ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
K1W4G5 | MAPHADDAAVCGSNGACSAPKKNQELFSVTSPNVVYTDSSILSKYSYRTTLVDEVDGKFVATPKETVYDFKTDRQVPKTGMMLVGLGGNNGTTVTAGIIANRDKLSWATREGDRAANYYGSLVMGSTVKLGTNAKTSKDVNIPFQNVLPMVHPNDLVIGGWDISGMNLADAMDRAAVLEPTLKAQVKKEMSAMVPLPSIYYPDFIAANQEDRADNILPGSKASLEHVEKLRKDIRDFKANNGLEKVIVLWTANTERFAELIEGVNDTADNLMKAIENGHEEVAPSTVFAVACILENAPFINGSPQNTFVPGAIDLAERHN... | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
EC: 5.5.1.4
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Length: 1005
Sequence Mass (Da): 108512
|
A0A355J275 | MESRNYFLYPLVSAVLLSIPWLFEFPGWLLFVGFVPLFLFENYLSGLPGKGSKYVFLNWILICFFLWNLLSAWWLGYATIVGLALFLFLNTFLMGTIWYLYHLFKKRTHENLALVFLVSLWLSFEFLHLNWDIQLPGMTLGGAFGNQVKIVQWYEFTGVLGGSLWILAVNIFIYKLVKFFLNFRKISFQHILSVLAVLLVPIVFSMFLYFSYSEKGEKLEFAVLQPNIDPYTEKFDKLRPDEQLEILLSLIDSAKGASFIIGPETALAPFGEDSIDLIPEIQQLKDAVSGLPEKKIIVGANTKKFLSENENTTITTRFLN... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A961JE42 | MTKLPSPVLALAAMAAATPAFAASGPFFSLHNTNFIVLLAFIVFLAVLVYFKVPAMVAGMLDKRAAGISAELAEARALREEAQTILASYERKQK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Membrane
Sequence Length: 94
Sequence Mass (Da): 10041
Location Topology: Single-pass membrane pr... |
A0A355J1L8 | MSLFIIAGAIGAWEIVAIVAIALLLFGGKKIPELMKGVGQGMKEFKKAVSGDSSKKEEEEEKEKEKIEK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 69
Sequenc... |
A0A355IWR1 | MSDTIDWSKLSEMEKLKHDSNYLRGTLVGSLANPITGAIADGDTQISKFHGMYQQQDRDLEKERKRQKLEPAFSFLIRVRIPGGKVSPKQWLQMDGLADTYANHTLKLTTRQAFQLHGVVKWYLKKTLQKINDVLLDTIAACGDVNRNVMSHANPAESAAHKELADLARQISEHLLPKTTAYHEIWLDKQLIAGGEKDHEPIYGGRYLPRKFKLALALPPYNDTDVFSQDLAFIAIQEKEKIVGYNVLVGGGMGSTFGMPETYPRLGNVLGSCKPEQVIDVAEKVLLVQRDYGDRSNRKHARLKYTIDNRGIDWFKNELN... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required... |
A0A545TNI6 | MTDLYAKHIDNKMAVYREVFDITPWRKVIIHAGSEHVQFRDDVHYPFKANPYFKEWLPLADYPDAYLVIEADQSLPRLLVKQVEDFWHSPAQPPAAAIVEAFDIAHYSSGAQLQAGLGIDAATVVIAEGGDDIARQLQRPEQHNNTEVLHIVDYHRACKSDYEIDCMSEANRIAVRGHRAAAAAFHEGGSEYAIHQAYLAATEHTENELPYGNICALNEHAAVLHHMHLNKTPPAERRSFLIDAGATCAGYAADITRSYQTDGPLQDPDFAALLAGIDAYQQQLVQRCRVGMDYLDLHLSMHTLLTRLLCEMGVFKLEPE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
EC: 3.4.13.9
Sequence Length: 444
Sequence Mass (Da): 49374
|
A0A350YYR7 | MIQIRHTFPPEERLKGVREISGLFTAGQSFLVYPVKVVWMLTDSHQTVPVRAAFSVSKKNFKKAVHRNLLKRRMKEAYRLQKHQLVMAAGEKKMICMFVYIAKEELPYPVIEKSLITATSRLGRNLKQATLK | Function: 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... |
A0A945Q921 | MAEERTADLIELARAVSGARVEGAENVQVCGMEFDSRRAMAGNLFVAVPGFEVDGHEYARAAVDAGAAALVLEREVDGIPADFPRIIVPSSREAMALIADAFYEHPSGELALVGVTGTNGKTTTTFLIDAILGAAGRVTGQMGTIQYRVGSQVIENPRTTSEAPDLQFYLSQMLEAGASHAVMEVSSHALDLGRVLGCEFKAAVFTNLTQDHLDFHGDMERYFQAKLRLFTEMAPENSILNLDDPWGWKIADEAAIRGAVIGYGMNEKADVRAEGLSISAEGMRFDLVAPEGNVPVESALTGQHNVSNILAAAAACLALG... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A433FCM7 | MATHRGSANANEPRPDLGNNAVENKPKGKRRAPAPKVNEEKPAAGGDASEPHRKGKRAAAPAETVGETSSEPANQSAKGASEAPRKARSRWKILGRVLEVAVVTAAVGILISTFFLSVLQIRGTSMEPTFHDGDLAVATHSKSLETGDIVAFYYNNKVLLKRVVGFPGDWIDFAEDGRVIVNGEKLDESYVLDPGEGGNVDITFPYQVPEGRYFVLGDHRSTSIDSRSEHLGTVAEDQVLGTVKAVVWPLTHVTWVD | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 257
Sequence Mass (Da): 27692
Location Topology: Single-pass type II membrane protein
|
A0A945C762 | MKNILIIFGGKSGEHEISVRSAKSIEENIDKTKFKTLAMGITHQGQWHSGPNIESVTHDGKVSSPKNPSLIPDKQILDADIIFSILHGPNGEDGTMQGLLELLNVAYVGPRVLGSALSMDKVIQKQVCAFYDIPQTKYISFSSYEWENSSDLVIQNINQQLQYPLFIKPANMGSSVGITKADSKEELKESIQEALQYDHKIIVEESIGEMREIEISVLGNNNPKASVCGEIVPNTEFYDYETKYITDDIKVAIPADIPQEVADEIRATAVETFRALDCIGLARVDFFYQPQTGKHFLNEINTLPGFTSISMYPKLWEATD... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 351
Sequence Mass (Da): 39... |
A0A0R1QE71 | MHTWAVICEIHVNNDCMVPFNAIEAELKEVSARVSGKFLNEVPPFDRINPTLENLTTYFFEVISNILRKSNAVLTRLEIGESPTRFYCMTLDQWSGQ | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 97
Sequence Mass (Da): 11152
|
A0A944VEN8 | AGGLTLAAERLMPVRGRVENFVTELEGWLSGGARVSIVAADRTQSLRVQSLLRDRGLGVSILPQGESPPEEGDKLVIAEGRLSASVRLPDEQRIFFRADDLLQRSRTREKSRAGKIPSGEGLSDIKVDDFIVHIDHGVGRYLGVRVLDHVEGQDEFLHIAYAGGDKLYVPMDDIDRVHIYRGTGQAPVLDKLGGTRWTKAKVGVKKALQSIARDLVRLYSERSSVEGISFGPEGAWDAEVASGFEFEETRDQDQAIRDVLADMEKSRPMDRLVCGDVGYGKTEVALRAAARAVSSGRQVALVVPTTLLAHQHWQTFAERF... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence ... |
W7BG95 | MLGYLLAQNFLNPLTKMAKTMNDIRDNGFQKRIEPTVITKDEIGELTLVFNDMMAQIERSFEQQKQFVEDASHELRTPVQIMEGHLKLLNRWGKDDPAVLDESLNASLTELERMKKLVQEMLDLSRAEQISQTKELQLVCVNDVLEQVRRNFEVMHEDFTFTLKEDDKDLHALIQHNHLEQILIIISDNAVKYSGDSKQIEMHIGKDQDKINVSVKDYGVGISKDEIDKIFNRFYRVDKARSREVGGNGLGLAIAKELVSGYLGSIQAQSEDSVGTTITITLPLIEKKEESAE | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 293
