ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A0A1Z3GBK8 | MGIVALILIKAAMSLILSSFPLFRSSRSSPASASLAGSGLPKTTPPKTASLQSHSPMFEETKGRIAKLFKKNEVCISTYDTAWVGMVPSPFSSDQPCFPDSLFWLLDNQCPDGSWAQPHHHSHSHSPSLLNKDVLSSTLASILALHKWGLGQHHIAKGLHFLELNFASATDNSQITPLGFDIVFPAMLDHAADLSLNLRLDPTTLNDLMNRRDLELQRCTENGSAETEVYMAYIGEGMGKLHDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSALNKFGSAVPAVYPLDIYSQLCIVDNLERLGISRFFST... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of ent-copalyl diphosphate (ent-... |
A0A1D6KUI6 | MASLSFASSHASLFCCQQSSSAIILRPAGALLRLSRRQPSSHTISTTDQLFPRRSRMPRNVDTHAAAERNSPSTMSSLEAVDELETNGDSAVVVVREQQQQQHLLMGATDDGLPPSPYDTAWVAMVPAPGNPLVPRFPQCVDWILQNQRSDGSWGPDGGSGDHPSSPLGKDALMSTLACVLALKTWDAGEEHVRKGLSFVGNNSPSCVMTGDERDAPVGFSVIFPGMLARAIDMGLDIPMMTQANVDAFIRLRDTELNRMAATTGSKAFMSYVAEGLGDVLDWDEAAMVYQRQNGSFFNSPATTAAAAIHGNNDRALRYL... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses . In response to fungal infection and in associtation with AN2, is involved in the production dolabradiene, a type of antifungal phytoalexin . Converts ent-c... |
Q0JEZ8 | MASPMEAVARSSLVLAPRRRRALGLLPAAAAAAPFVLDCRRRHNGGMRRPHVSFACSAELDTGRRQLPSTGTRAVMSSCPGYVEGRMVGENTSQINMGWEARILRHLENPEFLPSSYDIAWVAMVPLPGTDHLQAPCFPECVEWILQNQHSNGSWGVNEFDSSASKDILLSTLACIIALEKWNVGSEQIRRGLHFIAKNFSIVIDDQIAAPIGFNLTFPAMVNLAIKMGLEFPASEISIDQILHLRDMELKRLAGDESLGKEAYFAYIAEGLEESMVDWSEVMKFQGKNGSLFNSPAATAAALVHRYDDKALGYLYSVVN... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of momilactone A and B phytoalexins. Catalyzes the conversion of syn-copalyl diphosphate to the phytoalexin precursor syn-pimara-7,15-diene.
Catalytic Activity: 9alpha-copalyl diphosphate = 9beta-pimara-7,15-diene + diphosphate
Sequence M... |
A0A1Z3GCD1 | MFSSSLKLKTNPLMDNKIHRSSSDRDFRGSTISSVKCSLNNSEDLIVKVRERVKGKVEISPSAYDTAWVAMVPERDYSGQKPRFPECLDWIVENQNADGSWGVQSSSMLKHSLSCTLACLLPLRKWNVASPQLLRNGVEFIRSSSSAATDKNQISPIGFDIVFPMMIQYANDLNLELLLNQDLVNILFQNREAQLTRNKNLEYVAEGLGSSIDWNKVLMHQRSNGSLFNSPATTAAALIHRHDKKCLEYLNSLLSIYKTWVPTIHPMDVYARLCLVDHLQGLGVDRFVHPEIEVVLQETFRLWQQKDDKIFTDATCRAMA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of (+)-copalyl diphosphate ((+)-... |
A4KAG8 | MMLPMSSACSGGQFPGASPHGIIPKQFSRAPRIRVSIRGAAGVEKSLGLGRNAGSQQGMHKNELHDKIRKQLRDVQLQPSSYDTAWVAMVPVQGSHQTPRFPQSIEWILQNQYDDGSWGTNLPGLVVNKDILLCTLACVVALKRWNTGRDHISRGLNFIGRNFSVAMDEQTVAPVGFNITFSGLLSLATRTGLELPVMQTDIDGIIHIRKIELERDAYGTASSRRAFMAYVSEGLGNLQDWNQVMAYQRKNGSIFNSPSATAATIIHGHNYSGLAYLDFVTSKFGGPVPVMYPQNAYSQLCMVDTLERMGISESFACEIS... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products . Catalyzes the conversion of ent-copalyl diphosphate to the phytoalexin precursor ent-isokaur-15-ene .
Catalytic Activity: ent-copalyl diphosphate = diphosphate + ent-isokaurene
Sequence Mass ... |
P37537 | MSGLFITFEGPEGAGKTTVLQEIKNILTAEGLQVMATREPGGIDIAEQIREVILNENNILMDPKTEALLYAAARRQHLVEKVKPALEQGFIVLCDRFIDSSLAYQGYARGLGIDEVLSINEFAIGDMMPHVTVYFSIDPEEGLKRIYANGSREKNRLDLEKLDFHTKVQEGYQELMKRFPERFHSVDAGQSKDLVVQDVLKVIDEALKKIQL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23866
Sequence Length: 212
EC: 2.7.4.9
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Q6G5D6 | MSGYFITFEGGEGVGKTTQIFLLAQHLYGKGYDVLTTREPGGTAGAEVIRHILLSGQVQQHYGPLIEAILFTAARIDHVSEVIMPSLQKGKVVLCDRFIDSTRVYQGLNDKVSSSTLAVLECLALNKIKPQITFLLDIPARCSMKRANLRREKAETIDYFEKDELKIQEQRRQAFLQLAKQEPHRFRVIDGTDTVEVIAQQIRDICDQVMLDQLP | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24249
Sequence Length: 215
EC: 2.7.4.9
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Q6MP28 | MRCKMKFIVFEGLDGSGKSSLMAALERELQNRAINFLRTREPGGTPLGDEIRNMILRKEGPAPTPRTELLLYEASRSQHVDQVIRPALAAGTWVLCDRFAASSVAFQSGGRAISEADVVMLNTFATGGLKADITVLLDLSVEESRRRRQGRGAVTGETEDRIESEADTFHENVRQSFLKQSREDAAAWIVLDARETPEVLFKQLLQSLTERKVL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23819
Sequence Length: 214
EC: 2.7.4.9
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B9KKV1 | MGAQGFFLAVEGIDGSGKSGIVRSLAAHLGAEGRDVLVTREPGGTPEGEAIRGLVLAGADEAWDPMAELLLMTAARVQHVRRVIAPALAQGQVVISDRYAGSTLAYQGTGRGLSEAFIRTLHAEATGDLWPDLTLVLDLEAGIGLARSRRRLTGETLDEGRFESLDLAFHERIRAAFLAQAARDPGRHAVIDASGTPEEVQARACAALTPFLAQAPV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22858
Sequence Length: 217
EC: 2.7.4.9
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Q8KCU7 | MLISFEGIDGAGKSTQVMKLKRYLQERGREVLALREPGGTPVAEEIRELLLERRNDITPVGELLLFAASRAELVQQVIQPALENDSDVILDRFFDSTTAYQGYGRGLDLDMLAEINRIASCRLVPDVTFYLDLTPEDALMRKFSEKSLPLAFESEELDRMENSGLDFYRRVREGYHKIGGENPNRIIIIDALLSPSEIHRKIISSIDALCTKTA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24147
Sequence Length: 214
EC: 2.7.4.9
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O84191 | MFIVVEGGEGAGKTQFIQALSKRLIEEGREIVTTREPGGCSLGDSVRGLLLDPEQKISPYAELLLFLAARAQHIQEKIIPALKSGKTVISDRFHDSTIVYQGIAGGLGESFVTNLCYHVVGDKPFLPDITFLLDIPAREGLLRKARQKHLDKFEQKPQIFHRSVREGFLALAEKAPDRYKVLDALLPTEASVDQALLQIRALI | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22473
