ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
P46479 | FTTQETITNANTAKQWFLKSAKDSKFVANHFVALSTNAKLVQEFGIDKANMFEFWDWVGGRYSLWSAIGMSIALNIGFENFEHLLSGAHWMDNHFKSTPIERNIPVILAVLGIWYGNFYGAETQALLPYDQYMHRFAAYFQQGDMESNGKYVVRAGDKVNYSTGPIVWGEPGTNGQHAFYQLIHQVPHHPCDFNSPVKSHNSELRDGLHHTILLSNFLAQTEALMKGKDRQTVEKELKAAGKSEDEIKSIGPHKEFTGNRPTNSIMVDTVTPFTLGAMIAMYEHKIFTQGIIWDINSYDQWGVE | Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 34460
Sequence Length: 304
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q9PMD4 | MLNNTLFFKQSEIHTISSYANRINDEVKSGDIGYYHLIDTSLNLIDESLQFIQDKEYVKNIVLVGMGGSSCGVKALRDMLFNEKSNQRELFILDNTSSHSFNKTLEKIKLEESLFLIISKTGSTIEVVSLFKLLIEHFKLDMQELKKYFVFITDKDSKLHQEGENLGIKCFFIPANVGGRFSILSAVGIVPLCFCGYNAKALLEGAKACFEDFFTHKKDEILQKAYHYCTHKNANINVLFSYSDAFKGFNEWYIQLIAESLGKKQGYKRIGLTPIALIGARDQHSFLQLIMDGPKNKTVTFLKIKDAQKAPIIPDIHFKFLDSLSNKVNLHELLNAQCDATMHALIAENLSVDVIELEKLDAWHAGYLMYYYELFTSTCGVMLGINTYDQPGVEVGKLILKNILNS | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 46013
Sequence Length: 406
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q3AFH3 | MALKIDFNNVFHPYLQKERLGEADIDGYKEKFTSALVSLREKKEKGELGFFHLPYLPEEEIAEIEKTAREVREKFKYFVVLGIGGSALGPLAVHTALNNLRYNELSEELRGGPKFYVEDNIDPERMASLLKVIEPEKTVFNVITKSGATAETLSQLLIVTEVLKKKVGKRFTEHLIFTTDPEKGSLRALARELGVKTFAIPPNVGGRFSELTPVGLLPAAVTGINIRELLAGAREMAERCERENLWENPAGLAAAIHVLLLERGKNMAVMMPYADSLKYMADWYAQLLGESIGKRLNRRGEEVFVGQTPVKALGVTDQHSQVQLYTEGPFDKLLIFLEVERYRNRVVIPPDFPQYAELKFLGGHTLNELIIAEKKATEFALLKARRPNYTVIFPEVNPYTVGELLYFLEAKIAFMGEYLDINAFDQPGVEEGKKATYALLGREGFEEKRQEVLKVKKEPRFILE | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 52456
Sequence Length: 464
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q9ABK5 | MADLDAAWTRLEAAAKAAGDKRIVEFFDAEPGRLDALTLDVAGLHLDLSKQAWDEAGLEAALDLAHAADVEGARARMFDGEAINSSEGRAVLHTALRAPAGADVKALGQPVMAEVDAVRQRMKAFAQAVRSGAIKGATGKPFKAILHIGIGGSDLGPRLLWDALRPVKPSIDLRFVANVDGAEFALTTADMDPEETLVMVVSKTFTTQETMANAGAARAWLVAALGEQGANQHLAAISTALDKTAAFGVPDDRVFGFWDWVGGRYSLWSSVSLSVAVAAGWDAFQGFLDGGAAMDEHFRTAPLEQNAPVLVALAQIFNRNGLDRRARSVVPYSHRLRRLAAFLQQLEMESNGKSVGPDGQPAKRGTATVVFGDEGTNVQHAYFQCMHQGTDITPMELIGVAKSDEGPAGMHEKLLSNLLAQAEAFMVGRTTDDVVAELTAKGVSDAEIATLAPQRTFAGNRPSTLVLLDRLTPQTFGALIALYEHKTFVEGVIWGINSFDQWGVELGKVMANRILPELESGASGQHDPSTAGLIQRLKR | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 57526
Sequence Length: 539
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q9RDY2 | MIRNSMKSHTELLSWNLLQKEADRVRLNSDSLTCVVPDSNNYESSKQINCIEYDYSRQRVNRTIIDLLIDLANEVKLQEKIDNLINGKKINISENRPALHTALRDLGNKSIMIDGLDIMSAVINTREKIKVISNQIREKKWLGHSGLPITDIVNIGIGGSDLGPRVCINALSNYISKEFNYHFISDVDPASFNDVIAKINPQTTLFIVSSKSFTTKETLLNARKAFALYEDTASIDQHFIAVTAHPERAYQMGIKTVLPIWDWVGGRFSFCSAVNLITAIAIGYEQFVELLAGAHDIDTHVQFTDFKNNIPVLMALIGIWNNNFLNIHYDLIGYNFKEYFVPYVQQLDMESNGKSIDVNGRMVDYATGPIVWGGLGNQAQHSYFQLLCQGTHRCVGDFITLKTNDEHEINSMCHYKMKVLSEGIQTIENPYGYIPGNMPMNHLILSDCSPYTLGALVALYEHKIFEQSVIWNINPFDQPGIESAKSAHREITLSSES | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 56092
Sequence Length: 497
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
B1Y2Y7 | MNTPRCDQTAAWAALAAHHQGAGRQFDLRTAFGADAGRFDAFSLQAPEVFADLSKNHWDATTRGLLLGLARQCQIESRRDAMLAGEPINHTEGRAVLHTALRAPRGAAPFSDDVHGVLDAMLAYVEQVRDTATSGIKHVVNIGIGGSDLGPQMVVPALDAYAQRGLQLHFVSNVDGHDIAPVLRDLNPRETLVIVASKTFTTQETMANAQVARTWFLAGYGEGGEAAIAKHFAASTTNVAAAAKFGITTTFGFWDWVGGRYSLWSAIGLPIALAVGAENFRALLAGAHAMDRHFATAPLESNLPIQLGLLDVWYRNFLGYTSRSIAPYHQGLRRLPAYLQQLEMESNGKCVDLDGASLPYGTCPVVWGEAGTNGQHAYFQMLHQGTDVIPVEFIAVKTPNHGPDVADELKAGLADQHVKLLANCLAQSQALMLGKTTDDALTDKAPTASTALDALTVARHRTFPGNRPSSTLVLDRLSPASLGALIALYEHRVYTSGALWGINSFDQWGVELGKALCNQLLPRFASGESAGLDASTAGLLARLRG | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 58306
Sequence Length: 545
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q72MT7 | MIRLETRFASSFIQSSKLEPFLEKSESARLTLHSSQGQGKEYLGWLYLPKELKNSEIERMTQVAERLRNSSEVIVVIGIGGSYLGSRAVLEATLPFFKKPSIGNPEIIFAGHHLESRYFSELIEYLEDKNFSINVISKSGTTTEPAIAFRLLWELLRKKYGSSASSRVVATTDSSKGVLKKFADSEKLDTFTIPDNVGGRYSVLTPVGLFPLAVAGISISKFILGFQNILNDIHSITDPTRNPATYYSALRNYFLSEGRYIEVLANFNPSLRYVSEWWKQLFGESEGKENKGIFPASMDFTTDLHSLGQYIQEGKRILFETVLSPSEVCSNLTLKPTQDNLDSLNFLSGNTLGYVNEQARLGTLLAHADGGVPCLELVFPDISPQSLGELMYFFEYSCAISGYSLGVNPFDQPGVEAYKKNMFALLNKPGFEQEGETLRKRISRN | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 49735
Sequence Length: 445
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
A5VIL5 | MTHIKFDSSALKQFVHENELGEMQAMVNAANDELRNGTGAGADFRDWLHLPTEYDKEEFARIKKAADKIQRDSDVLVVIGIGGSYLGAQMAIDFLHNTFYQAQNAKDRKAPLVVFAGNSLSSTYVHDLIQLIGDKDFSINVVSKSGTTTEPSIAFRIFKGLLIKKYGENEANKRIYATTDKTKGALKTEADAHGYETFVIPDGVGGRYSVLSAVGLLPIAASGADIDKLMEGAAQAEKDYVDPDLTKNEAYQYAAYRNILYRKGYETELLENYEPNMRMFAEWWKQLAGESEGKDQKGIYPSSANFTTDLHSLGQYIQEGRRFLMETVVKLDKPNYDMEIPTEPDNLDGLGYLEGKTMDYVNTKAYEAVVAAHTDGGVPVMTVHIPQEDEYTLGYLIYFFEVAMGISGYLNGINPFNQPGVEAYKTNMFGLLGKPGYEEIGKELRAKMDKND | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 50351
Sequence Length: 452
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q1GTU1 | MTIASDAWQALADWQPQKLTDLVAADPDARLQALVRNVADIRFDFAKTHLDAAAIAILANLAEAQDFGGRRKTLFSGGIANPTENRAAEHSAERGDGAPESVHAAQALHQRMRMMIDAIEAGAFGEIRHLLHIGIGGSALGPDLLVDALGRHSDRYDVAVVSNVDGAALDEAFAKFSPEHTLVAVASKTFTTTETLLNANSALQWLDEAGVADPVGRFIALTANPGRAMEWGIDETRILPFSETVGGRYSLWSSIGFPAALALGWDAFADLLEGAAEMDRHFRLADGADNICLLAAFADQVYANRLGCQTRAVFAYDERLRLLPAYLQQLEMESNGKSVTLDGAPLAQHSAPVTWGGVGTDAQHAVFQLLHQGTHLVPVEFIVAREPDHLLDDAHHETLVANCIAQGAALMAGRASDDRARAYPGDRPSTTILLDQVSPRSLGALIAFYEHRVFANAVLLGVNPFDQFGVELGKEMAKGLAEGTVDFDPATQALMKAALGD | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 53610
Sequence Length: 501
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q2FZU0 | MTHIQLDFSKTLEFFGEHELKQQQEIVKSIHKTIHEGTGAGSDFLGWIDLPVDYDKEEFSRIVEASKRIKENSDVLVVIGIGGSYLGARAAIEMLTSSFRNSNEYPEIVFVGNHLSSTYTKELVDYLADKDFSVNVISKSGTTTEPAVAFRLFKQLVEERYGKEEAQKRIFATTDKEKGALKQLATNEGYETFIVPDDVGGRYSVLTAVGLLPIATAGINIEAMMIGAAKAREELSSDKLEENIAYQYATIRNILYAKGYTTEMLINYEPSMQYFNEWWKQLFGESEGKDFKGIYPSSANYTTDLHSLGQYVQEGRRFLFETVVKVNHPKYDITIEKDSDDLDGLNYLAGKTIDEVNTKAFEGTLLAHTDGGVPNMVVNIPQLDEETFGYVVYFFELACAMSGYQLGVNPFNQPGVEAYKQNMFALLGKPGFEDLKKELEERL | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 49822
Sequence Length: 443
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
A0R4Q0 | MPAPSAADFARLRSLVAIEDLDARQSRPIEEVFTGRELTTIPVGTAEDVAAAFAKARAAQRGWAHRPVAERAAIMERFRDLVAKNRDFLMDVAQAETGKARSAAQEEIVDMMLNARYYARQAVKLLAPKRVQGLLPGVVKTVVNHHPKGVVGVISPWNYPMALSISDSIPALLAGNAVVVKPDSQTPYCTLANAELLYEAGLPRDLFAVVPGPGSVVGTAIVENCDYLMFTGSTATGRTLAEQCGRRLIGFSAELGGKNPMIVTRGAKLDVAAKAATRACFSNAGQLCISIERIYVERAVADEFTAKFGEQVRSMRLAATYDFTADMGSLISEDQIKTVSGHVDDAKAKGATVIAGGNIRPDIGPRFYEPTVLTGVTDEMECARNETFGPVVSIYPVESVAEAIEKANDTEYGLNASVWAGSKTEGEAIAAQLQAGTVNVDEGYALAFGSTAAPMGGMKASGVGRRHGADGILKYTESQTVATSRVLNLDPPLGISGTLWQKAMTPMIRAVQKLPGR | Function: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Although it has succinate semialdehyde dehydrogenase activity, is likely to act physiologically on a different aldehyde(s) (By similarity).