Sequence Mass (Da): 33408
Location Topology: Multi-pass membrane protein
|
A0A7C2E2G3 | MKVLVTGGAGMLARAVGAEFAARGVKAVSLTRQQLDITSGAAVAEALREYRPRVVVNCAAYTDVDGAEEEPYRAFLVNGLAVKRLAALCRVEGVKLVHISTDYIFDGTKGEPYRVYDPPAPVNRYGESKWWGEAALREEGGDYLIVRISWLFGPGGRHFVGTVLKRAEAGEEMRVVDDQYGCPTYAPDAARAVADLIAAGAQGTFHATNSGVTTWYRFARAVLEISGLKTRLHPCATEDFPRPARRPRYTALDDFPLKEVIGYRLPSWEDALRRYLTKR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 279
Sequence Mass (Da): 30757
|
A0A2H6EZY5 | MTIVNQVVREEAGDKEGEISVVFLPDEAIQGINRSFLKHDYPTDVIAFNLEDNPGEVLDGEVYIGFEQARMHAKEYGVSYREEIHRLIIHGVLHLCGWEDDTPPKKRKMAVRENYFLTKILN | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 122
Sequence Mass (Da): 14058
|
A0A2E8X8L9 | MQKNNEVYLLPELPEVETVSRGLKFKIVGKKISKYQQFREDLRWPIPTCMKELIEGTIIKSIGRRGKFLLINLDIDYTIIIHLGMSGRLLIYNPFDKYRKPSKEKEMGVFLHTLVKLGKHDHIKIDFDDGSQMVFNDVRRFGAIDLIRSEKLFFHKWLSKLGPEPLSNNFSSQVLQKKIENKKCSIKAAILDQGIVSGIGNIYACEALWEAKISPFKICSKMTEQDCYLLVKELRNVLKKAINFGGSSLKDFKSTGGELGYFQNLLSVYSRERLNCKRVLCKGKIKRKVQSGRSTFFCINCQS | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A0A090SG47 | MVGTGHSVYPLLPVIYDVSIKRGIRPERPMAIATVASQMGITASPIAAAAAVVMATAATNNLDITLGQVLMVTIPATLTGVLIAATWSLKRGKELNDDPEFLERMKDPQFKAQLIDTSEASAGEAGMKENQTAKRGLTVFLLGILTVICVAMFGKDLGLLPDGVSTSTALQFLMLSVGAIILLTTNVDPKKIVNTNVFIAGMSAVIIIFGIAWMSDTIIAYNKPYIISLVEDVVKSHPWTFAIAMYVSSVFLKSQAAVLTIMLPLGFALGIPAEVLIGVLPACYAYYFFPFYPSDLAAITFDRSGTTKIGKYILNHSFLI... | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 372
Sequence Mass (Da): 39680
Location Topology: Multi-pass membrane protein
|
A0A126QYI9 | MNTNRFETFFDAVLAIIITVLVLKLAQPIAPTFEAILLLNTNFITYAICFLVIFILWYDNHNLFQVVDEIDNKVLAIYAIQIFAITLLPYFSTWVVLDTNSVVAETMFGIDFIIISISYILSIYAVFRANPYNCGLCEANFRSVYKYIPLLISILGFLITYTVFTPGIYVCVLVSSVFWLFFARLQRPDKGTTDRFEAFVDAIIAIIITILVIEIPMLTNGSWEAFLDIKLDFIVYAVSFLVCFNFWNYGNNIFHIVNKVNSKVIWSTGVSLFFLSLIPYLTTFVGLNPNSFVPCFLYGLDFIVVAILLIITSNALKSSD... | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 379
Sequence Mass (Da): 42898
Location Topology: Multi-pass membrane protein
|
C7LRM9 | MSTFDQGLIAQIKARLRIEDVIGRHVELRPAGNRLVAPCPFHQETKPSFSVNPEGGFYYCFGCQASGDIIEFYRAINGLEFVEAVEALAREAGLEVRRRPEYMAPGEISRSQCLDMHALAAVFYREVLGRAPGQAARDYIARRGLASEIVERFCLGWAPAGWNELRDHLRGRGFPEAVAEKAGLVSKSAKGSYYDRFRERLIFPIMNLSAQTVAFGGRSLVDGDGPKYLNSSETPIYTKGEHLYGLYQARRAMSHSKSVLLTEGYVDVLSLHQFGFENSCGVLGTALTPEQVHRLSGLVGQVDLVFDGDNAGRKAALRSA... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 567
Domain: Contains an N-termi... |
K0K3Z3 | MIELKTPAELDAMRAAGLVVADALAAVRDHARIGVSLLELDEVAADVIRGAGAGSSFLGYQPSFATTPFPGYICASVNDVIVHGIPTGYRLRDGDLVSIDCGAHLDGWHGDSAISFVVGTAAPADLALIETTERALAAGIAAAVPGAKLGDVSAAVGRIGRAAGYGMPSDFGGHGIGRAMHESPGVPNEGRPGRGLTLRAGMAIAIEPMFHSGGRDPYYEAEDGWSLLTSDGSRAAHVEHSVAVTDDGPRVLTAPRLPAASTTS | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
D3LU99 | MAKGSEQLKNFEANFSKLETLVNELEATDLTLKESLDIYEKAMKVSNACVQALDYAQQRATELANTRPVLTERVRESDDESV | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A291IRY6 | MVIINGDINDIQKIPGLKKSIVVVGNFDGIHTHHEKLLRKAQELAIKNDLQLVLVSFDRSWRTLFNQEDDRILKKEEKIEIMDGFFAIDYYIELEVNENLKSYQPKQFMEWMKKTLKCQMVAEGSDFTFGTNSKGTVKELKEFFGDDNVYVMRRKNLTTSSTKIRKLIADGKVDKANKLLYSPFKIYFATEGKRSREIIYPNIKIKEGYYQAKLNDKVNAVLRIDNKAAILISKTGEIEEPVIYAILEKKISKPTK | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 256
Sequence Mass (Da): 29652
|
A0A101DJT3 | MALRLQDLPAPAAHLVLKVERFLRQELKVSTQNKSLLLSLSGGPDSTALALILTLLKKRLKLKEIAGFYLDHGLRKESKEEKRFLEDLSQRQGFSLYFFSTRVDLIAQKTGKGLEEIGRNLRYKLLTYLTKKYGFELVALGHHLNDLAEDVLMRFIRGTGWPALGGMEAKIEQDFFTLLRPLIFLTKEEILKFLELVGQGYCVDKSNEDLSFLRNRVRHNILPLFLKENPLFLKNVFKIWKISQLERRDLKQILNKIEIKKDDCCIEVKRKDLEGLASLDRLNLLAFYLDKIGKGQVLFDNLYRLELFLEQDSSSAKTFE... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A0W0W165 | MKKVIAMKKGVFQANHKKSSLQKNGLLFNSSRNEIEIAALLLTDDFKIYDANLCGINSLFNKKKSSLIGQSFIDLLDVQQMDIQALLKAFKKSRKSRFQSIKLEHPILKKWYCIIITALDDFSLVSFAVTLITTNYSYQALQTYINAIINNLPGAVYWKDLEGHYMGCNKFVAQMAGYENPEQMIGKTDYDFCWSEFADDWRLLDNKVVKENSTIAREEMVKLANGNVRTELTFKSPLKNEHNEIVGIIGTSLDITERKEMEAALHESQLAAESANIVKTNFIQNMQHDIRTPASSIWAVLEDLVENNKTPDRELLVLLR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 833
Sequence Mass (Da): 94690
Location Topology: Multi-pass membrane protein
|
M8BB85 | MNVARLNMCHGDREWHQKVISSVRMLNEEKGYAVAVMMDTEGSEIHMGDLGGAPAAKAEDGEIWTFSVRSFEAPLPELTVHVNYEGFAEDVRVGDDLLVDGGMARFEVVEKLGPDVKCRCTDPGLLLPRANLTFWRDGSVVRAKNAMLPTITSKDWLDIDFGIAEGVDFIAVSFVKSAEVINHLKSYIAARSRGRACSFFSYFIRRMLVTKLQPSHIFLHYPYVTFLPPSTARATESCQPSKSPRKAEIHPFIAAYWKIIH | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 261
Sequence Mass (Da): 29252
|
