ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O19914 | MILIIDNYDSFSYNLVQSVGEINSDLIVLRSDEIDVSKLQNLNIKHIIISPGPGHPDEYTICKQVVKFFAPYTPILGICLGHQIIATCYNASIKKSSPVFHGRASKIYCLKDKLFLGIHAPFTAARYHSLVVDQDKRGLDLTTCLKTIAITREGVIMACKHRYYHFTYGIQFHPESMLTIQGTKLLKNFLSLSYG | Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 21985
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subcellular Location: Plastid
EC: 4.1.3.27
|
P48261 | MILLIDNYDSFTYNLAQYLSELNIKVLVKRNDKITLDEIKNLNIQGIIISPCPGGPEDSGISQGIIKYLGNQIPILGVCLGHQTIGHVFGGKIIKAPKLIHGKPSIIFHDGKGVFQNLKNPITATRYHSLIIEKESCPDELEITAWTEDGLIMGIQHKKYKQLQGIQFHPESILTESGKQILQNFINCLN | Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 21202
Sequence Length: 190
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subcellular Location: Plastid
EC: 4.1.3.27
|
P71381 | MANILFLDNFDSFTYNLVDQFRVLGHNVTIYRNDCDLEKLVETALNTPDTILALSPGPGTPSEAGILLPLIERLKNQVPIIGVCLGHQALIQAFGGKVVHAGEVLHGKVSRISHDNEAMFKDLANPMPVARYHSLMGQDLPKEFIVNAEYNGIIMAIRHRDLPICAFQFHPESILTVQGSQLLQQSIEWLLNR | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
Q9HPG6 | MNVVVVDNYDSFTYNLVEYLSAQPRDDHAPDVTVLKNTASLAAVRAADPDAVVISPGPGHPDTPRDVGVTTDVLRAVSPRVPTLGVCLGMEAAVHEYGGTVGRAAEPMHGKTTPVSHDETGIFADIQQDFPAARYHSLVCTSIPSCFAVTATTRDGSLPMAIRHRDHPLACVQFHPESVLTGVGHDVIGNFLDAAAAH | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
P33974 | MIRLVVVDNFDSFTYNLVEYFSEQTVEGEPLDIEVRKNTASLDEIRDLDPDAIVISPGPGHPKNDRDVGVTNDVLTELSTEIPTLGVCLGLEAAVYAYGGTIGHAPEPIHGKAFPVDHDGAGVFAGLEDGFPAGRYHSLVATDVPDCFDVSATTDHDGEALVMGVRHRDYPIECVQFHPESVLTGSGHGVVRNFLTAVAGFDVA | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
O25868 | MKIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMDLMNEESKTPLLFISPGPGNPNSSGNLLKIIAMAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKATAIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMTLQGRALLEQSVGFLEGLL | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
Q02003 | MILIIDNYDSFTYNLVQYVGVLTDVAVVKNDDDSLGNMAEKADALIFSPGPGWPADAGKMETLIQQFAGQKPILGICLGFQAIVEVFGGKLRLAHQVMHGKNSQVRQTSGNLIFNHLPSKFLVMRYHSIVMDEAVALPDFAITAVATDDGEIMAIENEKEQIYGLQFHPESIGTLDGMTMIENFVNQVNENKESSNEK | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
P20441 | MKVLILDNYDSFTFNLYQIVGEILEEREKPFQLDVIRNDEKPFEWIKSANYDKIIISPGPGHPADPAYFGVSADILKELGKTPPVLGICLGMQGMATVFGGEVVRANIAMHGKLSPIEHDGKGVFSGLTQGIEIMRYHSLVAKEISLPNDLEITARVSAGEGKGEIMGLRHKSLKIEGVQFHPESFGSEEGKCLLRNFINS | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
Q57690 | MEVKKVLVIDNIDSFVWNLVQYVGTLGYKVKLVDNKITLDEIKKINPDRIIISPGPKTPKEAGNCIKIIQEVDIPILGVCLGHQCIVEAFGGEVGRAKRVMHGKASLINHDGEGIFKDIPNPFYGGRYHSLIAKEVPKELKITAKSLDDNYIMGVRHKKLPIEGVQFHPESILTESDNLKFPDLGLKLIKNFVESEY | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
P11596 | MKMDADSSGTQHRDSRGSRSRSRREREYHGRSSERDSRKKEHKIPYFADEVREQDRLRRLRQRAHQSTRRTRSRSRSQSSIRESRHRRHRQRSRSRNRSRSRSSERKRRQRSRSRSSERRRRQRSPHRYNPPPKIINYYVQVPPQDFYGMSGMQQSFGYQRLPRPPPFPPAPYRYRQRPPFIGVPRFGYRNAGRPPY | Function: Member of the regulatory pathway controlling female somatic sexual differentiation, regulated by Sxl. Activates dsx female-specific splicing by promoting the formation of a splicing enhancer complex which consists of tra, tra2 and sr proteins. Together with tra-2, plays a role in switching fru splicing from t... |
Q0C8A2 | MSPTREDLVATAKLFIAKYNEFTPESIISVRTPNSVSHRLFPTRNATRNIGESMEACANAKEVFKSLTVSVIDDNDTIVDERTRKVVFYLASRGDTIVGEWKSECIFIFQMSEDGKLVDRIWAGFDTAYMDEFESRLDGITF | Function: Isomerase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-DMOA by the polypreny... |
Q0C8A7 | MPSIISDPQAYDIMLRLLQFSCWSLSYINTVRTTLSDQLPSVSFMSICCDVAWEFVYAFVYPIASSHWAGGIRIWFAMHCVMLFIVAKYAPNDWDHVPLMKRFARLAYVAITIGFMAGHLALASEIGPALGFFWSGALCQITASLGSLCLLVCRGSTRGASIKTCPLCWFYIAITLTLDAIYPVFFFYFRAIEHPKKDSERKVE | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-DMOA by the pol... |
Q0C8A1 | MLEPVSTAQSLWSFGLWILVILSPVLFFASRELGILNAKKRFAKNGFEEVLAGLRKSDVFGLMTINGPKIVLAPKFAQEIRSNPALSVSAFSSSELHAHIRGFDVFRQGEADDILQDTVRSKITQSIGDLIQPLSEECSLTLKPKWTDSPEWHEVCPHTTILDIIARLSSRAFIGDELCRNPKWLRLTVDFTVDSFRAAEALNWWPYALRPLVARFLPSCLKLHKYIQDADNMMKPVLESRRQAQAKDPQKSYPDTIQWFEETAQGRPYDPVRLQLTLAFASIHTTADLVIQTILDLCSAKNWDELCRSLREEIISSFRE... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-D... |
Q0C8A0 | MTGQAEAIRRVHPTVSPKQAAQMLQEDGVIILKSFLAPDVMQRFQAEVDEDVEKTSTGARMKAYKLVNDKTKHMADLIVRSEVFRSDILTHPLYHAIADELFRADYGDHWLNASAVLQLMPGAPAQQLHRDEEIFAASKFRSPTDPQLSLSCLVALTEFTEENGATRLIPGSHLWDSAHPAPSPDQTVPAIMQPGEAILFLGSLFHGGGENRTENVRRGLGMSLIPCQFTPYSSHMHVPRTIIETMTPLAQKLVGWRTVESHRQYPFWQGGDRRLEDVLGLASREA | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-DMOA by the polypre... |
