ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
C1F686 | MKYLWVALGGALGALARYTVGVWIYERLGTRFPYGTFAINVTGCFLIGLALTVLDAHMDLSPAWRLAIPTGFIGAYTTFSTFEYETLRAAQHGQMGTAVLYFGSSLALGILAVWLGMVVGNRIVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13514
Sequence Length: 125
Subcellular Location: Cell inner membrane
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B7J9Q0 | MFATFGFIALFAVLGAWARYGQTLLVQAAFGRGFPWATLSINVLGCFLMGFLFFETLERISVSPELRTGMLTGGLGAYTTFSTFSLETLVLFENGEAVKGLLYMFTSLFLCVGAAFAGAWISHST | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13553
Sequence Length: 125
Subcellular Location: Cell inner membrane
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A4STL2 | MQTWLFVAAGGAIGACLRFGISELMALLLGRHFPYGTLVVNVVGSFIMGIAFALISHGHVVEHPMKPLLMVGILGALTTFSSFALDTVVLAQQGAYLKAVLNMGLNLSLCLAMVLLGMQLVASRV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13188
Sequence Length: 125
Subcellular Location: Cell inner membrane
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Q21Y62 | MRLMISVLAICIGASLGALARWRLGLWLNPGAVLPLGTLAANLIGGYLIGICVAVFQALPNLDPVWRLALITGFLGGLTTFSSFSAEVVGMLGQQRYALGFGTAGLHLFGSLLLTLAGIKTATFLIAFNT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13564
Sequence Length: 130
Subcellular Location: Cell inner membrane
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Q4FV70 | MQWLAIGLGAAFGACLRGWLARFNPLHHWIPLGTLGANVLGGLLIGLALVWFERMGSGLSPNIRLFVITGFLGGLTTFSTFSAEVFTFIHHGRLLAALGLVGLHVGMTLLATALGFYCFKLVL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13169
Sequence Length: 123
Subcellular Location: Cell inner membrane
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A9WPV3 | MIVIFVGLAGVLGALMRFGLDSFFAQRGRFAHGQAHHFPLATLSVNVLGSFIIGLAGGFASHAELSPDWHSAISIGIAGGLTTFSSFAVATVSLWQLGNKFSAMVNIGLNLVLGLGAAWLGLSLAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12969
Sequence Length: 126
Subcellular Location: Cell membrane
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Q98N26 | MFNLLLVVVGGGIGAGIRHLTNMGALRLVGPNYPWGTMAINIVGSFAMGLFIAILARRGGSNEVRLFVATGIFGGFTTFSAFSLDFATLWERGATLPAFGYALASVIGAIIALFLGLWLARSLP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13022
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q92QE1 | MNHILLVGAGGALGSVLRYLVGLWMLQRAGPAFPWGTLFVNVTGSFLIGFLAEFIMHKMGASPEMRVFLITGVLGGYTTFSAFSLDAIALLEHGQTMSGLAYIVASVGLSMLAVFAGLALMRAMV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13200
Sequence Length: 125
Subcellular Location: Cell inner membrane
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Q7UHW8 | MTFVSDLFAIALGGSIGAVLRYLITLTVVSAPLSGWLTLHGSVGTTLANLLGCCALGGLFQFSQALVASDWVATGWAASLAHPRTLLAVRIGVLGSLTTFSTLIGETAVFASQGRILASSMLLGINVIAGWCLFWAAAAVVRNWTS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15085
Sequence Length: 146
Subcellular Location: Cell inner membrane
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B6IQX6 | MKMILAVAAGGGLGAVARYLTGVGLGHWLGTAYPWATMTVNVTGSFAMGVLAGLGAHVWQPAPELRAFLMVGVLGGFTTFSSFSLDVALLVERGAIGAAAAYVAASFLLSVGGLFAGLALIRTAVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12629
Sequence Length: 126
Subcellular Location: Cell inner membrane
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P61394 | MAYLLVFVGGGLGAMFRHFINTLSGRLLGTAFPYHTFFINVTGSIVMGLIAGYLAFKGGSSQHFRLFLMTGILGGYTTFSAFSLDAALLYERGAVGLAVVYVLGSVVLAIAGLFGGMALIRAMT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13057
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q4WAZ3 | MLGRHECTISESVSALDPTAQEPEYTLVPSTSRDLVRDMTLNMEDAQAHLKEHGWVKIPAVLSKAEAEDALSRLWEAKAASEARGECTFQPILDPNPANVRVFYLPELDAYWRDMLVNPTALDLAKSLLGDQLLVSNFSANIARPGAESMALHSDQSIVLPAPWLDVWAVNVIWCLTRMTKENGATLYIPGSNKWTTWEDVPDNAPDLLVPFEADAGDIVVIDGRLWHTSGSNVTEDEDRAILFAYYSAPHMRPLTNWSAKLPKELQETLSPQLKELLALSHIGYVVKGDLTYMAQKYPSEKGTTAVSA | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the dioxygenase af480 acts as a 5-dehydro-6-demethoxyfumagillol... |
Q4WAZ6 | MAYELSTLQLSCVAFVAFMAVLVFRTRTRNLKQNVPPGPRPLPIIGNFFDLPPKGQPEYLHWFKHKDAYGPVSSINVMGTTLVIFHDKDAAHAVMGKKAQKTSARPQLNFAQLCGFENFLITHQYNDKYRLHRKMVHQEIGTKGLSAGFRPIQEQESIRFILQTFNRPDDILQHLKTLAAAIVLKITYGYSIERKGQDPLVELIEHAMENLSQAFVPLAWAVDSVPAIKYLPDWFPGMSYRKTARKWRAINEAAAELPYDFVKRQMAHKAHQPSYVSNLLEKHMIKSEDNKINVSAADEEAIKWTAVSLYAAGSDSTVAI... | Function: Multifunctional cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the multifunctional cytochrom... |