Sequence Length: 203
EC: 2.7.4.9
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Q1QX49 | MTPGRFITLEGGEGVGKSTNVAFVCDWLSARGIEVVRTREPGGTPRAEAIRELLLDPAPQEPLDETAELLLMFAARAQHLAARIRPALARGAWVVCDRFTDATFAYQGGGRGLDETRIATLEALVQQGLQPDLTLLLDMPVEAAQRRVERRGIERDRFERERGAFFNAVRESYLARAAQAPTRFAVIDADRSLEAVQASIAAHLTERLASWS | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23342
Sequence Length: 212
EC: 2.7.4.9
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Q6AGT5 | MSVPTNRPGLFITLEGGDGVGKSTQAALLERWLLGLGRAVVRTREPGGTDLGAEIREIVLHRRGDIAPRAEALLYAADRAHHVATVVRPALERGEVVLQDRYLDSSVAYQGAGRVLDAGEVRELSLWAAEGLLPDLTILLDLDETTARARLGSARTRYDRLEAERSEFHARVRAAYLALAAEPQRFLVVDASRPVEEIAAEIRCRLDGRV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23010
Sequence Length: 210
EC: 2.7.4.9
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Q72NL9 | MKNKKPIFVVFEGIDGSGKSTLCKSLTEKLIELGIPSAAFTEPTNLETGKYLRKFLRGEIELGKEEQIEAFLNDREESLKQNILPALNSDKNVLLDRYMYSTAAYQSGDDLSPEMILKKNLNRNFKIPDLLFYLDLSPSIALERLNRRKEGKERFETLAQLEKIRSAYEKILPKDTIRIDGNKNQNQIVQECLEIFLTNIKSKS | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23421
Sequence Length: 204
EC: 2.7.4.9
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B2GAE1 | MSGRFISFEGPDGAGKTSVLTAIRTGLVNQLGDQVVYTREPGGNPIAEQVRAVLLDKQNGAMDDWTEALLYAASRRQHVVETLKPALEAGKLILCDRYLDSSIAYQGGGRELGIDRIWELNQYAIDGLLPDLTIFLDLPVETGLARIEKGRAETINRLDEQTTNFHRRVRQAYLTLAERFPERIVKVNADQELARVIEDVRSAIHARYADLFTN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23939
Sequence Length: 214
EC: 2.7.4.9
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A5VIC6 | MDGKFISFEGPDGAGKTSVIQQIQLELEDQLGTEKVMYTREPGGNKISEQIRQVLFDGQNTDMDGRTEALLFAAARRQHIVSEIIPGLKAGKVILCDRFVDSSIAYQGAGRGLGEKEIWQINQFAIDGLMPALTIYLDIESEIGLKRIAEHRSNQVNRLDEEKLEFHRTVRQSYLKLYQNYPERIELIDASQPLEKVIEDVKATIHDRFSDLF | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24198
Sequence Length: 213
EC: 2.7.4.9
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Q8Y3Y6 | MKAIFITLEGPDGSGKTTVGTLLNQKMTEAGIDFIKTREPGGSPISEKVRNIVLGIGNEEMDPKTEVLLIAGARRQHVVETIRPALAAGKSVLCDRFMDSSLAYQGAGRDMNMEQVLQVNLYAIEDTLPDRTYYLDVPAEVGLARIAANKGREVNRLDKEDITYHEKVQAGYEKVINMFPERFMRVDATKTPEEITETILADILRQLA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23083
Sequence Length: 208
EC: 2.7.4.9
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A0L8T5 | MQGRFITFEGGEGAGKSTQIAQLTQSLQAHGVKVLCTREPGGCPISERIREILVTGQGDDLDGTSELLLILAARHEHIRQVIRPALASGHWVLCDRFEDSTLAYQGGGRGGDGPWLRQLGQWIRGDVFPDLTLLLDLDPTVGLARSKRRGGQEQRFEQEALSFHQQVRQAFLQMAQQEPQRMIPIDADQPVQMVAATIWREVEGRFFVSF | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23419
Sequence Length: 210
EC: 2.7.4.9
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Q30RH7 | MYIAIEGIDTAGKSTQIAKLQEHFSDAIITKEPGGTEAGKEIREIVLNAKIKSKKAEFLLFLADRAEHIQEVIEPNLSKMIISDRSVVSGVAYALVQGEISETAILHLNRFATGGIYPQKIFLLQLTNEELSLRLSQKKLDGIELRGIEYLLKIQDALIKASNLLNIELVLIDATKNIDSITQEILNNINI | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 21182
Sequence Length: 191
EC: 2.7.4.9
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A6Q9Z8 | MYILFEGIDTCGKSTQMELLTQKHPGIITTHEPGGTAFGQQAREILLSDSLRSKRAELLLFLADRAEHYEEVVEPNHDKIVVSDRGFVSGIGYALANGDFDFDELVALNRFALKDHFPDRIILFMTDMETLKQRISEKELDGIELRGLEYLLRVQEHMKESILKLGIPHLFIDATDSIENIHQSILTYLKV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 21773
Sequence Length: 191
EC: 2.7.4.9
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B2V7X0 | MGFFITFEGIEASGKTTQINLLYDYLKSIGKNVIKTREPGGTKIGQKIREILLSKWDEKFPYIAELLLYESDRNIHIQSIVKPSLDAGYIVLSDRYIDSTTAYQHYARGIDYEIVSYLNTLATDGLKPNLTFLIDIPVEISLKRLSESKDRIESEDIEFHKKLREGFLKIAENEKGRFVVIDGTMDIMEIHKIIVDSLKQRSII | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23437
Sequence Length: 204
EC: 2.7.4.9
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Q67JB0 | MSVFISFEGVDGSGKSTQIRLLLQYLDEQSVPYVFTREPGGTPIAEQIRRVLLDPANRGMSVITEALLFAAARAEHVSRTIRPALEEGKVVICDRFVDSSLVYQGVAGGLPVEFLTQINEMATGALRPHRTIVLDLAPEVALARRTGEEADRIERQSREYHQLVREGYLDLARAEPRRVKVVDASRSVEEVQKDIRRLVEEVLPRRFRGAGTRP | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23977
Sequence Length: 214
EC: 2.7.4.9
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Q2LUB1 | MAYFISFEGIEGCGKTTQLKLAAQYLRTLKIPVGTTEEPGGTPLGKKIRNILLNRGPFEICAEAETLLFVAARAQHVREVILPSLARGQWILCDRFSDATAVYQGCVRGIDEAWIRQLDSFATSFLKPNLTLLFDLPAETGLHRAMQRMTGIPENSREDRFEQEGLNFHEKIREGYLALARQESERFRIINAAADIPSIHREVCRHLDVLRQQPEAGLP | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24691
Sequence Length: 219
EC: 2.7.4.9
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A5GQJ8 | MRGRFLVLEGIDGCGKTTQLKALADWLPASGLMPSGAQLITTREPGGTALGQALRQLLLHPPEEQAPATRAELLLYAADRAQHVQTRLEPALAAGDWVLSDRYCGSTAAYQGYGRGLDLDLITQLEQLATAGLQPDLCLWLELSPELAAQRRSGQQQDRIEAEGLAFLARVHQGFAELSQRPLWRRVDASLPPEQVHQQVQHLVREGLELAL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23226
