ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A0N4VAG3 | MNESFLSAFIPNLSFQLVARLFSFVLNIYLIRIVDLSLLGVVNVSLFLYYGTIIFLVREPFRRTFLSNTVPFSSILGHCWLCPLLYVVVAVLLYPLWIYTSWPSVVGSPTKALFLFGFSAWLESFADPFVIIASLFYLVVAYYFARHCLYEGRYVLAGGIFPQFHLSVSKRELKTFSSFVWHSFAKHFSTEGANFVLTFAANMSHENQAVYDAIDKLGSLVVRIVLTPLDQAAEMYFARYLKRGENVNKQNEINVRRGTTCLMGLVHLALLVGLTVCTFAVPYSSLGVWIYGGERFAEKSAANILRFYCVYVLIIAVNGVIECFATSTMDNIQTVKHGTFLSIASFAQFVVSAFACRHLGAYGIILGNSLNVLIRIFYNWRRIQEYLNGKVSFTEVLPSFTIFFLLLFALATSSLSFLIFGREKGIIHNSAHLAVGGALFMFVVNYVYHNDEALAVLLREYSHVQKD | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 467
Sequence Mass (Da): 52742
Location Topology: Multi-pass membrane protein
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A0A0R3R662 | MLGLKRRPHKRRNANIHLRRLTQAYLTTVNQFQPLVVRTAYEKVDSVYYLVQKLILNQQSVTSGLFPRYSEKCEIGFVKDSIYCALACWTCSIAYKRLDDDRGRQTELRQSAVKAMRGIMFCWMQELDNLNHFKENISPEFSLHARFDLHTGMVLSTPNEKKYGHLQMDLIALYLLALVQMTAAGIQVIYTHDEVCFVQNLVFYIERTYRTPDFGMWETGSRYNVGERELHASSLGMVKAALEAINGFNLYGTAGTSSSVIYVDIDGHNRNRTTFETILPRESNSKVSVR | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 290
Sequence Mass (Da): 33372
Location Topology: Lipid-anchor
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A0A947M974 | MTLPAPLLLITDRTQNPRPVVDTVAAALEGGCRWVMLREKDLPPEALLAMAWELAALAKRHHAVLSVNSDLEAAKAVGAGLHLPAGRDIAAARNALGSTSLIGASAHSLAEAQAAEAAGADYVTLSPLFATASKPGYGPALGLDGLRHAVAALRLPVVALAGIDASNAADCLAAGAAGIAVMGGVMRADDPEAEIAGLIAALQTA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: 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).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 205
Sequence Mass (Da): 20528
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A0A813GJ26 | MRCAAHPQLGPTGNLATLRLSATSADALAALHCRRRHWDGCEISSKSTRSGWGRSWRKLNGRQARRFYALVVLAGTGVAKRIAARPSSSQTRLVIAEKPMVMRMIAEAVGGLKQRPDKTGKLQYFEGDGLLLAAASGHLVNLQQVDWNSPLPIFPSPFKLEVSPASHLPKLNLIRELASRADILVNGCDAGREGELIFRRIIEFLGLESKPSERLWLQSLTPDAIRNAMQSCRPGSEFEPLAAAARLRQESDWLVGINATVALRRRSHIPNTTSTGRVQTPTLSMVTDREKHILKFKPEPYLLVHAAFSAAPGQKYEGTHSTLEQSGSLAPVNWEQLADTWEIGVVGKIVKDAHVDTTENPKPLHDLAELQRECSQRFKLTPQQTQGEAQKLYESGLVTYPRTDSRHLPKDYVKQVKDMLLASSATVGAASALPASLLQKAADGVSQVGTRVFNDSKVSDHFAIHPTEKGLATFLSSKESSVSQKVLGCIARRFVAAFLPASRFRTVRRTTSVDGHLFTTTMKDLVEPGYLEVEGKKAPSQTRALKALPAGTKVSLCKKLRIERLETQPPTRFTQATLLTAMEHCGRIVKDAELKRGLDTGLGTAATRGQIIEKLLTSKLLVPVDGKTASGFLKPTAQAIQLVDLLRGELDLQELALPELTGRWELDLRGIEHSKKKHQSLHSAFETSIRAFVLKIVERAQTCSPFGSALCRVGKHKGKTFEETLANDPVYCRWILSLGLEEAGPFAGFQVFLLENRKDLGAVEVPQAGPPFKSGKSRGKTLDIKVVADDPDYGDSVPQSGPEASGSVVPHVTKRQTKKGALAPQKPQGGNAKLKCGKHIGKTFKKVLADDPQYCDWVLGLKSQAGVEEGTRFSGFQTFLSERKADPQGLDAQPTGQVRSKIKKCPALAADAPKKSGLSKNGPGRPKNGSKDASKLALSAKNIPSLSKATLKEELFSRGLAVSGGITELQNRLFTALSLAARKPHEMRSTSRTQSRFCGEKPPRSLRSRSGSRS | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 1014
Sequence Mass (Da): 110491
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A0A6A1VKA5 | MEHAMSENSCQLCAVEKLTFEPPPIYCTPCGARIKRNAMYYTMGAGDTRHYFCIPCYNEARGDTIVVDGTSIPKARLEKKKNDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGEAEYTCPNCYIQEVERGERKPLPQSAVLGAKDLPRTILSDQIEQRLFKRLKQERQERARLQGKSFDEVSGAESLVVRVVSSVDKKLEVKQRFLEIFQEENYPTEFPYKSKVVLLFQKIEGVEVCLFGMYVQEFGAECQFPNQRRVYLSYLDSVKYFRPEIKAVTGEALRTFVYHEILIGYLEYCKKRGFTSCYIWACPPLKGEDYILYCHPEIQKTPKSDKLREWYLAMLRKAAKENIVVDLTNLYDHFFVSNGECKAKVTAARLPYFDGDYWPGAAEDLIYQMRQEEDGKKQNKKGPTKKTITKRALKASGQSDLSGNASKDLLLMHKLGETICPMKEDFIMVHLQHACTHCCILMVSGNRWVCNQCKSFQLCEKCYEAEKKREERERHPINQREKHPLYPVEITDVPADTKDKDEILESEFFDTRQAFLSLCQGNHYQYDTLRRAKHSSMMVLYHLHNPTAPAFVTTCNICRLDIETGQGWRCEVCPDYDVCNACYQKDGGIEHPHRLTNHPSIAERDAQNKEARQIRVLQLRKMLDLLVHASQCRSPLCQYPNCRKLHARACKESECHVPRCRDLKEHLRRLQQQSDSRRRAAVMEMMRQRAAEVASNAG | Function: Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation.
EC: 2.3.1.48
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Length: 728
Sequence Mass (Da): 84447
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A0A813JJY5 | MYFCGMLYSFLGVSIVADMFMAGIERITGVKKCKRVPGTSRFVTSPIWNETVANLTLMALGSSAPEILLSLNDVIKNNFQAGKLGAATIVGSAAFNLFCIIAVCINSIPEGEIRYIKETGVYALTAFYSIFAYVLLLFICSLNTPDVIDVSEGVFVFLCFPALVTTSYYADIGILTVANVKALFISKKSSESTEKAPTTYLDKFRAQHAAELEEEEDEGTKAAKAKLEAAKAAKKVVRAQQGGCCSRLMGRKGKAEEAEGEVGELLGVREEELLADPDCPILDEDDNPIENDAGILTFDRYSMTVDAGLEECEYTVQVIRKNGAEGKVTCQYKMEQISAIPGFDYEEEEGTIQFRDGVRSAEITIKILPKKKGEQSDRFQLVLFEPEGGAEINPDYDGGEECNRLTIMIYNTLGRGNSKIVSIIDSFVNLDEIRQGTQAWKEQILEAIYVGGSKEDQDNAGVLEWVVHLVWLPWTSLFAIITPPPVFLGGWVCFIISLGHIAWLTIIIGDIAELFGCVAGVDDAITAITFVALGTSVPDLFASRAAAKQDEYADASVVNVTGSNSVNVFLGIGLPWMMAAVYWKIVGGNHFRVNSEGLGFSVIAFTVYAIVALLLIQARRVKFGGELGGPSHAKIYSSFFLVLLWLSYISLSTWKYSNPDASISSQVIAVCASFPLIGLLVLGFAGFRMALSVSKKYIGEEGFWGIFVALLVLGLRLLIFFTFQFQ | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 726
Sequence Mass (Da): 79254
Location Topology: Multi-pass membrane protein
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A0A7S4E7I9 | MAANCASCAAATEFDAGTNYDVVIAGAGPCGLALLSALHAQEGNLTDEQQATMQARSRQNRIKKSEREALKVCVVDPAGAFLHEWRGRFDALDIALLRSPAWAHPDFFSEAALQEYAWRRGREAEIHSIDDFTTTSLRRLTEVNAGLFRLPGAGLFSDFCCDLSKTLPHAMLRGEASAVEKRSEGGYAVAVGDASVRTRAVVFALGAATTPCVPPQFALAPTIVHSNDWRALRDLDFGSKDTVLVVGGGLSAAQAALRAAKRGAGRVVLCSRRKLCTRTYDLELDWMNRRSTGKGSARRRLYEFKGAPLEERRAFVAKARGGATVPQYYLDLLKTAEDRGAIAHFVDEVCDVQEVDGAHRVAFNKSEPLVATKIILATGSQLDCGTIPLLRDTAKRLALPVVSCLPAVDDSLRWGDEDLFVVGALAQLRVGPDAGNPTGARRAAEICAANLGSHDDLVEDYNVLANTYDVFGDSSDTESETESSSTD | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 487
Sequence Mass (Da): 52408
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A0A183W8I9 | MKXXXXXXXXXXXXXXXXREYRSGLWPSVRRRMCKWGYLFLVSKRLGTRLFGTYLFIKFLYLLNAXXXXXXXXXXXXXXXXXXXXXXXXXXIFMMQSFLGLKTDNYTLFGIAISKNILAGLDWEVTMIFPRVGFCLVPLKHIGSNNYATAQCVLPVNMLNERIYMFLWFWIVLAATITAISIPTWFTRMSYEKSRTHFIKKYLKLGEQVTKKDKYMIDKFTQCFLRNDGVFLLRMIAINAGELICSEIICQLWHTFCEKYFYRDLTRKRNRRLIPHLHLKRGIIGFKDKGDCKERKYPPPLPLPIESSATAPPSHLVLSSDAPIDTPDTDEDGYSRDDEDDDDNLKRHLKKKYTGEYKESV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 361
Sequence Mass (Da): 42133
Location Topology: Multi-pass membrane protein
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A0A0R3QSV3 | MVPNPGDSSTESTCQSKRGGRLDERMDEDDWEEEKMNEAKHLKLISDELRAKGCPLFGGKYCDRLPKDIREKAGALEARLDSLISGSVASPFKSDTRDELRLLIAQGLTTAAFKDKMKKYDFSLKCNAVWSADAIAYRCNTCAFSPCIICLLLKTDYWLCMSLCSSCFKNSNHDGHDFNRFFSQAGGACDCGDVDVLNESGFCFRHGPNARRPPVPSPDIVSLGEFIIPKLFVRLFLCFRGWTRQYNACKDGSSRESFSNHLVNRAHILIELIQELVDCGGPIRDVIIGNLLDRQLYHDLNKRSSDDDMRDHDRSPDFSLDWRTRDLFLEDLQSLKPIVDSDQTNACYDPECLLDELIFWMVRLIFPQIIINLCLSLLSDVQYRDVFAKRFFSLYLCIADILVDFSKSEGDSAIYAIGSRIIHISVQILSSEAQCLKLDDEINLKDKIILSAYGVLKTGVQKSTVTQALEYFYENAPPPTNDDKLFKWFVYSVGDANNPLRKASYWTLVNDLQNLLTHGEIARRFFRDKKSMGNYVALIAPMQGMNLNYRVIAGNHLEYDAAHPYQLAFHLEWEVSAVNMFNTLAALTVETECMNTYLLHWKTILEEWFNAIGLTKNDVCIQPYCVSYHIPLHRHLSAGILRCIELPAFISCLNILIEDEDFLRKAVFHPLRIHVCRAEASAGMWARNGNAVRNQAFYYALTNYNIAFLDCDITLIKFIACFVDTEWFIEIVSTAFYVDDCLVLCGFLLDDIVLLPQKRRIVTRKEWVDFLIDGILRFLLDIMVIKWNMDGNVSNSLENEIVAALAVSDLTHSKLKAAIPERGSRPFVDDKVFDSTLEKVCIFGRIWDLL | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
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: 850
Sequence Mass (Da): 96935
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A0A0N4V125 | MTAYFGGGDALSCWTPQQFRRGWDQYVNDFCLVENTYFLPLENASLPEKIETRENGKLPYYQWVPFVLALQAIMFCIPHMFWRALNWMSGIVCCFAFSIRNSVIWGLQMLRRLFRGSEWTQTSVFPRVTVCDFEIRELGNLHRWSVQCVLPLNMFNEKLFILLWCWINFVLIVTIINTINWMIKVLCIRSGIKFYVNVLEAAQVRSQLLITTTDTRSVR | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 219
