ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1D0S7 | MLYLLYEVIQNSEAGRVLNFLRYPTFRIIAAGVFALLLGMLIGPKLIARLRLKQHGQSNVREDTPDSHQKKKGTPTMGGALILLCIAAGTLLFADLKSRAVWVMLLLTLGYGFIGFLDDWLKLSKRNSKGLAGRKKMVLQTFFFLVAVFGLLTTWTLPDGSFGPTLLINTKLTLPFIPTRWFNPDLGWFYVFFAWIVVVGTSNAVNLTDGLDGLAIVPTIVSAITFAVLCYVAGTTLSIADYEVVGGASKLVATPLYQYLGILQVPGGAELAVFCAAIVGAGISFLWFNTYPASVFMGDIGSLALGGALGGLAMLSKNEVVSAIIHGIFFAEILSVMIQVTSFKMTGKRVFKMAPVHHHFELKGMAEPKIIVRFWIVSILCGGVALLSLKLR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42590
Sequence Length: 392
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q9K0Y6 | MFLWLAHFSNWLTGLNIFQYTTFRAVMAALTALAFSLMFGPWTIRRLTALKCGQAVRTDGPQTHLVKNGTPTMGGSLILTAITVSTLLWGNWANPYIWILLGVLLATGALGFYDDWRKVVYKDPNGVSAKFKMVWQSSVAIIASLALFYLAANSANNILIVPFFKQIALPLGVVGFLVLSYLTIVGTSNAVNLTDGLDGLATFPVVLVAAGLAIFAYASGHSQFAQYLQLPYVAGANEVVIFCTAMCGACLGFLWFNAYPAQVFMGDVGALALGAALGTVAVIVRQEFVLVIMGGLFVVEAVSVMLQVGWYKKTKKRIFLMAPIHHHYEQKGWKETQVVVRFWIITIVLVLIGLSTLKIR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39328
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q8CPK7 | MIFIYAIIALLITFILVPILIPTLKRMKFGQSIREEGPQSHMKKTGTPTMGGLTFLISIIISSIIAIIFVDHSNPIILLLFVTIGFGLIGFIDDYIIVVKKNNQGLTSKQKFLAQIIIAVIFFVLSDVFHLVHFTTDLHIPFVNFDIPLSFAYVIFIVFWQVGFSNAVNLTDGLDGLATGLSIIGFAMYAVMSYMLDSPAIGIFCIIMIFALLGFLPYNLNPAKVFMGDTGSLALGGIFATISIMLNQELSLILIGFVFVVETLSVMLQVASYKLTKKRIFKMSPIHHHFELSGWGEWKVVTVFWTVGLITGLIGLWIGVH | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35603
Sequence Length: 321
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
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P56833 | MKQILFAGVIGLFLTLVGTPLLIKLLARKGYGQYIRDDGPREHASKRGTPTMGGIAFILATVAAYFLAKGITSYLDPDIDAGPTFSGLLVLGLMVGMGLVGFLDDYIKIVKRRSLGLRARAKMIGQLTVGIAFAVLSLQFADNRGNTPASTKLSFITDFGWTIGPVLFVVWALFMILAMSNGVNLTDGLDGLATGASVLVFGAYTFIGVWQFQESCANALTLTNPGACYEVRDPLDLAVVASALMGSCLGFLWWNTSPAKIFMGDTGSLALGGVLAGLAICSRTELLMAILGGLFVLITMSVVIQVGSFRLTGKRVFRMAPLQHHFELKGWSEVLVVVRFWIIQGICVIVGLGLFYAGWATDK | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38893
Sequence Length: 363
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
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P44469 | MNLKKFFNTPTHEPFRDKKAERNLFARRTLVAFLGILLLTGVLFTNIYQLQIVNFDTYQTRSNGNRIKLLPLPPTRGLIYDRYGKLLAENLTFFGLYIVPEKTENLDRTLDELRYIVGLTDNDIENFKKERRRGTRYTPILLKPNLTEEQISRFAVNGYQYPSLEVRPYFKRHYLYGETMAHILGYVGKMNDKDVERLKREDKFANYAGTNDIGKLGIERYYEDILQGTTGFEEVEINNRGKVIRTLRSRPAVAGKSIHLTIDLALQRYITELLSGLKGAVVVLDPKDSSVLAMVSTPSYDNNLFVDGISSEDYKRLLNDLARPLYSRATQGAYPPASTVKPFIAVAAQTENVITPNTTIFDPGYWVLPNSTKRFRDWKKTGHGDTDLNKAITESSDTYFYQVAYNMGIDRLSNWMKDFGFGMPTGIEIQEETAANIPTREWKQKRYKRPWVQGDTISVGIGQGYWTATPLQVAKATTILVNNGKVNTPHLMKAIEGAVLEPYEDPLLYPDINTPKVAAWEAAKRGMYNVVNAANGTGRKAFADANYRVAGKSGTAQVFSLKENEKYNTAGLKKELHDHAWFTAYAPYDNPKLVVTVILENAGGGSSNAAPLARKVMDYYLNQRLPQVEKYNVPIQQKKDLSQESEQINGR | Function: Catalyzes cross-linking of the peptidoglycan cell wall.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73813
Sequence Length: 651
Domain: Has a penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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E1WGF1 | MTFKDFDAEEKLFLRRVIVAFGVVVVCFGILIFNLYNLQIRQHHYYTTRSNENDIKMLPVAPTRGIIYDRNGIPLVRNVTWYDIAVTPYKIADMDALLKQLTPIVDLSPDDISDFRRALKSSSRYRPVVLKNALTDVEIARFAVNQFHFNGVTINSYQDRQYPYGAELAHVLGYVSKINDNDLKALDKKGLAENYAADHNIGKQGIERYYENDLHGKTGYQEVEVDNHGRIVRLLKDVPPIAGKNIHLTLDLHLQEYIESLLAGQRAAVLVEDPHDGSVLAMVSMPSYDPNPFVKGISYQDYGKLLHDKNLPLINRVTQGLYPPASTVKPYMAMSALLCGIITPQTTFFGAPTWTLPGTQRHYRDWKKTGHGMLDVTKAIEESADTFFYQVAYMMGIDRIDTMLSQFGYGKPTGIDLNEEYDGLLPSRAWKQRVHKKAWYQGDTISVGIGQGYWIATPIQMVKAMVALINNGKVIAPHLLLNEESGKTVVPYRPSGTPAQIADPASPYWGLVRQAMYGMANAPNGTGYKFFHTAPYGIAAKSGTSQVFSLKENQTYNAKMIPIRLRDHVFYTAFAPYKNPKVAIALILENGGSDGVTAAPIMRKILDHLFDPQADTTQPDQAP | Function: Catalyzes cross-linking of the peptidoglycan cell wall.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69833
Sequence Length: 623
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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O18330 | MTRLFMLVCLGIVCQGTTGNILRGESLNKSLPILHEWKFFDYDFGSDERRQDAILSGEYDYKNNYPSDIDQWHDKIFVTMLRYNGVPSSLNVISKKVGDGGPLLQPYPDWSFAKYDDCSGIVSASKLAIDKCDRLWVLDSGLVNNTQPMCSPKLLTFDLTTSQLLKQVEIPHDVAVNATTGKGRLSSLAVQSLDCNTNSDTMVYIADEKGEGLIVYHNSDDSFHRLTSNTFDYDPKFTKMTIDGESYTAQDGISGMALSPMTNNLYYSPVASTSLYYVNTEQFRTSDYQQNDIHYEGVQNILDTQSSAKVVSKSGVLFFGLVGDSALGCWNEHRTLERHNIRTVAQSDETLQMIASMKIKEALPHVPIFDRYINREYILVLSNKMQKMVNNDFNFDDVNFRIMNANVNELILNTRCENPDNDRTPFKISIHL | Function: Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20-hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.
PTM: Glycosylated.
Sequence Mass (Da): 48886
Sequence Length: 432
Subcellular Location: Secreted
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O77061 | MTRWLFMVACLGIACQGAIVRENSPRNLEKSLNVIHEWKYFDYDFGSEERRQAAIQSGEYDHTKNYPFDVDQWRDKTFVTILRYDGVPSTLNVISGKTGKGGRLLKPYPDWSFAEFKDCSKIVSAFKIAIDKFDRLWVLDSGLVNRTVPVCAPKLHVFDLKTSNHLKQIEIPHDIAVNATTGKGGLVSLAVQAIDLANTLVYMADHKGDALIVYQNADDSFHRLTSNTFDYDPRYAKMTIDGESFTLKNGICGMALSPVTNNLYYSPLASHGLYYVNTAPFMKSQFGENNVQYQGSEDILNTQSLAKAVSKNGVLFVGLVGNSAVGCWNEHQSLQRQNLEMVAQNDRTLQMIAGMKIKEELPHFVGSNKPVKDEYMLVLSNRMQKIVNDDFNFDDVNFRILGANVKELIRNTHCVNNNQNDNIQNTNNQNDNNQKNNKKNANNQKNNNQNDN | Function: May play an important role in honeybee nutrition. It is found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.
PTM: N-linked core structure contains mannose (which consists of 8-alpha-mannosyl residues, one beta-mannosyl residue, and chitobiose).