Q4WAZ4 | MLGLPNELSGSQVPGATEYEPGWRRVFKVEDLPGLGDYHIDNQTAVPTSIVCVIALAAAMDISNGKQANSIELYDVTIGRPIHLGTSPVEIETMIAIEPGKDGADSIQAEFSLNKSAGHDENPVSVANGRLRMTFAGHELELLSSRQAKPCGLRPVSISPFYDSLREVGLGYSGPFRALTSAERRMDYACGVIAPTTGEASRTPALLHPAMLEACFQTLLLAFAAPRDGSLWTIFVPTQIGRLTIFPNSSVGINTPASVTIDTHLHEFTAGHKADLPMIKGDVSVYSSEAGQLRIRLEGLTMSPIAPSTEKQDKRLYLKR... | Function: Stereoselective keto-reductase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the keto-reductase af490 acts as a 5-dehydro... |
P04953 | MKSLQKGFTLIELMIVVAIIGILAAIAIPQYQNYIARSQVSRVMSETGQMRTAIETCLLDGKEGKDCFIGWTTSNLLAAAGGSTTNNATAADPGQGGLNITYALESTAENKIEATFGQNAAATLHGKKLTWTRSPEATWSCSTDVDEKFKPTGCKK | Function: Major component of the type IV fimbriae that plays an essential role in twitching motility, natural transformation, and protease secretion.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16637
Sequence Length: 156
Subcellular Location: Fimbrium
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Q9VZW5 | MSGTAVARLLLRLELPSPGVMPPPPTDYDYGGPISDDEFLASAMATEGPTVRYDLFPQNNSQPTLQIVLNHTEVQTDLQYPHYEDLGLDPDPNWTRICEDVYNPLLENNRIEFWVCGVLINIVGVLGILGNIISMIILSRPQMRSSINYLLTGLARCDTVLIITSILLFGIPSIYPYTGHFFGYYNYVYPFISPAVFPIGMIAQTASIYMTFTVTLERYVAVCHPLKARALCTYGRAKIYFIVCVCFSLAYNMPRFWEVLTVTYPEPGKDVILHCVRPSRLRRSETYINIYIHWCYLIVNYIIPFLTLAILNCLIYRQVK... | Function: A receptor for the FMRFamide peptides . Reacts with high affinity to FMRFamide and intrinsic FMRFamide-related peptides . By stimulating intracellular calcium signaling through the inositol 1,4,5-trisphosphate receptor, Itpr, in dopaminergic neurons, may be involved in the maintenance of neuronal excitability... |
A3DCX5 | MRIVFMGTPEFAIPSLEMLVRERYEVAAVVTQPDKPKGRGKKTAMPPVKEFAIKNNIEVLQPSKVKTPEFVSTIRELRPDLLVTAAYGKILPQEVLDIPPYGCVNVHGSLLPKYRGAAPINWAIINGEKVTGITTMYTDAGMDTGDMLLKAEIEISDDMTAGELHDKLACLGAEVLRETLKKIEDSTLQRIPQPHEQATYAPMLDKTVGCINWSKSARDVHNLVRGTNPWPVAFTYYKGQKMKVWVTSVLDEENHNFTPGTILKVGKDGLVVACGVGKVVIKEVQFDSSRRMTVEEYICGHKVGEGEVLGQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
A1TW87 | MKIIFAGTPEFARVALERLLAAGAEVPLVLTQPDRPAGRGMKLQASPVKQCALAHGIAVAQPRGLRLDGRYAEDAAAARAALEAAGADAMVVAAYGLILPQWVLDLPRLGCLNIHASLLPRWRGAAPIHRAIEAGDAETGVTIMQMDAGLDTGAMLLIEKTAIAPRETTATLHDRLADLGGRLIVEAMELAACGGLAATPQPAEGVTYAHKIEKAESAIDWKLPAAAIDRRVRAFDPFPGASTQCSAETIKVWGCEPLQVPPPEGAQPGEILQVDDAGVDVACGGPDGAAGVLRLTVLQRAGGKRLPVGDFLRGHPLAPG... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q6F6P9 | MKIIFAGTPDFAATALDALIKTPHDIVAVYTQPDRKAGRGQKLTPSPVKQLALEHNLPVLQPLHFKSSTEEGLAAQAELAAFNADVMVVAAYGLILPQIVLDTPKYGCLNIHGSLLPRWRGAAPIQRAIAAGDAETGVTIMKMAAGLDTGDMMFKTYCPIEASDTSASLYEKLAAQGAEAICTVLECEQQLQKFLAEREVQDENQTVYAHKLVKAEAQIDWTQDAIQIDRNIRAFNPWPVAFIPLDDKNNLRVWESTVSKLIAPDAEAGKIIAMDKHGIHVACGTGVVCLTALQWPGGKALNPVQIIQTQKLNIGQVLA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B7I2C3 | MKIIFAGTPEFAATALAALLKTSHEIIAVYTQPDRKAGRGQKLTPSPVKQLALEHNIPVYQPLHFKASTEEGLAAQQELAALGADVMVVAAYGLILPQAVLDTPKYGCLNIHGSLLPRWRGAAPIQRAIATGDDETGITIMQMAAGLDTGDMMYKTYCPIASEDTSATLHDKLAAQGATAICAVLESEETLQKYLAEREVQDESLTVYAHKLVKSEARIDWSMNAVQVDRNIRAFNPWPVAFIQLDENNALRVWNSIISSQSKVNAQAGEIIAIDKQGVHVACGENTFICLTSVQWPGGKALNAQQIAQTQKLHVGQILP | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
C1F542 | MKLVFCGTPAFAVPTLEALLQAGHDVALVVTQPDRPSGRGMQVLAPPVKQTALAAGLPVVQPEKIKNNLEFRAQLEAIAPDAIIVVAYGRIIPKWMLDLPRYGNLNLHASLLPKYRGAAPIQWAVAMGETVTGATTMRIDEGLDTGDMLLQDEMEIPPAMTAEELFPLLAEMGAPLMVETLAGLEQGTVTPQKQDEAQATLAPILTREDGRVDFARSAAEIYNRWRGFQPWPGAWTMLGGKKLTLHRMLLAEREDRAEPGMVRVHAGRLFFACGDGGWLEIAELQLEGKKRMPVTDFLRGNTLAPETRLGA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B7J3C1 | MTEKQRIVFAGTPEFARITLAELRQGPEAVVGVFTQPDRPAGRGRTLQASPVKQEALAAGIPVFQPESCKTGEALELLRSLAPDLLIVVAYGQILPQAILALPTRGAINVHASLLPAWRGAAPIARAIAAGDKESGVAIMQMEAGLDSGPVLWEERLPIAADDTAASLHDRLARLGGKALRHVLDDLWAERLKPVPQDPALVTYAHKLKKEEALLDWRLPAATLERLVRAFNPSPVAHTLFRDKGLRVWQARVLGAGGDQAPGSISAVEKDGVVVTCGEDRLQLLAVQPAGKGVLSGSDFARGYRPQVGEVLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q8K974 | MKKLTIIFAGTAYFSMRYLDALTKSEHKVIAVITQPDRPSGRGQKIIFSPVKILSIKRNIPIFQPSELKNEKIQREIFNLNADMMIVVSYGKLIPKEILTMFPKGCINVHTSLLPRWRGATPIQSAILFGDKETGISIIKMNEKMDAGTIINSVKCNILPNDTTETLTFKLIEIGIQVLLKTLYYINKNIVVEKEQNEKHATFSKKISKKDALLNWNTEAYLLERLIRAFNPWPVCYFIVNQIAIRVWQAKIIPTVMKSACVGEIVAFNKNGIQINTAHQILNLQKIQFPGKKIINVEKIISSKKHWFHIGKII | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
P59557 | MILNTLNSLKIVFAGTDKFSKDHLKILVTNTTHKILGVITKPDQPLGRGKQITSSLTKKLAKKLKIPVFQPTALNTSTFYNQIYNLNADIIIVVSYGKIIPQLILNIFPLGGINVHTSLLPRWRGPSPIQSALLNGDKLTGITIIKMNNNIDTGDIIYSSSCIINKSDTSVTLQNKLKILSCQGLIQVLKNFKSSYFPIRQSNLATYSNKINKEDAKLIWLKSAIQLERSIRAYNPWPICYFKINNQLSIKVWSANVIIHFNQHKYQIGEIILINKHGMQIKTSKNILNITTVQLPGKKIMHANNLCNSKNKWCIPGTKL... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