A0A2D0NL26 | MLVLAEKYMQRCFELARLGTGSTAPNPTVGAVIVYQDRIIGEGYHTRYGHPHAEVEAVRSVSAEDRHLIPRSTLYVSLEPCSVHGRTPPCTDLIIREKIPEVVISYIDRSPGVNGEGVARLREHGVEVVEGVLSEAGKLLSAPRNIFVTRQRPYLILKYAVSANGYLGLPDGKPFWLTNGYSKRLVHRWRSEVDAIMVGTSTALYDNPRLNTRLFPGSSPIRVIPDRNLRLPLHLHVFDDSIPTLIFTHQNPPDHEFTQTEYIQLEPEDFFGALLRELHRRNIQTLMVEGGQVILEHFQKTGLWDEARIFRTPHYLEEGL... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A914DUY1 | MLSRKMLIFLLSLIFSTCIAVLDIGAPGYSCAANLMMRSPTRPTSAHAVRPADIDIVMAMGDSLTAGFCTDDVDKCHAEYRGLSFGGGEWRGLDTHITLANIIQKYNPKAVGGGLNGTGGWNDFPVAQLNCAISGMRANNLPYQAQNIINTLKAHPDLFDMQNDWKLLNIFIGYNDLCNCGGNDCYCHNKTAFDAQNYANWIRTALNLIRSNVPRVIVNLVQMTHLEHFAGCGTGACGICNNVTVADLTTLINQYQAAEKALETDGEFDTTDDFTLVVQPWFTNNTKPYYPNGTINREFWAVDCYHYSSYGHALLSSWWW... | Catalytic Activity: 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+)
EC: 3.1.1.3
Subcellular Location: Apical cell membrane
Sequence Length: 393
Sequence Mass (Da): 43002
Location Topology: Single-pass type I membrane protein
|
A0A545TLS9 | MTPPLIVCMGVSGAGKSTSAQILAAKFELTLIEADDLHSLSNKQKMQAGAALTDADRAPWMQAVCRQLSTCAERGIGCVLAHSALRRAHREQLRSCGLRTLFLHLDAPRETIARRLREREHHYMNAELLDSQFEALQPTDGEADVVTLTALDREALMAQASARVVDFIAQGTITGDTGHAVTTHH | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 185
Sequence Mass (Da): 20138
|
A0A1J4XCF8 | MSKSKIVGAIEIGTGKVAVLVGEIVNGRSLNIISLGESVSSGVKKGEIINFERASQATHAAISQAEKSGGIELESVYLSQTGRHLNGFYDTGSINVSASDHRVSKADISRVVREAKSRELEQNRVYIHHVQNEFKVDGRTVENPFGMEGRKLEVGYWSIHGDVRRIRDQIHIINGFGMQVEDMIVSSIASGCMVASDIEKKNGVLVIDIGCGTTDFVVYKDSYIVYTGVIAVGGDHFTNDISLGVRVSCDEAEYLKTEYGKAYVDEDTRSDEIKVDQEKRVIRREALYDILQARAGELFSLIRRQLEGSVKLEELAGGAI... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 400
Sequence Mass (Da): 43482
Location Topology: Peripheral membrane protein
|
A0A6B9QR88 | QELKFGRKTIFSTKKNMHVMDDMQNGTYTPGVIPPVDATRPIPLGRRDVPGRRTRIIFILPYEYFIAQHAIVEKMLSHAKHTREYAEFYSQSNQLLSYGDVTRFLSSNSMVLYTDVSQWDSSQHNTEPFRKGIIMGLDALTRLTNDPKVINTLKLYKQTQINLMDSYVQIPDGNIVKKIQYGAVASGEKQTKAANSIANLALIKTVLARISNDYSFSTKIIRVDGDDNYAVLQFNTEVTKQMVQDVSNAVRDTYSRMNAKVKALVSTVGIEIAKRYIAGGKIFFRAGINLLNNEKRGQNTQWDQAAVLYANYIVNKLRGF... | Function: RNA-directed RNA polymerase that is involved in both transcription and genome replication. Together with VP3 capping enzyme, forms an enzyme complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a dou... |
A0A1J4XCF7 | MLAIPETIAPLLKRPVGVFGKGVTGKAVVDLLKVMGAAYVVYDEKCLECSVFDSIAAKQHNLVIYSPGFSQEHPWLKLARENGCTCLAEMDFAAVFWQGEIIAVTGTNGKTTLTEFMAQALCQLGKKAIAVGNNGSPLSGFWRNFEDKAAVAVCETSSFQSEDLKYLQPDAVLWTNFDEDHMDRHQTMEKYFNAKWNLIERLQNGIAIIGESVYQWAKKMNKTMPANLYIAEDQSHMPTGTIFEKYPQSENFAIARKYWVEKDYALAILLEAASAFKLPKHRLQKVAKIGEVSFWNDSKATNFHATQAALRGFEKPIIWI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
F4NUV9 | MSTTSSAPPHQPPATDPELTDFLLRLRKKNTDPVAHKSTVDSYAKYWDVDHKQGLENTEDSVAERRKDSDILTNHFYDLVTDFYEYGWGTSFHFARMFKYSSIQHCLARQEDYLALKLGLGAGMKCIDVGCGVGGPLREIVKFSGAHVTGLNNNAYQVKRCHYLAEKHGISNLCDAVKGNFEDMPFEANTFDAAYAIEATCHARRLENPYSEVFRVLKPGAKFACYEWLTTKAYDESNLSQKKIIHGIEEGNSIAKLYTIPQTIAALKSIGFEILEYADLADPKSAMYEAQDPWYTPLEGSYSLNLESIARWRMNPVGRI... | Pathway: Steroid metabolism.
Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of lanosterol to form eburicol.
EC: 2.1.1.-
Catalytic Activity: lanosterol + S-adenosyl-L-methionine = eburicol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 376
Sequence Mass (Da): 42138
|
W0QCS8 | MALLNLSNAYLGFGDHPLLDHTELHIEPNERVCLVGRNGAGKSTLMKVLAGEVQLDDGKLIFEKDIVVTRLEQDPPRHIQETVFDYVAEGIAHLSDLLKQYHHISQQMLTDYSDELMAKLSAVQAQLEHNNGWQFENRIQDTLKLLELDPEKRLCELSGGWVRRAALARALVADPDILLLDEPTNHLDVEAITWLEELLLNFKGSIIFISHDRSFIRKIATRIVDLDRGKLVSYPSNYDKYLEEKAEDLRVEALQNELFDKKLAQEEVWIRQGIKARRTRNEGRVRALKALREERRNRREVQGTAKIQIDNTARSGKIVF... | Function: Part of the ABC transporter complex LktBD involved in leukotoxin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.
EC: 3.6.1.-
Subcellular... |
A0A1V0HU13 | MTANRAERDGAPEKASDKASDGGGPLLWLHNPPPDERAAAAELIRELALERPDLRVLVTGRDALPGWPAHATGLSGVSVDLVPSDGHRASVAFLDRWRPELALFYPDHLPSTLISLADTRGTALFLISRDLPRSWRSRWRVGIAGTGRLLRRFDRIFAQTPGTAGELRALGLPRWQISPCGPLSEGSAALSCSEAEREALAEVIGGRPAWLAAATRPEEDAAVIAAHAWTTRHAHRLLLILCPEPFGRGRALAARLRADGWDVALRSDDEEPSTETQIYVADTEDEFGLWLRLAPVCFIGGTLAANAGPDPYRAAALGSA... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A109E1P6 | MIASPPANAAALSDPFGVLSATPVRYCIDIQPSDELSLADAVVLSLCRDPGLAGAIFSERNAQAAVGMAKAAYLPSLSLQGDVGRQSSTITGASTNSGNASDLTASLSYVLFDFGKRRATLQQSLANASVQRYARVGTYQQVMLDTAADYIALISLQLQAKAASDEAAAADEALTMASAKYKAGEVARSDVLQAKTVAAQARLTVVQAESTLRTAQAKLAVALGWPVNSPIRLTPAEVRDAAAADLQPLDAMLAEAATARPDILAAKAQLQADGDQITIARAQYLPTLSVTASSGTSTLPGSPRTRTGSAMLSLRIPLFN... | Function: CyaE is necessary for transport of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin).