Sequence Mass (Da): 51074
Sequence Length: 452
Subcellular Location: Secreted
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Q8SRI3 | MATLSQKKLMESVRLMEREWVKMHKALVRSRCGEVKEVRYRYVEMIGRGSFGVVVKIMDDRHNFFALKRVYQDRRYHNRELGILMEVDHPNIVRLVSYFHTDKTSSGAYLNIITDFVGMNLEEYIKANRGVETEEIRSVYRQILEGLRYLHEKNICHRDMKPSNILIDTNGLVKICDLGSAKVIKSGERNITYICSRFYRAPENLLDYKEYDFKIDIWSVGCVIAEFRHPGPIFKGDTSGSTLNRILEIVRVTSDDLIGLGCLKPDLKQGVGIRKYLEAFFSDPDLLEVLEKSLAFSPCKRSTASELLRKQFFQQAHE | Function: May play a role in the initiation and completion of mitosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36918
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P21647 | MKQRSICPGRLSTAIAVALCCFPPFSSGQESPGTIYQFNDGFIVGSREKVDPSRFSTSAISEGVYSLDVYTNGEWKGRYDLKITAGKDGKMGVCYTKAMLMQYGISPEKLNPQLSEKEGFCGRLQEWRHEDNVKDTLIQSSLRLDIAVPQIYEDQRLKNFVSPQFWDKGVAALNLGWMANAWNSHISSANGSDNSSAYLGVNAGLSWDGWLLKHIGNLNWQQQQGKAHWNSNQTYLQRPIPQINSIVSGGQIFTNGEFFDTIGLRGVNLATDDNMFPDGMRSYAPEIRDVAQSNALATVRQGSNIIYQTTVPPGPFTLQDVYPSGYGSDLEVSVKEGDGSVEVFSVPYASVAQLLRPGMTRYALSAGKVDDSSLRNKPMLYQGTWQHGLNNLFTGYTGVTGFDDYQAFLLGTGMNTGIGALSFDVTHTRLKSDTLDEHGQSYRATFNRMFTETQTSIVLAAYRYSTKGYYNLNDALYAVDQEKNYNSNYTVWRQKNGMTFTVNQNLPDGWGGFYLCGRVADYWNRSGTEKQYQFSYNNMYGRLSWSVDAQRVYTPDSSGHRRDDRVSLNFSYPLWFGENRTANLTSNTAFNNSRFASSQIGVNGSLDSENNLNYGVSTTTATGRQHDVALNGSYRTPWTTLNGSYSQGEGYRQSGVGASGTLIAHQHGVVFSPETGPTMALIEAKDAAGVMLPGSPGTRIDSNGYAILPYLRPYRINSVEIDPKGSNDDVAFGSTVAQVVPWEGSVVKVSFDTTLQNNITLRARQANGLPLPFAATIFGPSGKEIGVVGQGSMMFISDASAPKATVKWSGGQCSVELSQEKTKETLCR | Function: Involved in the export and assembly of the type 3 fimbrial subunit (MrkA).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91049
Sequence Length: 828
Subcellular Location: Cell outer membrane
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Q75BD5 | MPTQLQRPLARLLALALLVLLARAAEDEPPFCAVRNRSTGSYIDLSPLASNVSGTPPNWLVRGWQYGANFTLGVCTSPLGDGPAAYYSDTGRRVSIGRVATTPRYTGKKLTLTYEGGDLCPNRVDRKSSLLYFVCDRDIHTIAQVSLLGVLHNCSYLFEVRSVHACAAARAAGDRSVLGIFAAILLVFAAVELARRCCAAPLRRRFRPDFPADRPRWAPAPTGWAARTRAFFARAAEPRQAIKLASSPPGHPASDMEAQNTLLDSLDVRSSGA | Function: Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29567
Sequence Length: 273
Subcellular Location: Golgi apparatus
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Q06815 | MLKRSSLIYLSCVLIITIPILLHVYNGPGLSHEANEHRASHKQKRTLANPDKPKSENDEDLFCAVTNPVTGSYIDLSQLSSTPNKLREGQKQISGNNKHESSKTKWSVRGWGYDTNFTLGICSSPVGEAESQQLSNLTGAFYVDQLNENNLVSIGDFSTRPALVGGSTAKKLTLKYENGSMCPNGKDKKATLLNFVCDKEIQSKAQISYIGNLHNCSYFFEVRSIHACPTSNKKNEVNVLGIFIGIFAIFFLVEFAGRRWIYAKLNRHLKNDDELHDISPSLNEQPHWDLIEDGSRWSKFFNGIIKTTRRFTKSLMRSLVRGRNSRQGGIRLRSSPSASSSSLANREFFRDMEAQNEIIDSLDINSHTTESDHPTLADNSV | Function: Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole. Involved in the delivery and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar proteinase B).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42706
Sequence Length: 381
Subcellular Location: Golgi apparatus
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B8APK3 | MASVSSSPSYSSQAAVLLLLHQPPHQHGHGGACLRYRGSQSQGRGNAVATSLGLSAAGRGGAGGLLLLPPLPALRAAEGKDGRAVTKDEEEEAAAAAVEEEGEVEVRREEDKPGDDGSREAAARGSGSGRFSADYISLGIREPVYEVIEVKSNGRMSTKKISRRQLLKSSGLRLRDTRSVDPSLWLMNSMPSLLVREQAILVNLGSLRAIAMHERVLIFNYNSPGGKAFLDSLLPRLNPRNINGGPAMPFQLEVVEAALLSRIQRLERRLMRIEPRVGALLEVLPNRLTADVLEQLRLSKQALVELGSRAGDLKQMLIDLLDDPHEIRRICIMGRNCTLDKLSDNMECSVPLEKQIAEEEEEEIEMLLENYLQRCESIHGQAERLLDSAREMEDSIAVNLSSRRLEVSRVELLLQVGTFCVAIGALIAGIFGMNLKSYLETNAWAFWATTGGIVVGAVAGFFIMYSYLKTRKIL | Function: Magnesium transporter that may mediate the influx of magnesium in chloroplast.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51892
Sequence Length: 474
Subcellular Location: Plastid
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Q058N4 | MALTPIPSTFTSLFNFSDHSPYPSPSLHYLLPGSSPSFSLQLSALSRTPIYFEALKVLSRSKCFAKSPTTAEDFVGDYESLNVSDDDDGSDSNSSDGDNGGGRDDSKKIDSSSSSSSSDSTSLGIREPVYEVVEVKATGAISTRKINRRQLLKSSGLRPRDIRSVDPSLFMTNSVPSLLVREHAILLNLGSLRAIAMRDRVLIFDYNRRGGRAFVDTLMPRLNPRSMNGGPSMPFELEAVESALISRIQRLEQRLMDIEPRVQALLEVLPNRLTADILEELRISKQRLVELGSRAGALRQMLLDLLEDPHEIRRICIMGRNCTLRRGDDDLECTLPSDKLIAEEEEEEIEMLLENYLQRCESCHGQAERLLDSAKEMEDSIAVNLSSRRLEVSRFELLLQVGTFCVAVGALIAGIFGMNLRSYLEEQASAFWLTTGGIIIGAAVAFFLMYSYLSRRKIF | Function: High-affinity magnesium transporter that mediates the influx of magnesium in chloroplast.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51093
Sequence Length: 459
Subcellular Location: Plastid
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A2YFN7 | MSAAAASSAAGDSAKQPLLHHQRGNPPHVASVSSPSLPSAPPGALAGGRRFPGGLDVPNLKKRGGGTRSWIRVEAATASVQTLEVDKATMMRRCELPARDLRLLDPLFVYPSTILGRERAIVVNLEQIRCVITADEVLLLNSLDSYVLQYAAELQRRLLQRAEGDELPFEFRALELALEAACSFLDAQAAELEIEAYPLLDELTSKISTLNLERVRRLKSRLVALTRRVQKVRDEIEQLMDDDGDMAEMYLSEKKLRTEASFYGDQSMLGYNSVGDGTSFSAPVSPVSSPTESRKLEKAFSLCRSRHDSVKSSDNTATEHIQELEMLLEAYFVVIDSTLNKLTSLKEYIDDTEDFINIQLDNVRNQLIQFELLLTTATFVVAIFGVVAGIFGMNFETSVFSIQNAFQWVLIITGVIGAFIFCGFLWFFKYKRLMPL | Function: Magnesium transporter that may mediate the influx of magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48473
Sequence Length: 436
Subcellular Location: Membrane
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A2XV81 | MDHDPKERLLLPPRAAAAAAANGPHRRAAPAAGGGGGGVAIDVHGLKRRGGGRRSWVRVDAATGASEAVEVAKPALMRRLDLPARDLRLLDPLFVYPSAILGRERAVVCNLERIRCIITADEALILRDPDVAGGGAETEEAVRRYVAELQRRLVDRADDLPFEFIALEVALEAACSFLDAQAVELEADAYPLLDELTTKISTLNLERVRRLKSKLVALTRRVQKVRDEIEQLMDDDGDMAEMYLTEKKRRMEASLLEEQAFQGMGNSGFGSSFSAPVSPVSSPPASRRLEKELSFARSRHDSFKSADSSQYSIEELEMLLEAYFVVIDYTLSKLTSLKEYIDDTEDFINIQLDNVRNQLIQFELLLTTATFVVAIFGVVSGVFGMNFEVDLFNVPHAFEWTLVITGVCGLVIFCCFIWYFKKRRFFPL | Function: Magnesium transporter that may mediate the influx of magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47668
Sequence Length: 428
Subcellular Location: Membrane
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Q7XQQ1 | MAARRRHVAAGAGAPAPAAGEWAAVTAGGGAAWALSPVEEVGTKQELMRRTGLPPRDLRALDPALSSAASASSCRPSAITGRDRAVVVNLDRARAVITASEVLVPSPRDPAVAPLVRELRARLALAASPTPAPSPSPPQHGMAVGMDGSISPSQASRGGEEAAGNGKDGEALGGGDKALPFEFRALEVCLEFACKSLEHETCTLEKEAYPALDELTSKVSTLNLERVRQIKSRLVAISGKVQKVRDELEHLLDDDMDMAALHLTEKLAYQSSRFDIDKEASELEDHSSRDEEGVEGGGGGDGDDETIAGGGSFSPNTDELEILLESYFVQIDGTLNSLSTLREYVEDTEDYINMMLDEKQNQLLQMGILLSTGTLVSSCAIAVTGVFGINVHISLYDSPASSAAFPCAAAGIVAGSLALYLAALLCYKRAGILQ | Function: Putative magnesium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45555
Sequence Length: 434
Subcellular Location: Membrane
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A2WXD3 | MERRAQPVSAAVAPVTGRRKGAAASRKWMVVPAVGEERRVEFGKHQIMKMTGLPGRDLRVLDPVLSYPSTILGRDRAIVVRLQGVKAIITATEVLVPDHDDVLLASFLLDLRSRLSLPDAAPSTNPAAADRGNGTEQGDQGSVPGLAISGAGNAKIPPFEFKVLEVCLEHACKDLESQTRSLEKEAYPALDKLGSKVSTLNLDHVRNLKSRMVDLSGRVQKIRDELEHLLDDDMDMSEMYLTRKLSFQGLSGSLSRADSHKYASVDHDDDREEEDHDDETESGRESSVYVKPDIEELEMLLEAYFVQIDGTLNTLYHIREYADDTEDYINIMLDEKQNQLLQMGVMLTTATVVVTAGIVVVSLFGMNIHIDLMKDPETPEMVRMSNMHFWETTFGTVAGCIAIYLLAIYAGRKSKILQ | Function: Magnesium transporter that may mediate the influx of magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46401
Sequence Length: 418
Subcellular Location: Membrane
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A2WY50 | MRPSAAAGGGGGGGGRRKAAAAAAAASREWLVVPASGQARVEEAGKHAVMARTGLPARDLRVLDPLLSYPSTILGRERAIVVNLERVKAVITAAEVLLPNSKDPAFASFVCDLQARVLASSSDQAAEFTDMEGESSAVTSPFPALTSTTPNELEMTNKNSNVVGGMTHSNSMPTLTAAKDGNTKVLPFEFRALEVCLESACRSLEEETSTLEQEAYPALDELTSKISTLNLERVRQIKSRLVAISGRVQKVRDELEHLLDDEMDMAEMYLTEKLTRQEISETSSRVEVDDPSQLEVDRDEDYRSEADVSNGTFIGYKPHIEELEMLLEAYFVQIDGTLNKLSHLREYVDDTEDYINIMLDDKQNQLLQMGVMLSTATVVITAGVAVVGLFGMNIGISLYADPTNEEEKRASNMKFWETTLGTIAGCTVMYIVAMGWGKRSGLLQ | Function: Magnesium transporter that may mediate the influx of magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48356
Sequence Length: 444
Subcellular Location: Membrane
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A3BV82 | MGRRSGGRKLPFFASNASTSSSTKRTRSARRLPSLTRPRASSSPSPASPSPPPPSASHPAPPSPPLAVSPAGAGKVGKKKAGARLWMRLDRWGVSETLHLDKGSIIRRAGLPPRDLRILGPVFSDSSSILAREKAMVINLEFIRAIVTADEILLLDPLTIDVIPFVEQLTHHLPLKNLVCGNGQPGGDDHGEKHDDSHGDQVPRLNEATGAEHELPFEFQVLELALETVCSSFDVNVSGLERRATPVLEELTKNVSTRNLDRVRTLKSDLTRLLAHVQKVRDEIEHLLDDNEDMAHLYLTRKQLQNQQVEALISSAASNSIVPGGTSLSRLNNSFRRSVSIATSMHLDNDVEDLEMLLEAYFMQLDGIRNRILSVREYIDDTEDYVNIQLDNQRNELIQLQLTLTIASFGIAVNTFIAGAFAMNIQSKLYSIDDGSFFWPFVGGTSSGCFMICIVLLWYARWKKLLGP | Function: Putative magnesium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51671
Sequence Length: 468
Subcellular Location: Membrane
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Q10S25 | MALPCAFLSAAAAANATSFSSSPESRRCRSVHRVPSRPRPPLAPPARVMGKGNSKRKAANTRLWMRLDRRGGCEMILCDKSFVARRSGLPARDLRVLSPLLSRSPSILAREKAMVINLEFVRAIVTADEVLVLEPLAQEVLPFVEKLRKHFPLKSLDVDDVSTHMHTENQDGELAQDVSCYEVEGANHELPFEFQVLDFALEAVCLSYNSTISDLNRSAIAVLDDLMKSVSTRNLERVWSLKSSLTRLLASVQKVRDEVEHILDDNEAMAHLCTARKTKGQKDLLNTILFPETRLCRTHSSIENSTGIRTCVPSDSDAHILDMLLEAYFKQLDGIRNRIFLVRQYIVDTEDYISIQLDNKRNELLGLQLTLIIASFGIAINTFIAAAFAMNIPHRGYHFVIGVPFGQFVGATSFLCMSIVILLFTYAWRNRLLCT | Function: Putative magnesium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48747
Sequence Length: 435
Subcellular Location: Membrane
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Q10D38 | MAAAVVVAGEAAAAAAAAGAGGKKRGASRSWILFDAAGEERVLDADKYAIMHRVDINARDLRILDPLLSYPSTILGRERAIVLNLEHIKAIITAEEVLLRDPLDDNVIPVVEELRRRLAPSSATQHDVEGAEEDESPFEFRALEVTLEAICSFLGARTTELESAAYPALDELTSKISSRNLDRVRKLKSGMTRLNARVQKVRDELEQLLDDDDDMADLYLSRKLAGAASPVSGSGGPNWFPASPTIGSKISRASRASAPTIHGNENDVEELEMLLEAYFMQIDGTLNKLTTLREYIDDTEDYINIQLDNHRNQLIQLELFLSSGTVCLSLYSLVAGIFGMNIPYTWNDNHGYVFKWVVLVSGLFCAFMFVSIVAYARHKGLVGS | Function: Magnesium transporter that may mediate the influx of magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42189
Sequence Length: 384
Subcellular Location: Membrane
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Q01416 | MAAVVEVILAVMVVFLWPLTSVASSNVSSTLQCDKTNKRLATETISTPQATLKLACPSSTTFLPTYTGDAGTQTVYLTQDGSSTEKLQTALPGATAKQEDSQTNEMTLTFPQLPDTSQTVYFHCLGTENIAGQGSRKEVCGFAVTLTAPPPQGPQACVVPGTTIRLGIANEGDTTRFTCGGDLKLSPTAADKVFKEDCSTEESLKDLKRSEDKNSYFVLTATKTPSKTTHCYLCEPDPTKKGHNDKNCAVLIAVGAGSRPTARSVFGVAAPCILALLHFT | PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29679
Sequence Length: 280
Subcellular Location: Cell membrane
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P19599 | MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMANEGSNTNSVGANAPNADTIASGSQRSTNSASTSTTNNGESQTTTPTAADTIASGSQRSTNSASTSTTNNGESQTTTPTAADTPTATESISPSPPITTTESSKFWQCTNKTDGKGEESEKQNELNESTEEGPKAPQEPQTAENENPAAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLSNSSNIASINKFVVLISATLVLSFAIFI | Function: May play a role in the merozoite attachment to the erythrocyte.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27890
Sequence Length: 264
Domain: The N-terminal region appears to be involved in lipid binding.