Sequence Mass (Da): 25819
Location Topology: Multi-pass membrane protein
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G1FKC2 | MPQLETSAWFHVAGLTIINIFCLFQLQLIGIEMIYIYPPEEILKLPEIPFPWEKKWTKIYLPLSSALLL | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular Location: Membrane
Sequence Length: 69
Sequence Mass (Da): 8104
Location Topology: Single-pass membrane protein
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A0A0P0V9U5 | MAGNPAAAAPSSSGSSSVFLPPPSPSDGELLRPLHRLARDLSAVDTPAPFLRAAFASISRRSKLLAAAFDDLLLCGAAGELPRSASLCLREVLLVLQRFKAIVADCSARSRMRLLLESDEMEAELRELNHDLATLLDLLPVVELGLADDVLDVLALASRQCRRCSPAPESEEALKASVLSLIQEIEREIVPERERLEEILVEVGINDPASCSEEIESLEQEIGDRASEKWTASMIALVGLLRYAKCVLFSATPRPSDSNSKADVEAEDGEPPVPPSDFRCPISLDLMRDPVVVASGQTYDRESIDRWFSSGKSTCPKTGQVLANLELVSNKALKNLISKWCRENGVAMEACEASKSEQAQAVAANKAALEAARMTASFLVKKLSVSFSPDAANRVVHEIRLLSKSGSENRAFVGEAGAVPLLVPLLYSEDAGLQLNAVTALLNLSILEANKKRIMHADGAVEAVAHIMSSGATWRAKENAAAAVLSLASVHSYRRRLGRNQSVVEKLVHLVRTGPTSTKKDALAALLTLAGERENVGKLVDAGVAEVALSAISKEETAAAVLAALAKRGGAEAIVNIDGAVARLVAEMRRGTDWARENATAALVLLCRRLGAPAVTQVMAVPGVEWAIWELMSIGTERARRKAASLGRICRRWAAASAADGERGGGCPVATVVPPAMMAS | 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: 680
Sequence Mass (Da): 72322
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A0A1V6EBF3 | MEIREAINSEFAKKMGTEDLRKAFLVEKVFIVGDMTAIYSHVDRMIIGGIVPTSVPIALPVSKELGTEFFLERREMGIINIGGEGSIEVDGNTYDVGQRDALYISMGSKYVIFSSKNPKEPAKFYFNSAPAHRACKTRLITFDQANHVALGSDAECNKRVINQYIHPTVLETCQLVMGMTTFSEGSVWNTMPAHTHERRMEAYLYFDMPDDRVVFHLMGKPQETRHIVVRNEQAIISPSWSIHSGVGTGKYTFIWGMAGENQTFDDMDNVNMTDLR | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 4/5.
Function: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
EC: 5.3.1.17
Catalytic Activity: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate
Sequence Length: 276
Sequence Mass (Da): 31133
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I1EEE5 | MKRKERTKVKYSKLVSISNDREDEYHDDQFTENSPVKIPVRSIVLATFLFLVGSVLLILAGLLIGGVFGDTPDASSAPLLLIGSITFIPGFYHVRLAYYAWKGYHGYSFSDIPSYDD | Function: Involved in trafficking and recycling of synaptic vesicles.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 117
Sequence Mass (Da): 13124
Location Topology: Multi-pass membrane protein
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A0A6A3Z6D7 | MSVIQAELQPAYGFVPLLVVLLVFVNLWAGMKVGKARKLYGVEYPQMYAEQSDKNAKAFNCVQRGHQNIMENVPLFLALLFTSAVYRPQIAAIAGLVRILGFIAYMRGYSSGDPKKRLQGGFGYLGLLVSLGLSVEASLRILGLLCYIRSAHAPEPRGAVVSATPRSFAEKRTPPPANGVRPRAQLPHPLGTHSPSALGPPQQTPVNLKLMGEVTTASLAVALSAAAAAAFIVQRQQKKSKKSGVSKALPFPMTRTPLERVPLDQLPKLKNDLLLRALHGDRTERVPVWCMRQAGRHLPEFRELRDMGYDFFTMCGVPELAVEVSLQPLRRYHMDAVIIFSDILVIPQAMGMEVTMVPKVGPVLPDPIRTPEDIDKLDLNPNIEETLGYMLDALNLARQKINGEVPLIGFVGAPLTLMCYMIEGSGSRTKALLKTFLYQHPEAAHKLLQGITDVCVNFLLAQQRAGAQALQVFESVGAEVLTQDHFYEFVFPYLVQIADRVKAEIPDTPMVCFCKGTQYAYEKLVATKYDCIGLDWQSDPVEVRQLARGRVSLQGNMDSSVIYASTETIYDEVKKMLKRFGTQKYVANLGHGCFPDMEPAHVDAFIKAVQQISLEMNSR | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
EC: 4.1.1.37
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Length: 619
Sequence Mass (Da): 68456
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Q3SZX1 | MFPLVRNALSSLRIRRIQQIRQSHSKHSPDFHDKYGDILLASGTSFCLVTWVFLVTQIGIQWGCSPVGRVTPQEWNEE | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 78
Sequence Mass (Da): 8983
Location Topology: Single-pass membrane protein
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A0A0R2G0G5 | MDDLSIALFAFLGGVSRYGLGLWLPTWHAFPVATLSVNLLGSFLLVFIGQYVAHQGWLSARLIAGISSGFLGAFTTFSSFSVDTMKLFQQHLFGTAGLYIGLSCIGGFFCAELAYQLAHRLLKREHA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 127
Sequence Mass (Da): 13838
Location Topology: Multi-pass membrane protein
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A0A922CNP8 | MISSGSFLISIFTVLITAVYYYFKNVNSYWKKSGVVGPEPILFFGNAKLSALRQTHIAILYKQMYEEFTHEKMVGFYRLTTPSLLIRDLDIAKHILIKDFEVFPDRGFEFSKEGLGDSLFHCDFNTWRALKGHLTPLYTTGRLKIIVSLLNERSEKFIDYVESVCLKNPEQEVMSLFLKYTTASIMASAFGVNVDTHQDNSNLFEKIDNAIFTLNYTNEMDLLFPGILKKTNLSIFNEIVQRFCYEVVETVKLQKKDSSAVNDAMDILLALQQQGEAKSMRRQDNEKEASLKLTDHVLAGQAFVFFAAGYGNNTIVLSNAMYHLAKDSEIQDKLITEIDEVLEKHHGDVTYESIKEMVYLEQIFNETLRMHPTTNAIQRSAKRDYVVPGTDIKIEKGTPIVISPLAIHHDEKLYPNPEKFVPERFMVEAVKSRHTCAYLPFGAGPRSCLGMRFAKLQFKACVVKLLSKFRVEPSRRTKDEYFINPRRSLLCPEGGIYLNFVPRTI | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 505
Sequence Mass (Da): 57862
Location Topology: Peripheral membrane protein
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A0A452CA91 | MESGSGPGSPSTVSLVPGDAVPSPEDKMASVLPVLLVCVVGVVGNATVVLVVLNTRDMHTPTNRYLVSLALADFTVLVAAGLPNVSKSLAGQWVCGHAGCLGVTYLQYLGIRASSCSILAFTVEREVHPDPCCRPGLPGHDAW | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 143
Sequence Mass (Da): 14781
Location Topology: Multi-pass membrane protein
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A0A8D8U0T4 | MNYSIRWKCLVSCFSRKLSTVHKPQSENIVEYLNKSEWRSVVGLEVHVQIASLSKLFSGAKFDFTSPVNGCVSLFDSAIPGTLPVLNQKCVEAAVLTALALNCKINHVSRFHRKHYFYSDLPAGYQITQYDQPIAKLGQIKFNVFTPGIHKTAYEKVCNLTQVQLEQDSGKTIHDDFENRSLVDLNRAGVALMELVFDPDLSNGEEAAALVKELILILQCIGTSSCKMEEGSLRVDANVSVTPRSSPLLGTRSEVKNIGSIRGVANAVNYEIVRQVETLQRGEVVVNETRAYDAASRSTVAMRDKENIQDYRFMPDPNLLPLKVSETLIQKLKASLPPLPNQLRSLLQDKYKLNTDITNVLSRDTHLLHLFYNIVNTKQSRSPKMVAFMLVLHVMAFVNKHKIDLDDTDFNSDHLGDILDAWQGEQITKEIIIVLLEKRMIEQDTRTVQDIIEQDELKQIGDVETVTRIVQEYIRDNEDTARTYTKKSEKKRVKLFGSMMRSLAEQNGNRLNMMMTKQVLETELKKKDEENG | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
EC: 6.3.5.-
Subcellular Location: Mitochondrion
Sequence Length: 532
Sequence Mass (Da): 60341
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A0A6P0RYV6 | MVTKVEKTEAEWKEQLTPEQFKVTRKKGTERAFTGEYWDNKEKGIYKCVCCGTELFHSDTKYDSGTGWPSFWEPIKEENVTEEADNSLFMRRTEVLCSSCGAHLGHVFNDGPQPTGLRYCMNSAALKFEKS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 131
Sequence Mass (Da): 15018
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A0A8J4Z1R9 | MIMMGPEYDVELHPGVSLSKDSTPKAPRARVIVKLLAAGQWIPREAGIAELLKSGSISSTELCELCIQRAEKTKFLNSYVLLTAEKCRQQSQLSDERIQKGTILSALDGIPISIKDNFNLENVTTTCGSKMLANYVSPYTATVVQKLIDNGGTIMGKTNMDEFAMGSDGTDSAFGNVKNIWKLNVESKFSNPSSIHSTNELNASKLEDYYIPGGSSSGSAVSVASGSCFASIGSDTGGSVRVPAAHCGLVGLKPTYGTVSRYGLISLVNSLDVPGIFSRSVDDAATMLGIISGYDENDSTTIPDFNRSIQLPDDIKVSTLTVGIPQEYYLDIMSDELRDIWARVADLLEQGGANVIPVSLPHSKYSLLCYTALNCCEIASNMARYDGLEFGLRADVEESTNELMAATRHAGFNQIVRQRILTGNYLLVKKNYEDYFNQALKVRRLIKNDFDEIFKEKKVDLLLTPMTVSEPCKFSEISGKNRLISDFYAAPVNMAGVCAVSIPVTLSRNNLPIGLQLIADNFQEEKLLSAAKYIENIVKFKALDLCL | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
EC: 6.3.5.7
Subcellular Location: Mitochondrion
Sequence Length: 547
Sequence Mass (Da): 59661
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A0A218VW47 | MASSRKPFRSSLLFFLLIIVLACPYGLCARNMPGNKLDVKPETGNMARQRFDFSKFTHAGLGSQISGMSELKRYLHRFGYLAPQPTGSNFNDDFDAGLKSAIVKYQKRLGLQATGRVDPDTVASFMSPRCGVRDMHHHEASSPKTRLFHVTKHYKITDGRPIWDLSKPMTLKYAFYPDAMIDSLSREEIRAAFAQAFAKWAEVIPVKFEETSDHLFAQVRIGFYKGDHGDEDPFDGPWRMLVHAFPYPSGELHLDAEENWAVNFKTNRAPLKAFDLESVAIHEIGHVLGLGHSSLKESIMYPITPAATKKVDLSIDDVEGIQSLYGPNPDFKLSSLAHAPRLTLRLVVYRAGSGCLHFS | Cofactor: Can bind about 5 Ca(2+) ions per subunit.
