPMKEKRREALKRFREKEEKLLQEENRKKKKVDENKHSNIDDEIRKNKQLQEFMETMKPSSQVTSWEKVGIDKSIEDEKLKREEEDSSVQGNSLLAHALALKEENNKDEAPNLVIENESDDEYSALNRNRDEDQEDAGEEEKMISISNLKDTDIGLVNDDANSDEKENEKRRNLAQDEKVSDLDWFKQRRVRIKESEAETREKSSSYATEQNESLDTKK... | Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA. | Q06106 |
P80174 | SODC_CARCR | Superoxide dismutase [Cu-Zn] | Caretta | MATVKAVCVLKGEDPVKEPVKGPVKEPVKGIIYFEQQGNGPVTLSGSITGLTEGKHGFHVHEFGDNTNGCTSAGAHFNPPGKNHGGPQDNERHVGDLGNVIANKEGVAEVCIKDSLISLTGSQSIIGRTMVVHEKEDDLGKGGNDESLKTGNAGSRLACGVVGIAKL | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | P80174 |
B9KER1 | RL21_CAMLR | 50S ribosomal protein L21 | Campylobacter | MYAIIKHSGKQYRVSQGDELKLDRFEAEVKSSVEVSEVLAVCDKELKVGAPFVAGAKVVLEVIAHGKDKKVVIYKKRRRKDSKLKRGFRRQFTRVRVVDIKA | This protein binds to 23S rRNA in the presence of protein L20. | B9KER1 |
Q8NSL2 | PRPB2_CORGL | (2R,3S)-2-methylisocitrate lyase | Corynebacterium | MAGLFSSAVAPTERRKALRAALAAPEIARMPGAFSPLAARAIQEAGFEGVYVSGAVVAADLALPDIGLTTLTEVAHRSRQIARVTDLPVLVDADTGFGEPMSAARTVSELEDAGVAGCHLEDQVNPKRCGHLDGKEVVGTDIMVRRIAAAVNERRDEQFVICARTDAAGVEGIDSAIERAKAYADAGADMIFTEALYSPADFEKFRAAVDIPLLANMTEFGKTELLPAQLLEDIGYNAVIYPVTLLRIAMGQVEQALGDIANTGIQTDWVDRMQHRSRLYELLRYNEYNAFDQQVFTYSADSYKPIF | Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate. | Q8NSL2 |
Q81JW0 | RPOE_BACAN | RNAP delta factor | Bacillus cereus group | MDFKQYSPEELKECSMIEVVHSVLGDKRQATTFNELVQEIAQVLGLSQEQVNAKIAQFYTDLNIDGRFINLGENRWGLRSWYPYEQIDEEILPQPKPKKKRKVEDDGFDDYIEEDEDFDDADVTEDEDDDVEDLDKVLEDEDGDDDDLDDLDEDEDDFAEEELEYDETEEEEEEL | Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. | Q81JW0 |
Q9HIC2 | PGMI_THEAC | Phosphomannose isomerase | Thermoplasma | MLRSHCMEFSEELKTLKDQVRFDGSFRTGTFSNIVIAGMGGSGIAGRIFSEMYSAKPVFVCDDYHIPEFVDGNTEFIAVSYSGNTEETLSAAEEAIKKGAKVHAITSGGRLSEMGVDTIKIPGGLQPRSAVGYLTMPIINTFIRPKHEDIEEAAGLLSDLDKNNTVQENIATEIYAGRRIPVIYGSTPYRSVAYRWKTQFNENAKILAYSNYFSELNHNDTMPLRDTYRKDEFYFMAFDSTDERIRKRIEVTQKITGTSFKKIEARGSSLIARIFYLIHFGDYVTYHLARIRNVDPQDVSAIEDLKKRIS | Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency. | Q9HIC2 |
B1IND6 | CLPX_CLOBK | ATP-dependent Clp protease ATP-binding subunit ClpX | Clostridium | MSKLDEKKQLKCSFCGKTQDQVRRLIAGPGVYICDECIELCSEIINDEFEDDIQVDLTSLPKPTEIKTYLDQYVIGQEDAKKSLSVAVYNHYKRINSNTNNDDVELQKSNILLLGPTGSGKTLLAQTLAKFLNVPFAIADATTLTEAGYVGEDVENILLKLIQNADYDIEKAEKGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVAAVPPQGGRKHPHQEFIQINTTNILFICGGAFDGVDKIIERRTRTSSLGFGAEIQSKKEKDLGKLLKDIMPGDLLKFGLIPEFIGRLPIVVTLDKLDREALIKIL... | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | B1IND6 |
Q5HEU3 | CPFC_STAAC | Coproporphyrin III ferrochelatase | Staphylococcus | MTKKMGLLVMAYGTPYKESDIEPYYTDIRHGKRPSEEELQDLKDRYEFIGGLSPLAGTTDDQADALVSALNKAYADVEFKLYLGLKHISPFIEDAVEQMHNDGITEAITVVLAPHYSSFSVGSYDKRADEEAAKYGIQLTHVKHYYEQPKFIEYWTNKVNETLAQIPEEEHKDTVLVVSAHSLPKGLIEKNNDPYPQELEHTALLIKEQSNIEHIAIGWQSEGNTGTPWLGPDVQDLTRDLYEKHQYKNFIYTPVGFVCEHLEVLYDNDYECKVVCDDIGANYYRPKMPNTHPLFIGAIVDEIKSIF | Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III. | Q5HEU3 |
Q38X88 | AROE_LATSS | Shikimate dehydrogenase (NADP(+)) | Latilactobacillus | MISGYTALYGLIAHPAQHSLSPFIHNTGFHQIQMDARYAVFDSQATPAAITSAIKTLGIRGVNLSMPYKQSLVPLVDNLTSTAKLVGAINTIKNEAGRLTATNTDGDGFWCALQKAHPQRRYRSVTILGAGGAALAVIEAAVRYGVQQVTVFKRANATYDSVIQRLAQISLASGLQIIVEPYDDQLALATALQNADCLINATNIGMTATPGNPLPINLLQYLPEDSLVADLIYAPRETAFLKTAQKAHYQIQNGLGMLIEQAALSFEFWTNESMATMPIYQHLTGGNDAS | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). | Q38X88 |
B5Z937 | MIAA_HELPG | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Helicobacter | MDAEIFSLDSLSIYKDINIASAKPSLKERKNIKHYALDYLNIDEKNNAQLFKTLLEDAMRVSSKEILLIVGGSSFYLKSILEGLSDTPKISGEEVVKIEREIATLSNPYIFLKSIDPNMAFKIHSNDTYRIHKALEIFYATHTPPSEYFKANPKKPFAHAISLFALSVEKNALHNNIKQRTKNMLHSGLIEEIKALYTQYPKDSQPFKAIGVKESILFLEKRLTLKELEETITSNTIKLAKRQNTFNKTQFNNLYTGSVKEVRHAILKHSKSGIKG | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | B5Z937 |