P44787 | MKSLNIIFAGTPDFAAQHLQAILNSQHNVIAVYTQPDKPAGRGKKLQASPVKQLAEQNNIPVYQPKSLRKEEAQSELKALNADVMVVVAYGLILPKAVLDAPRLGCLNVHGSILPRWRGAAPIQRSIWAGDVQTGVTIMQMDEGLDTGDMLHKVYCDILPTETSTSLYNKLAELAPSALIDVLDNLENGKFIAEKQDGSQSNYAEKLSKEEAQLNWSLSAMQLERNIRAFNPWPIAYFSTEDKDGNAHTLKVYQAKVLPHQDKPAGTILSADKNGIQIATVDGVLNLLQLQSAGKKPMSAQDLLNGRAEWFTIGKVLA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q9K9Y6 | MKIVFMGTPDFSVPVLRRLIEDGYTIAAVVTQPDRPVGRKRVLTPPPVKVEAEKHQIPVLQPEKIRDEAELERLFSFEPDLIVTAAFGQILPNALLEYPKHGCINVHASLLPKYRGGAPIHQAIIDGEKETGITIMYMAEKLDAGDILTQVTVPIADDDHVGSLHNKLSEAGAALLAKTIPPLIKGELQSIPQDDQLATFAPNITREKEEIDWRKEGERIYNQIRGLHPWPVAYTLWNGKPMKIWWAEKVSSPKKEAPGTVIALEENGFLVATGDETALKVTDLQPAGKKRMLARDFLRGAGSQLSVGSVLGGQDGS | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B8CWS7 | MNIVFMGSPDFAVPGLEKLYNEPGITIKAVVTQPDRKKGRGHKLRPTPVKQMAHKLGLKVLQTDNINREEFITNLRDLSPEAIVVVAFGQKLGKKVLELPSYGCINLHASLLPRYRGASPIHRAIINGDKVTGVTTMYMDEGWDTGDIIYKKEVKINREDTAGTLHDKLASIGGDLLVKTLNDIEKGVAPREKQSEDKASYAYKIDRKIGELDWSRSSEDIFNLVRGVNPWPGAYTTWKGKLLKIWWVEPLKLTVTENDKKMEAGEVITASQEDGIIVKTGDDAVKIIELQLAGRKKITADKFVLGYNIKEGDKLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
C4K6Y1 | MSESLKIIFAGTPDFSACHLQHLLSHRQKILGVFTQPDRPAGRGKKLAFSPVKILATQHHIPVYQPHSLGLKEEQQSILDLDADVMVVVAYGLLLPQAVLNMPRLGCINVHPSLLPRWRGAAPIQRAIWAGDQETGVTIMQMDSGLDTGNMLYKTVYPIQPDDTGASLQAKLAALGSQDLLLTLKKMAEGKMHGETQDEQKTTYAHKLTKKEARLDWLLPAAHLERCVRAFNPWPVSYFIINEQIIKVWEAQAMPDSQQVSHLQPGTVLKADKNGIQILTSEGVLNMTKFQLPGKKIISAWDFLNSRNEWFQIGKQLLS | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B0TGS9 | MRLVFMGTPDFAVPTLEAIVAAGHEVALVVTRPDRPRGRGQKPQPSPVKEAALRLGLPVDHPACLDNEFVQKLKDLGVEAGVVVAFGRILPPRLLDAFPQRWINVHASLLPKYRGAAPIHRAVIDGEKETGITTMLMSEGLDEGDMLLKRSLAIGPDDTTGQVHDALAELGARLLVETLAAMEAGRLQPQPQDGSQASYAPMLARADEQVDWSAPAEAVHNRVRGMNPWPGAFTMDEGKILKILRGRLRHEGLPLPDPTGSAAHPGEILQIVGDEVAVATGAGVYWLSEVRPAGGKTMTAGAYARGRRIGPGFRFG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
P56461 | MRIVFMGTPGFAEVILRALVGDKDIEVVGLFTQMDKPFGRKKELKAPETKTYILENHLNIPIFQPQSLKEPEVQILKDLKPNFIVVVAYGKILPKEVLTIAPCINLHASLLPKYRGASPIHEMILNDNKIYGISTMLMDVELDSGDILESASFLREDYLDLDALSLKLAHMGAALLLSTLKNFSSITRKSQDHMQASFCKKITKSDGLVGFKDAKSLFLKSLAFKSWPEIFLENGLKLLEVELVENEKSHKEGEILEIDEKGVLVGCLKGSVRIARLQAVGKKPLKAKDYLNGKRLKIGGILA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
A9B2Z9 | MRILYLGTPEIAVAPLELLHASGHEIVGVVTQPDRPAGRKNVLTAPPVKLAAERLGIPVFQPETLKDPAAVARLRAFEPEVGVVAAYGEILRKQVLAIPALGYLNIHPSILPLYRGPAPVTGAILAGDDLVGVSIIKLTAKMDAGPILGQMVMPLANDARAGEWTAQLMRQGGELLAQVLPAYAAGQIQAQIQDDSQASYTQMISKNDGLINWNLPALVIERMTRAYDPWPGTAVKLNDQPFKILRAKAHTSWSGTIQPGTLFEQQGQILVATGSGALELLEVQPAGKRPMAANDWRRGAKDIEQL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q96DP5 | MRVLVRRCWGPPLAHGARRGRPSPQWRALARLGWEDCRDSRVREKPPWRVLFFGTDQFAREALRALHAARENKEEELIDKLEVVTMPSPSPKGLPVKQYAVQSQLPVYEWPDVGSGEYDVGVVASFGRLLNEALILKFPYGILNVHPSCLPRWRGPAPVIHTVLHGDTVTGVTIMQIRPKRFDVGPILKQETVPVPPKSTAKELEAVLSRLGANMLISVLKNLPESLSNGRQQPMEGATYAPKISAGTSCIKWEEQTSEQIFRLYRAIGNIIPLQTLWMANTIKLLDLVEVNSSVLADPKLTGQALIPGSVIYHKQSQIL... | Function: Methionyl-tRNA formyltransferase that formylates methionyl-tRNA in mitochondria and is crucial for translation initiation.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 43832
Sequence Len... |
Q31J85 | MTQPLRIIFAGTPDFSVPPLKTLIDSEHEVVAVYTQPDRPAGRGRKLTASPVKQTALEHDIPVYQPVSLKTPEAQAELEALQADVMIVVAYGLILPKAVLDMPKYGCLNIHASILPRWRGAAPIQRAIQMGDAETGVTIMQMDVGLDTGDMLTILKTPIKPEDTAQTLHDRLSALGCDAMMTTLSNLQTDQLSPVKQDERQVTYAEKLNKAEAELDWQASAQTLARQVQAFNPWPVAFTQYQGQPLRIWQAEVGHASTQKSPGLVISVSKTGMEVATGKGSLLIKQVQPSGKKAMPAYDFAQARQLTGQTLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q1AVZ9 | MRVAFAGTPEFAATVLRGLLGSGHEVGLVISQPDAPRGRGRRTASPPVALLAREAGLPLLQPASISEAAGEISRHDALVVAAYGQILRPDTLYAARHGAYNVHASLLPAYRGAAPVERAIMDGERETGVTVIRMDEGLDTGPVALQRRVPIPPDMTGGELADLLARVGAEALVEVLDRLESGTLNLTRQDSSRASYAPRITRQDQEIDWSRDARRVHDQVRALSPHIGARTRHPEVEGPLKIWRTRVHREAGRELAPGELRAGDGRLFVGCESGVVEILELQLPGGRRLGAAEFLRGHSLTGALRR | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q5LNI8 | MRVVFMGTPDFSVPVLEALVAAGHEIAAVYCQPPRPAGRGKKDRPTPVHARALDLGLEVRHPVSLKGAEAQADFAALGADVAVVVAYGLILPQAVLDAPRHGCLNIHASLLPRWRGAAPIHRAIMAGDEATGICIMQMEAGLDTGPVLLRSRTPIRAEETTGALHDRLSAMGADLIVEALARLPELTPEPQPEDGVTYAAKIDKAEARVDWTRPAVAIDRQIRGLSPFPGAWTEIAGERVKLLASRLDEGQGTPGEVLDDALTIACGTGAISLIRLQRAGKAAQDADIFLRGWPVPKGTRL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B8I255 | MKIIFMGTPEFAVPSLEMLINEGYNVIAVVTQPDKPKGRGKKLAAPPVKEFALEHGIKVLQPAKIKTPEFVEQIRELGPDLLITAAYGKIISKDMLDVPPLGCINVHGSLLPAYRGAAPIHWSIINGEKVTGITTMFTDVGLDTGDMLLKRELEISSDMTAGELHDEMAILGAEVLKDTLIHLKNGTLVRSPQDDALSSYAPIITKEVGLIDWNKTVQQVHNLVRGTNPWPGAFTFINESKMRVWKTCIVDFGNSQEHCPGEIVSVDDKGILVKCCDGYIMIKELQFDSSKRMKVRDYIRGNKIDTGEKLGK | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