Subcellular Location: Cell membrane
Sequence Length: 359
Sequence Mass (Da): 40249
Location Topology: Lipid-anchor
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A0A094XFP3 | MNSFSFLPKKIINHSQGFTLIEVIVSLTLLLIFGLSFAYVLGNGMKANELNSEKIEATFLAQSELEKIRAARDLALGSIDNKFDYEIYESSTSNEDFVVSLQINPQNEHLIEVSVTVTAKNSSSPLYTTPITLMTNLFIGGEVTSE | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 16128
Location Topology: Single-pass membrane protein
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F2E5D9 | MGTLVWLRPTAAPAVPAGPSVAHVVAAAGMKGRTRWVSVASRCPSPRVLQAGRCRWLVVRSGVTAAAADDPEDSSRLPELQVASRIRGFFFYTVTAVAAIFLFIAMVVVHPLVLLFDRHRRRAQHYIAKIWATLTISMFYKLEVEGTENLPPNSSPAVYVANHQSFLDIYTLLTLGRCYKFISKTSIFMLPIIGWAMYLLGVIPLRRMDSRSQLDCLKRCVDLVKRGASVFFFPEGTRSKDGKLGIFKRGAFSVAAKTGVPVIPITLLGTGKLMPPGMESNLNSGSVKVIIHHPIEGNDAEKLCTDARNVIADTLLQHGYGVH | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 323
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 35415
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A0A3R7GZX0 | MLMRGRSAELLVAAAMTTHLLLCPYSKVEESFNMQATHDLLLLSPSDVSGFDHLEFPGVVPRTFIGSLTVATITQPLVYALNALQLKKFVIQYISRWVLGMLTLSALVFFSDGVEKRFGRDTSRFLLLICACQFHMMFYMSRTLPNVYALALVLFALGFWLRGKLQRCVYLFTFATVVFRGDTVVLFAPLVLNMLLSRRVSFFRMVWWGLSAGVLSLLMTVLVDSYFWQRWLWPEGEVLWFNTVQNKSSEWGIGMHERELARAVHIDVPAAMTGVSRFGEEFLAWSYSKDESVTSPEQLARFDYLLTAKDPTLLEDNFQYIAGFDAFTGVGLVNKRIALKTKKLVFLMRSRNFTSTEV | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 358
Sequence Mass (Da): 40843
Location Topology: Multi-pass membrane protein
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A0A7E5W4U0 | MSTEETLLNLDFDKPNTIISPPDDGVVSLSSSSEEICLVPEVGFEGNVDSPGVNRESQPLLGGRGDFEVSYNHFPDDPQFSELVWQAEVAIDNGIFPERIYQGSSGSYFVKNPGNKIIGVFKPKDEEPYGRLNPKWTKWMHKLCCPCCFGRSCLIPNQGYLSEAGASLVDSKIGLKIVPKTRVVKLVSETFNYLRIDRERSRLKRAITEQFPNLRFNRMGLPPKAGSFQLFVEGYKDADYWLRRFEQDPPPPHVMKKFQLQFERLVVLDYIIRNTDRGNDNWLIKYDAPAQQPPHADIDLRDPSEWRGAEVRIAAIDNGLAFPFKHPDSWRAYPYHWAWLPHAKLPFSQDTKELVLPLLSDMNFVQELCDELHILFKQDKGFDKGLFERQMSVMRGQVLNLTQALKDNKSPVQLVQMPAVIVERSKSGSTSSRFFDSFQQRFQHKSPFFSWW | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
EC: 2.7.1.67
Subcellular Location: Membrane
Sequence Length: 452
Sequence Mass (Da): 51972
Location Topology: Peripheral membrane protein
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A0A0C7K6X7 | MLSHPAEKYRPYPPIALPDRRWPDRQISHAPRWLSTDLRDGNQALAEPMDSARKLQFWDLLLECGFKEIEVAFPSASQTDFNFVRQLIDEQRIPEDVTIQVLTQARDPLILRTFEALRGARRATVHLYNAIAPLFRELVFGMDKAEVIALATRATRLIRQQCEQQPETRWQYEYSPETFCFTEPEFALEICEAVADVWQPCAERPMIVNLPATVEVNTPNVYADQIEYFCRHFSRRGEVCISVHPHNDRGTGVASAELAVMAGADRVEGCLFGNGERTGNVCLVTLAMNLYSQGIDPELRFEQMNRVVEVVENCNQIPVHPRHPWAGSLAYTAFSGSHQDAIKKGFDARQPGDPWQMPYLPIDPQDIGCSYEAVIRVNSQSGKSGSAWLIEQNHGLKLPRGLQQDFSQHVQQATDSDGKEMTHHALWQLFRTRYGLQAQPALTLLDYQSASQQDGQLSLQATLRHHGETRRLQGQGNGLLSAAASGLSALFRQPFMIKDYHEHTLGARSDSRSVAYIRCVFPQGESYWGVGIDNDVARASLQALCNALSAADQAGGRK | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
EC: 2.3.3.13
Subcellular Location: Cytoplasm
Sequence Length: 558
Sequence Mass (Da): 62688
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A0A7E5X5Y6 | MNDYCQNVFDNLLIQKDSSNYRYSREMYSKSTISEYIYKRIESHLTSENLLIFFLGCVVIYIIVYIFNVISQAYFSPNIYVKELTEVGFEHIAKGEDRKLRIARAQAARRMGNKIPPPYPNGWFAIGESEDLKTCKVLAVDALGQNLCLYRGRNGKAYCVDAYCPHLGANLAVGGTVTENCIECPFHKWSFDETGTCVRVPGVENAPKGVSLKHWLTVEVDGAIWIWHDAEGRDPLWEVPELPELEVWDSRGRNEFTVSAHIQEIPENGADVAHLNSVHSLSVLELFGHHVWSANWEPGEDHTASMDLTHDYILFGRKVGHIDVKITQIGPGHVRLLLKSPVGPILVSQSVTPLGPLQQKVVHRMFSPTKNAIFAMLLVNYEAKQFARDVAIWNNKRFVSAPAYVKTDKAIRAFRNWFSQFYSEKSISFKDAHQNNLDW | Pathway: Hormone biosynthesis.
EC: 1.14.19.21
Catalytic Activity: cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+)
Sequence Length: 439
Sequence Mass (Da): 49923
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A0A2A7SLQ4 | MKNTRVQKMVAVAMFAAIGLVLQYFAFPIMPAFGFLKIDFSDIPVLISMFLFGPLAGVVTAFLRSILHLVTTGFSPDNLVGDAASFLATSIFTLPIFYFFRKKKNEGRNKFAGVISGTLAMTLFMSVANYFVITPLYLMFLGLNANQMLGMPLTNYVLIGIVPFNLIKGFIVSAAFLVLHAKLLPWLSRKQHKLEQRHTVIK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 202
Sequence Mass (Da): 22506
Location Topology: Multi-pass membrane protein
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A0A483GRU3 | MEHLVNDLLHCRLQAWTFPAGIEARWLGEGILQLLPTAPWRQATILSAGVHGNETAPIELLLQLTHDLSQGRQPLTQALLIVFGNLPAIRAARRYLHNDLNRLFGGRHLAVTPGNESRRAFALEQAVQAFYRAADAAGPVNRGHLDMHTAIRGSLYRQFALLPAHAGDFSPDFYQLLQASGMDAVVRHTEAGGTFTHFTCEKFAAQSATLELGKVMPFGANDLSLFAAADAAIRAWIADAPLPPRDKAPVDYFLVEESIIKREGEFTLNLAADVENFTALPAGYEIARQAEKRWVVQARAPYILFPNAGVATGQRAGLLLRAADLRLPQPA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
EC: 3.5.1.96
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Length: 331
Sequence Mass (Da): 36221
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A0A1X6ZRF8 | MRIVILAAHMHAPTHAAPRGHAFSSATPALTLGALGVVVGDIGTSPIYALREGLAAAGGETGAPAPVTVIGTVSLLLWLLIGIATLKYVVLMLRADNNGEGGTLSLLALATRAVGRRSWGLMALGILGAALFFGDAMITPAISVLSAVEGVTLLAPGFEPWVIPAVIAILCALFWAQRGGTGGVSRLFGPVMLAWFLTLGSLGLVAVVRHPAILAALSPLPGLELLWHGGGAVVPILGAAFLAVTGAEALYADMGHFGRRPIRLAWTCIALPCLMLSYAGQGALVLSDPSAARDPFFLLAPGWALPGLIGLATLATVIASQAVITGAFSFAYQAMQLGLLPRMAVHHTSTTQRGQIYLPRINVMLLFCVVVLVLSFGSSSGLAAAYGIAVTGEMLITTLLAYVVMRRVWNWSRGLALPLTALILAVESALFGVNMTKVTNGGYVPLAVAAALCVVMATWLRGSVIVQDRSRARGVTMEALVKSLSHSSRLRRVPGTAVFLTAEPVMAPPALLHNIKHNGVLHERSYVVTVTISDQPHLDPEASLVVETLGDGIERVHVTFGYMDPPNIARALRRRLRFDIHATSFFLNRRTVLLSDRPGLARWRKKLFIGLTRTSAAAHDHYHLPSDRVIELGQQISL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 638
Sequence Mass (Da): 67492
Location Topology: Multi-pass membrane protein
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A0A6P8CFT4 | MEGYPLEASTKALALERPGSFDPVEAIKHGFLHFKREKFDKFPEFYEELAKGQNPKFMVFACSDSRVNPSHVLNFHPGDAFSFRNIANMVPPYDQTRYSGVGAALEYGVKHLGVGLYRCSELNCKTNLTVECILVFGHSLCGGIEGLMSLPADGSTSTDFIQDWVKIGLPAKNKVLAEHENEPFPIQCKHCEKEAVNTSLANLLSYPFVRDRLIKGTLALKGGYYDFVHGRFDLWGLEFRVHHDLSI | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 247
Sequence Mass (Da): 27706
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A0A662NYB2 | MRKMGGLYLVGIGLGEKGISVKGLEIARKSDMVLLDSYTNVIDENKVKTLSGLIGKEVRLADRTSLEENIDPLIEESKKKRICILVPGDPLLGTTHISIVVRARELGVKCEVIPGASIFSSIGLTGLSPYKFGRTVTIPHLEKSFKPRSFYYQIKLNKDVGLHTLVLLDTERGGMSPSVAVTILDEIENEERLGVVSNSDLIFVLSRIGEENQHICLDRLESVISKEFGPPPHSLVLPGKIDEVEREMIKALFGVEV | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
EC: 2.1.1.98
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Length: 257
Sequence Mass (Da): 28290
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A0A2K9EBY1 | MGKGIFIAGTDTGVGKTFITAGLNYCFQKANYKCCSFKPVQSGGIEKNGSLIPGDIEFVKKLTGIDEPYEKLNCYCLKEEVSPHLAAELEGVEIDTNKLLESFNYLKEKYNYTLVEGAGGLIVPIIRDKYYMYHLIKDLNLPVLLVARAGVGTINHTVLSCEFAKNTGIKIKGIIINGYTNTFCEKDNIDIIEKATGIPIVSVMPQINVYDFSHLKSYYKKHIELDKIISLCF | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 25956
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A0A0P0VAP7 | MADRLELQGRHGKSRVRVSRVWRRPAAAGGHVIVEWNVAVSVVSDCLPSYTSDDNSAIVATDSIKNTVYVKAKECTEIVSMEEFAVILGRHFTSLYPQVSEATVTIAERPWERVVVDGKPHSHGFKLGVEKHVTEVIVKKSGNLLINSGIQGYSLLKTTQVFLPDANLSHWGCLGSLVKTVYVLYF | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
EC: 1.7.3.3
Subcellular Location: Peroxisome
Sequence Length: 186
Sequence Mass (Da): 20567
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A0A8D8R7J3 | MQQDLMPSFSPTPMSHNPYMTPSSNYFNPAASGPNYPSVSPNSAKLLHLSCNSKSLPPLLTNNSAASPNSYTPSNGFLNPYSGYGTHQQNSMYSAFHNSYSPSPHSSLQDYESYSNPYAANQQAFANYYASQGYAQYRSSSTTASSPYNISKPMPESPSSEPSSPSRIENQTPGRKSSENRRGRGRKTAANTSTTSAGSGNTSVPLNPNQCPPSPTSTIGGHQIKERVFIWDLDETIIIFHSLLTGSYASKHGKTIQDVVHLGQKMEELIYGIADNHFFFNEVEDCDQVHIDDVSTDDNGQDLSGYNFSSDGFRSSVLNVPSAPPGLCLASGVRGGVDWMRKLAFRYRKIKEIYNNYRHSVEGLLTHQKRDEWIELRAEIERVTDNWLSMAIKCLETIKQRPNCTNVIVINTQLIPSLAKILLFGLGGIFDVENIYSSTKIGKESCFERIVTRFGRKCTYVVIGDGPEEENAAKQRIFPFWRISSHSDLVAMYHALENGFL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
EC: 3.1.3.48
Subcellular Location: Nucleus
Sequence Length: 501
Sequence Mass (Da): 55610
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M0LFY5 | MSGGYAEATATVSAGARLHVGFQNLSLARDRLYGGIGVGLEEPRVTVTAEPAEGVETDDPLVADYARRAVAILDVPGVAVDLESALPRHVGLGSGTQLALSVLAATAHAYGLEPRVRERAPALGRGGRSGVGVATFEAGGFVVDAGHPTNRFTTDPPAEGDWAVPPVVARHDLPDRWRFLVAVPEADPGRNGDDEDASMREVVERADPTVSDEIAGVVTRKLLPAAAEGRLEAFGDAVAEIGRKNGSWYADAQGGVFRPPAGALVEALEECPVLTGIGQSSWGPVVYGVTDRRHAAEAKAAAEDALADLDCDGQVLLSVPAGAGTNASTSANASASSDRNPDPEPRTTGGARVTLEDDT | Pathway: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.