Subcellular Location: Cell outer membrane
Sequence Length: 438
Sequence Mass (Da): 45499
Location Topology: Peripheral membrane protein
|
W6MNG6 | MSFDINWESLVSDAAVNEKLATFLNDQLSSITLPEYLSGLKVIKCELGDRAPEITVRNIDVPFPEFYKDVRQSKEESGDEYAESDTVVRHGTVSPCGQTPSDMVTGLGVTMESSISSLGGLHDTSSMSTTPLQSPSHLTPSVLPGFMNRGLLVSTPLSHPASGSFNYLSHHGHGVGISGSYFPSFASRSNSQFSSRQASPPPLPQHSEMSFDSPKSDPNSRSRTPEFNESFTNAETNEGVETKNQDVKDRDLQVIAEIKFDGDIYIEVTANLLVNFPAPNFISLPVRLKITDLQIHSIAVLAYLESRLYVSFLCDVEDNE... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A0A5C5XBF5 | MVYAVLLPILLFMGLGLLPVANSIRGTIGIRRLVTSVAALQLAISLIAMTAFIFAGRVPQFLEIISVGESSPIGLNLYYDGYSSLMLLLVSFVGWIICCYSSRYLDGDEYESRYYRWTAFTIAAVSLMVVAGNLLMFFMAWVLTSSGLHMLLTHYAERTAATRAAWTKFFISRIGDIALIMAIVLTFQEYRTFDFPELFAAVRLNVVEGVPASVNSLIIGWLLMLGAVTKSAQFPFHVWLPQTLETPTPVSALMHAGVVNAGGYLIIRVSPMLVYCPGVLETLAVVGGFTACFAAIVMTTQTSVKKMLAYSTVAQMGFMM... | Function: Part of an energy-coupled inorganic carbon pump.
Subcellular Location: Cell membrane
Sequence Length: 523
Sequence Mass (Da): 57195
Location Topology: Multi-pass membrane protein
|
A0A0C2WYM7 | NFKAYNINFVNGYGAGAQAVAVTANGNKQGYYGCSFKGYQDTLYAKSGLQYYSNCYVEGAVDYIFGKAAAWFGECIIASNGGGYITANSRETSSDTSWYVFDHSTITAASGASVVGKVYLGRPWRVLARVIYQNSVLTNVVNAAGWTTMADGATPIFQEYNNSGAGSDTSKRHEYFTAATSAVSKNTLWGSDWQSWVDTSY | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
EC: 3.1.1.11
Subc... |
A0A0C2WYU8 | MSLFRPASAQIPVQTRVYCDRCQRWFVNDRALEQHTSASFRHNVCSGCDFDYITRDEMEDCDCDGSEDDDEDLSDEYGSAGTLSDDGGGAQDPSAYGFVLGDRFNTYYTVPGAWRGGTRTTPSPSGSSLYAYPDDTYDPETLGGYESEDYGTPSEASYSHSEDATEEDEDEEDEEPHRDVGQLPAQNAEASPYCQRCNRVFNTVNGMHMHNRMSNMHPWYCSSCRIDYDREDDLERHNSTVHANGAQPAARQQSTAGVADTRSRAVTTVLGHLSTQLRGMLDRSAPADADTSSSTIQPTTINAPVPPPLPSTQAEPIPMD... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 4... |
A0A011AAB5 | MLYPVAGIVAEYNPLHKGHLYHAERARETCGAEAAVAVLSSNFVQRGEPALLDKWTRAKTALSCGIDLVLELPVIFSSHNAGVFANAAVDILAATGAVTHLSFGAENPDCLVDSIIDILLEEPEPFKLSLKKYLTAGFSYVEARARAAEELLPGSAALLAGSNNTLALSYMMRIKKKNYPMRPVPVKRLGSAYNCAELEEIPSATAIRAALREERRSEALLYMPAAAAGILEDALNTGRACVSHDTFWKLLRAVILRTKTEELANCAEIGEGVEYKMREAAREAKSFKEWTDACTSKRYPAGRIRRSAVHAALGLDHWTN... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
W6MRK5 | MGEPNEPTTKVLSEAQLRAQAKRQEKLARRKVYGDLLVQGTNDSSIVSKRSVERLYGSVIAAANGKKAPEYFKPFVRKPQRRSPVINRGYWIRVQAISRILDEIASKSADGTIIINLGCGYDPLPFERIDNAENVFCIDVDYPELIKNKTHMITSSPEILEIIGPKVSPKHPAIGIQTERYAAVGCDLRDLKLFKEVLSSLGVYESNTTSIFVAEVSLAYMLPEFADPVIAETSAVAKSHFVLLEQIMPAGKDHPFARTMLKHFNKIGTPLGCVSKYHNTELQEQRFRDLGFLFVKSTDLWTSWKETDAKTKHLIETIEG... | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
Function: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of euka... |
S5U0C6 | IGTLYFIFGTVAGVLGASLSTIIRIELSTPSSFIGNDQMFNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGSPDMAFPRMNNMSFWLLPPSLVLLVLSSAVESGAGTGWTVYPPLSSNIAHSGSSVDLTIFSLHLAGISSILGAVNFITTIINMRSTGMTLDRTPLFMWSVMITAILLLLSLPVLAGAITMLITDRNMNTSFFDPIGGGDPILYQHLFWFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1I4JL42 | MWWLVTPGNPLKDPGQLAPLDERIAQARRVATDPRIIVTGFEAAIGSRYTVETLVWLRRHRPDLRFVWIMGADSLGSFHRWRRFEEIARLMPIAVIDRPGHTLAAPAARAARRYADARLPEFEAPALPSRKPPAWVFLHGPRSALSSTALRAGRSA | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A7J5ZAG6 | TQFSCFVAKRPSGGGKGKERGETDVLERKKAEGKVSSQAVDGYSSAPVKEDTAGPDCSLPRPVPRMSSKAHSSNSIAHARRTVQQLRIEASIERIKVSKASADLMNYCSEHARNDPLLMGIPTSDNPFKDKKTCTIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
A0A6N0HUD0 | MNYQHAKHAGNYGDLLKHSVLCQVLQSLTQQDKPLFYSETHAGAGGYRLDQRGVDPFGIERLWGVSNAPQALADYLTMVAAFNRSEILQNYPGSPWFAQQLLRGEDRMRLFELSPEPYQQLVKSFSHDVRIELFAGDGYSGVVEPIPGMRCRQVVLIDPPYESVSDYSDAVDTLLEIYRREPQGCYLLWYPTHDRQRIESMEQRVRAGVFNALCVCELAFGRGDEARGSGLFILNADTDLIRKITETLAWLAAEVDAAGTGRYRVEPMSADVS | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 273
Sequence Mass (Da): 30747
|
A0A7J5XE36 | MCTLVKPPWMYNLTIQVTTFLFFFLPMLTISALYTLIGLQLKREKMCHTLEAKTVFGQDSFCNIRTQQQKARRRQVTKMLFVLVVVFGICWAPFHTDRLMWSFINNWTDNHLHIFQYVHIISGVFFYLSSAVNPILYNLMSTRFREMFKEVMCHRPHDIIPRKHSLSVTRMTLRSTLSDAPLSSGAAVVEAEAEDGEVRIKSETSFSC | Function: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
Subcellular Location: Cell membrane
Sequence Length: 208
Sequence Mass (Da): 24197
Location Topology: Multi-pass membrane protein
|
A0A914EMR9 | MLPSKNQQCLFILSLICFILLGVGLFGNDHINKGVNSAIASLDDVNRNVKLAISQCDNLNSTQYSAVQHVEELVKLVERKAKETPDINQTAYKEVDAALTAVSDKVDEIKTQLVKIGEILVDVKFLEKAEVYGDRIEFERWILGATLLSIMFAVLFAGIIAFCRQSRKGAIVFSGLGLAIFILAWIIFSVVFPLSIAHADFCVSGNKFLSSKLNKEIIESLHFYKTCEYHPAHDNVPPNIPLAKLSTHLTSTQEAETHLENLLNNFFNQSVEIQNVTRLIDADVSQAFKNIGALESTLSCYAIREDVVSMHEGFCTAGIL... | Function: Probable chloride channel.
