ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q59S50 | MDDDDELLLNFAAPDTSSVAASKNQNVKVSGGRWKDRRKLQLALQGRTKKRQPETGVNLIPVDESKRKRDSEDKVQLDSNKRSKFTESKGENGGKGDSYVSSLFTNNQPTSHLAPTSTTKELTYLPSNAPMKDATNFSGLGLNEKLSIHLTDHLRFMHPTKIQQLVIPSLISTENDLFVKAQTGSGKTLAFVLPIFHKLMRENKFKINRESGLFAIILTPTRELATQIYGVLETLTRCHHWIVPGIVIGGEKKKSEKARLRKGCNILVATPGRLADHLENTKTLDISQLRWLVLDEGDKLMELGFEDTIAQITAKIDSNS... | 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 bo... |
P0CQ95 | MADDIELNFAVPASGLVRQVAPKKGGRWTDRVRAKREARDAFKSMKANHLTVQNPSMPTVSASELVPKPAVIKPAPTSASVSRHPQPKSQVVAPPRFTNATAGPSRPAPSPQAASSNVPKSASIPAPATIKHRTSLPTNAFERPPLPPQAGPSRPHPAEKLKTPQFISSLFTSAPLPGVKSSVAPEISTGAPSNAPVDTTTFQGLGLNKLLINHLKGKMGVEKPTGIQRNCLPYMLSSPLNPDKKAGDEGPKEEPLRDVLIQAQTGSGKTLSYLLPIVQTLLPLSRLSYIDRSIGTLAIILAPTRELAQQISKVLEQLLH... | 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 b... |
Q5BGX6 | MADDGMLLNFALPSDVIKPQTKIKGGSWRERLSVKKIAARRATNPKRTADGDGNKDGNESGPRNPNRIQVSGSRPAKRQKTDGGFQKLGEGQAHGQGSGQSKGPKKGQGGSVVSSLFSKNPRPRNAVEEDKNDEPMEDAKPTNAPLIDGLDTFTNLGLSPTLAAHLLTKLELKAPTAIQKASITQLLKEETDAFIQAETGSGKTLAYLLPLVQRIMALSRAKNEGDAKGDTSVHRDSGLFAIILAPTRELCKQISVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVL... | 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 bo... |
Q96286 | MALSAIGFEGYEKRLEVTFFEPSIFQDSKGLGLRALTKSQLDEILTPAACTIVSSLSNDQLDSYVLSESSFFVYPYKVIIKTCGTTKLLLSIPPLLKLAGELSLSVKSVKYTRGSFLCPGGQPFPHRSFSEEVSVLDGHFTQLGLNSVAYLMGNDDETKKWHVYAASAQDSSNCNNNVYTLEMCMTGLDREKAAVFYKDEADKTGSMTDNSGIRKILPKSEICDFEFEPCGYSMNSIEGDAISTIHVTPEDGFSYASFEAVGYDFNTLDLSQLVTRVLSCFEPKQFSVAVHSSVGANSYKPEITVDLEDYGCRERTFESL... | 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 inv... |
Q42613 | MSLSAIGFEGLRERLEVSFFEPSLFLDTHGKGLRALSKSQIDEILAPAECTIVSSLSNDELDSYVLSESSLFIFPYKIIIKTCGTTKLLLSIEPLLRLAGGVSLEVKSVRYTRGSFLCPGGQPFPQRNLSEEVSVLDGHFAKMGLSSVAYLMGDDDETKKWHVYSASAPAKNSNGDNNVYTLEMCMSGLDKDKASVFFKNESSSAGSMTDNSGIRKILPQSQICDFEFEPCGYSMNSVEGDASSTIHVTPEDGFSYASFEAVGYDFTTMDLSQLVSRVLTCFEPKQFSVAVHSSVAQKSYDHSGLSVDLEDYGCRETTVG... | 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. Tw... |
Q9S7T9 | MAMSAIGFEGYEKRLEVTFFEPGLFLDTQGKGLRALAKSQIDEILQPAECTIVSSLSNDQLDSYVLSESSLFIFPYKIVIKTCGTTKLLLSIEPLLRLAGELSLDVKAVRYTRGSFLCPGGQPFPHRNFSEEVSVLDGHFAKLGLSSVAYLMGNDDETKKWHVYSASSANSNNKNNVYTLEMCMTGLDKDKASVFYKNESSSAGSMTDNSGIRKILPQSQICDFEFEPCGYSMNSIEGDAISTIHVTPEDGFSYASFEAVGYDFTTMDLSHLVSKVLTCFKPKQFSVAVHSTVAQKSYDSGLSVDLDDYGCKESTMESLG... | 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 inv... |
D3Z6H8 | MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDHLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNF... | 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 i... |