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 54992
Sequence Length: 517
EC: 1.2.1.79
|
P94428 | MPDQLTVYNPATGEEIKTIPQQSATEVEEAIERSHQAFKTWSKTSANERTSLLKKWYELIVEHKEELADLITKENGKPYQEAVGEVLYGAGYIEWFAEEAKRVYGRTVPAPTTGKRIVVTRQPVGPVAAITPWNFPNAMITRKAAPALAAGCTFIIKPAPDTPLSAYELARLAYEAGIPKDVLQVVIGDGEEIGNVFTSSPKIRKITFTGSTPVGKILMKNSADTVKHVSMELGGHAPLIVDEDADIDLAVEQAMASKYRNAGQTCVCANRLIVHESIKDEFAAKLSEQVSKLKVGNGLEEGVNVGPIINKRGFEKIVSQIDDAVEKGAKVIAGGTYDRNDDKGCYFVNPTVLTDVDTSMNIMHEETFGPVAPIVTFSDIDEAIQLANDTPYGLAAYFFTENYRRGIYISENLEYGIIGWNDGGPSAVQAPFGGMKESGIGREGGSEGIEPYLETKYLSIGL | Function: Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 50262
Sequence Length: 462
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 1.2.1.79
|
O32507 | MTATPQASARPERPFATVNPYTGETVKTFPFLESAEIPALIERADQAYREWGQRPVTERAAIMRRAAELMLERTDELASLITLEMGKLLREAKGEVALAASILNYYGEQGPSFLEPKTIPVPQGEAAVLHAPLGVLLGIEPWNYPLYQVVRFAAPNLVVGNTVLLKHSELCPQSALALEQLFHDAGVPQGAYTNLFLRIADIEQVIAHPAVQGVSLTGSERAGASVAELAGRHLKKCVLELGGSDPFIVLDAEDLDTTVKAAATGRLSNTGQACIAAKRLMVVDDLYDEFVSRLGQTFSAFVPGDPADPSTRLGPLSSEQAARDLQAQVQDAIDKGATVVAGGQRPEHPGAFVQPTVLTDVTPDMRAYHEELFGPVAVVYRVRDEDEAVALANASTYGLGGAVFSSDLDRAQRVAERLDTGMVWINHPTSSAADLPFGGVKRSGFGRELSSMGMLEFTNQKLVRAFPTKQKPAQVAG | Function: Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 51240
Sequence Length: 477
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 1.2.1.79
|
P25526 | MKLNDSNLFRQQALINGEWLDANNGEAIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERATILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGVPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDNGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL | Function: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate . Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth . Also catalyzes the conversion of glutarate semialdehyde to glutarate, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate .
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 51720
Sequence Length: 482
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 1.2.1.79
|
P55653 | MTLTSALTRHLKCPELFRNLANEPHPSVAGQRQRFSVFNPSTGELLAEVPDMGAADAHAAIERADAAQEPWSGLTARARSDILWKWHRFILEHSDDLAAILTAEMGKPLGEAKSEVQHAAAYLQWYAEEANRIYGETISAPSTDRRMLVIKQPIGVVGAITPWNFPASMVARKISPALAAGCTVVLKPAEQTPLVAGAMFALAKLAGFPDGVLNLVYASEGDAIGRELCTNPKVRKISFTGSTEVGRLLMRQCSDQIKRISFELGGNAPFIVFDDADIDAAVDGAIQAKFRNAGQTCVSANRIYVQSGVYAEFAEKFTERVRTLKVGDGFDPNVAIGPLINQEALKKIELHISDAVQKGARVRSGGRRTGSSGTFFEPTVVTDVSKTMRLAEEETFGPLAPLLRFDDADHVVREANDTIYGLAAYFYASNLKRVWRVAEALEYGMVGINTGRMSSEAAPFGGVKQSGIGREGSRHGLEDYLDMKYLCVGGL | Function: Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 53254
Sequence Length: 491
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 1.2.1.79
|
Q55585 | MAIATINPATGQTVQTFIAHSQVEVNAKLDLAQETFQSFRHLPFAQRGQWLRKAADILEQRRDEWAALMTLEMGKSIPQAIAEVNKCALVCRFYADKAEEYLADEVVTTDASQSFIAYQPLGVILAVMPWNFPFWQVFRFAAPALMAGNVGLLKHASNVPQCALAIAEIFQTAGFPEGAFQTLLIGGKVASELMADDRIQAGTLTGSEPAGASFASAAAGQIKKTVLELGGSDPFIVLEDADLDQALKVAVPARMQNNGQSCIAAKRFIVQASVAEEFFQRLTKAFQALKVGDPSLSTTDIGPLATPDILADIVAQVEQTIAAGAHCRCGGQALDQPGNYYPPTLLTDVPPNAPTYRQEFFGPVALGFTVDNLEEAIALANDIPFGLGASAWTTNPENQQKLIRGIEAGAVFINGMTKSDPRIPFGGIKRSGFGRELGRMGILEFVNAKTVWIA | Function: Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.
Catalytic Activity: H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
Sequence Mass (Da): 48749
Sequence Length: 454
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 1.2.1.79
|
Q1RMI3 | MSLVDLGKKLLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNPESPDTVTIHAATPQFIIGPGGVVNLTDETGVSAVQFGNSSTSVLATLAALAEASAPLSNSSETPVVATEEVVTAESVDGAIQQVVSSGGQQVITIVTDGIQLGNLHSIPTSGIGQPIIVTMPDGQQVLTVPATDIAEETVISEEPPAKRQCIEIIENRVESAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV | Function: Transcription factor capable of interacting with purine rich repeats (GA repeats). Acts as a a master regulator of nuclear-encoded mitochondrial genes.
PTM: Acetylated by EP300/p300. Deacetylated by SIRT7, promoting heterotetramerization and activity.
Sequence Mass (Da): 41321
Sequence Length: 383
Subcellular Location: Nucleus
|
Q06547 | MSLVDLGKKLLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNPESPDTVTIHAATPQFIIGPGGVVNLTGLVSSENSSKATDETGVSAVQFGNSSTSVLATLAALAEASAPLSNSSETPVVATEEVVTAESVDGAIQQVVSSGGQQVITIVTDGIQLGNLHSIPTSGIGQPIIVTMPDGQQVLTVPATDIAEETVISEEPPAKRQCIEIIENRVESAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV | Function: Transcription factor capable of interacting with purine rich repeats (GA repeats) . Acts as a a master regulator of nuclear-encoded mitochondrial genes (By similarity).
PTM: Acetylated by EP300/p300. Deacetylated by SIRT7, promoting heterotetramerization and activity.
Sequence Mass (Da): 42483
Sequence Length: 395
Subcellular Location: Nucleus
|
Q6L1T2 | METIKSVDIYELGSPGEKSSPWSSTILIVKLTSSNGNIGYGEAPTTFMTLPVKESMREVERVFKDQNYFNIEKNMREFYKHSFYLSRSMEATSALSAFEIASWDLIGKDLGTPVYNLLGGEYNSELRAYANGWYSDCLEPDDFVSRAKEYIKKGYTAFKFDPFRNNFDRIGNDGIKKAVDIVSAMRSELGENIDLLIECHGRFSTKYAIKVGQALDEFNPLFIEEPIHPEMELGLFDFKRYVNTPVALGERLLNKEDFARYISQGMVDIVQADLTNSKGILEAKKISAIVESFGGLMAFHNAFGPVQTAATLNVDYTLTNFLIQESFEDSWPDWKRNLFSGYRIENGHFKLSGKPGLGITADEKLMEKLIYDGMEEFNKNEPSWVVSGTYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in the degradation of glucose and galactose via the nonphosphorylative variant of Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is also able to catalyze the dehydration of galactonate to produce 2-keto-3-deoxygalactonate (KDGal).
Catalytic Activity: D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 44345
Sequence Length: 391
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 4.2.1.140
|
Q97U27 | MRIREIEPIVLTSKEKGSATWASIMIVTRVITENGEVGYGEAVPTLRVISVYNAIKQVSKAYIGKEVEEVEKNYHEWYKQDFYLARSFESATAVSAIDIASWDIIGKELGAPIHKLLGGKTRDRVPVYANGWYQDCVTPEEFAEKAKDVVKMGYKALKFDPFGPYYDWIDERGLREAEERVKAVREAVGDNVDILIEHHGRFNANSAIMIAKRLEKYNPGFMEEPVHHEDVIGLRKYKASTHLRVALGERLISEKETAFYVEEGLVNILQPDLTNIGGVTVGRSVIKIAEANDVEVAFHNAFGSIQNAVEIQLSAVTQNLYLLENFYDWFPQWKRDLVYNETPVEGGHVKVPYKPGLGVSINEKIIEQLRAEPIPLDVIEEPVWVVKGTWKNYGV | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also use divalent metal ions such as Co(2+), Mn(2+) and Ni(2+).
Function: Involved in the degradation of glucose and galactose via the branched variant of the Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is also able to catalyze the dehydration of galactonate to produce 2-keto-3-deoxygalactonate (KDGal).
Catalytic Activity: D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 44729
Sequence Length: 395
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 4.2.1.140
|
Q704D2 | MASAMASSALREATCTMTRLAADVAASVSSIFSCKDSAGPRPVVPATKTTSTPLDVMFFTWFAKSSGSSLPPLKVVMTGATISIDSTRGALKKLARKGIKGWLNQYMATIKEIEPIVLYEQETDARWASYSILVRVVTSDGRVSYGEAVPTLRILPVVSAVRQTARAFLGRDPHEISAAFYEWYRQDFFLSRSFESATALSAIDMALWDLKARELGAPLYELLGGKLRDRVKVYANGWYGGCRDPQCFAEKAKEVVARGYDALKFDPFGPSFNSITSEELRRAEEAVAAVRDAVGDDVDILIEHHGRFNANAAVEIAKRFEPYRPYFMEEPLHHEDIEGYRKYRSLTSARIAMGERLISAKEALQYLVEGLVDVIQPDACNIGGVTGSMKVAALAEAFSVEVSYHNAYGPVQFALEVQLSAVTPTLYRLESFYDYWPQWKRDLIGDPFRLSQSSVEVPRGPGIGVAVNERVLEKYRAEPSEIPVGEEPVWVVRGTWR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is not able to use D-galactonate as substrate.