Sequence Length: 212
EC: 2.7.4.9
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Q55593 | MAALFIVLEGIDGSGKTTQGDLLLAHFQRQGLAAVLSPEPTNGPVGRLIRQALQGDLFTYNDARQFEAQMGYLFAADRHYHLYHPGDGVEAKLAQQCHVITTRYYFSSLAYNCHTEADWEFVQRLNQSFPQPDWVIYLDLPVDLALQRLGDRQQLEDQAPRECYEQREKLISVHRNYDRIFAHYQGQLCRLDASLPVEQLHQAIITKVEEML | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24350
Sequence Length: 212
EC: 2.7.4.9
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A0A218QXE6 | MKLDIVLIMFVTFSTTLAQHDEREEWYPFRFGNGHVGCSNRLGMSENDFCRKLCNQDGKWRNSKCKEHYCYCGPQRFYRVIKL | Function: Reversibly inhibits potassium channels.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 9947
Sequence Length: 83
Subcellular Location: Secreted
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A0A218QWZ8 | MKAFYGILIIFILISMIHLSQQVFINATCTLTSQCRPKCLEAIGRPNSKCINRKCKCYP | Function: Potently blocks Kv1.1/KCNA1 (85%), Kv1.2/KCNA2 (91%), Kv1.3/KCNA3 (89%), Kv1.6/KCNA6 (94%), and Shaker (97%).
Sequence Mass (Da): 6723
Sequence Length: 59
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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Q9FQ08 | MELDPDDVFRDEDEDPENDFFQEKEASKEFVVYLIDASPKMFCSTCPSEEEDKQESHFHIAVSCIAQSLKAHIINRSNDEIAICFFNTREKKNLQDLNGVYVFNVPERDSIDRPTARLIKEFDLIEESFDKEIGSQTGIVSDSRENSLYSALWVAQALLRKGSLKTADKRMFLFTNEDDPFGSMRISVKEDMTRTTLQRAKDAQDLGISIELLPLSQPDKQFNITLFYKDLIGLNSDELTEFMPSVGQKLEDMKDQLKKRVLAKRIAKRITFVICDGLSIELNGYALLRPAIPGSITWLDSTTNLPVKVERSYICTDTGA... | Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair. When associated with KU80, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA. Plays a role in maintaining telomere l... |
A5V2F7 | MRNDIADPEGPPRKGRLREEGMAALTLGALGVVFGDIGTSPIYAFREALGQAAEDGIVAGEILGVLSLALWALILVVTCKYVLFLMRADNNGEGGVLALMTLAQRSTRRRRTLVMALGAIGAALFYGDGVITPALSVLSAVEGLKTIPGLEHSVSRGEILLITSAILIGLFLMQARGTRIVGRLFGPVCLVWFVTIGGIGLIHIADQPAILAALLPHNGVLFMANHGVAGMFVMGAVFLTVTGAEALTADMGHFGAKPIRTGWLAIVFPALALNYLGQGAFALHRLEVASARGVEFVNQDWFFLMAPGLARIPLVILATC... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69844
Sequence Length: 648
Subcellular Location: Cell inner membrane
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A6U6M1 | MSQLSAPGAENTRRLLAMALGSVGVVYGDIGTSPLYAFREALRPVSHDGVTDVEIVGLISLMIWALTIIVTIKYVLFLLRADNQGEGGTLSLLALLMKTANGHTAILFFMGIAGAALFIGDAMITPALSVLSAVEGLKLVTPALSDYVVPIAVVILLFLFAVQSKGTAAVSKFFGPITLVWFLVMGAVGFMHIADDLSIFRAFNPYYAVAFLFNEGYVGIVVLGAVFLTVTGAEALYADLGHFGRRPIQWAWFTVVFPALTLNYLGQGAFVLKNPEAMSDPFFLMFPKWALLPAVILATAATIIASQAVITGAFSLTRQA... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69121
Sequence Length: 630
Subcellular Location: Cell inner membrane
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Q8G7Q3 | MAIVALGVVYGDIGTSPLYTAQTFLAGQGGLGSVDREAVLGMLSLVFWSITLITTVKYVLIAMRIDNNGEGGIFALYSLIRKYGAWLAIPAMLGGAAFLADSVLTPAVSISSAVEGLQTLPPLEGLFDENPSLTLMITVVIIVILFSVQSRGTESIGKVFGSMVLVWFGFLAIVGVTNLSNDWSVFEALNPVYGIKFLFSPNNAAGIALMGTVFLSTTGAEALYSDMGHVGRGNIYFTWPFIKVALVLNYFGQGAWMLANSDNPQYTAMESLNPFFQMMSPNVRYLAVILSVSAGVIASQALITGAFTMVSEATRLNWMP... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80558
Sequence Length: 736
Subcellular Location: Cell membrane
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Q74AA5 | MKTEAQSYWGGIIKSMGLVFGDIGTSPIYTLTVIMTLTKPDAEHVLGILSLIVWTLIILVTVEYAWLAMSLGRKGEGGTIVLKEILIRLLKSGRQMAFAGFLAFLGVSLLLGDGVITPAISILSAVEGMRLIPGLEDLAQGGLILVAAVIAVFLFIFQFKGTDKVASAFGPIMVVWFSALTVSGLVSIIGTPTVVQAISPHHAVLFLKHNGLAGFFVLSEVILCATGGEALYADMGHLGRKPIIRAWYFVFCALVINYLGQGAFILRNPEAKNILFSMVKSQVPMLYIPFLLLTISATIIASQALISGVFSIVYQGITTR... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66673
Sequence Length: 605
Subcellular Location: Cell inner membrane
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Q0SIZ9 | MGSGPADEEHTVDTEPGVSPPRRTVGGRETVRAAVVVGALGVVFGDIGTSPIYTIQTVFNPEDPHPVPISTNNVYGVVSLIFWSVMLIVTATYVLLVMRADNDGEGGVMALITLLRRMGAVRGSRVTAVLAGLGIFGAALFFGDSMITPAISVLSAVEGLKVVEPGLEEWIVPITAVIIVALFSVQRRGTAAVGRLFGPVMIVWFVSIGACGVSGIARHPEILKALSPTYALSFFFGHFGIAFFALAAVVLAVTGAEALYADMGHFGRRAITRGWLVLVLPACVLSYLGQGALLLGDQSAVSSPFFLLAPGWARWPMVLL... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70418
Sequence Length: 657
Subcellular Location: Cell membrane
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A7RMN1 | MFSARLVLVFAVVLCIQLCNASWLDERAMTQEKRCNGKYQKCTSNSQCCDQKDYAKRKLRCLTQCDEGGCMKYKQCMFYAGTQK | Function: Neurotoxin that is probably only defensive (Probable). Acts as a voltage-gated potassium channel (Kv) inhibitor (By similarity). In vivo, induces a rapid increase in swimming speed on zebrafish larvae, as well as death which occurs between 2 and 18 hours later .