A4FBJ4 | MRLVFAGTPEPAVPSLRALIESANHEVAAVVTRPDAPAGRGRKLMRSPVGALADEHGIEVLTPAKASDPEFLARLRELEPECCPVVAYGALLRQTALDIPEHGWVNLHFSLLPAWRGAAPVQAAIKHGDQITGASTFRLVPELDAGPVYGVVTEEVRDTDTSGVLLERLSVSGAKLLVATLDGIADGTLRAEEQPADGVSYAPKVEVEDARVDFTAPARAVDRLVRSVTPDPGAWASFRDERLKLGPVSIVDEDLGLAPGEIRVERRRVLAGTGSAPVALGEVQAQGKKRMAATDWARGSRIEQGERLK | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q9H479 | MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNRRTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEWQDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDLWSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQRLLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK | Function: Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate . Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions . Involved in intracellular deglycation in e... |
Q9ER35 | MEQLLRAQLHTTTLRAFGSSGGGCISEGYAYYTDSGPVFVKVNRRTQARQMFEGEMASLEALRNTGLVRVPKPMKVIDLPGGGAVFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKSKTRQNTVGCGAEGAEPQGVTKFGFHTVTCCGFIPQVNEWQEDWPTFFTRHRLQAQLDLIEKDYADRETQELWSRLQVKIPDLFAGIEIVPALLHGDLWSGNVAEDDQGPVIYDPASFYGHSEFELAIASMFGGFPRSFFTAYHRKIPKAPGFDKRLLLYQLFNYLNHWNHFGREYRSPSLGVMRKLLR | Function: Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate . Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (By similarity). Involved in intracellular d... |
P14738 | MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTI... | Function: Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and ineffici... |
Q96RU3 | MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGK... | Function: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and ... |
Q8R511 | MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNELNDYAGQHEVISENMTSQITVDLVRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQMRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELKFGGKSRGKL... | Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances a... |
Q8UHU0 | MAVVIDGKAKAASVTEAVRKSAEALEAEKGVKPGLAVVIVGNDPASHAYVNSKSKMAKQCGFNSIQHTLPEETTQAALLKLVGELNTDASIHGILVQLPLPKHFNSDEIIQSILPEKDVDGLSVLNAGKLATGDLATGLISCTPAGAMLLVRGIHGDDLSGLNAVVIGRSNLFGKPMGQLLLNANATVTMAHSRTKDLVTVCKTADILVAAVGRAAMVKGDWVKPGATVIDVGINRIAAPEKGEGKSKLVGDVAFDEASAVAAAITPVPGGVGPMTIAMLMANTVIAAHRALGKTAPKF | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
B2UM17 | MQIIDGKQVASQVLEEVERDIARLREQGITPGLAVVLVGEDPASQVYVNSKVKKCAELGMNSRKIVLPSDASQEELLRIVRELNVDPSVHGILVQSPPPPHIDEAAVVLEIDPAKDVDGFHPENVAKLVLEDETGFVPCTPLGCMRLLKAAGIETAGANAVVIGRSMIVGKPMAHLLMSKQANATVTVAHSRTKNLPELCRSADIIVAAIGRPAFVTADFVKDGAVVVDVGINRVEDASAKRGYRIVGDVAYDEVAPKCRAITPVPGGVGPMTIAMLMANTVKACRQQTGA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q0VQ92 | MTAQILDGKTLAQQFEQEMRLRVDVLKAKANGHTPILATILVGADPASATYVKMKGNACQRVGMESVAIELSEETTTAQLLAKIDELNNNQDVHGILLQHPVPAQIDERACFDAISLEKDVDGVTCLGFGRMSMGEAAYGCATPKGIMRLLEHYQVELEGKHAVVVGRSAILGKPMAMMMLEANATVTICHSRTQNLPELVKQADIVVGAVGKPEFIKADWIKDGAVVVDAGFHPERCGDIELAPLVDRVAAYTPVPGGVGPMTINTLIFQTLQSGEKAFG | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q894G6 | MAVAIDGKRVSEELRKELKNFIDERVEKGLKVPCVSSILIGNDKGSLFYIKNQRRICKEIGIEFKNIVLEENIEEDKIIEVIEDLNKDENVHGIILQMPLPKTLDEEKIVNKICPSKDIDGLTDINAGRFYKGEKCFIPCTAQGIIEIIKSTKESISGKKAVVLGRSVIVGKPVAQLLVNEDATVTICHSKTKDIKSLCKEADIIVSAMGIPKFVKEDFIKDGAIVIDVGFSVLDGKMVGDIDYDNVFKKAGFITPVPGGVGSVTPTMLIKNLCEVFK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
B5Y9D1 | MALIMKGKPVADAIYEELQPMTSLNLTLGIIKYKGSDAGGYLSGLSKAAQRLNVQLRVNEVEQFQELTQSVVVMGKDSQVHGILLLKPFPKEWNFRQASDLIPPEKDVDALHPVNLGKLAQGRGNLVPATPQAVLSILDFYNVLPLEGASALVIGRSEAVGLPAFLQLMQRNATVTVAHSRTKDLPSLSRQADLVVVAVGKPNFLTKDHVKEGAVVIDVGTNVLEDGKVVGDVDRENVEPLVRAITPVPGGVGSVTTACLFKNLFLCYQEQTR | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q8FRU9 | MTAIKLDGNLYRDEIFADLAQRVAALKEKGIVPGLATVLVGDDPASHSYVKMKHRDCEQIGVNSIRRDLPADISQEELFAVIDELNADDSCTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPVNLGKLVLNEPAPLPCTPNGSISLLRRFGIELNGAKVVVIGRGVTVGRPIGLMLTRRSENSTVTLCHTGTKDLAAETRAADVIVAAAGQPHMLTADMVKPGAAVLDVGVSRKDGKLLGDVHPDVWEVAGAVSPNPGGVGPLTRAFLVHNVVERAEKLAGL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