Q9LSU6 | MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDNNPQRWHVYSASSTEESAVCDKPVYTLEMCMTGLDNIKASVFFKTNSVSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSIEGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQERELE... | 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 inv... |
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 biosynthe... |
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 biosynthe... |
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 biosynthe... |
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 biosynthe... |
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 biosynthe... |
Q42472 | MVLTKTATNDESVCTMFGSRYVRTTLPKYEIGENSIPKDAAYQIIKDELMLDGNPRLNLASFVTTWMEPECDKLIMDSINKNYVDMDEYPVTTELQNRCVNIIARLFNAPLEESETAVGVGTVGSSEAIMLAGLAFKRKWQNKRKAEGKPYDKPNIVTGANVQVCWEKFARYFEVELKEVNLSEGYYVMDPDKAAEMVDENTICVAAILGSTLNGEFEDVKRLNDLLVKKNEETGWNTPIHVDAASGGFIAPFIYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVVWRAAEDLPEELIFHINYLGADQPTFTLNFSKG... | 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 L... |
Q05329 | MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRIL... | 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 | MVLSKTVSESDVSIHSTFASRYVRNSLPRFEMPENSIPKEAAYQIINDELMLDGNPRLNLASFVTTWMEPECDKLMMESINKNYVDMDEYPVTTELQNRCVNMIARLFNAPLGDGEAAVGVGTVGSSEAIMLAGLAFKRQWQNKRKAQGLPYDKPNIVTGANVQVCWEKFARYFEVELKEVNLREDYYVMDPVKAVEMVDENTICVAAILGSTLTGEFEDVKLLNDLLVEKNKQTGWDTPIHVDAASGGFIAPFLYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVVWRTKTDLPDELIFHINYLGADQPTFTLNFSK... | 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 Leng... |
P69909 | MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRP... | 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... |
Q05924 | MIRLPRLYQRYLLYLVVFVVIALFYFLQAPRVEEHIGFDLALPISHVDNLWFQNKGLEGFSNDDKLVVNIGYDECFHIGRFYEGCFNRHELKSTLTDGHQYLQRKRIHKDLRGSFGRRWFGKSEYLYYDVLYPALVDYFGSNLEKLNVEAVTGISKYPKDKSLPFMDVSITFEPISIELLQKRSYISDINILFGVDCIQPIANWTLQKEFPLVKYRYSEPAYLTYKFVGTRPVDTGAQRLQETDEGKFKIVQLADLHLGVGESECIDEYPKHEACKADPKTETFVQQVLDIEKPQLVVFTGDQIMGDRSIQDSETVLLKA... | 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 m... |
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 A... |
Q9FF86 | MKIKIMSKTHVKPTKPVLGKKQFHLTTFDLPYLAFYYNQKFLLYKFQNLLDLEEPTFQNEVVENLKDGLGLVLEDFYQLAGKLAKDDEGVFRVEYDAEDSEINGVEFSVAHAADVTVDDLTAEDGTAKFKELVPYNGILNLEGLSRPLLAVQVTKLKDGLAMGLAFNHAVLDGTSTWHFMSSWAEICRGAQSISTQPFLDRSKARDTRVKLDLTAPKDPNETSNGEDAANPTVEPPQLVEKIFRFSDFAVHTIKSRANSVIPSDSSKPFSTFQSLTSHIWRHVTLARGLKPEDITIFTVFADCRRRVDPPMPEEYFGNLI... | 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 | MASQVSQMPSSSPLSSNKDEMRPKADFQPSIWGDLFLNCPDKNIDAETEKRHQQLKEEVRKMIVAPMANSTQKLAFIDSVQRLGVSYHFTKEIEDELENIYHNNNDAENDLYTTSIRFRLLREHGYNVSCDVFNKFKDEQGNFKSSVTSDVRGLLELYQASYLRVHGEDILDEAISFTTHHLSLAVASLDHPLSEEVSHALKQSIRRGLPRVEARHYLSVYQDIESHNKALLEFAKIDFNMLQFLHRKELSEICRWWKDLDFQRKLPYARDRVVEGYFWISGVYFEPQYSLGRKMLTKVIAMASIVDDTYDSYATYEELI... | 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/Gl... |