PTM: Contains 4 disulfide bonds.
Sequence Mass ... |
C0HJC4 | GCKGKYEECTRDSDCCDEKNRSGRKLRCLTQCDEGGCLKYRQCLFYGGLQ | Function: Inhibits voltage-gated potassium channels (Kv1/KCNA) . Is potent on Drosophila Shaker IR channels (IC(50)=94.25 nM), and rKv1.2/KCNA2 (IC(50)=172.59 nM), and moderately active on hKv1.3/KCNA3 (IC(50)=1006.48 nM), rKv1.6/KCNA6 (IC(50)=2245.93 nM), and Kv1.1/KCNA1 (IC(50) around 3 uM) . In vivo, induces a rapid... |
Q8PM33 | MTDPLSRAHAAALDAADPLRNLRDAFVFPQHGDDDQTYFVGNSLGLQPRAARAMVDEVLDQWGALAVEGHFTGPTQWLTYHQLVGDALARVVGAQPGEVVAMNTLSVNLHLMMASFYRPTAERGAILIEAGAFPSDRHAVESQLRLHGLDPATHLIEVEADEPNGTVSMSAIAEAIAQHGPHLALVLWPGIQYRTGQAFDLAEIVRLARAQGAAVGLDLAHAVGNLPLTLHDDGVDFAVWCHYKYLNAGPGAVGGCFVHARHATSDLPRMAGWWGHEQQTRFRMDPQFVPSPGAEGWQLSNPPVLALAPLRASLALFDQA... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 45845
Sequence Length: 423
Pathway: Amino-acid degra... |
Q05979 | MEKALELDGEYPESLRDEFNIPTFKSMGLSSDDKPVTYLCGNSLGLMPKSTRNSINAELDAWSDCAVESHFKHPEEARGKVPWVSIDLPILPLLAPIVGAQENEVAVMNSLTANLNSLLITFYKPTEKRFKILFEKGSFPSDYYAFYNQCKIHGISEPENVFIQIEPREGETYIRTQDILDTIEVNQDELALVCLSGVQYYTGQYFDIGRITSFAHQFPDILVGWDLAHAVGNVPLQLHDWGVDFACWCSYKYLNAGPGGIGGLFVHSKHTKPDPAKESLPRLAGWWGNDPAKRFQMLEVFEPIPGALGFRQSNPSVIDT... | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 51032
Sequence Length: 453
Pathway: Amino-acid degra... |
Q8C8H8 | MELKKDSNAVAIDMLLIVHSEKRRAAQATHLDPQANPGALLQNRGGFQGVRNGIRKWQELEENSFQGNLPEKQCLQQPQVITSYDNQGTQLTVEIHPQDAMPQLLKKFSLAKRLQGDKNGNMRPRQPGGKDAHAYPWDRSSLKSMPLDLRLFEKLDASASQVTVKSGLNELVSDLLQEAHSDLERVRAIWIWICHHIEYDVEAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRVAGVQCVTVPGYSKGFGYQTGQSFSGEFDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKFTFLYNEFYFLTHPALFIEDHFPD... | Function: Probable cytoskeleton-associated protease required for normal muscle growth. Involved in function, maturation and stabilization of the neuromuscular junction. May act by cleaving muscle-specific proteins such as FLNC.
Sequence Mass (Da): 75090
Sequence Length: 661
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q5XGR8 | MSLSVLPRLEQLSSRVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGEPAVPEYISCLKQALIEFNTSIQEIIVTHWHVDHVGGIADISRDIMKGCNFSINKLPRNPHQEEVIADHKYNYLKDGDIITTEGATLRVLYTPGHTDDHMALELLEENAIFSGDCILGEGTAVFEDLYDYMKSLEKLLEMKADKIYPGHGPVVLGARAKIQEYISHRHAREQQILQALQENRGKSFTSMDLVKIVYKDTPEYLHKAAEFNLTHHLQKLKKEGKISEEQSPTVRWRSNL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Endoribonuclease; cleaves preferentially 3' to purine-pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double-stranded RNA or DNA. Required for normal mitochondrial function and cell viabil... |
P02754 | MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI | Function: Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
PTM: Alternate disulfide bonds occur in equal amounts in all variants examined.
Sequence Mass (Da): 19883
Sequence Length: 178
Subcellular Location: Secreted
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P23495 | MRIAIGCDHIVTDVKMAVSEFLKSKGYEVLDFGTYDHVRTHYPIYGKKVGEAVVSGQADLGVCICGTGVGINNAVNKVPGVRSALVRDMTSALYAKEELNANVIGFGGMITGGLLMNDIIEAFIEAEYKPTEENKKLIAKIEHVETHNAHQADEEFFTEFLEKWDRGEYHD | Catalytic Activity: aldehydo-D-galactose 6-phosphate = keto-D-tagatose 6-phosphate
Sequence Mass (Da): 18926
Sequence Length: 171
Pathway: Carbohydrate metabolism; D-galactose 6-phosphate degradation; D-tagatose 6-phosphate from D-galactose 6-phosphate: step 1/1.