Q0C899 | MSVYRLFTVSIMDMCVLKANCKDPLGFTVEYTCVFGISSPIPGLHGGEHVNSYGEGVCVITFHNKDGRVFWFIIEKLPKKYTYPISPRFTPQDASEFCGRLADVHVFNDVTVGHLWRNRTVVSMNALEEGLLSTWSFERMVLLGDSVHKMTPNIGQGANTAIEDAAALASLIHQMINPMTPQNASKAAIGHLFQKFQDLRMSRVQSTVQRAHFGARFHTRDDHLKALVGRYIFPYVGNLVMARTVKVIGGGHKIEFLPPPKRSMPWTAQTDHSQHKMHGSKVLWAYLSHPDQHWSDDPRGTAQLRSQSLGTHRTSTVGRT... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-DMO... |
Q0C898 | MALDQGAKVFGVDIAASPAPLANHPNYKFLKADLCDKQTPKDVVQACVKMFGGRIDGLLNIAGIMDSNQSVDSVSDEMWDRCIAVNLTAPIRLMREVIAIMREQKSGNIVNVASKAATSGAVSGVAYTASKHGLVGATKNVAWRFKHDNIRCNAVCPGGVVGTGVHNEMDIQKWDKEAMKTMFLIHQSHSCDKDKGIGLRAEDIARPLLFLVSDRSKGINGAILPIDNAWSTI | Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 . DMOA is then prenylated into farnesyl-DMOA ... |
A0A2N6JFX7 | MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP | Function: Involved in the degradation of triuret (carbonyldiurea), an impurity in agricultural urea fertilizer, and an intermediate of uric acid oxidation endogenously found in human urine and in prokaryotic metabolism. Catalyzes the hydrolysis of triuret to 1-carboxybiuret and ammonia. The product, carboxybiuret, chan... |
Q814C2 | MDRIKCTVAYDGMHFCGYQIQPNHRTVQQEIEKALQKLHKGELVRVQASGRTDSTVHAKGQVIHFDTPLSLEEWQWSNALNTMLPDDIVIRQVEKKTEEFHARYGVEKKEYRYRVLLSKTADVFRRNYVYQYPYPLEINSIRKAIPYFIGTHDFTSFCSAKTDKKDKVRTIYEIELIEQDDEIIFRFVGNGFLYNMVRIIVGTLLSVGQGKLDPDSIPEILAKQNRQFAGKMAPGHGLYLWEVNYNN | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28787
Sequence Length: 247
EC: 5.4.99.12
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Q8KDR7 | MARSKRTIKMQIEYDGTGYSGWQRQPGDVVTVQGEIERVLERIMQEPVSIDGAGRTDSGVHARRQVASFATCSPMPLGRLIYSANSLLPSTIRINAMRQAPESFHARFSATSREYRYFLLEHPSAIDSRFAGCSHGKPDVGAMNRLALMLIGTHDFAAFSKETPDQYGTLCTVTAARWYRSGRFHVFRIEANRFLRSMVRFLVAGMIEVGMGRLEEGAFARMLESGHRPPKLKPADAAGLFLWKVRY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27738
Sequence Length: 247
EC: 5.4.99.12
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O84469 | MTKKIVLQIAYQGTSYSGWQYQPNALSIQEVLETILKKIAGFRISVISSGRTDAGVHAQGQIAHFHCPDHPHFTDPRQIQKMLNALLPHDIVIRDAVMTDEDFHSRFSAIAKEYRYTLSLLPKPLPHHRLFCFSPRYKLNIARMQEAAQYLVGTHDFASFANLGREYSSTIRTLYTLDLSEQEHLVTVICRGNGFLYKMVRNIVGALLDIGKGKYPPEHLLDMLATKDRRKGPPSAPPYGLSLHHVCYPPPYQWFCKHEHNNSSEGK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30427
Sequence Length: 267
EC: 5.4.99.12
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B5EFM8 | MRNIKLIIEYDGTAYCGWQVQPNGRTVQEVLQEALAAMLGEKTPLHGSGRTDAGVHARGMVACFKTDKAMPLRAFREGLNCLLPGDIAVREACEVPLEFHPRFDAHAKHYRYTILLDDLRSPLSRLTVWRLKGKLDIQAMRAACAAFVGEHDFAAFRASNCAAKTTVRRIYSMDLVQEGCLLHLDVKGSGFLKNMVRIITGTLIEVGQGKKSVEDVARLLQGGDRQQNSGMTVPPQGLCLMQVYYQEKCD | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27769
Sequence Length: 250
EC: 5.4.99.12
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A8ADR1 | MSAVEQPPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPVNVFCAGRTDAGVHGTGQVVHFETTALRKDAAWTLGVNANLPGDIAVRWVKAVPEDFHARFSATARRYRYIIYNHRLRPAILGHGVTHFYEPLDAERMHRAAQCLIGENDFTSFRAVQCQSRTPWRNVMHINVTRHGAYVVVDIKANAFVHHMVRNIVGSLMEVGAHNQPESWIAELLAAKDRRLSAATAKAEGLYLVAVDYPERFDLPKTPLGPLFLAD | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30333
Sequence Length: 270
EC: 5.4.99.12
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Q97EL1 | MKNVKLTLEYDGTNYCGWQKQKNVVTVQEEVEKIIGEITGEKIDVIGCSRTDSGVHAKAYTCNFKTNTVIPPEKFYLVLNSVLPDDIVALNSEEVPMDFHSRFDNKGKTYSYTILNRLQRAAIDRNYVYQYGHKLNCDLMREATKYILGTHDFTSFKSTGSKVKSNIRTIYEARIVEDENKVIFYVTGDGFLYNMVRIIVGTLLEVGEEKITPLNVKTIVESKDRTKAGRVVPAKGLCLEKVMY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27779
Sequence Length: 244
EC: 5.4.99.12
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Q6AD25 | MTDQATRFRLDIAYQGTDFAGWARQPDLRTVQGTLEEALATIFRCSGEPPSLTVAGRTDAGVHATGQVAHVDLSPEQVALLRRPHGKREPQLAHDALKRRVNGVLGPVPDVLVSRATEAPAGFDARFSALWRRYEYRVADRIALRDPLQRHRTAWVPNTLDVDAMDRGAHGMLGLHDFASYCKAREGATTIRTLQAFSWRRDAEGVLLGEVAADAFCHSMVRALVGACVEVGEGKLRPGDLVTLRDERQRTSAFKVMPARGLTLREVGYPVDAELGRRAEQTRGLRTL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31786
Sequence Length: 288
EC: 5.4.99.12
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B0SC03 | MPNYALLVEYDGTHFNGWQKQKNLPTVQSSIESALGIILRRNPASRLSVAGRTDTGVHALGMVCNFKTEHPIPNFHKLLVSLNALTPTGVSVKNVVEVPSDFHARFSCTGREYIYKLYYSKYESSFVEGRAFWVKGHIDWERVKKQLQVLVGEKDFRSFTKAKSMAGKRAVREILAIQLENLSPEWYQIRIRANGFMHNMVRITVGTLLDIGKGRWESRSIDSILEEKNRTQAGVTLPPDGLYFVRAYYEDHPEIHELYKIPLP | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30213