Q5DT36 | KLRI2_MOUSE | Killer cell lectin-like receptor subfamily I member 2 | Mus | MHKKKHIKHGTNKQEIINIGTKSPTFQEKQRPSKTDQRSTVWREEQKKQELKVHRIFHPQPRTGFDVGKGIDPWLTTWQMITVILATLCIILVTKVGFLIPSLFSKGEKQSRKFSLLDPLCDRNDDSSCDFCSSDWIAFGNNFYCVFRENSKTWVESQSACEELNSHLVIIDSKAEVENLLLFEMDGWILHRMDGTNSSRLWGNDIKIRNTLMNDSEKKNHSCHYLRGNIFMPDECSAKKTYICEFNI | Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates NK cell cytolytic activity. | Q5DT36 |
F4I366 | NRPA2_ARATH | Nuclear RNA polymerase A2 | Arabidopsis | MVVNAKDSTVPTMEDFKELHNLVTHHIESFDYMTLKGLDVMFNRIKPVSVYDPNTENELSIWLENPLVFAPQKESFKSTSRKEPLLPFECRQAKISYTGTFMADVCFKYNDGVVVRDKFDFGQFPIMLMSKLCSLKGADCRKLLKCKESTSEMGGYFILNGIERVFRCVIAPKRNHPTSMIRNSFRDRKEGYSSKAVVTRCVRDDQSSVTVKLYYLRNGSARVGFWIVGREYLLPVGLVLKALTNSCDEEIYESLNCCYSEHYGRGDGAIGTQLVRERAKIILDEVRDLGLFTREQCRKHLGQHFQPVLDGVKKESLSIV... | Essential for the completion of the three rounds of mitosis in female megaspores required for the development of mature gametophytes. | F4I366 |
Q8WHY0 | RK23_PSINU | 50S ribosomal protein L23, chloroplastic | Psilotum | MNEIKNQIITEKTIRLLQKNQYTFNVDSKLTKTKIKDWIERFFDVKVKSINSLRSPRKKSQKRLPQTSLNDKRMIITLKPEYSIPLFINE | Binds to 23S rRNA. | Q8WHY0 |
Q5HC98 | SSRP_EHRRW | Small protein B | Ehrlichia | MDIIIENRKVRFNYFIIQEFDAGIVLIGSEVKSLRQRKVSIAESYVTERNMELWLCNLHISEYTQANTKNHNPTRPRKLLLKKKQIYKISGNMKNDGFTVVPLFLYFNDKGIAKAKIVIVKGKKLHDKRETIKARDWNREKSRILRGG | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | Q5HC98 |
A5FR86 | RNH2_DEHMB | Ribonuclease HII | Dehalococcoides | MPATVICPSRAEEKLLRKQGFILIAGLDEAGRGCLAGPVVAGAVIMPPRLKGDWVEMVRDSKVLSPAKREYLYCHIVSMAVTFGVGAVDNEQIDSMGIAPATRLAMKQAVEDLTCQPDFLLVDYLKLPDIPLPQKGIVDGDALCFSIACASIVAKVSRDRLMSKLDMEYPGYYLAKHKGYGTALHVECICQKGISPIHRRTFAPLKGMIDGL | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | A5FR86 |
Q1GLQ5 | PANC_RUEST | Pantoate-activating enzyme | unclassified Ruegeria | MTPPILRRLDDLRALRRDWMKKGDTLGLVPTMGALHAGHLSLVEAAKAACDHVVVTIFVNPKQFNSPEDLANYPRTEHEDAQKLAPYGVDAIYVPDPDQIYPEGYATTVSLTGVTDVMEGPNRPGHFEGVATVVAKLFLQSGADRAFFGEKDYQQLMVVRRMARDLDIPIEVIGCPTVREASGLAMSSRNMRLSAAATKTAGQLNPLMEAAATRLRAGEDYAPLEAEMRAQLSDLGFAEIEYIDLRCAQDLTSLDRLDRPARMFVAAWLDGVRLIDNIAV | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q1GLQ5 |
Q9PPB0 | NADE_CAMJE | NH(3)-dependent NAD(+) synthetase | Campylobacter | MDWQKITEKMCDFIQEKVKNSQSQGVVLGLSGGIDSALVATLCKRALKENVFALLMPTQISNKANLEDALRLCADLNLEYKIIEIQSILDAFIKQSENTTLVSLGNFAARIRMSLLYDYSALKNSLVIGTSNKSELLLGYGTIYGDLACAFNPIGSLYKSEIYALAKYLNLHENFIKKAPSADLWENQSDEADLGFSYTKIDEGLKALETNDEKLLRTLDPSLIAMLKNRMQKNAFKGKMPEILEI | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Q9PPB0 |
Q5PQM9 | KMCP1_RAT | Solute carrier family 25 member 30 | Rattus | MSALNWKPFVYGGLASITAECGTFPIDLTKTRLQIQGQTNDAKFREIRYRGMLHALMRIGREEGLRALYSGIAPAMLRQASYGTIKIGTYQSLKRLAVERPEDETLLINVVCGILSGVISSAIANPTDVLKIRMQAQNSAVQGGMIGNFISIYQQEGTRGLWKGVSLTAQRAAIVVGVELPVYDITKKHLILSGLMGDTVSTHFLSSFTCGLVGALASNPVDVVRTRMMNQRDLRDGRCSGYKGTLDCLLQTWKNEGFFALYKGFWPNWLRLGPWNIIFFLTYEQLKKLDL | Probable transporter. | Q5PQM9 |
B4JII0 | SPAST_DROGR | Spastin | Hawaiian Drosophila | MVRTKNQSSSSSASSSTKSPVKISGGTTNRSRSCSDALIDDGNSKSSSKPTSNNRQRTTTNNNTTAITTTPGSSPDNDDDDTTTTDADLTPTSGNAPRGGNSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRSPNRRDCNIEIVVQNSKEQQQQHQHQQAIIHCPLERRGNISGIEQTLAQALPQRQRAIQPLEMAGNRAGGNYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLQLQ... | ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in a... | B4JII0 |
Q6G7H4 | PDP_STAAS | Pyrimidine-nucleoside phosphorylase | Staphylococcus | MRMIDIIEKKRDGHTLTTEEINFFIDGYVKGDIPDYQASSLAMAIYFQDMNDDERAALTMAMVNSGDMIDLSDIKGVKVDKHSTGGVGDTTTLVLAPLVAAVDVPVAKMSGRGLGHTGGTIDKLEAIDGFHVEIDEATFVKLVNENKVAVVGQSGNLTPADKKLYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGSGAFMKTLEDAEALAHAMVRIGNNVGRNTMAIISDMNQPLGRAIGNALELQEAIDTLKGQGPKDLTELVLTLGSQMVVLANKAETLEEARALLIEAINSGAALEKFKTFIKNQGGDE... | Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate. | Q6G7H4 |
Q117Z4 | UREF_TRIEI | Urease accessory protein UreF | Trichodesmium | MINSDISEQLALMQLSDSFFPTGSFTFSHGLETLVQTGKIQSQPEILYFLQILLRNKVGVSDVVALIHSYRGCKNGDIEAVRVADRMLFVQTAIAKNRETQRQSGRALLMVASSTWQDERLKTLNIDAVSGNIHCLHPVIFGAVTSVVGLDERNAVLAFLHGLVTNILGAAIRLGILGHIQAQQILLQLVPDIEAVWSTAVSMNLEQMWSCTPFIDIAQMQHPKLAHKLFAN | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q117Z4 |