EC: 5.3.1.26
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Q9T0A0 | MSQQKKYIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFC... | Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 74508... |
Q9T009 | MTSQKRFIFEVEAAKEATDGNPSVGPVYRSTFAQNGFPNPIDGIQSCWDIFRTAVEKYPNNRMLGRREISNGKAGKYVWKTYKEVYDIVIKLGNSLRSCGIKEGEKCGIYGINCCEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHAEVSIAFVEEKKIPELFKTCPNSTKYMKTVVSFGGVKPEQKEEAEKLGLVIHSWDEFLKLGEGKQYELPIKKPSDICTIMYTSGTTGDPKGVMISNESIVTITTGVMHFLGNVNASLSEKDVYISYLPLAHVFDRAIEECIIQVGGSIGFWRGDVKLLIEDLGELKPSIFC... | Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 74064... |
Q8LKS5 | MEFASPEQRRLETIRSHIDTSPTNDQSSSLFLNATASSASPFFKEDSYSVVLPEKLDTGKWNVYRSKRSPTKLVSRFPDHPEIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQ... | Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (Probable). Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate as substrates . Can use myristate and linolenate as substrates . Functions redundantly with LACS6 in lipid m... |
Q9SJD4 | MEDSGVNPMDSPSKGSDFGVYGIIGGGIVALLVPVLLSVVLNGTKKGKKRGVPIKVGGEEGYTMRHARAPELVDVPWEGAATMPALFEQSCKKYSKDRLLGTREFIDKEFITASDGRKFEKLHLGEYKWQSYGEVFERVCNFASGLVNVGHNVDDRVAIFSDTRAEWFIAFQGCFRQSITVVTIYASLGEEALIYSLNETRVSTLICDSKQLKKLSAIQSSLKTVKNIIYIEEDGVDVASSDVNSMGDITVSSISEVEKLGQKNAVQPILPSKNGVAVIMFTSGSTGLPKGVMITHGNLVATAAGVMKVVPKLDKNDTYI... | Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 78343... |
Q9CAP8 | MIPYAAGVIVPLALTFLVQKSKKEKKRGVVVDVGGEPGYAIRNHRFTEPVSSHWEHISTLPELFEISCNAHSDRVFLGTRKLISREIETSEDGKTFEKLHLGDYEWLTFGKTLEAVCDFASGLVQIGHKTEERVAIFADTREEWFISLQGCFRRNVTVVTIYSSLGEEALCHSLNETEVTTVICGSKELKKLMDISQQLETVKRVICMDDEFPSDVNSNWMATSFTDVQKLGRENPVDPNFPLSADVAVIMYTSGSTGLPKGVMMTHGNVLATVSAVMTIVPDLGKRDIYMAYLPLAHILELAAESVMATIGSAIGYGSP... | Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 76176... |
P83111 | MYRLMSAVTARAAAPGGLASSCGRRGVHQRAGLPPLGHGWVGGLGLGLGLALGVKLAGGLRGAAPAQSPAAPDPEASPLAEPPQEQSLAPWSPQTPAPPCSRCFARAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDIPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMMKENVAFEQEKEGKSNEKNDFTKFKTEQENEAKCRNSKPGKKKNDFEQGELYLREKFENSIESLRLFKNDPLFFKPGSQ... | Function: Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism . Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism . It is unclear whether ... |
Q9EP89 | MYRLLSSVTARAAATAGPAWDGGRRGAHRRPGLPVLGLGWAGGLGLGLGLALGAKLVVGLRGAVPIQSPADPEASGTTELSHEQALSPGSPHTPAPPAARGFSRAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDLPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMVKGTPPPSDQEKELKEKGGKNNEKSDAPKAKVEQDSEARCRSAKPGKKKNDFEQGELYLKEKFENSIESLRLFKNDPLFFK... | Function: Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (By similarity). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (By simil... |
P02920 | MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKT... | Function: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, the synthetic disaccharide lactulose or the analog methyl-1-thio-beta,D-galactopyranoside (TMG), but not sucrose or fructose . The substrate specificity is ... |
P59832 | MKFSELAPRERHNFVYFLLFFFFYHFIMSAYFPFFPVWLADVNHLTKTETGIVFSSISLFAIIFQPVFGLMSDKLGLRKHLLWTITVLLILFAPFFIFVFSPLLQMNIIAGSLVGGIYLGIVFSTAPGVGS | Function: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system).
Catalytic Activity: H(+)(in) + lactose(in) = H(+)(out) + lactose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14959
Sequence Length: 131
Subcellular Location: Cell... |
P22733 | MKKKLVSRLSYAAGAFGNDVFYATLSTYFIVFVTTHLFNAGDHKMIFIITNLITAIRIGEVLLDPLIGNAIDRTESRWGKFKPWVVGGGIISSLALLALFTDFGGINQSKPVVYLVIFGIVYLIMDIFYSFKDTGFWAMIPALSLDSREREKTSTFARVGSTIGANLVGVVITPIILFFSASKANPNGDKQGWFFFALIVAIVGILTSITVGLGTHEVKSALRESNEKTTLKQVFKVLGQNDQLLWLAFAYWFYGLGINTLNALQLYYFSYILGDARGYSLLYTINTFVGLISASFFPSLAKKFNRNRLFYACIAVMLLG... | Function: Responsible for transport of beta-galactosides into the cell, with the concomitant uptake of protons (symport system), and also for transport of homologous and heterologous exchange of beta-galactosides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68289
Sequence Length: 627
Domain: The ... |
Q90617 | MAPPRCPAGLALLLLLLGACGFFQSYAVEVDVKDASNFTCLYAQWMMKFLIKYETNSSDYKNASLDLTSTVTHNGSICGSDTQAALLAVQFGDGHSWSINFTKNNETYRAEFITFTYNTNDTAVFPDARRQGPVTIVVKDAMHPIQLNNVFVCHHTTSLEAENVTQIFWNVTMQPFVQNGTISKKESRCYADTPTAAPTVLPTVANVTTASTTISPAPTTAPKPAENPVTGNYSLKTGNKTCLLATVGLQLNISQDKPLLINIDPKTTHADGTCGNTSATLKLNDGNRTLIDFTFIVNASASVQKFYLREVNVTLLNYQN... | Function: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them... |
P13473 | MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSY... | Function: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live . Functions by binding target proteins, such as GAPDH, NLRP3 and MLLT11, and target... |
Q9UQV4 | MPRQLSAAAALFASLAVILHDGSQMRAKAFPETRDYSQPTAAATVQDIKKPVQQPAKQAPHQTLAARFMDGHITFQTAATVKIPTTTPATTKNTATTSPITYTLVTTQATPNNSHTAPPVTEVTVGPSLAPYSLPPTITPPAHTTGTSSSTVSHTTGNTTQPSNQTTLPATLSIALHKSTTGQKPVQPTHAPGTTAAAHNTTRTAAPASTVPGPTLAPQPSSVKTGIYQVLNGSRLCIKAEMGIQLIVQDKESVFSPRRYFNIDPNATQASGNCGTRKSNLLLNFQGGFVNLTFTKDEESYYISEVGAYLTVSDPETIYQ... | Function: Lysosomal membrane glycoprotein which plays a role in the unfolded protein response (UPR) that contributes to protein degradation and cell survival during proteasomal dysfunction . Plays a role in the process of fusion of the lysosome with the autophagosome, thereby modulating the autophagic process . Promote... |
Q7TST5 | MPGQISAVAVLFLSLTVILHGYQIREKEFPKARGYLQYTATSAEQITTKPLLQLINQRSHITLASRFKDDYIQMAAETSAIENTAHITMKTVTPVTTKSLPPISSASYTFVRSNNAHMTASSTDDTIGSGSIAHLPVPTTRASLAIVNYITGRATQLGGQTTLPKTFFTASHKSTTNQRPTLSTNVLGTSTPTHKDRSTTSPVPLVPRPTLVTWSSPAKIGTYEVLNGSRLCIKAEMGLALIVQEKDLDSATQRYFNIDPSLTHASGKCDSQKSNLFLNFQGGSVNITFTKEENLYYISEVGAYLTISNTEKTYQGKKNT... | Function: Lysosomal membrane glycoprotein which plays a role in the unfolded protein response (UPR) that contributes to protein degradation and cell survival during proteasomal dysfunction. Plays a role in the process of fusion of the lysosome with the autophagosome, thereby modulating the autophagic process. Promotes ... |