Function: Catalyzes the condensation of 4-aminobenzoate (pABA) with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
EC: 2.4.2.54
Catalytic Activity: 4-hydroxybenzoate + 5-phospho-alpha-D-ribose 1-diphosphate + H(+) = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate
Sequence Length: 359
Sequence Mass (Da): 36979
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A0A351U7U0 | MGPNIEDFDYDLPKALIAQYPEKDREASRLLVFDRGEETIAHRSFRDITQYLSKGDVLVLNDSKVLPARLRARKDTGGAVDILLVERISDTRWLCLAKGIKAGNKEQKVSVGPMEARLTKGEDYWVIDFHNDGDTFDVMRRYGTMPLPPYIKRNDGNGAIDDERYQTVYAEMSGSIAAPTAGFHFSVGLLETIKRMGVHVVTITLHIGVGTFFLIKKRNVQDHHMHGEYYHITPEAKAFIGKAKGDGRRIIACGTSAVRTLETVYSESGKPLAGKTDLFVYPGYRFKMVDAMITNFHLPRSTPLLLVSAFAGPERIRRCYKEAMERGYRFYSYGDAMLIL | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
EC: 2.4.99.17
Subcellular Location: Cytoplasm
Sequence Length: 340
Sequence Mass (Da): 38357
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A0A7E5WR10 | MVVGRRNVSVMRLGRCVAFLAAAAILLPFTILLMVADQQYNLTYSSKRVFYQERDFYKINGTYYAPAFTITTPTMLRTQYIFENGTHEEGLLTRDKFMEVNARMEARRDFLKNECSKLGLDTSSQKSNAWEYLINRQYHVIWCNIFKAASTSWMYNFNLMANYTAAFLDKTKEVPLELARKKYARPTAEMIKKAQGDSITFLIVRHPLERLASAYNDKIVHAWPKSFHDKMGQRIIRKYRKKQTQESPSLPEKYPIFQEFVSYVLDEAKAKRSLDMHWTPYTTFCTPCKFNFDVILKFETLDEDQRFLIQLAHLQEIIKPEWRNSGKGTNTLHNINHLYSGLKKNQLDGLYNLYKYDFQLFNYTIDNYYEIVGQDETSSHG | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 381
Sequence Mass (Da): 44802
Location Topology: Single-pass type II membrane protein
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A0A2X3CIA9 | MNALVFIMDPRHPLFEPDTSAQVIAPLIARASGPLGTNAQYLFSLEQALRKLGMHDASLDDLVASVRALLGESPTPGLA | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 79
Sequence Mass (Da): 8399
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A0A8B7HMN5 | MDSMPFSRGSDVGPWGNSSGANTSQEAEDLGEGGGARGDVRNEELAKLEIAVLAVTFAMAVLGNSSVLLALHRTPRKTSRMHLFIRHLSLADLAVAFFQVLPQMCWDITYRFRGPDWLCRVVKHLQVFGMFASAYMLVVMTADRYIAVCHPLKTLQQPARRSHLMIAAAWVLSLVLSAPQYFVFSMIEVNNVTKARDCWATFIQPWGSRAYVTWMTGGIFVAPVVILGTCYGFICYNIWRNVRGKTASRQSKGAEEASGVFPKGRLLAPCVSSVKTISRAKIRTVKMTFVIVTAYIVCWTPFFVIQLWSVWDEKSVWTDSENPTVTITALLASLNSCCNPWIYMFFSGHLLQDCVQSFPCCQNITQKFNKEDTDSMSRRQTSYSNNRSPTNSTGIWKDSPKSSKSIKFIPVST | Function: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system.
Subcellular Location: Cell membrane
Sequence Length: 413
Sequence Mass (Da): 46194
Location Topology: Multi-pass membrane protein
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A0A534LVU8 | MAVRHPLDGATVLVAASEDLVERLAHAVREHGGRAIPFPTVRVTPPPDLRKLDQGLRMWHRLDCVVFTSAQGVEAVVERAQSLGLDLSRFAGTVAVVGPATGAAAEAAGFPASILPEEFLTDAIPNALGDVRGQTIFLPRSRLARKGLAEELRARGAKVLEADAYDAVPAEPDLASVRRERKFDFVLLTSASAANNLATLLPDDLRKRLIDEAGAVCIGPIAAEAARSLGFRVRAIAREHTVPGLVECLLEVQAHG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 256
Sequence Mass (Da): 27234
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A0A1B6K579 | ESRLNLVQRNLDIFKHIIPQLVKHSPDTILLIVSNPVDVLTYVAWKLSGLPKNRVIGSGTNLDTSRLRFLVSQKLNLSVESVHGYIIGEHGDTSVPVWSGVNVAGVRLRDVNDDIGRKNDTESFNLIHKQVVDSAYEIIRLKGYTSWAIGLCVAKLCQSILHNAHSVHAVSNAAKGFHGIDQDVFLSLPCVLGENGVSHVIKQPLREEELQQLKKSAKTMADVIKGLKF | Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
EC: 1.1.1.27
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Length: 229
Sequence Mass (Da): 25313
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A0A0R2J635 | MSVKQTFLKACQKDCYWSPESRILLAVSGGVDSMVLLDLVSHLPPSIKPWFAVVHFNHQLREVSDIEEQFLQSYCLEREIPFYSKRWESVDLPQNGVEAAARSARYTYFQLIMEQVGATHIVTAHHGDDQVETILMRLVRGSHLIGISGIKTKRPFAKGILVRPLLSSTKKELVSYSQQYAVPYYEDESNQNLMYTRNRYRNEIVPLLRKENTNLVEHFMDFSDDLSDIISLVQPLINEVFKQVVKIRSPEYYEVDFPELITHPKEMQRQVVSQLLSQLADQNPFEYKREHINQIVDLANDSKSNSYLTLPEGFICRKGYQLIVISKELNEPKKAIDFTVILEMNQWQNLPNGDRIGLFNSHMLEDSVPGLKIYLDCHSVQLPLTVRHRQDGDRMSIKGLNGGTKKIKDILIDQKIPIEERNSAYLVTDLTKKIIWLVKYKESQLSIGKETDKIQYILVYQNHELY | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 466
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 54024
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A0A2A7SR60 | MEFEWRYEKEQPQQLKYFLKEKGISKGLLAKIKFQGGTIKVNDKRENVLFSLSDNDKVTIVIPAEGEHETVLLDETPIDIIYEDEHLLVVNKPAGISSIPAQYHPNGTMANRVKAYYKRQGYEDQVVHVVTRLDRDTSGLMLFARHGFAHAKLDVQLREKKFIKKYQALISGSLDDLKEHGWIDLPIARDYSSLLKRQVHVDGRSAQTEYWLEKRDSEIALVDIQLHTGRTHQIRVHFSEIGCALLGDEMYGGRMDLGIERQALHCYDLRFYHPFTQKLLEFKQPLAQDMAAIVQRFED | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 299
Sequence Mass (Da): 34643
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A0A218VY62 | MESSRYVVEELPTMAKDVSLLELRQRLAEFAHVRGWDQFHSPRNLLLALVGEVGELSEIFQWKGEVARGLPNWTPRDKEHLAEELSDVLLYLIQLADVCGLDLGEAALSKIIKNARKYPVIDRNYSSPDH | Function: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism.
