ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q59S50 | MDDDDELLLNFAAPDTSSVAASKNQNVKVSGGRWKDRRKLQLALQGRTKKRQPETGVNLIPVDESKRKRDSEDKVQLDSNKRSKFTESKGENGGKGDSYVSSLFTNNQPTSHLAPTSTTKELTYLPSNAPMKDATNFSGLGLNEKLSIHLTDHLRFMHPTKIQQLVIPSLISTENDLFVKAQTGSGKTLAFVLPIFHKLMRENKFKINRESGLFAIILTPTRELATQIYGVLETLTRCHHWIVPGIVIGGEKKKSEKARLRKGCNILVATPGRLADHLENTKTLDISQLRWLVLDEGDKLMELGFEDTIAQITAKIDSNSKIADTAEKWQGLPSRRINMLCSATLHSNVKKLGSIVLKDPEMISVETASVAGTVSFDETIATTTSTAPDQLIQNVVVVPPKLRLVTLDALLLKISKHSAERTIVFFSCSDSVDFHFDVFTRDGKKFKKVTDEETGEVKTVLVSPEDDENDGLLTAPQLSDNTIIYKLHGSLSQQTRASTLQSFVKDNNSYNKILFCTDVASRGLDLPNVANVIEYDPPFTIDDHLHRIGRSARLGNEGNATLFLLPGIEEGYVDGKLRVAHPREGNLRVKNYEKILQEGFAQGNIKSKDNKLGKWDIHATTWHLDVERWLLEDQASHDEAVRAFTSHIRAYATHLSSEREFFNVKLLHLGHLAKSFGLRETPKKLGKSVGNNSNYSESKKGKKEDPRKKMLRMAKMAVKSASSEFNY | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81139
Sequence Length: 727
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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P0CQ95 | MADDIELNFAVPASGLVRQVAPKKGGRWTDRVRAKREARDAFKSMKANHLTVQNPSMPTVSASELVPKPAVIKPAPTSASVSRHPQPKSQVVAPPRFTNATAGPSRPAPSPQAASSNVPKSASIPAPATIKHRTSLPTNAFERPPLPPQAGPSRPHPAEKLKTPQFISSLFTSAPLPGVKSSVAPEISTGAPSNAPVDTTTFQGLGLNKLLINHLKGKMGVEKPTGIQRNCLPYMLSSPLNPDKKAGDEGPKEEPLRDVLIQAQTGSGKTLSYLLPIVQTLLPLSRLSYIDRSIGTLAIILAPTRELAQQISKVLEQLLHMSFAASKEGSDDEDEDDRPFTRWLVSGLLTGGSTRTHEKAKLRKGVPILVSTPGRLLDHLQNTMSFQCAKTMFLVLDEADRLMDLGFEETIQGIIKALEGRRRNEINIEKEMDKEGGGTMRWPFWDRGRLNVLCSATVDAKVERLAGAALRDPVLFRSEKDEAEAKKKAEGKDDAVIKALNEAQAIVIPQESEEKFTPPSQLSQKYVVLPTKLRLVALVALLRSLISSVAKGISVSNGTKVIVFLSSTDAVDFHWKLLGGVQMGQQGQQADGEKEEDEEEEGESVEERESDGESKAKKSKRKAKSKSTDDIVSLASPLFPNTTLHRLHGSLPLRTRLASLKAFATSSSQPSVLFATSVASRGLDLPLVRAVVQYDLPTEGGANEYVHRVGRTARAGKGGEAWAFVSPSEEGWVKWIEGKMGAAEGKSGVNLGQVGVEDVLRKGFGGKSYEYEARATDVQLSFENWVLASEQNAALARKAFASFVRAYSTHPLEEKQFFHTKLLHLGHLAKSFALREAPAQLASALSAGKSKRPKSKAASSATHPGKRKRDEDEDEMEERGGKELTARNETERRMYEAVRKQGRTIKSGGKLGEFSGKGQNKGQKAAATGGEFHIVNTGELERLVARRK | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 102839
Sequence Length: 948
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q5BGX6 | MADDGMLLNFALPSDVIKPQTKIKGGSWRERLSVKKIAARRATNPKRTADGDGNKDGNESGPRNPNRIQVSGSRPAKRQKTDGGFQKLGEGQAHGQGSGQSKGPKKGQGGSVVSSLFSKNPRPRNAVEEDKNDEPMEDAKPTNAPLIDGLDTFTNLGLSPTLAAHLLTKLELKAPTAIQKASITQLLKEETDAFIQAETGSGKTLAYLLPLVQRIMALSRAKNEGDAKGDTSVHRDSGLFAIILAPTRELCKQISVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEGDRLMELGFEKELQEIISKLDARQRPSRIPGVPAKRATILCSATLKMNVQKLGEISLKDAVHIKADPADEDGEKTAEDKDGDAFRVPAQLKQSYAIVAAKLRLVTLTAFMKRTFMRKGSVMKAIIFVSCADSVNFHFEVFTRKLAEQLEGDNPDEGSDSEHEKEKEKEKPTPASTHGTVAPATAFSNSSNAVTMYKLHGSLPQHVRTSTLSSFAKNRDPSVLICTDVASRGLDLPNVDLVVEYDPAFSADEHLHRIGRTARLGRDGRALVFLLPGCEENYVEILKRGYRDGGKALTRSTTDDILKRGFGGNIESQKWQLELERWALDNPEYLEMARRAYQSHIRAYATHVANERHIFNIKELHLGHLAKSFALRDRPGKINVPGLRPGKEDTKKDFKAERKSAGGKKRKATGYGGGRDDDDDDDRPSATTDTTLAAQKMRAKMKEQLAGASEFNLA | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85214
Sequence Length: 778
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q96286 | MALSAIGFEGYEKRLEVTFFEPSIFQDSKGLGLRALTKSQLDEILTPAACTIVSSLSNDQLDSYVLSESSFFVYPYKVIIKTCGTTKLLLSIPPLLKLAGELSLSVKSVKYTRGSFLCPGGQPFPHRSFSEEVSVLDGHFTQLGLNSVAYLMGNDDETKKWHVYAASAQDSSNCNNNVYTLEMCMTGLDREKAAVFYKDEADKTGSMTDNSGIRKILPKSEICDFEFEPCGYSMNSIEGDAISTIHVTPEDGFSYASFEAVGYDFNTLDLSQLVTRVLSCFEPKQFSVAVHSSVGANSYKPEITVDLEDYGCRERTFESLGEESGTVMYQTFEKLGKYCGSPRSTLKCEWSSNNSCSSEDEKDEGI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.
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.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 40403
Sequence Length: 366
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q42613 | MSLSAIGFEGLRERLEVSFFEPSLFLDTHGKGLRALSKSQIDEILAPAECTIVSSLSNDELDSYVLSESSLFIFPYKIIIKTCGTTKLLLSIEPLLRLAGGVSLEVKSVRYTRGSFLCPGGQPFPQRNLSEEVSVLDGHFAKMGLSSVAYLMGDDDETKKWHVYSASAPAKNSNGDNNVYTLEMCMSGLDKDKASVFFKNESSSAGSMTDNSGIRKILPQSQICDFEFEPCGYSMNSVEGDASSTIHVTPEDGFSYASFEAVGYDFTTMDLSQLVSRVLTCFEPKQFSVAVHSSVAQKSYDHSGLSVDLEDYGCRETTVGVSRRRERNSDVSEVREAGNVLWFSEIDLKCEWSSNSSCTSEDEKEEGI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
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 (By similarity).
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 40453
Sequence Length: 368
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q9S7T9 | MAMSAIGFEGYEKRLEVTFFEPGLFLDTQGKGLRALAKSQIDEILQPAECTIVSSLSNDQLDSYVLSESSLFIFPYKIVIKTCGTTKLLLSIEPLLRLAGELSLDVKAVRYTRGSFLCPGGQPFPHRNFSEEVSVLDGHFAKLGLSSVAYLMGNDDETKKWHVYSASSANSNNKNNVYTLEMCMTGLDKDKASVFYKNESSSAGSMTDNSGIRKILPQSQICDFEFEPCGYSMNSIEGDAISTIHVTPEDGFSYASFEAVGYDFTTMDLSHLVSKVLTCFKPKQFSVAVHSTVAQKSYDSGLSVDLDDYGCKESTMESLGEERGTVMYQRFEKLGRYCGSPRSTLKCEWSSNSSCNSEDEKE | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.
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 (By similarity).
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 40010
Sequence Length: 362
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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D3Z6H8 | MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDHLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
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.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 38295
Sequence Length: 334
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q9LSU6 | MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDNNPQRWHVYSASSTEESAVCDKPVYTLEMCMTGLDNIKASVFFKTNSVSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSIEGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQERELEELGLGGSVLYQRFVKTVECCSPKSTLGFC | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.
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.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 38290
Sequence Length: 349
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q11TJ6 | MILSGLEIKDKLGSDIVIEPYDDSRLNPNSYNLRLHNELLVYDNNELDMKKPNTASPLIIPEEGLLLETGKLYLGRTIEYTESHNYVPMLEGRSSIGRLGLFVHVTAGFGDVGFCGFWTLEIFCVHPIRVYPGVEICQIFYHTIEGKYENYKSGKYQHNKGIQPSLLYKDFEK | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 19809
Sequence Length: 173
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.
EC: 3.5.4.30
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B8DYK8 | MILSDKDIKKYLEERKLVIHPIDDPQKQIQPSSVDLRLGNSFLHFKVEGRAYIDPTKDNPQDLMEIIEIEEGKPFFLRPGEFVLGTTIETVKLPDDLVARVDGRSSLGRLGIIVHATAGYVDPGFCGQITLELSNINRVPVALYPGMRICQISFYKLTSPAETPYYKKAGSKYHNQKGPTASKLNIDFCVKEDK | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 21824
Sequence Length: 194
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.
EC: 3.5.4.30
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Q9KFV3 | MILSGKTISEKLTEKELEITPLTEEQIQPASVDLRLGPHFVTIDDSKEAVISFERPIRYREWTTSDETIVLPPHTFLLATTMETVKLPNHLTAFVEGRSSVGRLGLFIQNAGWVDPGFNGQITLELFNANRLPIELPIGRRICQLVFAEVTGEVAPYQGKYLFQKGATMSEIYKDAF | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 19897
Sequence Length: 177
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.
EC: 3.5.4.30
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B4U7Y7 | MILSDKTILDYIKSSKIIVEPFDESSLQCSSLDLRLSNSIAFYEELDIIDIKSPIQAKTVTFEEYFIINPGEFLLASTMEYIKLPEFITAFVEGRSSLGRLGLFIENAGWVDAGFEGQITLELYNANKYPIKLYKGMRICQLVFAKLDEIPSKVYRGKYLCQKGATPSKIFMDFDKK | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 20186
Sequence Length: 177
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.
EC: 3.5.4.30
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B0SH49 | MILTGKEILKRLGSDIKIEPYDEKLLNPNSYNLRLHEDLLVYSEFPLDMKKPNPVRTLKIPEEGLLLEPGNLYLGRTIEFTETHNLVPMLEGRSSIGRLGMFVHITAGFGDVGFKGFWTLEIQVTHPLRVYSGVQICQIFYHTVEGEISEYKSGKYQANQGIQPSLLYKDFEKK | Function: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Catalytic Activity: dCTP + 2 H2O = diphosphate + dUMP + NH4(+)
Sequence Mass (Da): 19933
Sequence Length: 174
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.