Q9UJQ1 | MDLQGRGVPSIDRLRVLLMLFHTMAQIMAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQADIALTRGAEVKGRCGHSQSELQVFWVDRAYALKMLFVKESHNMSKGPEATWRLSKVQFVYDSSEKTHFKDAVSAGKHTANSHHLSALVTPAGKSYECQAQQTISLASSDPQKTVTMILSAVHIQPFDIISDFVFSEEHKCPVDEREQLEETLPLILGLILGLVIMVTLAIYHVHHKMTANQVQIPRDRSQYKHMG | Function: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 31472
Sequence Length: 280
Subcellular Location: Cell membrane
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Q9D387 | MDLRVRTLLGGDRLRILLMFFHVMVQTVAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQAEISLTRGAEVKGHCGHNESELEVFWVDHAYTLRMLFVKESHNTSKGPEATWNLNKVHFVYDSSEKTHFKAPVKVNKYIASSHHLSALVTPAGMSYECQAQQTISLASSDPQKTVTMILSAVHIQPFDIISDFVFSEEHKCPVDEQEQLEETLPLILGLILGLVIVITLVIYHIHHKMTANQVQIPRDRSQYKHMG | Function: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 31721
Sequence Length: 280
Subcellular Location: Cytoplasmic vesicle membrane
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Q5R5V2 | MDLQGRAVPSVDRLRVLLMLFHTMAQIMAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQADIALTRGAEVGRCGHSESELQVFWVDRAYALKMLFVKESHNMSKGPEETWRLSKVQFVYDSSEKTHFKDAVSAGKHTANSHHLSALVTPAGKSYECQAQQTISLASSDPQKTVTMILSAVHIQPFDIISDFVFSEEHKCAVDEREQLEETLPLILGLILGLVIVVTLAIYHVHPQK | Function: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29190
Sequence Length: 261
Subcellular Location: Cytoplasmic vesicle membrane
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B2KPR3 | MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine and ajmalicine) biosynthesis pathway. Catalyzes the methylation of loganic acid (6S,7R) to produce loganin . Weak activity with secologanic acid as substrate. Inactive... |
Q7V8T1 | MSEEQLKAFIAKVQADTSLQEQLKAEGADVVAIAKAAGFSITTEDLEKEHRQTLSDDDLEGVAGGFFCVQGTANRFTINVC | Function: Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria . Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is... |
P14789 | MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-Gly-|-X substrates where X is Ala or Gly . Enhances the elastolytic but not prote... |
P33883 | MIVQIGRREEFDKKLLGEMHKLRAQVFKERKGWDVSVIDEMEIDGYDALSPYYMLIQEDTPEAQVFGCWRILDTTGPYMLKNTFPELLHGKEAPCSPHIWELSRFAINSGQKGSLGFSDCTLEAMRALARYSLQNDIQTLVTVTTVGVEKMMIRAGLDVSRFGPHLKIGIERAVALRIELNAKTQIALYGGVLVEQRLAVS | Function: Required for the synthesis of PAI consisting of 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation.
Catalytic Activity: a fatty acyl-[ACP] + S-adenosyl-L-methionine... |
P80171 | MNPNCARCGKIVYPTEKVNCLDKFWHKACF | Function: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell typ... |
Q99MZ8 | MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGIEPERREAQDSSSYRRPTEQQQPQPHHIPTSAPVYQQPQQQQVTPSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI | Function: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell typ... |
Q24188 | MGCATTSVKIASIVLNAVLGFLAAGAIGWIAYNADTETEEFVIAAYIACSLILVFALLGIFAAIRESVVLTATSAVFLLILAILQIVSTCLFLHEFDVKSGRDMVEVAWQANNMDSLQQKHECCGQSSAQDYIHLSLLIPPSCYADLQQTPDHLYLDGCIEKVQSFYESDKLRFIIVSWVLVAFELICFALAVFLAISFKNKQRRMEF | Function: Facilitates synapse formation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23005
Sequence Length: 208
Subcellular Location: Membrane
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Q06379 | MNKKHGFPLTLTALAIATAFPAYAAQAGGATPDAAQTQSLKEITVRAAKVGRRSKEATGLGKIVKTSETLNKEQVLGIRDLTRYDPGVAVVEQGNGASGGYSIRGVDKNRVAVSVDGVAQIQAFTVQGSLSGYGGRGGSGAINEIEYENISTVEIDKGAGSSDHGSGALGGAVAFRTKEAADLISDGKSWGIQAKTAYGSKNRQFMKSLGAGFSKDGWEGLLIRTERQGRETRPHGDIADGVEYGIDRLDAFRQTYDIKRKTREPFFSVEGERESKPVAKLAGYGKYLNNQLNRWVKERIEQNQPLSAEEEAQVREAQAR... | Function: Unknown. May be an iron-siderophore receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105681
Sequence Length: 943
Subcellular Location: Cell outer membrane
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Q54LL8 | MELIEEIINLDEAIQGETRTEIIYTKSQTPSNIKIIVIAGNPGIESFYQEFVKVLNLSFNSKYDIYGVGHIGHCGKIENKTFSVEEQIKHKELFLEYLLKNKYGDKDRKDIKFILIGHSVGSYISLKVVSRFSEKFEFLSVVNLFPTFKNLYDGLSPFIKMVVMRESTRNGLSTFLHYIPSIVVSNVLKWILPSDESRIAVQSKINYYSALNILYMAYTETEDIKEIDDECHSVFNSRLNQLLFIYGQTDSYTPKSFYDEMKQLYPAGNIEYSSSYVPHAFVLHHSQEVALRVSEWLSLNILKN | Function: Probable serine lipid hydrolase associated with lipid droplets. Appears to lack cholesterol esterase activity. Appears to lack triglyceride lipase activity.
Sequence Mass (Da): 35128
Sequence Length: 304
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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Q9W0H3 | MQEAYVNINSIPTHIFTWGRWIEETITEKEIVICITGNPGLPGFYTEFAGTLQKELGDLPVWVIGHAGHDDPPEASIREVPQLSGNEELFNLDGQIRHKIAFIEKYVPSDVKIHLIGHSIGAWMILQLLENERIRSRIQKCYMLFPTVERMMESPNGWVFTKVAMPLYSVFGYIFFSFFNFLPVWLRLMLIQIYFLIFSIPRQFLGTALKYSKPSVAEKVVFLADDEMARVRGIQREIVEQNLDLLKFYYGTTDGWVPISYYDQLKKDYPKVDAQLDTKKIDHAFVLRHSQPMAVIVRDMIQQHRRV | Function: Probable serine lipid hydrolase associated with lipid droplets (By similarity). Appears to lack cholesterol esterase activity . Appears to lack triglyceride lipase activity . Involved in negatively regulating juvenile hormone (JH) and possibly, insulin signaling activities such as triacylglycerols (TAG) stora... |
Q9H6V9 | MDSELKEEIPVHEEFILCGGAETQVLKCGPWTDLFHDQSVKRPKLLIFIIPGNPGFSAFYVPFAKALYSLTNRRFPVWTISHAGHALAPKDKKILTTSEDSNAQEIKDIYGLNGQIEHKLAFLRTHVPKDMKLVLIGHSIGSYFTLQMLKRVPELPVIRAFLLFPTIERMSESPNGRIATPLLCWFRYVLYVTGYLLLKPCPETIKSLLIRRGLQVMNLENEFSPLNILEPFCLANAAYLGGQEMMEVVKRDDETIKEHLCKLTFYYGTIDPWCPKEYYEDIKKDFPEGDIRLCEKNIPHAFITHFNQEMADMIADSLKD... | Function: Probable serine lipid hydrolase associated with lipid droplets. Appears to lack cholesterol esterase activity. Appears to lack triglyceride lipase activity. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages.
