ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q503M4 | MAQEKKKGGVLPPDGGWGWMIVAGCFVVTVCTRAVTRCISIFFVEFQMHFAKDYSGTAWIHSLVDCTTMLCAPLGSLIGNQLSCRIAVILGGFLASVGLVLSSFATSLEYLYATLGLLTGLGFALCYTPAIAMVGIYFCERKALAYGIAMSGSGIGTFILAPVVQLLIEHYSWRGALLILGGFVLNLCVCGALLRPIILKEEEACPLPVDSECGYSVKPPTLNGGPTRSAASDAKQRCFQSMQEYHFLLMPDFLVLAGSFLLLASGCSLPFVYLVPYALDVGVGHQHAAFLMSILGVIDIVGNITFGWLTDRRCLKKYRN... | Function: Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na(+), Cl(-), or pH. Contributes to the process of creatine biosynthesis and distribution.
Catalytic Activity: creatine(in) = cre... |
P34720 | MKPFIKWAGGKNSLLDEIQKRLPDFVHSQDFCLVEPFVGGGAVSLWALSDLPHLKQLVINDCNADLINVYQVIKNNPDDLIGYIENLQSHYDKLTDLESKKPYFYHKRDVFNQRTSNDIEQAGLFIFLNKSAFNGLYRVNKNNQFNVPIGNYKKPTFVDKENILNISKKLQNTKILSGDFELVLAHLPNNFPCLFYLDPPYRPISDTASFTSYSDNGFDDNEQKRLANFCKKIDKLGHYFLLSNSDPKNTNSSDEFFDELYQDFKIERIQANRTISANSNGRKKVNEIIVSNGV | Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the MboI endonuclease (Probable). This seems to be a stronger methylase than M2.MboI (Probable).
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosy... |
Q57983 | MNVIDLFSGCGGFSKGFLDENFRILGAIENFKPVVKTYLYNIKAPVWMDDIKRIPPKAFDEFIKNEKVDVIIGSPPCEPFTKANKLIKDNPLDRLYKDKVGRLVLYYIDYVNYFTQRNDDLIFVMENVPQIKEIKDELKKLFGDIGHKVYFNILRAEDYGNPSKRARMFISNIKLKPKKVDKLVVVEEALKDIPKDAKNHEIKKLSKEKVEMISKLKWGEALYRYRGKKKLMFNWYKLHPKKLAPTVKGRSRFIHPYEDRLLTVREQARLMSYPDDFVFFGGRDVQYNQIGESVPPILGRAIAKEIKKQL | Function: A putative methylase that may protect DNA from cleavage by an unknown endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36290
Sequence Length: 310
EC: 2.1.1.37
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P25240 | MKFKADQTSQKLRGGYYTPQNLADYVTKWVLSKNPKTILEPSCGDGVFIQAIANNGYNSNIELFCFELFDTEASKALERCKLNNFSNATITEGDFLVWANECLKKNKQIFDGALGNPPFIRYQFLERNFQEQAQLVFEHLDLKFTKHTNAWVPFLLSSLALLKQGGRIGMVIPSEISHVMHAQSLRSYLGHVCSKIVIIDPKEIWFEDTLQGAVILLAEKKQYPDEASQGVGIVSVSGFEFLQEDPNVLFNDTAGINGETVEGKWTKATLSIDELQLIKRVIAHPDVRKFKDIAKVDVGRYCDGANNYFLVDNETVKLYK... | Function: A gamma subtype methylase that recognizes the (non-palindromic) double-stranded sequence 5'-CTGAAG-3', methylates A-5 on both strands, and protects the DNA from cleavage by the RM.Eco57I endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine i... |
Q8U4Q8 | MPKIGIIGGSGVYGIFEPKETVKVHTPYGRPSAPVEIGEIEGVEVAFIPRHGKYHEFPPHEVPYRANIWALHELGVERVIAVNAVGSLKEEYKPGDIVIIDQFIDFTKKREYTFYNGPRVAHISMADPFCPELRRIFIETAKELNLPVHEKGTYICIEGPRFSTRAESRMFRQFADVIGMTLVPEVNLARELGMCYVNISTVTDYDVWAEKPVDAQEVLRVMKENEEKVQKLLKRAIPKIPEERKCGCADVLKTMFV | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
Q2RXH9 | MSEAYRQPVLGVIGGSGVYDIDGLEGARWQTVESPFGDVSDQILRGTLDGLEMAFLPRHGRGHVLAPSDVNYRANIDALKRAGVTEILSVSAVGSLAEDLPPGTFVIADQFIDRTFAREKSFFGKGLVAHVSMAHPVSAWLGDRVEEVLADLAIPHRRGGTYLCMEGPQFSTLAESNLYRQWGCHVIGMTNMPEAKLAREAEIAYCTVAMVTDFDCWHPDHDHVSVEAVVRVLLQNADKARSLVKAMPAKLKDRPYPLPDGSHRSLDNAIITHPDRRNPGMARKLSAVAGRVLG | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate . Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adeno... |
Q97W94 | MIEQNEKASIGIIGGSGLYDPGIFSESKEIKVYTPYGQPSDFITIGKIGNKSVAFLPRHGRGHRIPPHKINYRANIWALKELGVRWVISVSAVGSLRMDYKLGDFVIPDQFIDMTKNREYSFFDGPVVAHVSMADPFCNSLRKLAIETAKELNIKTHESGTYICIEGPRFSTRAESRTWREVYKADIIGMTLVPEVNLACEAQMCYATIAMVTDYDVFAEIPVTAEEVTRVMAENTEKAKKLLYALIQKLPEKPEEGSCSCCNSLKTALV | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
Q09816 | MNKQAEPILLGVIGGSGFYDLPGFDIVESVNPITPWGYPASPISIARTTSGFLIAFLARHGVGHIYTPTEVPSRANIAALKSLGVLAIVSFSAVGSLREDIPPEDFVLPTQIIDRTLCARPNTFFESGCVAHVSFGDPFDQDLYEILSSCGSNLKNGSKLHTKRKGDDLTVVCMEGPAFSTRAESNLYRSWGASIINMSVIPEAKLAREAEIAYQMVCMATDYDCWRMNEEPVTVETVMEHISNNKDNAKIFLLEAVKKLEAPLLQGFLGRNLRESVQNGIQTNHKHRNPDAIRRLQFLFPNLTIPH | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
Q8DJE4 | MTAKIGIIGGSGLYKMEALTDVEEVRLTTPFGDPSDAFICGKIGGVPVVFLARHGRHHHLLPTEIPFRANIYGFKSLGVEYLLSASAVGSLQEAVKPLDIVVPDQFIDRTRNRISTFFGDGIVAHIGFADPVCPALAGVLADAIADLNLPDVTLHRQGTYVCMEGPAFSTLAESNLYRSWGGTVIGMTNLPEAKLAREAEIAYATLALVTDYDCWHPEHDSVTVEMIMGNLQRNVKNAQAIICETVKRVHAHPPVSKAHRALKNAILTPLDQVPAATKEKLHLLLAKYL | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
Q4PH43 | MSVPTVTSWTGAPILLGVIGGSGLYKLDSITPVAEISISTPWGSASSPITIAKTSAGNHVAFLARHGRDHAILPSNVPNLANIAALKHLGVKAIVAFSAVGSLREEIAPKDFVIPSQIIDRTKGVRRASFFGFGDEESVVAHAGFGDPFCETLRPIVYSTVQATLASHPIKVHTDKTVVCMEGPQFSTRAESLMYRTWGGDIINMSVLPEAKLAREAEIAYVLIATATDYDAWRPSTAAVNVAEVMESLKANVEASNLVTTKVLDRVWLEIDTDEKPAVKNIKDSTKFSIMTKSQVIPDKAKQNLRFLHPWFARD | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
F6V515 | MAGVCAVKVGIIGGSGLDDPDILEGRLEKYVDTPFGKPSDALVLGKIKNVDCVLLASRHGRQHTIAPTNVNYRANIWALKSEGCTHILVTTACGSLREEIQPGDIVIVDQFIDRTTKREQTFYDGGPSCLPGVCHIPMAEPFCAKTREVLIDIAKRLGIKCHSKGAMITIEGPRFSSKAESQMFRLWGADVINMTTVPEVILAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKATSILLTAIPQIAAMDWTELLQSMKSTVQLSVMLPKH | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
Q07938 | MNRIKNTFSVAKRLKLSKVMTNSELPSIFEGTVDLGIIGGTGLYNLDCLEPIALLPPMVTPWGTTSSPVTISQFVGTNSHFHVAFIARHGINHEYPPTKVPFRANMAALKNLNCKAVLSFSAVGSLQPHIKPRDFVLPQQIIDRTKGIRHSSYFNDEGLVGHVGFGQPFSQKFAEYIYQFKNEITNPESEEPCHLHYDKDMTVVCMEGPQFSTRAESKMYRMFGGHVINMSVIPEAKLARECELPYQMICMSTDYDAWRDEAEPVTVETVIGNLTNNGRNANILASKIIVSMAKEIPEFMHTGDGLRGSIKKSISTKPEA... | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenos... |
P71039 | MKYQVKQVAEISGVSIRTLHHYDNIELLNPSALTDAGYRLYSDADLERLQQILFFKEIGFRLDEIKEMLDHPNFDRKAALQSQKEILMKKKQRMDEMIQTIDRTLLSVDGGETMNKRDLFAGLSMKDIEEHQQTYADEVRKLYGKEIAEETEKRTSAYSADDWRTIMAEFDSIYRRIAARMKHGPDDAEIQAAVGAFRDHICQYHYDCTLDIFRGLGEVYITDERFTDSINQYGEGLAAFLREAIIIYCDHQENPRP | Function: Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.