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 | MNKKKLSIRWKITILSYILVIFSFLIGGIVLIGNIQHTEERELKKRLMNTARTVSEMTEVKEALARKKQTEAVRHAVEEIRMINEADYIVVMDMNHIRYTHPVSTSIGKKSEGADEEAAFAEHIYFSEAKGEIGTAVRAFYPVKDQDLNQIGVVLVGKTLPGIADILLHLKRDIAFIVVLTLGFGLAGSFLLARHIKKQMFQLEPHEIVRMYEERTATFHSMNEGVIAIDNRLVITIFNEKAKQIFEVQGDLIGKVIWEVLKDSRLPEIVERNKAVYNEEIRVSGKVIMSSRIPIVMKKKVIGAVAIFQDRTEAAKMAEE... | 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
S... |
Q5ZTY0 | MFDLNQSLFLRALRRQPVERTPIWIMRQAGRYLPEYRKVREHAGDFLNLCKNPELACEVTLQPLRRYALDAAILFSDILTIPDAMGLGLYFAEGEGPRFTNPLQDTKAIHTLKIPSIPESLSYVFDAARLIRQEMPKELPLIGFSGSPWTLACYMVEGGSSRDFKRILNLIYTEKEAAHLLLNKLAVSVTAYLIEQIKAGVNAVMIFDTWGGVLTPQNYKDFSLAYMHQIVQQLKKEYPDIPVILFTKNGGQWLEWMAETGCDALGVDWTCDLASARKRVGGKVALQGNLDPAVLLTTKNCIRSEVGSVLASYGYGTGHI... | 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 b... |
P16891 | MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEISLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPIRTAEQVAAVHDLDPEEATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSKTYANIKHLAFSEPTILHELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDTFALPYQQRVFQQVKAKHPEVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRLGPDIGLQGNIDPGVLFGSQDFIRDRILDTVRKAGNQRHI... | 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 b... |
Q2JX97 | MSHSPAQLSASPSSVGDGDRLLRAARGEVVDRPPVWMMRQAGRYMAAYRELQSKYTFKQRCEIPELAIEISLQPFRAFAPDGVIMFSDILTPLEGMGIPFELVEQQGPIIDPPIRSQAQVEQIRLLEPEESLPFIKTILSTLRREVEGKATLLGFVGSPWTLACYAVEGRSSKDYAHIKSLAFTQPQVLHQLLSKLADSIARYVIYQIECGAQVVQLFDTWAGQLSPGDYETWALPYQKQIVDQVKARCPQVPLILYINGSAALLERVGKAGIDVFSLDWMSDMAEARARLGSLAVQGNLDPMVLLGSPKFIRQRTLEVI... | 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 b... |
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
Seque... |
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
Seque... |
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
|
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
|
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
|
P32270 | MTFDDLTEGQKNAFNIVMKAIKEKKHHVTINGPAGTGKTTLTKFIIEALISTGGTGIILAAPTHAAKKILSKLSGKEASTIHSILKINPVTYEENVLFEQKEVPDLAKCRVLICDEVSMYDRKLFKILLSTIPPWCTIIGIGDNKQIRPVEPGENTAYISPFFTHKDFYQCELTEVKRSNAPIIDVATDVRNGKWNYDKVVDGHGVRGFTGDTALRDFMVNYFSIVKSLDDLFENRVMAFTNKSVDKLNSIIRKKIFETDKDFIVGEIIVMQEPLFKTYKIDGKPVSEIIFNNGQLVRIIEAEYTSTFVKARGVPGEYLI... | 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 ca... |