Catalytic Activity: dCTP + H2O = dCMP + diphosphate + H(+)
EC: 3.6.1.12
Subcellular Location: Cytoplasm
Sequence Length: 130
Sequence Mass (Da): 14827
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A0A0B5DHM8 | MSWLVTGGAGYIGAHVVRVMRDGGESVVVYDDLSTGRADRVPDGVPLVVGSVLDRDLLERVIRDHGVTGVVHIAAKKQVGESVERPLHYYRENVTGLQTLLEAMSATGVGAIVFSSSAAVYGMPDVDLVTEDTACAPMSPYGETKLIGEWLIKAAVTAYGMRGASLRYFNVAGAASPELSDTGVFNLVPMVFERLEAGEAPRIFGDDYTTPDGTCVRDYIHVQDIASAHLAAARRLEDAPRGTALTLNIGRGEGSSVREMVDRILKVTGNEGVTPEVTDRRAGDPARVVAAADRIRGELGWSARHGLDEMIESAWQGWRHHRR | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 323
Sequence Mass (Da): 34796
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Q29RR7 | MSWLFPLTKSASSSAAGSPGGLTSLQQQKQRLIESLRNSHSSIAEIQKDVEYRLPFTVNNLTININILLPPQFPQEKPVISVYPPIRHHLVDKQGVYVTSPLVSNFTMHSDLGKIIQSLLDEFWKNPPVLAPASTAFPYLYSNPGGMPPYASQGFPFLPPYPPQEANRTISSLSVADTVSSSTTSYTTAKPAAPSFGVLSNLPLPVPTTDTSTPISQNGFAYKMPDIPDTFPELSELSVSQLTDMNEQEDVLLEQFVTLPQLKQIITDKDDLVKSIEELARKNLLLEPSLEAKRQTVLDKYELLTQMKSTFEKKMQRQHELSESCSASALQARLKVAAHEAEEESDNIAEDFLEGKTDIDDFLSSFMEKRTICHCRRAKEEKLQQVIAMHSQFHAPL | 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: 397
Sequence Mass (Da): 44249
Location Topology: Peripheral membrane protein
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A0A218W4L6 | MSSSVPSRRFLDSSPSLGEPPTGPNGTVGESYMNDPNFDTNMVIILAALLCALILALGLNSIVRCVMRCGQRLGPNTPERAAARLATTGLKKHALRRIPVAVYGSAEGVFTATECPICLGEFVDGEKVRVLPKCNHGFHVRCIDAWLASHSSCPNCRHSLLDPPPPPPPPPPRNRPGLEHVVVVVNDNAS | 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: Membrane
Sequence Length: 190
Sequence Mass (Da): 20304
Location Topology: Single-pass membrane protein
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A0A218W0L8 | MASNSGLHREIEAFRQLLLDEGFLNDAFKLNVENVGSMIGKPNFVEEIMTTYFRDSAKYIEKAEKLLDDDMPINIVELNRILRNLNRSSAIIGAHRVSNETSKLRDYGLDGNWVCCKASLQLVKREHAELKGRMATYLQMKRQAGPVEAAERPMSSGRNKAEPAETTKRP | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 170
Domain: Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence Mass (Da): 19241
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A0A1S6LQZ2 | TYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGFDF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 177
Sequence Mass (Da): 19607
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A1L539 | MPSWIGAVILPLSGLLLSLPARAEVKARSCGEVRQAYGAKGFSLADIPYQEIAGEHLRICPQEYTCCTTEMEDKLSQQSKLEFENLVEETSHFVRTTFVSRHKKFDGVTASISVLLQHHPKMEVERKSLHPEMDLIRKRVLSSWHSQLQDCIWI | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 154
Sequence Mass (Da): 17550
Location Topology: Lipid-anchor
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A0A2I1M934 | MFDFNNAKNRLDEVITPTHLFYSEFFSDIASNNVYIKPENLQKTGSFKIRGAYNKLSKLDDASKDVGIITASAGNHAQGVAYSANKLGIDATICMPEQTPMIKVDGTLKYGANVVLHGDNFDACKEHAIKLAEENGYTFIPPFDDLDVIEGQGTIGLEIVDELEYVDYVIVPVGGGGLIAGIAKCIKEISPLIKVIGVEPYSARSMQESIRKGKIIKLEGVDTIADGTAVAEVGSYTYDIAKDYVDDWITVTDEEVLMAFINLMEKHKLVAEPSGALSLAALDKLNFYNKNVVSIISGGNIDMSFISQLINRGLFETGRITRINVEVPNIPGKLQDLLADIAYTKANIISIDHDSLKEASRFKNINVSITLETNGPDHVKKIRDVIAKKGYIIH | Pathway: Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 1/4.
Function: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
EC: 4.3.1.19
Catalytic Activity: L-threonine = 2-oxobutanoate + NH4(+)
Sequence Length: 394
Sequence Mass (Da): 43123
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A0A078GE47 | MIVLSASGDLGPLRFQPVSLHAHVIVPDLDHVNIENPEDFIEDYCSTIVNTSMDMSIPPWEFHVLNLKTSNAESVGIVKFHHSLGDGMSLMSLLLACSRKTSDPNALPTIAATTKKHQKSNDKGWWFIGSGFWYMIRFIFINFVEVFKFVLTLCFLRDTKSDLSSESVDEIQPKKVIHRIINFDDVKLVKNIMQMKRILLYSLEAFNFYGIIKLTMKFFGEKVVQAISKRLFDHTTLTYLNVMGPDKEISIFDQPISYLAASALTGSQVLNIHFVSYVNKLTISLAVDATVIPDPHRLCDDLVESLNIIKSTALEKFRIS | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Subcellular Location: Cell membrane
Sequence Length: 320
Sequence Mass (Da): 36223
Location Topology: Single-pass membrane protein
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A0A2U2BER3 | MKITMLGTGAALPDPDRAQSSILVTLENGKNYLFDCGEGSTRQMVKANINPADVPWVFLSHLHYDHVCGLPFFVLSSWVFNREGKLKVFGPKGTQDFVDHSFENGAFRVDIQARAAYPARQKNIEAVRPEVFEVEPGLMYEDEDVKIYIDVVDHIPTEITDCFGIRMEAEGKVVAFSGDTAPCESMIRLAQDADLLIHECTFPESFLKHRAESGVGTFAHTSPLQLGEIARKANVKSLVATHFGHYDSTSPVIKRAAGNHLPVDLMGPERLDEVARDIRKSYKGDLRLATDLMRIDL | Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Length: 297
Sequence Mass (Da): 33049
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A0A8D9EUG0 | SSQTKTENKAINDELHLVKPRIKLLYVTPERAVTDSFRYLLQHLLRYNKLAYFVVDEAHCVSEWGHDFRPTYRRLGELREITGIGVPIVALTATAEPKVKQDIINVLKFNKPYKVFKTSTFRSNLFYDVIFDDLLKDSYAHVKEFIEKCLGKDNKDNNCGIIYCRTREHTVDLADALRRKGIPCTPYHAGISKHERTRVQEAFMKGELNVITATISFGMGIDRQNVRFVIHWGMPASIPAYYQESGRAGRDGLQSYCRIYHSEHSKKSLEYVIKTDQTTKRDQLELKFKNYLSMLEYCEQANCRHAVFAKYFDDEKPGCRSHCDVCTNRKDVETKLEQFGERSLSRFRNRFGITSSETDNTDMYGGGRTGQKEERWEYEQSSGGYGDEPGTSSGAGDGQARTQELRKLLQLRTAAKKMTDKIQSRPETGHYKIKCPESTEAKLNGAPPSFREQYRFLLEGHLTKNARSCKFSFSNNSESVMAIDWEYEVFSQAKGKPMYTNLMVKATREIKQMTENKELHPRLLSSMFMKNTMSGW | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 536
Sequence Mass (Da): 61822
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A0A6P6U627 | MSGESSTALSNGNAGAPSDPHRTYEVVVAATSKMGIGMDGKVPWKLPTDLKFFKDITVTTSDPTKKNAVIMGRKTWESIPLERRPLPGRLNVVLTRSGSFDIATAENVVICGSLLSALELLAASPYCLSIEKVFVIGGGEILKESLNAPECDAIHITEIDADIECDTFIPAIDSSVFQPWYSSFPSIENKLRHSFTTYVRVRNSGVEPISQTNGVIPGNSLDIAKIEGKTFSFLPKMIFDRHEEHKYLRLVEDIILNGTAKDDRTGTGTMSKFGSQMRFNLRKSFPLLTTKRIFWRGVVEELLWFISGSTNAKVLQEKGIHIWDGNASRDYLDSIGLAEREEGDLGPIYGFQWRHFGARYTDMHADYTGQGFDQLMDVIGKIKNNPDDRRIILSAWNPSDLKLMALPPCHMFAQFYVANGELSCQMYQRSADMGLGIPFNIASYALFTCMIAHVCDLLPGDFVHVIGDAHVYRTHIRPLQDQIQKQPKPFPVSITHILKINPQKKDIESFVPADFTLLGYDPHQKIDMKMAV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Length: 532
Sequence Mass (Da): 59400
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A0A5N6RND2 | MSKAKTAEWVSRSRSWSHDRPALVDAVIPFYHSIDFEVHRHWLALTHSFPLSQWYSDAPGPSTTLHSLLTSSTLTKDLDSRRRISIWVLIIWSPMLVIVRTRNARNVIEKPLQQKCQKRRRAPLTFFSPGEHRWTV | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 136
Sequence Mass (Da): 15929
Location Topology: Multi-pass membrane protein
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A0A078JQ88 | MSKKMIVLKSSDGESFVVEEAVARQSKIISFLVEELPDQELPFTNLTSEILRNVIEYCKKHVVEYGSGDSSSSSSDDLKKWDVKFVGEIDQPTLMDLIMAANYLHIPSLLDVTCQKVADMIAACEDEKEIRSTFNIENDFTEEEVEAIRMENQYPN | Pathway: Protein modification; protein ubiquitination.