Sequence Mass (Da): 29936
Sequence Length: 257
Domain: The central dimerization domain of the first subunit forms a two-heli... |
P0C0Y5 | MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAARGCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKCQVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDGSVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITASMSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVNSISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKGAYVYFASDASTYTTGADLLIDGGYTTR | Function: Interconverts D-mannitol and D-fructose. Not active with fructose 6-phosphate or NADH.
Catalytic Activity: D-mannitol + NADP(+) = D-fructose + H(+) + NADPH
Sequence Mass (Da): 28464
Sequence Length: 267
EC: 1.1.1.138
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P42754 | ILSPFKFSRRATGDNDVRFKVLYCGVCHSDLHMVKNEWGMTTYPIVPGHEIVGRVTEVGSKVEKFKVGDAVGVGCLVGSCLSCENCDDDSENNCAKQVQTYAFTNVDGSITYGGYADSMVADQHFVLRWPENLPLDSGAPLLCAGITTYSPLRYHGLDKPGTKVGVVGLGGLGHVAVKMAKAFGAHVTVISTSESKKQEALEKLGADEFLVSSDSDQMQAATGTLHGIIDTVSALHPVVPLLGLLKVNGKLVMVGAPEKPLELPVFPLLMGRKVLAGSNIGGLKETQEMLDFAAQHNITADVEVIPVDYVNTAMERLVKS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level (By similarity).
Catalytic Activity: D-man... |
O00058 | MTFTIDLKDQCIIVTGGNRGIGLAMSQACADAGAAVGIIYNSAKDAEDRASEISKKYGVKCKAYQCDVGQQHKVKEVFKKINEELGPVTGLIANAGVSVVKEALQYNKDDFNKIFDVNVFGVFNCAQAMAQIWTDTGFQRGSVVIISSMSSQICNRPLTQCFYNSSKAAVSNLGKCLAAEWAEKSIRVNMLSPGYVKTDQTSHMDQKLRDFQADGVPLKRFAEPEEMAGQAILLLSPKASYMTGGEYFVDGGNLVW | Function: May be involved in hexitol or pentitol metabolism.
Catalytic Activity: D-mannitol + NADP(+) = D-fructose + H(+) + NADPH
Sequence Mass (Da): 27842
Sequence Length: 256
EC: 1.1.1.138
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P9WLZ7 | MAAEMDWDKTVGAAEDVRRIFEHIPAILVGLEGPDHRFVAVNAAYRGFSPLLDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSGSEWRLQTDYDGSGVEERYFDFVVTPRRRADGSIEGVQLIVDDVTSRVRARQAAEARVEELSERYRNVRDSATVMQQALLAASVPVVPGADIAAEYLVAAEDTAAGGDWFDALALGDRLVLVVGDVVGHGVEAAAVMSQLRTALRMQISAGYTVVEALEAVDRFHKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADASARYVEPTGAGPLGSGTGFPVRSEVLNIG... | Cofactor: Binds 2 manganese or magnesium ions per subunit.
Function: Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon . Possesses both phosphatase and kinase activities . The kinase domain functions as a classic anti-sigm... |
Q9HUH5 | MTNYLYLAIAIAAEVVATTSLKAVAGFSKPLPLLLVVGGYVLAFSMLVLVMRTLPVGVVYAIWSGLGIVLVSLVAMFVYGQRLDPAALLGIGLIIAGVLVIQLFSRASGH | Function: Confers resistance to ethidium bromide, acriflavine and methyl viologen.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11489
Sequence Length: 110
Subcellular Location: Cell membrane
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O29544 | MVVKVGVLKMGAIGTALLVEYLLDERADREDIEVRVVTSGAKMQPEEAVVAEKLKEFDPDVVIVVSPNAALPGPKAAREAFEGKPVIVISDAPAKKAKDELKEKGFGYILINADSMIGARREFLDPTEMALFNADVVKVLAATGAFRLVQEAIDKVIEDIKAGKQPELPQIVVTAEKAVEAGKFSNPYAKAKAMAAFYIAEKVADIDVKGCFIEKDPEKYIPLVASAHEMMRIAAILADQAREIEKSNDTVFRNPHAKDGKILGKTQLMAKPE | Function: Catalyzes the oxidation of methylene-H(4)MPT to methenyl-H(4)MPT(+).