Subcellular Location: Cell membrane
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B6JGA5 | MLKEFREFAMKGNVVDLAVGVIIGAAFGAIVSSLVGDVIMPVIGAITGGLDFSNYFIGLSKEVTATNLVDAKKQGAVLAYGSFLTVTLNFLIIAFVLFIVIRLINRIKRSEEAKPAEAPAPTKDQVLLTEIRDILKTK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14842
Sequence Length: 138
Subcellular Location: Cell inner membrane
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B7GLN3 | MWQEFKKFAVRGNVIDLAVGVIIGGAFGKIVSSLVNDIIMPLVGLILGGIDFSGLSWKVGEAEVKYGAFLQTVVDFLVIAFSIFLFVKLLNNLHERIKKQEETKQTAPTMTKEQQLLTEIRDLLKQQKETP | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14651
Sequence Length: 131
Subcellular Location: Cell membrane
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C1DER3 | MGMLSEFKAFAVKGNVVDMAVGIIIGAAFGKIVSSFVGDVIMPPLGLLIGGVDFSDLAITLKQAQGDMPAVVLAYGRFIQTVIDFLIIAFAIFIGVKALNQLKRKEAEAPSLPPAPTRDQQLLEEIRDLLKTRGKS | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14545
Sequence Length: 136
Subcellular Location: Cell inner membrane
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Q65QF7 | MSFMKEFREFAMRGNVVDMAVGVIIGGAFGKIVSSLVGDVVMPVLGILTGGVDFKDLKFVLAEAVGETPAVTLNYGLFIQNVFDFIIIAFAIFMMVKGINKLKKPVEEAPKGPTSEELLSEIRDLLKK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13930
Sequence Length: 128
Subcellular Location: Cell inner membrane
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Q1H3M0 | MFKEFKAFAMRGNVVDMAVGIIIGAAFGAIVKSLVDDVIMPPIGLLLGNVDFSNLFIVLKDGAEVAPPYASVAAAQAAGAVTLNYGLFINAVVSFTIVAFAVFLLIRAINKLKAEEPAAPEVTPEDIVLLREIRDALKK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14734
Sequence Length: 139
Subcellular Location: Cell inner membrane
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B2HEA6 | MLKGFKEFLSRGNIVDLAVAVVIGTAFTALVTRFTDSIITPLINRVGVNEQSDLGILKIGIGRGQSIDLNVLLSATINFILVAGVVYFLVVVPYNTLRKKGEVEQADDAQIVLLTEIRDLLAQTNSNSSGRHEAPGTAGTPPPNYGPRADT | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16135
Sequence Length: 151
Subcellular Location: Cell inner membrane
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A1TDR0 | METARLLFVHAHPDDETLTTGATIAHYVARGAQVHVITCTLGEEGEVIGDEWAQLAVDRADQLGGYRIGELTAALAELGVDRPRFLGGAGRWRDSGMDGTPARQQQRFVDGDFAEQTATLAAAIDELRPHVVVTYDPNGGYGHPDHIHAHRVTTAAVAASTWQVPKLYWTVTSSSALAAALASMGAVPEEWIRVSADDLPLFGYSDEAIDAALDLTAHESARVAALRAHRTQVSVSPDGRSFALSNNVALPVDPTEYYVLAAGSAGARDERGWETDLLSGLSVG | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 30238
Sequence Length: 284
EC: 3.5.1.103
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C8XJN6 | MYVADVPARLLAVHAHPDDESLTMAGTLAGAALAGAEVTLVTATLGEEGEVIGDELQGLIAARADQLGGYRLTELAAAGAALGVRERVMLGGLGAFRDSGMAGTPSAEHPRAFIRAQRGGPDHDRAARALAREIDRVRPHVLLTYDEDGGYGHPDHVAVHQVVLAALPLAAWPVPRVLAVIRPRTVTQADFAALTTPPGYLAAAADEVGFLAADDSVAVAVPVTAAAARRRAALAAHATQVELLPGEVFALSNRIAQPLPAAEYFRVLAGSPVPVGPDWTVPADVAAGLDLDR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 30266
Sequence Length: 293
EC: 3.5.1.103
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A4XB95 | MTTLPARRLLLVHAHPDDEAIGTGATMAHYAATGAHVTLVTCTLGEEGEVHVPELAQLAAAEADQLGGYRIGELAAACRALGVTDHRFLGGAGRYRDSGMMGLATNEHPRAFWQADLDVAAGQLVEVMRELQPQVLITYDGNGFYGHPDHIQAHRVAMRAHELAAAEGFAPAKVYWTAMPQSVLEAGMTHFAGSSDNPFEGIQEAVELPFCTPDERIAARIDATGQHVAKEAAMRAHATQIPDNSWLYSIAGNFGSEFMGVEYYTLAVGDKGPGFGPYGWEDDLFAGLPVAEGSDRTPVADGADRAPVGATGQR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 33394
Sequence Length: 314
EC: 3.5.1.103
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D6ZE32 | MNDNDSPRALFVFAHPDDETILSGGTMARLAAEGAHVSLLTCTLGEEGEVIAPELRELAADRADQLGGWRIAELRSALDRLGSPRGARISQHWLAGPGRWRDSGMAAGRNTHPRAFIGGDFGEQARAAAKTIREVRPHVVVTHDPEGGYGHRDHIYANRLVVEAVKIAAAETHSEFGAPWQVKKLYWTGIGESAWRRAIKELGRRAIPDGFELVHADVAKPRRDEEITTVVDIGDYRAAKLAALAAHATQITVCHELAAFALSNKALTPVPAEEHFLLVPLRFGAVDNQDLDNRNPNSQPPADQAREDHLLTGLGFA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 34501
Sequence Length: 317
EC: 3.5.1.103
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Q9F344 | MTDLPGRRLLLVHAHPDDESINNGVTMARYAAEGAHVTLVTCTLGERGEVIPPALAHLSGAALGGHRRGELADAMRALGVDDFRLLGGPGRYADSGMLGLSDNDDPGCLWQADVDAAAALLVDVIREVRPQVLVTYDPNGGYGHPDHIQAHRIAMRAAELAAEAGCPVAKVYWNRVPRSRVEDAFARLRDDLPGLPFEKAAGVEDVPGVVDDERITTEIRGEGTAYAAAKAAAMRAHATQITVAEPYFVLSNDLAQPILTTEYYELVRGERGGEGRENDLFAGIAGTFDTGEATS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate
Sequence Mass (Da): 31433
Sequence Length: 295
EC: 3.5.1.103
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Q5Z297 | MGDITVRWTQRLDGETADAVRELLAAASAADGVAPVSEQAVLSLGEPGAARHLLAEHDGELAGYANLVPAHGDHPAMAEAAVAPARRGRGIGTALVREALAAGGADARVWAHGDRPAAKAVAARLGLRTARELWQMRRSLATPQLPELVVPDGIVLRTYAGPADDAELLRVNNAAFDWHPEQGGWTQRDIAVRRAESWFDPAGLFLATDTAAPDRVLGFHWTKVHADEQPPVGEVYVVGIDPAAQGRGLGRLLTLAGLHHLRERGLGGVLLYTEADNTAAVNTYTKLGFAPAHVDVAYAANGA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 31936
Sequence Length: 303
EC: 2.3.1.189
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A1SPL0 | MDDHAADLLAAVAEVARAAEAADGAAPLDEATWLALRHHPERVRSWVRAGGFALVIGADLSLVVHPQARGRGLGAGLLSSALAGLSAGMPLEAWSHGDHPAAAALARSHGFERARELWVMRRQMASALPQLRAPDGVTVRAFRADSGDAEEVLRVNAAAFAHHPEQGSMDATNLAERMAEPWFDPDGLLLATSAAADGGEQVLGFHWTKVHPGDAGAGAGPGVEVGEVYVVGIDPAAQGRGLGKVLTLAGLHHLAGRGVPEVLLYVESDNRPAIAVYAGLGFTHADDDTHVQYRR | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 30832
Sequence Length: 295
EC: 2.3.1.189
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A1R8Y2 | MSHAHPENWPVLIIAGALDTELLRDVKTLAAAAGESDGNPPFSEQTLVTLRGADAGDHSVLSFVLYAPDEDSDPATAEDLAGVAVVVENGDESGVLELAVHPSYRNQGVAGRLLDALQGKRGLGGLSAWSHGNHEAAAELATRFGYGPVRELWKMRLMSSTSALPDAGLPDGVSLRAFVPGQDEQAWLTANSAAFSHHPEQGSMTRADLEARKAEDWFDPEGFLLAVNAEGELLGFHWTKVHPRQGPHPAIGEVYVVGVTPEAQGLGLGKALTVAGIKHLQDQGLHAVMLYVDADNEAAVALYQKLGFVRWDTDVMYGPLTKN | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34421
Sequence Length: 323
EC: 2.3.1.189
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D7GG24 | MNPVVTGPIIRLSADDRDHIADLVRACTEHDGVSPLNESGWFGLQGLTASHTHWIARDGKQVVGYAQADAREHTVQLMVAPPARRQGIATTLAKAAWQLHPAMWWSFGDCPGARELATQLGLREVRKLLKMSLPMPADQPHDAHLPEGLRLDHFRDDDLDQLVAVNHAAFVHHPEQGAMTAEDARNRMAQDWFDPAGLLVARDEAGTLVGFHWTKVADEDGRPRGEVYVLGVDPDFEGKGVGRALLDAGILHMRELGVEAIDLYVEGANERVVHMYERAGFSVVSTDVGYAPAKPARHQDHGRQSSPQERDA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34330
Sequence Length: 312
EC: 2.3.1.189
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A9WNI5 | MTTGPATPPQTNHAEDRTEWPIQVLRAAPETYLLQEILKLAEVAIDTDGHPPFSDQTLIQLRSANAPLLILLSYVPAAPEVPAALAGVAVVLEHDGQPASGTLELVVHPTYRNQGVGQVLLKSLQSARGFESLNAWSHGSHAAAQQLADQFGFEAVRALRRLRLALDAGHQLPAASLPTNISLRSFVPDQDEAAWLAVNAAAFAHHPEQGETSLADLKSLMEEQWFDAAGFLLAVDETDQIMGFHWTKIHAAPAGHQAIGEVYVVGIAPAAQGKGLGKALTLAGIDYLQKKGLSSIMLYVDADNTAAVSLYQSLGFARWDADTMYSYPSATNSNNKFQ | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 36273
Sequence Length: 338
EC: 2.3.1.189
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D2NRH2 | MMVDNQTPDSSTLSTASTPVYAEPQLTEELLERFDSFAQKVARHDGVSAFSEQTRIELSKALRESTLTPPRFFVAEDNGTLAAVFVALTPANDEDTGVIEAAVAPEYRGQGVGSAFFDHAVRQLGDDATRYRLWVHGSATDTGIESPAHAFATLHGFEPVRVLYKMVLPLDAQTREELVERSDARTLPENLRMRTFTGADEFPWLRVNAAAFAHHPEQGKLTLADLRERTGSPWFRPEGFFIASEVEDDSAIAAFTWTKIPTGQEQSELSPSGEIYVVGVNPQAQGGGLGRTLTLRALAYLACAEDENGEPLRAIDLYVDADNTAAYSLYTSLGFGVATVDRMYAPAQQDEPAA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 38639
Sequence Length: 354
EC: 2.3.1.189