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.... |
A0Q323 | MKKKVAILFGGQSTEHEVSRVSASSVLKNIDLSKYDVYPIGITKDGKWFEYTGAIDKIESGEWEKDEFYKNPNGQEILFNREVDVVFPVMHGLYGEDGTIQGLCKLLTIPCVGPGVMSSAVCMDKVYTKYVLENFGVKQADYVVVNAHDYKNNKMDIISTIENKLGYDVFIKPSNSGSSVGISKAHNREELEAGLEEALKFDRKVLVEVALNAREIEVAVLGNDEPVAATPGEIVPANEFYDYEAKYSNAQSKLLLPANLSPEKLEKVKELAVRIFKMLDCAGMSRVDFLVDKETEEVYLNEINTIPGFTKISMYPKMWQ... | 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.... |
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.... |
Q8NQV2 | MSNSNSGKVRVAVVYGGRSSEHSVSCVSAGAIMAHLDPEKYDVIPVGITVDGAWVVGETDPQKLTLIDRTMPEVEHHEEVRPSLDPAHRGEFHFSDGSLYATADVIFPVLHGRFGEDGTVQGLFALSDIPVVGPGVLASAAGMDKEYTKKLMAAEGLPVGREVILRDRTELTEAEKNLLGLPVFVKPARGGSSIGISRVTAWEDFNKAVGLARAHDEKVIVESEIVGSEVECGVLQYPDGRIVASVPALLSGTESGAGGFYDFDTKYLDNVVTAEIPAPLDEKTTELIQSLAVESFQALACEGLARVDFFVTANGPVLNE... | 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.... |
A9KGD2 | MAEKLHISVLCGGQSTEHEISIQSAKNIVNTLDAAKYLISVIFIDHVGRWYLIDQPEMFLAHSPDHLVKEGSARPITIAFGDAAKPWQSLNGDGRRYSADCVFPMVHGTQGEDGALQGLLELLNLPYVGANVQSSAVCMEKDLTKTVLRAGGIPVVDWHTLSPRDATEGVYQRLLDRWGTSELFVKAVSLGSSVATLPVKTETEFTKAVKEVFRYDDRLMVEPRIRGREIECAVLGNGAPKASLPGEIIPHHDYYSYDAKYLDPNGATTTTSVDLSESVTKQIQQIAIDAFKMVHCSGMARVDFFVTPNNKVLVNEINTI... | 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.... |
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.... |
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.... |
Q03EM9 | MKIAVLAGGKSTERNVSLSSGSKITNALRSKGYDATMIDLFLGYELEDGQSYEDVFKSSNTSTDYEISDAVLTEEDIEELRTDGTVGLFGKNVLPILQAADFVFLALHGGDGENGKVQAVLDLNHIKYTGSGSLASGIAMDKAISKEIMLYNNIKTAQFAVLHAKDGIHPQLAFDYPMVVKPNSGGSSIGTRIVHDEAELAESLKDAYRFDDEIIVEEFITGREFSLGVVNGQAMPAIEIVVNDGWYDYEHKFQTGSTTKFVTPPEIEDDVHDEMKRVAVQTMDALGMTNYGRVDFLTNDTGVYVIEANNLPGMTPLSLL... | 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.... |
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.... |
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.... |
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.... |
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.... |
A1WRL3 | MSLFDPHLDGASLGKVAVLMGGVSAEREVSLLSGAGVLRALRARAVDAHAFDTAQGDLGALKREGYARCFIALHGRHGEDGTVQGALELLGIAYTGSGVMASSMALDKTMSKRIWRSEGLPTPDWRLVTSGAEAGQALQTLGAPMIVKPAREGSTIGLSKVHQAQQCASAYLLAARYDPEVLCEQFIAGDELTCTVLDQGRRASAQALPLIRIVAPDGNYDYQHKYFSDATRYHCPSGLPEAQERAIGRLAEQAFSALGCRGWARADIMLRASDQQPFLLEINTAPGMTDHSLVPMSARAAGISYEDLCLRLLAMATLDT... | 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.... |
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.... |