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 29645
Sequence Length: ... |
Q8THT2 | MRKMVNIGFIKMGNLGMSQVINLIQDEIAAREGITVRVFGTGAKMGPADAADTESFKQWNADFVVMISPNAAAPGPTAAREIWKDVPCIVVSDGPTKKEAREALEQEGFGYIILPVDPLIGAKREFLDPVEMASFNSDAMKVLSSCGVVRLIQEELDRVTEQVASGKSGEDLELPHIFAKPEKCVEHAGFANPYAKAKALAALHMAEKVAQVNFPACFMLKEVEQVCLTAAAGHEIMGAAAILATQAREIEKSNDTVFRQPHAKNGTLLKKVKLYEKPE | Function: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 30268
Sequen... |
Q58441 | MVVKIGIIKCGNIGMSPVVDLALDERADRKDIAVRVLGSGAKMDPESVEEVTKKMVEEVKPDFIIYIGPNPAAPGPKKAREILSQSGIPAVIIGDAPGLRVKDEMEQQGLGYIIIKCDPMIGARREFLDPVEMALFNADVIRVLAGTGALRIVQEAIDKMIDAVKEGKEIELPKIVITEQKAVEAMEFTNPYAKAKAMAAFTIAEKVGDVDVKGCFMTKEAEKYIPIVASAHEMIRYAAKLVDEARELEKAMDAVSRKPHHPEGKRLSKKALMEKPE | Function: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 30306
Sequen... |
P94951 | MTVAKAIFIKCGNLGTSMMMDMLLDERADREDVEFRVVGTSVKMDPECVEAAVEMALDIAEDFEPDFIVYGGPNPAAPGPSKAREMLADSEYPAVIIGDAPGLKVKDEMEEQGLGYILVKPDAMLGARREFLDPVEMAIYNADLMKVLAATGVFRVVQEAFDELIEKAKEDEISENDLPKLVIDRNTLLEREEFENPYAMVKAMAALEIAENVADVSVEGCFVEQDKERYVPIVASAHEMMRKAAELADEARELEKSNDAVLRTPHAPDGKVLSKRKFMEDPE | Function: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 31382
Sequen... |
Q8T3C8 | MTPVEEIIKKDIFRETPLRYLGYANEVGEAFRSLVKPVVVKFSYVVAFGYVAADSIDKGLQEYIKTHSTSTEKTKKVAIAAVDTVLWQTFASVLIPGFTINRFCFFSNLLLQKSTKLPTNMRKWTVTCLGLATIPFIVHPIDSFVEEAMDKTARKIYNEPTISNKE | Function: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function leads to apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18778
Sequence Length: 166
Subcellular Location: Mitochondrion inner membrane
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Q6PCS6 | MEPSADTHSKPVDIYRDTWVRFLGYANEVGEAFRALVPVGAVWASYGVATTYVTADAIDKGRKAAAAHGERPGKAVCVCVAVVDTFVWQALASVAVPGFTINRVCAASHFLLSRTTRWPLPVRKWTTTAIGLSTIPFIITPIDRSVDLLLDSSLRKLYSEGEKED | Function: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function leads to apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17984
Sequence Length: 165
Subcellular Location: Mitochondrion inner membrane
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Q9UDX5 | MSEPQPRGAERDLYRDTWVRYLGYANEVGEAFRSLVPAAVVWLSYGVASSYVLADAIDKGKKAGEVPSPEAGRSARVTVAVVDTFVWQALASVAIPGFTINRVCAASLYVLGTATRWPLAVRKWTTTALGLLTIPIIIHPIDRSVDFLLDSSLRKLYPTVGKPSSS | Function: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function induces the release of cytochrome c, which activates the caspase cascade and leads to apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18010
Sequence Length: 166
Subcellular Location: ... |
Q9CRB8 | MSEQQRQGAERDLYRDTWVRYLGYANEVGEAFRSLVPAAVVWLSYGVSSSYVLADAIDKGKKAGEVPSPEAGRNTRMALAVVDTFVWQSLASVAIPGFTINRLCAASLYVLGTMTHWPPTVRKWTTTTLGLLAIPVIIHPIDRSVDFLLDSSLRKLYPSVEKPSTP | Function: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function leads to apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18314
Sequence Length: 166
Subcellular Location: Mitochondrion inner membrane
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P50192 | MGFHSKNNSEYNGDFIILSSIYYWMILLYCIKFFLSKYLIYCMSLTYIDLFSGAGGFSLGFDRAGFHQLLSVEIEPHYCDTYRANFPDHQVLQQDLTTLSDDNLLRHINHRKVDVVIGGPPCQGFSMAGKIGRTFADDPRNHLFKEFVRVVKLTQPKFFVMENVARLFTHNSGKTRAEITEQFERLGYKVKCKVLNAADFGVPQLRSRIVFIGRKDGGEITFPEPSHTEYNTVGDAIGHFPKLNAGENSLILNHEAMNHSTQMLEKMSFVKNGGDRNDIPESLRPISGDVRKYIRYHSDKPSVCVTGDMRKVFHYEQNRA... | Function: A methylase that recognizes the double-stranded sequence 5'-GGTGA-3' and protects the DNA from cleavage by the HphI endonuclease . Probably methylates C-2 on the bottom strand (Probable) .
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-a... |
P50193 | MNNPKYPKVNYIGNKEKIAEWICEQLPVDVRTIADVFSGGCSFSFEAKKRGYQVIANDILNINYQLALALIVNNQEILTACDVDFIFSNPPKSGFMTKNYSDVFFFKEECRELDAIRANILKLNNTYKQALAFALMRRAMIRKMPYSRFTISWEKVKQLRDEEYSYSKYGRRRAYHNQSFEFHFRENLNSYNQAVFNNGNIHQAYNEDVFELLDHIQADAVYLDPPYTGTMNNYFGFYGLLDSYMSGEIRQPFDNHFMDKNQAVELFEKLIEKLKPFKYWLLSYNNVSRPNREELTAMLSRNGRKVTVLETPHVYKVTGK... | Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GGTGA-3', probably methylates A-5 on the top strand, and protects the DNA from cleavage by the HphI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+)... |
Q9FJI2 | MLAKTVFPRGLLVLRSFSSVASKTLLKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAVYVSQSLHFRSPVYIGDEILGLVQAIALRETKNKYIVKFSTKCFKNHNELVVIDGEATAILPNLDMLQKSPSE | Function: 3-hydroxyl-[acyl-carrier-protein] (3-hydroxyl-ACP) dehydratase required for mitochondrial fatty acid synthesis (mtFAS) . MtFAS are essential for photorespiration and plant development, probably by influencing mitochondrial membrane lipid composition and other lipid metabolic pathways .
Catalytic Activity: a (... |
P44414 | MDESKKISLGQFFTPTHIVKYMIGLMTKNKNASILEPSSGNGVFLDSLIQLGYTNLTSYEIDGDIISHPFVINSSFITSYDKPQYDSIIGNPPYVRWKNLSELQKKELKDNSIWKMYCNSLCDYFYIFIIKSILQLKVGGELIFICPDYFFSTKNAEGLRKFLINNGSFEKIILFNESKVFHGVSSSVVIFKYIKGKNIDNINIINIDSKSPIKSEDIESLGESYYIPRFSSSDVWVTSPNHIKVALDKFESYCKTIKKVQPKSLFDDLEFSRIGSVCDIGNGMVSGLDKAFQMNDINYSELELLNSICVAKAKHLDAFC... | Function: A gamma subtype methylase, recognizes the double-stranded sequence 5'-GTYRAC-3', methylates A-5 on both strands, and protects the DNA from cleavage by the HindII endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl... |
Q9XWE6 | MSAIKEVKSELRQFMKTLLGKISKEETQRQTEAVFEKIIESKWFQESKRLSVYVSTSGEIQTDSIIQKALEMGKEVFIPQFTKGSTAMDMVRVPDQTAFDNLPSTLWGIRQPEPKWKWQSYHETGPLDLILAPGVAFSPYGLRCGHGKGYYDRFFSTHHKHFPENSPKKIGLALREQIIGTIPISETDVELDEVIYEGETIIFDTI | Function: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-m... |
P49914 | MAAAAVSSAKRSLRGELKQRLRAMSAEERLRQSRVLSQKVIAHSEYQKSKRISIFLSMQDEIETEEIIKDIFQRGKICFIPRYRFQSNHMDMVRIESPEEISLLPKTSWNIPQPGEGDVREEALSTGGLDLIFMPGLGFDKHGNRLGRGKGYYDAYLKRCLQHQEVKPYTLALAFKEQICLQVPVNENDMKVDEVLYEDSSTA | Function: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltet... |
Q9D110 | MAAVTVNSAKRGLRAELKQRLRALSAEERLRQSLLLTQKVIAHNQYQNSKRISIFLSMQDEVETEVIIKDIFKQGKICFIPRYQFQSNHMDMVRLTSSEEIALLPKTSWNIHQPGEGDVREEALSTGGLDLIFLPGLGFDKDGNRLGRGKGYYDTYLKRCVQHQEVKPYTMALAFKEQICPQIPVDEHDMKVDEVLYEDSPAS | Function: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-m... |
P75430 | MDKNALRKQILQKRMALSTIEKSHLDQKINQKLVAFLTPKPCIKTIALYEPIKNEVTFVDFFFEFLKINQIRAVYPKVISDTEIIFIDQETNTFEPNQIDCFLIPLVGFNKDNYRLGFGKGYYDRYLMQLTRQQPKIGIAYSFQKGDFLADPWDVQLDLIINDE | Cofactor: Magnesium. It can also use divalent cations such as manganese, calcium, zinc, iron, cobalt and copper.
Function: Involved in folate metabolism. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltetrahydrofolate.