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A4FQD4 | MALLRETERADGVAPVGEHVILRLKAHLDVVHQIEPVQADVPGSEHFVVRDSGGELAGYAHVDTAEEKTAGQLVAELAVHPRHRRRGAGARLVEALLDRADLPVEPSPDDTDTARLRIWSHGEHPGALRLAERYGLVRARELWRMGRPLDTELAEAELPPGVTIRAFRTGVDEPAVVRVNHRAFSWHPEQGAMTEDDLRLKEREDWFDPAGFLLAVDSHDTLLGFHWTKIHPDGTGEVYVVGVDPDTQGNGLGRSLTVAGLRHLRAKGCAQVMLYVEADNTAAIKVYQRLEFARWDTDVQFGR | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33638
Sequence Length: 303
EC: 2.3.1.189
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A4X1M6 | MNSTEPDSDRVTRTDRLNAPEIADVQALARAAGDADGADPFDEHTLLRLRDPHAPTHHLTARTANGTLTGYAHLDITNPTSGTGVELAVHPAYRRRGTGRALARSVRAAVTGPLRAWAHGDHPSAAALAVDLDYRRARVLWQLRRPLTAPIPEPPLPDGVTLRAYRPGADDDAWLALNAKAFADHPEQGQWTAADLQARRDEPWFDAAGFLLAVDPAGQLLGFHWTKIHERPGSARIGEVYVLGVDPTAHGGGLGKALTAAGLAYLRDQRGLDRVMLYVDESNTAAVALYERLGFARWSAHVNYQLG | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33261
Sequence Length: 307
EC: 2.3.1.189
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D1BE23 | MDHSEIDVETSPLTAADAQAVHRLARAAEHVDQVAPLSEQPLLRLLDAEAPTTHLMVRAADDLAGYAQVDRGAPGTASAELVVHPFARHHGVGTALLEHALELMDAEGRVLSVWAHGDLPAARSLAARTGLVVVRELWKMHLPLDGSTSTPESAPAAPLAPGVSLRAFRPGEDDAAWLAVNARAFASHPEQGRLTQTDLAARVAEPWFDAGSFLLAERDGDLVGFCWLKVPADQPQDAPRVGEIYALGVDPSAQGLRLGTALTAAGLDRLREVGVEVVELYTEGDNTVAIRTYTAAGFTRATVDVQMARPSDATA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33381
Sequence Length: 315
EC: 2.3.1.189
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D6ZEJ5 | MDDLVREELPNGTRRLFARDAQGGEAGFAVIEPGRPGQPAMVEVQVRPEHRSCGLGGRLVRAALDEAGPGAYLWDHENSPASQAIVRRNGLVPVRTLCQMRRWLAYPPLPEPVFPDGVSVRQYQGPQDDEELLRVNNAAFDWHPEQGGWSIEKLRERLAQPWVDPAGIFLARDEQDRLIGFHWTRTHPQTQTEHKLGEVYVLGVDPACHCKGLGKALTLVGLRHLRDQGLAQAKLYVEQTNAPALATYRGLGFTVHAQDVAYVRG | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 29499
Sequence Length: 265
EC: 2.3.1.189
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D3Q4A8 | MIRVEIYERLEAAAVAEVLELVEAGARADGLSALNEQTILNLRHGGAEAEPGAHLMIRDAEGTLVGYANLELDNDGVAAVEMLVHPTHRHNGHGEALLAALIKRATAAKCRALTIWAHGDHPTALLLADRHDFTRDRVLWQMRRHLTDADGDGEPAAGITIRSFVPGRDETRLLEVNNAAFADHPDQGGWTVRDIAMREREDWFDPEGLLLAERDVDGQVLGFHWTKVHGSGDSAIGEIYVLGVAPEAQGLKLGAALTTAGLRYLRGRGLDTVMLYVDESNVRAVRLYTGAGFTRWTTDVNYHKKL | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33514
Sequence Length: 306
EC: 2.3.1.189
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Q9KZV0 | MTSDDTVRPGRPRSIETLAELTPEQTDAVLALLTEAARTDGQHAVSEQGRLQLRGPAREGVVHLLLTLDGGELVGYAQLEGTDPVEPPAAELVVHPSHRGQGHGRALGSALLAASGKRLRIWAHGGHSAARHLAQVLGLSLFRELRQLRRPLTGLDLPEPRLPEGVSVRTFVPGQDDAAWLAVNAAAFAHHPEQGSLTQRDLDDRKAEPWFDPAGFFLAERDGELIGFHWTKVHAEERLGEVYVLGIRPDTQGGGLGKALTTIGLRHLEGQGLPTAMLYVDADNKAAVAVYERLGFVTHETDLMYRTET | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33519
Sequence Length: 309
EC: 2.3.1.189
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P33748 | MTVDHDFNSEDILFPIESMSSIQYVENNNPNNINNDVIPYSLDIKNTVLDSADLNDIQNQETSLNLGLPPLSFDSPLPVTETIPSTTDNSLHLKADSNKNRDARTIENDSEIKSTNNASGSGANQYTTLTSPYPMNDILYNMNNPLQSPSPSSVPQNPTINPPINTASNETNLSPQTSNGNETLISPRAQQHTSIKDNRLSLPNGANSNLFIDTNPNNLNEKLRNQLNSDTNSYSNSISNSNSNSTGNLNSSYFNSLNIDSMLDDYVSSDLLLNDDDDDTNLSRRRFSDVITNQFPSMTNSRNSISHSLDLWNHPKINPSNRNTNLNITTNSTSSSNASPNTTTMNANADSNIAGNPKNNDATIDNELTQILNEYNMNFNDNLGTSTSGKNKSACPSSFDANAMTKINPSQQLQQQLNRVQHKQLTSSHNNSSTNMKSFNSDLYSRRQRASLPIIDDSLSYDLVNKQDEDPKNDMLPNSNLSSSQQFIKPSMILSDNASVIAKVATTGLSNDMPFLTEEGEQNANSTPNFDLSITQMNMAPLSPASSSSTSLATNHFYHHFPQQGHHTMNSKIGSSLRRRKSAVPLMGTVPLTNQQNNISSSSVNSTGNGAGVTKERRPSYRRKSMTPSRRSSVVIESTKELEEKPFHCHICPKSFKRSEHLKRHVRSVHSNERPFACHICDKKFSRSDNLSQHIKTHKKHGDI | Function: Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes. May be regulated via WHI2-PSR1 complex phosphatase activity.
Sequence Mass (Da): 77861
Sequence Length: 704
Domain: The 9aaTAD motif (residues 261 to 269) is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Cytoplasm
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P33749 | MLVFGPNSSFVRHANKKQEDSSIMNEPNGLMDPVLSTTNVSATSSNDNSANNSISSPEYTFGQFSMDSPHRTDATNTPILTATTNTTANNSLMNLKDTASLATNWKWKNSNNAQFVNDGEKQSSNANGKKNGGDKIYSSVATPQALNDELKNLEQLEKVFSPMNPINDSHFNENIELSPHQHATSPKTNLLEAEPSIYSNLFLDARLPNNANSTTGLNDNDYNLDDTNNDNTNSMQSILEDFVSSEEALKFMPDAGRDARRYSEVVTSSFPSMTDSRNSISHSIEFWNLNHKNSSNSKPTQQIIPEGTATTERRGSTISPTTTINNSNPNFKLLDHDVSQALSGYSMDFSKDSGITKPKSISSSLNRISHSSSTTRQQRASLPLIHDIESFANDSVMANPLSDSASFLSEENEDDAFGALNYNSLDATTMSAFDNNVDPFNILKSSPAQDQQFIKPSMMLSDNASAAAKLATSGVDNITPTPAFQRRSYDISMNSSFKILPTSQAHHAAQHHQQQPTKQATVSPNTRRRKSSSVTLSPTISHNNNNGKVPVQPRKRKSITTIDPNNYDKNKPFKCKDCEKAFRRSEHLKRHIRSVHSTERPFACMFCEKKFSRSDNLSQHLKTHKKHGDF | Function: Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes.
Sequence Mass (Da): 69723
Sequence Length: 630
Domain: the 9aaTAD motif (residues 237 to 245) is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Cytoplasm
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P40873 | MSIKKDYDVIVVGAGSMGMAAGYYLSKQGVKTLLVDSFHPPHTNGSHHGDTRIIRHAYGEGREYVPFALRAQELWYELEKETHHKIFTKTGVLVFGPKGEAPFVAETMEAAKEHSLDVDLLEGSEINKRWPGVTVPENYNAIFEKNSGVLFSENCIRAYRELAEANGAKVLTYTPVEDFEIAEDFVKIQTAYGSFTASKLIVSMGAWNSKLLSKLNIEIPLQPYRQVVGFFECDEKKYSNTHGYPAFMVEVPTGIYYGFPSFGGCGLKIGYHTYGQKIDPDTINREFGIYPEDEGNIRKFLETYMPGATGELKSGDVCMYTKTPDEHFVIDLHPQFSNVAIAAGFSGHGFKFSSVVGETLSQLAVTGKTEHDISIFSINRPALKQKETI | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidative demethylation of sarcosine.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 43294
Sequence Length: 389
Subcellular Location: Cytoplasm
EC: 1.5.3.1
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P40854 | MSPTYDVIVIGLGGMGSAAAHHLSARGARVLGLEKFGPVHNRGSSHGGSRITRQSYFEDPAYVPLLLRAYELYEELERATGRNVATLCGGVMAGPPDSRTVSGSLRSATEWDLAHEMLDAKEIRRRFPTLAPDDDEVALFEAKAGLLRPENMVAAHLQLATRQGAELRFEEPVLRWEPYRDGVRVHTGENTYTAGQLVICPGAWAPQLLADIGVPITVERQIMYWFQPKGGTGPFVPERHPVYIWEDADGVQVYGFPAIDGPEKGAKVAFFRKGQHTTPETIDRTVHAHEVRAMADHMSALIPDLPGTFLKAATCMYSNTPDEHFVIARHPAHPESVTVACGFSGHGFKFVPVVGEILADLALTGATAHPIGLFDPARLTAPAARGVQP | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidative demethylation of sarcosine.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 42263
Sequence Length: 389
Subcellular Location: Cytoplasm
EC: 1.5.3.1
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P54815 | MTDRNELIGVAIRVVAAAAVSFLSVRYLVKYLDPNYSVNEESKKKVAQLFHELGIDRQIELSEHEIRIATQFVGGEDVGADWDEIGGCEELVAELKDRIILPLRFASQSGSHLLSPPRGILLYGPPGCGKTLLAKAVARAAGCRFINLQVSNLTDKWYGESQKLAAAVFSVAQKFQPTIIFIDEIDSFLRDRQSHDHESTAMMKAQFMTLWDGFSSSGDQIIVMGATNRPRDVDAAILRRMTARFQVPVPNAKQRSQILNVILRNEKINNTVNLGEIAQAAEGLSGSDLKEVCRLALLARAKATVASGGSVNQLLPLEQSDFESAVHKYMRAAHLLVEETLD | Function: Involved in intramitochondrial sorting of proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37662
Sequence Length: 342
Subcellular Location: Mitochondrion outer membrane
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B0BK71 | MKLFSASVFAAIIASHYASATAHIRAPNVKPRRTNSLLTAPPQQPPLPSAQQAASASSSAGLNLTDIQGDILIGMKKNKELFFFFSITDAATFKAKLGSDILELITSTNQLLAVATQPITAVNVAFSSTGLKALGITDDLKDPVFEAGMLSNAVSDLSDPGTGNWVPGFVGTSVHGVFLLASDTIDNVNTELANIQTILNGSITEIHRLQGEARPGDQQGHEHFGFMDGISNPAVDGFTPPAEIRPGQALIPPGIMLLGEANDTFQNDRPPWAKDGSFLVFRQMQQRAPEFNKFLQDHALNMPNMTSEQGADLLGARIVGRWKSDAPIDLTPLVDDPVLAADNQRNNNFDFSDATNQTRCPFSAHIRKANPRGDLGGINKFPNQHIIRAGIPYGPEVTDAEKASNSSSTDPSLERGLAFVAYQSNIQNGFVFLQKNWVDNTNFFRPGTGVDPLIGTNSRNSGTDAPNTPRVVSGLDPNNATSTIEIGIDFVVSRGGEYFFSPSLSAIRTVLSV | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer.