Sequence Length: 264
EC: 5.4.99.12
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Q8CXS6 | MIVNFKTQRVIQNFSKFLLSLNAITDSGLSILNMTEVDENFDSRFSCNSREYEYWILNTKYPRPTWKNRTFWYQHRIDVPRLEAELELLKGEHDFRSLAKVASLKGRSTVRTILDVKLERSLELEGLLKVKIRANGFLHNMIRILTGTLLEISNGKRKDTNVLEILSSKDRTIAGITLPPYGLYFIRAYYDSYPKIDFMYSHLDFLK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 24296
Sequence Length: 207
EC: 5.4.99.12
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B1W3X8 | MSDQAEPGFVRVRLDLSYDGKDFSGWAKQTSRRTVQGEIEDALRTVTRSSVTYDLTVAGRTDAGVHARGQVAHVDLPEAVWAEHEEKLLRRLAGRLPLDVRIWRAAPAPAGFNARFSALWRRYAYRVGDRPGGVDPLTRGHVLWHDRPLDLDAMNEAAALMVGEHDFAAYCKKREGATTIRTLQKLRWVRDPATGVLTATVQADAFCHNMVRALIGAALFVGDGRRPAAWPAEVLAAKVRDPGVHVVRPHGLTLEEVAYPADALLAARAAEARNVRTLPGAGCC | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31111
Sequence Length: 284
EC: 5.4.99.12
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B2FNZ6 | MRYALGVEYDGSDFRGWQNLGEGGPSVQASLEQALSSVADTPLQVVCAGRTDAGVHGQCQVVHFDTDVVRDPRAWMLGTTTRLPRSIAVRWCVPVADDFHARFSARARRYRYRLLNREVRPALDRQTLSWERRALDETLMHAAGQALIGENDFSAFRSVQCQALHARRELQSLQVSRQGEVIEVAVQGNAFLHHMVRNIVGSLILVGSGEKPVEWIAELLAGRDRTVAGPTAPPQGLVFLGPLYPDNWHLPAEVTL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28400
Sequence Length: 256
EC: 5.4.99.12
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Q3B200 | MEAEHTSTKGVPEAGEFLLLDKPLDWTSFDVVAKIRNTYKRGGLKRKVGHSGTLDPKATGLLILATGRKTKEIASLEGLDKEYLAVIKLGARTASHDVETPETDHTPAGHITLAMVRAAALAFVGPRLQQPPMHSASWHEGKRLYALARKGEEVKERKAKEIVIHQFEVTHMQGPLVYCRLLVSKGSYIRVIADELGMALGVGAYLAGLRRTAVGPYRVEDAMSVEDARARILSQIAVDEQQPGGVLAQHEREGSRALDSAAGNAEHDREEARIADNNREDRSRQHADR | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 31718
Sequence Length: 289
EC: 5.4.99.25
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O84096 | MELATESIEGVLLVDKPQGRTSFSLIRSLVRLIGVKKIGHAGTLDPFATGVMVMLIGRKFTRLSDIMLFEDKEYAAVAHLGTTTDTYDCDGKIVGRSKKVPTMDEVLTCTSYFQGEIQQVPPMFSAKKVQGKKLYEYARQGLSIERRFATVTVNLRLVKYEYPRLHFVVQCSKGTYIRSIAHELGNMLGCGAYLEELRRLRSGSFSIDQCIDGNLLDEPGFDVSPYLRDANGLILQPAPVL | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 26863
Sequence Length: 241
EC: 5.4.99.25
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Q1QSZ2 | MARRRRGTPIDGVLLLDKAPGVSSNRALQQVRRLYDAQKAGHTGTLDPMATGLLPVCFGEATKFSAYLLDADKTYRTWVRLGEVTDTGDAEGTVIEHHSVPALDERDIEAALAGFRGEVEQVPPMYSALKHQGRPLYELAREGKHVERAARRVTVYDMRLLSCEAEGFELEVRCSKGTYIRTLAEDIGHALGCGAHITSLRRLRSGPFEADAMHAFSALEDLDAASREARLLPVDTMLTHLPSLEVAASASRRLLHGQRAQIDTAGLAAQSTARLYRDAAFLGLVTVTECGEVAPRRLLNTASLASE | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33460
Sequence Length: 307
EC: 5.4.99.25
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Q97I48 | MDGILNIFKPIGLTSFDVVRQVKKISKEKKVGHTGTLDPLASGVLPICIGKATKIVDFVMEGKKIYDAEMKLGEISDTYDREGKILKVNQVTSSENNIVEAIMSFQGEILQVPPMYSALKVNGIKLYDLARQGIEIERASRKIHIYAIKILSIDIPFVKFRVECSKGTYIRSLCYDIGNKLGCGALMYNLTRVSSGNFNSSFSIPLEDLNEQNITENIINVDKCLENYDEIAVDEKFEKLLVNGVKVSDRRLIEKIPDNKTYRVYNMERKFLGLGNLSEEGFKIIKLLT | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 32560
Sequence Length: 289
EC: 5.4.99.25
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Q18BH7 | MNKIISILKPTGMTSHDVVSRVRKILNIKKVGHTGTLDPDASGVLPICIGKATKVCEVILNKDKSYICELTLGISTDTYDASGEILKKVDDFKFSNEDIERAFDTQRGEINQLPPIYSALKVNGKRMCDLVRSGRQSEITLKTRRVNIKDIKILSIKGNKVMFYVECSKGTYVRSICHDIGEYLGCGAHMSFLNRTSSGKFDLDNSITLEELELFYENKTLDKYLYDIDYVLDSFNYVVLNPNAIKYYSNGGSIDDKRFLKNNFDKDDEFVRVYSTDNFLGLGKLSKHNNTISVKSDKMFI | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34091
Sequence Length: 301
EC: 5.4.99.25
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Q92SW2 | MSRPRKPKGRPISGWLILDKPLDFGSTEAVSKIKWLFKAQKAGHAGTLDPLASGMLPIALGDATKTVPYVMDGRKIYEFTVAWGEERSTDDLEGEAVRSSAARPEEEAIRALLPKYTGVIAQVPPQFSAIKIGGERAYDLARDGETVEIPAREVEVFRLSLIGSAPNLAHFEIECGKGTYVRSLARDMGRDLGCFGHIASLRRTFVAPFGEEDMVPLADLVALEAIEDDAERLAALDAYLIDTGEALSDLPHIAVNDDQAHRLRMGNPIILRGRDAPLPTPEAYATAQGKLVAIGEIAEGEFRPKRVFATQ | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33846
Sequence Length: 311
EC: 5.4.99.25
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P59883 | MDPNGEHSPLGFLPCYKPPGATSRDLVNRAQRRLRGEFGLRKLKVGHTGTLDPLAEGLVLLAIGSAARLTPWVLQHGKRYLADFRLGVSSESGDLESELVTQTDVKLPTAAEIEQVLKDFHGVVEQTPPAHSAIKVDGERAHKRARRGEDFEMPKRRILIDSVKLISYEPPMMRLDVRCGSGTYLRTLGMDVAAACGCAAVMTKLIRNEVGRFTLDDTLDCAFMFDDDDREKMSSEPMVKYLRPAIEGLTHMPAMNLDRQQIGMLQAGIRISGTPEAPSEPLPEAWIGCIDQVDTFDRNTDVLDCIGVDRSDGSSGPWGE... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 38421
Sequence Length: 348
EC: 5.4.99.25