Catalytic Activity: (6S)-5-formyl-5,6,7,8-tetrahydr... |
O27564 | MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILG... | Function: Calcium-gated potassium channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37314
Sequence Length: 336
Domain: The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators o... |
Q9SE60 | MKVVDKIKSVTEQGQTAFSFEFFPPKTEDGVENLFERMDRLVSYGPTFCDITWGAGGSTADLTLEIASRMQNVICVETMMHLTCTNMPIEKIDHALETIRSNGIQNVLALRGDPPHGQDKFVQVEGGFACALDLVNHIRSKYGDYFGITVAGYPEAHPDVIEADGLATPESYQSDLAYLKKKVDAGADLIVTQLFYDTDIFLKFVNDCRQIGINCPIVPGIMPISNYKGFLRMAGFCKTKIPAELTAALEPIKDNDEAVKAYGIHFATEMCKKILAHGITSLHLYTLNVDKSAIGILMNLGLIDESKISRSLPWRRPANV... | Function: The probable reversibility of the MTHFR reaction in plants suggests that they can metabolize the methyl group of 5,10-methylenetetrahydrofolate to serine, sugars and starch.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequenc... |
Q10258 | MKISDKLLHPDWKEKVTYSYEFFPPKTSTGVQNLYNRIDRMKTWGRPMFVDVTWGAGGTSSELTPGIVNVIQTDFEVDTCMHLTCTNMSTEMIDAALKRAHETGCRNILALRGDPVKDTDWTEGESGFRYASDLVRYIRTHYNDEFCIGVAGYPEGYSPDDDIDESIKHLKLKVDEGADFIVTQMFYDVDNFIAWVDKVRAAGINIPIFPGIMPIQAWDSFIRRAKWSGVKIPQHFMDTLVPVKDDDEGVRERGVELIVEMCRKLIASGITRLHFYTMNLEKAVKMIIERLGLLDENLAPIVDTNNVELTNASSQDRRIN... | Function: Major methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. Performs 80 to 85 percent of the total methylenetetrahydrofolate reductase activity of the cells.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofola... |
P46151 | MSIRDLYHARASPFISLEFFPPKTELGTRNLMERMHRMTALDPLFITVTWGAGGTTAEKTLTLASLAQQTLNIPVCMHLTCTNTEKAIIDDALDRCYNAGIRNILALRGDPPIGEDWLDSQSNESPFKYAVDLVRYIKQSYGDKFCVGVAAYPEGHCEGEAEGHEQDPLKDLVYLKEKVEAGADFVITQLFYDVEKFLTFEMLFRERISQDLPLFPGLMPINSYLLFHRAAKLSHASIPPAILSRFPPEIQSDDNAVKSIGVDILIELIQEIYQRTSGRIKGFHFYTLNLEKAIAQIVSQSPVLSHIVNESSEEEGEDET... | Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH
Sequence Mass (Da): 73942
Sequence Length: 657
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.20
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O74927 | MKIVDLIDKIPNGNAFYSFEYFPPKTTVGLENLSSRITRMSRNMMPLFSSVTWGTAGSTAEVSIYLAKMLEQHHKIPACLHLTCTNVDKAIIDKALETAKEYGIRNILALRGDPPLNSDHWEGKVSEFEHAVDLVRYIREKYGDYFCIGVAAYPEGHVDSNVPELSKDPLRDIPFLIEKVEAGADFIITQIFYEPEAFIKFENFVRNHSSNALRNIPIIPAIMPIQSYGSLKRMTRLCGCSVPSSLMQRLNAAKPDDEAIKNIGVEHIVDMIKKIMDNVQGRVHGFHFCTLNLERSVALILKNSGLLTKRWKQVESEMED... | Function: Major methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. Performs 15 to 20 percent of the total methylenetetrahydrofolate reductase activity of the cells.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofola... |
P53128 | MKITEKLEQHRQTSGKPTYSFEYFVPKTTQGVQNLYDRMDRMYEASLPQFIDITWNAGGGRLSHLSTDLVATAQSVLGLETCMHLTCTNMPISMIDDALENAYHSGCQNILALRGDPPRDAENWTPVEGGFQYAKDLIKYIKSKYGDHFAIGVAGYPECHPELPNKDVKLDLEYLKQKIDAGGDFIITQMFYDVDNFINWCSQVRAAGMDVPIIPGIMPITTYAAFLRRAQWGQISIPQHFSSRLDPIKDDDELVRDIGTNLIVEMCQKLLDSGYVSHLHIYTMNLEKAPLMILERLNILPTESEFNAHPLAVLPWRKSL... | Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH
Sequence Mass (Da): 68560
Sequence Length: 600
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.53
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Q13614 | MEKSSSCESLGSQPAAARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSADNFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD... | Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate . Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinosit... |
Q22712 | MTVTSSAAIDIGGGGGGRRSDRLDSDRTSEDMSFIASPANESFQIGASFVDVQNESSGSIDTATATLHELNYTFGMPPVTEESENMPQNYETVVELLPGEERAPINKLTEFPIEGGSLFVTNFRIVVILKDKEVEEALRFLVFPLQDIEQIDLAIPAFIHLSLKIGRMFTICFKTAEDAALVHKILYTAFQRLNRPISSIYTSRPQDWTSKNTDNPMQSLNAFAWKFSEAVDELDRDGKLPSWLLRADSVAQEITHIDFNRLGMSEHFQISSVNENFEVCPTYPEKIIVPKGITDDDIRKGAPYRSIGRFPAVIWRCRKT... | Function: Preferentially dephosphorylates phosphatidylinositol 3-phosphate (PI3P), and has some activity towards phosphatidylinositol 3,5-bisphosphate (PI35P) . May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues (By similarity). Positively regulates autophagy and is recruited to autophagosom... |
G5ED68 | MRFEDIGISKVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLF... | Function: May dephosphorylate phosphatidylinositol-3-phosphate (PI3P) . In association with mtm-9, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels . Regulates fluid phase endocytosis in coelomocytes . Controls the endosomal localization of sorting nexin snx-3 and the ... |
Q9Y217 | MEHIRTTKVEQVKLLDRFSTSNKSLTGTLYLTATHLLFIDSHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRTVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDSERLQGWQLIDLAEEYKRMGVPNSHWQLSDANRDYKICETYPRELYVPRIASKPIIVGSSKFRSKGRFPVLSYYHQDKEAAICRCSQPLSGFSARCLEDEHLLQAISKANPVNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGTKGLSVNDFYSGLESSGWLRHIKAVMDAAIF... | Function: Phosphatase that acts on lipids with a phosphoinositol headgroup . Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate (Probable). Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphat... |
Q8VE11 | MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAQQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERRNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCRQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLNAIANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIF... | Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P... |
Q7U4U9 | MSITHLLIDIEGTTCPVSFVSEVLFPYAKQSLSSYLNDHQEDLDLKNILQEAEREWDGDPSPDSIKLRQATRNQNLNFIDSIKVYFEYLINVDRKSTALKDLQGKIWDNGYRKGEITSHLFNETTECLKRWHRRQLSLSVYSSGSIQAQKLLYRHTNDGDLEHLFDHWFDTHTGNKKECASYRKIATKISTNPSEILFISDNGEECDAAGASGMETLFSLRDGNPDQSPRSHRVIKTLNDVDEYL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