Catalytic Activity: D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 55119
Sequence Length: 497
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 4.2.1.39
|
Q9M0B6 | MPSIEDELFPSTPGKFKIDRSNRQLHRCFASTSTMFLWALFLIALTASYLSFQSFVDSGSRYLTASWGGIQWEKQVRTSAQIHRSGGISVLVTGATGFVGSHVSLALRKRGDGVVGLDNFNNYYDPSLKRARRSLLSSRGIFVVEGDLNDAKLLAKLFDVVAFTHVMHLAAQAGVRYALENPQSYVHSNIAGLVNLLEICKAANPQPAIVWASSSSVYGLNEKVPFSESDRTDQPASLYAATKKAGEEITHTYNHIYGLAITGLRFFTVYGPWGRPDMAYFSFTRNILQGKPITIYRGKNRVDLARDFTYIDDIVKGCLGSLDSSGKSTGSGGKKRGAAPYRIFNLGNTSPVTVPILVDILEKHLKVKAKRNFVEMPGNGDVPFTHANISSARNEFGYKPTTDLETGLKKFVRWYLSYYGYNTKAKLVH | Function: UDP-D-glucuronate 4-epimerase involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Catalytic Activity: UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47458
Sequence Length: 429
Subcellular Location: Golgi apparatus
EC: 5.1.3.6
|
O22141 | MSRLDDIPSSPGKFKMEKSSYLHRLRFQSSLTKFAFFSFFLLCLISLLFLRSPPSINPSSPSDPSRRSLRTNTYGGPAWEKRLRSSARIRTSTNNGITVLVTGAAGFVGTHVSAALKRRGDGVIGLDNFNDYYDPSLKRARRALLERSGIFIVEGDINDVELLRKLFKIVSFTHVMHLAAQAGVRYAMENPSSYVHSNIAGFVNLLEICKSVNPQPAIVWASSSSVYGLNTKVPFSEKDKTDQPASLYAATKKAGEEIAHTYNHIYGLSLTGLRFFTVYGPWGRPDMAYFFFTKDILKGKSISIFESANHGTVARDFTYIDDIVKGCLAALDTAEKSTGSGGKKRGPAQLRVFNLGNTSPVPVSDLVRILERQLKVKAKKNLIKMPRNGDVPFTHANISLAQRELGYKPTTDLQTGLKKFVRWYLSYYSGDKKAAAR | Function: Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Catalytic Activity: UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48536
Sequence Length: 437
Subcellular Location: Golgi apparatus
EC: 5.1.3.6
|
Q9STI6 | MSHLDDLPSTPGKYKTDKVPPYGILHHHRYLRLSKLTLWASLFLALFLFYLVLSPPPSPSRRNLNDSSSISAAKYGGSHWEKQVRKSARPRSHGGLTVLVTGASGFVGTHVSIALRRRGDGVLGLDNFNRYYDPKLKRARQGLLERSGVFVVEGDINDAVLLRKLFDVVLFTHVMHLAAQAGVRYAMQNPGSYVNSNIAGFVNLLEVSKSANPQPAIVWASSSSVYGLNSKVPFSEKDRTDQPASLYAATKKAGEGIAHTYNHIYGLSLTGLRFFTVYGPWGRPDMAYFFFTKDILKGKTITVFESPDKGSVARDFTYIDDIVKGCLGALDTAEKSTGSGGKKKGPAMFRIYNLGNTSPVPVTKLVTILEKLLKMKAKKKIMPLPRNGDVEFTHANITLAQAELGYKPAVDLETGLKKFVKWYMGFYTGSKKKSSW | Function: Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Catalytic Activity: UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48165
Sequence Length: 436
Subcellular Location: Golgi apparatus
EC: 5.1.3.6
|
Q9LIS3 | MPLSATADTSKTVKLERYNSYLRKIHSTKVLNASSKVLFRATLLVALVLVLIFAINYPPLSDSRAAAAHHLHRRSFLSTGLFSSSSSSSSIGGAAWEKRVRQSSTAKRPHGLSVLVTGAAGFVGSHCSLALRKRGDGVLGFDNFNDYYDPSLKRARQELLEKQQVFIVEGDLNDGPLLRKLFDVVPFTHILHLAAQAGVRYAMKNPQSYIASNIAGFVNLLEVAKAANPQPAIVWASSSSVYGLNTENPFSEEHRTDQPASLYAATKKAGEEIAHTYNHIYGLSLTGLRFFTVYGPWGRPDMAYFFFTKDILHGKSIDIYRTQDNQEVARDFTYIDDIVKGCVGALDTAEKSTGSGGKKRGQAQLRVYNLGNTSPVPVGRLVSILEGLLGTKAKKHLIKMPRNGDVPYTHANVSLAYKDFGYKPTTDLAAGLRKFVKWYVGYYGIQPRVKKETSHAEDSA | Function: Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Catalytic Activity: UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50570
Sequence Length: 460
Subcellular Location: Golgi apparatus
EC: 5.1.3.6
|
J8H9C1 | MKFSNITIKNFRNFEKVNINLDNKNVIFGMNDIGKTNFLYALRFLLDKEIRKFGFNKSDYHKHDTSKKIEIILTLDLSNYEKDEDTKKLISVVKGARTSANADVFYIALESKYDDKELYGNIILKWGSELDNLIDIPGRGNINALDNVFKVIYINPLVDLDKLFAQNKKYIFEESQGNESDEGILNNIKSLTDQVNQQIGEMTIIKGFQQEITSEYRSLKKEEVSIELKSEMAIKGFFSDIIPYIKKDGDSNYYPTSGDGRRKMLSYSIYNYLAKKKYEDKIVIYLIEEPEISLHRSMQIALSKQLFEQSTYKYFFLSTHSPELLYEMDNTRLIRVHSTEKVVCSSHMYNVEEAYGSVKKKLNKALSSALFAERVLLIEGPSEKILFEKVLDEVEPEYELNGGFLLEVGGTYFNHYVCTLNDLGITHIIKTDNDLKSKKGKKGVYELLGLNRCLNLLGRENLDEITIDIPEDIKGKKKKERLNERKKEIFKQYKNEVGEFLGERIYLSEIDLENDLYSAIGESMKRIFENEDPVHYLQKSKLFNMVELVNNLSTKDCFDVFEHEKFACLKELVGSDRG | Cofactor: Rapid, sequence-specific cleavage at physiological concentrations of Mg(2+) (4-5 mM) or Mn(2+) (15 uM). In presence of >20 uM Mn(2+) has rapid non-specific cleavage activity.
Function: Component of antiviral defense system Gabija type I, composed of GajA and GajB. Expression of Gabija type I in B.subtilis (strain BEST7003) confers resistance to phages phi105, phi29, rho14, SpBeta and SBSphiC . An endonuclease that nicks double-stranded DNA within the sequence 5'-TNNNCGGGNNA-3' in the absence of nucleotides (NTP, dNTP and NDPs), cleaving after C-1. Has no detected ATPase activity. Expression of Gabija type I in E.coli B (strain ATCC 11303) confers resistance to phage T7 . It is thought that this enzyme is strongly suppressed during physiological growth (in E.coli total nucleotide concentration is over 8.7 mM in mid-log phase), but during viral replication, when nucleotides are rapidly consumed, it is de-suppressed and degrades target DNA (Probable).
Sequence Mass (Da): 66986
Sequence Length: 578
Domain: The N-terminal ATPase-like domain seems to have lost ATPase activity, but may still bind nucleotides (Probable). The C-terminal Toprim (topoisomerase/primase) domain probably has the endonuclease activity, but when expressed alone (residues 348-578) has not activity, showing it requires the N-terminal ATPase-like domain for function .
EC: 3.1.-.-
|
Q7LDI9 | MGQTKSKIKSKYASYLSFIKILLKRGGVKVSTKNLIKLFQIIEQFCPWFPEQGTLDLKDWKRIGKELKQAGRKGNIIPLTVWNDWAIIKAALEPFQTEEDSVSVSDAPGSCIIDCNENTRKKSQKETEGLHCEYVAEPVMAQSTQNVDYNQLQEVIYPETLKLEGKGPELVGPSESKPRGTSPLPAGQVPVTLQPQKQVKENKTQPPVAYQYWPPAELQYRPPPESQYGYPGMPPAPQGRAPYPQPPTRRLNPTAPPSRQGSKLHEIIDKSRKEGDTEAWQFPVTLEPMPPGEGAQEGEPPTVEARYKSFSIKKLKDMKEGVKQYGPNSPYMRTLLDSIAHGHRLIPYDWEILAKSSLSPSQFLQFKTWWIDGVQEQVRRNRAANPPVNIDADQLLGIGQNWSTISQQALMQNEAIEQVRAICLRAWEKIQDPGSTCPSFNTVRQGSKEPYPDFVARLQDVAQKSIADEKARKVIVELMAYENANPECQSAIKPLKGKVPAGSDVISEYVKACDGIGGAMHKAMLMAQAITGVVLGGQVRTFGRKCYNCGQIGHLKKNCPVLNKQNITIQATTTGREPPDLCPRCKKGKHWASQCRSKFDKNGQPLSGNEQRGQPQAPQQTGAFPIQPFVPQGFQGQQPPLSQVFQGISQLPQYNNCPPPQAAVQQ | Function: The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution.
PTM: Myristoylation is essential for retroviral assembly. Alteration of the glycine residue leads to a block in the budding of particles and an accumulation of Gag inside the cell (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 74079
Sequence Length: 666
Domain: HERV-K Gag polyprotein contains regions homologous to the matrix (MA), capsid (CA) and nucleocapsid (NC) proteins from infectious retroviruses. Evidence suggests that HERV-K(HML-2) Gag polyprotein can be cleaved into mature MA, CA and NC under certain circumstances. However, the exact boundaries as well as the size of processed Gag proteins have not been precisely determined yet.
Subcellular Location: Cell membrane
|
A5U003 | MTVSYGAPGRVNLIGEHTDYNLGFALPIALPRRTVVTFTPEHTGAITARSDRADGSARIPLDTTPGQVTGWAAYAAGAIWALRGAGHPVPGGAMSITSDVEIGSGLSSSAALIGAVLGAVGAATGTRIDRLERARLAQRAENDYVGAPTGLLDHLAALFGAPKTALLIDFRDITVRPVAFDPDACDVVLLLMDSRARHCHAGGEYALRRASCERAAADLGVSSLRAVQDRGLAALGAIADPIDARRARHVLTENQRVLDFAAALADSDFTAAGQLLTASHESMREDFAITTERIDLIAESAVRAGALGARMTGGGFGGAVIALVPADRARDVADTVRRAAVTAGYDEPAVSRTYAAPGAAECR | Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
Sequence Mass (Da): 37572
Sequence Length: 363
Pathway: Carbohydrate metabolism; galactose metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.1.6
|
Q9HHB6 | MSKITVKSPGRVNLIGEHTDYTYGYVMPMAIDLYTIITAEKYDKVQLYSEHFNEEKTFTLDNLTKEGSWIDYVKGVLWVLIQEGYKIGGLKGKITGDLPLGAGLSSSASFEVGILEVLNQLYNLNIDPLKKALLAKKAENEFVGVPCGILDQFAVVFGKKDNVIFLDTQTLQYEYIPFPKDVSVLVFYTGVKRELASSEYAERKRIAEESLRILGKESSKEVTEKDLGKLPPLHRKFFSYIVRENARVLEVRDALKEGDIEKVGKILTTAHWDLAENYRVSCEELDFFVKKAMELGAYGARLTGAGFGGSAIALVDKDKAKTIGDAILREYLAKFSWKAKYFVVKPSDGVGV | Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). Is very specific for its substrate, since it is not able to use D-glucose, D-fructose, D-mannose, 2-deoxy-D-glucose, and D-glucosamine as substrates.
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
Sequence Mass (Da): 39375
Sequence Length: 352
Pathway: Carbohydrate metabolism; galactose metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.1.6
|
A7NI09 | MLDTGTLRARFQQHYGIHPSVIVRAPGRVNLIGEHTDYNDGFVFPVAIDRATYVAARLRHDQLVRVASSDLNEEDTFAIDQIERSNRPWHNYIRGVALALRVAGHPLLGADLLIASDVPRGAGLSSSAALEVAVGYAFQVLNNLNILGEELALLAQGAENNFVGVQCGIMDQLIAVLGRADHALLIDCRDLSYRAVPLPPSVAVVICDSHIPRTLAASAYNQRRQECDMAVQLLRRWYPGIRALRDVSEDHLAAHSDALPEPIRSRARHVVRENRRTLQGAEALERGDVVTFGRLMNESHASLRDDYQVSLPDIDILVETAHHLAGCYGSRLTGAGFGGCTVSLVERNEVESFSRDLLRVYHNATGRTATIYVCRASDGVGRATDNAGPQE | Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
Sequence Mass (Da): 42820
Sequence Length: 391
Pathway: Carbohydrate metabolism; galactose metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.1.6
|
A5UZX0 | MLDTGELRERFQQHYGIHPHVIVRAPGRVNLIGEHTDYNDGFVFPVAIDRATCVAARPRTDRIVRVMAADLHDEDLFSIDQIERSNRAWHNYIRGVVLALRTAGHTLSGADMLIASDVPRGAGLSSSAALEVAVAYTFQVLNRLNILGEELALLAQGAENTFVGVQCGIMDQLIAVFGRADHALLIDCRDLTYRAVPLPPSVAVVVCDSHIARTLAASAYNQRRQECDAAVRALQQWYPGIRALRDVSEDQLAAHQHELPEPLRARARHVVSENRRALQGAAALEAGDIATFGRLMNESHASLRDDYQVSLPDIDFLVTTAQSLAGCYGSRLTGAGFGGCTVSLVERSSVETFRHDLAQAYHDATGRTATIYVCRASDGVGRVMDNARPQE | Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
Sequence Mass (Da): 42730
Sequence Length: 391
Pathway: Carbohydrate metabolism; galactose metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.1.6
|
O43603 | MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQPCILEPCPGPSWQGPKAGDSILTVDVA | Function: Receptor for the hormone galanin and GALP. Receptor for the hormone spexin-1 . The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41700
Sequence Length: 387
Subcellular Location: Cell membrane
|
O08726 | MNGSGSQGAENTSQEGGSGGWQPEAVLVPLFFALIFLVGTVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLRYLWRTVDPVTAGSGSQRAKRKVTRMIIIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRPAPRRASGRVSILAPGNHSGSMLEQESTDLTQVSEAAGPLVPPPALPNCTASSRTLDPAC | Function: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40676
Sequence Length: 372
Subcellular Location: Cell membrane
|
O60755 | MADAQNISLDSPGSVGAVAVPVVFALIFLLGTVGNGLVLAVLLQPGPSAWQEPGSTTDLFILNLAVADLCFILCCVPFQATIYTLDAWLFGALVCKAVHLLIYLTMYASSFTLAAVSVDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVAVVSLAYGRTLRFLWAAVGPAGAAAAEARRRATGRAGRAMLAVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYALASRHFRARFRRLWPCGRRRRHRARRALRRVRPASSGPPGCPGDARPSGRLLAGGGQGPEPREGPVHGGEAARGPE | Function: Receptor for the hormone galanin . Receptor for the hormone spexin-1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39573
Sequence Length: 368
Subcellular Location: Cell membrane
|
O88626 | MADIQNISLDSPGSVGAVAVPVIFALIFLLGMVGNGLVLAVLLQPGPSAWQEPRSTTDLFILNLAVADLCFILCCVPFQAAIYTLDAWLFGAFVCKTVHLLIYLTMYASSFTLAAVSLDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVAVVSLAYGRTLCFLWAAVGPAGAAAAEARRRATGRAGRAMLAVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYSLASRHFRARFRRLWPCGRRRHRHHHRAHRALRRVQPASSGPAGYPGDARPRGWSMEPRGDALRGGGETRLTLSPRGPQ | Function: Receptor for the hormone galanin and spexin-1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40410
Sequence Length: 370
Subcellular Location: Cell membrane
|
Q8EMJ9 | MKITDLELHAVGIPRHTGFVNKHVIVKIHTDEGLTGIGEMSDFSHLPLYSVDLHDLKQGLLSILLGQNPFDLMKINKELTDNFPETMYYYEKGSFIRNGIDNALHDLCAKYLDISVSDFLGGRVKEKIKVCYPIFRHRFSEEVESNLDVVRQKLEQGFDVFRLYVGKNLDADEEFLSRVKEEFGSRVRIKSYDFSHLLNWKDAHRAIKRLTKYDLGLEMIESPAPRNDFDGLYQLRLKTDYPISEHVWSFKQQQEMIKKDAIDIFNISPVFIGGLTSAKKAAYAAEVASKDVVLGTTQELSVGTAAMAHLGCSLTNINHTSDPTGPELYVGDVVKNRVTYKDGYLYAPDRSVKGLGIELDESLLAKYQVPDLSWDNVTVHQLQDRTADTKS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the regioselective dehydration of galactarate into 2-keto-D-threo-4,5-dihydroxyadipate ((2S,3R)-dihydroxy-5-oxohexanedioate). Is not active on other acid sugars.