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known . In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 . Also degrades beta-carotene .
Catalytic Activity: 2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate
Sequence Mass (Da): 54972
Sequence Length: 513
Subcellular Location: Secreted
EC: 1.11.1.19
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Q7VI69 | MAVIYLAGGCFWGIQGYFDKLKGTLCSQVGYANSAVENPSYEFVCSGNSGAVEALELHYDEDLLPLREIIGRFLSVINPCALNFQGNDIGTQYRNGVYFVQESDESIIKECLKLWEKKHHKKAVTEVEKLQNFYSAELYHQKYLEKNALGYCHINTDLALQKWEE | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18816
Sequence Length: 165
EC: 1.8.4.11
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Q9UJ68 | MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAAKHHVNGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCSEKTGHAEVVRVVYQPEHMSFEELLKVFWENHDPTQGMRQGNDHGTQYRSAIYPTSAKQMEAALSSKENYQKVLSEHGFGPITTDIREGQTFYYAEDYHQQYLSKNPNGYCGLGGTGVSCPVGIKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 26132
Sequence Length: 235
Subcellular Location: Mitochondrion
EC: 1.8.4.11
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A9KPX7 | MNKTIYIAAGCFWGGEKYFSLIHGVLSTKVGYANGTTSNPTYEEVCHNNTGHAETVEIQYDDSILPLEKLLRLYYEVIDPTSVNKQGGDQGIQYRTGIYYIDEADLEIIKPSLEELAKKYDKPIAIEVKQLLHFYDAEEYHQKYLDKNPSGYCHIGQCAFDSAKNA | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 18816
Sequence Length: 166
EC: 1.8.4.11
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Q04PP8 | MEQATLGGGCFWCLEAVYQMVEGIESVVSGYAAGQTKNPDYRSVCSGTTGHAETVQITFDSKVISYFEILEIFWISHDPTTLNRQGNDVGTQYRSIILYHSPEQKKQAEQSIQKAGEHFSDPIVTQVEILKEFYPAEDYHQNYFRTNPKQAYCHYVIKPKIDKYLKTGFKVKKEGS | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 20065
Sequence Length: 176
EC: 1.8.4.11
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Q03W54 | MAIETAIFAGGCFWCMVQPFDSLDGIEKVRSGYTGGHVENPTYEQVLTHTTGHTEAVKIWFDSEKISYRELVEIYWEQTDPTDAMGQFQDRGDNYRPVIFVNSPEQREIAEESRAALAASNRFDEPIVTKIEDAKPFYEAEEYHQDFYKKDPEREALEMAQRLQFKADKWN | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 19875
Sequence Length: 171
EC: 1.8.4.11
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Q1WU33 | MSKDTAIFAGGCFWCMVEPFDKMPGIISVRSGYTGGFVENPTYEQVCSHTTGHTEAVKIVFDPEIISYAELVNIYWRQTDPTDAMGQFQDRGDSYRPVIFVHDEEQRKIAEESKKALAESGEFDKPIVTQIEDAKPFYEAEEYHQDFYKKNPERYALEEMGGREQFRNQHWN | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 19941
Sequence Length: 172
EC: 1.8.4.11
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Q92AE8 | MTKESLEKATFAGGCFWCMVKPFDTQPGIEKVVSGYTGGHTVNPTYKEVCSGTTGHTEAVEITFDPAVFPYEKLVEVYWQQTDPTDAAGQFVDRGDSYRPVIFYHNEEQRQIAEKSKAALDASGRFKKPVVTEIAKAETFYPAEEYHQDFYKKEKAHYEGYQVASGRAAFIDANWKG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 19933
Sequence Length: 177
EC: 1.8.4.11
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B7LQ21 | MANKPSVDDLKENLSEMQFYVTQKHGTEPPYTGRLLHNKRDGVYRCLVCDTPLFNSQSKYDSGCGWPSFYEPVNENSIRYLTDLSHGMERIEIRCGHCDAHLGHVFPDGPQPTGERYCVNSASLSFTDEKSGDQIKG | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15463
Sequence Length: 137
EC: 1.8.4.12
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B0UUL6 | MKKLTSNDVTPEEIFYQRRKIIKAFGLSAVATALPTFSFAQESSDLKALEYKKSTESTLILTPENKVTGYNNFYEFGVDKGSPAHYAKKFQVNPWKLEIGGEVENPFTLNYDQLFTQFPLEERIYRFRCVEAWAMVVPWIGFELNKLLEKAKPTSKAKYVVFHTLYDPEQMPGQKNHFFGGGIHYPYVEALTLAEAMHSLTLMSVGLYGKALAPQNGAPIRLVVPWKYGFKSIKSIVKITLSETRPRTTWESLAPNEYGFYANVNPKVDHPRWSQASERVIGAGGLLRVKRQPTLMFNGYEREVAHLYKGLDLRINY | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 36226
Sequence Length: 317
Subcellular Location: Periplasm
EC: 1.8.5.-
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Q88DZ2 | MLIKLPRSSECKASEITPEGIYLSRRTLLGGSLAGLALGALPGGVGAAQMSRYADVQAGAAPAWFTDKLAATRWQAVTVKDEAITPFKDATHYNNFYEFGPDKGDPAANGDSLKTEPWSIVVDGEVRKPGRYALEDFVKPYQLEERIYRLRCVEAWSMVIPWLGFPLAQVLKQVEPTSSARYVRFETLKDPQHMPGQRSGFALIDWPYREGLRLDEAMHPLAILAVGMYGRELPNQNGAPLRLVVPWKYGFKSIKSIVRISLVAEQPGTTWEGLAPDEYGFYANVNPTVDHPRWSQARERRLPSGLFSPNVRETQMFNGYADEVASLYTGLDLRKNY | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 37688
Sequence Length: 337
Subcellular Location: Periplasm
EC: 1.8.5.-
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Q6Z401 | MAGGVVVNNGGGKDYPGKLTMFVLFACIVAATGGLIFGYDIGISGGVTSMNPFLIKFFPSVYRKEQAAEKNQSNQYCKFDSPLLTMFTSSLYLAALVASFFASTVTRVAGRKWSMFGGGVTFLVGAALNGAAKNVLMLILGRVLLGVGVGFANQSVPLYLSEMAPARLRGMLNIGFQLMITIGILCANLINYGTAKIKGGWGWRVSLALAAVPAAIIAVGALFLPDTPNSLIDRGHTDAAKRMLRRVRGTDDIEEEYNDLVAASEESKLVAHPWRNILQRRYRPQLTMAIAIPLFQQLTGINVIMFYAPVLFKTLGFADDASLMSAVITGLVNVFATFVSIVTVDRLGRRKLFLQGGTQMLACQIVVGSLIGAKFGFSGVADIPKAYAAFVVLFICAYVAGFAWSWGPLGWLVPSEIFPLEIRSAGQSINVSVNMLFTFIIAQAFLPMLCRFKFILFFFFGAWVVIMTLFVAFFLPETKNVPIEEMVLVWKSHWYWGRFIRDEDVHVGADVEMPAAGNRNGKVDPAKLAN | Function: Mediates active uptake of hexoses by sugar:proton symport (Probable). Can transport glucose, fructose, mannose, galactose, xylose and ribose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57732
Sequence Length: 530
Subcellular Location: Cell membrane
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G4NEB8 | MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELFERDPFVQAAKRTPVDLREWAFGLMERDNRKSHLAPQLSPATADLLRSSDSPTATYHGDDRPLETPTSAYRVDPRRGPAEGSAGLADQVDRLYIRD | Function: Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth . The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes . MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46171
Sequence Length: 415
EC: 2.7.11.24
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O83293 | MFSVRIETLGCRLNHVESESLAALFLQEGFAVCRGNTSTAPVVLCVINTCTVTSKAEQKARRLVRLLLRTYPTAIALVTGCYAQLEPASLEAMDDRVLAFPGKQKDALSLLPSCLRALLVQRGPAPIDQYVCGMRALLASLKKKIISLELTSEFPSQTHMPTRNALPQLTGVPHAPRVSVSSFSEPTAVPRFALYAPRFLFHSRASIKVQDGCNSGCAFCRIRFARGRAVSLETHEVIGRVQALEARGMSEVVLTGVNLSQYRSGSIDFAGLLELIVQETHTIHIRISSLYPESVTSAFLRAIAHTRVSPHFHLSVQSGSDRVLRRMRRAYTRADIYQAVSDLRSVREEPFLGCDIIVGFPGETEEDFADTQRMCKTLRFAGIHVFPFSARPGTEAFAMDAKVPQRIAGERVAAMQQLAEKNYRAYLEYWNGRELCAVVEQSVARVLTENYLSLPIIERGGVAASAGSHVRIRVHNEGAILL | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53173
Sequence Length: 482
Subcellular Location: Cytoplasm
EC: 2.8.4.5
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O29701 | MILIKNAKILTPKGIVEGNLKVEGKKISEIGGKAVKSDVVIDGSRKAVIPGFFNTHTHAAMTLFRSYADDMQLHEWLEKKIWPLEAKLDDKAVYWGTKLACVEMLKSGTVFFNDMYFFPEAIARAAEECGIRACVSAAFFDFFNPDLLELNLKNAVKSLREIEKYDVLRAIGPHAVYTVSLDGLRRAAEIAEEMDIFMHFHLAETEKEVLDFKKQHGKLIVQALDEIGFLSKRLIAAHSVWLEDAEIEILAKKGVSVAHCPASNMKLCVGKAIRYEAMKRAGVNFTLATDGAASNNNLDMLEEMKFAALLQKFHHSNPTLLKAEEVFEAATLNGAKAFGIKSGVIKEGYEADIVLVDLAKPYMQPEHSLIANLVYAASSGCVDTVIVKGEVVVEGGVFRSEEEELKIIEKANEVAKRLTGSA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 46595
Sequence Length: 422
EC: 3.5.4.28
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O29265 | MHDLVIRNGLCFINGEFVECSVGVDGNRITHVAKEVERGEIEIDAAGCLVMPGCFNAHTHAAMTLLRGYAEGLPLREWLEKVWEVEARLDEDAVYWGTMLACVEMLKSGVTAFADMYIHMDAVAEAVGESGMRAVLGYGMADRGDEERARKELEIGLEFAEKWNGGFEGRVTTMLAPHAPYTCSPEFLKVVSDASKDKGFLKHIHVSETLWEVKEVRERYGKRPVEFLDSIGFLDSSTVLAHAVWLSEAEMKILAERGVSVAHCPTSNLKLSSGIAKVSELLEMGVNVGIGTDGAASNNMLSVLSDARVGALLQNLRGRTLKPGHWLEMATEGGYRAYNLKGGRIEEGYLADIVVFSKTCRNAPMHDPAAMLYVENQALHAVVDGVLVMEDGILVNVEEEKVIEKAEETALELVGG | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 45487