EC: 3.5.4.30
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Q42472 | MVLTKTATNDESVCTMFGSRYVRTTLPKYEIGENSIPKDAAYQIIKDELMLDGNPRLNLASFVTTWMEPECDKLIMDSINKNYVDMDEYPVTTELQNRCVNIIARLFNAPLEESETAVGVGTVGSSEAIMLAGLAFKRKWQNKRKAEGKPYDKPNIVTGANVQVCWEKFARYFEVELKEVNLSEGYYVMDPDKAAEMVDENTICVAAILGSTLNGEFEDVKRLNDLLVKKNEETGWNTPIHVDAASGGFIAPFIYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVVWRAAEDLPEELIFHINYLGADQPTFTLNFSKGSSQIIAQYYQLIRLGFEGYKNVMENCIENMVVLKEGIEKTERFNIVSKDQGVPVVAFSLKDHSFHNEFEISEMLRRFGWIVPAYTMPADAQHITVLRVVIREDFSRTLAERLVADISKVLHELDTLPSKISKKMGIEGIAENVKEKKMEKEILMEVIVGWRKFVKERKKMNGVC | Function: Catalyzes the conversion of glutamate to 4-aminobutanoate (GABA). The calmodulin-binding is calcium-dependent and it is proposed to directly or indirectly form a calcium regulated control of GABA biosynthesis.
Catalytic Activity: H(+) + L-glutamate = 4-aminobutanoate + CO2
Sequence Mass (Da): 56141
Sequence Length: 494
Domain: The C-terminus (463-494) binds calmodulin in a calcium-dependent fashion.
EC: 4.1.1.15
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Q05329 | MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL | Function: Catalyzes the production of GABA.
PTM: Phosphorylated; which does not affect kinetic parameters or subcellular location.
Location Topology: Lipid-anchor
Catalytic Activity: H(+) + L-glutamate = 4-aminobutanoate + CO2
Sequence Mass (Da): 65411
Sequence Length: 585
Subcellular Location: Cytoplasm
EC: 4.1.1.15
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Q9ZPS3 | MVLSKTVSESDVSIHSTFASRYVRNSLPRFEMPENSIPKEAAYQIINDELMLDGNPRLNLASFVTTWMEPECDKLMMESINKNYVDMDEYPVTTELQNRCVNMIARLFNAPLGDGEAAVGVGTVGSSEAIMLAGLAFKRQWQNKRKAQGLPYDKPNIVTGANVQVCWEKFARYFEVELKEVNLREDYYVMDPVKAVEMVDENTICVAAILGSTLTGEFEDVKLLNDLLVEKNKQTGWDTPIHVDAASGGFIAPFLYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVVWRTKTDLPDELIFHINYLGADQPTFTLNFSKGSSQVIAQYYQLIRLGFEGYRNVMDNCRENMMVLRQGLEKTGRFKIVSKENGVPLVAFSLKDSSRHNEFEVAHTLRRFGWIVPAYTMPADAQHVTVLRVVIREDFSRTLAERLVADFEKVLHELDTLPARVHAKMANGKVNGVKKTPEETQREVTAYWKKLLETKKTNKNTIC | Function: Catalyzes the production of GABA. The calmodulin-binding is calcium-dependent and it is proposed that this may, directly or indirectly, form a calcium regulated control of GABA biosynthesis (By similarity).
Catalytic Activity: H(+) + L-glutamate = 4-aminobutanoate + CO2
Sequence Mass (Da): 56005
Sequence Length: 493
EC: 4.1.1.15
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P69909 | MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT | Function: Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity).
Catalytic Activity: H(+) + L-glutamate = 4-aminobutanoate + CO2
Sequence Mass (Da): 52685
Sequence Length: 466
EC: 4.1.1.15
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Q05924 | MIRLPRLYQRYLLYLVVFVVIALFYFLQAPRVEEHIGFDLALPISHVDNLWFQNKGLEGFSNDDKLVVNIGYDECFHIGRFYEGCFNRHELKSTLTDGHQYLQRKRIHKDLRGSFGRRWFGKSEYLYYDVLYPALVDYFGSNLEKLNVEAVTGISKYPKDKSLPFMDVSITFEPISIELLQKRSYISDINILFGVDCIQPIANWTLQKEFPLVKYRYSEPAYLTYKFVGTRPVDTGAQRLQETDEGKFKIVQLADLHLGVGESECIDEYPKHEACKADPKTETFVQQVLDIEKPQLVVFTGDQIMGDRSIQDSETVLLKAVAPVIARKIPWAMVWGNHDDEGSLTRWQLSEIASVLPYSLFKFSPHDTHDNTFGVGNYIYQIFSNNDTEVPVGTLYFLDSHKYSTVGKIYPGYDWIKESQWKYIEDYHDVNLKFKTGLSMAFFHIPLPEYLNIESKTHPGEKNPLIGMYKEGVTAPKYNSEGITTLDRLSVDVVSCGHDHCNDYCLRDDSTPNKIWLCYGGGGGEGGYAGYGGTERRIRIYEINVNENNIHTWKRLNGSPKEIFDFQSMLDGNSPESV | Function: Required for cell cycle progression. Has a role in the completion of START.
Sequence Mass (Da): 66463
Sequence Length: 578
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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P0AEE1 | MRNLVKYVGIGLLVMGLAACDDKDTNATAQGSVAESNATGNPVNLLDGKLSFSLPADMTDQSGKLGTQANNMHVWSDATGQKAVIVIMGDDPKEDLAVLAKRLEDQQRSRDPQLQVVTNKAIELKGHKMQQLDSIISAKGQTAYSSVILGNVGNQLLTMQITLPADDQQKAQTTAENIINTLVIQ | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis . Essential for lipoprotein maturation under conditions where membrane fluidity may be altered .
Location Topology: Lipid-anchor
Sequence Mass (Da): 19787
Sequence Length: 185
Subcellular Location: Cell membrane
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P85870 | SLLSLIRKLIT | Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide . Has antibacterial activity against the Gram-positive bacteria S.aureus CCT 6538 (MIC=40 uM), S.saprophyticus (MIC=40 um), B.subtilis CCT 2471 (MIC=40 uM), and B.thuringiensis (MIC=40 uM), and against the Gram-negative bacteria E.coli ATCC 25922 (MIC=80), E.coli CCT 1371 (MIC=160), K.pneumonia ATCC 13883 (MIC=80), and A.faecalis ATCC 8750 (MIC=40) . Has antifungal activity against C.albicans (MIC=40 uM) . At high concentrations exhibits activity in stimulating degranulation from rat peritoneal mast cells . Has very weak hemolytic activity towards human and mouse erythrocytes . In vitro, inhibits the growth of L.major promastigotes (IC(50)=72 uM) .
PTM: The natural peptide is not C-terminally amidated. However, amidated synthetic analogs show a much more potent activity in all the biological assays.
Sequence Mass (Da): 1257
Sequence Length: 11
Subcellular Location: Secreted
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Q9FF86 | MKIKIMSKTHVKPTKPVLGKKQFHLTTFDLPYLAFYYNQKFLLYKFQNLLDLEEPTFQNEVVENLKDGLGLVLEDFYQLAGKLAKDDEGVFRVEYDAEDSEINGVEFSVAHAADVTVDDLTAEDGTAKFKELVPYNGILNLEGLSRPLLAVQVTKLKDGLAMGLAFNHAVLDGTSTWHFMSSWAEICRGAQSISTQPFLDRSKARDTRVKLDLTAPKDPNETSNGEDAANPTVEPPQLVEKIFRFSDFAVHTIKSRANSVIPSDSSKPFSTFQSLTSHIWRHVTLARGLKPEDITIFTVFADCRRRVDPPMPEEYFGNLIQAIFTGTAAGLLAAHGPEFGASVIQKAIAAHDASVIDARNDEWEKSPKIFQFKDAGVNCVAVGSSPRFRVYEVDFGFGKPETVRSGSNNRFNGMMYLYQGKAGGISIDVEITLEASVMEKLVKSKEFLLSEEEEEDDGKKLTNGNGHVNGNGNGYVNGNGNGFV | Function: Required for incorporation of 9(10),16-dihydroxy-hexadecanoic acid into cutin.
Sequence Mass (Da): 53514
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 2.3.1.-
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Q39761 | MASQVSQMPSSSPLSSNKDEMRPKADFQPSIWGDLFLNCPDKNIDAETEKRHQQLKEEVRKMIVAPMANSTQKLAFIDSVQRLGVSYHFTKEIEDELENIYHNNNDAENDLYTTSIRFRLLREHGYNVSCDVFNKFKDEQGNFKSSVTSDVRGLLELYQASYLRVHGEDILDEAISFTTHHLSLAVASLDHPLSEEVSHALKQSIRRGLPRVEARHYLSVYQDIESHNKALLEFAKIDFNMLQFLHRKELSEICRWWKDLDFQRKLPYARDRVVEGYFWISGVYFEPQYSLGRKMLTKVIAMASIVDDTYDSYATYEELIPYTNAIERWDIKCIDEIPEYMKPSYKALLDVYEEMVQLVAEHGRQYRVEYAKNAMIRLAQSYLVEAKWTLQNYKPSFEEFKANALPTCGYAMLAITSFVGMGDIVTPETFKWAASDPKIIQASTIICRFMDDVAEHKFKHRREDDCSAIECYMEEYGVTAQEAYDVFNKHVESAWKDLNQEFLKPTEMPTEVLNRSLNLARVMDVLYREGDGYTYVGKAAKGGITSLLIEPIAL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Responsible for the cyclization of trans,trans-farnesyl diphosphate (FPP) to (+)-delta cadinene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (1S,8aR)-delta-cadinene + diphosphate
Sequence Mass (Da): 64138
Sequence Length: 554
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.13
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Q9HU17 | MHALARVWARLEEGLIAFLLAAMTLVTFVYVVLNNLYTLLYDLADLWEGGNETLLAIGDGVLTLAQEMTWSNALTKALFAWLIFLGIAYGVRTAGHLGVDVLVKLASRPVQRVLGVIACLACLGYAGLLCVASYDWVKTLFIAGIGAEDLDHFGIRQWHIGLIVPVGFALVFIRFAEILVRILRNRQTGLGLADEAADALKLTEHEEPKA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22963
Sequence Length: 210
Subcellular Location: Cell inner membrane
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O07837 | MLRILDRAEEVLIAALIATATVLIFVSVTHRFTLGFVADFVGFFRGHGMTGAAAAAKSLYTTLRGINLVWAQELCIILFVWMAKFGAAYGVRTGIHVGIDVLINRLDAPKRRFFILLGLGAGALFTGIIATLGANFVLHMYHASSTSPDLELPMWLVYLAIPMGSSLMCFRFLQVAFGFARTGELPHHDHGHVDGVDTENEGIDAEGDVLLHSPLTPRDLVEKPKDN | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24763
Sequence Length: 227
Subcellular Location: Cell inner membrane
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Q9KQS0 | MSVRHTIRAMYHMEQSWFSRVGQFTDSIEEFLIAFFMGAMTLLTFANVIMRYLFNDNILWALEGTVFMFAWMVLVGASFGVKRHFHIGVDVLINIAPARLRKLYALVAVACCLAFSILLLIGSWNYWHPFITERAWYETDDIPMPDMLQFLADWVNEGERYEKLPRFIPYAALPIGMALLTFRFLQIAWQIITGKLDRMIAGHEAEEDLEALKAELSEAGEAMMPKTQGKEK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26773
Sequence Length: 232
Subcellular Location: Cell inner membrane
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P96602 | MARKEWKVLLIEDDPMVQEVNKDFITTVKGVTVCATAGNGEEGMKLIKEEQPDLVILDVYMPKKDGIKTLQEIRKQKLEVDVIVVSAAKDKETISLMLQNGAVDYILKPFKLERMRQALEKYKQYKQKIEANDTLSQEQLDAILNIPQQAVQDLPKGLNHFTMNEVTAFLKQQTASLSAEEVAKALGIARVTARRYLDYLEKTGIIKLDVQYGGVGRPVNRYVLKG | Function: Member of the two-component regulatory system DctS/DctR. Essential for expression of dctP.