Catalytic Activity: galactarate = (2S,3R)-dihydroxy-5-oxohexanedioate + H2O
Sequence Mass (Da): 44342
Sequence Length: 391
EC: 4.2.1.158
|
O22807 | MRKEVLPPVLSTTTVCFEKKPIIATLLALSLVMIVWNLPPYYHNLISTARPCSAVTTTTTTTLLSSSNFTSAENFTTSLSTTTAAASQKYDSTPSDPNKRVFQPFGNAAALFVLMGAYRGGPTTFSVIGLASKPIHVYGKPWYKCEWISNNGTSIRAKAQKILPDWGYGRVYTVVVVNCTFNSNPNSDNTGGKLILNAYYNESPKLFERFTTLEESAGIYDESKYSPPYQYDYLYCGSSLYGNVSASRMREWMAYHAWFFGDKSHFVFHDAGGVSPEVRKVLEPWIRAGRVTVQNIRDQSQYDGYYYNQFLIVNDCLHRYRYAANWTFFFDVDEYIYLPHGNTLESVLDEFSVNTQFTIEQNPMSSVLCINDSSQDYPRQWGFEKLLFKDSRTKIRRDRKYAIQAKNAFATGVHMSENIVGKTLHKTETKIRYYHYHNTITVHEELCREMLPNSAKKKVTLYNKLPYVYDDNMKKLVKTIKEFEQKKLGTDVKNFS | Function: Involved in the biosynthesis of beta-1,4-galactan. Can transfer galactose residues from UDP-galactose to beta-1,4-galactopentaose in vitro. Forms specifically beta-1,4-galactosyl linkages and can add successive beta-1,4-galactosyl residues to the acceptor. Beta-1,4-galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56865
Sequence Length: 496
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q9LTZ9 | MAKERDQNTKDKNLLICFLWNFSAELKLALMALLVLCTLATLLPFLPSSFSISASELRFCISRIAVNSTSVNFTTVVEKPVLDNAVKLTEKPVLDNGVTKQPLTEEKVLNNGVIKRTFTGYGWAAYNFVLMNAYRGGVNTFAVIGLSSKPLHVYSHPTYRCEWIPLNQSDNRILTDGTKILTDWGYGRVYTTVVVNCTFPSNTVINPKNTGGTLLLHATTGDTDRNITDSIPVLTETPNTVDFALYESNLRRREKYDYLYCGSSLYGNLSPQRIREWIAYHVRFFGERSHFVLHDAGGITEEVFEVLKPWIELGRVTVHDIREQERFDGYYHNQFMVVNDCLHRYRFMAKWMFFFDVDEFIYVPAKSSISSVMVSLEEYSQFTIEQMPMSSQLCYDGDGPARTYRKWGFEKLAYRDVKKVPRRDRKYAVQPRNVFATGVHMSQHLQGKTYHRAEGKIRYFHYHGSISQRREPCRHLYNGTRIVHENNPYVLDTTMRDIGLAVKTFEIRTIGDRLLRTRQ | Function: Involved in the biosynthesis of beta-1,4-galactan. Beta-1,4-galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59956
Sequence Length: 519
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q8A2H2 | MKNVSRLLPLLPGIALLTGCNQKVQKDNGQNSQKPNIIYIFADDLGIGDLSCYGATKVSTPHIDRLAGQGVQFTNAYATSATSTPSRFGLLTGMYPWRQENTGIAPGNSELIIDTACVTMADMLKEAGYATGVVGKWHLGLGPKGGTDFNGHITPNAQSIGFDYEFVIPATVDRVPCVFVENGHVVGLDPNDPITVNYEHKVGDWPTGEENPELVKLKPSQGHNNTIINGIPRIGWMTGGKSALWKDEDIADIITNKAKSFIVSHKEEPFFLYMGTQDVHVPRVPHPRFAGKSGLGTRGDVILQLDWTIGEIMNTLDSLQLTDNTILIFTSDNGPVIDDGYQDQAFERLNGHTPMGIYRGGKYSAYEAGTRIPFIVRWPAKVKPNKQQALFSQIDIFASLAALLKQPLPEDAAPDSQEHLNTLLGKDYTSREYIVQQNLNNTLAIVKGQWKYIEPSDAPAIEYWTKMELGNDRHPQLYDLSADPSEKNNVAKQHPEVVRELSELLESVKTR | Function: Exosulfatase involved in the degradation of the glycosaminoglycans (GAGs) chondroitin sulfate (CS) and dermatan sulfate (DS). Catalyzes the hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units . GAG-specific sulfatases play a key role in the persistence of the major human gut symbiont B.thetaiotaomicron in the host gastrointestinal tract .
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Sequence Mass (Da): 56324
Sequence Length: 511
EC: 3.1.6.-
|
A0A1D8PK89 | MPEKELDYIRSTDAAGSTEKDGGIYIDAFDKQDNAPPKKGFAKFIDGFRRADAEELGIDPNLSEAEKIAIMTANSPLTRSLKNRHLQMIAIGGSIGTGLFVGSGSSLHTGGPAGLLIAYILIGTMIYCTVMSLGELAVTFPVSGAFVTYNSRFIDPSWGFAMAWNYAMQWLVVLPLELVAAAMTVKYWDAKTNSAAFVVIFYVLIVAINFFGVRGYGEAEFIFSAVKVLAVLGFIILGIVLCAGGGPQGGYIGGKNWYIEGAPFPNGAKGVITVFVNAAFAFAGTELCGLAAAETENPRKSLPKACKQVFWRITLFYVICLTLVGLLVPWNDERLLGSSSADASASPFVISIRNAGIKGLPSVMNVVIMIAVLSVGNSSVYGSSRTLAALAASNQAPKIFGYIDKQGRPLVGIIAQLLVGLLCFLAASDKQGEVFNWLLALSGLSSIFTWGSINVCLIRFRRALAAQGRDTGELVFTSQVGVIGAIWGAFLNTVVLCLQFWIAVWPLHSSPSAEAFFSAYLTVPVVIVFYVGHKLWTKNWQVYICAKDIDIDTGRRELDLDLVKQEVAEEKAYIASLPFYRRVYNAWC | Function: Amino-acid permease with broad substrate specificity . GAP2 is the only amino-acid permease with very broad substrate specificity, none of the other GAP permeases is able to transport such a variety of amino acids . GAP2 is also able to transport thialysine, and thus probably also lysine . Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63545
Sequence Length: 588
Subcellular Location: Cell membrane
|
A0A1D8PN88 | MTTKEKDEFNIGSLQNSPESSTNMSPDVITTPISKWQAFKDSFKPPEQKPLASSSSSTSSLSASSPHHNDVANNYDIEKSLRPDQQGELKRELKNRHVQMIALGGSVGTGLLIGSGGALHQGGPAALLIAWGITGTMVFCIIHSLGELCVAFPVNGAFSTYANMFVDSSWAFAVGWNYAIMWLIVLPLELVAAAMCITYWNDEINPASWVAIFYVLIVVINIFGVKYYGDAEMYLTIFKIIAIVGFIILGVVLVCGGGPTHEFIGNKYWKQDGAFANGFKGVATTFVTASYSMAGSEMVGLASAEVANPQKSLPKAIRQVFWRIFLFYFLSLTFIGLLVPSNSPQLLGASGTSASPFVIAIKNGGIYALPSIFNACILLSVLSVGNSAVYGCSRTIQSLGAQGLGPKIFAYVDRKGRPLGGLVMSAIFGLLCFLSAYHDEATIFNWLLSVAGLATIFSWFNIGLCHVRFRLALRKQGRSLQELTFTALTGVWGSVYSMIFLCVVLVIQFWTALFPLGSKGKANAENFFQNYLGAVVILIFYVGHKLYTRNWKLCVKLEDIDLDSGRRSFDLDLIRAEIEEEKAANKAKPLYKRLWNYWC | Function: Amino-acid permease that is able to transport phenylalanine .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65578
Sequence Length: 599
Subcellular Location: Cell membrane
|
Q8I5I8 | MGNKCSRSKVKEPKRKDIDELAERENLKKQSEEIIEEKPEEVVEQVEETHEEPLEQEQELDEQKIEEEEEEPEQVPKEEIDYATQENKSFEEKHLEDLERSNSDIYSESQKFDNASDKLETGTQLTLSTEATGAVQQITKLSEPAHEESIYFTYRSVTPCDMNKLDETAKVFSRRCGCDLGERHDENACKICRKIDLSDTPLLS | Function: Component of the glideosome complex, an inner membrane complex structure involved in parasite gliding motility and host cell invasion . During the asexual blood stage, required in schizonts to recruit MTIP and MyoA to the inner membrane complex where they assemble with GAP50 to form the glideosome complex . By regulating the formation of the glideosome, plays an essential role during merozoite invasion of host erythrocytes .
PTM: Phosphorylated at multiple sites . Phosphorylation increases during the schizont stage and peaks in segmented merozoites . May be phosphorylated by PKB . In schizonts, phosphorylated at Ser-89 and Ser-149 in response to phospholipase C-mediated calcium release . Phosphorylation at Ser-149 begins in early schizonts while phosphorylation at Ser-103 begins in late schizonts . Phosphorylation at Ser-89, Ser-103 and Ser-149 appears to be dispensable for GAP45 inner membrane complex localization or GAP45 inclusion in the glideosome complex . Phosphorylation is not required for interaction with GAP50; however, it may regulate the interaction with MTIP and MyoA .