C0QPL9 | MIKAVLIDIEGTVSPISFVKEVLFPYSKERIEEFIKKNLDNPDIKRIIQDIKNIEGRDLTLEEVVNTLIRWIDQDKKITPLKEIQGYIWEEGFRSGRLKAPVYEDAYRKLKEWKEKNIPMYIYSSGSVKAQKLFFSHTEYGDLTGFFSGFFDTKTGNKKDPQSYLKIAEAVGLKPENILFLSDNPDEIRAAAEAGMKVIKISRPEDSPYIDNFPYRQVDSFDQITDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q7V8Y7 | MITHILLDIEGTTCPTSFVSDTLFPYADTHLEGFLNEHIENNEVQSLIDEAWHEWQADEDPSSKDLLSKAFRENSSEIENICSYLHHLITIDRKSSALKDLQGRIWREGYEKGDISSSLYPETIEVLNKLKQQDYILAVYSSGSISAQKLLYRHTTNGDQTALFSHWFDTRTGNKKESKSYSDISIAMNIPVEKVMFVSDSCAECNAAKKAGMSVLFSLREGNPEQDPHDHQPIKDLRCLFDYLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q9I340 | MTIKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERVIAILLQWIAEDRKATPLKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLDGHPTVASSPTSSWSERAGYPEGTLLLGSIAPWVPPSAG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
B0JUK9 | MAILRLENGTTYTQLADISLELAKLNVTLNYWPIENEATRQLLKQASLTDEEKEIVLTSLDGYFEQLKQEAGYQARDLIVLHPEIANLDTLLAKFERCHTHADDEVRYIIDGEGVFGFVFADGSQGELTIQPQEYINVPAHSEHWFHLTASKRVKAVRYFTSTAGWVPEYTETVIRFPSLTAV | Cofactor: Binds 1 Fe(2+) cation per monomer.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobuty... |
A9VCM7 | MKSWYMADVPEGGDPREPYMTDPLQEVSAEQLKALGVLYWHIPVEDHEEKLKAVCDERNYAAQDMITCSREKLPNYEDKLKTFFTEHLHEDEEIRYVTAGTGYFDVRSKDDRWIRIQVQPGDLLILPSGIYHRFTLDTDNYIQAKRLFQAEPKWTPINRPADDNSFRVEYLKALQN | Cofactor: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Function: Catalyzes 2 different reactions between oxygen and ... |
Q8YTJ3 | MATLLLEDGTIESNLDEIVRELAPLGIYLKHYDPGTSILFPHLLTQDALTDKEKCHIVDLHNSVFEFIQQENGYLWCDLLNVHPGSPNLQTLIATYAQYHTHTAPEALYVLAGEMIFGFVKPDGSQVQLLVQSQDYLHIPSGVEHWCSLTASLNFKAVRYFTAADGWVPNYTGTRLNDSLNK | Cofactor: Binds 1 Fe(2+) cation per monomer.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobuty... |
Q0UG91 | MRAYWFDNLEGDQRQPHDSGRAVDPAYLSKLGVLYHHISSQSEVDELAKARDYKNRDEITVSPEKMGDIYEEKVKSFFHEHLHEDEEIRYILDGAGYFDVRSEGDDWVRIWLEKGDLIILPSGIYHRFTTDEQNYTKAMRLFKDEPKWTPLNRGEETDENQFRQEYLKLRQGLAA | Cofactor: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Function: Catalyzes 2 different reactions between oxygen and ... |
A2CBN5 | MSRLSIHPEGNTNATSPAEPLLESDDPAVIKAELAKRGIEFQHWPAKVKLHQNSIESDILAAYAVEIARVQADGRYPTVDAIRITPDHPDREALRQKFLAEHTHAEDEVRFFVEGRGLFCLHIGAEVLQVLCEQNDCINVPAGTRHWFDMGSKPQFCAVRFFDNPEGWIASFTGDAIAERFAKLP | Cofactor: Binds 1 Fe(2+) cation per monomer.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobuty... |
Q3KFI8 | MSSLSVYHVSSPEIPNKVLTHFEDIASTLAEQGVRFDRWQAAAKIQPGASQEEVIGAYKEQIDKLMTERGYITVDVISLNSDHPQKAELRAKFLEEHRHGEDEVRFFVAGRGLFTLHIDDYVYAVLCEKNDLISVPAGTKHWFDMGENPHFVAIRLFNNPEGWVANFTGEDIAGRFPRLED | Cofactor: Binds 1 Fe(2+) cation per monomer.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobuty... |
P51052 | CHSLRYDRLYSRRNTCLYLLLTWMLTALATVPNFLVGSLKYDPRVFSCTFTQTASSSYTVCVVLIHFLVPLGVVSFCYLRIWTLVIRVKGRVRPNPKVRAADLRNFLTMFVVFVLFAVCWAPLNFIGLAVAINPAKVAPNIPEWLFVTSYF | Function: High affinity receptor for melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibits adenylate cyclase activity (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17277
Sequence Length: 151
Subcellular Location: Cell membrane
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P49219 | MMEVNSTCLDCRTPGTIRTEQDAQDSASQGLTSALAVVLIFTIVVDVLGNILVILSVLRNKKLQNAGNLFVVSLSIADLVVAVYPYPVILIAIFQNGWTLGNIHCQISGFLMGLSVIGSVFNITAIAINRYCYICHSLRYDKLYNQRSTWCYLGLTWILTIIAIVPNFFVGSLQYDPRIFSCTFAQTVSSSYTITVVVVHFIVPLSVVTFCYLRIWVLVIQVKHRVRQDFKQKLTQTDLRNFLTMFVVFVLFAVCWAPLNFIGLAVAINPFHVAPKIPEWLFVLSYFMAYFNSCLNAVIYGVLNQNFRKEYKRILMSLLT... | Function: High affinity receptor for melatonin. Likely to mediate the potent effects of melatonin on pigment aggregation in melanophores. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity.
Location Topology: Multi-pass membrane protein
Sequence Mas... |
Q13585 | MGPTLAVPTPYGCIGCKLPQPEYPPALIIFMFCAMVITIVVDLIGNSMVILAVTKNKKLRNSGNIFVVSLSVADMLVAIYPYPLMLHAMSIGGWDLSQLQCQMVGFITGLSVVGSIFNIVAIAINRYCYICHSLQYERIFSVRNTCIYLVITWIMTVLAVLPNMYIGTIEYDPRTYTCIFNYLNNPVFTVTIVCIHFVLPLLIVGFCYVRIWTKVLAARDPAGQNPDNQLAEVRNFLTMFVIFLLFAVCWCPINVLTVLVAVSPKEMAGKIPNWLYLAAYFIAYFNSCLNAVIYGLLNENFRREYWTIFHAMRHPIIFFS... | Function: Does not bind melatonin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67369
Sequence Length: 617
Subcellular Location: Cell membrane
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O88495 | MATVPKSNMGPTKAVPTPFGCIGCKLPKPDYPPALIIFMFCAMVITVVVDLIGNSMVILAVTKNKKLRNSGNIFVASLSVADMLVAIYPYPLMLYAMSVGGWDLSQLQCQMVGLVTGLSVVGSIFNITAIAINRYCYICHSLQYKRIFSLRNTCIYLVVTWVMTVLAVLPNMYIGTIEYDPRTYTCIFNYVNNPAFTVTIVCIHFVLPLIIVGYCYTKIWIKVLAARDPAGQNPDNQFAEVRNFLTMFVIFLLFAVCWCPVNVLTVLVAVIPKEMAGKIPNWLYLAAYCIAYFNSCLNAIIYGILNESFRREYWTIFHAM... | Function: Does not bind melatonin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65130
Sequence Length: 591
Subcellular Location: Cell membrane
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Q62953 | YCYICHSLQYNADLQPANTCIYLVVTWVMTVLDVLPNVYIGTIEYDPRTYTCYFNYVNNPAFTVTIVCIHFVLPLIIVGYCYTKIWIKVLADRDPAGQNPDNQFAEVRNFLTMFVIFLL | Function: Does not bind melatonin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13837
Sequence Length: 119
Subcellular Location: Cell membrane
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Q9NAA5 | MADRKSDEGEDEYQHKEQMVTNRTSSFQPKSTEDSISKLAKMRAADRREEFMEERASFSAVKRGYQAGDDEEDDFTAEEEPPAKKPLTVAERLMAAMGHKAGEGLGKHGQGISEPIASSTQRGRTGLGHNAGKATARDFNEVWDETTEEKTVVERVEWMTDIEEEKRAEICEQLKDDKWMVIGKEKRTIDDETKFCSQQSITEMIEAKNVFDLMSDKDLREARTRANPYETIGSAFFQNRAAMKTANMDKIYDWILSRENTENDRFLLKNPLQESQTAENVDRSEDLFYFADVCAGPGGFSEYMLWRKGFYNAKGFGFTL... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation.
Catalytic A... |
P14751 | MANRSHHNAGHRAMNALRKSGQKHSSESQLGSSEIGTTRHVYDVCDCLDTLAKLPDDSVQLIICDPPYNIMLADWDDHMDYIGWAKRWLAEAERVLSPTGSIAIFGGLQYQGEAGSGDLISIISHMRQNSKMLLANLIIWNYPNGMSAQRFFANRHEEIAWFAKTKKYFFDLDAVREPYDEETKAAYMKDKRLNPESVEKGRNPTNVWRMSRLNGNSLERVGHPTQKPAAVIERLVRALSHPGSTVLDFFAGSGVTARVAIQEGRNSICTDAAPVFKEYYQKQLTFLQDDGLIDKARSYEIVEGAANFGAALQRGDVAS | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-GAATTC-3', methylates A-3 on both strands, and protects the DNA from cleavage by the RsrI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-... |
Q54WR1 | MFQSNQYDEYNKTNKSDEENESNENENENENENENRSEDGDQDSEDSFIYEEDDEEEEDTPKLSFGAKFLAKHGHIEGQGLGKEKDGRIDLIEVDRFQSTKGLGFAENDLPEFYRVTKHILEDEDVDFPSKQRFEWISCNSEGYNFWEGFPVDHTLVKFVANDSITDKPRRGHCSVELLMELDQHKNALDTLDPNRFYVARKKSNPYESIKGSIFINRAAVKMANIDKLADLLTPIIPVPGKPRDFIYFGDVCAGPGGFTEYVYWKKTRGGKIKGEEGLDLDDVVKGFGFTIKGQCDWNVEKFSKQIPIHNFVKEYGLDD... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation.