A9KGQ5 | MIARILDGRTCAEKVKARVKENIRLLQEKGLPSPGLAVILVGNDPASATYVAHKERACQAVGIRSTVYRMPNTITESELASKIDECNRDSNTHGILLQLPLPAHIDPANLLERIRPDKDVDGFHPYNLGRLVQRRPALRPCTPYGVMTLLTETHENLEGKHAVIVGASNIVGRPMALELLLAKCTVTVCHRFTRDLAEHVKSAELLIVAIGKPGIIQSEWIKPGAIVIDVGFSRLSPNKIAGDIDFETAKERASWITPVPGGVGPMTVATLLENTLQAAQTFL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q7NAE4 | MFIKLDGTKLSQKLKEDLAKKVNNQKIKILIIISDPSEASRIYVRNKINYCDSLGIQTEVYDLSKIDDTNQFIVEMNQKISLSNPNGVLVQLPIKERLDTNKIIENIPIRLDVDAFLYHRFDQDQKEKVIPCVLNAVLELFKEYQLSFLDKKILLIGNGITSNQPIVNYLNEHQIKFDLITKENSQLLEEKTKVADLVISAVGKAKFLANYQFKRGVIFIDIGIDKYFDPEQSKYLICGDFDYDKLKEIASYGTPTPGGIGPLTIYSLVKNLINLSEIQKVNK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
P47259 | MSFDGKLKAQSILETYKNFDWSKCKLVIIQANDDDSSDSFIKQKLIACNTVGAKSELIKLSNQITQAELIEKIISLNHDVNVTGIILQLPVYPHLDKNSLLEAINPLKDVDGLTTNHLAEIKPCIVEAIITLKELFNLEFNNQKIVVVGLGITGGKPIYEFLKTSGYKVQACDKDTPNTFELIKSADIVFTAIGKSHFFQAKNFKKGVILFDIGVSRNKQNKLCGDINPEGIEKKARWWTKTPGGVGPFTVLAIIKNLWILHEKNKRCLQSSI | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q6MSL3 | MVILDGKLVSKQIKQTLKKQIDTYLNKNYKKPKLAVILIGNDPASELYVSNKIKACNLVGIESVLLRFGQNITSEMLSDQINQLNNDNSVDAILLQLPLPKHLDEQEFLQAIDPLKDVDGFHYINQGKMLEGYDTIYPCTPIGIINLLKAYNIDVRSKDITIIGTSNIVGKPLAIMLSNMGATISMCNKNTKSLKKYTKRSDIVISTTGKQALIKKDMIKKNAIVIDVGIIKDPITNKIVGDVDFENVKELCSYITPVPGGVGPMTVSMLLENTFKLYKLHIKENYEN | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q98QV3 | MMKKLLSNELVQIKRAELKEKFSKLDQKVKFAIVLIGDNASSKIYVKKKIEFAQDIGVEAKLFHFEENVDFNLLKDAFKKIDKEYDGIILQLPVLHFDVNELLLMIDKNKDLDGLNPENEKAFYENRECIIPATARAIWTFLKFHKISVENKKVFVVGQSRLVGKPISQFLKNNNAIVRVFDKSTGLKGTEEADILIVATGVAQLIKAENIKENSILIDVGFSKINNKIYGDLDIESIKEKALKYTPPIGAIGPVTVLSLFENLYEIILKKK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
A0QSY5 | MGAISLDGKTTRDEIFVDLKERVAALTAAGRTPGLGTVLVGDDPGSQAYVRGKHADCAKVGINSIRRDLPADITTEQLNETIDELNANPDCTGYIVQLPLPKHLDENAALERIDPAKDADGLHPTNLGRLVLGKQAALPCTPRGIVHLLRRFDVPIAGAHVVVIGRGVTVGRPMGLLLTRRSENATVTLCHTGTRDLPALTRQADIIIAAVGVPHMVTADMVKPGAAVVDVGVSRVDGKLTGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVEAEESKLA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q4A6B1 | MKILSGREKAEQDLKQLKKELDELNLNRPIKLAIIQVGDKMESNRYVEQKLKKAKEIGIEAKCFKFDENITQKRLLLAMDEINENWDGILIQLPLPKHLPKEVILDAVPYEKDIDGLSHRNEFILYNEKNSDDKFFVPAAARAVLELIEHHEINYKKKKVAVVGRSHLVGKPVAHILKRRGASVSTFDENTPIKLVASADIVIVAIGVPKYIKAENIKQGAIIIDVGTNYDQNDPSVIFGDVDHESVKTKASAITPVPGGVGPLTVVCLLKNLVEIYK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
K0I977 | MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAG... | Function: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolife... |
K0I7Q2 | MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKH... | Function: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolif... |
Q5Z9N5 | MPPTLLLLLLLLPPSLASPDRDIYALAKLKAALVPSPSATAPPPLADWDPAATSPAHCTFSGVTCDGRSRVVAINLTALPLHSGYLPPEIALLDSLANLTIAACCLPGHVPLELPTLPSLRHLNLSNNNLSGHFPVPDSGGGASPYFPSLELIDAYNNNLSGLLPPFSASHARLRYLHLGGNYFTGAIPDSYGDLAALEYLGLNGNTLSGHVPVSLSRLTRLREMYIGYYNQYDGGVPPEFGDLGALLRLDMSSCNLTGPVPPELGRLQRLDTLFLQWNRLSGEIPPQLGDLSSLASLDLSVNDLAGEIPPSLANLSNLK... | Function: Receptor-like kinase protein that regulates the size of the floral meristem.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 105512
Sequence Length: 994
Subcellular Location: Membrane
EC: 2.7.11.1
|
B5RHS5 | MALYCGDNFGVYSQPGLPPPAAAAAAAAAAPGAPPASRAPYALADYAAPPAAAANPYLWLNGPGVGVGVGVGVGGPPAAAAAAAAAYLGAPPPPPPPPGGAAGPFLQPPPAAGTFGCAQRAFAQPAPAAPASPAGPAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADSFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRRSEASSASTSTVAAGTTKSEEGLSSGLGSGVGGKPEGDSPSALLRPPQSPEPPEGTKSTASSPGGSL... | Function: Transcription factor required for pharyngeal arch development, and which is involved in hair, ear, jaw and dental development . May act as a pioneer transcription factor during pharyngeal arch development (By similarity). Required for the development of the epithelium of hair and whisker placodes and that of ... |
D3Z120 | MALYCGDNFVYSQPAAAPGAPPTSRAPYGLSDYAAPPAAAANPYLWLNGPGVGGPASAASYLGAPPPPPGAAPGPFLQPPAAPGTFAGAQRGFAQPSASAPASPAGSAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADNFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRRRRAEASSNLTVPSGTSKSEGQSSRLRVSGKLEGDSPSSILRPSQSPEPPEGTKSTASSPGASTLTSTPCLNTFLSTFNTLNVNSSSSMGNQRTLPGS... | Function: Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development . May act as a pioneer transcription factor during pharyngeal arch development . Required for epithelial cell differentiation within the epidermis . Acts at multiple stages of otic placode... |