Location Topology: Lipid-anchor
Sequence Mass (Da): 23632
Sequence Length: 204
Subcellular Location: Inner membrane complex
|
Q59WB3 | MSYKGNDIEKQQSASTATGFNDKQIASTSEDATDRSHNIHGDTSSLDSRYTYETVDQEKNYFKRVYNSFKPMNLEEQGIDTSQLTPVERTIIASAKHPLARRLKARHLQMIAIGGSIGTGLFVGSGYALANGGPGAVLIGYVIVGYALLTVVNALGELSVQFPVSGSFNAFFSRFLEPSFGGTFGILYAASWCISLPSELIAAAMTIQYWNTEVNPAVWVAVFWVVIVVINLFGVKGYGEMEYFLSIIKVLAVVGFIILGICITCGVGDQGYIGGKYWHNPGAFNHGLKGVTSVFISAAFSFGGIELVALAASETANPRISLPAAVKSTFWRIFIFYILTAIIIGCLVPYTNDDLLNGTGIAASPFVIAVSQGGIRVVPHIMNAVVVIAVISVGNSSVYGCSRTLASLAVQGLLPKSMGYIDRGGRPLIAILFTSAIGLLGFLVVVDNEGDVFTWFFSICSLSSFFTWGAINVVHLRWRFALAAQGRSTDEIIFRSPLGTFGSWTGILVLILIVIGEVWVSIWPIGSPADVQQFWKNCLSLPLMIVMWAGFKTYHRSWNMLWVKLEDIDLDTGRREIDVELLKQELAEERQIIKSKPFVYRIYKFFF | Function: Amino-acid permease involved in S-adenosylmethionine (SAM) transport and required for SAM-induced morphogenesis . GAP4 is also able to transport arginine and thialysine, and thus probably also lysine .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66478
Sequence Length: 607
Subcellular Location: Cell membrane
|
Q8I2X3 | MNYCKTTFHIFFFVLFFITIYEIKCQLRFASLGDWGKDTKGQILNAKYFKQFIKNERVTFIVSPGSNFIDGVKGLNDPAWKNLYEDVYSEEKGDMYMPFFTVLGTRDWTGNYNAQLLKGQGIYIEKNGETSIEKDADATNYPKWIMPNYWYHYFTHFTVSSGPSIVKTGHKDLAAAFIFIDTWVLSSNFPYKKIHEKAWNDLKSQLSVAKKIADFIIVVGDQPIYSSGYSRGSSYLAYYLLPLLKDAEVDLYISGHDNNMEVIEDNDMAHITCGSGSMSQGKSGMKNSKSLFFSSDIGFCVHELSNNGIVTKFVSSKKGEVIYTHKLNIKKKKTLDKVNALQHFAALPNVELTDVPSSGPMGNKDTFVRVVGTIGILIGSVIVFIGASSFLSKNMK | Cofactor: Binds 2 metal cations . The role of the metal cation is unclear .
Function: Component of the glideosome complex, an inner membrane complex structure involved in parasite gliding motility and host cell invasion . During the asexual blood stage, may play a role in the assembly and anchoring of the glideosome complex to the inner membrane complex . During the sexual stage in the vector mosquito midgut, protects gametocytes against host alternative complement pathway-mediated elimination by interacting with host complement inhibitor factor H . Has phosphatase activity towards nucleotides such as ATP, vitamins B1 and B6, phosphorylated sugars, glycerol phosphates and inositol triphosphates . However, the phosphatase activity is controversial .
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
PTM: The N-terminus signal is likely to be cleaved.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 44604
Sequence Length: 396
Domain: The C-terminal transmembrane and cytoplasmic domains are required for the trafficking of the protein to the inner membrane complex.
Subcellular Location: Inner membrane complex
|
A0A1D8PMB1 | MSKKYSEENTSSIPLTDLTSPSTGETSSQQQRQRASQQQPPQQPESNTATGSRWSNFVDSFKPAIENEKLAMRYRDANADVEEDAGGYYNSTDQLTEIQRININSSKSNLKRKLKNRHLQMIAIASSIGSGLLIGTGGALATGGPGGILIAWILSGISILCTIQAMAELAVTFPVSGGFNVLFSRFIDPSVGFSVAWNYVLQYLVLLPLELVAASMTIQYWNTDINPDVWVIIFYVTVTSINFFGVRLYGEVEFILSSLKVIAVVGFIILSIVLAAGGAPNGVHHGTKYWHDPGAFANGFKGVSSTFITAAFSFAGTELTGLTSAEAENPRKALPKACKQVFWRILLFYVVSIILITFLVPYDNPRLLGASDVSASPFVIAIQDGGISGLASVMNSVILISVISVGSSSVYATSRTLVSLAEQNLAPKICGYVDRAGRPLVAILITNVFGLLSFIAASGKEDEVFTWLLSISGLSSIFTWLCICISHIRFRRALHVQGRNTDELTFVSQTGVIGSWFGILLNVLVLVAEFWLAIFPLGEKSNAKSFFETYLGFVILIIFYFGHKLWRNNWILFIRSRDIDIDSGRRETDLEALKRELQEEREVLRNKPFWYRAYHFWC | Function: Amino-acid permease that is able to transport phenylalanine .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68203
Sequence Length: 618
Subcellular Location: Cell membrane
|
A0A1D8PNP3 | MPKEASSPECYTTSTSSNEISEKPGMWRNFKDSFKPPVPIDDIENGSISSTQLKGGQNVPLQQSLKKRQLQMIALGGCVGSGLLVASGAALRNGPASLLIAWFIVSTFLYCTMQCLAELSSTFPVSGSFAVYSIKFIDPSWGTAMGYNYALFWVVVMPLELVASSMTIKFWPSNINTSVWVAVFYVLIIGTNLFGGTRAFGETEFVASVIKLLGIVGFNILAIVLICGGGDQGYIGGKNWHPPFTTGVKGVISVLLTATYSLAGTELVGLTSAEAAGDARKVLPKAIKQVLWRILIFYLLTLTLVGFLVPASDPQLIGGGSGASASPFVIAIREGGIKGLPSVFNVVVLVALLAIANSAVYGFSRTILALAEQGVAPSIFKYVDRQGRPLAGIATSAIVGLLSFVSASKQQEQVFDWLVALSGLSTFFTWGSINAAHIRFRIAMKVQGRSLDELPYKANTGVLGAYYGLIMNVAVLALQFWLAVWPIGGKPDATYFFKQYLAAVLVLAVYVIHKVATRNWKFMVDYKDMDLDSGRSDIDIDILKQELEEEREAYKRQPWYYKFYQFWC | Function: Amino-acid permease with rather broad substrate specificity . Transports many amino acids including proline, methionine, leucine, valine, isoleucine, phenylalanine, tryptophan, threonine and tyrosine, but not basic ones (arginine) and citrulline . Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61796
Sequence Length: 568
Subcellular Location: Cell membrane
|
Q9SNX8 | MAGSGVYADIIEGDVFKYYSDGEWKKSSSGKSVAIINPTTRMTQFKVQACTQEEVNKAMETAKKVQKQWAKTPLWKRAELLHKAAAILKEHKAAIADCLVKEIAKPAKDSVTEVVRSGDLVSYCAEEGVRLLGEGKFLVSDSFPGNERTKYCLTSKIPLGVILAIPPFNYPVNLAVSKIGPALIAGNALVLKPPTQGAVACLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLVASNVIKGGFSYSGQRCTAIKVILVMQSVADTLVEKVNAKVAKLTVGPPEDNSDITPVVSESSANFIEGLVKDAKEKGATFCQEYKREGNLIWPLLLDNVKPDMRIAWEEPFGPILPVIRINSAEEGIHHCNASNFGLQGCVFTRDINKAMLISDAMESGTIQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKIKTTVINLPSPSYTMG | Function: Important as a means of generating NADPH for biosynthetic reactions. May be a main source of cytosolic NADPH for mannitol biosynthesis in leaves.
Catalytic Activity: D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADPH
Sequence Mass (Da): 53174
Sequence Length: 496
Subcellular Location: Cytoplasm
EC: 1.2.1.9
|
Q1WIQ6 | MAGTGLFAEILDGEVYKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEGKFLLSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGDTGISISKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVINLPTPSYSMG | Function: Important as a means of generating NADPH for biosynthetic reactions.
Catalytic Activity: D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADPH
Sequence Mass (Da): 53060
Sequence Length: 496
Subcellular Location: Cytoplasm
EC: 1.2.1.9
|
Q9YB80 | MRRAYTVKQLLESYRAGDTDPVEHVSRVLDALRRWERDVNAFISLEAEEVLIDAAEEAARRWRRGEARRLEGVVVGVKDNISTSFLPTTAGSRMLDGYIPPFNATVVERLLMEGAIIIGKTNLDEFAMGSTGEFSAFGPTRNPWDLSRVPGGSSSGSGACLAYGACDAALGSDTGGSVRLPAAYTATVGLKPTYGLVSRYGLIPYANSLEQISPMARSSEDVMLLLEVIAGGDEYDATSIYSKPTTASREEGLKPEDLSLCIPEELVEHSEEAVRKAFYNTVGKLEGLGARLEYVGLGGAEAYALPAYYTIALAEAASNLARYDGSLYPVRGSSGDYWRQAAEARGIGFGLEVKRRILMGVYVLSEGYKDEYYLAATKLRRVIRDAMLKTVGKCLVATPASPIMPPRIGERVDDPLKLYAMDVYTVLANLSGLPAIALPIEIHGGLPVGLQLIGPRLGERLLAGAANIIEDLTGLAGVVAG | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 51640
Sequence Length: 481
EC: 6.3.5.7
|
C0NYZ7 | MSLLREAEKCLANQKTYASLNAFITPLQRAGPWRDRVRDSDTRRERGVTKSPLDGKLVAIKDNICTRDMPTTCASRILDTYTSPFNATVVESLEKSGAIIAGKTNLDEFGMGSHSMHSHFGPVKNVTESRREPISPGGSSGGSAVAVATGQCYAALGTDTGGSVRLPAAYTGTVGFKPSYGHVSRWGVVAYANSLDTVGVLGSSISTIREVYKTINHPDLHDPTNLPPATRTRLTAAVHNSSTTRSSPSPYLRIGIPTEYNIHELSPTVRTAWQRSIVHLQRMGHTILPVSLPATKHALAAYYVLAPAEASSNLARYDGVRYGTRDTDAPDDAEPGGYLYASSRGKGLGSEVKRRILLGAFSLSADAIDNYFLQAQRVRRLVQADFERVFRVKNPLLPAVDVDADVDGRDKKQIAGDNAGVDVLVVPTAPTLPPTVESLKRASTVETYMNDIFTVPASLAGLPALSVPVQMRGLSTVGDGDESKGDGADAAFGSVGIQAIGQFGDDEMVLHVGEMLEGMHG | 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
Sequence Mass (Da): 55651
Sequence Length: 521
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
Q8YC57 | MSELTALTIAEARDKLKAKAITATELTDAYLSAIDAANDAINAYVAVTHDQARSMAKASDERIAKGEAGALEGIPLGVKDLFATKGVHTQACSHILDGFKPEYESTVTANLWADGAVMLGKLNMDEFAMGSSNETSYYGPVKNPWRAKGSNADLVPGGSSGGSAAAVAAHLCAGATATDTGGSIRQPAAFTGTVGIKPTYGRVSRWGTVAFASSLDQAGPIARDVRDAAILMKSMASLDLKDTTSVDLPVPDYEAALGRSVKGMKIGIPREYRVDGMPGEIEELWQKGIQYLKDAGAEIVDISLPHTKYALPAYYIVAPAEASSNLARYDGVRYGLRVPGKDIADMYEQTRAAGFGKEVKRRIMIGTYVLSAGYYDAYYLRAQKVRTLIKKDFEDVFAKGVDAILTPATPSAAFSLADEVLANDPVKMYLNDIFTVTVNMAGLPGIAVPAGLNGQGLPLGLQLIGRPFEEETLFQAAHVIEQAAGRFTPAKWW | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 52477
Sequence Length: 493
EC: 6.3.5.7
|
Q8Y6D2 | MGLFDFSVKELHDKLVKKEISPFDLVSESFNRIESVEDKVGSFITLNKEAAFGVAEELGDAGIDPNNMLAGLPIGIKDNIVTKNLRTTAASKILENFDPIYDATVVSKLKNAQTINIGKLNMDEFAMGSSTETSYFHKTHNPWDLSRVPGGSSGGSASAVAAGEVLFSLGSDTGGSIRQPAAFCGVVGMKPTYGRVSRFGLIAFASSLDQIGPITKNVEDNAYLLEAISGLDANDSTSINQPVERFSDSLTGDIKGLRIGVPKEYLAEGVDPGVKQAVLDALKTLEKLGATWDEVSLPHSEYGVASYYILASSEASSNLSRFDGVRYGYRSPNATTLEELYTKTRSEGFGDEVKRRIMLGTYALSSGYYDAYYKKAQQARTLIKQDFINVFENYDVIIGPSSPTTAFKIDGMINDPITMYSNDILTVPINLAGVPAISVPCGFSDGLPVGLQIIGNYFEESLLYKVAHAFEQETTFHKEKPNL | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 52352