Q8D2Y5 | MKKTVAVLFGGESKEHEISLQSSISIINAIDKKKYNIILIGVEKNGKIGIRSINNYILFKYNINYIKLAPAVSYLYIIPGKNNYQFYSLKNKKMLKIDVIFSILHGSNGENGAFQGLFNTIYTPFVGSNVLSSSICMDKDISKRILSTFGISVVPSITLYYENYKKKINKIINNIKFPCCIKPSNQGSSFGVNVANDFISLKESIDVAFLYSKKILIEPFIQGREIEVGVLGNRNVISSVCGEIKFKKIFYDYKEKYISKKTKIIIPAKISNEISNKIKKIAKLAFISLECSIMARVDFFLTKNKKIFLNEINTIPGFTK... | 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.... |
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.... |
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.... |
Q54ZI9 | MKNKILFSFSNPMNSNSSNNIENNNNSNNNNNNFKNNFKNFSRKRTNDIEIEDNITFSELLLQKEVLKGLEDGGYQRPSPIQLKAIPLGISGVDLIAQAKSGTGKTIVFGVIALECVLRESKLLRQKQELNKTQLTNQTNKQLLEMDDDTYVETMVGIIRKPLVLIIAPTREIAVQIKDVIKSISKYCKRIKCEVFIGGLNSNNNKDENNNNILNNEDVNRLNGTQIIVGTPGKIKSLIENLHLRTDTLKMVIMDEADKLLDASFSKTINWIYSAIGNGNSNKNNSSSGSGIQMLAFSATYPSYLINLLKLYMNNENLVE... | 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 S... |
Q9UHI6 | MAAAFEASGALAAVATAMPAEHVAVQVPAPEPTPGPVRILRTAQDLSSPRTRTGDVLLAEPADFESLLLSRPVLEGLRAAGFERPSPVQLKAIPLGRCGLDLIVQAKSGTGKTCVFSTIALDSLVLENLSTQILILAPTREIAVQIHSVITAIGIKMEGLECHVFIGGTPLSQDKTRLKKCHIAVGSPGRIKQLIELDYLNPGSIRLFILDEADKLLEEGSFQEQINWIYSSLPASKQMLAVSATYPEFLANALTKYMRDPTFVRLNSSDPSLIGLKQYYKVVNSYPLAHKVFEEKTQHLQELFSRIPFNQALVFSNLHS... | 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 S... |
Q9NR30 | MPGKLRSDAGLESDTAMKKGETLRKQTEEKEKKEKPKSDKTEEIAEEEETVFPKAKQVKKKAEPSEVDMNSPKSKKAKKKEEPSQNDISPKTKSLRKKKEPIEKKVVSSKTKKVTKNEEPSEEEIDAPKPKKMKKEKEMNGETREKSPKLKNGFPHPEPDCNPSEAASEESNSEIEQEIPVEQKEGAFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIK... | 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 loc... |
Q9JIK5 | MPGKLRSGAKLGSDGAEESMETLPKPSEKKTRKEKTKSKTEEATEGMEEAVSSKAKKTNKKGPSEDDVDPPKSRKAKKQEEEPQDDTASTSKTSKKKKEPLEKQADSETKEIITEEPSEEEADMPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEADIPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEVDIPKPKKMKKGKEASGDAGEKSPRLKDGLSQPSEPKSNSSDAPGEESSSETEKEIPVEQKEGAFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL... | 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 nu... |
Q54Y81 | MDPPKLTFISKRDTKKKDEVNKEQPTKNLKILDLFSNDEEFSNPTQEEPTNTLQEKLMNVDPLEFFSKGGLKEEQKKERDDHRDDYRDSRDRDRDYRDNGGRDRDRDYRDGGGGGGGRDRDRNRDRDRDRDRDYRDGGGGRDRYRDNDRYRDTDRYRDNDRRDGSGSGSSRRRDERRENSGRRDYRDNDRRDDRRDNGRYGRDNDNSGGGGSGKNSSDKKEEINPVSNNNDIHKDRIKRDTTQFSHKVFEQINNKRDREDPELRDIKVDYMGIKRDENRKKIKGEKGKFVFEWDSSEDTSSDYNTLYTKKLEIQPQFGHG... | 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.... |
Q9BUQ8 | MAGELADKKDRDASPSKEERKRSRTPDRERDRDRDRKSSPSKDRKRHRSRDRRRGGSRSRSRSRSKSAERERRHKERERDKERDRNKKDRDRDKDGHRRDKDRKRSSLSPGRGKDFKSRKDRDSKKDEEDEHGDKKPKAQPLSLEELLAKKKAEEEAEAKPKFLSKAEREAEALKRRQQEVEERQRMLEEERKKRKQFQDLGRKMLEDPQERERRERRERMERETNGNEDEEGRQKIREEKDKSKELHAIKERYLGGIKKRRRTRHLNDRKFVFEWDASEDTSIDYNPLYKERHQVQLLGRGFIAGIDLKQQKREQSRFY... | 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 associate... |