Catalytic A... |
P52284 | MKLFEDKSVEFHKRLSKKERSDGGVFFTPKDIRDIVFEELGDFEPTNILEPTCGTGEFISDCRKVYKNSRIIGVEIDPRSAELARDGSKNEIIVHDFMTWDTDEKFDLIIGNPPYFTRPTGFKHDPSVVKCRSNICIEVLHKCITRHLADNGMLAMVLPVSILNSKFYTPTIDLITDTMDVVSARAIKKNNFMGTNVRVMVFIIRKRTPGFVSKYTFKTSLGKVIINPDGERLGSIVSGKKTIGSLNVNISFGVTLASVKEYFVDKSCSGSFPLICYNNIAKKGDLLFVSDKYSKKRFNGRAILIPRGYAHGDYSFNFID... | Function: A gamma subtype methylase, recognizes the double-stranded sequence 5'-TGCA-3', methylates A-4 on both strands, and protects the DNA from cleavage by the CviRI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-... |
Q38AH0 | MPAVADCTVVFPLRHDPASTHPDVSGLVGKAFERVNWRDAFDTFLAEERSALWAAKTAFDNTDTSAYIAARDALFPQAVSGVHGAVAFRNRAGHKLHETMEAVGLWEYLKGGATRAKGTFTFVDVCGGPGAFSQALFAMGKEHKLRLRGFGLTLRNVKGLDWYTDLPSRSFFPCYGIDGTGDVFKLENIESLCSLTCKENVRLVVADGGFDVPTEVVNFQETISCRIVYGQWLSAVKLLRPGGCFVLKLFDCFSPFTRAILFLTTHLYESVQVVKPRHSRVVNSERYLVCIGFIGAPKQWLEHFERCYQEGFVDNDNIPT... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of spliced leader and U1 small nuclear RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher l... |
Q4E123 | MSEVTDKTVEFLLRHSASRRPPDIGSLKEKAFERVNWRDAFDRFQETERLTLWETKSELDGVDEGAYRVARDALFPFAVSGSQGAVSFGNRAGHKLREVMEATGVWEHLQRETSGQKGAVVFADVCGGPGAFSQALFEMSRQYKLRMRGFGMTLRNVRGLDWYSSLPLGKFLPTYGIDGTGDIFNLANIEALLSLTIRERLKLVVADGGFNVPFNIANYQETLSGRILFGQWLAALKLLRPGGCFILKLFDTFSPLSRALLYLSTYLYDRVHVVKPRHSRVVNSERYLVCLGFLGTPGPWMEYFEHCYQVGFSDNDSIPK... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of spliced leader and U1 small nuclear RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher l... |
A2RVR7 | MRVLIRPNFLSNLIRYCSRGTHSHDRSLRSVLSSNMIRLYTTGMEPQLSPDLIKIMDQRLSAIEHRNAVLQKLINQPEYSPEEFSRANKELRKLRDSMLLINDLRAKQKEIDGLKSLVSESSDDKDMLDLAVGELDEAVEEEKRLQTLLLKSLLPKDEADERDCILEVRAGTGGEEASLFAMDIFRMYERYSQKKGWKFDIVDITESDMKGYKEASAAICGASVYGKLKFESGIHRVQRIPITEKSGRIHTSAISVAILPQADEVDVQLRNEDLRIDTYRSGGSGGQHANTTNSAVRIIHLPTGMMVSIQDERSQHMNRA... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA in mitochondria.
PTM: Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 46828
Sequence Length: 413
Subcellular Location: Mitochondrion
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A5WUX7 | MTLFFSHRLFTVWRLKCGVMDIGWPSVLPAAGKKYQIELPVVHEEELEEQFVRGSGPGGQATNKTSNCVVLRHIPSGIVVKCHETRSVDLNRKRAREILREKLEVAYKGEESELLKMKKESMQKKQDKRRKVNENIEKKRRFKEMLNSKQEDDKST | Function: Part of a mitoribosome-associated quality control pathway that prevents aberrant translation by responding to interruptions during elongation. As heterodimer with MTRES1, ejects the unfinished nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome bio... |
Q9H3J6 | MSTVGLFHFPTPLTRICPAPWGLRLWEKLTLLSPGIAVTPVQMAGKKDYPALLSLDENELEEQFVKGHGPGGQATNKTSNCVVLKHIPSGIVVKCHQTRSVDQNRKLARKILQEKVDVFYNGENSPVHKEKREAAKKKQERKKRAKETLEKKKLLKELWESSKKVH | Function: Part of a mitoribosome-associated quality control pathway that prevents aberrant translation by responding to interruptions during elongation . As heterodimer with MTRES1, ejects the unfinished nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome bi... |
Q80VP5 | MSSRSTWALLRLPLPLIRICSGKWGLRLQEKPALLFPGMAASTVQVAGRKDYPALLPLNESELEEQFVKGHGPGGQATNKTSNCVVLKHVPSGIVVKCHQTRSVDQNRKIARKVLQEKVDVFYNGENSPVHKEKLEAERRKRERKKRAKETLEKKKLLKELREASQNITEKKADADGIPRGFQE | Function: Part of a mitoribosome-associated quality control pathway that prevents aberrant translation by responding to interruptions during elongation. As heterodimer with MTRES1, ejects the unfinished nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome bio... |
Q58262 | MGVEVSNKPNVSSIQSYVEDLEYKVGLITRNRGLESGTESAGTKGLIIGVVSAIVLMGIPLALYFLMK | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
Q8TVA7 | MAEEGSELKEVIIGAPAMADTDRADTYVNDVRDSSQFFGRDARLYFGLNVNRFAGLACGMVFAGVLLVPLLLLAF | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
P80654 | MAEEHEKGVPMVLAPQMGAIDATVESIRYRAQLIARNQKLDSGVAATGIIGFAAGFLFSLLMVIVLPVAVGL | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
Q50773 | MIILSNKPNIRGIKNVVEDIKYRNQLIGRDGRLFAGLIATRISGIAIGFLLAVLLVGVPAMMSILGVI | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
Q58263 | MSEDEKLPQVIMDPADYEALKKRLDELEKKVENTNAELFQLAGKKVGRDIGILYGLVIGIILSYILPALIKIIQILSLKVLVQQ | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
O32868 | MAEEESVPKMVAPEDDIREIHSRLDEIERRLDFVWGEVYQRFGKRIGRDIGILYGLVIGLYLCMLYILLGVAFR | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
P80656 | MDGKAPAAFVEPGEFNEVMKRLDQIDEKVEFVNSEVAQRIGKKVGRDIGILYGGVIGLLLFLIYVQISSMFM | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
Q6LWY8 | MSEIPTVVTPTKDYKRLQAKLDEIENTVENTNAEIIQRTGKKAGRDVGIAYGLAIGFIFVYVLGTVLPLFDLIK | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tet... |
P03079 | MDRILTKEEKQALISLLDLEPQYWGDYGRMQKCYKKKCLQLHPDKGGNEELMQQLNTLWTKLKDGLYRVRLLLGPSQVRRLGKDQWNLSLQQTFSGTYFRRLCRLPITCLRNKGISTCNCILCLLRKQHFLLKKSWRVPCLVLGECYCIDCFALWFGLPVTNMLVPLYAQFLAPIPVDWLDLNVHEVYNPASGMTLMLPPPPADPESSTILTQEDTGPTLMGQQDTLTSRRNTGKSFSLSGMLMRTSPAKKSYHHQKMNSPPGIPIPPPPLFLFPVTAPVPPVTRNTQETQAERENEYMPMAPQIHLYSQIREPTHQEEE... | Function: Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, th... |
P03077 | MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPKRRSEELRRAATVHYTMTTGHSAMEASTSQGNGMISSESGTPATSRRLRLPSLLSNPTYSVMRSHSYPPTRVLQQIHPHILLEEDEILVLLSPMTAYPRTPPELLYPESDQDQLEPLEEEEEEYMPMED... | Function: Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with host Ppp2/PP2A the Src tyrosine kinase components S... |
O14322 | MYTTKRFQQLLKEFEVALLLKFSKQLLLLGKIESYLNNGSSMKHEECKSQIYDCRMAVKIYVCSITANKSTNLKHFVRLFFLLGDSERVNLCIKRLIYTFIGSINSVIDKKEDIEQELYSSCMHCSIMSPKLQKVMLAQKSLILNKVFDYLFFLYGLSGTSILYTAGDHIRKLDFKDSGFITPFFQLLLLVLLFTLTFKSKHSLNAYSLTASQFSGHTVCNESSLKPNENSCDLNLSRTATIKLESAEDDACQRVLGLIKSYMRPRTLEELKLEFRFEHKSVQDITTCILDEVDGVQMARVLEINPDAPILAF | Function: Has a role in meiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35852
Sequence Length: 313
Subcellular Location: Mitochondrion inner membrane
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Q9R0L9 | MSGSSRRLLWAATCLAVLCVSAAQPNITTLAPNVTEVPTTTTKVVPTTQMPTVLPETCASFNSCVSCVNATFTNNITCFWLHCQEANKTYCANEPLSNCSQVNRTDLCSVIPPTTPVPTNSTAKPTTRPSSPTPTPSVVTSAGTTNTTLTPTSQPERKSTFDAASFIGGIVLVLGVQAVIFFLYKFCKSKERNYHTL | Function: Sialomucin that may play a key role in hematopoiesis. May be involved in cell adhesion (By similarity). Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes.