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Q4ULJ9 | MNSYWLNIYKPRGISSAKLVSMVKKILGKEVKVGHAGTLDVEAEGILPLAVGEATKLIQLLIDAKKTYIFTVKFGTKTDSGDYAGTVIATKDYIPSQEEAYNVCSKFIGNVTQIPPAFSALKVNGVRAYKLAREGKEVELKPRNITIYNLKCLNFDEKNATASYYTECSKGTYIRTLAEDLALSLQSLGFVIELRRTQVGIFKEENAIRIKSPDEITKNFLEEKSIKIEAILDDILVLDATDSQAQQIKYGQKCLFNYEEDFRRLSKFAYREEFEENTERSTAAYTLVREDANTGLTYKLPLEVELSVSLLWVRYKGNLL... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 38192
Sequence Length: 339
EC: 5.4.99.25
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Q9ZD46 | MGNYWLNFYKPRGISSAKLVNIVKKIIGKTKIGHAGTLDVEAEGILPLAVGEATKLIQLLIDARKTYIFSVKFGTQTDSGDYTGKVIASKDYIPSQEEVYTVCSKFIGNIRQVPPIFSAIKVNGVRAYKLAREGKIVELKPRNITIYDLKCLNFDKENAIATYYTECSKGLI | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 19116
Sequence Length: 172
EC: 5.4.99.25
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Q9KU78 | MARRRKGRVIHGVILLDKPTGISSNDALQKVKRLYGAEKAGHTGALDPLATGMLPICLGEATKFSQFLLDSDKRYRVIAKLGERTDTSDSDGQVVQTRPVHVDYDTLLACIAKFRGETDQVPSMFSALKYQGRPLYEYARQGIEVPREARKITVYEIELHRFEGDEVEMEVHCSKGTYIRTIVDDLGEMLGCGAHVTMLRRVGVANYPYERMVTLEQLNALVEQAHRDEKAVADVLDPLLLPMDTAVEALPEVNVIPELMTLIQHGQAVQVSGAPSDGMVRITGGEQKLFLGVGEIDDNGKVAPKRLVVYGE | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34488
Sequence Length: 312
EC: 5.4.99.25
|
Q8D2X8 | MIYLIIILLKFQKNLYDLLYSVIIKEDYLRNINGILLLDKPIGLSSNLILQKIKKLFKAKKAGYIGTLDPIASGMLPIFFGDATKFSDYLLNTNKWYKIKAKLGEKTNTLDSFGKIICIRPILNIKKLNIEKILSEFQGEIYQKPPMFSSLKHLGKPLYKYARQGIYIPREKRKVYVHYIKLLSFSKKYFSLTIKCSKGTYVRSIVDDIGEKLFCGAHIVKLRRTKLFNYKESHMIDSNKLYNIKKKFNDLKKLDECLLPIESIFKKLPIIVVNDDIINRLRNGIKLNFWKIKKNNLFKIISKDTKKFVGIIDINKYGRA... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 38162
Sequence Length: 327
EC: 5.4.99.25
|
B3CM19 | MVNGWLNLDKPTGMSSAQAVTQIKRIFGIKKAGHLGTLDPLASGILPIALGEATKTIPYLSCDLKAYNFTIKWGKQTTTDDLGGDIIRTSDIKPEYNQINCAIKDFIGEITQTPPQFSAVKIKGARAYKLARSGQKVNIKPRQVKIHELKMIFLDTINNIADFSMICGSGVYVRSIARDLGIELNCFGHITQLRRTMVGDFKEDESVTIEQLTKKNTTTYSPQCLTLDTNTYKSCNGQKILGAYVKNNVRDEIGLIPVLDTGMTSEGGMTEDDGGNTKGFIIPIESALKSMFKVEISLEEAEKIRKGQEIILNNLRNLKN... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 39052
Sequence Length: 353
EC: 5.4.99.25
|
Q7M9J1 | MEANKGKFYHETGGESLKPNALFVGYKPMFMSSNHYLQRLKRRFGVKKAGYSGTLDPFAKGVLVVAFGHYTRLFDHLNQEPKVYRATLWLGLHSDSLDIENILGVEVIPPYSKERVEEIMGALEGEISYTPPKYCAKRIGGRRAYDMARNKEEVELPILTMRVGRLSLLHYTHPFVHFEAEVSKGSYIRSLGGMIASRLGCYGALSSLERLSEGEMRFEGYRELEPLEILPYPKIDATSLKEEFLHGKKLLASDLGNPKEGKYIAEFEEFFSIIEIKEGQVVYLLNRMEKC | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33161
Sequence Length: 291
EC: 5.4.99.25
|
Q8PJ57 | MKPRIVYRPLHGILLLDKPSGLSSNNALQAARRLLRAEKGGHTGSLDPLATGLLPLCFGEATKIAGLLLGSAKAYDAEIVLGVTTDTDDADGESLRERAVPDLSEADLQAALAPFIGRIQQQAPIYSALKQGGEPLYAKARRGERIEAPVREVDVQAIEVLGYGAPRLRLRVTCGSGTYIRSLARDLGEALGCGAHIASLRRLWVEPFRAPQMITLEALSAVLEAGAEAQTLLLPIEAGLADFARIVLDQTRAARFRMGQRLRDAAFPTGQVAVFGPDGTPSGLGLVDADGRLSPQRLFNGLNEIPAC | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 32789
Sequence Length: 308
EC: 5.4.99.25
|
Q39243 | MNCVSRLKCLISKARSFARLGGESTLSQPPSLASAAFSSSAVMNGLETHNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGWMANDIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETVTKVDFSSKPFKLFTDSKAILADAVILATGAVAKRLSFVGSGEASGGFWNRGISACAVCDGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGERDVLGGLKVKNVVTGDVSDLKVSGLFFAIGHEPATKFLDGGVELDSDGYVVT... | Cofactor: Binds 1 FAD per subunit.
Function: NADPH-dependent thioredoxin-disulfide reductase that reduces thioredoxins O1, O2 and F3.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 39626
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 1.8.1.9
|
P32821 | MKICIFFTLLGTVAAFPTEDNDDRIVGGYTCQEHSVPYQVSLNAGSHICGGSLITDQWVLSAAHCYHPQLQVRLGEHNIYEIEGAEQFIDAAKMILHPDYDKWTVDNDIMLIKLKSPATLNSKVSTIPLPQYCPTAGTECLVSGWGVLKFGFESPSVLQCLDAPVLSDSVCHKAYPRQITNNMFCLGFLEGGKDSCQYDSGGPVVCNGEVQGIVSWGDGCALEGKPGVYTKVCNYLNWIHQTIAEN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 26901
Sequence Length: 246
Subcellular Location: Secreted
EC: 3.4.21.4
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Q15661 | MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP | Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small... |
P27435 | MLKLLLLTLPLLSSLVHAAPSLAMPREGIVGGQEASGNKWPWQVSLRVNDTYWMHFCGGSLIHPQWVLTAAHCVGPNKADPNKLRVQLRKQYLYYHDHLLTVSQIISHPDFYIAQDGADIALLKLTNPVNITSNVHTVSLPPASETFPSGTLCWVTGWGNINNDVSLPPPFPLEEVQVPIVENRLCDLKYHKGLNTGDNVHIVRDDMLCAGNEGHDSCQGDSGGPLVCKVEDTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIYRYVPKYF | Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity (By similarity).