Sequenc... |
Q8BVA5 | MASEVEEQIPVREEFFLCGGVETKIIKCGPWTNLFEKQDVSKPKQLIFIIPGNPGYSAFYVPFAKALYTLMKSRFPVWIISHAGFSVTPKDKKVLAAPQEESNAQKIEDVYGLNGQIEHKIAFLRAHVPKDVKLILIGHSVGTYMTLHVMKRVLELPVAHAFLLFPTIERMSESPNGKFATPFLCQFRYLLYATSYLLFKPCPEVIKSFIIQKLMGQMNIKLELPLTDILQPFCLANAAYLGSQEMVQIVKRDDDIIKEFLPKLKFYYGKTDGWCPVKYYEDMKKDFPEGNIYLCEKGIPHAFVLDFSQEMATIVAEWIN... | Function: Probable serine lipid hydrolase associated with lipid droplets . Appears to lack cholesterol esterase activity . Appears to lack triglyceride lipase activity . Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages .
Seq... |
P25587 | MFVVDWSVQLCMGVISPLFRALVQLPLSIFVWNGFQLVALPINIPLRLFLGTSLSRLVAQTSTLDFYVVLTLFQYFAVLCAFGSIIGLIFGFILGVFHSICGVPSVYISLEWKRWFAPIRTVLERASTSIVNIMRGQTIAPIPMPKPNPTHISKPNMKKFHDEPGADDMTITHDVNCYITPCQTPTNEKIQHYNNDSFNTTTTDDEPTDIWDRSDTYQNSFVTNETLMSLSNRAKLRRNASDADIVNIKILRRNSR | Function: May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29024
Sequence Length: 256
Subcellular Location: Membrane
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Q86U70 | MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPTRQQPSKRRKRKMSGGSTMSSGGGNTNNSNSK... | Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts... |
P70662 | MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSK... | Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors . May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions . Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1 . A... |
P70060 | MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKESFHNNFVSLDCDQCTMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDER... | Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. Acts as a coactivator together with otx2 to stimulate lhx1/lim1-mediated activation of the gsc promoter in the Spemann organizer. Acts synergistically with lhx1/lim1 and ssbp in axis formation.
PTM: Undergoes rnf12-media... |
Q6NVL6 | MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKESFHNNFVSLDCDQCTMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPNKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQDVMVVGEPTLMGGEFGDEDERLI... | Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. Acts as a coactivator together with otx2 to stimulate lhx1/lim1-mediated activation of the gsc promoter in the Spemann organizer. Acts synergistically with lhx1/lim1 and ssbp in axis formation (By similarity).
PTM: Under... |
O43679 | MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPDVMVVGEPTLMGGEFGDEDERLI... | Function: Transcription cofactor. Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors.
PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome.
Sequence Mass (Da): 42793
Sequence Length: 373
Subcellular Location: Nucleus
|
P0DQV8 | DAEPPSPAEECAAVKMESCGDDWLYIDENRKVKYFETPKTFQEAQDHCESEDGNLVAMHTEFQKYVVACLSWIYNHKLHRMWIGAGRSEGETQNIDGSDFDYAKWKGGQPDNFGGNEDCIEANFIDWGYLNDVECSEKLPFMCA | Function: The role of this hemagglutinin in the venom is unknown, because it is masked by the high venom hemolytic activity. Lectin with specificity to galactose. Induces hemagglutination.
PTM: Glycosylated with a carbohydrate of 383 Da.
Sequence Mass (Da): 16450
Sequence Length: 144
Subcellular Location: Secreted
|
Q40987 | MAFYRTNLPTRELFSLVSVVIVLLATNINSVQALSFNFTKLTTANSGVTFQGDAQILPSGLIALTKSSPFPPGQYFTTVGRALSSNLVPLWDSATGKAASFVTSFSFVIDTTEGPITDGLIFFIAPPGTVIPQNSTTPFLGVVDSETSINRFVGLEFDLYRNSWDPEGRHIGIDINSIISTKTVTYNLVSGSLTKVIIIYDSPSSTLSAAIIYENGKISTISQVIDLKTVLPNTVQIGLSAATLTGESYSIHSWSFVSDLETTASYVSNI | Function: Involved in symbiosome development.
PTM: Glycosylated in a boron-dependent manner. Glycosylation is required for localization to symbiosomes. 3 different glycosylation variants, NLEC-1A, NLEC-1B and NLEC-1C, have been identified.
Sequence Mass (Da): 28958
Sequence Length: 270
Subcellular Location: Symbiosome
|
P18839 | QNWAKFQEKHIPNTSNINCNTIMDKSIYIVGGQCKERNTFIISSATTVKAICSGASTNRNVLSTTRFQLNTCIRSATAPRPCPYNSRTETNVICVKCENRLPVHFAGIGRC | Function: The S-lectins in frog eggs may be involved in the fertilization and development of the frog embryo. This lectin preferentially agglutinate a large variety of tumor cells, but it does not agglutinate non-transformed cells and erythrocytes.