B0RED7 | ATPD_CLAMS | F-type ATPase subunit delta | Clavibacter | MGSASRASLDSARRVLAELGGVDLSTAGQLLGAGRAIGGSTHLLSALADTGIAPEVKHSIVDRVFGATVQEPTLRVLRAVVDGRWSSHDELLAGIEELGIRAVAISAPEGTPVESELFTFGRAVSTDDGLELAFGDKLGDPEAKSTLVHRLLDGRASEQTVVIVEQLVQQPRGRRIGELVRHAATLVADQAGLTIATVSVASPLSPEQSERLAQALSRRYSRRIELNQVVDRDLVGGLRVQIGDDVIDGSVATRINDLRLQFA | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | B0RED7 |
Q49XD2 | GUAC_STAS1 | Guanosine 5'-monophosphate oxidoreductase | Staphylococcus | MKIFDYEDIQLVPNKCIVNSRSECDTTIQFGPRSFKLPVVPANMQTVMNETLAEWFAENDYFYIMHRFDEEGRIPFIKKMQEKGLFASISVGVKEREFGFVESLAAENVIPEYITIDIAHGHSDSVINMIKHIKKHIPEVFVIAGNVGTPEGVRELENAGADATKVGIGPGRVCITKIKTGFGTGGWQLSALNHCSKAARKPIIADGGIRTHGDIAKSIRFGASMVMVGSLFAAHEESPGETVELDGKMYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLFNTLTEMQQDLQSSISYAGGKDLNSLRKVDYVIVRNSIF... | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. | Q49XD2 |
Q5HGQ4 | BSHC_STAAC | Putative cysteine ligase BshC | Staphylococcus | MDCKVVSLNEKDQFIPKIKSSDPVITGLFQYDAAQQTSFEKRMSKENNGREAALANVIREYMSDLKLSSEQELNIQHLANGSKVVIGGQQAGLFGGPLYTFHKIFSIITLSKELTDTHKQQVVPVFWIAGEDHDFDEVNHTFVYNENHGSLHKVKYHTMEMPETTVSRYYPDKAELKQTLKTMFIHMKETVHTQGLLEICDRIIDQYDSWTDMFKALLHETFKAYGVLFIDAQFEPLRKMEAPMFKKILKKHQLLDDAFRATQQRTQNQGLNAMIQTDTNVHLFLHDENMRQLVSYDGKHFKLNKTDKTYIKEEIINIAE... | Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH. | Q5HGQ4 |
P60322 | NANO2_MOUSE | Nanos homolog 2 | Mus | MDLPPFDMWRDYFNLSQVVMDIIQSRKQRQEGEVAEEPNSRPQEKSEQDLEGYPGCLPTICNFCKHNGESRHVYTSHQLKTPEGVVVCPILRHYVCPLCGATGDQAHTLKYCPLNSSQQSLYRRSGRNSAGRRVKR | Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is requi... | P60322 |
B1YVM2 | LEPA_BURA4 | Ribosomal back-translocase LepA | Burkholderia cepacia complex | MDHIRNFSIIAHIDHGKSTLADRIIQVCGGLADREMEAQVLDSMDIERERGITIKAQTAALSYRARDGKVYNLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTAIELGVEVVPVLNKIDLPAANPENAIEEIEDVIGIDATDATRCSAKTGLGVEDVLESLIAKVPPPKGDPAAPLQALIIDSWFDNYVGVVMLVRIVNGTLRPKEKIKMMATGAQYPVEHVGVFTPKSRNLESLSAGQVGFIIAGIKELTAAKVGDTVTHVAKAASEPLPGFKEVKPQVFAGLYPVEANQYDALRESLEKLKLN... | 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-t... | B1YVM2 |
Q13VE3 | DADA_PARXL | D-amino acid dehydrogenase | Paraburkholderia | MRVVVLGSGVVGVTSAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYASPWAAPGVPLKAVKWMFQKHAPLAIRLDGTQFQLQWMWQMLQNCTSSRYAVNKGRMVRLAEYSRDCLQALRAETGIQYEGRTGGTLQVFRTQQQFEGAAKDIAVLREASVPYELLSPAELAQAEPALAAVSHKLTGGLRLPGDETGDCQMFTTRLAALAEQLGVKFRYNTPIDALAMAGDRIAGVKCGEELVRADSFVVALGSYSTQFLSGLVKIPVYPLKGYSITAPIVNEASAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGFD... | Oxidative deamination of D-amino acids. | Q13VE3 |
C4K8Y6 | DUT_HAMD5 | dUTP pyrophosphatase | Candidatus Hamiltonella | MKKIDIKILDKRIGDVFPLPTYTTSGSAGLDLRVCTQAPQHLSPGETRLLPTGLAVHIADPHLAAMILPRSGLGHKNGIVLGNLVGLIDSDYQGELMLSVWNRSQIDFLINPGDRLAQMVFVPVVQVELNIVSEFTSSQRGSGGFGHSGRQ | 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. | C4K8Y6 |
P61897 | MDH_PECCC | Malate dehydrogenase | Pectobacterium | LRRKPGMDRSDLFNVNAGIVRNLVEQIAVTCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPQDINVPVIGGHSGVTILPLLSQVPGISFSEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQVPG | Catalyzes the reversible oxidation of malate to oxaloacetate. | P61897 |
A0A0G2JMI3 | HV692_HUMAN | Immunoglobulin heavy variable 1-69-2 | Homo | MDCTWRILLLVAAATGTHAEVQLVQSGAEVKKPGATVKISCKVSGYTFTDYYMHWVQQAPGKGLEWMGLVDPEDGETIYAEKFQGRVTITADTSTDTAYMELSSLRSEDTAVYYCAT | V region of the variable domain of immunoglobulin heavy 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 recep... | A0A0G2JMI3 |
Q0VSM4 | RL10_ALCBS | 50S ribosomal protein L10 | Alcanivorax | MPLNLEDKRAIVASVNAVAAEALSAVVADYRGLTVSQMTELRSKARETGVYLKVVRNTLAKFAVKDTEFECLNDALVGPTVLAFSKDDPGAAARLIKDFAKDHDALEVKALAVGGVTYGAQDIDVLAKLPTRDEAISQLMSVMQAPVAKFVRTLNEVPGKFVRTVAAVKDQKQSAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | Q0VSM4 |