PTM: Glycosylated.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted sp... |
P21845 | MLKRRLLLLWALSLLASLVYSAPRPANQRVGIVGGHEASESKWPWQVSLRFKLNYWIHFCGGSLIHPQWVLTAAHCVGPHIKSPQLFRVQLREQYLYYGDQLLSLNRIVVHPHYYTAEGGADVALLELEVPVNVSTHIHPISLPPASETFPPGTSCWVTGWGDIDNDEPLPPPYPLKQVKVPIVENSLCDRKYHTGLYTGDDFPIVHDGMLCAGNTRRDSCQGDSGGPLVCKVKGTWLQAGVVSWGEGCAQPNKPGIYTRVTYYLDWIHRYVPEHS | Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Plays a role in innate immunity.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
Sequence Mass ... |
P35047 | MRLFLALLALGFAAVAAVPANPQRIVGGSTTTIQQYPTIVALLFSRNGNTFFQACGGTILNNRNVLTAAHCPHGDAVNRWRVRSGSTFANSGGAVHNLNSVRIHPNYNRRNLDNDIAIMRTASNIAFNNAAQPARIAGANYNLGDNQVVWAAGWGAIRSGGPSSEQLRHVQVWTVNQATCRSRYASIGRTVTDNMLCSGWLDVGGRDQCQGDSGGPLYHNGVVVGVCSWGEECALARFPGVNARVTRYTSWISNNS | Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 27474
Sequence Length: 256
Subcellular Location: Secreted
EC: 3.4.21.4
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Q9BZJ3 | MLLLAPQMLSLLLLALPVLASPAYVAPAPGQALQQTGIVGGQEAPRSKWPWQVSLRVRGPYWMHFCGGSLIHPQWVLTAAHCVEPDIKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSHIHTVTLPPASETFPPGMPCWVTGWGDVDNNVHLPPPYPLKEVEVPVVENHLCNAEYHTGLHTGHSFQIVRDDMLCAGSENHDSCQGDSGGPLVCKVNGT | Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
Sequence Mass (Da): 26584
Sequence Length: 242
... |
P35005 | MLKFAVLLSVLACALAGTIPDGLLPQLDGRIVGGYETSIDAHPYQVSLQRYGSHFCGGSIYSHDIVITAAHCLQSIEAKDLKIRVGSTYWRSGGSVHSVRSFRNHEGYNSRTMVNDIAIIRIESDLSFRSSIREIRIADSNPREGATAVVSGWGTTESGGSTIPDHLLAVDLEIIDVSRCRSDEFGYGKKIKDTMLCAYAPHKDACQGDSGGPLVSGDRLVGVVSWGYGCGDVRYPGVYADVAHFHEWIERTAEEV | Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 27810
Sequence Length: 256
Subcellular Location: Secreted
EC: 3.4.21.4
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Q9NRR2 | MALGACGLLLLLAVPGVSLRTLQPGCGRPQVSDAGGRIVGGHAAPAGAWPWQASLRLRRVHVCGGSLLSPQWVLTAAHCFSGSLNSSDYQVHLGELEITLSPHFSTVRQIILHSSPSGQPGTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYSLREVKVSVVDTETCRRDYPGPGGSILQPDMLCARGPGDACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWIRRHITASGGSESGYPRLPLLAGFFLPGLFLLLVSCVLLAKCLLHPSADGTPFPAP... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33817
Sequence Length: 321
Subcellular Location: Membrane
EC: 3.4.21.-
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Q9QUL7 | MALGPNCGILLFLAVSGCGHPQVSNSGSRIVGGHAAPAGTWPWQASLRLHKVHVCGGSLLSPEWVLTAAHCFSGSVNSSDYQVHLGELTVTLSPHFSTVKRIIMYTGSPGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLKPPYNLQEAKVSVVDVKTCSQAYNSPNGSLIQPDMLCARGPGDACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHHIPEAGGSGMQGLPWAPLLAALFWPSLFLLLVSGVLMAKYWLSSPSHAASEL | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32656
Sequence Length: 311
Subcellular Location: Membrane
EC: 3.4.21.-
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Q8ZLN0 | MNNNLPIGSIAAAVDLLNKENVIAYPTEAVFGVGCDPDSETAVTRLLALKQRPVDKGLILIAASFEQLKPYIDDSILTAAQRKAVFDCWPGPVTFVFPAPATTPRWLTGRFDSLAVRVTNHPLVVALCNAYGKPLVSTSANLSGLPPCRTVEEVRAQFGDDFPVVEGATGGRLNPSEIRDALTGELFRQG | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
Q8EKQ3 | MLQLHPSDIKDVVLNGGVIAYPTEAVYGLGCDPDNDTAIQKLLAVKQRPWQKGLILVASEFSQLLAYVDESQLTDEQLELAFSKWPGPFTFVMPIKPHVSRYLCGEFDSIAVRVSAHEGVRALCQALGKPLVSTSANLAGEDPALSGDEILNVFEGKIDALVLGQLGEQRQPSTIIDARSGKILRNGQ | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
Q1LK37 | MLVLGIESSCDETGLALYDTEAGLLAHALHSQIAMHREYGGVVPELASRDHIRRVLPLLQQVLDDAGRTRADIDAIAYTQGPGLAGALLVGASVANALGFALGVPMIGVHHLEGHLLSPLLTSAPPPFPFVALLVSGGHTQLMEVKGIGDYKLLGETLDDAAGEAFDKTAKLLGLGYPGGPEVSRLAEFGNPGAFELPRPMLHSGNLDFSFAGLKTAVLTQTRKLSNACEQDRANLARAFVDAIVDVLAAKSFAALKQTGDKRLVVAGGVGANRQLRERLNEMGKRRKVEVFYPDLAFCTDNGAMIAFAGAMRLKAAPEL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q2GEG6 | MNNHLILGVETSCDETSVAIVSEEGEVCFHEIFTQDHSKYNGVYPEFASREHLKILPQILRRAVQAHDLEKLTAIACTVGPGLVGSLIVGVMMARGLAFSLKKPVFGVNHLEGHLLAVRLVEKINFPFVCLVISGGHSQLIDARGIGDYVLLGETLDDAFGEAFDKLATMLGFTYPGGKTVEKLAIKGDSERFRLPAAMINQSGCNFSLSGIKTALKKIITSLPQITEKDKADICASFQACVARIMVNKLEQAVKICGHSRIVLAGGVGSNRYIRETLEEFAKNHNLSLHFPEGILCTDNAAMIAWAAIERLKAGCTELS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q3JF13 | MRVLGIETSCDETGVAVFDSKQGLLADILHSQAKLHAGYGGVVPELASRDHIRKLLPLLRKVLNQAGLNKEDIDGVAYTGGPGLIGALLVGAAVGRSLAWALGKPAIAVHHMEGHLLSPLLEPNPPGFPFCALLISGGHTMLVTVNRIGAYRILGESLDDAVGEAFDKTAKLLQLGYPGGPALAKLAEQGNPDRFYFPRPMLDRPGLNFSFSGLKTYALNTLHKNGSEAAADIARAFQDAVVDTLTVKCRRALQQTGLNRLVVAGGVSANQALRQRLKAMGTQENVQVYYPRLAFCTDNGAMIAFAGCQRLLAGEQTSSG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q3A3G6 | MLLLTLESSCDETSAAVVRDGRQVLSNVIASQIDVHALYGGVVPELASRKHMEAVAVVVDDALRQARVALGDIEGIAVTRGPGLVGALLVGLSMAKAMAMSLDIPLVGVHHMEGHILAPLLEQDVPFPYLALAVSGGHTHLYRVDGIGRYRIVGRTLDDAAGEAFDKVSKLLGLGYPGGAVIDRLAAEGNPKAFDFPRPLLKKPNFDFSFSGIKTALLYYAQSQKGPIEGDHLRDVAASFQQAVVEVLCKKTLRAARETGLQRIVVAGGVACNKGLRRMMGERSAKEGFQVFFPSPGLCADNAAMLGVAGDAYLAGGCTS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0LNI2 | MIILGVESSCDETAAAVVEDGSRVLSDVVASQAALHGPYGGVVPELASRKHVEAILPVLGEAMHEAGVTWGQVDAIAATQGPGLVGALLVGLSAAKALAYALKKPMVAVNHLEGHIQAAFLGREELTRPFVCLVVSGGHTALYRVDPDGTTSFLGSTRDDAAGEAFDKVAKLLALGYPGGVEIERLAAGGDPHAFNFPRAFIDGRSLEFSFSGLKTSVATFVRQHGPPSESGEQGAYRLADLLASFQEAVVEVLVNKTVRAAGMCSVGDIAVVGGVAANLRLRERFEEEAGMHRFELHLPARRYCTDNAVMIAAAAYRTW... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q0AVU0 | MVLVQESLILGIETSCDETAAAIVRNGKEILSNIVNSQIDIHQQFGGVVPEVASRKHIENIAGVVHRAFSEAQLAYSAIDAVAVTNRPGLVGALLVGVSFAKAFAYALEKPLIAVNHLHGHIYANFLEHRDIEFPAICLVVSGGHTSLLLMSNPNKMEVLGETRDDAAGEAFDKVARFLGLGYPGGPAIQEAATKGKAGQLQLPRVFLDRNDFEFSFSGLKTAAMNQWNKLQRRGQANVFDMAAEFQAALVEVLVEKSIKAAAKYQVRTIMMAGGVAANQELRNLMKKRTKEAGLKLFYPSLKLCTDNAAMVAANAHYHY... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
P74034 | MAIILAIETSCDETAVAIVNNRNVCSNVVSSQIQTHQIFGGVVPEVASRQHLLLINTCLDQALQASGLGWPEIEAIAVTVAPGLAGALMVGVTAAKTLAMVHQKPFLGVHHLEGHIYASYLSQPDLQPPFLCLLVSGGHTSLIHVKGCGDYRQLGTTRDDAAGEAFDKVARLLDLGYPGGPAIDRAAKQGDPGTFKLPEGKISLPQGGYHPYDSSFSGLKTAMLRLTQELKQSSAPLPVDDLAASFQDTVARSLTKKTIQCVLDHGLTTITVGGGVAANSRLRYHLQTAAQEHQLQVFFPPLKFCTDNAAMIACAAADHF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
B7IGB4 | MIVLGIETSCDETSVAILSDGKILSNVVSSQIDIHKKFGGVVPEIAARHHLSNLPIVFKNAIDMANISIDQIDLISVTYGPGLIGALLVGISFAKGLSLRLGKPLIGVNHIVGHVFANYITYPHLKPPYIVLMVSGGHTEILLVKQDDEIEVLGKTVDDAAGEAFDKVARILGLGYPGGPEIDKLSKNGDENKFNFPRPMMDSKSYNFSFSGLKTAVLYTVQKFDKDNVPKEDIAASFQKAVVEILLKKTFKAAKDLNVNTIVLAGGVAANSYLRKKAQKLSEKQNIKVLIPPLEFCTDNAAMIAMAGYKLYKKGISSDS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A6LKP0 | MIVLGIETSCDETAVAVLENEKILSSVVSSQIDVHKKFGGVVPEIAARHHLSNLPVVFKNALSQAKISLNDIDLISVTYGPGLIGALLVGISFAKGLSLKLNKPLIGINHIVGHVYANYLTYPNLKPPFIVLMVSGGHTEILHIQNEKIEVLGKTLDDAAGEAFDKVARILGLGYPGGPEIEKIAQYGNDKAFNFPKPLYDSKDYNFSFSGLKTAVLYTIKKLDKIPKEDVAASFQRAVTDILLHKTFKAAKDKKINTVVLAGGVAANKYLRTKALEISKKEGIILLIPPIEFCTDNAAMIAIAGYKLFDGTSDLNIDAM... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q9WXZ2 | MRVLGIETSCDETAVAVLDDGKNVVVNFTVSQIEVHQKFGGVVPEVAARHHLKNLPILLKKAFEKVPPETVDVVAATYGPGLIGALLVGLSAAKGLAISLEKPFVGVNHVEAHVQAVFLANPDLKPPLVVLMVSGGHTQLMKVDEDYSMEVLGETLDDSAGEAFDKVARLLGLGYPGGPVIDRVAKKGDPEKYSFPRPMLDDDSYNFSFAGLKTSVLYFLQREKGYKVEDVAASFQKAVVDILVEKTFRLARNLGIRKIAFVGGVAANSMLREEVRKRAERWNYEVFFPPLELCTDNALMVAKAGYEKAKRGMFSPLSLN... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
B9KXJ0 | MIILGIETSCDETAAAVVRDGRFVLSNIIRSQVDLHQRYGGVVPELASRRHVTSIVPVLDLALEQAGIGPSAIDAIAVTEGPGLAGSLLVGINVAKTLAFVWEKPLIPVNHLEGHIYANWLTLPGQDEVPEPTFPLVCLIVSGGHTELVLMRGHGDYVLLGRTLDDAAGEAFDKAARLLGLGFPGGPAIQKAAEQGRPGRFSLPRAWLGESYDFSFSGLKTALLRVLEQYQRRPARRVAAGQPFPEYVAPEYGPSVPIADLAAEFQAAVVEVLAEKTARAAREFGATMVLLAGGVAANAALRQRLREISPVPVRYPPPIL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
D4GPW1 | MSFAAGLLNATVQAATVLLLAGLGELISERAGVLNLGVEGMMLVGALGGFVVTAVTGNYWLGFGVGIACGMALAAVHAFLCISLKSNQVISGVMLTLLGTGLTTFFGSGWVQESITGFPQMTFPIVGRYLVHLPLVGEAFFRSTATDYLALLAVPVVWFFLYRSNLGLEIIAVGEDPEMADTMGVPVFKFRYLAVIIGGGFAGAAGAHLSLAFSQLWVPGMTVGRGWIAVALVVFAQWRPSRMLVGAYLFGLLDALQLRSQSLSLALDPNAPLAGVLNPLVNTLMNPQIMSTYPYLTTIAVLSYAVIRTESVRLAVPSAL... | Function: Part of an ABC transporter complex involved in glucose import (Potential). Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34876
Sequence Length: 329
Subcellular Location: Cell membrane
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D4GPW3 | MTREPFLRMENIVKAFPGVVANDHIDLTVERGEIHGLLGENGAGKSTLMKILYGLYSQDDGEISLSGTRLRLDSPQDAIDAGIGMVHQHFMLIPRLTVAENVVLGEREPATPFRPDADAGGWLPDAVRSNSLVQSLAGRFSLGLDVPERRIQELADRYGFDIDVSAKVWELGVGQQQRVEILKALYRDVDLLILDEPTAVLTPTEADLLFDSLERLTDEGVSIIFITHKLEEVEAVVDRVTVLRDGENVGTVSTSDVSRADLAEMMVGREVLFTVDRERVAPGEPVLRARNVSATDDRGIEALSNVDLTVRRGEVVGIAG... | Function: Part of an ABC transporter complex involved in glucose import (Probable). Responsible for energy coupling to the transport system (By similarity).
Catalytic Activity: ATP + D-glucose(out) + H2O = ADP + D-glucose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59405
Se... |
Q9UI38 | MGRWCQTVARGQRPRTSAPSRAGALLLLLLLLRSAGCWGAGEAPGALSTADPADQSVQCVPKATCPSSRPRLLWQTPTTQTLPSTTMETQFPVSEGKVDPYRSCGFSYEQDPTLRDPEAVARRWPWMVSVRANGTHICAGTIIASQWVLTVAHCLIWRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQRFWSWVGQANDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQFRTIQEKEVIILNNKECDNFYHNFTKIPTLVQIIKSQMMCAEDTHREKFCYELTGEPLVCSMEG... | Function: May be involved in proteolysis through its threonine endopeptidase activity.