PTM: Phosphorylated by DctS.
Sequence Mass (Da): 25539
Sequence Length: 226
Subcellular Location: Cytoplasm
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Q9K998 | MAKEPLIRVLLIEDDPMVQEVNRMFVEKLSGFTIVGTTATGEEGMVKTRELQPDLILLDIFMPKQDGLSFIKQIREQYIDVDIIAVTAANDTKTIKTLLRYGVMDYLVKPFTFERLKAALTQYEEMFRKMQKEAELSQDSLDEMIKQKQAQANMDDLPKGLHAHTLQQVIERLEELDEPKSAEEIGRDVGLARVTVRRYLNYLESVGQVEMDLTYGSIGRPIQTYKLKQG | Function: Member of the two-component regulatory system DctS/DctR. Essential for expression of DctP (By similarity).
PTM: Phosphorylated by DctS.
Sequence Mass (Da): 26376
Sequence Length: 230
Subcellular Location: Cytoplasm
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P37740 | MSFTVHIVDDEESLRDSLGFLFASRGIATRTWAAGADLLAEWPLADCGCLILDVRMEGMSGPQLLDALQARPEGLVPPVIFLTGHADVPLAVQSLKAGAFDFVEKPFNDNHIVDIALSAIAAHEGRLAEAQAREAVAARRASLSAREAEVMALMLEGLMNKQIAERLGIAMRTVEVHRSRVLAKMGARNIADLARMT | Function: Member of the two-component regulatory system DctS/DctR involved in the transport of C4-dicarboxylates. DctR functions as a transcriptional repressor of genes for C4-dicarboxylate transport.
PTM: Phosphorylated by DctS.
Sequence Mass (Da): 21271
Sequence Length: 197
Subcellular Location: Cytoplasm
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P96601 | MNKKKLSIRWKITILSYILVIFSFLIGGIVLIGNIQHTEERELKKRLMNTARTVSEMTEVKEALARKKQTEAVRHAVEEIRMINEADYIVVMDMNHIRYTHPVSTSIGKKSEGADEEAAFAEHIYFSEAKGEIGTAVRAFYPVKDQDLNQIGVVLVGKTLPGIADILLHLKRDIAFIVVLTLGFGLAGSFLLARHIKKQMFQLEPHEIVRMYEERTATFHSMNEGVIAIDNRLVITIFNEKAKQIFEVQGDLIGKVIWEVLKDSRLPEIVERNKAVYNEEIRVSGKVIMSSRIPIVMKKKVIGAVAIFQDRTEAAKMAEELTGVRNFVEALRVQNHEHMNKLHTIAGLIQLGKSEKALQLAFQASTEQENVTEFLHRSIQNDAAAGLLLSKIRRGRELGIAVHIDENSSLQQFPEHVDQHDIVVLLGNLIENAFGSFETVQSEDKRIDISIEQTDDILAILIEDNGCGIEPTHMPRLYDKGFTVNKTGGTGYGLYLVKQIIDKGSGTIEVDSHAGQGTSFSIVFPMKGEEAQHGS | Function: Member of the two-component regulatory system DctS/DctR. Probably activates DctR by phosphorylation (By similarity). Essential for expression of dctP.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59942
Sequence Length: 535
Subcellular Location: Cell membrane
EC: 2.7.13.3
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Q5ZTY0 | MFDLNQSLFLRALRRQPVERTPIWIMRQAGRYLPEYRKVREHAGDFLNLCKNPELACEVTLQPLRRYALDAAILFSDILTIPDAMGLGLYFAEGEGPRFTNPLQDTKAIHTLKIPSIPESLSYVFDAARLIRQEMPKELPLIGFSGSPWTLACYMVEGGSSRDFKRILNLIYTEKEAAHLLLNKLAVSVTAYLIEQIKAGVNAVMIFDTWGGVLTPQNYKDFSLAYMHQIVQQLKKEYPDIPVILFTKNGGQWLEWMAETGCDALGVDWTCDLASARKRVGGKVALQGNLDPAVLLTTKNCIRSEVGSVLASYGYGTGHIFNLGHGITPDVPPENVAIMIEAVHEISPQYHL | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39383
Sequence Length: 352
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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P16891 | MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEISLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPIRTAEQVAAVHDLDPEEATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSKTYANIKHLAFSEPTILHELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDTFALPYQQRVFQQVKAKHPEVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRLGPDIGLQGNIDPGVLFGSQDFIRDRILDTVRKAGNQRHILNLGHGILPGTPEDNARHFFETAKNLDQLLAASH | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39278
Sequence Length: 354
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q2JX97 | MSHSPAQLSASPSSVGDGDRLLRAARGEVVDRPPVWMMRQAGRYMAAYRELQSKYTFKQRCEIPELAIEISLQPFRAFAPDGVIMFSDILTPLEGMGIPFELVEQQGPIIDPPIRSQAQVEQIRLLEPEESLPFIKTILSTLRREVEGKATLLGFVGSPWTLACYAVEGRSSKDYAHIKSLAFTQPQVLHQLLSKLADSIARYVIYQIECGAQVVQLFDTWAGQLSPGDYETWALPYQKQIVDQVKARCPQVPLILYINGSAALLERVGKAGIDVFSLDWMSDMAEARARLGSLAVQGNLDPMVLLGSPKFIRQRTLEVIQKAGSRGHIMNLGHGVHHTTPEANVHHFFETVRQAAELLKAL | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 40242
Sequence Length: 362
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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O08557 | MAGLSHPSVFGRATHAVVRAPPESLCRHALRRSQGEEVDFARAERQHQLYVGVLGSKLGLQVVQLPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADSLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDMAANCIYLNIPSKGHVLLHRTPEEYPESAKVYEKLKDHLLIPVSNSEMEKVDGLLTCCSVFINKKTDS | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Mass (Da): 31426
Sequence Length: 285
EC: 3.5.3.18
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O95865 | MGTPGEGLGRCSHALIRGVPESLASGEGAGAGLPALDLAKAQREHGVLGGKLRQRLGLQLLELPPEESLPLGPLLGDTAVIQGDTALITRPWSPARRPEVDGVRKALQDLGLRIVEIGDENATLDGTDVLFTGREFFVGLSKWTNHRGAEIVADTFRDFAVSTVPVSGPSHLRGLCGMGGPRTVVAGSSDAAQKAVRAMAVLTDHPYASLTLPDDAAADCLFLRPGLPGVPPFLLHRGGGDLPNSQEALQKLSDVTLVPVSCSELEKAGAGLSSLCLVLSTRPHS | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Mass (Da): 29644
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 3.5.3.18
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P71889 | MENTQRPSFDCEIRAKYRWFMTDSYVAAARLGSPARRTPRTRRYAMTPPAFFAVAYAINPWMDVTAPVDVQVAQAQWEHLHQTYLRLGHSVDLIEPISGLPDMVYTANGGFIAHDIAVVARFRFPERAGESRAYASWMSSVGYRPVTTRHVNEGQGDLLMVGERVLAGYGFRTDQRAHAEIAAVLGLPVVSLELVDPRFYHLDTALAVLDDHTIAYYPPAFSTAAQEQLSALFPDAIVVGSADAFVFGLNAVSDGLNVVLPVAAMGFAAQLRAAGFEPVGVDLSELLKGGGSVKCCTLEIHP | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA).
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Mass (Da): 32960
Sequence Length: 302
EC: 3.5.3.18
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Q9I4E3 | MFKHIIARTPARSLVDGLTSSHLGKPDYAKALEQHNAYIRALQTCDVDITLLPPDERFPDSVFVEDPVLCTSRCAIITRPGAESRRGETEIIEETVQRFYPGKVERIEAPGTVEAGDIMMVGDHFYIGESARTNAEGARQMIAILEKHGLSGSVVRLEKVLHLKTGLAYLEHNNLLAAGEFVSKPEFQDFNIIEIPEEESYAANCIWVNERVIMPAGYPRTREKIARLGYRVIEVDTSEYRKIDGGVSCMSLRF | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA).
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Mass (Da): 28470
Sequence Length: 254
EC: 3.5.3.18
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Q9X7M4 | MPSKKALVRRPSPRLAEGLVTHVEREKVDHGLALEQWDAYVEALGAHGWETLEVDPADDCPDSVFVEDAVVVFRNVALITRPGAESRRAETAGVEEAVARLGCSVNWVWEPGTLDGGDVLKIGDTIYVGRGGRTNAAGVQQLRAAFEPLGARVVAVPVSKVLHLKSAVTALPDGTVIGHIPLTDVPSLFPRFLPVPEESGAHVVLLGGSRLLMAASAPKTAELLADLGHEPVLVDIGEFEKLEGCVTCLSVRLRELYD | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA).