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Subcellular Location: Nucleus
Sequence Length: 156
Sequence Mass (Da): 17706
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A0A162F8H9 | MTALPTVPVRVVVVMGVSGSGKSTVASLLAERLGWEFLEGDDLHPQANVDTMHAGVPLTDEDRAPWLAEIARVVDERVTAGRPVVVTCSALRRRYRDVLRRDDLVFAHLAGSRDRIGEHLASRVGHFMPTTLLDSQFDALEPLDDDEFHVLVDVGRAPDEEITEILDRLGLAPAGASPQGV | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 181
Sequence Mass (Da): 19693
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A0A218W864 | MRTRREEGEEEEEEEGGMAEETESGSRRFYGCYLLVSLSPRHKGQTYIGFTVNPRRRIRQHNGELRSGAWRTKNKRPWEMVVCIYGFPTNVSALQFEWAWQHPRESVAVREAAANFKSLSGITNKIKLAYAMLTLPPWQSLNVTVNYFSTKYSKHSAGCASLPKKMKVCICPMDELPCYVDRSLIQNDNEWEDFGEASSESGSLNELVADGAVHTSPADELVEPSEANGRQQLTEAPLVGAQSGSQSCSANSPMRASSPIMPNLSCLEDTQNGRSMFASIQEFGVKLDQPPGNQANMLDKVQGPTSSNPVASKEVEIIELITPPPDPRSRRLQGKRRRVSTVCPEIIDLTNSPVFVQL | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 358
Sequence Mass (Da): 39829
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A0A193SNE6 | MHATLEHMTIWGLISDASLLVKAVMLILLLASLVSWYLIIQRSLVLRHYERSLDAFQQRFRSAADLAPLQAQASSAQRDAAGIEDVFQTGYAEYMQLKQRAGIEPDVVLSGVERSLQVAISEQELQLEKGLQFLATVGSVSPYIGLFGTVWGIMNSFIGLSQVQQATLSTVAPGIAEALIATAIGLFAAIPAVIAYNRFAARGQTLTARYYSFGNELQVRLNRTLQGLTRNMAAAA | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell inner membrane
Sequence Length: 236
Sequence Mass (Da): 25706
Location Topology: Multi-pass membrane protein
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F2D138 | MATAAASSLLSPASKFALQSRRSSPKTAPRSVRFLPVRAQQQVKEEEPAATVPPPQEEGQATTAAAAKGPAQSLPRQPRAESKNMGREYGSQWLSCTTRHVRIYAAYIDPETNAFDQTQTDKLTLMLDPTEEFVWTDETCQMVYNEFQDLVDHYEGAPLSEYTLRLIGSDLEHYIRKLLYDGEIKYNMRSRVLNFSMGKPRVKFNSSQIPDVK | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Plastid
Sequence Length: 213
Sequence Mass (Da): 24022
Location Topology: Peripheral membrane protein
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A0A7E5WDG0 | MTSTPFRRLCHWGPICVLGIIKLITWAMVHLLGMWWPPHGSLAGALHAGLFLTLAGSTLYYFLQSLLEGPGFVPLGWKPEYEEDKQYLQFCSVCNGYKAPRSHHCRKCGYCVKKMDHHCPWINCCVGHNNHGYFNMFLMSAVLGCFHASVVLIICMYHAINRVWYVHHGTGREPMIYLTLTTLLLTLLAIGMAVGVVLAVGALFYLQMKGILRNRTTIEDWIVEKAAGRREELNLPPFVYPYNLGWKNNLKMVLYGSRYDGIKWPLKEGCGEYDLTREQQAQKLDKLVRSRVLVCVREYSGRVLPLWSRPRAALAAPCSDEPRLPLRPGDLVRATRHRRSVTLCTAGACCRCGRGPAPRWPRPAATSRACRCGPGTSCGPPGTGGQLHYVQRARAAAVVAAPRRAGRALQRRAAPAAAARGPRAGHQAQEVSYTMYSGRVLPLWSRPRAALAAPCSDEPRLPLRPGDLVRATRHRRSVTLCTAGACCRCGRGPAPRWPRPAATSRACRCGPGTSCGPPGTGGTGCSVRRY | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 530
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 58492
Location Topology: Multi-pass membrane protein
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A0A830G3K4 | MRSISGARGGGQLVRSAAAFACLTGEAVAVTDVRAARETPGLKRQHVAALDALAAITDADLDGARVGSERVAIDPGPVAGGDARVEIGTAGSVPLVVDAVLPLAARLDDPFRLTVTGGTDVRWAPPLDYLRCVKLPLLRAHGLDASLTCERRGFYPAGGGAVTLTLRPSDLDSLSLSARGARRGIDVRSVASESLADADVAERQADAARDALPGDGETSVAYVPADSPGSVVTLVARYAGVRAGFSALGERGKPADDVAREAVAAFEAFEATAASVDTHLADQLLPFAALAGGEYVAPERTAHLETHAALLETFGVDVTLANDADGETKGRGDTTKGEGDARAGDGTESDGDTDGPVRVRVAPGFSR | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
EC: 6.5.1.4
Subcellular Location: Cytoplasm
Sequence Length: 367
Sequence Mass (Da): 37471
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U5P9W7 | MEMLFVVLMFLLSISLILLVLFQPRQQQSLSTDATSNLGKPNYWLARRGMKLATLIVSVLFFLVLLIYLLLARA | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 74
Sequence Mass (Da): 8457
Location Topology: Multi-pass membrane protein
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A0A3R7JRL9 | MLLIGVSTLIPIIGCLYAALLDSYGTLEQELKQEQTRMLEAQQEGWSQKQERKHPKRVLMYLYSGHLLSAWVRELTGRDADGLHKPEWTWTLTLLFAGILVCGGLGQVLNEAQTLAIERDWVVIIAQGSGEERSTVLAGLNTVLRRIDLACKFLGPLAFGIIMQFAGHDPTTRSLIGVSTVAIWNALSTPLEYFMTRDIYRLVPELDTKGEPEKQNGEQQRQESVDGGFALSVYAAMWRNYSRHPVFLLSFSYCALYMTVLDNGSLNTAYLKWRGVPDSLLGTSRGVGAAFGLIGTVLFPYLRHIISRLERVAVVSIWLFLLCLAPVLAAFLLAGESRVSDYVMLCCMVGARMWLWSADLAETQIMQEWIEPSHRGAINAMQTATYQLFYLLIQVVGVVFHDPQQFEALVFFSVATVFAAAVGFTWWDVTVGRHRSQYVHFMPNNGPTSALP | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 452
Sequence Mass (Da): 50568
Location Topology: Multi-pass membrane protein
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A0A450VQ26 | MLIIFALLCAAIALIYGAVSVTSILSKPAGNPKMQEIASAIQEGAGAYLNRQYTTIGIVGLILFLIIGFVLSWVTAIGFAIGAVFSGAAGYIGMNISVRANVRTAQAAGNGLNAALQIAFRGGAITGLLVVGLGLMGVAGYYGILTHFMGVESKAALGALVGLGFGGSLISIFARLGGGIFTKGADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDCAGMAADLFETYAVTVIATMLLGGLLFGADSRETAILYPLVLGGVSIIASVIGTFFVKATEGAKIMNALYKGLIASGILAAAAFWGVTEYMAGSTGLTLASGAVISSGALFSAAMIGLVLTGAMVYITEYYTGTEFKPVQNIAAASVTGHATNMIAGLGISMKATAIPVLFICASIWGAYELAELYGIAIAATAMLSMTGIIVALDAYGPITDNAGGIAEMAELPDKIRNITDPLDAVGNTTKAVTKGYAIGSAGLAALVLFADYTHELGVHFGNDVQFLLSDPRVIIGLFIGGMVPYLFGAMAMEAVGRAAGSVVMEVRRQFREIPGIMEGKARPDYSRSVDLLTKAAIGEMIIPSLLPVLAPIIVGFVLGPKALGAMLIGTIVTGLFVAISMTVGGGAWDNAKKHIEDGNHGGKGSEAHKAAVTGDTVGDPYKDTAGPAINPLIKIINIVALLIVPVLPSSGLL | Function: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate
EC: 7.1.3.1
Subcellular Location: Cell membrane
Sequence Length: 686
Sequence Mass (Da): 69847
Location Topology: Multi-pass membrane protein
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A0A078HPC7 | MILLFRVRLINPTFERSTVATKRQNPKTTPSFHCKASSFESKTMSHSSAPRMRKCRQTKKEEEEPLGGDMEDLFSEKETENIRLSLLGWYDENQRDLPWRKTRSETEKERRAYEVWVSEIMLQQTRVQTVMEYYKRWMHKWPTIYDLAHASLEEVNEMWAGLGYYRRARFLLEGAKMVVAEKEGFPNKASSLMKVKGIGEYTAGAIASIAFNEVVPVVDGNVIRVLARLKTISANPKDRLTVKNFWKLAAQLVDPSRPGDFNQSLMELGATLCSVSKPSCSSCPISSQCRAYSLFLENGSIPVTEYPTKVVKAKPKLDFCCVCVLEILIQENNRSGGRFVLVKRPEEGLLAGLWEFPSVILDKEASVAARRKAINLYLKEAFHLEPKETCTVVSRKELGEFVHIFTHIRRKIYVELLVVQLAEGGTIDMFKDEAKDTMTWKCVDSDVLSTMGLTSAVRKVYSMVEAHKQDLSVSSNRTAISRKRRIT | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 487
Sequence Mass (Da): 55549
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A0A8B7EF62 | MDCWGNSHGRIEPAAGAGAARKTQRLPPRTARVNGWSRPGDWYQVASWAVIFVMAVTMLGIFIPFLPYHWKMLAYVVIGGLLTVHLIVHLIAITIDPAEANVRMKKNYLDAVPLFDRTKHQHVIEDQYCHLCEVTVGAKSKHCKMCNKCVTGFDHHCKLLNNCVGTRNYSYFFGSVVSAAFNLIFIMAVLLYFLVQLLMDPEQLQQNAELTDAEVDLDLWPLFLPLFPVNVNVTVILCILFLTIFLAVGSILVIWRLLLFHLFLISKKLSTFEYIMQKREKEQGETEEKEEEEKEVKTRSPPFRGAHEEPRHSFRHLSLTPSNISLPPSPSEIQRKDTASVVPVAWADDNSEVLTLGAEGGWKNVSPSVLLKTLPSTEILPIELVPPNSVADSMAMIADPEGLVPREAWRLPRAPPEDPEAAANYWDALTSRLAKAFPGSKGESREEPPTLVVSMKDSRSSEGKEEPEPEL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 471
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 52831
Location Topology: Multi-pass membrane protein
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A0A662P2Z7 | MFNLVLADSELETIPKEIWSHPSISRYCSRRRKKPRETILDSSYHYKALRHLEDGYRRGRPDIVHFSLLYALGTPLCKKRMLNIFVHTRRNLVIEVDPETRLPKHYNRFIGLMEQLFREKRVPPTGKPLLLLRRASLSDILKEKGDLTILIREGGKKLNPSKLISLAENGEKVNLVVGGFPHGDFISKFDFEMEFSVYEDPLEAWVVIGKVIHSIEEEMGIG | Function: Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA.