PTM: Highly N- and O-glycosylated; contains sialic acid.
L... |
Q9FZ97 | MTGLGVRSSSYGSLEKTGLNGVVLPIQITTTTRTKPSKMQKDREGIVHWICKFAGRKKVGMLLLFLISAVVFLRVLYVGKGEDSQEGQGPPSLHFNGSSGVNYSNMLQTNEELNMNIGNISFKAKEVIVFPPPPIHFLGYSLPQGHPCNSFTLPPPPADRKRTGPRPCPVCYLPVEEAVALMPNAPSFSPVLKNLTYIYEEPLNRETEFGGSDFGGYPTLKHRNDSFDIKETMSVHCGFVKGPQPGRNTGFDIDEADLLEMKQCRGIVVASAVFDAFDDVKAPQNISKYAEETVCFYMFVDEETESILKRERGLDGNKKV... | Function: Probable glycosyltransferase involved in pectin and/or xylans biosynthesis in cell walls (By similarity). Together with IRX14, required for xylan and pectin synthesis in seed coat epidermal (SCE) cells . Collaboratively with GAUT11, essential for the accumulation of seed mucilage, a gelatinous wall rich in un... |
Q8TAX7 | MKTLPLFVCICALSACFSFSEGRERDHELRHRRHHHQSPKSHFELPHYPGLLAHQKPFIRKSYKCLHKRCRPKLPPSPNNPPKFPNPHQPPKHPDKNSSVVNPTLVATTQIPSVTFPSASTKITTLPNVTFLPQNATTISSRENVNTSSSVATLAPVNSPAPQDTTAAPPTPSATTPAPPSSSAPPETTAAPPTPSATTQAPPSSSAPPETTAAPPTPPATTPAPPSSSAPPETTAAPPTPSATTPAPLSSSAPPETTAVPPTPSATTLDPSSASAPPETTAAPPTPSATTPAPPSSPAPQETTAAPITTPNSSPTTLAP... | Function: May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili.
PTM: N- and O-glycosylated. Contains fucose, mannose, galactose, N-acetylglucosamine and N-acetylgalactosamine.
Sequence Mass (Da): 39159
... |
C1F8M5 | MDKFVIRGGNPLIGTVRVSGAKNSALPCMAAAILTEDEVILENIPQVRDIETERKLLTSMGAEVELGYGRAQHRTTISCRVLSDPTAKYEIVKTMRASALVLGPLVARTGLARVSMPGGCAIGARPIDLHIKGLEQMGATIVYEHGYIEARAERLKGAQIHFDKITVTGTEDLMMAAVLAEGETVLENAAREPEVTDLAALLTAMGAQIEGAGTSEIRIQGVEKLHGARHRINPDRIEAGTFLIAGAITGGDLCVSHCNPAHLGAVIAKLEEAGVRIDVLGKDSLRVRSEGHLKPIDVSTEEYPGFPTDMQAQYMALATQ... | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 46718
Sequence Length: 436
Pathway: Cell wall biogenesis; peptidoglycan biosynthe... |
P33986 | MDKFVIQGGVKLEGEVRISGAKNAALPLLAAMILADTPITLKNVPDLKDVRTLVKLIGGLGITMSYEGETVIANTSTLDNQFAPYELVKTMRASILVLGPLLARYGSAKVSLPGGCAIGSRPVDQHLKALEALGAQIEVEAGYVHAKVDGRLKGGEVIFDMVTVGGTENILTAAVLAEGVTTIRNAAREPEITDLALMLIKMGAKIEGLDTDTLVVTGVESLHGCEYSVVADRIETGSYLAAAAITGGKVKTTHTDPNLLESVLDKFEEMGAEVTRGEDWIELDMLGKRPKAVSFRTLPHPEFPTDMQAQIMAVNAIGRG... | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 44680
Sequence Length: 419
Pathway: Cell ... |
B2UNJ3 | MEKLVVHGGFTLRGAVNISGSKNASLPILAASLLTDEPVVVRRVPDVSDTNFMVQIMGQLGASVERSSGNVRVEARNLHSEAAYEQVRKMRASICLMGPLMARMQRCVIPLPGGCVIGDRPVDLHIRAIQALGAQVQIERGNLIIEAPRGLKGATVDLSGDHGPTVLGTDNLMMAAVLAEGTTVIESAASEPEVVDLANFLTKMGANIQGAGTRRIVIEGVEKLRGCNHTVIPDRIEAGTFMVAAAMMGDGVTLRRVCEEHMTVVTDLLRKCGHHVEFNERGDTVTIIAGKTPKCGEIKTAPYPGYPTDMQAQMTALFAT... | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 45409
Sequence Length: 425
Pathway: Cell wall biogenesis; peptidoglycan biosynthe... |
A1U459 | MDKLLIRGRKPLDGEIRISGAKNAALPILAATLLADEPVTVGNLPHLNDITTMIELLGRMGVELLIDEKMSVEVHANTIKHFHAPYELVKTMRASILVLGPLVAHFGEAEVSLPGGCAIGTRPVNLHIHGLEMMGADIKVENGYIKAKTNGRLKGAHIFLDTVTVTGTENLMMAAALAEGKTILENAAREPEVVDLAECLIAMGADIKGHGTATIEINGVERLHGCHYNVLPDRIETGTYLVAAAATGGRVKVKDTREDILEAVLLKLEEAGAHITTGPDWIELDMKGKRPKAVSLRTAPYPAFPTDMQAQFAAMNAVAE... | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 45094
Sequence Length: 420
Pathway: Cell wall biogenesis; peptidoglycan biosynthe... |
Q0BV27 | MIVSAQQNPDVFTALRGRVTHAAPLAPQTWFRVGGQAETLFRPADTDDLCTLQRRVSNLVPMTIIGAASNLIIRDGGLPGITVKLGRGFNEITTDGDGMIAGAAALDATVAEHAAQAGLAGLEFLCGIPGTIGGAIAMNAGAYGSDIASVLDWVELALDGDIARLEASRLSLSYRHAALPPGCAVVRARLRTRPGNTADIIARMQDIRAARDAAQPVRARTGGSTFRNPDGQKAWELIDAAGCRGLSRGGAQVSEKHCNFLLNTGEATAADLEALGEEIRQRVQASCGTTLHWEIKRIGIPFHHPECQS | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 32576
Sequence Length: 309
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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P44605 | MQNLQPFHTFHIQSNAREIIEAHSIEQLQQVWANSKSENLPTLFLGQGSNVLFLDDFNGIVILNRLMGITHEQDANFHYLHVNGGENWHKLVEWSINNGIYGLENLALIPGCAGSAPIQNIGAYGVEFKDVCDYVEVLNLNTNETFRLDTEQCEFGYRESIFKHRYQQGYVITAVGLKLKKDWQPILKYGSLVEFDPKTVTAKQIFDEVCHIRQSKLPDPNEVGNAGSFFKNPVVSSEHFEEIKKHHENLPHFPQADGSVKLAAGWLIDQCNLKGFQIGGAAVHKKQALVLINKNGATGQDVVKLAHHVRQTVAEKFGVY... | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 38344
Sequence Length: 341
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q7VJ12 | MQTHIINFAKYSSIKIGAPLEVSLIQTPQDAISALSQNMRIIGKANNLLVSPAAQKLAMLDKHFAYLKDCGNYIEIGGAYSSGRIFSYFKSHNLAGAEFLQALPGSLGGLVKMNAGMKSYEIKQLLQAINVNGKWQDRESFPMNYRDSGIEGVILAARFHKREGFNNALQADFIALRKNHPKEPSCGSCFKNPKGDFAGRLLESVGLKGYCIGDAAFSEKHANFLINKGKATFEDALSLITLAKKRVFEASGIDLECEVQILQ | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 28840