Sequence Mass (Da): 43088
Sequence Length: 385
Subcellular Location: Endoplasmic reticulum
EC: 3.4.25.-
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Q8BLH5 | MEPWCGAEVRGQGPQGPRVPGASRSRSRALLLLLLLLLLLLPRRPAGERIRPRRPPRHAHPRPPLTRWRPSTGYLAAGASPGTLSTTVPTGPGVSCGSRGICPSGRLRLPRQAQTNQTTTAPPNSQTMAPLKTVGTLGMMDTTGSVLKTVHSSNLPFCGSSHEPDPTLRDPEAMTRRWPWMVSVQANGSHICAGILIASQWVLTVAHCLSQNHVNYIVRAGSPWINQTAGTSSDVPVHRVIINHGYQPRRYWSWVGRAHDIGLLKLKWGLKYSKYVWPICLPGLDYVVEDSSLCTVTGWGYPRANGIWPQFQSLQEKEVS... | Function: May be involved in proteolysis through its threonine endopeptidase activity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48676
Sequence Length: 439
Subcellular Location: Membrane
EC: 3.4.25.-
|
Q5TGU0 | MRLQGAIFVLLPHLGPILVWLFTRDHMSGWCEGPRMLSWCPFYKVLLLVQTAIYSVVGYASYLVWKDLGGGLGWPLALPLGLYAVQLTISWTVLVLFFTVHNPGLALLHLLLLYGLVVSTALIWHPINKLAALLLLPYLAWLTVTSALTYHLWRDSLCPVHQPQPTEKSD | Function: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum . Required to meet cholesterol demands during erythropoietic differentiation . May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-med... |
Q9CRZ8 | MQLQGPVFVGVPLLGPILICMLIHQPSSRCEDERKLPWCPPHKVILLVWVTIYSVMGYASYLVWKELGGGFRWPLALPLGLYSFQLALSWTFLVLFLAADSPGLALLDLLLLYGLVASLVFIWQPINKLAALLLLPYLAWLTVTTAITYRLWRDSLCPTYQP | Function: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum . Required to meet cholesterol demands during erythropoietic differentiation . May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-med... |
O82245 | MDSQDIRYRGGDDRDAATTAMAETERKSADDNKGKRDQKRAMAKRGLKSLTVAVAAPVLVTLFATYFLGTSDGYGNRAKSSSWIPPLWLLHTTCLASSGLMGLAAWLVWVDGGFHKKPNALYLYLAQFLLCLVWDPVTFRVGSGVAGLAVWLGQSAALFGCYKAFNEISPVAGNLVKPCLAWAAFVAAVNVKLAVA | Function: Stress-induced membrane protein that can bind heme and may play a role in the transport of tetrapyrrole intermediates during salt stress and contribute to the detoxification of highly reactive porphyrins in the cytoplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21062
Sequence Length... |
O28797 | MNILKLVASILAVLAIGFAGSFFTAQSVQTWYAGVEKPFFTPPNWLFGPAWTLLYFLIGIVLYIAWENGFWNDSRVKATFFTQLGLNFLWSILFFGLQNPLAGLVDIIALDIAVILTIVYIYHHSKASLLLLPYLGWILFASALNFAIYLLNA | Function: Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX . May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17185
Sequence Length: 153
Subcellular Location: Cell... |
Q81BL7 | MFMKKSSIIVFFLTYGLFYVSSVLFPIDRTWYDALEKPSWTPPGMTIGMIWAVLFGLIALSVAIIYNNYGFKPKTFWFLFLLNYIFNQAFSYFQFSQKNLFLATVDCLLVAITTLLLIMFSSNLSKVSAWLLIPYFLWSAFATYLSWTIYSIN | Function: Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX . Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation . May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By simi... |
Q9RFC8 | MNMDWALFLTFLAACGAPATTGALLKPDEWYDNLNKPWWNPPRWVFPLAWTSLYFLMSLAAMRVAQLEGSGQALAFYAAQLAFNTLWTPVFFGMKRMATALAVVMVMWLFVAATMWAFFQLDTWAGVLFVPYLIWATAATGLNFEAMRLNWNRPEARA | Function: May play a role in the transmembrane transport of tetrapyrroles and similar compounds, and thereby contribute to the regulation of tetrapyrrole biosynthesis . Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX . Binds protoporphyrin IX, hemin, and coproporphyrin III, but does... |
Q8KBX2 | MNKQILTLALCIGLCLAVGFAGSTFTPKPASWYYTTLVKPSWNPPDWLFPPVWTILFIMMGTALAKVLGTGWKKNEVNVGVVLFAIQLMLNLGWSASFFGMQSPLAGLVDIVLLWIFIVLTMLAFARVSKPASLLLVPYLCWVSFASYLNFTILQLNP | Function: Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX . Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation . May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By simi... |
P30536 | MAPPWVPAMGFTLAPSLGCFVGSRFVHGEGLRWYAGLQKPSWHPPHWVLGPVWGTLYSAMGYGSYLVWKELGGFTEKAVVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLLLVSGAAAATTVAWYQVSPLAARLLYPYLAWLAFTTTLNYCVWRDNHGWRGGRRLPE | Function: Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism , but its precise physiological role is controversial. It is apparently not required for steroid ... |
Q8W4P9 | MWLSFLRPRDRFSLAELRYLTDQLRKIQIVNEANKDLVIEALRSIAEILTYGDQHDPLFFEFFMEKQVMGEFVRILRVSKTVTVSVQLLQTMSIMIQNLKSEQAIYYLFSNEYVNYLITYTFDFQHEELLSYYISFLRAVSGKLNKHTISLLLKTENDVVVSFPLYVEGIQFAFHEENMIRTAVRALTLNVYHVGDESVNDYVVSPPHTEYFSKLISFFQKQCMDLSAMVLNTLKSPSPDSGGKLFSAVDGIEDTLYYFSDVISAGIPDIGRLITDHILQHLTLPLLLPSLCSEAVNDISVDPVTSLYLLSCILRIVKIK... | Function: Involved in membrane trafficking and vacuole development through membrane fusion at the vacuole. Required for membrane trafficking machinery and accumulation of flavonoids in the seed coat.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94742
Sequence Length: 837
Subcellular Location: Golg... |
Q74GW7 | MEFIDNIRYKKIKNAVGRAVADFGLIRDGDRIAVAVSGGKDSYTLLHILEGLRRRAPVKYELVAVTIDSGYPGFRSDVIASYLREQGFAHHLETTDHYDIIREKRRPGSSYCSICARLKRGVLYTLAQKLGCNKLALGHHLDDFVETLLLNQFFVGTLKAMAPRMLADNGETTVIRPLVYVEEREIIPFARENRFPVVCCSCPVCGTADLQRRRMKKLLTELEKENPAVKRSLLRALGNVQPRYLLDLELQRLCDVP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
Q9LVM5 | MAMEIGEDEWKVCCGSSEFAKQMSTSGPLTSQEAIYTARDIWFNQVNVTDWLEAFSAHPQIGNTPSPSINSDFARRSVSEQSTAFATTSASALQELAEWNVLYKKKFGFIFIICASGRTHAEMLHALKERYENRPIVELEIAAMEQMKITELRMAKLFSDKAKVISETDSSSSPVSTKPQDRLRIIGGHLNVAAEAKAPKRSRPPITTHVLDVSRGAPAAGVEVHLEVWSGTTGPSFVHGGGGVWSSVGTSATDRDGRSGPLMDLVDALNPGTYRISFDTAKYSPGCFFPYVSIVFQVTESQKWEHFHVPLLLAPFSFST... | Function: Involved in the last two steps of the degradation of uric acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its stereoselective decarboxylation to (S)-allantoin, a major ureide compound . Might function as a negative regulator to modulate brassino... |
O55245 | MAFHSMLLVFLAGLVFLTEAAPLVSHGSIDSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE | Function: Thyroid hormone-binding protein, with a much higher binding affinity for triiodothyronine (T3) than for thyroxine (T4). Probably transports triiodothyronine from the bloodstream to the brain.