Sequence Length: 483
EC: 6.3.5.7
|
A4QR60 | MLVHGRRLGLLLGRSHVAAPKHTSHLPRRTVHLNHFVSKGEAASEAEPPQSTFTVAVKDNIATQAHPTTCASNILRDYTSPYEATVVRQLRRRGARVVGTTNLDEFGMGTHSTHSAHGPVASPAGRSAGGSSGGSAVAVAAGEVEVALGTDTGGSVRLPAAYNGVVGFKPSYGMLSRYGVVPYANSLDTVGLLARSVERIRDLVVGEGLWAQHDDKDPTSLSAAARLRCASGRTGYKGEAAKVGWEGLTFGIPLEYNIFELDPLIREAWEEVAALLQSLGANVVPVSLPTTRQALSAYYVLAPAEASSNLAKYDGVRYGNPGPESENEGGVLYSAARGAGFGDEVKRRILLGAYSLSSEAMDNYFVQAQKVRRLVRGDFDRVFLLDNPLVDKEPTEEGFGEEAEQADLADLHEDVPLLNKRGPARVDFILSPTAPTPAPTLDEALSQTSLDSATNDVFTVPASLAGLPAISLPVDMKEDVHGVGRFAGIQIIGQYWDDARLLDVAVALRGVLGRGLV | 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
Sequence Mass (Da): 54881
Sequence Length: 517
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
Q2W6Y6 | MSKLTDLTMAEARDGLAKGAFTAVELTDAHIKATEAQRHLNAFIVETPDLALEAAKASDARRQAGTAGSMDGLPIGIKDLFCTEGVQTTAASHILEGFKPPYESTVSGKLKAAGAISLGKLNLDEFAMGSSNQTSYFGAVENPWKKTSDPKAKLVPGGSSGGSAAAVAARMVLGATGTDTGGSIRQPAAFCGITGIKPTYGRCSRFGIVAFASSLDQAGPMARTVRDCAIMLGAMAGHDPKDSTSVNMAVPDFERALTGDIRGLKVGIPKEYRPDGLSDEVAKVWDRGIEWLKAAGATPVEISLPHTKYALATYYIIAPAECSSNLARYDGLRYGLRVPGKTLDDMYKKSRAAGFGAEVRRRILIGTYVLSAGYYDAYYAKAQKVRRLIAEDFRKAFETVDVILTPTAPSAAFGMGEGTDDPVTMWLNDVFTIPTSMAGLPGLSLPAGLSADGLPLGLQLIGRPFDEETVFRVAGVMETAANFTAKPEGV | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 51672
Sequence Length: 490
EC: 6.3.5.7
|
C6BSE9 | MSALIEKSLTEIHAMLMTKEVTATEAVKACLEQIAKSEPETKALLHICNDEALKQAEEMDAAGPDASKPLWGVPVVIKDALATNGIPTTAGSKILEGFTPFYDSTAVAKLKEAGAIIVGKANMDEFAMGSTTENSAYQTTTNPWDASRVPGGSSGGSGATVAAGQCYAALGTDTGGSIRLPASFCGCVGVKPTYGRVSRYGMIAYGSSLDQIGPMTRTVEDAARVLNVIGGHDQRDSTSAEQPMEDFVAALEERKDLSGLTIGLPEEYWGEGLSKEVSEACRAAIAKAEELGAKTVPVKLSMTEYAIATYYIIAMAEASSNLSRFDGVRYGHRTEDPKELAELYTKSRTEAFGDEVQRRIIIGTYVLSAGYYDAYYRKAAQIRRLLREDFNKAFESCDIIASPACPTTAFPVGELTSDPLQMYLQDIFTISLNLVGMPGMSLPVAFGKETNMPVGLQFMAPAFDEKTMLQAAHVLEKNLPELPKVKL | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 52280
Sequence Length: 487
EC: 6.3.5.7
|
Q8THJ1 | MMAKWMSVAQVKDKIKESSAEEVTAGYLEVIEKSKINGYITVSDKALEQAKKIDVEGHEGPLAGVPIAIKDNISVVGLPNSCGSKILEGYVPPFNAHVIEKLLDAGAVILGKTNLDEFAMGSSTETSYYGPTANPWDLERVPGGSSGGSAAVVAAGEAPFALGSDTGGSVRCPAAFCGVVGLKPTYGAVSRYGVVAYANSLEQVGPLANNVEDIAILMDVIAGYDRRDSTSIDSKTEYQKALVDDVKGLKIGVPKEFFGEGIHPGVEKAVWNAIHKFESLGATRQEVSMPNINYALASYYIIAMSEASSNLARFDGTRYGFRANGENWHAMVSKTRAEGFGTEVKRRILLGTYALSAGYHDKYYLKALKVRTLVKQDFDKALSTVDLLMAPTMPNPAFRIGEKIEDPLTLYLSDVNTCPINLAGVPSVSVPCGFTDGLPVGLQIMGKPFDEPTVLRAAYTFEKNTDYHTKRPPEVA | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 51114
Sequence Length: 476
EC: 6.3.5.7
|
Q12VH1 | MTKWLSISDVKEKIAATSAEEVTASYLELIDKSSINGYTCTSDGALDTAKMVDKGEVAGPLAGVPIAIKDNISTKGLATTCSSKILEGYVPPYDAHVIERLKEAGAVIIGKTNMDEFAMGTSTESSCYGVTLNPWDHERVPGGSSGGSAAVVAAGEAPISLGSDTGGSVRCPAAFCGVVGLKPTYGAVSRYGLISYANSLEQIGPMATCVEDIAAVMDVIGGYDARDSTSIDKKIDHQAALIDDVKGLKIGVPDEYFGEGVDSGTENAVWDAINKYEEMDASWEKVSMPNTKYALAAYYTIAMSEASSNLARFDGTRYGPRNDGENWHVMASKTRAENFGKEVQRRILLGTYALSAGYQDKYYLKALQVRTLVKQDFDRAFANFDVLMAPTMPLPAFKIGEMVEDPLSQYLIDVNTVPMNLAGVPCISVPCGSSDGLPVGLQIIGNHFDEAALIRAAYSFEKNTDHHKARPGEVA | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. 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
Sequence Mass (Da): 50722
Sequence Length: 475
EC: 6.3.5.7
|
B9MQ85 | MEYEVVIGLEVHAELATKSKIFCSCTTEFGGEPNTHCCPICTGMPGVLPVLNKKAVEYAIMAGLATNCQIARYSKQDRKNYFYPDLPKAYQISQYDLPLCYNGYIDIEVNGQKKRIGIKRIHIEEDAGKLLHDQWEEGSLVDFNRCGVPLIEIVTEPDLRSSEETRIFLEKLKAILQYTEVSDCKMQEGSLRVDVNLSVRPKGSKEFGTRTEMKNLNSFRSVVRAIEYEARRQIEVLESGGVVVQETRRWDDPKGISLSMRTKEEAHDYRYFPEPDLPPIVVDDSWIEEIRKRIPELPDQKKERYIKEYGLPEYDAGVLTSSKAIANYFEECIKYTQNIKAASNWMMGEIMRILNDKGLEPEEINNIKIKPNQLASLINLVDNKTISNTIAKQVFEEMFETGKDPEVIVKEKGLVQITDRNVILEAVKQAIANNPKSVEDYKNGKDKAFGFLVGQVMKITKGKANPQLVNEILREELEKI | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 54776
Sequence Length: 480
EC: 6.3.5.-
|
Q8RC39 | MKYEAVIGLEVHAELLTDSKIFCGCSTKFGSEPNTQVCPVCLGLPGTLPVLNKKVVEYAVRAGLALNCTIANFSKMDRKNYFYPDLPKAYQISQYDLPLCSNGYIEIEVEGGTKRIGIKRIHIEEDAGKLLHEGTDGSLVDYNRAGVPLIEIVSEPDISTPEEAYQYLVKLKSILEYTEVSDCKMQEGSLRVDTNVSVRPVGTTELGTKIELKNLNSFKAVQKALEYEIKRQIKVLEEGGTIVQETRRWNEAKGITEPMRTKEEAHDYRYFPEPDLVPIIVTEEWKEEIRKTLPEMPDAKRERFITQYGLPEYDAKVITSSKKMADFFEKCASNYHSPKIVSNWLMGEFARLLNDTGKEIDEVPITPDMLIELLKLVDDNVISGSIAKTVFEEMFFTGKNPQIIVEEKGLRQIADEGELRRIVRKVIEENPKSVEDYKKGKEKALGFLVGQVMKETKGKANPQLTNQLLREELSK | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53803
Sequence Length: 475
EC: 6.3.5.-
|
Q6FXR9 | MYKNSIRTRPLKRFISNHAKGKFALDPAYKLKCGLEIHTQLNTRYKLFSYTSNEAENLTISPNTSTSHYDISLPGTQPRLNYEAVLYATKLALSLDSDINLISQFDRKHYFYGDQPQGYQVTQHYKPFAKNGKLTLYGAYEDINENEKTIRIEQLQIEQDTGKSLYASGADMTTMIDLNRSNVPLIELVTKPDFEDLKQVRAFIKKYQDLVRRLNICTGNLETGSMRIDVNLSVNDFARVELKNLPNTSSIMNAIKFEYERQLHIIKNGEGERLLRDTETRGWTGSETVKLRSKETSIDYRYMPDPEIPFITIADDVVHKVKSTLPVSADALLREFMNKPYNLPIKHAKILCISGNQNEMYDHEQLRKYYKDVCVHYQKEYPDDNLKIPSNWILNEFIGNLNKLETKLNEIYEILTPSTFFELIRLMKQGVITGNSSKLLLFHIVNNVKTGVFTKSSQINLKQLINEYELQAADQINEHELEEICRSIIDDIKDEKLLQNLISGKKKTSLKFLVGQGMRLSQGRLNPNELEKMFRQVLDIKW | 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
Sequence Mass (Da): 62767
Sequence Length: 542
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
A9KJ27 | MKVYETVIGLEVHVELATKSKIFCGCTTQFGGEVNAHCCPICMGMPGTLPVLNKKVVEFAIAAGLAMNCDITKNCKFDRKNYFYPDLPKAYQVSQLYLPICRNGSIEIEVDGIKKSIGIHEIHMEEDAGKLVHDPWEDCTLVDYNRCGVPLIEIVSEPDMRSAEEVIAYLEKLKLILQYLGVSDCKMQEGSLRADINLSIREVGEPEFGTRTEMKNMNSFKAIARAIEGERKRQIELLEDGKKVIQETRRWDDNKDTSFAMRSKEDAQDYRYFPEPDLVPMEISEEWLTEIKGREPELRDAKMLRYVKEYEIPEYDAGIITGSKNLADIFEATVSLCNKPKEVSNWLMVETMRLLKESEQDAEELKLSPANFASLIELIDAGKINRTIAKEVFEQIFKANVDPNAYIEEHGLGMVSDDGVVRSTIENILKENVQSVSDYKNGKDKAFGFLVGQTMKAMRGKANPSVINEILRELLSKA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 54085
Sequence Length: 478
EC: 6.3.5.-
|
Q1MPL6 | MSHFEAVIGLEVHVQLGTKSKLFCSCPTTFGTPPNTNICEICAGMPGALPSLNKLAVEYAVKAGLALHCTINTHSFFSRKNYFYPDLPNGYQISQGTHALCTSGYLDLTIKNNNKRIGIHQIHLENDAGKSIHSPHENKSFIDLNRAGVPLIEIVSKPDINTPSEAVAYLKSLHAIVTYLGISDGNMEEGNFRCDANISLRPYNSKHLGTRTEIKNLNSFRNVQRALEFEINRQQDILEDGKTIIQETRLYNSDKDITTPMRDKETAHDYRYFPDPDLVPIYVTIQEIEKWKGEIPELSDSRQKRFVIEWGLAHQDAEILTSSRELADFFEKAVKLYPKPKKIANLIKILLLHMLNEHNITIQQCTMKPEAIAELAAIIDENLISIKIAHDIFEDLFSKQLMPKDYVIKHGLTQISDTKTIDTIVVEVLAENPTEVAAYKNGKTKLLSFFIGQVMKKMQGQANPALVNQALHNILSK | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53709
Sequence Length: 477
EC: 6.3.5.-
|
Q980Q3 | MVKIGLEVHVHITALKTKLFCSCPSDYTGKDPNTVTCPVCLGLPGAIPVLNENAVKYGILTALALNCQIAEKLIFDRKHYFYPDMSKNYQISQYDGPGSMAIAKDGYIKLNDKIIRIRRINIEEDPAKIVYPTGSILTSKYTLLDYNRSGTPLLEIVTEPDLRSAKEARFFLEKLRSILEHLGVCDCGIEGAMKADVNISVKGGERVEVKNVGSPKDVEDAINYEIARQRASILQGIKIERETRHWDNERRVTVPLRTKETEEDYRYFPDPDLPPYSITPELIEKFKREMPELPDQRAERFVKQYNVTPYQAQVLVNEKALADLFEEITNNYKNYAKVANLLINDYMRWLNENNITVTQSKAKANHIIELFEYLDSGLISIKIVKELLPEMILTGKTPGQLIKEKGMTNIKDENYLERIIDEVLNEEKEAVEKAKRDPKVVNYLVGMVMKKTGKRADPQMTVEIIKKKLGLT | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53848
Sequence Length: 472
EC: 6.3.5.-
|
Q2S1B9 | MAYERYEPVIGLEVHVQLQTNAKIFSPDAAAFGAAPNTQVDPISLGHPGTLPVLNETVVKHALRLGVATHCSIADRSAFARKHYFYPDLPKGYQISQYDTPICYDGYLEVFPGEEEDASPSAPDSRRVGLTRIHMEEDAGKSVHASAGGTTRLDNNRCGVPLLEMVTEPDLRSPREASLFLQRLRQLVRYLGISDGNMEEGSLRCDANVSVRPQGREAFGTRTELKNMNSMRHVEQALDYEIARQIAAEERGESITQQTLLWDADAGTTRPMRSKEEAHDYRYLPDPDLVEVRIEDATVDEVRANLPELPRARRRRFVEEVGLPAYDAGVLTEERAVADYFEEALRHLYKRTKGGDTDAQAKAVSNFIMTEVMRVLNERDLSVSELGVGPERLAQLVFLRLQDKVSSNGAQEVFEAMLDAPDKSAGRIADERDLIQVTDRGAIAPVVEDVLNDNPDKVNTYLGGKDGLLGFFIGQVMQRFDGSPNPELVRSLLREKLDARRDTANVDE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 56610
Sequence Length: 508
EC: 6.3.5.-
|
B6JYB6 | MSSLARWIITIGLEVHVQLSTKLKLFSRALAENHKAPNSAVSFFDISLPGTLPIVNPEAIRLATKAALVCNCEIAPSLEFDRKHYVYSDQRAGFQITQKRRPLGTNGFVRLNAALDGVEKDQLVEIKCLQLEQDTGKTVNELNEDLVLLDFNRANVPLIEVVTAPCFHSPHDAACFLRKLQTILRLANVSDAKMELGNMRCDVNVSVASAENPTKQLATVELKNLPSIRYVEIASELEAKRQIELLNNGSSPVPETRSYDVEKNATVFLRKKRGPSDYMYLPEADIPEITLTSAYVDDVRKSIGPSVDELLETLLQKKYFNLQDAKALLQTEDGLSYYQVLVGELEKVTSSMSPDVQLKAEKLIPFWLVNEYVGDCANAPDEKRDLDTIPPADLAFLLGNLANGTLSAYAAKHILQLAVQDPKKNSIYKLVNENANAEFDENTLKDLVNELIQANGDKVNALKVGKDGVLNWFIGNVMRRSSGKAKPDEIKRLINNTVLCENSSK | 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
Sequence Mass (Da): 56067
Sequence Length: 505
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