P42128 | MAEVGEDSGARALLALRSAPCSPVLCAAAAAAAFPATTSPPPPAQPPPGPPALPAEPGPGPVPSTVATATTTAPALVAAAAASVRQSPGPALARLEGREFEFLMRQPSVTIGRNSSQGSVDLSMGLSSFISRRHLQLSFQEPHFYLRCLGKNGVFVDGAFQRRGAPALQLPQQCTFRFPSTAIKIQFTSLYHKEEAPASPLRPLYPQISPLKIHIPEPDLRSLVSPIPSPTGTISVPNSCPASPRGAGSSSYRFVQNVTSDLQLAAEFAAKAASEQQADASGGDSPKDESKPPYSYAQLIVQAISSAQDRQLTLSGIYAH... | Function: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis, muscle cell differentiation and autophagy . Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context . Toge... |
Q01167 | MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALSSEKREKQEASESPVKAVQPHISPLTINIPDTMAHLISPLPSPTGTISAANSCPSSPRGAGSSGYKVGRVMPSDLNLMADNSQPENEKEASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVP... | Function: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context . Together with FOXK... |
B1Y3P5 | MPELPEVEVTRLGLVDRIGGATVRALQLGKPLRWPIGVAPQQLAGQRIGELARRGKYIWMPLQDGSTPAGGLLWHLGMSGSLRFEAQLPPPGPHDHVELVTDRGSLRLTDPRRFGAVVWSPSLQAGCAARLLGGLGVEPLEDGFTASVLHQGLRGRRVAIKQALLAGDIVVGVGNIYCSEALFVAGIDPRLAAQRLSLARCERLVQAIRQVLRQALMAGGSTLRDFRDAHGMGGAFQLQAQVYDRADQPCRRCGALVRRIVQGQRATYFCPVCQRR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q1WUN7 | MPELPEVETVRRGLEKLVLNKKIKDIRVLYSKTIVNEESEFIEKLTNKTIKKIDRRGKYLLFRFSSDLTMISHLRMEGKYFVEPSTKEVEKHTHVVFDFTDGTSLRYNDVRKFGRMQLVKTGMEIQTAGLAKLGPEPKEKTFIVEDFSKNLKRRKKAIKNALLDQTIVAGLGNIYADEVLWMSKIHPETPANKLTEEEVKVLRDNIIKELALATEAGGTTIRSYTDAFRHSGGFQFSLHAYQRTGDPCERCGTPIQRIVVGQRGTHFCPKCQVVKS | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q8Y6W7 | MPEMPEVENVRATLQELVPGKKIDQVIVRVPKMIVSTPPDEFVHMLVGQEIEGVRRRGKFLLFDLTNCTILSHLRMEGKFRLMDENEEVSKHTHIIFHFEDHTELRFLDVRKFGTMEVTNKYGEGETRSIKKLGPEPLTQAFTLTDFATGVKKTSRAIKTALLDQKLVAGVGNIYADEICFEAKVRPERAANSLSDKEIKRIFKATKSIMTEAVALGGSTVRTYVNSQGKLGQYQNKLKVYGKTDEPCVVCGTPIEKIKLNGRGTHFCPNCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
C6BUX8 | MPELPEVEVISRGLAESLEGKTIESVKILNHSSVKMPWYLFSSRVAGEKITRIHRRAKLLIMDLGDDLHITFHLKMTGRVLAHEGPTTPEPHTRIVFGLTDGGSIEFHDTRKFGEVRALNNEELQEWDFYKNLGPEPLEVTAEELAERITGRKAQIKGLLLNQSVVAGCGNIYADESLFRSGIHPKAKASDLSNESLVKLFTELQAVLKQAIQENGSSIRDYVDAGGDAGGFQNSFKVYGKKGEPCPDCGKIFEGATVAGRTSTFCSNCQKMKD | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q6KHS0 | MPELPEVKTVILHLKKLILDKTISKIEIFIPKMIKEISSEEFKKYLENETIFNIENEGKFIVFFLSNNKIMLSHLRMEGGYNFYSKKRQKEIHDRLIFHFTDGSSLHYHDSRMFGTFHFRNSENYLKIKPLSLVAPVPWKIDLDEFFKLLKRKKTAIKKILLDQQIIAGLGNIYVDETLFASKVHPEFKANQLSLEQVKLILKNATRILQESTKLGGSSIRSYTSLNEKEGSFQNFLQVHTKFNKPCPNCGELIQKIKLGGRGTYFCKKCQQLN | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q1H3I3 | MPELPEVEVTRRGLEPLIGATVTQAVIRQPAMRWPIPSHLPQVLHGARLLELRRRGKYIIARFESGCLILHLGMSGRLCLLESDTFPEKHDHFDLHFADGRVMRMRDPRRFGAVLWAGDQPDEHSLLKVLGQEPLDEAFNGEFLQQAIRTRSSPIKTVIMDSHLVVGVGNIYASESLFRAGIHPETPARALTLAQCRRLVEEVKLTLQDALQAGGSSLRDFFGADGNPGYFQQTYFVYGRTGQPCRVCQTPIAVLRLGQRSTFYCPACQQGQPPSNAMP | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
B1ZGU8 | MPELPEVETVRRGLAPAMVGARFARVTLRRPNLRFPFPERFAERLEGTTVRELARRAKYLTAHLDSGESLILHLGMSGRFDVRMPDGSNLSPGDFYLEGALGTPKHDHVVMAFANGATVTYNDARRFGFMDLVATRDLETCRHFAAMGVEPLSDALDGAVLARLFARKITPLKAALLDQRLIAGLGNIYVCEALHRSGLHPALPAGALAKPDGAPTPKAKKLVKEIKAVLTEAVAAGGSTLRDYARPDGERGAFQHGFRVYDRVGHACPTKGCTGRIGRIVQGGRSTFFCETCQVR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q9X3X1 | MPELPEVETTIRGLSEVLMGEKIIDVKVRRASLRRPIPSDIQERLIGSTIISLSRRAKYGIIVNDRDDALIFHLGMSGRWKINPENFEKHDHFVLQTKNNFIVSLYDPRRFGSLDLVKKNQLLEWSYFRNIGPEPLTGNFNPEYLQKKLFSSSAPIKKILLDQKVVAGIGNIYACEALHQAKIHPQRPSKNLNFDEITSLVFSIKNILQKAIAEGGSTLKDYARPNGELGYFSTKFKVYGKEGEQCECGHTIERYTLGGRSTFLCSSCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
P53739 | MAGHHHEHEQERDHEQEHEHDSLQRPTTGSERTRSISFSKLLTRSWKRNASSSNNMSVSSVNLYSDPENSRESDHNNSGSEGQSSRFSKLKSMFQSGNSSKNASAHNSSQSSLEGDSASSSSKLRYVKPMTSVANASPASPPLSPTIPETDVLQTPKMVHIDQHEHEREHSNCGSPIMLSSSSFSPTVARTGTGRRRSPSTPIMPSQNSNNSSSTSAIRPNNYRHHSGSQGFSSNNPFRERAGTVRSSNPYFAYQGLPTHAMSSHDLDEGFQPYANGSGIHFLSTPTSKTNSLTNTKNLSNLSLNEIKENEEVQEFNNED... | Function: Flippase activator that phosphorylates DNF1 and DNF2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. ... |
Q6MLJ0 | MKVQSLLRIETQLLLGRLLTRSGDQAWDFVVPFALLVIFPGKLQVAAFYYLIVKIGTFLLTPSSGKWIDTHPRIQVVKWGVWLQFFAILAGMVFFGMLDGLVRAGGRESWLLSVLFIALALSGVMASLGSQITDISVGNDLAPSLVAPEKLTHFNSWLRRIDLATEVGAPILAGALFAFHPEQLPLAGLFLIGLWNLVSFVPEYFLLRNVIQRSGLKIKVLTEAQSWKDTFHINLRGSFSDPIFWLILSYALLWLSVLSPHGVLLAAYLKDEMRLPETEIGLFRGLGAVFGLISTVSFPYLVRRLGLISSSRWHLGFQGV... | Cofactor: The cofactor facilitates a conformational change critical to the transport cycle. The binding of Ca2+ from extracellular fluid activates the transporter by triggering a conformational change that enables the transition from the open outward to open inward states.