Subcellular Location: Cell membrane
Sequence Length: 473
Sequence Mass (Da): 52196
Location Topology: Multi-pass membrane protein
|
A0A963TFD3 | PLIYGTLGEVPVLGLPGNPVSVGVTSALFLRAAMAVMLGLGDGTPEIRTALLGRDLEANDQRQDYLRAALSRTADGDLVATPFDRQDSSMMAFFARADALVVRAPHAPPARAGERVEIVPFGLGTLSF | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 128
Sequence Mass (Da):... |
A0A1T4L7G2 | MATGNLELEEGRTLSPRFDDKGLITAVVTDVNSGGLLMVAHMNREALDLTLQTGVAHYFSRSRQALWRKGETSGALQTVKEVRVDCDQDAVWLKVEVARPEDTCHTRRTTCFYRTVEWRDGAPVLTTTESRAGD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
EC: 3.5.4.19
Subcellular Location: Cytoplasm
Catalytic Activity: 1-(5-pho... |
A0A1I4GK58 | MIFTRLELKNFKSHAKTKLDFNPGISLIIGENGAGKSTIFEGISFALFKVYSTKTISDLARSNKNIGDKVEMMVKLSFISNGIEYRVERGVTLNKSSSKSTSNLFKITNAKDEIIASGNKEVDNEIEIILSMDFSTFLNAIHIRQGEIADLIDKTPATRKKLIGKLLKLEELEKAYDNLPRIIEDYKTRKAILEDRIQAESELNFELKKAKQEDFNLSEKNNALKEDFEGLKGEIEEKNREKEELDKEKSEFESLKLKFIHENDNKNSLNKSKEEYFNKYNEILRNEGEMNLLKSSSDKLPIYKAFKESLLKLDKLKEDE... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
A0A368NHC5 | MGNFLQPSYAPSPSALFSALNNIRRIIDRGIRYAGDLVAWCGGIMMLLIMLIVVLRYLFNLGWIALQESVMYLHATAICFGAAYTLQQDKHVRVDIFYRRFNARQRAWLSIGGTLCLLMPMCSMIFSVSWPYVMDSWLHHESSQETGGLSGLYLFKSLLLVLPTLLYLQGVSWIISALECLFGPSQGRAQ | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 190
Sequence Mass (Da): 21450
Location Topology: Multi-pass membrane protein
|
W6MGX6 | MLKNIQGGYPLFIRQRLSLYRQIHTPRLYDGSSSRRKEKLTGFLAFKKIITSVLDNEVEKRKHTWKSRLPDLQLKYDPREIGGFDTFGVSPLVVQALNQTFPEVKDPTETQKKILSVLGSGFSVIAKETQGSGKSFSALLHALSRPRALTYLGKPATTTLILVKTSSLARQYELQLLRILDRFDGETAKVAQFLYRCNDKTEEKAQLEKWKTLEPPHIIVATPQRLLDAILESGSPNGLGLSDLRLIICDDAEFLFVDGATSMAKKKNKKKKPAESVMNYLLELRDSERDPKLGTPIRKQSAQMAFFIDTMSSEFIQMLQ... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 601
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 67993
|
A0A261SPY1 | MIARIPFRPVKTVLVTVALAAALTACSGGKWGFPYKADIQQGNWITSEQVALLQQGMTREQVRFALGSPTLTSVLHGDRWDYPYYFKPGYGKAEERQFTVWFENDRLTRWSGDEQPELQPFQINKPDAAALKRTDKEEAREEKRDESEEKAPRPQINAPANPATQYPGAPGSSPEPIR | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 178
Sequence Mass (Da): 20064
Location Topology: Lipid-anchor
|
A0A914D8B1 | WNPVYLLLLAVSWHLMSLVWKAFKNYTDAYMTDFIIDAKLAYKLSYKYDEMTKRYKDEVLKALKFLRTSGIGTQVVFGYLVSMWITFLVHLAQFFIVTNFAAEESYLWGFYAVSNSWKSGTWVQLKSFPYISFCNMDRAV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 140
Sequence Mass (Da): 16516
Location Topology: Multi-pass membrane protein
|
F4NSR1 | MSRLLLRLLPTVRPLAIAAPTRFVAPRATAPMASLLSIRNYASHELDPANKSEYDAYVQQWMKHFTNVEDDFELERGLNHIFAADWVPSVELVALTLKAARRLDSFPTAVRILEGLKDKAYKPEQYQAYIRELKPLLEELGIPEKQDLGEFDIIRERNPWTE | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
F4P104 | MEHSSKDNSPAKWRELYHGIKAYRQDHVAPVDVVGCAMLGDKTDPKIYRYQTLTALQLSSQTKDAVTAGAIANLKSHEPGGLTVESILAMDPKTLDGYISKVGFHNRKALYMKQTAEILKTQYNSDIPDTLSGLMSLPGIGPKMAHLAMQEAWNQTVGIGVDTHVHRISHRIGWTKYLKTPEHSRKELEEWLPRQYWNEINKLLVGFGQTLCLPVGPKCTECPVSHLCPRIGVKTTSAMQNKLVQIQSPFFNDSPRPAKRTKTTDR | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base exc... |
A0A2R6FEK4 | MDCFYAACERLREPALRGQPLVVGMGYESDEAHGAVATASYEAREFGVESAMPISEALELLPRKVDAATDPDLDVEEAGFYRPVDLDYYDEVGSEVKAVLHEHADVVREVSIDEAYLDVTDRVHWDGDATAGGTVGGATGAGATVDGVTGDETDTQRVTGFARELKERIREEVGVVASVGVAPTMSAAKIASDYDKPEGVVVVEPGEVREFLAPLDVAEIHNVGPVTARTLRDMGIETAGDLADADPDRIRDRFGERGLEVRRFARGEDPREVTPVGEPKSLSRESAFTEATEDFEEKRKRVRALAADVAERAEREGALY... | Cofactor: Binds 2 magnesium ions per subunit.