Q9UT77 | MSFGRWAASIGLEIHLQLATVKKLFSPAKVNPLAQPNTCVAYFDVSLPGSMPILNPEALKFAVKGALALNCEVANVCKFDRKHYFYPDLPAGYQITQKEIPIGRNGFIPLSAGLDNVPDTQIPIQHIQLEQDTAKSTSAKNPSRILLDYNRAGTPLLEIVTKPCFHDVNTVSAFLFKLQSIVRFAGISEALMENGGMRCDVNVSIAPVISSENLNELHFKNNGVISVEKSISHFPQLGTQLARVELKNLSNVRNVVNSIRHEVDRQVSLANMGVSWPSETRGFDDITGKTFPLRNKTTSDDYLFLPETDIPPIILSRSYVNSVLKSLPALPDELFQKLTTGSHAISHKEARTLLSVKEYYHYYRNAYHHIDSISHVNQSLKEDALRTLPYWITVELVGKVREIDPSPNINIVPPLQLADIVLLVSKKKLTAASAKLFLRSLIKSPSSKPISTLIQEKNFGTIGDSEKIKACVESVLSKHSKQFEELKNGKTSLIKWFVGLTMRELRGQASPKDIEMEVQSSLRREK | 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
Sequence Mass (Da): 58608
Sequence Length: 526
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
C5Y3V8 | MALTLLRGMRTPVSSGSNPGLFFAVLRPRLSRFTARAESAQATEPKAAPPPRSIQLATKEAAEQKTQGFEAVIGIETHVQLSTVTKAFCSCPYSYGAQPNSTVCPTCMGHPGTLPVLNEKVVECAVKLGLALNCEISMTSKFDRKQYFYPDLPKGYQISQFDIPIAKKGHVDLDLPVEFGGGHRKFGITRVHMEEDAGKLLHSESSSYSQVDLNRAGVPLLEIVSEPDMRTGIEAAEYGAELQRIVRYLGVSNGNMQEGSLRCDVNVSIRPVGQSEFGTKVEIKNMNSFSAINRAIDYEISRQILLHKEGQADQIVQETRLWDESSQKTFTMRKKEGLADYRYFPEPDLPEVVLTSDYINEISKSMPELPEAKRRRYENMGLSMQDVLFLANDDNIGHFYDSTLEHGADAKLAANWIMGDIAAYLKDEKVSIDEIKLTPLELSELIASIKNGTISGKIGKEILAELIAKGGTVKGVIEEKDLVQIADPAAIEAMVDKVIADNPKQLEQYRAGKTKLQGFFAGQVMKASKGKANPVLLNKILGEKLNAN | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and 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
Sequence Mass (Da): 60318
Sequence Length: 548
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
Q0ACB4 | MSLEESEVKHIAHLARVAIEADDIPGYARNLSDILDFVEQMKDIDTSGVTPMAHPLDAVQRLREDEVTEPDQRERFQAIAPATEAGLYLVPRVIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10655
Sequence Length: 95
EC: 6.3.5.-
|
B8JBQ2 | MALSLEEVRRIAVLARLRLSEEEERTFAGQLSAILDHVRQLEELDVTAVEPMTHALAAGELPARREDAVLPSLTPEEATAAAPAREGTAFKVPRIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10612
Sequence Length: 97
EC: 6.3.5.-
|
E3WSB5 | MIRGWTIFTLCKPSALVGSSHFNKQFNWAKSQLQFATKVPQQPYAKTESILPTLQEPDTKPAIDRHTVQLLERLSLVDLETNDALETLEDSIGFASRILTIGTEGVEPLYTVLERERLSLREDVVNDGDLQTDVLRNAAVTEEEYFVAPPGNIPLELQENSRPIAH | 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
Sequence Mass (Da): 18658
Sequence Length: 166
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
O67904 | MVDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLKELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPERKDGFFVVPRVVEV | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11215
Sequence Length: 94
EC: 6.3.5.-
|
F4JV80 | MATRALLAVIYASPNRCYISPSRIKIQSLTCSSSSHYYQRQSRKNHRIARSYSSDSDSSVLQPPDVARLAQTARISLTPAEIEECETKIRRVIDWFGQLQQVDVNSVEPAIRAEMDGGNLREDAPETFDNRDSIRASIPSFEDAYLKVPKILNKE | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and 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
Sequence Mass (Da): 17519
Sequence Length: 155
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
O27956 | MVSIEDVYHTAELAKIEITEEQAEKFRKEFETILDYFNILDEVEEDVEPTFHVLPLTNVFREDEPGECLKQEEALSNAKHKEEGYFKGPRVVE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10904
Sequence Length: 93
EC: 6.3.5.-
|
B0R4C0 | MTDAVDAEEIRHVADLARLRLDDEDVDTVVDHCGDILEHFERLEEVPEVDAEPELVNVMRADEIADSLDQDDALANAPETEDGRFKGPNVS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10129
Sequence Length: 91
EC: 6.3.5.-
|
B0TDK8 | MALTKAEVEYVAMLARLELSEADLERYTTQLNAILDYAQRLQGLDTKDVPPTAHVFPLHNVMRDDRIDPSMERERIVANAPEEEDGFFRVPRIV | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10813
Sequence Length: 94
EC: 6.3.5.-
|
O25626 | MQIDDALLQRLEKLSMLEIKDEHKESVKGHLAEVLGFVENIFALETSALKTDIELCTPLREDEPKSQPNTAKEILSQNKHSQDHYFVVPKIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10656
Sequence Length: 93
EC: 6.3.5.-
|
A9B090 | MSLTPEQVRQVAHLARLKLDEDEMERMRLQLSSILDHIEMLQAIDVTDVPITAQVTDLTNVTRIDAVTSSLPVDAALANAPDRQGDYFRVKAVFEE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10777
Sequence Length: 96
EC: 6.3.5.-
|
O43716 | MWSRLVWLGLRAPLGGRQGFTSKADPQGSGRITAAVIEHLERLALVDFGSREAVARLEKAIAFADRLRAVDTDGVEPMESVLEDRCLYLRSDNVVEGNCADELLQNSHRVVEEYFVAPPGNISLPKLDEQEPFPHS | 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
Sequence Mass (Da): 15086
Sequence Length: 136
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
Q31F52 | MSLEKTEVDTISRLAAISVDASEVDQLTAKISNVLDLFQRMEAVDTTNVEPMSHPLDQVQRLREDVVTETDHHEEYQKLAPAAEKGMYLVPQVID | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10695
Sequence Length: 95
EC: 6.3.5.-
|
B4U5L8 | MSISKEEVIKIAKLSRLELKEDEVEFFSAQIKNILEFVNKLNEVKAELLEEEYSDSTPLRKDEPETSLEVDKVLLNAPAKRLNMFEVPKIVDAN | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10821
Sequence Length: 94
EC: 6.3.5.-
|
B7PZ18 | MFRRSVSFVRSHVLRSFSSQPVVPVTPIVKNPASQGAGTIKLEQSTVELLERLSLVDFSNAEAVSRLEEAVKFASVIMNVDTTGVRPMVTPLEDTVLRLRDDVAEKCSSEDVLKNAAVIEEDYFVAPPGNIPLEPKANYGLGNS | 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
Sequence Mass (Da): 15703
Sequence Length: 144
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
A6SUD8 | MSLELSDVKRLSTLAQIELTTEQSAQTLDKLNGIFALVEQLRAVDTTGIEPLNHPIATMLPDLALRLREDVVSEANRRDDYQKVAPATQDGLYLVPKVIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11116
Sequence Length: 100
EC: 6.3.5.-
|
A6W7L6 | MSAISRSEVEHLARLARIDMTDEELDRMAGQLDAVLDAVAQVASVVTDDVPATSHPVPLTNVTRPDVVRPGLTAEEALAGAPASEDGRFRVPQILGEEA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10487
Sequence Length: 99
EC: 6.3.5.-
|
Q5FLL2 | MEITKDTIKHVATLSRLAFNEEELDKFTDQMGSIINMADQLSEVDTEGVEETVQVVDRDTVFREDIPEHWQGQTRETLMENVPEKANGYIKVPVIINKDEDE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11738
Sequence Length: 102
EC: 6.3.5.-
|
A7NR21 | MLLTMEDVEHVARLARLRLSPDELEHMRDQLSKILDHFQMLQQIDVSAVPPTAQVTDLINVMREDEVRPSLPREQALANAPEQQDGMFRVRAIFEEAS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11279
Sequence Length: 98
EC: 6.3.5.-
|
A5USE7 | MALTLQDVEHVARLARLRLSPAELEKMRDQLSNILDHFQMLQQIDVSAVPPTAQVTDLVNVLREDEIRPSLPHEQALANAPEQQDGMFRVRAIFEEE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11085
Sequence Length: 97
EC: 6.3.5.-
|
Q1AXT1 | MISEEQVRHVAELARLGLTDEEVARMGGQLGAILDSIEKIRELDLEGVPPTANPLNLTNVFRPDEPRESLRREEALAVAPETADGMFAVPRID | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10248
Sequence Length: 93
EC: 6.3.5.-
|
A8M5E5 | MAAISREEVAHLARLSRLAVTEEELGTLAGQLDVILQAVAQVGEVTAADIPPTSHSVPLTNVLRDDVVAPCLSPQEALSGAPDAEEQRFRVPRILDEDVAS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10708
Sequence Length: 101
EC: 6.3.5.-
|
Q2S325 | MSVTRDDVRHVAQLARLDFSEEEEARMAEELSEILGYVEKLDELDTAGVPPMSHVLDVTNVFRSDEIEERIDRGQALEPAPDADNEHFLVPQVVE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10762
Sequence Length: 95
EC: 6.3.5.-
|
Q9HJJ6 | MDTKIGLEVHFQLNTGKLFCRCPVEQSSGELMRFSRKLHISASELGNIDAAASYESMRSRSFQYVVTDNSCLVEMDEEPPKTPDERAIATAISVSKALNCDIVDHITYMRKIVIDGSNTTGFQRTAIVGINGHIETSKGPVRISTVCLEEDAARKIEEIGNTVVYSLDRLGIPLIEISTEPDIVDEDHAVEVARSIGYIVISTGNARHAVDAVRQDVNFSMGYGRVEIKGVSKLTQIRDVIRYEKERQENLRAAVDLIKSRGGLDRVSFNLKDVSDLFAGTKSKIIRSGIESGGVYAGILKNMAGTLKNGKLRMGKEIADLVRSYGIKGVMHSDELPGYGLTQDEVEALYRYLGKGDNDAVLLIAINQSRVKMIENSIFDRIQKIISMDLSETRGPAGEETVFLRPMPGKDRMYPETDIPVIKVDSKLMEMSSSIKPRTYAEVVQDLVDRYGISKQNAEYIASEMVVDAFRNIAEFVEAREAARILTQIVPDLERRTKKIIDHDRIIELCRRSKDLHFDRYQLEMALEILYERDDVASVLGDSRLKELSREEIKSIIREILSSGRNATQNSIIALIKEKTERVFDPRVAMECFNEVKNKNNVF | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 67704
Sequence Length: 603
EC: 6.3.5.-
|
Q75EI6 | MPLARLVEGEKHDECTYVAASSLLIGRHKMLRSLIYASRRWSSSVGARFSSREELQAYLARPAWQPEDYLPSAEDIARQQLSEEETRKLLKLSGLPEADIQEVRRRLATQLSFVSQLQSVEVDDCADPQYAKAMQRHPAAIGYEELVRRAELDAKDTSLGEKSGSWDSTATATLKKDGYFVLREGLLQKR | 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). Required for proper protein synthesis within the mitochondrion.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21486
Sequence Length: 190
Subcellular Location: Mitochondrion inner membrane
EC: 6.3.5.-
|
Q59X39 | MKSILRSTTRNLITSSRRFENLKTTEEIRNFLAESTWSINELLKSPTGSSQPEVSPEIVKKMLKLSGLNDLKDDQSVTKALNLQMMFINHLYDNDHETVTPSPKRNENNGIFRLLASDHLPQRPLELNNLLKQINELKPDPSKGEVDFTISDLQRDSFVINKRKE | 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). Required for proper protein synthesis within the mitochondrion.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18977
Sequence Length: 165
Subcellular Location: Mitochondrion inner membrane
EC: 6.3.5.-
|