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Mass (Da): 27571
Sequence Length: 258
EC: 3.5.3.18
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P32270 | MTFDDLTEGQKNAFNIVMKAIKEKKHHVTINGPAGTGKTTLTKFIIEALISTGGTGIILAAPTHAAKKILSKLSGKEASTIHSILKINPVTYEENVLFEQKEVPDLAKCRVLICDEVSMYDRKLFKILLSTIPPWCTIIGIGDNKQIRPVEPGENTAYISPFFTHKDFYQCELTEVKRSNAPIIDVATDVRNGKWNYDKVVDGHGVRGFTGDTALRDFMVNYFSIVKSLDDLFENRVMAFTNKSVDKLNSIIRKKIFETDKDFIVGEIIVMQEPLFKTYKIDGKPVSEIIFNNGQLVRIIEAEYTSTFVKARGVPGEYLIRHWDLTVETYGDDEYYREKIKIISSDEELYKFNLFLAKTAETYKNWNKGGKAPWSDFWDAKSQFSKVKALPASTFHKAQGMSVDRAFIYTPCIHYADVELAQQLLYVGVTRGRYDVFYV | Function: DNA helicase that stimulates viral DNA replication and recombination. Plays a role in T4 DNA replication initiation by selecting and activating DNA origins. Acts by dissociating and reassociating with the DNA molecule being unwound. Unwinds DNA as a monomer in a 5'-to-3' direction at a rate of 250 bp/s and can efficiently displace proteins from the DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49897
Sequence Length: 439
EC: 3.6.4.12
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B9E560 | MKVGIIMGGISSEREVSLNSGKSIINYMDKNKYEIVPIVIDKKNDVFEKVKDIDFAFIALHGKFGEDGIIQSVFQTMDIPYSGCSPLTSGICMDKDISKKLLYSANINTAEWICIKSIENIDYDYLEKMGYPVVVKPNSGGSSVATTIIEKSEDIEEAARLAFNYDEEVMIEKYIEGDEITCCILDGTALPILAIKPNKGSFFDYTSKYADGGSEEIVVEFEKPLQSKIEEISLKCWELFKCKGYVRVDMILKDKVPYVLELNTLPGLTKNSLFPKSANGVNISFTELLDKIIQCSM | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33188
Sequence Length: 297
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A0Q323 | MKKKVAILFGGQSTEHEVSRVSASSVLKNIDLSKYDVYPIGITKDGKWFEYTGAIDKIESGEWEKDEFYKNPNGQEILFNREVDVVFPVMHGLYGEDGTIQGLCKLLTIPCVGPGVMSSAVCMDKVYTKYVLENFGVKQADYVVVNAHDYKNNKMDIISTIENKLGYDVFIKPSNSGSSVGISKAHNREELEAGLEEALKFDRKVLVEVALNAREIEVAVLGNDEPVAATPGEIVPANEFYDYEAKYSNAQSKLLLPANLSPEKLEKVKELAVRIFKMLDCAGMSRVDFLVDKETEEVYLNEINTIPGFTKISMYPKMWQAEGKAYGELISEIIELAVERDNK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38355
Sequence Length: 343
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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B5Y8C8 | MNIVVLFGGTSPEREISLKSGENIAATLRARGHQVETLDTAVPNFVEQLMQLKPDCVFPALHGADGEDGKIQGLLSILHIPYVGSDVRASVITMDKYLTKLVALQSGIPTPSFIYVYDPHLVPDYWDVERKLGSPFIVKPCDVGSTIGLSLVRSASEYEVALEEAFRFSDRLLLEEFIDGFEVTVGLFRLGGDFLVLPPIYVVKPDRIFDYDTKYKPGGAKHVYDLPISVEARERLTSYSKRICKIVGIGGVARLDYIVKDETPYLLEINSIPGMTAESLVPDEVRHAGRDFGEFLEDLIKDAL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33710
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q8NQV2 | MSNSNSGKVRVAVVYGGRSSEHSVSCVSAGAIMAHLDPEKYDVIPVGITVDGAWVVGETDPQKLTLIDRTMPEVEHHEEVRPSLDPAHRGEFHFSDGSLYATADVIFPVLHGRFGEDGTVQGLFALSDIPVVGPGVLASAAGMDKEYTKKLMAAEGLPVGREVILRDRTELTEAEKNLLGLPVFVKPARGGSSIGISRVTAWEDFNKAVGLARAHDEKVIVESEIVGSEVECGVLQYPDGRIVASVPALLSGTESGAGGFYDFDTKYLDNVVTAEIPAPLDEKTTELIQSLAVESFQALACEGLARVDFFVTANGPVLNEINTMPGFTPISMYPQMFTASGVAYEELLDVLVQQALHRDN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38560
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A9KGD2 | MAEKLHISVLCGGQSTEHEISIQSAKNIVNTLDAAKYLISVIFIDHVGRWYLIDQPEMFLAHSPDHLVKEGSARPITIAFGDAAKPWQSLNGDGRRYSADCVFPMVHGTQGEDGALQGLLELLNLPYVGANVQSSAVCMEKDLTKTVLRAGGIPVVDWHTLSPRDATEGVYQRLLDRWGTSELFVKAVSLGSSVATLPVKTETEFTKAVKEVFRYDDRLMVEPRIRGREIECAVLGNGAPKASLPGEIIPHHDYYSYDAKYLDPNGATTTTSVDLSESVTKQIQQIAIDAFKMVHCSGMARVDFFVTPNNKVLVNEINTIPGFTNISMYPKMWEASGLPCPNLLDQLIELAIDRHQEQQKLIRCYEVKARSL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 41218
Sequence Length: 372
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q316H9 | MRILLIAGGWSEERDVSLSGARGIHAALERLGHQVTLFDPCRTLAGLLEAAQAHDFAFLNLHGQPGEDGLVQALLETAGVPYQGSGPAGSFLALNKAAAKEVFVRNGLPTPEWVFLPAHPGADWEPPFAFPAFIKSNNGGSSLALHRVSCPGELARALDELFTRGGEAIIEPAVEGVEVTCGVLGDEALPPILIRPLGAGFFDYASKYTPGQAEELCPAPLPGEVTAKVREYALRAHRALGLRGYSRSDFILTPAGALSLLEVNTLPGMTATSLLPQEAAAVGISFDGLIGRLIELGLAAHGKQQEKA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32382
Sequence Length: 308
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q13TZ4 | MSSIDPKQFGKVAVLLGGNSAEREVSLNSGRLVLQGLRDAGIDAHPFDPAERPLAALKEEGFVRAFNALHGGYGENGQIQGALDFYGIRYTGSGVLGSALGLDKFRTKLVWQQLGIPTPPFEAVLRGDDYEARAKEIVAKLGLPLFVKPASEGSSVAVIKVKSADALPAALIEAVKFDRIVVVEKSIEGGGEYTACIAGNLDLPVIRIVPAGEFYDYHAKYIANDTQYLIPCGLTADEEARLKVLARRAFDVLGCTDWGRADFMLDADGNPYFLEVNTAPGMTDHSLPPKAARAVGISYQELVVAVLALTLKD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33535
Sequence Length: 313
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q03EM9 | MKIAVLAGGKSTERNVSLSSGSKITNALRSKGYDATMIDLFLGYELEDGQSYEDVFKSSNTSTDYEISDAVLTEEDIEELRTDGTVGLFGKNVLPILQAADFVFLALHGGDGENGKVQAVLDLNHIKYTGSGSLASGIAMDKAISKEIMLYNNIKTAQFAVLHAKDGIHPQLAFDYPMVVKPNSGGSSIGTRIVHDEAELAESLKDAYRFDDEIIVEEFITGREFSLGVVNGQAMPAIEIVVNDGWYDYEHKFQTGSTTKFVTPPEIEDDVHDEMKRVAVQTMDALGMTNYGRVDFLTNDTGVYVIEANNLPGMTPLSLLPQEAEAAGISYEDLCESIVLGKQKLYDELKK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38351
Sequence Length: 351
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A1AU58 | MNDIRSRKIAVLMGGLSAEREVSLASGAAVCQALVARGFDALSVDVARDLPLVLSREGIGAAFIALHGRYGEDGCVQGLLELMAIPYTGSGVLASALAMHKLYSKQAFVSAGILTAPFHHFRRGERVSLSHLSFGLPLVVKPVQEGSSVGISIVKEESQLAAAVKLAFRHDDEILVEQFIKGQEVQVGILDDRPMGAIEIVSRNEFYDFEAKYTDGMAEHFFPARLEKGLYEEALRVGLAAHHALGCRCYSRVDLLVTPAGECYVLEVNTLPGMTALSLLPEIAAKGADLPFEELVERIILSADLSVKTG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33365
Sequence Length: 310
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A5D2F9 | MTLKVGVLMGGRSSEREVSLKTGEAVYNALKVKNYLAVKIDVGLDVVERIKEERIDLAFIALHGRYGEDGTIQGLLEMLDIPYTGSGVLASALAMDKAATKKIIQYEGLPTPPFMLVEKKEALKESLQACSERICREMGLPLVVKAPTQGSTIGMSFVHKEEDMAGALELAYDYDPVALVEQFIRGTEVTASILGNEEPVALPLIEIVSATGVYDYKAKYTAGMSDHIIPPRIPEKQQNAIKKLAVSTFKSLGCRGLARVDFIVDKQGNPFILEVNTIPGMTATSLFPDAARAAGIEFPDLIEKLVELAMENCGIRRR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34662
Sequence Length: 318
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q4FPK8 | MTKKILILSGGISKERLISLDTGKQVAKELIKNGYKVLISEPDKNLSKNITSFKPDVIFNALHGQFGEDGYIQAILETKKIPYTHSGVIASSIAMDKEISKKIFIKNKILTPKYIKFNHKKNKLNIIKLIEKNLKFPVVVKPINEGSSVHVYICDKTNILKNLKVLKSYNEILIEEFIPGREIQVAIMNNKSLGAIELEPRRKFYDYEAKYNSSAKTKHLIPVDLSKNNLAKITGIARAAHKIIGCKGVTRSDFKFFNGKFYLLEINTQPGMTKLSLVPEIAKHKGISFIKLIEWILKDASINR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34397
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A9BI46 | MYIPIITGGKSKEREISLTSAKNVFNSISNLGYKPVILDLIDDDFINKIQNYKFAFNVVHGDYGEDGRLPSLLEILGIDYTCSNPETCIATYDKFIFYSLFKNYIQMPQTTLTNKLILPPFEYPFIIKPRKSGSSKGVYIIHNENEYKFYLEKDLKEFQEVLVQEYIKGREITISYIQKNEEFILLPILEIIPKKEFYDYEAKYTNGLTELKPQLNSPEKIIQKINEIGNHVMQTLTFKDMFRIDAILKDDEVYVLEINTVPGLTELSDLPTSALAAGISFDELINIIIKNHVARVAG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34268
Sequence Length: 298
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A1WRL3 | MSLFDPHLDGASLGKVAVLMGGVSAEREVSLLSGAGVLRALRARAVDAHAFDTAQGDLGALKREGYARCFIALHGRHGEDGTVQGALELLGIAYTGSGVMASSMALDKTMSKRIWRSEGLPTPDWRLVTSGAEAGQALQTLGAPMIVKPAREGSTIGLSKVHQAQQCASAYLLAARYDPEVLCEQFIAGDELTCTVLDQGRRASAQALPLIRIVAPDGNYDYQHKYFSDATRYHCPSGLPEAQERAIGRLAEQAFSALGCRGWARADIMLRASDQQPFLLEINTAPGMTDHSLVPMSARAAGISYEDLCLRLLAMATLDTPPGALSGAARA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 35110
Sequence Length: 331
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
|
A5CW55 | MIAILMGGNSAERAISLKSGEAIYQTLNNQNIDCFTFDWYGDNLSEFWQQEFDQVFIILHGRGGEDGYIQKQLENRGICYTGSDSNASHNSMDKARTKIIWEQHSLTLAPSIIANIDQPINPINFPLPWAVKPTLEGSSIGISKVDNQMQLNDALMLAWQYAPYALIEQWIKGDEYTVAILGDKALPVVRIITDQNFYDYESKYHSNKTQYLCPCNLSLTQEKALQAIALKAFFAINAKGWGRVDFIINQHNKPYLLEINTVPGMTSHSLVPMAAKAIGISFNKLVTSIINEI | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32900
Sequence Length: 293
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
|
Q8D2Y5 | MKKTVAVLFGGESKEHEISLQSSISIINAIDKKKYNIILIGVEKNGKIGIRSINNYILFKYNINYIKLAPAVSYLYIIPGKNNYQFYSLKNKKMLKIDVIFSILHGSNGENGAFQGLFNTIYTPFVGSNVLSSSICMDKDISKRILSTFGISVVPSITLYYENYKKKINKIINNIKFPCCIKPSNQGSSFGVNVANDFISLKESIDVAFLYSKKILIEPFIQGREIEVGVLGNRNVISSVCGEIKFKKIFYDYKEKYISKKTKIIIPAKISNEISNKIKKIAKLAFISLECSIMARVDFFLTKNKKIFLNEINTIPGFTKNSIYPKLWSKSGLDFKSLINKLILLTIYKK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 39675
Sequence Length: 350
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