Q54TD7 | MAKKKFVENTNWKKIDTDNQLIFEQGGFLGLEEIDPNDYFLTDKNVDKIEKQQKQKQKQEQEQEQKPTNKLTTKSTTKSTPVQNKNQKPVDKKRKSKKGNDDSDNEYSGYQDDSDQDDEYSAAKKKPRIIKPTETVDMGTELLNSFVEGTVHNKKKQRKGIKVKQIIDDNDNDFEDEEEEVKPQQKLQKQKQQEQKQKQPQKQPQQPNKKNNKKELQKEEEEQMEEEKEEEEVQQEEEEEKEIKKPIKEKKVKTQKQIEAAKKNINKLEKIKKRKEISEQKTISKEEQDQLDMSEWNSYNLDPLILKGLRSLGFSKPTEI... | Function: ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 109176
Sequence Length: 940
EC: 3.6.4.13
|
Q9GZR7 | MKLKDTKSRPKQSSCGKFQTKGIKVVGKWKEVKIDPNMFADGQMDDLVCFEELTDYQLVSPAKNPSSLFSKEAPKRKAQAVSEEEEEEEGKSSSPKKKIKLKKSKNVATEGTSTQKEFEVKDPELEAQGDDMVCDDPEAGEMTSENLVQTAPKKKKNKGKKGLEPSQSTAAKVPKKAKTWIPEVHDQKADVSAWKDLFVPRPVLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHAVLQWQKRNAAPPPSNTEAPPGETRTEAGAETRSPGKAEAESDALPDDTVIESEALPSDIAAEARAK... | Function: ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 96332
Sequence Length: 859
EC: 3.6.4.13
|
Q9QY15 | MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEDDDDDEDDVVDLAANSLLNKLIRQSLIESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTEVTKQIIIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLC... | 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
Se... |
Q9QY16 | MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEEDDDEDDVVDLAANSLLNKLIRQSLVESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLNRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTDVTKQIVIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCE... | 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 Mas... |
Q6CTH5 | MSQFKRNASSKKLDSETKYKLETLSELFPDWTNDDLIDLVREYDDLETIVDKITTGAVTKWDEVKKPSKKEKPASHIEHQSHSSHQQLQQQAASHLDPEDSPSLINQHHSHQRQSRSTSKFSNNSANGKSVQQRQQHQSNNKDNKKQPSKDSLKPAPLPSKSNAGNNAGSWAAVLAEKKKAHEKKIDHTKSSNTIAHESTNEQSESNEHTEPTEVEVAPAQPVDSAPESVSHQHAPESESIATTNGDSKPKSWADIASAKSRQRQLQQQNKKQQQQQKSKPLDNFDALKEEVDQLSSEQTENGNHAISQEPEQQQQPYAQ... | 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 Mas... |
C5DGU9 | MSTQSRKSNSSKQPHSTHKKLDPELKFKLETLTELFPDWTNDDLIDLVQEYEDLETIIDKITSGAATKWDEVKKPSKKERQREQQQQQQQQQQAQLAAQQATQPSSQSHHNNHTHISPSHDGDHSHSAQTSHNHHQSKSSKFSSRERDSSSRSHKKSSNNAAASGPNGSGNARRERASGASRVPATSAASAASANASAVQPDHLKTAVSAAKTASSTSWAAMASDKKAAKQSAQAKKAEEQQQEQQSPQQAQHESTAPSPQQEAEPQSQSQSKSQPQSDNKSAESVSSTSTPATEDLEKPKKMTWAAIVKPKTKPSVKKS... | 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 Mas... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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 inhibiti... |
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 mola... |
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
... |
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 pote... |