Q6FSU2 | MSRFMIRAVFFRRYTAATVGKPFRNVAEVKQYLAKQTWSIDEILHGEDTGKAAKQGVPTEEEVRKLLALCAFPVEDADLQNSKRILVKQLSFINKLHETSVDDQDKNLDENYARLLPRQNKALTYDDLLKKIDGIKQDEATGEPTGSWDSTGLAKMRKDNYFIVRQGLLKNRK | 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). Required for proper protein synthesis within the mitochondrion.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19835
Sequence Length: 173
Subcellular Location: Mitochondrion inner membrane
EC: 6.3.5.-
|
C4Y3K5 | MFLRQFSTSPALLKGKVLPELKNAQEISQFLRKSTWNVHDLIPSKEHITNEVDSRVVRKMLRLSGLDENLPEPELNRWAEMLNTHVAFINHVSDLHSSTKGEIGSSVFRLLASDHKPESPLTLKELLRQVDEISDHVSDQRGERGFDTSELRTRINRAKSTAEKE | 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). Required for proper protein synthesis within the mitochondrion.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18879
Sequence Length: 165
Subcellular Location: Mitochondrion inner membrane
EC: 6.3.5.-
|
Q6BXL8 | MSRMLNQIPRLITRSFRTSSVGYKATLGPILENKSQIQDLVNKSEWNIVDIIKFSEDEVRNIKIDSRVITKMLRASGLKDSLSEDQKKSLIRGLKLQMIFIKYLYEGDEAEFHKIEESNDDVFRLILSDHKAPKPITLKSLLSSIENLENEVDAEKGEIKSSLDISKLNGNNPTYFTVRSNKE | 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). Required for proper protein synthesis within the mitochondrion.
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20976
Sequence Length: 183
Subcellular Location: Mitochondrion inner membrane
EC: 6.3.5.-
|
Q9HCG7 | MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCCNPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLRYLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMYQHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQLPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDDAPGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQQVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFGAKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSALFNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVHFYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDDEPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDKDHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILSRGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVRALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWEGFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASWPKVKQGTGLRTGPMFGPKEAMANLSPE | Function: Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as N-acylsphing-4-enine) . GlcCers are membrane glycosphingolipids that have a wide intracellular distribution (By similarity). They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties (By similarity). Involved in the transglucosylation of cholesterol, transfers glucose from GlcCer to cholesterol, thereby modifying its water solubility and biological properties . Under specific conditions, may catalyze the reverse reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to ceramide (such as N-acylsphing-4-enine) (Probable). May play a role in the metabolism of bile acids . Able to hydrolyze bile acid 3-O-glucosides as well as to produce bile acid-glucose conjugates thanks to a bile acid glucosyl transferase activity . Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers .
Catalytic Activity: a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 104649
Sequence Length: 927
Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.2.1.45
|
P97265 | MAFPADLVGGLPTAAYQVEGGWDADGRGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFSISWSRLLPDGTTGFINQKGVDYYNKIIDDLLTNGVTPVVTLYHFDLPQALEDQGGWLSEAIIEVFDKYAQFCFSTFGNRVRQWITINEPNVLCAMGYDLGFFAPGVSQIGTGGYQAAHNMIKAHARAWHSYDSLFREKQKGMVSLSLFCIWPQPENPNSVLDQKAAERAINFQFDFFAKPIFIDGDYPELVKSQIASMSEKQGYPSSRLSKFTEEEKKMIKGTADFFAVQYYTTRFIRHKENKEAELGILQDAEIELFSDPSWKGVGWVRVVPWGIRKLLNYIKDTYNNPVIYITENGFPQDDPPSIDDTQRWECFRQTFEELFKAIHVDKVNLQLYCAWSLLDNFEWNDGYSKRFGLFHVDFEDPAKPRVPYTSAKEYAKIIRNNGLERPQ | Function: Neutral cytosolic beta-glycosidase with a broad substrate specificity that could play a role in the catabolism of glycosylceramides (Probable). Has a significant glucosylceramidase activity in vitro. However, that activity is relatively low and its significance in vivo is not clear (By similarity). Hydrolyzes galactosylceramide/GalCer, glucosylsphingosine/GlcSph and galactosylsphingosine/GalSph. However, the in vivo relevance of these activities is unclear (By similarity). It can also hydrolyze a broad variety of dietary glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro and could therefore play a role in the metabolism of xenobiotics (Probable). Possesses transxylosylase activity in vitro using xylosylated ceramides/XylCers (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) as xylosyl donors and cholesterol as acceptor (By similarity). Could also play a role in the catabolism of cytosolic sialyl free N-glycans (By similarity).
PTM: The N-terminus is blocked.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 53745
Sequence Length: 469
Subcellular Location: Cytoplasm
EC: 3.2.1.21
|
Q9H227 | MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYYNKIIDDLLKNGVTPIVTLYHFDLPQTLEDQGGWLSEAIIESFDKYAQFCFSTFGDRVKQWITINEANVLSVMSYDLGMFPPGIPHFGTGGYQAAHNLIKAHARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQEAAKRAITFHLDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGTADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVPWGVCKLLKYIKDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQELFKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL | Function: Neutral cytosolic beta-glycosidase with a broad substrate specificity that could play a role in the catabolism of glycosylceramides . Has a significant glucosylceramidase activity in vitro . However, that activity is relatively low and its significance in vivo is not clear . Hydrolyzes galactosylceramides/GalCers, glucosylsphingosines/GlcSphs and galactosylsphingosines/GalSphs . However, the in vivo relevance of these activities is unclear . It can also hydrolyze a broad variety of dietary glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro and could therefore play a role in the metabolism of xenobiotics . Possesses transxylosylase activity in vitro using xylosylated ceramides/XylCers (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) as xylosyl donors and cholesterol as acceptor . Could also play a role in the catabolism of cytosolic sialyl free N-glycans .
PTM: The N-terminus is blocked.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 53696
Sequence Length: 469
Subcellular Location: Cytoplasm
EC: 3.2.1.21
|
Q6F754 | MPSKTSSRFANINPNVFVSTIMIIAIFLAIVILAPDAFELLTQQLKNWITESFSWFYVLSVAFFLIVLGYIACSSSGKIKLGPDHSQPDYSNSSWFAMLFTAGMGIGLMFFGIAEPIMHYVSPPSGEPETILAAQQSMRVTFFHWGLHAWGIYAIVALSLSYFAYRHDLPLKIRSSLYPLIGKKIYGPMGDAVDTFATIGTIFGVATTLGFGVTQISSGLNYLFGFEPTSFSKVVLIIIVSAMAALSVGLGLDKGVKRLAELNLVLAVTLLAFVFFTSATVYLLQTTIQNTGQYISNLFEMTFNLYAYQPNGWIGGWTIMYWAWWISWSPFVGMFIARVSRGRTIREFIIGVMLIPTGFTLIWMGFMGNAGLYSILHDGNLSLLNAVQRDSSVALFEFLHSLPFSGVMSLLATVLVVLFFVTSADSGALVVDYLTAKSEDSPVWQRLFWIVVMAGLAIILLLAGGLTALQSATIMSALPFTFIMLLICWGLIKALRIDSTKMQAIQEARTTPRAIQNPRSWQQRLGLIMHYPHSKVEVDAYIKKHVQRAFESLEREFKRRHLTVAISETDDGLQLKVDHHDEINFIYHVVSRETMPPSFMLEQEHNADVEKYFQAEVFLREGGQNYDVMDWTEEDLIQDIIDQYERHLYFLSVMRAQTGN | Function: Energy-dependent uptake of glycine betaine in response to high salinity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74117
Sequence Length: 660
Subcellular Location: Cell inner membrane
|
Q24SP9 | MNMGVDKKQNTVLYISSAIALLFVLWGVFLPENMANVVNKVFALLTTNFGWLYLLAVAIFIIFVFGIAISRYGKIKLGADDDKPEFSNFQWFAMLFGGGMGIGLVFWSVAEPIMHFNSPPFGEPGTVEAMQTSMRVVFFHWGIHAWVNFAIAGLALAYFQFRKGLPFLISSAFYPLIGDRIYGPIGKAIDILAVFATIFGIATSLGLGSSQIATGIQYIWGIPAGPLTISLVIAVITVIFTLATVSGLHKAMQSIANVKVWLSVAFMVFIFYFGGKVFILNTFTQSLGDYLQNFVGQTFWMANESWVGGWTIFYWAWWIAWAPFVGQFVARVSKGRTIREFVFAVTLLPVGFSFIWLAIYGGAAFNLDQISGGFIQNAVNADYTTALFALLQQMPLYAITGPLAILLIVTCFVGAADSATYVLAMLTSNGDMDPSKKLRSFWGIMQGAMTIVLIVVGGTAALKALQTASIASAFPFMLIMLVMCYSILKALRSDHP | Function: Probably acts in the uptake of glycine betaine. May function in the pathway that allows anaerobic methylotrophic growth of D.hafniense using glycine betaine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54338
Sequence Length: 496
Subcellular Location: Cell membrane
|
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.