EC: 2.1.1.-
Catalytic Activity: a pseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = an N(1)-methylpseudouridine in 16S/18S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 222
Sequence Mass (Da): 25710
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A0A351U741 | MVGIDIVDISRIGDVVKKYGDKFLSRVFTQQELEYAGKKRRMYESLAGRFAAKEAFIKAYGKRVGWREIEIIQRGGKPSIQCRGRLYEDVSISHERAYAVAVVMIGKGE | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 109
Sequence Mass (Da): 12389
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M0LJ43 | MRMSEETDADGDAEAEAEDLTHTTDDGDVQMVDVGDKPDSERRAVAAGEIRLQPSTVEAIRADEIGKGDVLATARIGAVQAVKHTWETIPMCHQIPITNVDTDFSLGEDRVECEVAVETTGKTGCEMEALEGVTTGLNVVWDMVKAVEKDEDGQYPETGIENVRVLEKRKRTP | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Length: 173
Sequence Mass (Da): 18858
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A0A8B7EPE0 | MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLLFGYWSITKWNRERRRLLIEDLEARIALLPLLQAESDRRVLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVTPMVGELYGLRTMEEILNANYGFMGHT | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 144
Sequence Mass (Da): 16568
Location Topology: Single-pass membrane protein
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A0A346PE93 | MTTRDLLEAAREIQSAAHVPYSEYTVGAALETADGEVFVGCNLENANYSNSLHAEAVAIAEAVKNGHTDFSRIAVSSGPRDGVTPCGMCRQTLAEFCADDLKVICDEGEGEEPTVYTLGDLLPNTITQDMLE | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Length: 132
Sequence Mass (Da): 14100
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X4QZH9 | MTQIGQPKAGYDLVIATDGSCSGNPGPGGWAWVEQYSGRSAAGGSPQTTNNIMELTAMISALEFAGPEADILLRSDSSYVIKSMTQWAPGWRRRGWKKADGKPVLNRDLIERMVNLYEARTGRTDIEWVRGHSGDAANELADRLAVEQTSLHAR | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 16792
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A0A428LFL4 | MPPRSEPGARRGEPRAGGEPAPRGPAGAARVDGARALVDRFGRAVTYVRLSVTDRCDFRCVYCMTQDMRFLPRSDVLTLDALAALARACVALGVRRIRLTGGEPLVRPGLTTLVERIARLPGLDELALTTNGARLAQFAAPLKAAGLARVNISLDSLREDRFGALTRTGRLRDVPAGIAAAKRAGFRRIRLNCVILRGRNDDEVLDLVRFARAQRLDLAFIEEMPLGAIDEHDRASCFVSSDEVLARIRGRYALFPSDVSTGGPARYFRMADGEIRIGVIAPHSHNFCGDCNRVRVTASGRLLLCLGNEHGVELRDVLRTNPGDDARLRGAIAAAMPLKPERHRFDLDAPHIVRFMNMTGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 361
Sequence Mass (Da): 39403
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A0A3L6L6E6 | MSATEHCPAALALMTALMFSLMQAGANVQAETNGPLLGPLCELLSLPAGAAGLEEKIYMAKASYHNLQDMNLTLSDSEWRQLFDKQAPDSERPKTPKAPHDTDKSRLEHWQDWLDNASRLDAKQVEEEILKKTNLANADRSKKAAVLAAIQPILRKASEYNKQLKLLTADSNDDSKMAIQKLINDSTYGDNIGATTEIIQASTTGAGTIVAVSTACGSATTSTKVKTTAGLAVCLCAKAATCGVGKVCAKGQAETATLADNFNNVGAVVATIDALCIRSRKQAITAASIRSAIGDMLKHLHTDTARSYLGEYTSTGCTGQANSGECVIYHSNAAAAKTAIQSSEWYTKLTAASDLLEKKQKRNTQIKTPNQLLEAEEQSAYSLALQMQLTPPDFAAAASTTKGSRSPSPTEKKTGCAAATNKTAAECKNLGCEHDKKENKCKPKAATENAAAGARGDKAEGAAGTAVSTGCPRHGTDKTACENDKTGNKKNCAWRKGKRVKMTRIKTSLCA | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 511
Sequence Mass (Da): 54096
Location Topology: Lipid-anchor
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A0A8D9FBB5 | MARKRPKASTSLSTATAAGTSIPTRPKAKSPRRKTRRANENFEGKLSHASPVSPNSKITKYFHPQEDELCSSQHCGNDLSLPTTPMILRTSPRKLLTQANLNTSVIHRGRPLPPALSGHDGSPPKTQHKPNGVMSPQLCNSMPPPPAPTEDKRFATPHKITSPPAAILSSRNSPSSALSTLSINSPQSNVSQPVGTTNKKSKRCLNPVIVPAGTNSTNQVSQSRITEFFPVRRSIRKTKKIVLQERQKSLEEAVLNNQEEGLEVHMFEGKGRGVVTNRKFYRGEFVVEYAGQLITMEVAKQREKLYAQDQNTGCYMYYFRHGNSQYCIDATAESPRLGRLVNHSRFGNLATKTIEINCEPHLVLIAKEDIEPGTEITYDYGDRSKESLRHHPWLLN | Catalytic Activity: L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine
EC: 2.1.1.361
Subcellular Location: Chromosome
Sequence Length: 396
Sequence Mass (Da): 44008
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A0A078G3T3 | MALRCFPIWVCPQTAYYHYPLLGFDTKRRRICLWECSSSASQRAITAVGGDVPYGRELKKPSDEMGLTQERPQLETFHRDLSMLPKPLTANSLTSSAWDDSKVRISFQGIPGAYSETAALKAYPNCETVPCDQFETAFQAVELWLVDKAVLPIENSVGGSIHRNYDLLLRHRLHIAQEVHLPVNHCLLGVPGVQKEDIKCVLSHPQALDQCVNSLNELGIQRVSAKDTATAAQTVSSSGERSIGAVASVRAANIYGLDILAQNIQDDANNVTRFLILARDPMIPRTDRPYKTSIVFSLEEGPGVLFKALAVFALRNINLSKIESRPQRGRPLRVVDGSNNGCAKYFDYLFYIDFEASMAETCAQHALGHLQEFTSFIRILGCYPMDLDSSLTILSSSKLSFKLFIAETNSSSREVVGQLESDCFSSDGRSKSSGICSPRASYLRKLADVASNGELLDWPKNDTRRFFHVVYRVGDLDRTIKFYTECFGMKVSRQRDVPKEKYSNAFMGFGSEKSHFAIMVLAHMKLKMDLGISPFQLKMQVYKMVETVRAKGGNVTREPGPVEGGSSIIAIVKDPDGYPFELIQRGPTPEPFCQVMLRVGDLDGAIKFYEKALGMRLLRRIEKPEYKYTIGMMGYNESVVLELAYNYGVTEYKKGNAYAQIAIGTDDVYKSGEVVKIVNKELGGDITREPGPLPGIDTKIVSFLDPDGWKTVLVDNKDFMKELG | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine.
Catalytic Activity: H(+) + L-arogenate = CO2 + H2O + L-phenylalanine
EC: 4.2.1.91
Subcellular Location: Plastid
Sequence Length: 724
Sequence Mass (Da): 80673
|
A0A2I1M6J1 | MIRKMEISDANEVYDIENQAFFEPWSKKNLIKDLKSNTFLNHYVAEIDGKIVGFYISSHVLDQVEIFTIAVDHGFKKMGIATSLLNHLVETSLSNNMKEIWLEVSTKNTPAINLYKKFGFEVMGIRKNYYQKLGEDAYNMKKEL | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 144
Sequence Mass (Da): 16720
|
A0A7E5VIL5 | MVTLMPCSYLGGGASPRCSLDHAEPKAKRPRPDPGTDASDRLSGEVNTSPCESESTSNSPPSLLQDATLPALLVSGSSTLFQNTTTTSNTALSLSAVDSLCLPGTSEVESCSLANGCATSSSLGLALPLTSAGGLCSTSSSAAVAWLMNEDSAGGVKSEVRSPGLCEADVALYGETLPYDQSALPYQYYNSMQQYGSGSAASSYVSSTLYNQPYGAYPPQHNTNNRSSCKATPTYLSAYGVSGVSGVPSTGFGAQPSPYAYSSYNGGLAQSFPTAQQDYSSYAAGYADHNVAQYSGYYATPSYSPYVSSPSSSGSAGHTSYHLGGALSESPSAMLPSINDASPLSPIKTEVHAASRRCRENSGESTASRSRGRGRRNASSSPAQHVPEPATDRVFIWDLDETIIIFHSLLTGTYATKYNKDTQQIVQLGFRMEEMIFSLADTHFFFNDVEDCDQEHIDAVSADDNGQDLSAYNFGADGFQAGAAPAGLCAPGVRGGVDWMRKLAFRYRKIKDTYNNYRNSVGGLLGPAKREQWLQLRAELEQATDNWLTLACKCLNMINSRENCVNVLVTTTQLVPALAKVLLFGLGGVFPIENIYSATKTGKETCFEKIKQRFGERCTYVVIGDGQDEEAAAKAKNYPFWRISSHSDIAALYNALDMGFL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
EC: 3.1.3.48
Subcellular Location: Nucleus
Sequence Length: 661
Sequence Mass (Da): 70506
|
C4WVJ1 | MDLYEVYIKAVSFSAGCASTAMMLTPLLVCKDIVKKKTSDHVNLSTFVGALFRSSLFFRQGFILNLQTVMFVHGMGLLINTLYLALYWYYSNKKMNVITTLFKTTLLSSVLLTYSFIESTDLVVTRFPIMVSIIHLSLIGWPLLSVRETIKTKKWSGHPKPILINSIVLCILWLLYSINIGNIIIFTQCSVAFIFSSAQLGLWAIYPEEKNQRDKMEKHE | Function: Mediates sugar transport across membranes.
Subcellular Location: Cell membrane
Sequence Length: 220
Sequence Mass (Da): 25095
Location Topology: Multi-pass membrane protein
|
A0A0F4LUM7 | MKKFQEWLEKYLVPFSNKLGQNKVLQSISSGMVMTLPVTIGASIFSIFASFPIKPVADWFAKVGITPSMTAIVNGTMNILAVFIAFTIAYDYAQKSKANGVVSGLLSLASFFILMPQVIPGKTPINAFKINYLGSEGIIVAILLSILIGVFYVKLSRNKKLTIKLPDSVPSMVSSSIEPLIIGIIIFVGVFIVRAIFDFSPFGNVFDFVNKLITTPLLHVGGSPITLILIMVLSNLLFTFGIHPAAIQSVIIPIVISMMVGSTPAYQAGKTIPYLSNLVVFSFANNDAAGATLSLVLVALVFGKSKRYKEFFKVSALPNIFNINEPIIFGMPIVLNPIMFIPFILSSFVSSGVALLAVKIGFITNYNPSLGMGMPWTMPKLVADAMIMGWQGAVIWIINFALMCAIYLPFFKVADKQALEEESK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Location: Membrane
Sequence Length: 424
Sequence Mass (Da): 46139
Location Topology: Multi-pass membrane protein
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A0A218W511 | MKVGKLVAAGISILLVVGVCIGVIVGVAHKNNSGDGKGISSTSKSVAAICDPTDYKEACINSLSVAAKNGTTDPKELIVAAFGSALKEVQASLSKSGTIGEGAKAPQQKMAFDDCKELLQYAIDELQASYSMVGDSSLHTMNDRVSELQNWLSAVISYQQTCVDGVTQQDLKNQIQTGLLNATQLTSNALAIVSAISGILTTFNIPAANNSASSRKLLEETEEDRDGYPSWFSVADRRLMAAQAKGQVTPNAIVAKDGSGKYNTIAAALASVPKKNKGRYVIYVKAGVYNEYLTVTKDQTNVFMYGDGPRKSVITGKKSFTDGITTYKTASFSTMGYGFIAKAMGFQNTAGPQGHQAVAVRVQADMAAFFNCRMDGYQDTLYVQTHRQFYRNCVISGTIDFIFGDASAVIQNSLIIVRKPMDKQQNTVTAQGRIDKHETTGLVIHNCRIVPDQQLYPVRLQVQTYLGRPWKGYSRTVIMESTLGDLIQPAGWMPWSGNFALDTLYYAEYANRGPGANTANRVKWKGFKVINRNEALQFTAGPFLQGNQWLKATGVPYLLSLRA | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
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
Subcellular Location: Secreted
Sequence Length: 563
Sequence Mass (Da): 61040
|
F2E695 | MAGELTVMICMAAAALLISLTGGAGVAAASAKELRRGFSATHDTSYSHFQPVLTDPTGAFAFGFLRVNSTTLDLAVLHLPSAFPLWRAMPDRPAPWSAAASLSFNGNLVLTDAATNQVLWSTAAAAGDRAVLLNTSNLQIRSSSSPVAVWQSFDHPSDTIVQGQNLTSSAALHSIDQRFAMRLGSNYFALYVEPPPLSSGSVAAAMYSRHTALEAKAQIVAGGGPIYVRVEADGYLGMYQKEGAPADVMSFDTFNHGVRALRRMTLEPDGNLRAYYWDGSRWVLDYTTITDSCELPTTCGAYSVCVQPSGRCACLANATDGPGCAAPSVGSGLCGTTGGEVGGLYSEVRRHGVEPANKELLGFEHAPSAGDCEALCARNCSCWGAVYSNGTGYCYLMDYPAQLMVAADKRKVGYFKVRSMEEAAARGGRAGGVKAALLAVGVAVVAAAAAFGAYRVWDRRRRAAAETRQQLGADGDGLSPGPYKNLGSFSSVELSSSFNSSRR | Function: Involved in sporophytic self-incompatibility system (the inability of flowering plants to achieve self-fertilization).