Function: Iron transpoter that exports Fe(2+) ... |
Q8PU58 | MIGDTMSGIIDSYIPVAIFLAVGLIMPPMTMFMVKQLSPRSKAASKYTTYESGSVPTGTARIQFNVEYYLYAIAFVLFDIEVLFLYPWATVYKGHGITSIAVVEMFVFIFILLFGYVYLWKKEALTWVK | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methano... |
F1SVH7 | MGEVKETKTNNSKENPEEEVPGVITTTTSAIHNFLKKTKAQDIINWGRKNSLWFMTQPMGCCGVEMIATGCAHYDTDRFGIIPRNSPRHADVMIISGYVTKKYLPALKRLWDQMPAPKWVIAMGDCAISGGPFYESYSTVQNIDEIFPIDVYIPGCPPRPEALIQGFVELQEKIKARKDRGTEY | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogen... |
F1SVL1 | MDARTIIESLTGKFPEAISEAGIESPIRIRAYVDKDKAKEVCEYLKGSLQFDHLCSVSGVDYPQRDELEAVYHIASYDHPVVLMLKARLPRDSPEIESVVSVYWNANWYERETYELYGIFFKNHPELKPLVLPDDMLGEWPLRKDYEGFPNRTARNLV | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methano... |
F1SVE4 | MEEMLESNEMIVHLGPQHPMQPGPFRLNLKLKGETIMDAEVEMGYIHKGIEKILENRTYLQGITIVDRICYLVALTNEECYVGCVEKLLDIEPPERAQYIRVILEELSRLQSHLLGLGEYGEFIGFVSMFMYTIKEREDILTLIDMVTGARVTHSYLRFGGVRDDLPEGFKEKTIPVLNKLKKVIRDYEEMFYSDTIYRERTIGIGVLTADEAKSLGVSGPVLRATGVPFDIRKNEPYLVYRDLDFKVCTETAGDCFARVQVRLNEMRESIYIIEQCLDMIPNGPIFPEGTPYGKRTPVMRVPAGEVFHRVEDPRGEMGM... | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methano... |
Q8PZ67 | MPPKIAEVIQHDVCAACGACEAVCPIGAVTVKKAAEIRDPNDLSLYEKGAAFQVCEGCLTCSRICPVVDGFIENELLNVRKFFGAKSKDNAGSQDGGVTSGILKALFNKGEIDCAVGITRNENWEPEVVLLTSAEDVERTRGTKYTSDPVVAALREAFEKYDRIAVVGVPCQAHAARLIRENVNEKIVLIIGLLCMESFHHDVMLDKIIPEIMKVNVRDIVKMEFTKGKFWVYTKDGEVHSVPIKDIAKYARNPCHHCCDYTSVFADISVGSVGAPDGWNSVFIRTEIGEKYFDMVRDEMEIMEDPKPGLELVGKLIEMK... | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogen... |
Q8PU59 | MTFMAIEIPEFIVPFVPWIRGTVGLVLVGAIFLGGMAAVWIERKLSADIQLRYGPSRVGKFGLLQLVADAIKLFTKEDVRPGNADRFLYDNAPVFMLTSLFLMLVAIPVGAVFIDGNLYPLAVTEMDISILFIEAVSAINIFGIFMAAYGSNNKYSLLGAFRNFARMIGYEVPLGIAIVSVAVMTGSLNIIDITSAQGSFVWNIFLQPIGFVVFFIALMADLGRLPFDQNESEEELVAGWVTEYTGMRFGLVFFAEYMHMILGSFLVALLFLGGWNVPAFVANNAVLGLIAPTGILLLKTVLVLMTIIGMRWAVPRFRID... | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methano... |
Q8PU60 | MGCPEVQDRPGSGYELEETPAPVPVEPCLGSRPWTLSGGLSMVLKNIKYALKNIPKERVTRLCPEVESPLSERFRGLQTLDKSKCIGCGICANTCPNSAIKIVKAPIAPGSEKKRWFPQIDIGHCLFCGLCIDQCPKGALSSGKEYCKGMVKWAHKDLLMTPEKLAREVDIQEGDER | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogen... |
Q8PU61 | MIDPGTVGAALETAVFGLLALVTVFFAIFVVIAKDVVRAGLALIMCMFGVAGLYILLNAQFLGVIQVLVYIGAIGVLILFAVMLTKREIGGGPVQINRPLAFLVCLLFVAVVVTGAFGTSWNTVSELPENPADPSNIEGIGMLIFTHFVAPFEVLSIVLLASLIGAIYMAKGEGNR | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methano... |
P17596 | MGRMLTIRVFKYDPQSAVSKPHFQEYKIEEAPSMTIFIVLNMIRETYDPDLNFDFVCRAGICGSCGMMINGRPSLACRTLTKDFEDGVITLLPLPAFKLIKDLSVDTGNWFNGMSQRVESWIHAQKEHDISKLEERIEPEVAQEVFELDRCIECGCCIAACGTKIMREDFVGAAGLNRVVRFMIDPHDERTDEDYYELIGDDDGVFGCMTLLACHDVCPKNLPLQSKIAYLRRKMVSVN | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
Catalytic Activity: a menaquinone + succinate = a menaquinol + fumarate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27165
Sequence L... |
Q5E2B5 | MSNRKPYVREMTRTWWKDHPFYRFYMVREATVLPLIFFTICLLVGLGSLVKGPLAWASWLDFMANPIVVALNIVALAGSLFHAQTFFSMMPQVMPIRLGGKTLDKKVVVLAQWAAVAAITLLVLVIV | Function: Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14339
Sequence Length: 127
Subcellular Location: Cell inner membrane
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Q8ZIX8 | MNQVPKRSDEPIFWGLFGAGGMWGAIIAPVIILLVAILLPLGAFPGDALSYERILAFCQSFIGRVFLLLMIILPLWCGLHRIHHAMHDLKIHVPAGKWVFYGLAAILSVVTFIGVLTL | Function: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cel... |
P32614 | MSLSPVVVIGTGLAGLAAANELVNKYNIPVTILEKASSIGGNSIKASSGINGACTETQRHFHIEDSPRLFEDDTIKSAKGKGVQELMAKLANDSPLAIEWLKNEFDLKLDLLAQLGGHSVARTHRSSGKLPPGFEIVSALSNNLKKLAETKPELVKINLDSKVVDIHEKDGSISAVVYEDKNGEKHMVSANDVVFCSGGFGFSKEMLKEYAPELVNLPTTNGQQTTGDGQRLLQKLGADLIDMDQIQVHPTGFIDPNDRSSSWKFLAAESLRGLGGILLNPITGRRFVNELTTRDVVTAAIQKVCPQEDNRALLVMGEKM... | Cofactor: Binds 1 FAD per monomer.
Function: Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentat... |
Q6QGJ4 | MITAMYAVGPNGEFGLRGKLPWGSFKEELDAFYSQLDVLNPDNIIIGAGTYLALPYAVRERMIGASDLFIRADRPLPDDITHDIYTPISMIGDTLPTFLKDQQTVVLGGANLLLEMYQHGHIESAFVSTIFSEQKLEADTHLDSMILDYNYESTRLVYAVGANSDNSLRFVQELVTY | Function: Provides the tetrahydrofolates necessary for the synthesis of nucleotides and amino acids. Bacteriophage T5 induces high levels of dihydrofolate reductase in the host cell, probably for the viral replication.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequen... |
B5XRB0 | MTSNERILQPFTLPNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGLAKIAEAIKAQGSKAILQIYHGGRMVDPQLIGGRQPVAPSAIAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDITHKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTSDPTPLIEKYCAMRSETLAQVPVMGVGGVVNVADAELGLDHGYDLIA... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the anaerobic reduction of fumarate to succinate . Uses NADH as the inherent electron donor in this process . Is involved in anaerobic fumarate respiration in K.pneumoniae .