Sequence Length: 416
EC: 3.5.4.28
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Q2LUH4 | MAKTELDLLIRGSVLLTMREEEAVIENPVVGIRNGKIVLIMQNDLFTEEEYTARKVLDRSNTLIMPGLVNTHTHLAMSCFRGLADDLPLMAWLHEYIFPAEARHVNPEMVYAGSLLAMAEMILSGTTTFCDGYFFVDQVARAAKDAGMRAVVCQGFIDFPTPDTSDPSRQMETAERFIGTWKDASPLIQPALFCHSPYTCSPETLVRIKEAARREKILYVLHLSETREEVSLIQDCYGKRPALHLHNLDVLDPDTLAVHCVWLDEEEQGVLADCGVRVSHTPQSNMKLAAGIAPVPAMQAMGISVSLGTDGSASNNDLDLFREMDSTAKIHKVATGNPAVMDAARVVRMATSEGAGALGLQDRIGSLEVGKAADLIILDLNQPHLTPMYHPFSHLVYAASGADVLTTVIDGNVVMENRKILSFDLEAIMREVEKIAEKIRKSCRK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 49005
Sequence Length: 445
EC: 3.5.4.28
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A3DEQ2 | MNILIKNADIITCNASDDVLQGAFLGIKDGYIDFIDTKEDALKDFKADRIIDAKGKLVMPGLVNAHTHSGMTILRNFANDLALEDWLFGNVLPVEEKLTPEDIYWGTLLGIAEMIKSGTTTFADMYLHMEEVARAVSETGIRANLCRSPLKDSDKSVEDAVRCFEYFKKWDNSFNGRIKVYIEVHSVYLFDEPSLRMSAEVAKEINTGIHIHVQETLKECEDSNKKYGMSPAEICCKTGIFDVPVIAAHCVHLSDGDMGIIRDKGVNVIHNPTSNLKLGSGIAKVDDMLKNGINVALGTDGAASNNNLNMFEEMHLAALIHKGVHMDPTLIGASCALKMATVNGAKALGFGGEIGEISKGMKADLILIDMDKTHLCPVNDPVSAVVYSAQSSDVDTVIIDGNIVMENRELKTIDEEKVKFNVKEIAKRVLR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47277
Sequence Length: 431
EC: 3.5.4.28
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O66851 | MEKYDLLIKNVLIPEKEGEWDIAVKDGKIEKIGKNIVGEAKYTINGKGKIAFPSFANMHTHISMTLLRGLGADLPLHDWLQKVIWPLEGEFVSPEFVKDGALLGIVESIRSGTTLFMDMYFFEEAVAEACEDVGIRAGLGFGILDFPTKVAKTPEEYIQRARKFAEEFKNRELVFPVICPHAPYTCSPNTLRMAKELADEYGLLLHIHVAETKEEVERIKEQYGKTPVEHLESIGFLDKNVLCAHMVWTTEKEREILKERDVKIAHCPESNLKLASGIAPVPDYVKRGITVTLGTDGAASNDNLNMLEETSTCAKFHKGYNLDAKAIDAGTALKIATENGFKVAGIKAGKVEEGYEADLILVDTDFPEFQPLYDPISQFVYSANSECIDTVICKGKVLMEKRELKTVDQEEIFAKARKWREKILSKLSSL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48152
Sequence Length: 430
EC: 3.5.4.28
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P10835 | MNVEQYTQVTTDFEKTLTKEKKSKQGIFFTPKTVREKLFGFTEHFQNTPGFSILEPSCGTGEIISECVERFPLASIKGVELDNDMSTICSKKYAEYNVDIVNEDFLLWKGGKFDFIVGNPPYVVRPSGYKNDNRIAKGRSNLYVEFLYKCITEHLKEDGILAFIIPSTIGNSSFYEPIRKLIITLDILSFEILDKHDFCDTNTRLCSIVIKNSPGTGKYTYRDYICDKDIPHHGNSYIGSLDLKFKTGFAWANVNKFFTDKSEIPFFTSSNIKLNEIHIGDKMKYLTQDTTKFFTGKALLIKTASAGKRGGRFEFGFSLYENDKWAVDNDIIVIQGPDTVLSIVQDVLMKDVTNEFINILVNNGHISMKLLKSIPLF | Function: A gamma subtype methylase that recognizes the double-stranded sequence 5'-TCGA-3' and methylates A-4 on both strands.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42895
Sequence Length: 377
EC: 2.1.1.72
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Q75AQ7 | MGSFLLCLLLVQLQWCLCSNVLDDLLQQTNIAFLSQQDVIGVIPVNQIPLVGVELCSMFETVGDGQDTLAAMLQTGVQTLVMDIGYDEDAGGWQMCGRTSLSEGISTVSRQIERLFPTLYANLVVLVLRGGAAEAHYEALRDAIGRVGRWTYSAEKVKATSPHLNSLLDDQEKRVLVVALDDSLCEALGTVAFGPEDVAYVEGNDTIDCSEHTDSWSFIEREFHWTDVREYVRLGCSPVITGKSVANISELEALVKVAQVWSWGAGEPALTDANSEMQRCASLGYDSATERATWKSTSCRQNLPVLCQAVNDRYSWLVGTRNLRFDQLNMDSCPSGYKPSVPRTPLEQREVERYLSEHHPSDGQYWIYLNSISVEKCWVVGGPETPCPYVALVSTRNFAAMIVTSSILVLLLLVLIILLDLVRVPIQDNRRSWKRALGSYSKAETEGVPM | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49856
Sequence Length: 450
Subcellular Location: Membrane
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Q6FR11 | MYWLLFLFFVHFLRHGLCDTSTRSNGSGTMNPAGINITNSTYMNATWQSNSLSHELAVRSQRDIMSNITIDQVPFPGINLNSVLFHKAFIVNNNGSHLPFNESIAFEYFQNIMVYGAQSFVVDIEVGMNYSWVLKETDVLLSDLLIQMRNFISATNNNLYGNVLMLLLRVDPTIKLASARNKTIYNSRLNFTDDLFNKFPNLNITGILDNTIGRSFIYTPSDFLGTYDPPYSIDNSTNFWPTLGALMYGRRKRLLAMEITNSFDALESNYIFTNHNLTYDVGNVSISCPYNRDQFISASETTFKFLEARYTKSEVEMYSGCGYSPMIANRFDSANITALIDLLAPAVVWSWAVGQPILTVSVPRKTSDLVAENCAAFNFAYNNFSANWFVENCYSKKRALCRSDKQIFNWTATNVKDSYFEMDGYRGETKCPNTYSFSIPRTPLEQRSILLQFEASQFNDDTLWIDLNSISVSNCWVSGGSYASCPYQRAVSTRNFVAMMVPVTVCSFVLLMMALYFSLFRIPIYDNRYNWRRVVNNYSKTEVDGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62477
Sequence Length: 548
Subcellular Location: Membrane
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C5MA32 | MKPVYCFSILALLQIFTVVVSESNWPTLNFTLEIASRAQRDISKLLPISQITTVGISLSSIFRNSGYTVDALSPLYDLLNGGNEAIMIDLYWNEFTSQWQLCPAPFPSNTTYNMNDVVDLSWENNDYQCQPGLSTENIMGIINSYIRDTNTNIGANFLRILFNLKSIHYENSNRTIDLQNIYKPSILNPVNIGNDTLNDTIASLGSYIFTPTVLSQYQSDASHVEKASSGSSINSTQAISYFYNQSNIIVPSLDTVLLSEYKRVSAHISSNELVNSSRVYQFTSYDTDLIFFNDVVPLVVENTTTGVAGRYCNELFNAYNSTGVDIETFNNLSLTTRLRFIVDSDENPFTVDTLSKFVRCGYSAIFNGTYDVGVNSSSLDFSDEVDEFIPYGFWSWSPGQPVDLNDTNSDSINNASMSSNNTDDSNGNSLAFKCVVLTETGWSVANCYDRHVIACQNSTSRNNWVLQETNKRNYFEIDKGDCPEGYTFSIPRSSTEMLSLQATVKQRNVPYPIWLDLNDITVPNCFVSGGPYAQCPYQRTITTNKFVRMIAPSFAVGVVVLVLILIENIFRTNPIQTNRKRYWKKAIQEYYNKNDFEGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67581
Sequence Length: 601
Subcellular Location: Membrane
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Q6BW46 | MISYTYITALSILVLNVLNVACTSVDDWPNLSPQIEIALRSQRDIGKYISIDQVTGMGVSLNTLVFDKDGYTLDALNDVSTLLDVGVQTLMINLYWNEFTQKWQLCPAPFPANISSDITTSKELYWDGRTYKCEASLTVDSLVRTINTYLAETNTNIKVNMVHLLFHLKSIRIDPPSGNVSSSEIKDYISTFQPTDSHFVALNNATLNDTVSSFGTSLFTPSDLSSYRKSNYRKGDKVGFYNETRKSFPNLNTFLLLDYKRVMTTVIANDLVKSQYTYNVTSSDKKSVFLEGSGVDTTVASLSDPDAVSQCNELIHYNQDNIEVFDNISLKEHFRIVVDDNGTSFTNVTFSDFVRCGFSPILNASYYNVYNDEEGVSEIDGSLSDIVDNFIPLSFWSWAENQLIEPNRGLNISDSTDTDNDEERDDNDNDDPLVRRDMDYKSSHTAFKCVVLDENGWKVSDCYSRQPIACQKSGSPNDWHIDVKTKREYFTAYKDDSCPDDYNFGIPSSSIEMLALMSYIERENISYPVWIDMNDITVPDCFVTGGPYATCPYQMTVTRLKLAGLIAPSFIVAVVILALILCEKIFRTNPIQSNRKRHWKKAINKYVEKYDYEGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69783
Sequence Length: 617
Subcellular Location: Membrane
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Q6CN26 | MLLYFLVVAPLWMLSGLVRAEVWPSFSDEMIYAIRSQRDLMQNISIDQVPLPGLALKNSLPGSITSNETESLTTILSLLHHGIQSFRVDLTFNSSAGEWFLEGTNIRFVKMLNTVNLFVMATNTNLDANILTILLRFDNDTLRNSNAIKEANFTAILEEGLSPGYVYSIADLERDRELNQTLSINGYSDTGWVGLSRFLFDVKKRVVFGFLNGAELFSEDDQDNLVFPPETFHYVTANNITCPLNTVEDIMRVSQIQWRFLEGNFSYENYLHYLECGYSLILTNPIDTRNDSSQGTSLQRHLSSLLLWSWNATAPDDKLDESEDSDDSESSSTSQYVAYRCGAFSYNDYEDLDPFKIGNCYRNLPYLCRFSDRAYFWNISEDTGTYFESDDKDMCPTGYKFGVPRTPLQQRSLRIHLNDMDIDNLDFWIDINSISVSNCWITGGPYASCPYQKYGSRRNYIAMTVPTSAIALVLLLVIFYFNWVHVPIQDNRNNWKRIINAYSKEEVEGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58593
Sequence Length: 512
Subcellular Location: Membrane
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C4QYK3 | MIIAFFLLIQCVYCVIWPPLSVDNEVALRSQRDVSYNVSVDQLVDVGVRLSTVIFERDTYTQPYLNRVDNLLNASVGNILIDAYWDEGGFNWQLCPAPFSANVTPIADGSTILQLEWDNKQYTCDRRLDLASIFTRIDEHIRASARSVSLNLITIYMSLHSIGTQNPTPVSQPGTLSRPLVRSIDQVQILTPASLRVAQLSNSTYQGLEFDPNGYPILGELLQSRGIRVIPIILENNMYEDTSYELERDSNLYFIQNSTIDVTQTNTADTKLTDLTTNITNWTIADSQALLSESFRLVMETEEDPFSLESYTNHISHGYSPFLNRKYNESEIRQFAVNRLWSWKNSYLPEVSVPLLGDQDDSNSANETLQCASFSNLSWIISSCDEPRQVACRNSSYWLQWTVTSTLSNYYGATEACPVGTFFDIPRTPLDSMTLQREIPLNSSVWIDLNTLDSGGCWISGGAEAECPYHRVTLVSLYVEILTPSSVVSIVLIAIVVLLHFVRIPIQKNRKYWRKLQDNIKDSDGIPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59673
Sequence Length: 528
Subcellular Location: Membrane