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... |
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... |
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... |
P35659 | MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPP... | 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 | MSAAAAPAAEGEDAPVPPSSEKEPEMPGPREESEEEEEDDEDDDEEDEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTVTQGKGQKLCEIERIHFFLSKKKPDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSTQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKSSSKGSKKERNSSGTTRKSKQTKCPEILSDESSSDEDEKKNKEESSEDEEKESEEEQPPKKTSKKEKAKQKATAKSKKSVKSANVKKADSSTTKKNQKSSKKESESEDSSDDEPLIKK... | 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 | MARKYIDILKKSKMMLFQDVGKSFEDDSPCKEEAPKTQIQHSVRDFCEQTTFHGVNMIFTTSLYWVRFLWVVVSLVCICLCMYSFSHVKDKYDRKEKIVNVELVFESAPFPAITVCNLNPFKNHLARSVPEISETLDAFHQAVVYSNDATMDELSGRGRRSLNDGPSFKYLQYEPVYSDCSCVPGRQECIAQTSAPRTLENACICNYDRHDGSAWPCYSAQTWEKSICPECNDIGFCNVPNTTGSGNIPCYCQLEMGYCVFQPESRVRRIWEFQGNKIPEKGSPLRKEYMEQLTQLGYGNMTDQVAITTQAKEKMILKMS... | 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 | MKREHQESFGGGVISNNNKTNTNHLNSSKNINFGECSSMQNTNTKQNMWREEKETNGGGMDELLAALGYKVRSSDMADVAQKLEQLEMVMGSAQEEGINHLSSDTVHYDPTDLYSWVQTMLTELNPDSSQINDPLASLGSSSEILNNTFNDDSEYDLSAIPGMAAYPPQEENTAAKRMKTWSEPESEPAVVMSPPPAVENTRPVVLVDTQETGVRLVHTLMACAEAIQQKNLKLAEALVKHISLLASLQTGAMRKVASYFAQALARRIYGNPEETIDSSFSEILHMHFYESSPYLKFAHFTANQAILEAFAGAGRVHVID... | 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, allowin... |
Q14154 | MWRLPGLLGRALPRTLGPSLWRVTPKSTSPDGPQTTSSTLLVPVPNLDRSGPHGPGTSGGPRSHGWKDAFQWMSSRVSPNTLWDAISWGTLAVLALQLARQIHFQASLPAGPQRVEHCSWHSPLDRFFSSPLWHPCSSLRQHILPSPDGPAPRHTGLREPRLGQEEASAQPRNFSHNSLRGARPQDPSEEGPGDFGFLHASSSIESEAKPAQPQPTGEKEQDKSKTLSLEEAVTSIQQLFQLSVSIAFNFLGTENMKSGDHTAAFSYFQKAAARGYSKAQYNAGLCHEHGRGTPRDISKAVLYYQLAASQGHSLAQYRYA... | 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 t... |
Q9DCV6 | MWRLTGILGRALPRLLGPGFRGITPKPTSSDGSQTTSPTLPLTRLSFDRSGSHGSKRSRDPKCCGWKDAFHWMSAHVSPNTLRDAISWGTLAVLALHLARQIHFHAPLVAGPQPAERSWHSPLYRFLSSSWWHPHSSLRRHVLPRSDCPAPRNTGLREPRQGQEDHPSAPSQCLPSDSSLRSGLLNLPEEEPSDFDFLHASRDFASQAKAAEAHPPGGKNEQDKAKALPLEEAVTSIQQLFQLSVAITFNFLGTENIKTGDYTAAFSYFQKAADRGYSKAQYNVGLCLEHGRGTPRDLSKAILFYHLAAVQGHSLAQYRY... | 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 th... |
Q8EHK2 | MKRTVIMMLDSFGVGAAGDAAKFGDVGSDTFGHIAKACAEGKADTGRKGPLALPNLARLGLAHAAMESTGAFAPGFADNVDLIGAYGHAQELSSGKDTPSGHWEMAGVPVLFEWGYFSEHQNSFPKELTDKILARAGLDGFLGNCHASGTTILEELGEEHMRSGKPIFYTSADSVFQIACHEGTFGLENLYRLCEIAREELEPYNIGRVIARPFDGTGPSDFARTGNRKDYSLEPPAKTVLDKLKAAGGEVVSVGKIADIYAYCGITKKVKANGLEALFDATLAEVKSAGENTIVFTNFVDFDSHYGHRRDVAGYAKGLE... | 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 biosyn... |