Q609K0 | QUEC_METCA | Queuosine biosynthesis protein QueC | Methylococcus | MKPAVVLLSGGLDSATTLAIARREGFACHAMSFDYGQRHGAELKAARRLAQSLGAIEHKTVHIGLDAIGGSALTDLRIAVPDHPQNGIPVTYVPARNTVFLSFALGWAEVLGALDIFIGVNAVDYSGYPDCRPEFIRAFEQLANLATKVGVEGGRFRIHTPLIDLSKADIIRTGTALGIDYAMTVSCYAADAEGLACGVCDSCRLRRQGFEQAGIADPTRYRS | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | Q609K0 |
Q3JAS2 | TTCA_NITOC | tRNA 2-thiocytidine biosynthesis protein TtcA | Nitrosococcus | MNKQSRKAQYNANKLQKRLRRLVGQAIETFNMIEDGDRLMVCLSGGKDSYALLDILLSLQKHAPVKFDLIAVNLDQKQPGFPEHVLPHYLESLGVSYRIVEQDTYSVVKRVIPEGKTTCSLCSRLRRGILYGTAEELGATKIALGHHRDDILETFFLNMFHGGTLKGMPPKLLSDNGRHIVIRPLAYCREKDLETYAHLKAFPIIPCNLCGSQANLQRQAIKAMMKAWDKQFPGRLETMFRALQNVKPSHLADSTLYNFQGLQKQESPFPEGDKAFDEEVFLESQEKSPPFHGSKIRVLQFK | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q3JAS2 |
B0BAL3 | MURD_CHLTB | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Chlamydia | MGLERVVVIGLGVSGRSIARFLAQKGVCVLGVDKSLHALQNCPYIQEKYLENEEFPSQVDYVVRSPGVSKEHPWVQAAIASHIPVMTDIQLAFQTEKFTERESLAITGTTGKTTTILFLEYLFKRSGIPAFAMGNVGIPILDGMQNPGVRIVEISSFQLADQEKSYPVLSGGMILNISDNHLDYHGNFSEYFQAKQNLALCMRNPDDLWVGDERFYGHLYLEEVQKYMRLLDKESALKPLYLHDKHNYCCAYLLAKIEFPISETSFIEAVATFNKPPHRMEYLGQKQGIHYINDSKATTVSATETALLGVGNQAIVILGG... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | B0BAL3 |
Q3SPN4 | LGT_NITWN | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Nitrobacter | MFLLITYPVFDPVAISLGPIAIRWYALAYIGGIMLGWLYARALLRSEKLWGGPAPISVVQLDDFILWVTIAIIVGGRVGYVLFYNPDYFIRYPAQIFQLWNGGMSFHGGFMGCVAAVILFCRRHGLPILSLGDVATAVGPIGLFLGRIANFINSELWGRPADPGLPWAMVFPNGGPLPRHPSQLYEAALEGILLFTILALMIRLGALKRPGLVLGSFIALYAMARIVAEFFREPDPQLGFLWGGLTMGMLLSIPMVIIGLAIVYAAWSRGSRASDAQASPNSGASTKVDRD | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | Q3SPN4 |
Q8J0F3 | MLCE_PENCI | Compactin biosynthesis protein E | Penicillium | MSEPLPPKEGEPRPQKEESQNDTLEATESKSQHITGLKLGLVVASVTFVAFLMLLDMSIIVTAIPHITSEFHSLNDVGWYGSAYLLANCALQPLAGKLYTLLGLKYTFFAFLCIFELGSVLCGAARSSTMLIVGRAVAGMGGSGLVNGALTILSTAAPKHKQPVLIGVMMGLSQIAIVCGPLLGGAFTQHATWRWCFYINLPIGAVAAFLLLVITIPDRISSTDSELSTDKPMANIKSTLRKLDLVGFVVFAAFATMISLALEWGGSTYTWRSSVIIGLFCGGGFALIAFVLWERHVGDAVAMIPGSVAGKRQVWCSCLF... | Efflux pump; part of the gene cluster that mediates the biosynthesis of compactin, also known as mevastatin or ML-236B, and which acts as a potent competitive inhibitor of HMG-CoA reductase . | Q8J0F3 |
B7IGA0 | RL11_THEAB | 50S ribosomal protein L11 | Thermosipho | MAKKVVAQVRLQLEAGKATPAPPVGPALGQRGVNLMEFCKKFNAATADKAGMIIPVIITVYEDRSFTFITKTPPASFLLKKAAKLNSGSQEPKRKMVGKVTRDQIKEIAEIKMKDLNANDIEAAMKIIEGTAKSMGIEVVD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | B7IGA0 |
B5E9D0 | NDK_CITBB | Nucleoside-2-P kinase | Citrifermentans | MERTFAIIKPDAVERNVTGKVLAMIEEGGFKIVGMKKIRLSKCQAEGFYYVHKERPFFGDLCAFMSRGPVIALVLEKENAIADWRGLMGATNPANAEAGTIRKALGVSIEENTVHGSDSPESASYEIPYFFNQLELV | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | B5E9D0 |
O43102 | CBF5_ASPFU | Small nucleolar RNP protein cbf5 | Aspergillus subgen. Fumigati | MAVSVTKEEMDYTIKPEAGASNISTEDWPLLLKNYDKLMVRTGHFTPIPAGCSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNDRHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMDENNGLVTLHDVLDAQWMYDNQRDESYLRRVIQPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIEVNEEVVLMTTKGEAI... | Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation... | O43102 |
A9KSS1 | HPRK_LACP7 | HPr(Ser) kinase/phosphorylase | Lachnospiraceae | MYTVELGKLVEKMNLENCTPEIDISSIQITQPDVNRPALQLTGFFDYFDSDRVQIIGNVEHAYMQKMEKDHGLGIMKKLMSFKMPCIVFCRGIEVSEDFKEVAIEEGVPIFRTEKTTSSFMAEVIRWLKVELAPRISIHGVLVDVYGEGILIMGESGIGKSEAALELIKRGHRLVTDDLVEIKKVSDDTLIGTAPDITRHFIELRGIGIIDVKTLFGVESVKNTQSIDLVIKLEEWNRDKEYDRLGLEEQYIEFLGNRVVCHNIPIRPGRNLAVICESAAVNYRQKKMGYNAAQELYNRVTNNLLKKSK | Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphor... | A9KSS1 |
Q98HV6 | PTH_RHILO | Peptidyl-tRNA hydrolase | Mesorhizobium | MLVFAGLGNPGAKYADNRHNVGFMAADAIARRHSFSPWSKKFQGLIAEGTIAGEKIILIKPQTFMNLSGQSVGEALRFYKLELSALTVFYDEIDLAEGKLRIKTGGGAGGHNGIRSIDGHIGNAYRRVRIGVGHPGIKEMVQHHVLGDFAKADREWLDPLLDAIADNAAMIVKGDESGFMNKAALAVQGKAIAELEKPAQKQQPKQQSHIRQARSQQAPAKLPETGPMAAMLKKLFGNKD | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q98HV6 |