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C5DDK8 | MNRVVYGLLLTLVLNVVRGQSFWPALSSDSLIALRSQRDVLSNISIDKVPMVGVQLNEVAFRGTSNETESLEILASLLNVGVQAYMMDIEFDESYNLTISGSDTSLGTTLSTFKRFISSSNNYLNADMLVLLLRLKQNTNTSTKGAPSNFPNITAILDLYLGSSTLYTPSQLAYDRSSGNVAPSYGNLNSPDWPSLNYFLYSIQKRAVVFYVDTASSDALQSPAIFNASNLNYETSNTPIVCPLTNNAQVLNTSSLSWRFLQKDYSPSDIREYTMCGYSPIIDNKYNPNSINTISNVLENSLLWSWASNEPNTSDDTRSNSTSLVARRCAVVHYTKSNSSSYWTVANCYDRKRALCKRDGNDFEWAVTQEGASYFSHHDQDGNGFCPDNFSLSLPQTALQEKSLDNYLSQLSPEGWEIWIDLNSVSVPDCWVPDGPYASCPYQKEVSTRNFVSMITPVSVFAAVTILMLIMLSWRRVPIQDNRKRWKRVINSHLGSKAEGVPA | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56101
Sequence Length: 503
Subcellular Location: Membrane
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A5DZQ4 | MFNLIKIFFLVSLLSKWVFCDESNNSNYNTNTSNTTSNTTSSSISASTINITESINTDVINVAVRTQRDVSKPIPIDQVGVAGISLNSVFDNQGYTADSLAELTNLLQLGTQVVLLTLYWNEFTSVWQLCPAPFPQNVTYYLNSLVNVTWNNNTYLCEYGFTTNDIMDTIFEYLQSSNTVFNVYFMHLLLNLKSIHYEKSNKTIDLENIYAPNSRTNIIGNTTLYDTVAPLSPYIFTPDVLESYQNSEANSTQSNYQQFYAQSNYTFPSLDSVLFLEVKRLLVNVVNNDLVDSRRVYSITLRDRSNIFFNNTMPSTTLDTAEADAFCDRVLNSANDIETFNNLSLYTHFRYVTDNNKKRFTMKGVRRYVKCGLSPVFNASSYQVTNDSFAQTSNQSYYPTANESLLDVEVAFEAFIPYNFWSFAPGQPIMNETTRGNVLSSDANVAYKCVAMNPDGWTVEDCYTEYQYACKNITSPNDWFISTRSRRSYFDIDNDACPDGYNFSLPRLSIEMAALYNVIKKENAEYPVWIDLNDITISTCFVSGGPYAQCPYQKTVTTKKFIRMIAPSSIVALVILFLIFLENLFRKNQLQTNRKKYWKKVLSEHYAKHEQEGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70317
Sequence Length: 616
Subcellular Location: Membrane
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A5DGH6 | MLLFLVCFVCNIWSVFGVQAASNVSDVVNTIVVASRTQRDISMLVPIGQTNNMGVSLNTVLFEKVGYNSSSLDYIRQLLDGGLQTWMLDLYYNNATSNWQLCPAPFPQNSSTNAYETRTVRWNNRDYHCQPSFTLDSVMQEFRSYFMSTNTNIAVNLIQIMFNLYDFDFSESKNKTIASKELKNYATFSNYGNSTLNSSLSSVSDMLYTPQDLTTYQKTQSGTGISAFYNTSAFDFPSSQTFLLNDYKRLITYVAENKVPKSALGSNDENTIFFNEDFADISYTSDESLLERCGSRTLSDFNQLSLNSNFRTVVDNENVPFTPSSFRKYVTCGYSPILNASRYSIPNKPATTDISDILTYYFPRSYWSWAPGQPHDRQHTANTSSFDKRDYKSSDNQMARKCVTLQESGFVLSNCYEEHKFACQKFNSPNEWKISVSSDTYFSDDYGDCPEGYSFNVPQSSIEVDSLRQEVANSGEKYPIWVDLNDITVANCFVTGGPYAQCPYQRTVSGRRLVELIAPSFVVASVIVVLIFIEKIFRVNPVQTNRKRYWRRAINEYNKQHGYEGVPS | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 64643
Sequence Length: 568
Subcellular Location: Membrane
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A7TEV4 | MIVMQLQQQLLIWVIFWLNYATALTNFTWSSDSPSMVYALRAQRDVMSSATIDQLPLVGVDVGRVFINGMVIENKDEDEEDEDLLVMLESLLEAGVQALSVDVEYKDEIWVVGNSTIAFDDFLLTVRDFLDGTNTDLSANILMVMLRIQPNSSDYGSPSTFNNYTHGYNYSDISDYNKDDIGDASDIEALIYSNIGRSYIYSPEDLVDDRNKSYTSDIYGLNSVNGWPTLSHFLYQKRKRVLFTELTTEMPYNTSSLLFNKTILHLDGGNIAISCPTSNSELTELSLVAWRFIENEFTDDSVRSYVDCGYSPIIANKYNQNNITHLLNLTQSALLWSWEVGQPSTNEKKNSDTLEAYNCVSFVYTANNYSAYWKVENCYDEKKGLCEAKTDLFSYIVSENVDSYFNFDSFDGSNCPDGFDFSIPKTPLEQLAVINYLRLRNSSDTEIWIDLNSISVNNCWVTGGPYATCPYETVMSRRNFTKMITPASITSFGLLVLVTCLNLLSLPIHDNRSNWRRMINKLSRNEFDGVPA | Function: May be involved in telomere capping.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60421
Sequence Length: 532
Subcellular Location: Membrane
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P44890 | MKKTKRIFTALSHLFSPKWWKKNWQRVVFCFFFAVFALLLIFRFVPIPFSAYMVQQKIANLLQGDFRYQIQYNWVSLENISPNIQLAVISSEDQRFLEHLGFDFEAIQRAIRYNEKSNKGIRGASTISQQTAKNLMLWHGQNWLRKGLEVPATMLLELTWSKKRILEVYLNIAEFGNGIFGVEAASRYYFKKSAKNLSQNEAALLAAVLPNPIIYKVNKPSLLVRKKQTWILRQMGNLGTEYLSHL | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28700
Sequence Length: 246
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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A6T2A4 | MKILRKLLFWLIVVPVLLVLLLQLYFFLQIGWWVNHNPGSTSFMRHQLSILQEKNPKAQLKHKWIPYNRISNNLKRAIIASEDSNFSEHEGVDWDALQKAYEKNIKKGKVVAGGSTITQQLAKNLFLSGDRSYLRKGQEVIITYMLEYWMDKERIFEIYLNVVEWGVGIFGAEAAAQHYYGVSAAQLGAPQAARLAVMLPNPRFYDGHRGTAYLARRTDLILRRMNSAALP | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26550
Sequence Length: 231
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q28VR9 | MAKRARKSKKNVSRARLLAQAMRRWLLRGMFGLGALMLVWIVAYAVVPVPTTIYMQQERARLGGIERDWVPMDQIAPVLARSVVAAEDANFCLHWGFDMTAIRDAIADGAARGGSTISQQTVKNAFLWHGRSWVRKALEAAITPVMELVWPKRRVLEVYLNVAEFAPGVFGAEAGAQHHFGVSAADLTARQASLMAAVLPNPQRRDAGSPSDLVNRRARSIADGAALIRADGRADCFAN | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26160
Sequence Length: 239
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q48465 | MTFRFSARCRLIKRFLLRLLLACAVLWGGGVALFSIVPVPFSAVMLERQLGAWLSGNFHYIAHSDWVGMDEISPWMGLAVIAAEDQKFPEHWGFDVPAIEKALAHNERNENRIRGASTLSQQTAKNLFLWDGRSWLRKGLEAGLTVGIETVWSKKRILTVYLNIAEFGEGTFGVEAASQRYFHKPASRLTAAEAALLAAVLPNPIRFRADAPSGYIRSRQAWILRQMRQLGGEGFMRANQLH | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27197
Sequence Length: 242
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q65S86 | MRLKTLKFPFVNKKNTRTFKKKCGRFLSYFIGLTVALTFLFRFVPIPFSAYMAEQKLAHIIQLDFDYKVNYDWISLEDISPYMQLAVIAAEDQNFPNHGGFDWNAIKSAIKYNEKSSRIRGASTISQQTAKNMFLWHGQSWIRKGIEVPVTFMLETLWSKKRILEVYLNIAEFGNGIFGVEAASRYYFKKPAKRLTQSEAALLAAVLPNPIIYKANRPSLLVRKKQAWIIRQMNSLGLNYLKKL | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28292
Sequence Length: 244
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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B5YKP5 | MHNKQQVKIGIIGGSGLSESEAKKEIITIKTPYGEPSCPYEIEKIDDIEVLFLRRHGQKHSIPPHKVNYRANIYGFKNFGIERIFGVFATGSLTENIPPGSIVIPNQIIDFTQGMRANTFYEEKKVVHIDFTEPFCSEIRHYLLETARKIGINVISHATYICVNGPRLETAAEIKFFKNIGADIIGMTIMPEASLAREVEICYAAVAVVANYAAGISKFPLTVKEVIETMEDSLDAVGFLIKETIKKLPEERKCLCKHALKNASF | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 29620
Sequence Length: 265
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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Q8PB40 | MSSNSIALAVIGGTGVYKLAQLDQVQTHEVDTPYGAPSGPIRVGMLLGHRVAFLARHGEGHSLPPHKVNYRANIAALQQIGATRVLALNTVGGITDSFGPRVLACPDQLIDYTWGRISTFCEEAGSEVQHVDFGHPYSPMFRSKVIAAAKVTGVTLVAGGCYGATQGPRLETIAEIARMRRDGCDLVGMTGMPEAALAREKGLEYACLAIVANWAAGCGDAQEITMAEVLSNVDAASSGLPELIGELARG | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26216
Sequence Length: 250
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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P25238 | MDNHANEINKLSRELGLLSNYEFNMDELKNLSPLDSTSSSIYIGDNLTYLQGLSKTSPKTIDFCYIDPPYNTGNKIIYHDNRKSVSSDIFGLHNEWMSFLLPRLFHAHKMLKDTGIIAISIDDYEFAHLKILMDKIFGEDNFIGNIVVCRSKNGKGSKRNIASAHEYLLVYGKSDMAELSGQPDDKSLYDKVDCFGEYRIDGMFRKKGDSSLRTDRPNMFYPLYFNPSTGEVQVEPELGLKTVYPIDSKGIERRWLWSKETARERSWELFASKNGVVYVKNYSSSHKRIKVRTLWNDSSFYTERATNEITKIFGSKVFDTPKALNYIMSIINCMAKPDALILDFFAGSGTTAHAAAVLNSLDGGSRKTILMESNHPITKTHIAYKSGFRKISDITISRLNYVSDNFPDFKYKKIEII | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-GGTACC-3', methylates A-4 on both strands, and protects the DNA from cleavage by the KpnI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47577
Sequence Length: 417
EC: 2.1.1.72
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Q7XR61 | MAAAAEQQQQQQQQGFRPLDEASLVAYIKATPALAARLGGSLDALTIKEVGDGNLNFVYIVLSDAGSVVIKQALPYIRCVGDSWPMTRERAYFEASALQKHRGLCPDHVPEVYHFDRAMSLIGMRYIEPPHIILRKGLIAGVEYPLLAEHMADYMAKTLFFTSLLYNSTTDHKKGVAQYCDNVEMCRLTEQVVFSDPYMLAKYNRCTSPFLDNDAAAVREDAELKLEIAELKSMFIERAQALLHGDLHTGSIMVTPDSTQVIDPEFAFYGPMGYDIGAFLGNLILAYFSQDGHADQANDRKAYKKWILKTIEDSWNLFHKKFVELWNKHKDGNGEAYLPPIYNSSELLCLAQKKYMTSLFHDSLGFGSAKMIRRIVGIAHVEDFESIEDASKRASCERRALNCAKAILKGRRQFESIGQVIVHVQSFDRD | Function: Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
Catalytic Activity: 5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 48413
Sequence Length: 430
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 2/2.