Function: 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'... |
A0A191ZKU2 | MSFLKLVQHSLIGLLVGLSFTTPQRALADDLLPPEQAFHATAEIHNNTLEITYHVANGYHLYQNKIEIKSDTPSLELGKPILPEGVVDNDPYLGKLIVYKKDFVVDVPVTKRAPGPVTLNLKYQGCSDTQGVCYPPQTQLIQMTLPAQSSSSAPTEPTASSANSLEALAGNMGGEADQTPLEPEQAFKPSITMKNGTVSLSWTIAKGYYLYRDRIKVALDATDARISGTDIGAGDLKDDPTFGKTFVFHHDLTTQVAIKAGKDKTAVLVAGYQGCAELGLCYPPMEKAWKIDLASDTVTALDSAPKVKLKPIADYPSLSA... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
A0A914DRF5 | MRPLIFLTQSRQKFLISYVPSFCSLCRCHVKKNDDHRIIGLGSRAQKYQDEFGTKRPRKKFEPSSLIFLVIPATTFALGCWQVYRLQWKTDLLERIRRRMKASSIDFPINDLENINDYEYSKVRINGRYLYEKQITIGPRRRFDKNAPTSQNDHATETDFGYQVITPFQIDGSDKVIMVNRGWFPDKNAPSGPSGTIPIDGIVRKSETKGLFGYENIPEQGVWYYKNAEQMARILGTLPIIVDASLETTIRGGPIGGQTLIALRNDHVSYFLTWYGLSIATSYIWWKRFIR | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 291
Sequence Mass (Da): 33708
Location Topology: Multi-pass membrane protein
|
F4NZL0 | MHGQYVAARPSNTTQQTCNTIQDSSAHLSWSRCIAIHVRSTSILDRIIKIDKYDFPLHLYFYYFGMSVLLETTLGELVIDLEVDKAPQACINFLKLCKLKYYNFVLVHSVQKHFVAQMGDPSGKGTGGNTVWGIIQDKDNQVFEPEIHPKLKHNRKGIVSMALVPCDGRLMAGSQFLITLVDTHLEYLDRKQAIFGQVAEGFETLDKINDAICDQEGRPYRDIRIKHTIILDDPFDDPEGLVVPIRSPIPSEEMLKLSRIGEEDELAPKLSEEEADRLRKKQEAEARALTLEMIGDLPFADIKPPENILFICKLNPVTRD... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Nucleus
Sequence Length: 521
Sequence Mass (D... |
A0A1S2DCW0 | MEGTTKQTFSDNHGAVATTALFIRYLLDIVLGSMMFVMCVVMAWQVFARYVLGDASSWSAEVARSLMVWMAMVGSAAVIQRGGHVTVTVLLDRLPLTIKGGILVIRDLIMLIILGVMFFYGLSFAEMNAIQLSAALEISMAWIYASLWVGSALMAVVLVLIRLERRAPDWTRDADGFE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 178
Sequence Mass (Da): 19629
Location Topology: Multi-pass membrane protein
|
A0A7J5YLS3 | MSSFNEKFSSYTMSQLNEVLEDDEKLSDMVQDMEEMHGVQQSKETTLVSNRTLAEQNLDLQPRLEQRKETLTQRYARLQENFDCSTTRKESALKADTDHTSGNTSLDILLALLQAEGAKIEEETENMADCFLDGDMPLDSSSTRTRATGSWPTCGG | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Subcellular Location: Endosome membrane
Sequence Length: 156
Sequence Mass (Da): 17540
Loca... |
A0A6G8F3W4 | MILPPDFECPELNDSKQLSEKKRARLRPFIEENALAWAVVMVDAAEIDRINILNASIIGMQRALDALSVTPQHILVDGNRFKPYRDIPHTTVVKGDAKYMSIAAASILAKTHRDELMESLAAQYPGYAWEVNKGYPTKAHREAIAKLGPTPLHRQSFRLI | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 160
Sequence Mass (Da): 17989
|
N1R3B8 | MQPPPFYFHAAVPVPSSAVPVRSVWAWNFREESDKLCHLAWNARYVAVDVHYPGLVHHADRNHNILTVEERYAVLKANVDALKPLQVGIALRDGHGRHLGAREFNLRDVCAVSDPHDENSLAYLAGRGLDVDRLRVRGLSAQMLREKLLRSGLNKCEHQDLNPGRLGIPPSL | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Nucleus
Sequence Length: 172
Sequence Mass (Da): 19303... |
A0A7J5Z0H5 | MLSAAPEWRKAQYKFENWGWTLSMAKLNEAIVRVLGKHGRLAHVNRAVAKQRSGCLSGFSVVVTPAQFNDNKGTLANRVRGRAINVVTQQINNYWQIYCSHVMSLPESFLNRVFMTVPCSFTLSPLSPSTLRRQSAPPAASSSSSSAGGVSGSSVTGSGFSASELIPPRKVLYTYPKGAGEMMEDGTDRFLCESVFSYQVPPHLNRSNVINKCLDWRNLRAWWRSWKQMSGGTNQLNSYWDSRRLK | Pathway: Protein modification; protein ubiquitination.
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degra... |
A0A368NQI3 | MVIRALYSLLLYLALPVGLLLLHWPKGSKPKIGKRWPEHLGFVPPVDGHPLWLHAVSVGEVIAVTPLVERLLAEYPKLPILVTTTTRTGADRVQAAFGERVIHRYAPLDLPDATSRFLRRTQPRLAVMMEMELWPNTLAACCRQKVPSLLINARMSDNSYRGYRRFRWLISPALQGFHSVLAQGGQDAAHLIELGADASRVTVSGSLKFDIKISEQTTKDGHSFRQNIAARRPVWIAASTHQGEDEILLDAHQRVRQQHNDALLIIVPRHPQRFDAVASLCQRRAEAEGMIFNRRSLNQLDPTCGIYLADTMGEMMLLLA... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
D6BPV3 | AIGLLGFVVWDHHMFTVGMDVDTRSYFTSATIIAVPPGGIKIFSWLATCHGANISFNPSFLWSLGFIFLFTLGGLTGVVLANSSIDIVLHDTYYVVAHFHYVLSMGAAFAILAESLQWFPLFTGMTLNNKFLKTQFLVM | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A4R6BSU4 | MMKYYQTKFEDFQNQTITEYIIETDHMQFSFLDYGARIHKILTDKNDDQSNIILSMNTIEDYNESGGYFGATIGRVAGRIARGRFDLNGKSYQLEQNDGENHLHGGSNAVDKRIWMTTVEEQQDAITLKFKTVIYERDDHYPGDITFEVHHTVTSDNVWKIEYFAVSTEDTLFNPTNHVYFNLNKDYHKKIMNHQLQLNHDQFVEIDETLIPTGHIKNSPNFDFSDFQALETGIMNQDEDNQLVDGYDHPFLLQKGDEKTFTLTTDSDDITIDVTTDRSCVVIYTSNMLNYRSSDDIVLEQYSGVTVETQEIPDAINHAD... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 342
Sequence Mass (Da): 39634
|
A0A1V0A0D2 | MTIEKAVAIDQAPAHARRLMAALGLPLDTPGLADTPARLVSALYELTAGMREDPGRHLEVTFPAESAQSGVIAVTDLPFISLCEHHLLPFTGSMTVAYLPSPGAPIVGLSKLARMAQGFAARPQVQERLGEQIVESLSTRLDCMGAACQVVAEHSCMTLRGVRAAGAKMTTLHLKGVFERDTLARRDFMGLCRA | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 194
Sequence Mass (Da): 20720
|
A0A920KZE7 | MWVLTRLNTILSKLSYSLAMLIVAIMVMALSLSAITRYISGTGYDWLIELPPILVCWLVFPLLGPLLKEGNHIQVDFISSVVPSNVILYIKVAMNMTAFLASLVFFKAGYDATMLYYRLGQMMELELDILSGGCTYLFQSGSLFWRCFRLK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 151
Sequence Mass (Da): 17095
Location Topology: Multi-pass membrane protein
|
A0A914CUQ7 | MNLIIYDWVSIPIIYTQCVNLTVRCYFVLNLMGRQYLKHDYEIPNAKTVNIIDLYVPIMTIFQLVFYLGWMKAAEVMLNPFGEDDDDFECNYILDRNLEVGMLIVDSCYENLPDSGDNDSGNFVYTTAEESMNENNLQGSCNKVKPXSWTRAPSLAKALAKFILNGEDLVH | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 171
Sequence Mass (Da): 19612
Location Topology: Multi-pass membrane protein
|