Sequence Mass (Da): 16412
Sequence Length: 150
Domain: The N-terminus strongly influences thyroid hormone-binding prop... |
P02766 | MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE | Function: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
PTM: Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading t... |
P36096 | MEIDGNTLVFIIVILFLFFSSPGGDGVSSQYEFNQLQRLKQQFRTEHNTFVNMTYTDSFRNITGLKLSYQDMLNNPLQNATYPLPGKDYDRWFPNQNYMVLPNDVIEAINTEVWNTSNDDASNLFPPNITSTLLGKIDLVSNNKYEKIRMPVPRFYEPATDFSEDIPPEGETYWSEWPSYGELHNVSFQHGEIAIQISHMSNLQDNNNYLRRNFINKKNDRWKLLNLQIDFSDKAEKEKHSIYSKAVYDIQRGRILSISQSSKFHSLFALPHYMSFQNDYNEKIFNDVKELVDEFWNFTDYTDVMTMKDVQDAYNNANFK... | Function: Catalytic component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control . Mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12... |
O00294 | MPLRDETLREVWASDSGHEEESLSPEAPRRPKQRPAPAQRLRKKRTEAPESPCPTGSKPRKPGAGRTGRPREEPSPDPAQARAPQTVYARFLRDPEAKKRDPRETFLVARAPDAEDEEEEEEEDEEDEEEEAEEKKEKILLPPKKPLREKSSADLKERRAKAQGPRGDLGSPDPPPKPLRVRNKEAPAGEGTKMRKTKKKGSGEADKDPSGSPASARKSPAAMFLVGEGSPDKKALKKKGTPKGARKEEEEEEEAATVIKKSNQKGKAKGKGKKKAKEERAPSPPVEVDEPREFVLRPAPQGRTVRCRLTRDKKGMDRGM... | Function: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylin... |
Q9Z273 | MPLQEETLREVWASDSGHEEDCLSPEPPLRPKQRPAQGQKLRKKKPETPDSLESKPRKAGAGRRKHEEPPADSAEPRAAQTVYAKFLRDPEAKKRDPRENFLVARAPDLGGEENSEEDSDDDDNDDDEEEEEKKEGKKEKSSLPPKKAPKEREKKAKALGPRGDVGSPDAPRKPLRTKKKEVGEGTKLRKAKKKGPGETDKDPAGSPAALRKEFPAAMFLVGEGGAAEKGVKKKGPPKGSEEEKKEEEEEVEEEVASAVMKNSNQKGRAKGKGKKKVKEERASSPPVEVGEPREFVLQPAPQGRAVRCRLTRDKKGMDRG... | Function: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells. Binds lipids, especially phosphatidylinositol 3-phospha... |
Q86PC9 | MSGINSRNQKMEQQRQLMEAYIRQKRASPGMVQASDLQINRPMSGMRSNSRELHAYDGPMQFISSPQNPDQILTNGSPGGINPVAMNTSRNHSNNMRSLSTINQEADLIEEISSHELEDEESSPVTVIEQHQQSASHSANSTQSQKPRARQHSFSDNLDEDDYTNRNVAGAAPVRPAGMASSPYKDATLDGSSNGTGNGTGGESEGDVIGNIDQFVMQPAPQGVLYKCRITRDRKGMDRGLFPIYYLHLERDYGKKIFLLGGRKRKKSKTSNYIVSCDPTDLSRNADGFCGKLRSNVFGTSFTVFDNGNKESTESPRLDL... | Function: Functions in regulating protein trafficking, retinal maintenance and lipid storage . Protects photoreceptor cells R1 to R6 against light-induced retinal degeneration by stimulating norpA-mediated endocytosis of the rhodopsin ninaE (Rh1) . In the auditory receptor neurons, functions as a cilia trafficking regu... |
Q13454 | MGARGAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLG... | Function: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of ... |
A4R2N5 | MTLKEEFATRNFSIYGQWLGVLSMILCFALGIANIFTFRLLLIIFSVICLVSSFVILFIEVPLLLRICPTSSTFDDAIRKVSTNYMRAAAYLVMGVVQWLSLLGGASSLIAAAVFLTLTAICYALAGVKGQAFVGSKTLGGSGVAQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16016
Sequence Length: 149
Subcellular Location: Golgi apparatus membrane
|
A1D708 | MTLAEEFRSRNFSIYGQWTGVLCIILCIALGIANIFSFAVLRIIFSVLCLYAMSGLILIFIEVPFLLRICPTSSKFDAFIRRFTTNWMRAAMYAIMSVVQWLSLLPGSGASSLIVAAVFLLIASIFYALAGLKSQEFVGSKTLGGQGLVQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16836
Sequence Length: 153
Subcellular Location: Golgi apparatus membrane
|
Q7S693 | MALKDEFATRNFSIYGQWLGILSMILCFALGIANIFTFRPIIIVFSVITLCFSFVILFVEVPLLLRICPTSPTFDNLIRKISTNYTRAAAYGVMAVVVFLSCIDRTTSLLVPGIFLSFTGICYALAALKGQAFVGSKTLGGAGVAQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16192
Sequence Length: 149
Subcellular Location: Golgi apparatus membrane
|
Q0V0G4 | MTLAEEFKSRNFSIYGQWTGVLCIFLCFALGVANIFHPTFVIAFSIVCLVSSFVIIFIEIPLLLRICPTSPKFDAFIRKFSSNYMRAAIYGVMSVVQWISIWPQATSLIVAAIFLMVAAIFYALAGFKGQQFQGSKTLGGQGVAQMII | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16397
Sequence Length: 148
Subcellular Location: Golgi apparatus membrane
|
B2AR67 | MTLKEEFQTRNFSIYGQWLGILSMILCFALGLSNMISSIFSLNIVIIAFSILAMVFSFVILFVEVPLLLRICPTSSSFDAAIRKISTNYMRAGAYGVMALVIWLSCISTRTSLIAAAVFLTLTGACYGLAGAKGQAFVGSKTLGGQGVAQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16427
Sequence Length: 153
Subcellular Location: Golgi apparatus membrane
|
O74375 | MFESIIVDRAKTTFLGELKSYNFSIYAQWLGILSIFLCIILGIVNLFHVTLVVLFSALTIIEGVLLIFIELPFLSRICPVSDKFQAFTNAFASNYYRGLVYFIFSVVTFLSCIFMATSLIATGIVLALTGLCYTFAGIKGQAFTSSSTLGGTGITTETPPSTMV | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17922
Sequence Length: 164
Subcellular Location: Golgi apparatus membrane
|
A6ZMD0 | MALSLGQFINVGGMVKDLKSFNFSVYGRWFGYINIILCIALGIANLFHVSGVIAFGIISIIQGLVILFIEIPFLLKICPLSDNFIEFIKRFETNGWRCLFYLAMAIIQYISIAVMATSLIVVAVGLTISSISYAVAYTKHQEFQNTNIIKNPTDDDFPHEAVVREML | Function: Golgi membrane protein involved in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18693
Sequence Length: 167
Subcellular Location: Golgi apparatus membrane
|
Q8LEK2 | MDPNNQIQAPVENYANPRTCLFHVLFKGAALAFYILSALFFNSFVIIFVVTVLLAALDFWVVKNVSGRILVGLRWWNEINDLGESVWKFESLDQESLARMNKKDSWLFWWTLYLAAAAWFILGVFSLIRFQADYLLVVGVCLSLNVANIIGFTKCKKDAKKQFQQFASQTIASRFQSTVQSAFTLV | Function: Mediates trans-Golgi-network trafficking and cell elongation . Required for keeping the appropriate balance between secretory trafficking and vacuolar targeting of a subset of proteins . The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins a... |
Q12792 | MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYTCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEEVHPKQHAHK... | Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (B... |
Q91YR1 | MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDSFVLPLLEDKQPCYVLFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVSVDTKHQTLQGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSARYHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRKIEIDNGDELTADFLYDEVHPKQHAHK... | Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
P... |
Q6IBS0 | MAHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFK... | Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. M... |
Q9Z0P5 | MAHQTGIHATEELKEFFAKARAGSIRLIKVIIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQEPCYLLFRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPTNVAQLPSRIPRDAARYHFFLYKHTHEGDALESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFK... | Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. M... |
P58605 | GSCIESGKSCTHSRSMKNGLCCPKSRCNCRQIQHRHDYLGKRKYSCRCS | Function: Potent and selective blocker of N-type voltage-gated calcium channels (Cav2.2/CACNA1B). Also blocks vertebrate Cav2.1/CACNA1A (P/Q-type) and Cav1.2/CACNA1C (L-type) channels at very high concentration (2 micromolar).
Sequence Mass (Da): 5594
Sequence Length: 49
Domain: The presence of a 'disulfide through dis... |
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