Subcellular Location: Membrane
Sequence Length: 503
Sequence Mass (Da): 52919
Location Topology: Single-pass type I membrane protein
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A0A6P6TMI2 | MAGGAGDRSLKETPTWAVAAVCAVFVIISVLIEHGIHSLAKWFQKSQKKALLEALEKIKAELMLLGFISLLITVGQKPISKICISKGAGDTMLPCKKVLDEEAADTGKDKNDSDRRKLLWYAGDALARRVLAAADGDDTDHCSKYKKVPLISQSGIHQLHIFIFVLAVFHVLYSVLTIVLARAKVKKWKSWEQETASLNYQLTNDPSRFRFVHQTSFIRQYSGFSTKPGIRWIAAFFRQFFCSVTKTDYLTLRHGFINAHFAANSKFDFHKYIKRSMEDDFKVVVGISIPLWTFAILFLALNVYRWYSLFAISLVPPIMLVIIGAKLQIIIMDMALHIQDRTTVVTGVPIVEPSNKYFWFNRPHFILGLIHFTSFENAFQMAYFLWTWYEFGLTSCFHENLPVILAKVFLGVAVQVLGSYITFPLYALVTQMGSHMKKAIFEEQTAKALMKWQKAAKERRKLRKAEGDMSPDLMSGNTTPSRGSSPIHLLHKYKMNSDIESSINNPTPRPYHSDADYSETEGPALNSSDDQNSRNHNSPKKEIVGKEPETYNWDFSFSKS | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 560
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 63553
Location Topology: Multi-pass membrane protein
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A0A450TW79 | MYIVQIVIGRIKVKQCPDHFSVQINTPNANPIEKYRMNLAHSPIRPKILALVGPTASGKSDYAVQLARLFDGEIVSADSRQVYRHLNLGTGKITHQEMLGIPHHLIDIIDPEITGPDIIDSGEDYSPAPQVRRSTTGNNPLISHCRIIEGICGARHYSLFDFQRDAYSAIESIARNKRLPIIAGGTGLYIAAVVEGYELLDVKPDPVARQELEGRSMDQLIEIIQRERPGALDAIGARTKRRLIRAIEIIQAGFDYEDAKRKSRRLDALMIGVQWEKDILHRRIRERLYRRLEQGMIEEVEGLRANGVPDRFLFAMGLEYRAILQYLQGGYPSRQHFIDHLETSIRQFAKRQMTWFRGRPGITWVAGADLLSPPTMDRIRSFLENESSDHRTRGFQPMNKKNVLVILGNGFEEIEALAPVDLLRRAQVPCQTASVESERLVTGRNGVRVEADVAFEEVRHRTFDALIIPGGPGTMELRKKTAVLEMVRAHRQQDKLVGAICAAPVVLLDAGVLPGPRHTGHMTILNELPGIEQGQAVVVDGKVITSRGAGTAIEFGLALVSALAGEEVAAEVAKSIHHGKL | Function: 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).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 581
Sequence Mass (Da): 64648
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A0A2A7N153 | MSDTNEIGTHGEFATAPHGEVSPAQVSSEPTLRRGAIDWKQVAILSVAGCGPASVIALNLQFMGQFAGAALVLAFVLVWPGILLLVNTFAEFSKKLPTSGGLYTWNSKAWGPNVGFVYGWMFIGAYLVFSAAGFAVFGGWVEEWLHTQFDISVPWWIFTFLALTYVSTLAYLGISQSLHAALGLLAFEIVVLLVLAAWIFISGPQTGGSFGTAPFEVSSAGSLALGGVGLAMTYGVLSHVGIEEGATLGLEVKEPKRQIPRGLWVAAVAVPAFYILVSYAMVYGYGIDKMTEFGEDPAPLQTIANSYWGQFGLAIVVLATLSSILAFSQTAFLAGARVLYTLGRERVLPQRLGVVSSRQTPGIAIAVMAAISMALGVPLAFLVGPFNVWGYFGFLISIAFLVSYICTNFGLIRYMRRIGEFKWFRHGVLGLIGSIVFLYPLYKTVWPLQTGIYGALPFIYIAWIILGIALLIYTLRKRPEVMQRIGTSLADTDDPHTKHH | Function: Probable amino-acid or metabolite transport protein.
Subcellular Location: Membrane
Sequence Length: 500
Sequence Mass (Da): 54121
Location Topology: Multi-pass membrane protein
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A0A0F7SBA4 | MPTLRGHCNCGALEYQLDATPANLRLSAFCHCTRCQRINGAPYIWTTHWKKEAVTWSSASASKSTASDAEVEKVMGAGVTTAQLYESVAGRKWKLRCSECGNPMGSWNEAKQQWSIWPSTLARPEGDKTGIPGIEAFSATAHTFYGAWKVATVSDDLPKFEGYPNESQQVDRNAQPLPANFSINDFNPHDPRDMVGYGPKPPHPRWPNNARIAVSFVLNYEEGGENITLNGDRAAEQYLTEYGAANGSTAPSNIRNLSVESAYEFGSHRGFWRILDLFKRNNLRFTSWSVGRAVEQNPAVVKAMEEAGCEVASHSYRWFDHSAMSQEEERAQIQSAVRAIKNASSKSREPRGWYTGRQSINTRRLVYSVYKEMGLEKELYDSDAYDEDLPYWVPAPDGTEGEHLLVIPYTLDNNDMRFAITPGFFNSESFSAYLIDAFETLVAETFLPEENPNSVPKMMSIGLHCRVVGRPGRFQGLQKFVDHVQSRNEELLEQGGGEGGVWVATREEIANHWRATHPPPSK | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan
EC: 3.5.1.41
Subcellular Location: Cell membrane
Sequence Length: 522
Sequence Mass (Da): 58436
Location Topology: Lipid-anchor
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A0A8R2H819 | MREFKVVVLGSGGVGKSALTVQFVSGRFMEKYDPTIEDFYRKEIEVDSSPCVLEILDTAGTEQFASMRDLYIKNGQGFVVVYSLTNHQTFQDIKPMKELITRVKGSERVPILLVANKIDLEHQREVPTIEGNTLAQIWGCPFVEASAKNRTNVNEVFAEIVREMNFSNDKEKKSYCCCTVL | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
EC: 3.6.5.2
Subcellular Location: Endosome membrane
Sequence Length: 181
Sequence Mass (Da): 20484
Location Topology: Lipid-anchor
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A0A7E5V9E2 | MYICLFQMSGKRTRSYNCAVHHRDREVSSENDFHLLLEDPTLFARMVHLVAMEMLPEERDRKYYQERYTCCPPPFFIICVTLLELGVFAWYAWGAGGMAAAAGPVPVDSPLVYRSDRRRELWRFLTYSVVHAGWLHLAFNLLVQLAVGLPLEMVHGAVRCAAVYLAGVLGGSLAASVLDPDVCLAGASGGVYALLAAHLANALLNFHTMRYGAVRLVAALAVASCDVGFAVHARYTKEAPPVSYAAHVAGALAGLTIGLLVLKHAQQRLWERLLWWAALGAYAACTLFAVLYNVFSAPVDELHYLPPDPPPDAGF | Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
EC: 3.4.21.105
Subcellular Location: Membrane
Sequence Length: 315
Sequence Mass (Da): 34546
Location Topology: Multi-pass membrane protein
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A0A3L6KWU4 | MASLQTSKAAQTRPLWAFLTMIIATGIITEASNYAFKATSMKPYCDFSMEAKTGTAKLKARQQTAFAAYSNWQRLHRAFLLTSLKLPNSTKASEALMIYANIKAEAANTRLQGQITAGIPALAKANYIAGHIDDFVQALEAMVQTAGDHNNAHACLHGESSAVATSIPGCKATSFTSKTESAMNSLTDKLNGQTGALSASDIQTARNCAFTANHGGRFTTTAAAAGVTFGLGMFTTSTSELSTAAATKTKKLGSLSFVQTEIENLKKLDAATAAVETPPADFATVKEIIKAAANDPTMAEALRIVNKAEERKTGAELEKQLKAAFGESDKTGDTPFLTALKQTKAENRATKTQEDILTLTTEDLTAAISHKLQALLSQANAKPTCDSQLQAQNPEGLCNQIEEQTTCNRTENCHYNSTKDGKKCTLKKEVKEKLEKAKENNLTSNAVDCSKLLTQQACENANKDGKKHCGWRSGKDNDDEKDKVKCRDSSFLLNKQFALSVVSAAFIALLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 511
Sequence Mass (Da): 54857
Location Topology: Lipid-anchor
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A0A5S6RBM5 | MEWGIMERGEGIYREEGKERERRRGVMRRRRGARGGEEMGARRRDGRRDGRAGLEAARRRARSDGTGDATAGRGSRRRRHARRGSGMATATAQRRRRAARSDDGTRRRRCAVAWGARRRDGRQRRGARGDGTVARRRDGDGDGAAAAVTARGSDGSDGDGGAGLGAAGRAQQRWRLALLEESLKKVDTSDPFAICGIIDQYSQQPSLKEKSALNRLEIINKCFSKRTVEEIIASLEQEAPNVADEWVASAIQSLRKASPTSLKISLRSIREGRTQTVGECLRREYRMVCHVMRGDFSRDFFEGCRAILLDKDRNPKWMPPRLEEVHDEVVEKYFSKVDDPEWEDLDLPPRRSHGRRLVPKL | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+)
Sequence Length: 361
Sequence Mass (Da): 40720
|
A0A1X0L7T8 | MPYTIKQTIRLEMGHRTWTHDMRTSRGGSELYTPELVANKCANLHGHTIFVSVTLTGDSLDEQYFLLDTDLLENAFRPILDEVDHAFVVDRKDPLYEDIAAVARKGGLKLCTVDFSPTFEALVRHFYDRLQSVIEEKGLADQLRIKEMKVLGEQTVEATYCGE | 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: 163
Sequence Mass (Da): 18581
|
A0A944RT55 | MEWSAFFLSLCLSLISVTILLVLGLLIARSLAWKRFVGKGVIEALITLPLVLPPTVLGYFFLRFLGRESMLGDWFESWFHEPLVFSFTGLVLASVIYSLPFAVQPMLRSFESIPQSIREAAWCCGLSHWQTFWRIELPLAMKGVLTGCVLSFAHTMGEFGVVLMVGGNIPGETRTISIALFDKVQTFDEGAADSMALFMLLFSLVLLILINLVGDKHLQGLK | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 222
Sequence Mass (Da): 24708
Location Topology: Multi-pass membrane protein
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A0A1X0BJK2 | MAGLKFRTIDSLVGQLTLAGRDGRLMHLRMVDQTYEPSRDGWAADETAFPDAVEQLEAYFAGDRTEFELDLDLVGTDFQRRVWAALLTIPYGETRSYGEIARQIGSAGAFRAVGLANGHNPIGIIVPCHRVIGSNGSLTGYGGGLDRKRALLALEKSRVSSALTLFD | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 167
Sequence Mass (Da): 18160
|
A0A377WCK7 | MTILVSEEPVDPKLIDQTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKSLYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTRPEELTAEERKVITDLLWKEMREIYYGRNIPAV | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 187
Sequence Mass (Da): 21788
|
A0A078F280 | MSSKASSSRGGESIVADCGRNTSTCGYCKSPTSSSISHGLWTERLTVHDYQALLDRGWRRSGCYLYKPEMAKTCCPSYTIRLRANDFVPSKEQQRVRRRLERFLDGELDLKPRERAEDQDVEVSEPVRKLLGSGKREQNNEVEPVMKDLSEQIDNAVQRCIQSGEFPSNIQIPKSSVKKVLSAKRKKLAEGSEELLYTSNIAFPIVAAIKQTQTSHKGEGSNSAETVSEKLLSEMNKVGEFPGLAVKVCKGHINFFSATQVTSSERDQGESLPSATTTTKSCSTNLQVRKKKLEIHLKRSSFDPEEYELYKRYQLRVHNDEPESISKTSYKRFLVDTPLIEVLPSSDGDDDDENVPPCGFGSYHQQYRVDGRLIAVGVIDILPKCLSSKYLFWDPDFASLSLGNYSALQEIDWVKQNQAHCSALEYYYLGYYIHSCNKMRYKAAYRPSELLCPLRYQWVPFEVAKPLLDKKRYSVLSDFTKASLSPAPQASETLVKSTREREDMEMNNSDEDSDSDSGVNGNDIANILISLNGARLRYKDLLRIINMAVRKQLEPMFISYRKVVGAELSERMVYELQ | Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
EC: 2.3.2.8
Catalytic Activity: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg)
Sequence Length: 577
Sequence Mass (Da): 65362
|
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