A0A3N1HSP6 | MTVVVCGLGSVGSALLRLVAARVEQVRRQHGVRLVVVGVVDSRGAALDAAGLDVPTVLATKEGGASVGDLPDVGVPGADAAQVLSRLGAAGHPVDVVVEAGPADLRTGGAGLAAVLAARAAGAAVVLANKAPLALAWEQVVEAPGPAVRYSACVGAALPTVDLLRSVAVSASPVRLEVVLNSTCQRVLGDVEAGLSAAEAVAAAQAAGLAEADPYLDVDGTDTAVKLVVLMAALGHRVRLDEVSVTGVREVTADLATRARERGEILVLMGTAVPAPRPREGWTLEVAPVALPRHHPLARMDRHETGLVVHTDVAGTIAAS... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 351
Sequence Mass (Da): 35354
|
A0A1T4SFT7 | MSAAWRVFEYFIAVLFSSLVLVILAQIVFRYFIGSSLSWADEGARYLFVWLVYLSGVLAAREGLNITFEMILEALPRPVWLVLFVASNIVVCAFLALAVWLGIEATAEMRQVSSILRIPMKYVYLAIPIGCFGMFLAQISFCVKRLKDPRHPHLDVT | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 157
Sequence Mass (Da): 17782
Location Topology: Multi-pass membrane protein
|
A0A914CCL3 | MRQYLEKSHKGWDYAKSASFLPQDARIVATPNVIDIYMNDRVQYQPSMVRPGDTVIVSKKKPECNHLWACLIGTIICIFLFVITYNMTRSSKVQQTKVLENGHCAGITGPKSTFLWTINAPHLTSTSYLFGTIHKPNLWNNVSSQAKNAFKNSDALALEIDLRDPGYIKKMNTCFKFPNGTAIELFPSKTDVRQRIKRMAEFFQMNVGEFKNPDGFNNLTNLTNEDPILDEVLSSMAKAEGKPVISVETADEDCERLKIYVVIENALVLFNEKLENILGDYEKNQYPYSRLSKNWRSKRSTNDHMSQEKDEVDHLLIKTY... | Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 443
Sequence Mass (Da): 51363
Location Topology: Single-pass type I membrane protein
|
N1QWI6 | MGHGRGYVHVAPLEQILLRPDTHVGSVEKHTQTLWVYEGGAMVQGCQNLDSIVRFYDFTIQTNLFDFMILIHQEEGVYLPDMIFGRLLTRSNYDENEWKATGRSNGHDAILDNIFSTEFVVETAHGCRKKKYKQVFSENMGKSFSDYVQLYIDSACKEGTELPRIYQRVNDCWEMLDLRLISTAWVGPPGRLPVLRPRRGDHRSQPHPMCFCEGDMDRDMHGDEQSRVDTNRGYKADRVVPEQRWKQRRRTHEKRGGTQVDYVANQIANHVMGVVNKRNKHPNMKLHTVKGYLWVFVNALIDNPAFDSQTNETLTTHQGS... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 573
Sequence Mass (Da): 66015
|
A0A7M3VAE3 | IQYGAVASGEKQTKAANSIANLALIKTVLSRISNKYSFATKIIRVDGDDNYAVLQFNTEVTKQMVQDVSNDVRETYARMNAKVKALVSTVGIEIAKRYIAGGKIFFRAGINLLNNEKRGQSTQWDQAAVLYSNYIVNRLRGFETDKEFILTKIMQMTSVAITGSLRLFPSERVLTTNSTFKVFDSE | Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.48
Subcellular Location: Virion
Sequence Length: 186
Sequence Mass (Da): 20794
|
R7W347 | MVSLQGPAEGPSHLSAGPVGEDMFHWQATIMGPQTALYCWSIFGEHPFPTGLSLQAPEGMNIFQVSFRTKVLLSICSLLTDPNPNDPLVPEISHMYKTDWAKYESTARSWTQKSSESSFVNMTASAADDVMKKWGAPNKIDFLSFLYKACRRCAAMFLFQKSALHKCNMAGKPAAVTRVVDSMTDNLRPTCADATDVANAVLDGSDAILLGAETLCGLYPVETISTIGRICDEAEKVFNQDLYFKRTMKYVGEPMIHLESIASSAARQSLIVRGLFPMLADPHHPAESTSTRNESVLKVSLDHGKASGVIKSHGLP | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 316
Sequence Mass (Da): 34478
|
A0A961PJ04 | MKRLAYWLTRGAEAISATLLAALFLTFLVQIVSRLVMQTPFGWTLELSLILWVWLVFFTAAFTLGERDHIRFDVFTRAAPRRLRRRLALVCAATIAVAMAWAVVPSWDYIDFLAIRKTATVRNPVTGAGIPMRSVFSVFAVFLLALAARYGWRAACLLQADLRGDGADDPLDATIGDDGA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 180
Sequence Mass (Da): 19966
Location Topology: Multi-pass membrane protein
|
A0A2E9G1J1 | MGAFGKMYSKKELQNFQNEIASQVYSEDSVLIGKFFDQNRTQVKYEQIPEHVVNALIATEDARFFEHGGVDTKSILRVAIKSILFSDKSSGGGSTITQQLAKNMFGRENHGLLSLPVNKVKEMLLASKIEEMYSKEEIITMYLNTIPFGENVYGIGSAAKRFFNKTVSELKPEEGAVLVGMLKANTYYNPRLHPENAVKRRNVVLSQMEKYGYLDQEAADTLTKLPLVMDYANLEAEGPANYFMVWVKKEANKILKELNEEADTTWDIEKSGLIVHTTLNYQLQLDALAAFKEHLSEMQKRLDTQYKSARFKSQLDNVAE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A7J5YH89 | MLSMFLESLGMALCLAGSLLVMVACGLPMWKVTAFIDSNIVVAQTIWDGLWMSCVVQSTGQMQCKIHDSMLALSQDLQTARALTVIAAVFGVLALAVTLAGAQCTNCIQDEALKGRIVFTGGVLYIFSGLFVLVPLCWMANNIIVDFHNPQIPPSKKREIGAAIYIGWASSALLLMGGECCAAPSPRGRGEGIQSNTPPPRASPPTGTRSTTFEEL | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 216
Sequence Mass (Da): 22966
Location Topology: Multi-pass membrane protein
|
A0A2D0MXQ2 | MKSSTEIYDFLSSIISAAPYGIIAVDMIGEVLLLNEQALRYLEIGHSPNEVIEKKLVDFLPHLPQLANVVNQCINFGRENFDVSETSPGRRHLTIRGRQILNGMILTIEDVTATKEVERATLNAMLDGQEKERRRWAQEIHDGIGPVLSSIKMNLDEVQEEVYAKSSPRYQDNFETAQELLKSVTRDLRSISHDLMPSALEDFGLVSALDSLCKKFQTGDGPALQFIVTGEIQRLNSSIELALYRAGQELLHNALKYAKATRISLQLIKHRDSIVLMVEDDGIGFNKNQFGADNGIGLKNIATRIQSTGGDFVLETEEAH... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
K1W9U3 | MEGLTASEQREFQNRMERKQVKETMGMFSNLVSHCFDACIDDFTTKSMIQRETGCVSRCVQKFMAGSERIGQRFQEQQVQMMNQPPPGR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
N1QU85 | MSDNYSCHDCSTTVVISGQLSCNLQKTWQLGSRGRWGTEVVRDVRARRQFHRTPQSQTLTSEGKQRAGELPHMPHTRVVLRGTQNQPSRAKIRAKGSATNAPPERPHQRGPNLSTKLRQLYWACRRRAPAQYHDPDEAALRHRLLAAVQQFELGQPPPLKSLLSDVGISDAASCQAEIDYLEEQILSQEEDTDLLLVGGVLALLRYSLFSQFDPGNAKAAQYWPSAGNLQRLPSWGGGGCDDTSFSVPKEFSCPISLDLMRDPVVASTGQTYDRPSIIQWIGEGHSTCPNSGQALADNRLVPNRALRSLISQWCGMYCFQ... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 678
Sequence Mass (Da): 73800
|
A0A2R6GLF5 | MSIDRTESRANVNIAEPPQGFADVVVGGQAGSEGKGAVAGHLARRNQYGGAVRPGSSNAGHTVYDADESPHIQQVIPSPGIVDPEVDLLMAAESSFGLGEIQDEIERLVDLHGEGTRDRIYVDPKAAIIDEGHRELERDRSLGEEIGSTVHGCGAVRSEKIWRSAGSADLAEDRPELQPYVDSRVASRLLEYGRRGESVIVEGTQGTQLSMNQSNHYPFTTSRDCTASSFLSSAGLPPSAVRDVWVVFRTYPIRAGENSGPMDTEEIDFETIAERAGHDEPPTELASVTERNRRVFEWSWQQFREAIELNDPDKIAITFL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: 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.