|
B3CPK8 | MLMVPNIAILSGGFSCEREISLMSGKAVKKALDSLSYNAIEIDVDSNIAQKLKKTNPALAFIALHGPYGEDGCIQGLLEILGIKYTHSEVMASAVAMNKVMSKHIFHSLNIDTPRGYVISREDVLKNNIKVDYPYVLKPINEGSSIGVHMIFSHEDYLELKNNSSTIMEKMIIEEYIPGIELHTAVLLNEAIGTMEIRPKNKFYDYEAKYTDGFAEHIFPAEIPNNIYRITLEHALKVHQFLGCKTVSRSDFRYNPQNNTLKMLEVNTHPGFTELSLVPEIAKLTRGIDFNELVKIIVEDSLHHRNIRDQADVEQCY | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 35815
Sequence Length: 317
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
|
Q9PF79 | MFGRVAVLLGGTSAEREVSLLSGRNVLEVLRVRGVDAQSVDGVPALAQALVERRFDRVFNVLHGHNGGGEDGVVQGLMQAFGVPYTGSDVLGSALSMDKVRTKQVWLALGLPTPRYASLSVCATAVEVRQAVEMLGFPVIIKPAKEGSSVGVSRVFALEHLEEAVALAARYEGELLMEQLIEGDELTVSILDEMALPSIRIVPQGQWYDYNAKYLAEDTQYVCPGLDDVAEAEIARLALAAFRAVGCRGWGRVDVMRERGSGRFFLLEVNTAPGMTTHSLVPKAASQLGMGFDDLVWRILEQTL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32889
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q54ZI9 | MKNKILFSFSNPMNSNSSNNIENNNNSNNNNNNFKNNFKNFSRKRTNDIEIEDNITFSELLLQKEVLKGLEDGGYQRPSPIQLKAIPLGISGVDLIAQAKSGTGKTIVFGVIALECVLRESKLLRQKQELNKTQLTNQTNKQLLEMDDDTYVETMVGIIRKPLVLIIAPTREIAVQIKDVIKSISKYCKRIKCEVFIGGLNSNNNKDENNNNILNNEDVNRLNGTQIIVGTPGKIKSLIENLHLRTDTLKMVIMDEADKLLDASFSKTINWIYSAIGNGNSNKNNSSSGSGIQMLAFSATYPSYLINLLKLYMNNENLVEIRLCSDTPSLEGIKQYYQIFRNDFTENNYKTFQNKCKSLVLVLEQVSFYQAIIFCNHKIRGEELTRQLNREGWPTAFIAGGQNQKDRLSTMSALKSFNIRILVSTDLISRGIDVERVNLVINLDLPKDHETYFHRIGRTGRFGTYGVSITFINMKSIQQQQQQQQQQQQQIENENENENNNNNEGFQEIDFINQLIQEYSVDITERVDNDIIPEELYSYQLSNPNDQQSLANLKLKQQQTILLNKQLEELKINENENENQYQNEDEEEEQEEDDYHYENQHQNEDEEEEQEEDDYHYENQHQNEEEEQEQQEEDDDNYNYENDNDSEEYEFIDDSIIEQTEYYYLNSNNNNNNNKNKYGNTINNNHYRNSSFNGPKNSINNNKFKNKNINNNDQRNSQSNGIKKKVNTNNNNFYPHYYNNPYPQNYYYDYQYFSDNSYYNNNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYQQHGNNPYGYNIPNSIQYSSNQFYYCTCPNCPTMNYHQYI | Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 99148
Sequence Length: 849
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q9UHI6 | MAAAFEASGALAAVATAMPAEHVAVQVPAPEPTPGPVRILRTAQDLSSPRTRTGDVLLAEPADFESLLLSRPVLEGLRAAGFERPSPVQLKAIPLGRCGLDLIVQAKSGTGKTCVFSTIALDSLVLENLSTQILILAPTREIAVQIHSVITAIGIKMEGLECHVFIGGTPLSQDKTRLKKCHIAVGSPGRIKQLIELDYLNPGSIRLFILDEADKLLEEGSFQEQINWIYSSLPASKQMLAVSATYPEFLANALTKYMRDPTFVRLNSSDPSLIGLKQYYKVVNSYPLAHKVFEEKTQHLQELFSRIPFNQALVFSNLHSRAQHLADILSSKGFPAECISGNMNQNQRLDAMAKLKHFHCRVLISTDLTSRGIDAEKVNLVVNLDVPLDWETYMHRIGRAGRFGTLGLTVTYCCRGEEENMMMRIAQKCNINLLPLPDPIPSGLMEECVDWDVEVKAAVHTYGIASVPNQPLKKQIQKIERTLQIQKAHGDHMASSRNNSVSGLSVKSKNNTKQKLPVKSHSECGIIEKATSPKELGCDRQSEEQMKNSVQTPVENSTNSQHQVKEALPVSLPQIPCLSSFKIHQPYTLTFAELVEDYEHYIKEGLEKPVEIIRHYTGPGDQTVNPQNGFVRNKVIEQRVPVLASSSQSGDSESDSDSYSSRTSSQSKGNKSYLEGSSDNQLKDSESTPVDDRISLEQPPNGSDTPNPEKYQESPGIQMKTRLKEGASQRAKQSRRNLPRRSSFRLQTEAQEDDWYDCHREIRLSFSDTYQDYEEYWRAYYRAWQEYYAAASHSYYWNAQRHPSWMAAYHMNTIYLQEMMHSNQ | Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 92241
Sequence Length: 824
Subcellular Location: Cytoplasm
EC: 3.6.1.15
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Q9NR30 | MPGKLRSDAGLESDTAMKKGETLRKQTEEKEKKEKPKSDKTEEIAEEEETVFPKAKQVKKKAEPSEVDMNSPKSKKAKKKEEPSQNDISPKTKSLRKKKEPIEKKVVSSKTKKVTKNEEPSEEEIDAPKPKKMKKEKEMNGETREKSPKLKNGFPHPEPDCNPSEAASEESNSEIEQEIPVEQKEGAFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHWTQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITLKGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICFYQHKEEYQLVQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHISGATSVDQRSLINSNVGFVTMILQCSIEMPNISYAWKELKEQLGEEIDSKVKGMVFLKGKLGVCFDVPTASVTEIQEKWHDSRRWQLSVATEQPELEGPREGYGGFRGQREGSRGFRGQRDGNRRFRGQREGSRGPRGQRSGGGNKSNRSQNKGQKRSFSKAFGQ | Function: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) . Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs . In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes . In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes . Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' . Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) . Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases . Involved in rRNA processing . May bind to specific miRNA hairpins . Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity).
PTM: Acetylation by CREBBP/CBP inhibits the helicase activity . Deacetylation by SIRT7 promotes the helicase activity and overcomes R-loop-mediated stalling of RNA polymerases .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 87344
Sequence Length: 783
Domain: The helicase and foldase activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q9JIK5 | MPGKLRSGAKLGSDGAEESMETLPKPSEKKTRKEKTKSKTEEATEGMEEAVSSKAKKTNKKGPSEDDVDPPKSRKAKKQEEEPQDDTASTSKTSKKKKEPLEKQADSETKEIITEEPSEEEADMPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEADIPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEVDIPKPKKMKKGKEASGDAGEKSPRLKDGLSQPSEPKSNSSDAPGEESSSETEKEIPVEQKEGAFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKAAITVEHLAIKCHWTERAAVIGDVIRVYSGHQGRTIIFCETKKDAQELSQNTCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHISGATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHDSRRWQLTVATEQPELEGPPDGYRGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRGQKRSFSKAFGQ | Function: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (By similarity). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (By similarity). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification (By similarity). Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (By similarity). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (By similarity). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (By similarity). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (By similarity). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (By similarity). Involved in rRNA processing. May bind to specific miRNA hairpins (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 .
PTM: Acetylation by CREBBP/CBP inhibits the helicase activity. Deacetylation by SIRT7 promotes the helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 93551
Sequence Length: 851
Domain: The helicase and foldase activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus.
Subcellular Location: Nucleus
EC: 3.6.4.13
|
Q54Y81 | MDPPKLTFISKRDTKKKDEVNKEQPTKNLKILDLFSNDEEFSNPTQEEPTNTLQEKLMNVDPLEFFSKGGLKEEQKKERDDHRDDYRDSRDRDRDYRDNGGRDRDRDYRDGGGGGGGRDRDRNRDRDRDRDRDYRDGGGGRDRYRDNDRYRDTDRYRDNDRRDGSGSGSSRRRDERRENSGRRDYRDNDRRDDRRDNGRYGRDNDNSGGGGSGKNSSDKKEEINPVSNNNDIHKDRIKRDTTQFSHKVFEQINNKRDREDPELRDIKVDYMGIKRDENRKKIKGEKGKFVFEWDSSEDTSSDYNTLYTKKLEIQPQFGHGNFGGYEKNNNNNGNHYNGNIYNNNNNNNNNNNNNNNINNNNNGSMIGGKQISELPDTHWSKKPLKSMTKRDWHIFKEDFNISTKGGIAPNPIRTWQESNLPREILEAIRQLGYEKPSPIQMQSIPISLTGRDILGIAETGSGKTCAFVIPMLIYISKQPRLTKDTEADGPYALVMAPTRELVQQIEKETRNFAQHFGFRVVSLVGGQSIEDQAYQVSKGCEIIIATPGRLNDCLEKRYLVLNQCNYIVLDEADMMIDLGFEPQVTSVLDAMPSSFLKSEDDEMAEKQESDRSHIYRTTILFSATMPPLVEKLSKKYLRRPCTITIGEAGKVVDRIRQTVIFVKSENDKKEHLTQLIKDGPPPPIIIFVNKKKHCDIIAPVLEECRVSYTILHSGRSQEQREAALEGFKKRKYEVLIATGVASRGIHVDGVTHVINFDIPKNIEDYTHRIGRTGRAGSAGLASSFITDKDVEIMYDLKQILTSTNNIVPIELLKHPSSQQKHGSSKDHNKSVIFK | Function: Probable ATP-dependent RNA helicase which may be involved in mRNA splicing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 95823
Sequence Length: 834
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q9BUQ8 | MAGELADKKDRDASPSKEERKRSRTPDRERDRDRDRKSSPSKDRKRHRSRDRRRGGSRSRSRSRSKSAERERRHKERERDKERDRNKKDRDRDKDGHRRDKDRKRSSLSPGRGKDFKSRKDRDSKKDEEDEHGDKKPKAQPLSLEELLAKKKAEEEAEAKPKFLSKAEREAEALKRRQQEVEERQRMLEEERKKRKQFQDLGRKMLEDPQERERRERRERMERETNGNEDEEGRQKIREEKDKSKELHAIKERYLGGIKKRRRTRHLNDRKFVFEWDASEDTSIDYNPLYKERHQVQLLGRGFIAGIDLKQQKREQSRFYGDLMEKRRTLEEKEQEEARLRKLRKKEAKQRWDDRHWSQKKLDEMTDRDWRIFREDYSITTKGGKIPNPIRSWKDSSLPPHILEVIDKCGYKEPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEESDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEHMPVSNQKPDTDEAEDPEKMLANFESGKHKYRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQKVFLMSESEKRKKLLAILEQGFDPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVVNYDMAKNIEDYIHRIGRTGRAGKSGVAITFLTKEDSAVFYELKQAILESPVSSCPPELANHPDAQHKPGTILTKKRREETIFA | Function: Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation . Independently of its spliceosome formation function, required for the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA .
PTM: In vitro phosphorylated by CLK1 and U1 snRNP-associated protein kinase . Phosphorylated by SRPK2 and this phosphorylation is required for its association with the tri-snRNP (U4/U6-U5 tri-small nuclear ribonucleoproteins) and subsequent spliceosomal B complex formation . May be phosphorylated by SRPK2 on Ser residues in the SR domain; the phosphorylation is required for the removal of inappropriate R-loops during transcription .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 95583
Sequence Length: 820
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q54TD7 | MAKKKFVENTNWKKIDTDNQLIFEQGGFLGLEEIDPNDYFLTDKNVDKIEKQQKQKQKQEQEQEQKPTNKLTTKSTTKSTPVQNKNQKPVDKKRKSKKGNDDSDNEYSGYQDDSDQDDEYSAAKKKPRIIKPTETVDMGTELLNSFVEGTVHNKKKQRKGIKVKQIIDDNDNDFEDEEEEVKPQQKLQKQKQQEQKQKQPQKQPQQPNKKNNKKELQKEEEEQMEEEKEEEEVQQEEEEEKEIKKPIKEKKVKTQKQIEAAKKNINKLEKIKKRKEISEQKTISKEEQDQLDMSEWNSYNLDPLILKGLRSLGFSKPTEIQSSVIPVAVSSGYDVIGAAQTGSGKTLAFGIPMVQRILQHLRKHGQNVENKANKQQNDNDDENEDVEEEEEEEEEEGRSKEYRKLFSLVICPTRELAIQVTNHIKSIISHTNLKVISIVGGMASQRQQRVLSKRPEIVVATPGRLWELITEGHQHLVELESLLCLGIDEADRMVEQGHFAELESILKTLPIHRTAMSKKERLKKKETEEKRNKRRKVDKLNDKGEMIKGDQDDMDDQIPDEEMEELEQEEQNHLTTTHKRQTFVFSATLVNIPGDGAPTSQKKKYRKLTPIENLIEKVRFQRDYKLIDVTQKRLTAKNLLETKIFCNLEEKDMYLYYFVERYPGRTLVFVNSIDCARRLIPIFNILEVPVFALHAQMQQKQRLKNLDRFRTLDNVVLIATDVAARGLDIPLVQHVIHYQVPRTTQLYIHRSGRTARSDQDGISVVLVTPKERPLYIKLDSSIEHDIGNFPTDIRYMEGVRDRIELAKEIDKLSHQSLKDNREKSWFKKQAEEMDIELDGDFFGENSDDEQSEDTRIAEQKKQFKLKQLRAQLKHLLSRSLLPRGVSQSYITASAIQELESKSQSSAATDFSNKAKNVIGKKAKQLAIENHSKFLTKNKKK | Function: ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 109176
Sequence Length: 940
EC: 3.6.4.13
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Q9GZR7 | MKLKDTKSRPKQSSCGKFQTKGIKVVGKWKEVKIDPNMFADGQMDDLVCFEELTDYQLVSPAKNPSSLFSKEAPKRKAQAVSEEEEEEEGKSSSPKKKIKLKKSKNVATEGTSTQKEFEVKDPELEAQGDDMVCDDPEAGEMTSENLVQTAPKKKKNKGKKGLEPSQSTAAKVPKKAKTWIPEVHDQKADVSAWKDLFVPRPVLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHAVLQWQKRNAAPPPSNTEAPPGETRTEAGAETRSPGKAEAESDALPDDTVIESEALPSDIAAEARAKTGGTVSDQALLFGDDDAGEGPSSLIREKPVPKQNENEEENLDKEQTGNLKQELDDKSATCKAYPKRPLLGLVLTPTRELAVQVKQHIDAVARFTGIKTAILVGGMSTQKQQRMLNRRPEIVVATPGRLWELIKEKHYHLRNLRQLRCLVVDEADRMVEKGHFAELSQLLEMLNDSQYNPKRQTLVFSATLTLVHQAPARILHKKHTKKMDKTAKLDLLMQKIGMRGKPKVIDLTRNEATVETLTETKIHCETDEKDFYLYYFLMQYPGRSLVFANSISCIKRLSGLLKVLDIMPLTLHACMHQKQRLRNLEQFARLEDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYVHRSGRTARATNEGLSLMLIGPEDVINFKKIYKTLKKDEDIPLFPVQTKYMDVVKERIRLARQIEKSEYRNFQACLHNSWIEQAAAALEIELEEDMYKGGKADQQEERRRQKQMKVLKKELRHLLSQPLFTESQKTKYPTQSGKPPLLVSAPSKSESALSCLSKQKKKKTKKPKEPQPEQPQPSTSAN | Function: ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 96332
Sequence Length: 859
EC: 3.6.4.13
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Q9QY15 | MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEDDDDDEDDVVDLAANSLLNKLIRQSLIESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTEVTKQIIIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKGKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSNIKQLDPEDMDEIEKIEY | Function: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development.
PTM: Phosphorylated on threonine residues. The phosphorylated form is found in the cytoplasm but not in the nucleus.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 54876
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q9QY16 | MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEEDDDEDDVVDLAANSLLNKLIRQSLVESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLNRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTDVTKQIVIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKDKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSSIKQLDPEDMDEIEKIEY | Function: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity).
PTM: Phosphorylated on threonine residues. The phosphorylated form is found in the cytoplasm but not in the nucleus.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 54791
Sequence Length: 483
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q6CTH5 | MSQFKRNASSKKLDSETKYKLETLSELFPDWTNDDLIDLVREYDDLETIVDKITTGAVTKWDEVKKPSKKEKPASHIEHQSHSSHQQLQQQAASHLDPEDSPSLINQHHSHQRQSRSTSKFSNNSANGKSVQQRQQHQSNNKDNKKQPSKDSLKPAPLPSKSNAGNNAGSWAAVLAEKKKAHEKKIDHTKSSNTIAHESTNEQSESNEHTEPTEVEVAPAQPVDSAPESVSHQHAPESESIATTNGDSKPKSWADIASAKSRQRQLQQQNKKQQQQQKSKPLDNFDALKEEVDQLSSEQTENGNHAISQEPEQQQQPYAQQSTFEEPAQQEEEVVAETTEQQQSQQPQQEEPAQPEVSQVQETAPVSLPEETNAANGVSNIQFGSEDKAAQQTLASQNYYQQQPNQQYAPQQVPQSAAAAAAAQAQAQQYYMYQNQFGYSYPGMFDNQSYLGYGQQFGAPQVPQGQVQPGQQAQPGQQPAAGSPNAQQGQTASAYGAPSGTGYQSQEVPQQSPAQQHVQPQQYSGYGMPYMYYQQSFPYGQPQYGMAGQYPYQMPKAGYNYYPPQPQSQQQGGQAQGSTQSQVEEEQANGQQGGANANAANASQQYQQYYQYQQAQTQPQQQAQQGMPYGYSSYDYSSQTSRGFY | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
PTM: Ubiquitinated.
Sequence Mass (Da): 71618
Sequence Length: 645
Subcellular Location: Cytoplasm
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C5DGU9 | MSTQSRKSNSSKQPHSTHKKLDPELKFKLETLTELFPDWTNDDLIDLVQEYEDLETIIDKITSGAATKWDEVKKPSKKERQREQQQQQQQQQQAQLAAQQATQPSSQSHHNNHTHISPSHDGDHSHSAQTSHNHHQSKSSKFSSRERDSSSRSHKKSSNNAAASGPNGSGNARRERASGASRVPATSAASAASANASAVQPDHLKTAVSAAKTASSTSWAAMASDKKAAKQSAQAKKAEEQQQEQQSPQQAQHESTAPSPQQEAEPQSQSQSKSQPQSDNKSAESVSSTSTPATEDLEKPKKMTWAAIVKPKTKPSVKKSEPLEELEDLKREAAQISTEEPEAAEKVIEQVIEQVEQTPEEVVEQVEVTVVPEEVSQESEEASAQQEETAEPAAPVVPAEPEAASSEEKAAPAQPEQGTYSPVAQQQQPQQQQQPQQQQQAQQQQQQPTAYSEDKQSQAQQAQSQQAQSFYQAQPQQYGSQTPQQTPQTLQQQNAAAAAAAAQQQYYMYQNQFPGYSYPGMFDSQSYPAGYGQQYAPQSQNGSQPQTASTQQSQSGQYGVPPGYASTGRDLGAASPMAAQVQLQQQQQQQPYGGSFMPYYHFYQQSFPYGQPQYGMAGQYPYQVPKAYNYMNQYQPQQGGQTPSSQSQQGEEAQQSAQQGQATASQGQAQGSGSQGQAQTNAQQQAQLQQYYQFQQQQQQQQAAAAAAAAQQGGVPYGYSGYDFSSQATRGFY | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
PTM: Ubiquitinated.
Sequence Mass (Da): 80081
Sequence Length: 733
Subcellular Location: Cytoplasm
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Q8H6Q1 | MARSICFFAVAILALMLFAAYDAEAATCKAECPTWDSVCINKKPCVACCKKAKFSDGHCSKILRRCLCTKECVFEKTEATQTETFTKDVNTLAEALLEADMMV | Function: Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea.
PTM: When compared to other plant defensins, the petunia defensins have an additional fifth disulfide bond.