PTM: Is flavinylated on Thr-447 by ApbE2, encoded in a neighboring gene . Flavinylation is ... |
Q5A446 | MKIQQLIVFLFAVVLIDARTPKRYSELDIVMSTCTTFIGKYGTVCTSTGKRSTNWNCYCKTDAGFGTISDCLVRGFNNNTNIISKFTESCNMTESKFHAKYDKIQAEFKTNGTEYAKMTTKSSSGSKTSASASKSSKSTGSSNASKSSTNAHGSNSSTSSTSSSSSKSGKGNSGTSTTETITTPLLIDYKKFTPYKDAYQMSNNNFNLSINYGSGLLGYWAGILAIAIFANMIKKMFPSLTNYLSGSISNLFRKHLFLPATFRKKKAQEFSIGVYGFFDGLIPTRLETIIVVIFVVLTGLFSALHIHHVKDNPQYATKNA... | Function: Ferric reductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity... |
P32791 | MVRTRVLFCLFISFFATVQSSATLISTSCISQAALYQFGCSSKSKSCYCKNINWLGSVTACAYENSKSNKTLDSALMKLASQCSSIKVYTLEDMKNIYLNASNYLRAPEKSDKKTVVSQPLMANETAYHYYYEENYGIHLNLMRSQWCAWGLVFFWVAVLTAATILNILKRVFGKNIMANSVKKSLIYPSVYKDYNERTFYLWKRLPFNFTTRGKGLVVLIFVILTILSLSFGHNIKLPHPYDRPRWRRSMAFVSRRADLMAIALFPVVYLFGIRNNPFIPITGLSFSTFNFYHKWSAYVCFMLAVVHSIVMTASGVKRG... | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity... |
P0DTV5 | DLLGTLGNLPLPFI | Function: Peptide with unknown biological function that may act on skin macrophages to produce a cytokine-mediated stimulation of the adaptive immune system in response to invasion by microorganisms . It does not show antimicrobial and hemolytic activities but stimulates production of the pro-inflammatory cytokines TNF... |
P36033 | MHWTSILSAILLFCLSGARASPAKTVIRNKVPLLVTNACTRIFQKVTWEYTSKSKRSSPVCSYEPAFQSMLYCIYETLDEKGYSNKTLEKTFSTIKKNCASYSDALQNMTNSEFYDVLNNGTRHMTPYVKGSANLTYPVEMDTQLRKAYYHALHGFYANLDVGNIYGGIICAYFVAIMAFAGVLHCMNYTPFKTVLLKQKLVGYVRGYLTLPTIGSKHASDFSYFRIFTGYLPTRLEGIIILGYLVLHTVFLAYGYEYDPENIIFKSRRVQVARYVADRSGVLAFAHFPLIVLFAGRNNFLEYISGVKYTSFIMFHKWLG... | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity... |
P25437 | MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFDLARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAVAGQEISTRPFQLVTGRVWKGSAFGGVKGR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also... |
P44557 | MEIKQINSTIKSRAAVAFAPNQPLQIVEIDVEMPRKGEVLIRNTHTGVCHTDAFTLSGSDPEGVFPVVLGHEGAGVVVAVGEGVLSVKPGDHVIPLYTAECGECEFCRSGKTNLCVSVRDTQGKGLMPDCTTRFSYQGQPIYHYMGCSTFSEYSVVAEVSLAKINPEANHEQVCLLGCGVTTGIGAVHNTAKVQEGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPAKFELAKQFGATDCLNPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRQALESAHRGWGQSIIIGVAGAGQEISTRPFQLVTGRVWKG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
Sequence Mass (Da): 40651
Sequence Length: 378
Subcellular Location: Cytoplasm
EC: 1.1.1.284
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P73138 | MKSRAAVAFEVGKPLQIVEIDVAPPQQGEVLVKITHTGVCHTDAFTLSGDDPEGLFPVVLGHEGAGIVVEVGEGVTSVQLGDHVIPLYTAECGKCLFCRSGKTNLCVAVRATQGKGVMPDGTSRFSYNGQSLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGGIGLAVVQGARQAKAGRIIAIDTNPAKFELAKQMGATDCINPKDHDQPIQQVIVEMTGWGVDHSFECIGNVEVMRSALECAHRGWGQSVIIGVAGAGQEISTRPFQLVTGRKWMGTAFGGVKGR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
Sequence Mass (Da): 39211
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 1.1.1.284
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A2A2Y4 | MFASCHCVPRGRRTMKMIHFRSSSVKSLSQEMRCTIRLLDDSEISCHIQRETKGQFLIDHICNYYSLLEKDYFGIRYVDPEKQRHWLEPNKSIFKQMKTHPPYTMCFRVKFYPHEPLKIKEELTRYLLYLQIKRDIFHGRLLCSFSDAAYLGACIVQAELGDYDPDEHPENYISEFEIFPKQSQKLERKIVEIHKNELRGQSPPVAEFNLLLKAHTLETYGVDPHPCKDSTGTTTFLGFTAAGFVVFQGNKRIHLIKWPDVCKLKFEGKTFYVIGTQKEKKAMLAFHTSTPAACKHLWKCGVENQAFYKYAKSSQIKTVS... | Function: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68772
Sequence Length: 597
Subcellular Location: Membrane
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Q7Z6J6 | MLSRLMSGSSRSLEREYSCTVRLLDDSEYTCTIQRDAKGQYLFDLLCHHLNLLEKDYFGIRFVDPDKQRHWLEFTKSVVKQLRSQPPFTMCFRVKFYPADPAALKEEITRYLVFLQIKRDLYHGRLLCKTSDAALLAAYILQAEIGDYDSGKHPEGYSSKFQFFPKHSEKLERKIAEIHKTELSGQTPATSELNFLRKAQTLETYGVDPHPCKDVSGNAAFLAFTPFGFVVLQGNKRVHFIKWNEVTKLKFEGKTFYLYVSQKEEKKIILTYFAPTPEACKHLWKCGIENQAFYKLEKSSQVRTVSSSNLFFKGSRFRYS... | Function: May be involved in regulation of cell migration . May regulate cell-matrix interactions via its interaction with ITGB5 and modifying ITGB5 cytoplasmic tail interactions such as with FERMT2 and TLN1. May regulate ROCK1 kinase activity possibly involved in regulation of actin stress fiber formation .
Location T... |
Q16658 | MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTAT... | Function: Actin-binding protein that contains 2 major actin binding sites . Organizes filamentous actin into parallel bundles . Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers . Important for the formation of a diverse set of cell protrusi... |
Q61553 | MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTAT... | Function: Actin-binding protein that contains 2 major actin binding sites (By similarity). Organizes filamentous actin into parallel bundles . Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (By similarity). Important for the formation of ... |
Q1LY10 | MDDQKESLRKIITTLALKNEEIQNFICSLKQSLENLEANSNRVQEDLESEFSSLHSVLDDLKEGMVTRIKQERASRTYELQSQLGACTKALESSEELLEFANQTLCSSENDSFTQAAKDIKDSVTMAPAFRLSLKAKASDSMNHMMVDFTHERNLLQSITFLPVPATPEIHVADCQVFDNTVTVVWTLPEPDSKIDHYILEHRKTNHEGPPRAREDYPWMVVEGIKETEYTLTGVRFDTRYMTFRVKACNKAVAGEFSEPVTLETHAFVFKLDASSSHQNLKVEDLSVEWDSSGGKVAVQDIRKEKNRTNSPMHSPARTA... | Function: May be involved in microtubule organization and stabilization.
Sequence Mass (Da): 55876
Sequence Length: 495
Domain: B30.2 box contains a microtubule-binding site.
Subcellular Location: Cytoplasm
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Q9BTV5 | MEEQREALRKIIKTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDSEDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPAR... | Function: May be involved in microtubule organization and stabilization.
Sequence Mass (Da): 55820
Sequence Length: 496
Domain: B30.2 box contains a microtubule-binding site.
Subcellular Location: Cytoplasm
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Q1DFW5 | MTLRAMTDVGAELGLSPEDVLPWGTHRAKVSLDALGKRGGRQGRLVLVSAINPTPPGEGKTTMSVALAMGLRKRGRRAVAALREPSLGPVFGVKGGGTGGGQASLEPAADINLHFTGDLHAITSANNLLSALVDNAVFYGQPVALDATRVRWRRALDMNDRFLRNVIVGLGGKAQGVPREDHFDITAASEVMAILALAEGLKDLEARLGRVIIGHTRDGQPVRARDVDAAASMVALLKDALMPNLAQTREGGPALVHAGPFANIAHGCSSVMGTRMGLAYADEVITEAGFGFDLGAEKFLDIKCRGSGLWPRGVVLVVTL... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58072
Sequence Length: 551
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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