EC: 6.3.4.4
Subcellular ... |
A0A7G6V4H7 | MFWGVLTDALLDEALACLPPEHLRLWFTRLLADIRSNRSGLPDLVRFWPDERRYELIEVKGPGDRLQDNQTRWLAYCIAHRMPVRVVDVEWAGEGVAHAEAAGLSA | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A1G0GKV9 | MKKFILIVFIGLSLSSCSLLHVHKTDVEQGNIITQEKIKRLHLGMTQEEVIAIMGTSLTENIFVPHRVDYIYTYQPGRSRMVEKRLTLIFKNGRLQDIQQTTFISNA | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 107
Sequence Mass (Da): 12335
Location Topology: Lipid-anchor
|
A0A6J0UW02 | MILRSMQPPSSLSRRPLRRGEGRRRRTALRCSPIVPCVSGFRMLALRGFSHLGRRFISSSVCLRAHGHDLAKTMMYIPRNEDTPLFPVLPFTPPSDIELPLTPEQQALKEKEKGPWSALTAEEKIALYNMKFPHTLAELYAYVPEWKTAWGIALLLLSFSGLFMIWAKMYVLPPYPHTMSDEWKAMQTKKMLDMKVNPIQGMSSKWDYEKNEWKK | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 215
Sequence Mass (Da): 24898
Location Topology: Single-pass membr... |
F4NV23 | MGNTLTLPSTQRSPSTETPNNTAVPGNASNHQPDNTSATIASMLQTNNTYFGPHFVFDNENQQAHPDQPLQANQAFWDEILNVLAGGPGAAETELAGLQNMYNQLPPAELKRTTTLQAQVAIQKNTVRLIRVPNSSSNLHTLEFLYDSIAACQICLFWNARESYVTNDLGQTTIRFIGPSDTPVIPWTFGPFPAGLGQKFTLPIEYALDPFSVLSKGTVSIPNSGPESPVSPLSPIHLSALSATAPLLNDSTPTSSGPLFESNNPIAVSTVENSVVNIDLHNDVSEIPQEGIEQFEASLVMPGALFPLCVHFEADLDRGV... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 498
Sequence Mass (Da): 53652
|
A0A1V0I2L6 | MAALIGVITLQIVSRVAFTAVGWTEEVARFLLIGLTFLGAALAWQRHRHIAVGVLIERLPDRAQKLATALALVIAVAFLISLAWVGQTYMTMQSFQKSAALRLPMSYVYAIVPVSAGLMAWLAATDLMRLLLTGARPDAGEPVE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 144
Sequence Mass (Da): 15576
Location Topology: Multi-pass membrane protein
|
H8MGB8 | MSDDIAFMQQALELAREAASLGEVPVGAVAVLDGNVVGTGYNRRECDRNPFAHAEMLALAAAAKARDAWRLSGVTLYVTLEPCAMCAGALVQSRVTRLVFGTMDPKAGAVGSLYNLVEEPRHNHRLQVTSGILAEDSRQLLKTFFERLRAKRREN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 155
Sequence Mass (Da): 16929
|
A0A2M8D4T0 | MLFLGSGRKLIDIFIDYRPILLPALEENLVKGLAHITGGGFLDNIPRILPEPVSVEIQLKVVPVSPVFDFLVNNGKMDLEEAYRVFNMGIGMVAVIAAENRNAFLGAVTEEPVLLGRVVSGDRTVRLLR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AD... |
A0A961NV50 | MVSAIFIIAVGLGAAFLLGLLKSAQKDLAFLVTIAALAFMSWVALDWTVALTRGTAQPTTILTAGTQPPFAINLYIGTAEAWLLTVINVTGLLSAFYMYDALRRLGRGAMSVLLVMVMALSGLVLTRDVFNLFVFFELIVIATGGLVLLSDDARAVAAGFKYLVVSQIVSILLLVGIIFTYHANGSLNIDDLAAVPLAFQGASLAMFLLLMALVLELKPFPANGWALDIYESAHPGFSAIFSAASGTAALFAADKLAAAAGPAWLPLLTGLGLLSFLGSNLLALAQDNDRRLLGYSSVGQIGLVLAIVGQRDILGDGYFY... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A2N2K565 | MEKKPYTPIIPELTKNAITVLERRYLKRDKEGKVLETPGQMFRRVADAIAAADGKFNEKADTAPFAEAFYRMMTQLEFLPNSPTLMNAGRELGQLSACFVLPVGDSMEEIFDAVKYTALIHKSGGGTGFSFSRLRPANDVVLTTTGISSGPISFMRVFDVAT | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
M8BY77 | MKEKMPLYRLKGLLDNAPPARDFVAALKASYDRTAVPALIAEVKKASPSQGVLRKNFDPVEIAQAYEKNGAACLKFFQGSFDYLEAIRNAGVKKSMIS | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 98
Sequence Mass (Da): 10780
|
A0A554LQA3 | MLQKNKYFFSEKDLHLYDLPQIFAASCVWHESELKNAVATFDLYVRDMPPHRNFLLFGGLDEIIQGIINWKYEKQEIQYLLEAGLITKSFSKYLESFKFNGDIKAMHEGSIFFNNEPVLRITAPIVQANLFTMFFMNAFTGNTKFMSKLIRSIIIVGPQRCAGVAGLRSDSFEYAMKNARGSYLLGAVGGNSVASFAKKFNLPLVQPQTNVFHAVIKSFPSEIEAMRKMGELYKGRVSLTVDTYDFFRGIKNAIVVIKELKQKGFETPSIFIDSGDLVERCKVARKILDEESLDKVKITVATNLDEYKIKKMVNQNIEAD... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 462
Sequence Mass (Da): 52894
|
A0A0K2WPI7 | FSVTHICRDVNYGWLIRYIHANGASMFFICLFIHIGRGIYYGSFMLTETWNIGIILLLTTMATAFVGYVLPWGQMSFWGATVITNLLSAIPYVGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPSGLNSNSD | Function: 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 membra... |
F2JGX5 | MVCNVLGKRRLYFDGAMGTAVQSRGLKLGEVPELFNITHPEIIEEIHRAYLEAGSNFVTTNTFGANRYKIEEKGYTVEQIISKAVEIAKAAKEDFPDSYIALDIGPSGKVLRPVGDVEFEEVYEIFKEQVIAGEKAGCDVILCETFTDLYELKAAVLAAKENTSLPVFCTMSFEENGRTFFGTSIESMILTLEGLGVSALGVNCSLGPKQLKEIVKRITKLSHIPVMVQPNAGLPVMQGENVHYDITAEEFAEIMKEFAEDGVSILGGCCGTTPEYIEKTVDKTKDIPYELLEREKVTGICSSSEVVYFDDVVVIGERLN... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
A0A1J4XKL6 | MKRLQKIAILVNQNKPRAEEFAAKVASLAEMEGCETKISLDYPVKDDFLAGQDACLSVGGDGTLLSTLKESVKHQVPIVGINLGKLGFLATYSEEDILNNLKDVIAGNYQVLYRGLFDCVSADNKSHVALNDVVIRQNYQSRLIRLEVYLDEQLVNNYYCDGLIFATATGSTAYNLSAGGPIIYPCDKVFALTPICPHTLTNRTVIFSDDNRLTVHCADEHSQLAVYFDGQKSLEGLDCFPLHISIAKQRLPLLLPQNYSYFQILRKKLKW | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A6G1QGJ5 | MKTAKMKTKNKRLSSGVQKSAKRGIVVKGKWKAVELDPSVYSEEGMEGLVCFEELTNYRLIDSEKTAAKAAKEMKKEKKKTMKRKVSEGEEEDEKAAVEGKEGEKVNEPAKKKAKKKRKRQIVMESVQDISTQITQKNQAANEEGVETGKEEASKDSAICSNVKSNIAKNRNKKKKRKQQMALSSLGFASPTPIQALALPPAIRDRMDILGAAETGSGKTLAFGIPIIHTILEWKNHSEKHEYSESSVKVESLYLPPTKSAEATTEDQEDCVNVEEDQHEGMRVQDQCDSDESATEDEEHGFEEDEKLGCVQVIDDAEFD... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 815
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 92604
|
C6XAP9 | MRIPFAPITLGKQLDRKNVLLEFAIVPCSFILTYLLAGYFELSEIFIDWTLTSQDEYDIDELPYALAASTLAMSWFAWRRWQEIKREVRSRNQTEQALLAERLQFQTLFNENLAGNAVVTTQGVIQMCNPAMACFLEIQTPELAVGNNLADCLQHGPSWSHLMEVVKEHQKVDVEQLCVIGVYGKRTYAMARILGHFSQDGSLQFLHVFAADITEIKTAESEISNLLRENHFLLRQALELQEEERRHIARDLHDDMGQYLNAIKANATSLVNMPDLPPSISEVALHIISHSDHIYRSARQLIHRLRPAALDELGLGAALQ... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.