Q4JV87 | LEXA_CORJK | LexA repressor | Corynebacterium | MSIDESSDNPTPRPKLGRPPKSEADKRAEKEAQKDGKKPALSTRQRRILEVIRDSTIIRGYPPSIREIADAVGLHSTSSVSYHLTQLEKRGYLRRDGKRPRAVDVRAFDGGQLTNESTKKNAGSPQPTSAAIPEPTTEGETMPEATYVPVVGQIAAGAPILAEQNVEAHFPLPQELVGNGELFLLQVVGESMHDAGIFNGDWVVVRSQSVAEFGDFVAAMIDGEATVKEFQKDADGLWLIPHNPLFEPIPAEEATILGKVAAVLRKI | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair... | Q4JV87 |
Q71XF4 | CPFC_LISMF | Coproporphyrin III ferrochelatase | Listeria | MTKKVGLLVMAYGTPYKDEDIERYYTDIRHGHKPSEEMIADLRGRYHAIGGLSPLAKITEAQAYGLEKALNESQDEVEFKAYIGLKHIEPFIEDAVEAMHKDGIEEAISIVLAPHYSSFSVEAYNKRAKDAADKLGGLRIKAINDWYKQPKFIQMWADRINETAKQIPADELLDTVLIVSAHSLPEKIKQHNDPYPDQLQETADFIFEKVVVPHYALGWQSEGKTGEPWLGPDVQDLTRELYGREKYKHFIYTPVGFVAEHLEVLYDNDYECKVVTDEVGATYHRPPMPNSDPEFLEVLRTVVWEKYSN | Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III. | Q71XF4 |
Q01854 | RDXA_CERS4 | Protein RdxA | Cereibacter | MSEPLYAPRTPIFPRQISGAFRTAKWWILAVSLGIYLLTPWLRWDRGPNLPDQAVLIDIAGRRFFLFGIQIWPHEFYFVAGLLIMAGLGLFLFTSAAGRVWCGYACPQTVWTDLFLLVERRIEGDRNAQIRLHRQAWTAEKVWKRLLKWSVWAAISLLTGGAWVFYFADAPTLLNGLVTLTAHPVAWITIFVLTATTFVFAGFMREQICIYACPWPRIQAALMDEETITVAYRDWRGEPRGKRSETGRGDCIDCMACVNVCPMGIDIREGQQMACITCGLCIDACDDTMDRIGRPRGLIGYLALSDEHLERAGDTPKPAW... | Predicted to be involved in a redox process. | Q01854 |
Q6G4G5 | PURA_BARHE | IMP--aspartate ligase | Bartonella | MANVVVVGTQWGDEGKGKIVDWLSERADIIVRYQGGHNAGHTLVVNGVNYKLSLLPSGLVRGKLSIIGNGVVVDPHHFVVELKKLRDQGVKIVPEILRIAENAPLILSLHRDLDAIRESGFSGLKIGTTKRGIGPAYEDKVGRRAIRVMDLAEANTLMAKIKRLLRHHNALRRGMGVAEIDSQALYDELMQVADEILPFMDCTWRLLDESYRMGKHVLFEGAQGALLDNDFGTYPYVTSSNTVAGQACTGSGMGPGAIHYVLGIAKAYTTRVGEGPFPTEQINDIGEFLGIRGHEFGVVTGRKRRCGWFDAVLVRQMVTI... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q6G4G5 |
A8FYV3 | DPO4_SHESH | DNA polymerase IV | Shewanella | MKKIIHIDMDCYFAAVEMRDFPELRGKPIAVGGRSDRRGVISTCNYEARKFGVRSAMASGYALKLCPDLILVPGRMSVYKEVSAQIREVFSHYTDLIEPLSLDEAYLDVTDCTQCQGSATLIAEAIRQEIFELTGLTASAGIAPIKFLAKIASDLNKPNGQYVITPNMIPAFVKDLPLIKIPGVGKVTGKKLEDIGLITCSDLQAYPEAALIERFGKFGSVLIERAQGIDTRNISPHRERKSVGVETTLAKDIYSLEQCQGVMPQLIQELATRIKRSAKDRTIHKQVVKLKFNDFKQTTIEHRSDEVSVKLFYDLLSQAL... | Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in... | A8FYV3 |
A0QVH7 | DXR_MYCS2 | 2-C-methyl-D-erythritol 4-phosphate synthase | Mycolicibacterium | MTTSAASGEPGRQRVLILGSTGSIGTQALEVIAANPDRFEVVGLAAGGGNPELLAAQRAQTGVAAVAVADPAAAEAVGDVRYSGPDAVTRLVEDTEADVVLNALVGALGLQPTLAALATGARLALANKESLVAGGPLVLKAAAPGQIVPVDSEHSAMAQCLRGGTRAELDKIVLTASGGPFLGWSAEDLKSVTPEQAGKHPTWSMGPMNTLNSATLVNKGLELIETHLLFGVDYDDIDVVVHPQSIVHSMATFTDGSTLAQASPPDMKLPIALALGWPDRIAGAAAACDFSTASTWEFLPLDNAVFPAVDLARFAGKQGG... | Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | A0QVH7 |
C1CZJ9 | RL21_DEIDV | 50S ribosomal protein L21 | Deinococcus | MFAIIQTGGKQYRVQEGDVIRVENLKGEAGDKLDLTPLFVGGDQALFGDAVSNFVVNAEVVEHGRGPKIYIRKYKSGVQYRRRTGHRQDYTAIKILGIKG | This protein binds to 23S rRNA in the presence of protein L20. | C1CZJ9 |
Q1BZG3 | MURG_BURCA | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Burkholderia cepacia complex | MTASQRTLMVMAGGTGGHVFPGLAVAHRMEAAGWRVVWLGNPAGMEATLVPKHGIPMEYVRFGGLRGKGLKTKLTLPVNLLRACWQSLGALRRVRPDVVLGMGGYITFPAGVMTALSGRPLVLHEQNSIAGLTNKVLAKLAKRVLVAFPGALPHAEWTGNPIRAELAHTEPPHARYASRSGPLNVLVVGGSLGAAALNEVVPRALALLAPGERPRVVHQAGVKHIEALKANYEAAGFAAGEDVRLVPFIDDMAAAYAAADLVICRSGAMTVSEIAAVGVAALFVPFPYAVDDHQTTNAAFLAEAGAAVLVQQRDLSAELL... | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | Q1BZG3 |
Q96BX8 | MOB3A_HUMAN | Mps one binder kinase activator-like 2A | Homo | MSNPFLKQVFNKDKTFRPKRKFEPGTQRFELHKKAQASLNAGLDLRLAVQLPPGEDLNDWVAVHVVDFFNRVNLIYGTISDGCTEQSCPVMSGGPKYEYRWQDEHKFRKPTALSAPRYMDLLMDWIEAQINNEDLFPTNVGTPFPKNFLQTVRKILSRLFRVFVHVYIHHFDRIAQMGSEAHVNTCYKHFYYFVKEFGLIDTKELEPLKEMTARMCH | May regulate the activity of kinases. | Q96BX8 |
Q9SJJ5 | CKS2_ARATH | Cyclin-dependent kinases regulatory subunit 2 | Arabidopsis | MGQIQYSDKYFDDTFEYRHVVLPPEVAKLLPKNRILSESEWRAIGVQQSRGWVHYAIHRPEPHIMLFRRPLNYQQEHQAQIAK | Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. | Q9SJJ5 |