Sequence Length: 263
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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B0TGC2 | MTQITRDFRGQWMQQEPMSRHTTWKIGGPADLFAIPADEADLAGLIRRCREKGIPWMVVGNGSNLLVADKGIRGVVIHLGRAFSDRRLDDRRLTAGGGCALSGLARFAVRAGLQGLEFACGIPASLGGAVAMNAGAHGGAMENIVRWVDVIDDEGRIRRYRGEEMDFAYRHSRLQREKAIVVRVGMELRWGDREALERWMEEKLALRRKSQPLEFPNAGSVFLNPPGSLSAGQLIEEAGMKGFAIGGAQVSERHANFIVNRGGATAADVLALIDAVRARVLATCGIELQSEVRVIGDSGGQVDGGGTEDSHQRG | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 33996
Sequence Length: 314
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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O25963 | MLETTIDFSRYSSVKIGTPLKVSVLENDDEISQEHQIIGLANNLLIAPSAKNLALLGKNYDYICDKGECVEIGGAANASKIFNYFRANDLEGLEFLGQLPGTLGALVKMNAGMKEFEIKNVLESACINNQWLEKEALGLGYRSSGFSGVVLRARFKKTHGFREGVLKACQSMRKSHPKLPNFGSCFKNPPNDHAGRLLEGVGLRGYCLKRVGFAKEHANFLVNLGGAEFEEALDLIELAKARVLQEYGIHLEEEVKILR | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 28592
Sequence Length: 259
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q0C566 | MTPTSPSPDLLPTLPDVRGKLLRGAELAPYTWFRVGGPADALFLPADEEDLEAFLKALDPAIPVTPLGVGSNLIVRDGGIPGIVIRLMGKYWGEIEALDGITLTARAGALDLAVAKAAAANGITGLEFLSGIPGSLGGATRTNAGCYGSELRDRLVALHGFRRDGSRVAYRGPGKPGALPEAHFSYRHTDLPDDLIVTRLILEGTGAGDPEAISADIAALQARRAQTQPIKEKTSGSTFANPDPPGTPDQRSAWKLIDAAGCRGLKVGGAQVSPLHCNFLINTGDATAADLEALGELVRARVLENSGVELRWEVRRMGRV... | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 34020
Sequence Length: 323
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q5QY76 | MIELAERHSFKLPAQCRALIELKSSDDVEQLAFEEPYYLLGEGSNTLFVDDFYGTVICNRLLGVCIEEQESSYLITAAAGENWHNFVADLRARSIDGLENLALVPGSVGAAPVQNVGAYGVEVSTFIEQVTAWDIKEKCWVSMNKEACQFAYRDSVFKQHPGRWLITSVVFRLPKDWQPVTHYAPLNQLQGHVSAQKIFDTVVEVRQKKLPDPKVIPNAGSFFKNPVINKAQLDGLLQKWPDMVYFPVADNHVKVAAGWLIEHLGLKSAFVGDAAVNPHQALVLINKAQATGSDITQLALKIMKQVADASGIMLEPEVRL... | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 36876
Sequence Length: 333
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q28NP1 | MTQDLPTPRGRLTPDKDLSGLTWLRVGGPADWLFQPADVDDLCAFMAELDPAVPVFPMGVGSNLIVRDGGLRGVVIKLGRPFMDISVEGDRITAGAAVLDARLAKEAADAGVDLTFLRTIPGSLGGALKMNAGCYGSYVADHFVGAQAVLRDGTQVTLTRDDITFAYRQTDIPEGVTITSVTLQGNREDSRVLHTRMEEQLAKRDATQPTKALTAGSTFRNPAGFSSTGQADDTHELKAWKVIDDAGMRGATRGGAQMSEMHSNFLVNKGGATAADLEGLGEEVRKRVFQTQGIDLVWEIMRVGVPEET | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 33118
Sequence Length: 309
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q5FL42 | MELLNLKKQGIDIKEQIPLSRYTFTKTGGEAEYLAFPKTTDEVEKLVKVTQENKIPLTIIGNASNLIIRDGGIDGLVIILTELKNIEVNGNEVTADAGATIVDTAFTAANHGLSGMEFAAGIPGSIGGGVFMNAGAYGGEMQEAVKSVNVLTRAGEYKTYSNQEMDFSYRHSIIQENGDIVLSATFSLKPGNKLQILDHMDYLNALRRYKQPLEYPSCGSVFKRPKGHFVGPMIIKAGLQGKQIGGAQDSTKHAGFIVNKGGATATDYLDLIHLIQKVIKEKYDIDLHTEVRIIGKEN | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 32433
Sequence Length: 298
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q9ZDS7 | MSILPIIKGEYKKDYNLKHLTWFKVGGNAEIFFKPFDFADLKSFLIQNKQKLPITTFGSGSNIIIRDGGIEGVVIKLGQNFNKIEFLDNHLIVGSSCLNYNLARFCQANAISGFEFLVGIPGTIGGGVIMNAGAYGSAFQDIIVQVEALDFSGNFLTFTNKEIGFKYRGNNLPKDLILLKAVFKVNKGDSQNILLKMNKINNTRSSTQPIKERTGGSTFINPEGRKSWELIDKAGLRGYRIGGASISELHCNFMINNGNATAKDLEDLGNFVRQKVFEDSGVELNWEIKRIGKYV | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 32752
Sequence Length: 295
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q1ASA8 | MHDGTLQRLFPAAKFDEPLRRYTAWKIGGPADALLEPSSIQELLSAVELAGEHGVPVTVLGGGTNVLVRDGGIRGLTIRLAKSLRGVKLSGETLVAEAGALYPVLANMTASRGLAGLEFATGIPGTVGGAVFMNAGAYGSETARVLLWADILRDGRVVRMGPEELGLSYRRSILHDHPGWVVLRAAYRLHPGDPEDLRERIREFRTLRMNGSPNRPSCGSTFKRPPGDFPGRVIEAAGLKGLRVGQIEVSTVHANYFVNLGGGTASDALRLMELVRERVRERLGVELEPEVRVVGEP | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 31998
Sequence Length: 297
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
C0QXF2 | MFTKRKEKIHFIGIGGIGMSAIASVLNAIGFTITGSDLAKTAKTESLESSGIKVYYGHKAQNIEDDVTAVVTSSAISPTNEEIIEAKSKKITVISRGEMLAELMRLRYGIAISGSHGKTTTTSLISQIMMHAGLNPVCIIGGNHFNLKSNAACNDLSSEYMVCEADESDGSFLRLSPVINVVTNIDNDHLDYYGNVEALRVAFLEFINKVPFYGCSFLCFEDNVVKDLSKSANKKYYSYGFSKDYDFYVDRDSIRVEAPITYFTAYHNSECLGEFSVPLIGIHNVLNSLASIGVGIHLGIDIADIKEGLKTFEGVGRRLN... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 51135
Sequence Length: 462
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
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