Sequence Mass (Da): 11361
Sequence Length: 103
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q7V8G6 | MAVKEILRMGNPQLRKVSNVVDDASDELIISLIKDLQDTVKAHQGAGLAAPQIGVPLRVVLFGGGGPNPRYPEAPSIPQTLLINPVLTPIGSDLEDGWEGCLSVPGLRGKVSRWSRIHYRALNEDGFEVEHCLEGFPARVIQHECDHLDGVLFPDRLVDSASFGFTGELETAGIIEKLSSAEQKASQQSRAD | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20788
Sequence Length: 192
EC: 3.5.1.88
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Q88RR1 | MAILNILEFPDPRLRTLAKPVTEFDDALRQLIDDMFETMYEAPGIGLAATQVNVHKQVVVMDLSEDRSEPRVFINPSVEELTHDMGQYQEGCLSVPGFYENVDRPLRVRVKAQDRDGKPFELECEGLLAVCVQHEFDHLNGKLFVDYLSQLKRDRIKKKLEKQHRQQA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19410
Sequence Length: 168
EC: 3.5.1.88
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Q8EHZ2 | MFKDEMRQTPNKPLPIAVVGEAILKQQAIEVRDFDDTLSQLASQMAASMVEAKGVGIAAPQVHSPLALFIMASRPNERYPDAPLMEPLVVVNPQIVLRSLQLEKGEEGCLSVPGQRFTIWRPQTIVVRYQNLAGQWQHSELTGFIARIFQHEFDHLQGITLLERSQMPEQKLMAQEGKPQA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20325
Sequence Length: 181
EC: 3.5.1.88
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Q826Q0 | MRHGSIPGTRGHVRPLALLGDPVLHAPCEEVTDHGPELARLVEDMFATMYAANGVGLAANQIGVPLRVFVYDCPDDEDVRHVGHVVNPRLIEADGVVLRGPEGCLSLPGLEAGTERYDRAVVEGFTTDGEPVRVLGTGWFARCLQHECDHLDGGVYVDRVSGWRHRRVMRQAARAPWNRQRAPEPR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20511
Sequence Length: 186
EC: 3.5.1.88
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Q9FCA2 | MRQGSIPGAHGRVRPLGLLGDPVLHARCAEVTDFGPELAALVEDLFATMYAAHGVGLAANQVGEAVRVFVYDCPDDEDERHLGHVVNPRLVETGGVVVRGPEGCLSLPGLEAGTERYDEAVVTGFTVAGEPVTVRGTGFFARCLQHECDHLEGRVYADRLTGRRHRKLMRQVARASWHR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19476
Sequence Length: 179
EC: 3.5.1.88
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Q9KN16 | MAVLEILTAPDPRLRVQSKQVTDVASVQTLIDDLLDTLYATDNGIGLAAPQVGREEAIVVIDLSDNRDQPLVLINPKVVSGSNKEMGQEGCLSVPDYYADVERYTSVVVEALDREGKPLRIETSDFLAIVMQHEIDHLSGNLFIDYLSPLKQQMAMKKVKKHVKNRAR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 18671
Sequence Length: 168
EC: 3.5.1.88
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Q8P4F9 | MALLPILEFPDPRLRTKAVPVDAAEVVSPAFQTLLDDMFQTMYEAPGIGLAASQVDVHKRFMVIDVSEEKDAPQVFINPEIVTRQGEQVYQEGCLSVPGIFADVSRADAITVRYLDRQGQPQELSTDGLLAVCIQHEMDHLDGKLFVDYLSPLKREMVRKKLAKLRKHVA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19047
Sequence Length: 170
EC: 3.5.1.88
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Q4GWV4 | MKVFVLLTLAVLLMVSADMAFAGFGCPGNQLKCNNHCKSISCRAGYCDAATLWLRCTCTDCNGKK | Function: Antibacterial peptide mostly active against Gram-positive bacteria (M.lysodeikticus, S.aureus, and the marine bacteria, B.stationis, and M.maritypicum) . It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis . It does not disrupt cell membranes . Is noticeably more potent than Cg-Defh1 . It shows no or limited activities against Gram-negative bacteria and filamentous fungi .
Sequence Mass (Da): 7008
Sequence Length: 65
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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A0A097PTA8 | MKLSTSLLAIVAVASTFIGNALSATTVPGCFAECIDKAAVAVNCAAGDIDCLQASSQFATIVSECVATSDCTALSPGSASDADSINKTFNILSGLGFIDEADAFSAADVPEERDLTGLGRVLPVEKRQNCPTRRGLCVTSGLTACRNHCRSCHRGDVGCVRCSNAQCTGFLGTTCTCINPCPRC | Function: Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa) . Is not active against Gram-negative bacteria . It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio), probably anchoring lipid II to the membrane, thus inhibiting cell wall synthesis . The interaction with lipid II involves the third position of the pentapeptide . Shows bactericidal activity at about 2-fold minimal inhibitory concentrations (MIC), but does not form pore across the membrane .
PTM: Contains a unique connectivity of 6 cysteine bonds in contrast to most other CS-alpha-beta defensins which are linked by 3 or 4 disulfide bonds.
Sequence Mass (Da): 18954
Sequence Length: 184
Subcellular Location: Secreted
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P00000 | MWIESDAGVAIDRHARGACSLGEAGCATYCFYQGKHHGGCCGENYTKCLGTCYCNGSGYEYRCHSCDL | Function: Shows antibacterial activity against numerous Gram-positive bacteria (Probable). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis .
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 7355
Sequence Length: 68
Subcellular Location: Secreted
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Q20A05 | LLTLAVLLMVSADMAFAGFGCPGDQYECNRHCRSIGCRAGYCDAVTLWLRCTCTGCSGKK | Function: Antibacterial peptide mostly active against Gram-positive bacteria . It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis . It does not disrupt cell membranes . Is noticeably more potent than Cg-Defh1 .
Sequence Mass (Da): 6439
Sequence Length: 60
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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A8LE21 | MSVRDIRLLGDPVLRTVADPVATFDRELRRLVDDLADTMRDAGGVGLAAPQLGVSLRIFTYLDDSDEVGHLINPVLGPFSEEMMDGEEGCLSLPGLAFDLRRPERVLAVGQNSHGDPVTVEGSGILSRCLQHETDHLDGILFIDRLDKETKRAAMKAIREAEWSNEPKPAVKVSPHPLFGRGR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20091
Sequence Length: 183
EC: 3.5.1.88
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Q8REF0 | MVYKIKKYGEDVLKQIAKEVELSEINDEFRQFLDDMVETMYETDGVGLAAPQIGVSKRIFVCDDGNGVLRKVINPIIVPLTEETQEFEEGCLSVPGIYKKVERPKRVLLKYLNEYGKEVEEIAENFLAVVVQHENDHLDGILFIEKISPMAKRLIAKKLANIKKETKRIKEENE | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19999
Sequence Length: 174
EC: 3.5.1.88
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B8CWS6 | MPVLQIRKIGDPVLRSKAKPVTEITKKTLSLIDNMVETMYQAEGVGLAAPQVGVSKRIIVVDTGEGQGLIELINPEIIETEGKDIMEEGCLSVPGQTGKVIRASKVTVKGLNRGGKEVRIRAEGFLARAFQHEIDHLNGILFIDKVVRIGEEMI | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 16799
Sequence Length: 154
EC: 3.5.1.88
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P35659 | MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS | Function: Involved in chromatin organization.
PTM: Phosphorylated by CK2. Phosphorylation fluctuates during the cell cycle with a moderate peak during G(1) phase, and weakens the binding of DEK to DNA.
Sequence Mass (Da): 42674
Sequence Length: 375
Subcellular Location: Nucleus
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Q7TNV0 | MSAAAAPAAEGEDAPVPPSSEKEPEMPGPREESEEEEEDDEDDDEEDEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTVTQGKGQKLCEIERIHFFLSKKKPDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSTQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKSSSKGSKKERNSSGTTRKSKQTKCPEILSDESSSDEDEKKNKEESSEDEEKESEEEQPPKKTSKKEKAKQKATAKSKKSVKSANVKKADSSTTKKNQKSSKKESESEDSSDDEPLIKKLKKPPTDEELKETVKKLLADANLEEVTMKQICKEVYENYPAYDLTERKDFIKTTVKELIS | Function: Involved in chromatin organization.
PTM: Phosphorylated by CK2. Phosphorylation fluctuates during the cell cycle with a moderate peak during G(1) phase, and weakens the binding of DEK to DNA (By similarity).
Sequence Mass (Da): 43159
Sequence Length: 380
Subcellular Location: Nucleus
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Q19038 | MARKYIDILKKSKMMLFQDVGKSFEDDSPCKEEAPKTQIQHSVRDFCEQTTFHGVNMIFTTSLYWVRFLWVVVSLVCICLCMYSFSHVKDKYDRKEKIVNVELVFESAPFPAITVCNLNPFKNHLARSVPEISETLDAFHQAVVYSNDATMDELSGRGRRSLNDGPSFKYLQYEPVYSDCSCVPGRQECIAQTSAPRTLENACICNYDRHDGSAWPCYSAQTWEKSICPECNDIGFCNVPNTTGSGNIPCYCQLEMGYCVFQPESRVRRIWEFQGNKIPEKGSPLRKEYMEQLTQLGYGNMTDQVAITTQAKEKMILKMSGLHPQRRAALGYGKSELIKMCSFNGQQCNIDTEFKLHIDPSFGNCYTFNANPEKKLASSRAGPSYGLRLMMFVNSSDYLPTTEATGVRIAIHGKEECPFPDTFGYSAPTGVISSFGISLRNINRLPQPYGNCLQKDNPQSRSIYKGYKYEPEGCFRSCYQYRIIAKCGCADPRYPKPWKRSAWCDSTNTTTLNCLTTEGAKLSTKENQKHCKCIQPCQQDQYTTTYSAAKWPSGSIQTSCDNHSKDCNSYLREHAAMIEIYYEQMSYEILRESESYSWFNLMADMGGQAGLFLGASIMSVIEFLFFAVRTLGIACKPRRWRQKTELLRAEELNDAEKGVSTNNN | Function: Probable sodium channel subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75474
Sequence Length: 664
Subcellular Location: Membrane
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A0A396IUP1 | MKREHQESFGGGVISNNNKTNTNHLNSSKNINFGECSSMQNTNTKQNMWREEKETNGGGMDELLAALGYKVRSSDMADVAQKLEQLEMVMGSAQEEGINHLSSDTVHYDPTDLYSWVQTMLTELNPDSSQINDPLASLGSSSEILNNTFNDDSEYDLSAIPGMAAYPPQEENTAAKRMKTWSEPESEPAVVMSPPPAVENTRPVVLVDTQETGVRLVHTLMACAEAIQQKNLKLAEALVKHISLLASLQTGAMRKVASYFAQALARRIYGNPEETIDSSFSEILHMHFYESSPYLKFAHFTANQAILEAFAGAGRVHVIDFGLKQGMQWPALMQALALRPGGPPTFRLTGIGPPQADNTDALQQVGWKLAQLAQTIGVQFEFRGFVCNSIADLDPNMLEIRPGEAVAVNSVFELHTMLARPGSVEKVLNTVKKINPKIVTIVEQEANHNGPVFVDRFTEALHYYSSLFDSLEGSNSSSNNSNSNSTGLGSPSQDLLMSEIYLGKQICNVVAYEGVDRVERHETLTQWRSRMGSAGFEPVHLGSNAFKQASTLLALFAGGDGYRVEENNGCLMLGWHTRSLIATSAWKLPQNESK | Function: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway (By similarity). Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes (By similarity). Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway (By similarity). Together with DELLA2, required to enable arbuscule development during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme) via the regulation of RAM1 which, in turn, regulates various AM genes (e.g. NSP1, NSP2, PT4, LEC5, RAM2, EXO70I, STR and RAD1) .
PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to its subsequent degradation.
Sequence Mass (Da): 65226
Sequence Length: 594
Domain: The DELLA motif is required for its GA-induced degradation.
Subcellular Location: Nucleus
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Q14154 | MWRLPGLLGRALPRTLGPSLWRVTPKSTSPDGPQTTSSTLLVPVPNLDRSGPHGPGTSGGPRSHGWKDAFQWMSSRVSPNTLWDAISWGTLAVLALQLARQIHFQASLPAGPQRVEHCSWHSPLDRFFSSPLWHPCSSLRQHILPSPDGPAPRHTGLREPRLGQEEASAQPRNFSHNSLRGARPQDPSEEGPGDFGFLHASSSIESEAKPAQPQPTGEKEQDKSKTLSLEEAVTSIQQLFQLSVSIAFNFLGTENMKSGDHTAAFSYFQKAAARGYSKAQYNAGLCHEHGRGTPRDISKAVLYYQLAASQGHSLAQYRYARCLLRDPASSWNPERQRAVSLLKQAADSGLREAQAFLGVLFTKEPYLDEQRAVKYLWLAANNGDSQSRYHLGICYEKGLGVQRNLGEALRCYQQSAALGNEAAQERLRALFSMGAAAPGPSDLTVTGLKSFSSPSLCSLNTLLAGTSRLPHASSTGNLGLLCRSGHLGASLEASSRAIPPHPYPLERSVVRLGFG | Function: Key activator of the integrated stress response (ISR) following mitochondrial stress . In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR . Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation .
PTM: Cleaved by OMA1 in response to mitochondrial stress, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1) that accumulates in the cytosol and activates the protein kinase activity of EIF2AK1/HRI . Protein cleavage by OMA1 can take place at different positions, and apparently does not require a specific sequence motif .
Sequence Mass (Da): 55920
Sequence Length: 515
Domain: The TPR repeats bind to and activate EIF2AK1/HRI.
Subcellular Location: Mitochondrion
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Q9DCV6 | MWRLTGILGRALPRLLGPGFRGITPKPTSSDGSQTTSPTLPLTRLSFDRSGSHGSKRSRDPKCCGWKDAFHWMSAHVSPNTLRDAISWGTLAVLALHLARQIHFHAPLVAGPQPAERSWHSPLYRFLSSSWWHPHSSLRRHVLPRSDCPAPRNTGLREPRQGQEDHPSAPSQCLPSDSSLRSGLLNLPEEEPSDFDFLHASRDFASQAKAAEAHPPGGKNEQDKAKALPLEEAVTSIQQLFQLSVAITFNFLGTENIKTGDYTAAFSYFQKAADRGYSKAQYNVGLCLEHGRGTPRDLSKAILFYHLAAVQGHSLAQYRYARCLLQSPGSLSDPERERAVSLLKQAADSGLTEAQAFLGVLFTKEPHLDEQRAVKYLWLAASNGDSQSRFHLGICYEKGLGAQRNLGEAVKCYQQAAAMGNEPARERLRTLFNVEAAGPSHLATTGLKSFSSPSLCSLNTLLAGASGLPHASSTGNLGLLCRSGHLGASHGAPSRTIPSLERSLVRLGFG | Function: Key activator of the integrated stress response (ISR) following mitochondrial stress. In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR. Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation.
PTM: Cleaved by OMA1 in response to mitochondrial stress, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1) that accumulates in the cytosol and activates the protein kinase activity of EIF2AK1/HRI. Protein cleavage by OMA1 can take place at different positions, and apparently does not require a specific sequence motif.
Sequence Mass (Da): 55430
Sequence Length: 510
Domain: The TPR repeats bind to and activate EIF2AK1/HRI.
Subcellular Location: Mitochondrion
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Q8EHK2 | MKRTVIMMLDSFGVGAAGDAAKFGDVGSDTFGHIAKACAEGKADTGRKGPLALPNLARLGLAHAAMESTGAFAPGFADNVDLIGAYGHAQELSSGKDTPSGHWEMAGVPVLFEWGYFSEHQNSFPKELTDKILARAGLDGFLGNCHASGTTILEELGEEHMRSGKPIFYTSADSVFQIACHEGTFGLENLYRLCEIAREELEPYNIGRVIARPFDGTGPSDFARTGNRKDYSLEPPAKTVLDKLKAAGGEVVSVGKIADIYAYCGITKKVKANGLEALFDATLAEVKSAGENTIVFTNFVDFDSHYGHRRDVAGYAKGLEYFDARLPEMLALLDEDDLLILTADHGCDPTWQGTDHTREYVPVLAYGAGLKAGSLGRRNSFADIGQSIASYFKLEPMEYGESFI | Cofactor: Binds 1 or 2 manganese ions.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 43508
Sequence Length: 404
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 1/3.
Subcellular Location: Cytoplasm
EC: 5.4.2.7
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B2KBN0 | MNKTAKLIDHTLLKPGATEFEIKTLCAEALKYGFASVCVNPFWVKLAASELEGSDVKVCTVIGFPLGANTTEAKVFEAKNALENGAQELDMVINIGAVKSGLYELAYHDIKLIRDLGKNFVLKVILETTLLTDAEKIKVCELSACAEADFVKTSTGFAGGGATIEDVKLMKANISSGMQVKASGGVRDLETLTKMVEAGASRIGTSSSIKIIESL | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22853
Sequence Length: 215
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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Q9KNB2 | MATPHINAQPGDFAETVLMPGDPLRAKYIAETFLEDVKQVCDVRSMFGFTGTYKGKKVSVMGHGMGIPSCSIYVHELIAEYGVKNIIRIGSCGAVRDDVKLMDVVIGMGASTDSKVNRIRFSGHDFAAIADYDLLETAVNQARAQQVPVKVGNVFSADLFYTPEPEIFEKMKKLGILGVDMEAAGIYGVAADLGARALTILTVSDHILRGEKLSSEDRQKSFNDMMKVALETAINI | Function: Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 25640
Sequence Length: 236
EC: 2.4.2.1
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Q9ZPH4 | MGKGGREKISSNEEEREGVMATDFFWSYTDEPHASRRRQILSCYPQIRQLFGPDPWAFLKITLVVILQLSTAAILHNSGWLKILSIAYFFGSFLNHNLFLAIHELSHNLAFSTPVYNRCLGIFANLPIGVPMSVTFQKYHLEHHRFQGVDGIDMDVPTYTEAHLVTNIFAKTIWVFLQLFFYALRPIFIKPKPPGYWEFINFLIQIVLDVSVVLFFGWRSFAYLILSTFVGGGMHPMAGHFISEHYVFNPNQETYSYYGPLNLLTWSVGYHNEHHDFPRIPGNKLHLVKEIAGEYYEGLESYKSWSQVIYMYIMDTTVGPYSRMKRKLSKSD | Function: Sphingolipid-delta-4-desaturase required for the biosynthesis of delta-4-unsaturated sphingolipids and derivatives. May be required for the biosynthesis of glucosylceramides.
Catalytic Activity: an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38507
Sequence Length: 332
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.19.17
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Q6H5U3 | MGAAAGDGREEEGVMATDFFWSYTDEPHATRRREILAKHPQIKELFGPDPLAFLKIAAVVSLQLWTATLLRDASWVKILTVAYFFGSFLNHNLFLAIHELSHNLAFTTPSYNRWLGIFANLPIGVPMSITFQKYHLEHHRFQGVDGIDMDIPSQAEAHAVKNTLSKSVWVVFQLFFYALRPLFLKPKPPGLWEFTNLIIQIALDASMVYFFGWKSLAYLILSTFVGGGMHPMAGHFISEHYVFNPDQETYSYYGPLNLMTWHVGYHNEHHDFPRIPGTRLYKVREIAPEYYNNLKSYKSWSQVIYMYIMDQTVGPFSRMKRKAPKKDS | Function: Sphingolipid-delta-4-desaturase required for the biosynthesis of delta-4-unsaturated sphingolipids and derivatives.
Catalytic Activity: an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37869
Sequence Length: 328
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.19.17
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O00273 | MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT | Function: Inhibitor of the caspase-activated DNase (DFF40).
PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.
Sequence Mass (Da): 36522
Sequence Length: 331
Subcellular Location: Cytoplasm
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O54786 | MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWIYNDSDGGTAWVSQESFEADEPDSRAGVKWKNVARQLKEDLSSIILLSEEDLQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGNILSNQKESKAALSEELDAVDTGVGREMASEVLLRSQILTTLKEKPAPELSLSSQDLESVSKEDPKALAVALSWDIRKAETVQQACTTELALRLQQVQSLHSLRNLSARRSPLPGEPQRPKRAKRDSS | Function: Inhibitor of the caspase-activated DNase (DFF40).
PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.
Sequence Mass (Da): 36572
Sequence Length: 331
Subcellular Location: Cytoplasm
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Q58CZ0 | MSAVLRKPKTFKLRSLHSEKKFGVAGRSCEEVLRKGCQRLQLPIPGSRLCLYEDGTELTGDYFWSAPDNSELVLLTAGQTWQGFVSDISRFLSVFQEPHAGVIQAARQLLWDERAPLRQKLLADLLGTVSENIAAETRAEDPPWFEGLESRFRSKSGYLRYSCESRIRSYLREVTSGASLVGAEAREEYLRLVGSMQQKLQAAQYNSSYFDRGAKAGRRLCTPEGWFSCQGPFDVDDCTSRHSINPYSNRESRVLFSTWNLDHVIEKKRVVVPALAAAVHDAEGREVDWEYFYRLLFTLENLKLVHIACHKKTTHKLHCDPSRVYCTPAAPRRKRHARHRL | Function: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology (By similarity).
Sequence Mass (Da): 38967
Sequence Length: 341
Subcellular Location: Cytoplasm
EC: 3.-.-.-
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O76075 | MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ | Function: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
Sequence Mass (Da): 39110
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 3.-.-.-
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O54788 | MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSDITRFLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYTSMVDEAAQEEYLRVLGSMCQKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLECDRSRIYRPQTGSRRKQPARKKRPARKR | Function: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
Sequence Mass (Da): 39449
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 3.-.-.-
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P40526 | MYFDEEQLLKYTIYAYRLSFFVGICSLFIAKSCLPEFLQYGKTYRPKENSKYSSILERIKKFTVPKAYFSHFYYLATFLSLVTLYFYPKFPIVWIIFGHSLRRLYETLYVLHYTSNSRMNWSHYLVGIWFYSVLLLILNISLYKNSIPNTLNMNAFIIFCIASWDQYKNHVILANLVKYSLPTGRLFRLVCCPHYLDEIIIYSTLLPYEQEFYLTLVWVITSLTISALETKNYYRHKFKDNHVAPYAIIPFII | Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30306
Sequence Length: 253
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.94
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Q99234 | MIIRLHFYYLLTLVYHLGLVGAYEKAARKRIQPPDLIPGPPGHKLGDERPPHYDHRPPYKKHIDNIPAYNLTDLIDDKLLNKYENSCTVNVLTGGFISLASNSWHLRAYNYTLNYPSFLIRCDNGSANPNFSHVLQDFVYDINNKFNVQDDSSKYIGKDPFPLGMIMITFASGCICVATWMLFLVVLLLPSDNHNRRNKVVHVYVLFSAIIRTVFLNETIAVIFDSQYHDDYQDASQFESFIVETAPYKICELVANILSDINWIYIVHYLQSNYGKPTWNWIPFKMKKGTHIIITVGCFLSLADNILFANLLWRKNLVVLKVFYKLIELLIYTIFISIICYFTWHNFAYILLPKTAEINTDGKCKTKLRILWENYHETIPLLAYNILIFILFYFTTIFFAAFTKHVRGWTFNFVHLLKVLITVNVWGLIGVLEKRELHISKKTVLGRKINNRDKFFANPTVNYYGEDLGKHLSAITLNRDLNTTKSNTTSHDSSSLVGSPSPTWKSPIERIRDRRRRHKIMKSENKFGQNPSFGSKSNGKPNTKTTLSKYRQLLRKPRRKTNSYEPKNGIGQNKEGSTVRPGADKHIRDSNYLATDISDNESMETELRTNHIYNYENSD | Function: Involved in invasion during filamentous growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71730
Sequence Length: 619
Subcellular Location: Membrane
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