A6VC62 | HEM1_PSEA7 | Glutamyl-tRNA reductase | Pseudomonas | MAFIALGINHKTASVAVRERVAFTPEQMVEALQQLCRLTTSREAAILSTCNRSELYLEIDHPTADDVLAWLADYHRLTLDELRACAYVHQDEDAVRHMMRVASGLDSMVLGEPQILGQMKSAYAVAREAGTVGPLLGRLFQATFSTAKTVRTDTAIGENPVSVAFAAVSLAKQIFSDLHRSQALLIGAGETITLVARHLFEQGVKRIVVANRTLERASLLAEQFGAHAVLLSEIPEELANSDIVISSTASQLPILGKGAVERALKQRKHKPMFMVDIAVPRDIEPEVGELDDVYLYSVDDLHEVVAENLKSRQGAAQAAE... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | A6VC62 |
A7I3J2 | DCD_CAMHC | Deoxycytidine triphosphate deaminase | Campylobacter | MGLKSDKWIREQSIKNGMITPFCEENMGVGVVSYGLSSYGYDIRVADEFKIFTNVGGTVVDPKNFDEKNIVDFKGDVCIVPPNSFALARTIEYFKMPRDVLAICLGKSTYARCGIIVNVTPFEPGFEGHITIEISNTTPLPAKIYANEGIAQVLFLQGDEICEVSYADKKGKYQRQKGITLPRILEGDKK | Catalyzes the deamination of dCTP to dUTP. | A7I3J2 |
B5XNX1 | MENH_KLEP3 | 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase | Klebsiella | MTLSAAVDNGQSGYPWLVFLHGFSGDRDEWREVGDAFPAWPRLYLDLPGHGGSADIAVQDFAGVNTLLLATLNSYNILNYWLIGYSLGGRVAMNFACQPRAGLRGLIVEGGHPGLQDAEARQARRSNDRAWAERFRRDPLAQVFADWYQQPVFASLDAAQRESLVALRSRNNGATLAAMLQATSLAGQADLRAPLQARDFPFHYLCGERDAKFRAIAQALAADTHIIHHAGHNAHRDNPAAVIACLAQILAS | Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). | B5XNX1 |
P28050 | FETA_GORGO | Alpha-fetoglobulin | Gorilla | MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSAGCLENQLPAFLEELCHEKEILEKYGLSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAEND... | Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. | P28050 |
P07105 | FANB_ECOLX | Fimbrial adhesin K99 B protein | Escherichia | MYIDNYLIMRKINMEETILSLTSYQLRPGKVDKKQFVLLIDVSSIRSYKVINALEDYFVNGKNRKEICDNHKINQGYLSLKIRELQDISLRIYNISHCI | Trans-acting protein involved in the regulation of the biogenesis of K99 fimbriae (FanC). | P07105 |
Q8ZZZ0 | QUEE_PYRAE | Archaeosine biosynthesis protein QueE | Pyrobaculum | MSATPRVRVLEIFASLQGEGINLGRPAVFVRLAGCPIRCIYCDTKYSWDFNAGVEMGVEEIVAKALALSVVGHVVVTGGEPLIWQRRGLEELACALRALGSVEVETSGAYPPTPELDRCVDFYDVSPKLSNAGVKAPFSPFYASSPKAWFKFVVSNADDVEEVERFVVAYGIPRGRVFLMPMAESPEEHGEALRRIWDAAVRGGFRVTPRLHIMAWGNARGK | Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. | Q8ZZZ0 |
P53565 | CUX1_RAT | CDP/Cux p110 | Rattus | MAANVGSMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA... | Plays a role in cell cycle progression, in particular at the G1/S transition. As cells progress into S phase, a fraction of CUX1 molecules is proteolytically processed into N-terminally truncated proteins of 110 kDa. While CUX1 only transiently binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110 make... | P53565 |
A8GVL0 | RNPA_RICB8 | Protein C5 | belli group | MFITSLKNQKEFELINKLGKKFHEKYFILVIAKNIPKIFLESKYNIFLGIKVSKKLNKKAVVRNKIKRRIKHLIRLICNNSNLKKLAMIIIPRKGFDTADFSVLNHELSKAILDFYNPKK | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the riboz... | A8GVL0 |
O08451 | ACNA_MYCAV | RNA-binding protein | Mycobacterium avium complex (MAC) | MQDKRTVKVGTVADTAVGGRTKSLGVEVTDSVNSFGARNRVKVGDKSYQIYRLDAVPNTEKLPYSLKVLAENLLRNEDGSNITKDHIEAIANWDPKAGASIEIQYTPARVVMQDFTGVPCIVDLATMREAIADLGGNPEKVNPLAPADLVIDHSVIADLFGTADAFERNVEIEYQRNGERYQFLRWLQGAFSDFKVVPPRRIVHQVNIEYLARVVMERVGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLTGEDPAPGAATDVVLTVTEICAKHGVVGKFVEFYGEGVAEVPLANRA... | Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-... | O08451 |
B5EZJ2 | RBN_SALA4 | Ribonuclease Z homolog | Salmonella | MELIFLGTSAGVPTRSRNVTAILLHLQHPTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSMAGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGALNARALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAALALAQGVDVMVHETTLDASMEEKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGCQRLLAECRAIFPATELAYDFSVFPV | Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities. | B5EZJ2 |
Q3C1I3 | PSBC_NICSY | Protein CP-43 | Nicotiana | METLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGLGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSIIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRALVWSGEAYLSYSLGALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQ... | 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 sub... | Q3C1I3 |