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;... |
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-phosphat... |
Q9ZPH4 | MGKGGREKISSNEEEREGVMATDFFWSYTDEPHASRRRQILSCYPQIRQLFGPDPWAFLKITLVVILQLSTAAILHNSGWLKILSIAYFFGSFLNHNLFLAIHELSHNLAFSTPVYNRCLGIFANLPIGVPMSVTFQKYHLEHHRFQGVDGIDMDVPTYTEAHLVTNIFAKTIWVFLQLFFYALRPIFIKPKPPGYWEFINFLIQIVLDVSVVLFFGWRSFAYLILSTFVGGGMHPMAGHFISEHYVFNPNQETYSYYGPLNLLTWSVGYHNEHHDFPRIPGNKLHLVKEIAGEYYEGLESYKSWSQVIYMYIMDTTVGP... | 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]... |
Q6H5U3 | MGAAAGDGREEEGVMATDFFWSYTDEPHATRRREILAKHPQIKELFGPDPLAFLKIAAVVSLQLWTATLLRDASWVKILTVAYFFGSFLNHNLFLAIHELSHNLAFTTPSYNRWLGIFANLPIGVPMSITFQKYHLEHHRFQGVDGIDMDIPSQAEAHAVKNTLSKSVWVVFQLFFYALRPLFLKPKPPGLWEFTNLIIQIALDASMVYFFGWKSLAYLILSTFVGGGMHPMAGHFISEHYVFNPDQETYSYYGPLNLMTWHVGYHNEHHDFPRIPGTRLYKVREIAPEYYNNLKSYKSWSQVIYMYIMDQTVGPFSRMK... | 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
Seq... |
O00273 | MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDL... | 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 | MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWIYNDSDGGTAWVSQESFEADEPDSRAGVKWKNVARQLKEDLSSIILLSEEDLQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGNILSNQKESKAALSEELDAVDTGVGREMASEVLLRSQILTTLKEKPAPELSLSSQDLESVSKEDPKALAVALSWDIRKAETVQQACTTELALRLQQVQSLHSLRNLSARRSPLPGEP... | 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 | MSAVLRKPKTFKLRSLHSEKKFGVAGRSCEEVLRKGCQRLQLPIPGSRLCLYEDGTELTGDYFWSAPDNSELVLLTAGQTWQGFVSDISRFLSVFQEPHAGVIQAARQLLWDERAPLRQKLLADLLGTVSENIAAETRAEDPPWFEGLESRFRSKSGYLRYSCESRIRSYLREVTSGASLVGAEAREEYLRLVGSMQQKLQAAQYNSSYFDRGAKAGRRLCTPEGWFSCQGPFDVDDCTSRHSINPYSNRESRVLFSTWNLDHVIEKKRVVVPALAAAVHDAEGREVDWEYFYRLLFTLENLKLVHIACHKKTTHKLHCD... | 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.-.-.-
|
O76075 | MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSR... | 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.-.-.-
|
O54788 | MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSDITRFLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYTSMVDEAAQEEYLRVLGSMCQKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLECDRS... | 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 promot... |
Q99234 | MIIRLHFYYLLTLVYHLGLVGAYEKAARKRIQPPDLIPGPPGHKLGDERPPHYDHRPPYKKHIDNIPAYNLTDLIDDKLLNKYENSCTVNVLTGGFISLASNSWHLRAYNYTLNYPSFLIRCDNGSANPNFSHVLQDFVYDINNKFNVQDDSSKYIGKDPFPLGMIMITFASGCICVATWMLFLVVLLLPSDNHNRRNKVVHVYVLFSAIIRTVFLNETIAVIFDSQYHDDYQDASQFESFIVETAPYKICELVANILSDINWIYIVHYLQSNYGKPTWNWIPFKMKKGTHIIITVGCFLSLADNILFANLLWRKNLVVL... | 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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