EC: 2.7.1.100
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P53594 | MDVHEYQAKELLASFGVAVPKGAVAFSPDQAVYAATELGGSFWAVKAQIHAGARGKAGGIKLCRTYNEVRDAARDLLGKRLVTLQTGPEGKPVQRVYVETADPFERELYLGYVLDRKAERVRVIASQRGGMDIEEIAAKEPEALIQVVVEPAVGLQQFQAREIAFQLGLNIKQVSAAVKTIMNAYRAFRDCDGTMLEINPLVVTKDDRVLALDAKMSFDDNALFRRRNIADMHDPSQGDPREAQAAEHNLSYIGLEGEIGCIVNGAGLAMATMDMIKHAGGEPANFLDVGGGASPDRVATAFRLVLSDRNVKAILVNIFAGINRCDWVAEGVVKAAREVKIDVPLIVRLAGTNVDEGKKILAESGLDLITADTLTEAARKAVEACHGAKH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: (S)-malate + ATP + CoA = (S)-malyl-CoA + ADP + phosphate
Sequence Mass (Da): 42074
Sequence Length: 390
Pathway: One-carbon metabolism; formaldehyde assimilation via serine pathway.
EC: 6.2.1.9
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P53595 | MSILIDEKTPILVQGITGDKGTFHAKEMIAYGSNVVGGVTPGKGGKTHCGVPVFNTVKEAVEATGATTSITFVAPPFAADAIMEAADAGLKLVCSITDGIPAQDMMRVKRYLRRYPKEKRTMVVGPNCAGIISPGKSMLGIMPGHIYLPGKVGVISRSGTLGYEAAAQMKELGIGISTSVGIGGDPINGSSFLDHLALFEQDPETEAVLMIGEIGGPQEAEASAWIKENFSKPVIGFVAGLTAPKGRRMGHAGAIISATGDSAAEKAEIMRSYGLTVAPDPGSFGSTVADVLARAA | Catalytic Activity: (S)-malate + ATP + CoA = (S)-malyl-CoA + ADP + phosphate
Sequence Mass (Da): 30519
Sequence Length: 296
Pathway: One-carbon metabolism; formaldehyde assimilation via serine pathway.
EC: 6.2.1.9
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Q9C6D2 | MSFEEFTPLNEKSLVDYIKSTPALSSKIGADKSDDDLVIKEVGDGNLNFVFIVVGSSGSLVIKQALPYIRCIGESWPMTKERAYFEATTLRKHGNLSPDHVPEVYHFDRTMALIGMRYLEPPHIILRKGLIAGIEYPFLADHMSDYMAKTLFFTSLLYHDTTEHRRAVTEFCGNVELCRLTEQVVFSDPYRVSTFNRWTSPYLDDDAKAVREDSALKLEIAELKSMFCERAQALIHGDLHTGSVMVTQDSTQVIDPEFSFYGPMGFDIGAYLGNLILAFFAQDGHATQENDRKEYKQWILRTIEQTWNLFNKRFIALWDQNKDGPGEAYLADIYNNTEVLKFVQENYMRNLLHDSLGFGAAKMIRRIVGVAHVEDFESIEEDKRRAICERSALEFAKMLLKERRKFKSIGEVVSAIQQQS | Function: Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate in the methionine cycle. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis.
Catalytic Activity: 5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 48071
Sequence Length: 420
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 2/2.
EC: 2.7.1.100
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O42662 | MPIYILIERSVKNGRIDFWNEDAIRTLGKAILDRDYSLRVEFPENRLCPMVPNRATYIRYIHDLLSSTSGQKDKKRIIGLDIGTGASCIYPLLGCRMYSYDFVGTEIDKFSFETAKSNILQNNMESQIKIVLRSKQDCLLPDTEGMEEFTFVMCNPPFYEHEEDFINFKQNPPSGVCTGVYHEMVTEGGEVGFANKILTESKKRKGIQWYTCMFGKKSSVPAVVDKLREQNISNYGIYELALGKTKRWIICWSFQAMRPHNELIRPSSTSLSKYFPHKVLQNWTLDPELCAQIDDILQKFLDDNKIPWSKKGSVLEISTKSITWSRKARRISKSQTSVSSLEGQMKCELNVIDNQLQCKWIEGYDYNVYESFCSALARALRDNKK | Function: RNA N6-methyltransferase that mediates N6-methylation of adenine of U6 small nuclear RNA (U6 snRNA).
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 44422
Sequence Length: 385
Subcellular Location: Cytoplasm
EC: 2.1.1.346
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P35516 | MRYLGNKTNLLNFIQQVIKKHDIQGQTFADLFAGTGSVGDYFKGEYTVLSNDYMYFSKVISEAKLLNSEKPKFDSFVKRYGKTPFQWLNEREYTPNDGYFVYNNYTPRAERMYLTEENALKIDGMRLDIEELFQEGVISKAEYSYLLASLLESVTKVSNTSGTYQAFFKFWESRALKKFTIMPLEMKDSLSVSKDNRCFNKNTNRLVREISGDIAYIDPPYTITQYTNSYHVLETIARYDNPELFGKTGRRVKREFSGYSNKSKAYYEFEDLFRQINFTHVLVSYSNQSIVPLDELVDLARRFAVDGIVEVETNEYREYSTNNSSMKGEGKKLQEVIIYFKKNLETNKSPLNYAGSKDDVIPRIFKLLPKHVTTFVDAMGGAFNVGANRTALNKVVYNEYHPFVFEMMQMIVNTPADELIRNVEQIVTRYSLEKKGKEAFNRLRDHYNNEEQTPINLYTLNIYSFQNILRFNQAKKYNTPIGNNEFNEGYKDRITRFVTRAPEVEMRLGSYSAINFNEYDDDTVFYFDPPYLVTTAGYNDGKRGFDGWDAEQEASLLKYLTELDSAGKKFMLSNVLEHKGKTNHLLMEWIQHHGFNVNTIGETGIKYPRREILVTNYNTFER | Function: An alpha subtype methylase that modifies unknown specific adenine residues, and protects the DNA from cleavage by the LlaI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 72513
Sequence Length: 622
EC: 2.1.1.72
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P53214 | MASCNPTRKKSSASSLSMWRTILMALTTLPLSVLSQELVPANSTTSSTAPSITSLSAVESFTSSTDATSSASLSTPSIASVSFTSFPQSSSLLTLSSTLSSELSSSSMQVSSSSTSSSSSEVTSSSSSSSISPSSSSSTIISSSSSLPTFTVASTSSTVASSTLSTSSSLVISTSSSTFTFSSESSSSLISSSISTSVSTSSVYVPSSSTSSPPSSSSELTSSSYSSSSSSSTLFSYSSSFSSSSSSSSSSSSSSSSSSSSSSSYFTLSTSSSSSIYSSSSYPSFSSSSSSNPTSSITSTSASSSITPASEYSNLAKTITSIIEGQTILSNYYTTITYSPTASASSGKNSHHSGLSKKNRNIIIGCVVGIGAPLILILLILIYMFCVQPKKTDFIDSDGKIVTAYRSNIFTKIWYFLLGKKIGETERFSSDSPIGSNNIQNFGDIDPEDILNNDNPYTPKHTNVEGYDDDDDDDANDENLSSNFHNRGIDDQYSPTKSASYSMSNSNSQDYNDADEVMHDENIHRVYDDSEASIDENYYTKPNNGLNITNY | Function: Involved in cell integrity signaling during vegetative growth at elevated temperature. Acts positively on the PKC1-MAPK pathway. Cell membrane sensor of oxidative stress in the cell integrity pathway upstream of PKC1. Required to transmit the oxidative signal to SLT2 and to restore the correct actin organization following oxidative stress. Multicopy suppressor of 1,3-beta-glucan synthase (GS) mutation. Also suppresses RGD1 null mutations.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 57528
Sequence Length: 551
Subcellular Location: Membrane
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P50179 | MNLLQKNKINLRPFTKWTGGKRQLLPHIQYLMPEKYNHFFEPFIGGGALFFELAPQKAVINDFNSELINCYRQMKDNPEQLIELLTNHQRENSKEYYLDLRSSDRDGRIDKMSEVERAARIMYMLRVDFNGLYRVNSKNQFNVPYGRYKNPKIVDKELIESISEYLNNNSIKIMSGDFEKAVKEAQDGDFVYFDPPYIPLSETSAFTSYTHEGFSYEDQVRLRDCFKQLDSKGVFVMLSNSSSPLAEELYKDFNIHKIEATRTNGAKSSSRGKITEIIVTNYGN | Function: An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the LlaDCHI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33078
Sequence Length: 284
EC: 2.1.1.72
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Q5F452 | MEHITTPKVENVKLLDRYTNRKAASGTLYLTATHLIYVDASAEVRKETWILHHHIATVEKLPLTTAGCPLLIHCKNFHVAHFVIGQERDCHEVYTSLLKLSQPVKPEELYAFSYNPKMSKDNREIGWKLIDLKVDYQRMGIPNDYWEITDLNKDYEVCNTYPPEIVVPRAASKATVIGSSRFRSRGRIPVLSYLYKENNAAICRCSQPLSGFSARCLEDEQMLQAIREANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYDNIRFKFIGIENIHVMRSSLQKLLEVCETKSPSMSDFLTGLENSGWLRHIKAVMDASVFLAKAVKDEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRAFKGFMVLIEKEWIAMGHKFSHRCGHLDGDPKEVSPVFTQFIECVWQLMQQFPCTFEFNEHFLLEIHDHVYSCQFGNFLGTCHKEREDLKIFEKTHSLWPFLLQKKQELRNPLYRGFTAYKELQPNTLPFSFQFWCGMYNRFDKGMHPKQCVLDHLLSCMNQKIKLEDNASELENKLPFLDGPLPNEACFLSKVGCAASKTPMLNTPQDYEGEAPPVLTNGISVGDINVTSDVDQRNKENLANHRDLHLNDSVDVLNSEAKDGKPQHH | Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (By similarity). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
Sequence Mass (Da): 71967
Sequence Length: 629
Subcellular Location: Nucleus envelope
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Q96EF0 | MDHITVPKVENVKLVDRYVSKKPANGILYLTATHLIYVEASGAARKETWIALHHIATVEKLPITSLGCPLTLRCKNFRVAHFVLDSDLVCHEVYISLLKLSQPALPEDLYAFSYNPKSSKEMRESGWKLIDPISDFGRMGIPNRNWTITDANRNYEICSTYPPEIVVPKSVTLGTVVGSSKFRSKERVPVLSYLYKENNAAICRCSQPLSGFYTRCVDDELLLEAISQTNPGSQFMYVVDTRPKLNAMANRAAGKGYENEDNYANIRFRFMGIENIHVMRSSLQKLLEVCELKTPTMSEFLSGLESSGWLRHIKAIMDAGIFITKAVKVEKASVLVHCSDGWDRTAQVCSVASILLDPFYRTFKGLMILIEKEWISMGHKFSQRCGHLDGDSKEVSPIFTQFLDCIWQLMEQFPCAFEFNENFLLEIHDHVFSCQFGNFLGNCQKDREDLRVYEKTHSVWPFLVQRKPDFRNPLYKGFTMYGVLNPSTVPYNIQFWCGMYNRFDKGLQPKQSMLESLLEIKKQRAMLETDVHELEKKLKVRDEPPEEICTCSQLGNILSQHLGSPLTNPLGFMGINGDLNTLMENGTLSREGGLRAQMDQVKSQGADLHHNCCEIVGSLRAINISGDVGISEAMGISGDMCTFEATGFSKDLGICGAMDISEATGISGNLGISEARGFSGDMGILGDTGISKASTKEADYSKHQ | Function: Phosphatase that acts on lipids with a phosphoinositol headgroup . Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate . In complex with MTMR9, negatively regulates autophagy .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
Sequence Mass (Da): 78919
Sequence Length: 704
Subcellular Location: Nucleus envelope
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