Q98Q75 | RSMH_MYCPU | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Mycoplasmopsis | MQLHKPVLLKDVIENLEINPEGIYVDLTLGYAGHSSEILKKLSSKGKLIGFDQDSFAIEKSRQRLSQISDNFVLINDNFVNFKVYLDKMNISFVDGFLLDLGVSSVQLDFAHRGFSYSKLGPLDMRMNLDQPLKADDIVNGYDQESLCKIFIENADVKLAKQVAKGIVNNRPIKDTLELVEVIRSSLPAALVRKKNPAKAVFQAIRIAVNDELIVLKKFLAQSLDFLKKDSKMLIITFHSIEDRIVKDFFKRQVKNKHDRRLPIMEQKDYQVKTIKPTEEEIAQNRRAKSSKLRIIKKL | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Q98Q75 |
Q3ILP2 | HSLO_PSET1 | Heat shock protein 33 homolog | Pseudoalteromonas | MQQDLLHRYLFDNLDVRGELVQIENAYNEMIANHNYPDAVKALLGELLVATCLLTATLKFEGEIAVQLQGDGPVKYAVINGDDKQNMRGIARLQSEVTGSTVKELIGQGYMVITITPTKGERYQGIVPLEHETLSECIEAYFEQSEQLKTRLWFATDTTEGNAKACGLFLQVLPVDKQKSIEDFAHLEALSHTIKDEELLELDANTVLTRLYHEDNPRVFEPQSIQFKCGCTREKTMTALVNIGQQALLDDVAEHGEIKISCHYCLKDYLFDEQDVKNIFN | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Q3ILP2 |
Q6ECI4 | ZN470_HUMAN | Chondrogenesis zinc finger protein 1 | Homo | MKSQEEVEVAGIKLCKAMSLGSVTFTDVAIDFSQDEWEWLNLAQRSLYKKVMLENYRNLVSVGLCISKPDVISLLEQEKDPWVIKGGMNRGLCPDLECVWVTKSLSLNQDIYEEKLPPAIIMERLKSYDLECSTLGKNWKCEDLFERELVNQKTHFRQETITHIDTLIEKRDHSNKSGTVFHLNTLSYIKQIFPMEERIFNFHTDKKSLKTHSVVKKHKQDRGEKKLLKCNDCEKIFSKISTLTLHQRIHTGEKPYECIECGKAFSQSAHLAQHQRIHTGEKPFECTECGKAFSQNAHLVQHQRVHTGEKPYQCKQCNKA... | May be involved in transcriptional regulation. | Q6ECI4 |
Q9AG20 | MINC_NEIGO | Probable septum site-determining protein MinC | Neisseria | MMVYIMNAFDIKSTKMDVLSISLHTSDLFDLEDVLVKLGKKFQESGVVPFVLDVQEFDYPESLDLAALVSLFSRHGMQILGLKHSNERWAAVAMKYHLLFCLSHSENVKELGQVEVQKTEDGQKARKTVLITSPVRTGQQVYAEDGDLIVTGAVNQGAELIADGNMHIYAPMRGRALAGAKGDTSARIFIHSMQAELVSVAGIYRNFEQDLPDHLHKQPVQILLQDNRLVISAIGSE | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | Q9AG20 |
Q12GW4 | RL16_POLSJ | 50S ribosomal protein L16 | unclassified Polaromonas | MLQPARRKYRKEQKGRNTGVATRGNSVAFGDFGLKCTDRGRLTARQIEAARRAISRHVKRGGRIWIRVFPDKPISQKPAEVRMGNGKGNPEYYVAEIQPGKIVFEIVGVPEELAREAFRLASAKLPLRTTFVSRMIGQ | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q12GW4 |
Q9CAK6 | HIP15_ARATH | Heavy metal-associated isoprenylated plant protein 15 | Arabidopsis | MIVWMGVYDQRSKGKITKSISDLPGIHSSYMDLKEGTLVVMGDVDPVELVRNLRKKWGKAKLTLYVPYDALKEAKIAEAKQKREEIEREALYRYNREIRDIFNDKEEQGCVIC | Probable heavy-metal-binding protein. | Q9CAK6 |
Q4ULS3 | DPO3B_RICFE | DNA polymerase III subunit beta | spotted fever group | MLKLIVETKTLVQSLGFASSVVEKRNVIPEYANIKLSAKDGNLELSSTNMDLYLSQKIAVQVVSEGELTVSTKTLNDIVRKLPDSELTLTDLGTTGLEIKGKNCKFNLFTLPVSSFPPMDSINPEASFKISCTDFAKIIESTKFSISLDETRYNLNGVYLHIKDKEFCSASTDGHRLSISWVTLEKQIKNFGVILPQKSAEEILKIVKDPKNINEDIEILLSSNKIKFICNENTIMLSKLIDGTFPDYSAFIPESSSSKLVINRKIFADSIERIAIITVEKFRAVKLSLSRETLEISAVGEARGNAKEVINSSQDKESFY... | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalyti... | Q4ULS3 |
B8GP00 | RIMP_THISH | Ribosome maturation factor RimP | Thioalkalivibrio | MQLKALLEPLVTRMGYQLWGMEFRVAKHSALLRLFIDSEQGITLDDCTEVSRQVSALMDVEDPIQVPYTLEVSSPGVDRPLFEAGQYARYVGEQVRVRTQWPIDGQRNFAGAIVSADEDSVTLDVDGREVRLPLEAIARGRLKGTLPPATQVEE | Required for maturation of 30S ribosomal subunits. | B8GP00 |
A9M8W0 | DXS_BRUC2 | 1-deoxyxylulose-5-phosphate synthase | Brucella | MSRPSTPLLDKAPTPDRLRALPEQDLPQLAEELRTELIDAVSTTGGHLGAGLGVVELTVALHHVFNTPYDRIIWDVGHQAYPHKILTGRRDRIRTLRQAGGLSGFTKRAESEYDPFGAAHSSTSISAGLGMAVASELSGEKRNVIAVIGDGSMSAGMAYEAMNNAGALDARLIVILNDNDMSIAPPTGAMSAYLARLVSGRTYRSVREAAKQVAQKLPKFLQDKARKSEEYARAFFTGGTLFEELGFYYVGPIDGHNLDHLLPVLKNVRDTQKGPVLIHVVTQKGKGYAPAEAAADKYHGVNKFDVITGKQAKPPANVPS... | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | A9M8W0 |
A4STQ4 | MNMG_AERS4 | Glucose-inhibited division protein A | Aeromonas | MQYHEQFDVIVVGGGHAGTEAATAAARMGLNTLLLTHNIDTLGHMSCNPAIGGIGKGHLVKEVDALGGIMARATDLAGIQFRTLNSSKGPAVRATRAQADRLLYKAVVRQMLENYPNLKIFQQACDDLIMDGDRVAGVVTQSGIRISGKTVVLTVGTFLNGLIHIGMENYKGGRAGDPPSIALAQRLREMPLRIDRLKTGTPPRIDARSVDLSVMQAQYGDDPRPVFSFIGDASQHPRQVPCYVTHTNERTHDVIRNNLDRSPMYAGVIEGIGPRYCPSIEDKITRFADKTAHQIFVEPEGLTTHELYPNGISTSLPFDV... | 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. | A4STQ4 |
Q2IY23 | YIDD_RHOP2 | Putative membrane protein insertion efficiency factor | Rhodopseudomonas | MHSRLPTHAADLLQALSRLPRNAGRGLIWVYRHSFSALVGSNCRHLPTCSQYGDEAIGRFGLWAGGWMTLARLIRCNPYGTSGIDNVPETPPPGARWYLPWRYARWRGVNGPDCGCGHHDE | Could be involved in insertion of integral membrane proteins into the membrane. | Q2IY23 |
O26273 | GLMS_METTH | L-glutamine--D-fructose-6-phosphate amidotransferase | Methanothermobacter | MCGIVACILKDGSAAPVLLECVRRLEYRGYDSVGIATSDPMIRIKKDSGKIDEVDAELDLADLPGTMGIAHVRWATHGLPTAENAHPHTDCSGEIAVVHNGIIENYLEVKEELESEGHIFRSETDTEVIPHLIEKYMDEGMDLEAATATALRKLRGAYAIAAVSSREPGRIVGARKESPLIVGVGEGEYFLASDVPAILNHTSRVIYLDDGEMVILDGDLRVTDMEGNTVEKEVHSIDWSADMAEKGGYDHFMLKEIHEEPSAVRDTLTEWDEVLGVVEEIGEVERICFVACGTSYHASLVGKYLFESLLGIPTDVILAS... | Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | O26273 |
Q5WJ30 | DNLJ_ALKCK | Polydeoxyribonucleotide synthase [NAD(+)] | Alkalihalobacillus | MDKHQAEKRLKELRLLLEDYGYHYYVLDTPKVPDSEYDRLMNELLQLEADYPDLVTEDSPSVRIGGPPAPSFKKVAHRVPMMSLSNAFNEEDLRAFDRRVRQAVGEHVSYVCELKFDGLAVSLTYENGKLVRGATRGDGTIGEDITNNLRTVPAIPLRLKQPYSIEVRGEAYMPKASFERLNEAKEQAGEEKFANPRNAAAGSLRQLDPKIAAKRNLSLFAYSIGEVEGKNVQTHFDSLMFLKELGFKVNEEAAECETIEDVIAYTEKWSERRHELPYEIDGVVVKVNSLADHEKLGFTAKSPRWATAFKFPAEEVLTVL... | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Q5WJ30 |
Q6AQ14 | ATPF_DESPS | F-type ATPase subunit b | Desulfotalea | MKENIKRVLPFLLVLLFAFAPLALASAPVDAPAPADAPADALPSAKVISAPADAGVIEAVELEHATVTGAHDVAVAHVADSLSHEKLMDLFWRVLNFAVLMAILIKFGAKPIANALSGRQQRVKSEVEDLEARRIVAEKEFRQFEAKLANVEKDIDSIVDKAVAQAEIEKAKILERAEQAAADIQKSAEQAIQNEIANAKRSLKNDAADQAAVMAEELIVKHLTADDQVKIVEDYLAKVGAV | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | Q6AQ14 |
B4TX73 | AAEA_SALSV | p-hydroxybenzoic acid efflux pump subunit AaeA | Salmonella | MKTLTRKLSRTAITLVLVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITHVNVHDNQLVKKDQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRQEASRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYAGEFITRGSTAVALVKKNSFYVQAYMEETKLEGVRPGYRAEITPLGSNRVLKGTVDSVAAGVTNASSTSDAKGMATIDSNLEWVRLAQRVPVRIRLDEQQGNLWPAGTTATVVITGKQDRDASQDSFFRKLAHRLREFG | Forms an efflux pump with AaeB. | B4TX73 |
A3MPU3 | HIS3_BURM7 | Phosphoribosyl-AMP cyclohydrolase | pseudomallei group | MNAEAKPGDWLGKVRWDANGLVPVIAQDAATNDVLMFAWMNRDALAKTIELKRAVYYSRSRQRLWFKGEESGHVQHVHEVRLDCDEDVVLLKVEQVEGIACHTGRRSCFFQKFEGTVDDGEWVAVDPVLKDPEHIYK | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | A3MPU3 |
A2BNZ7 | RL10_PROMS | 50S ribosomal protein L10 | Prochlorococcus | MGRTLENKQKIVTEIKSLLDDSEMAVVLDYKGLTIKEMSDLRSRLQTTNGICKVTKNSLMRKAIDGDSNWNDLESLLTGTNAFVLIKEDVGGAVKAIQSFQKDTKKSETKGALFEGRLLSDSEIKEIASLPSKEVLMAKIAGALNGVATKIAISINEVPSGLARSLKQHSEKSES | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A2BNZ7 |
Q10WQ4 | CH602_TRIEI | Chaperonin-60 2 | Trichodesmium | MAKRIIYNENARRALEKGMDILAESVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHVENTGVSLIRQAASKTNDAAGDGTTTATVLAHAMVKEGLRNVAAGANPIALKRGIDKAAGFLVEKIAEHARQIEDSKAIAQVGAISAGNDEEVGKMIAEAMDKVGKEGVISLEEGKSMQTELEITEGMRFDKGYISPYFATDMERMEASLEEPQILITDKKIALVQDLVPVLEQVARSGKPLLILAEDIEKEALATLVVNRLRGVVNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENAKLDMLGKAR... | 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. | Q10WQ4 |
Q6P2Y2 | DAW1_XENTR | WD repeat-containing protein 69 | Silurana | MRLKRFLLRYFPPGIILEYEKGGELKTKAIDLLELSPTTDVDLVVEEIQKAEPLITASRTQQVKQLILRLQEKIGQQDSRQFYLFKVLRAHILPLTNVAFNKSGSSFITGSYDRTCKVWDTASGEELHTLEGHRNVVYAIQFNNPYGDKIATGSFDKTCKLWSAETGKCYHTFRGHTAEIVCLAFNPQSTLIATGSMDTTAKLWDIQSGEEALTLSGHAAEIISLSFNTTGDRLITGSFDHTVSVWEIPSGRRIHTLIGHRGEISSAQFNWDCSLIATASMDKSCKLWDSLNGKCVATLTGHEDEVLDVTFDSTGQLVAT... | May play a role in axonemal outer row dynein assembly. | Q6P2Y2 |
A6U866 | RL16_SINMW | 50S ribosomal protein L16 | Sinorhizobium | MLQPKRTKYRKQFKGRIKGVAKGGSDLAFGEFGLKAQEPNRVNAREIEAARRAITRHMKRAGRVWIRVFPDVPVTAKPTEVRMGKGKGSVEYWACKVKPGRMMFEIDGVSEELAREALRLGAAKLSVKTRFVQRIAE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | A6U866 |
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