Sequence Mass (Da): 12326
Sequence Length: 111
Subcellular Location: Se... |
P44620 | MIYFTMFLLGGILGIALWFYLSGFITRLQQNIYAIYVELFPQNRSPFQPHFASIQQKKCGHILRYFFSIGVGFIFLQIAFKDSIFTVWIGLTLIILWTISYLDWHYQLISTTPCLWLLTLGLFGADNNFSLLTLSESIKSAASFFIVFYVIYWLAKFYYGKEAFGRGDYWLAMALGSFIHLETLPHFLLLASVLGICFSLIHRKKKEFLPFAPFMNLSAVIIYFVKYYGY | Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory appara... |
P15754 | MVENIALLPEFAAQYPFLWGSFLFLSGLAFGSFFNVVIHRLPLMMEQAEGINLCFPASFCPQCREPIAWRDNIPLLGFLFLKGRSRCCGQPISPRYPLMELATGALFVLAGYLMAPGVPLLGGLILLSLLLILAAIDAQTQLLPDGLTLPLMWAGLLFNLSATYVPLAEAVVGAMAGYLSLWSVYWVFRLLSGKEALGYGDFKLLAALGAWLGWQALPQTLLLASPAA | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
O68433 | MINALIINYPWFMYLVVGLFSLAVGSLLNVIIYRLPIILQEEWKEQCCELFHFEQRKEKIKLNLFLPRSFCPHCKAMVKAWQNIPLLAILVLRGRCYQCDSPFSIRYPFVETLTTVLSLYASWHFGFTIQLLFALLAIWILISLVFIDLDHQLLPDSLTLGLLWIGLIANTQNVFVSLDVAVLSCAGAYLALWLFINLFYLMTCKVCMGHGDFKLFAAFGAWLGWMYLPIILLISSITGAIIGLIYLKINGKSRDTAIPFGPFLCISGLIAMFWGDSIINWYIGYWM | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
O30387 | MTHSSLPGYFGPLFAVFLFVLGLCVGSFLNVVIARVPLDQSIVRPRSRCPRCGHVLAWYENIPLLSWLALRARCRGCGVPISVRYPLVELLTGLLFFACLRRFGWTYELVPALVLVSLLVPLAFIDLDHWILPLSMTVPGMLAGIALAFPLGMDAFRDALMGAAVGFLSFRMMEYVGWKVFQREALGAGDKYLVAMLGAFLTWRALLGVLLFASMQGAVVGILMLLATGRAGPRTENTQDEPAGDAPPLTMTWEFTQPGLPLWKRLLLVPVCLLVQPIPDAPLDEEGEEEEWVPERTSIPFGPWLALAGLELLLLGPWLS... | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
P33566 | MSDLSVLSPFAVPLAAVLGLLVGSFLNVVIYRVPVMMERGWTVFAKEHLNLPLTDDESRTFNLMKPDSCCPKCRVPIRAWQNIPIVSYLLLRGKCASCQTKISIRYPLIELLTGVLFGLVAWQYGWSWITLGGLILTAFLISLTFIDADTQYLPDSMTLPLIWLGLIFNLDGGFVPLQSAVLGAVAGYSSLWLLCAVYKLLTGKTGMGNGDFKLIAALGAWLGISALPVLIFVSSLIGLVAAIVMRVAKGRHFAFGPALTVSGWIIFTANDSVWRAVNWWLTHPVR | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
P31712 | MDDLREFAQLFPAWWFGALGVLGLIVGSFLNVVIYRLPIMLERRWRQDIELETGVADPDTRYNLWWPPSSCPHCQQAIAVKDNIPLFSWLWLRGRSRCCHQSVSVQYPLVEVITMLAFLAAGLLWLPGMALWGALILLSFLLVLTVIDIKTLLLPDELTLSLLWMGLLFNLSGTFVSLNDAVVGAMAGYLSLWLLYWAFKYATGKEALGYGDFKLLAALGAWLGWQALPNLVLVAALSGLVVTLIWRGLRKEDTAKPLAFGPWLAIGGVFGMIMNGFNL | Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory appara... |
P22610 | MPLLDYLASHPLAFVLCTILLGLLVGSFLNVVVHRLPKMMERNWKAEAREALGLEPEPKQATYNLVLPNSACPRCGHEIRPWENIPLVSYLALGGKCSSCKAAIGKRYPLVELATALLSGYVAWHFGFTWQAGAMLLLTWGLLAMSLIDADHQLLPDVLVLPLLWLGLIANHFGLFASLDDALFGAVFGYLSLWSVFWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQILPLTILLSSLVGAILGVIMLRLRNAESGTPIPFGPYLAIAGWIALLWGDQITRTYLQFAGFK | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
Q9ZEL6 | MTPVEFLASNPLAFVLCALVLGLLVGSFLNVVIHRLPIMMQRDWQSQAREFLELPAEPAGAAFNLFLPHSRCPHCDHQIRAWENIPLISWLALRGKCSACKASISKRYPLVELACGLLSGYVAWHFGFSWQAGAMLLLTWGLLAMSMIDVDHQLLPDSLVLPLLWLGLIINSFGLFASLEDALWGAVVGYLALWSVYWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQVLPLTILLSSVVGAVLGTVMLRMQKAESGTPIPFGPYLAIAGWVALLWGDQITASYLQFARL | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
P72640 | MDPLIAPLAFLLAIALGCAVGSFLNVVAYRLPEGLSLVHPPSRCPHCGHRLGPKENVPVVGWLWLRGKCRWCQTAISPRYPLVEAATGFLFALTCWRFGWQWQTFGYWILISFLISLTLIDWDTMTLPNSLTKPGLVLGLLFHLLLGWQRGHWIVPLVEAIASAVLGLWLFDLIRMGGSLLLGREGMGDGDPKLASMVGAWLGWPSLLLTTFIACFIGSIYGGLKLLLGTLQRRQGFPFGPFLAIGALISLFWGEKLITSYLNFVTPQF | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N... |
A5F385 | MEYVYLILFSIVSLILGSFSNVVIYRLPRKILLKNHFFYDIDSNRSMCPKCGNKISWYDNVPLLSYLLLHGKCRHCDEKISLSYFIVELSFFIIAFPIYWLSTDWVDSFVLLGLYFILFNLFVIDFKSMLLPNLLTYPIFMLAFIYVQQNPALTVESSIIGGFAAFIISYVSNFIVRLFKRIDVMGGGDIKLYTAIGTLIGVEFVPYLFLLSSIIAFIHWFFARVSCRYCLYIPLGPSIIISFVIVFFSIRLM | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
Q56740 | MDALQYYPWLYIGLASLFGLLVGSFLNVVIYRLPKIMELEWRQECAESFPEYNITPPTETLTLSTPRSSCPSCHTPIRVRDNIPVFSWLALRGKCHHCQTKISARYPFVEALSAFLCGLVAWKFGYAPITVALIGFTLVLIAATFIDLDTMLLPDQLTLPLTWTGIALALLEISPVSLQDSVFGAMAGYLCLWSVYHLFRLLTGKEGMGYGDFKLLAALGAWLGWQYLPMIILLSSVVGLIFGLIQLRLQKQGIEMAFPFGPYLAIAGWVALMWGDSLMSWYLNYLIGA | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino ... |
Q56763 | MAFLDQHPGLGFPAAAGLGLLIGSFLNVVILRLPKRMEWQWRRDAREILELPDIYEPPPPGIVVEPSHDPVTGDKLKWWENIPLFSWLMLRGKSRYSGKPISIQYPLVELLTSILCVASVWRFGFGWQGFGAIVLSCFLVAMSGIDLRHKLLPDQLTLPLMWLGLVGSMDNLYMPAKPALLGAAVGYVSLWTVWWLFKQLTGKEGMGHGDFKLLAALGAWCGLKGILPIILISSLVGAVLGSIWLFAKGRDRATPIPFGPYLAIAGWVVFFWGNDLVDGYLRFAGLR | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
Q7UX15 | MASKSSRSQEHIRNFCIIAHIDHGKSTLADRLLESTGTVDNRGKKTQMLDDLALEQQRGITIKARAVAMRYKRDGIEYELNLIDTPGHVDFQYEVSRSLACCEGALLLVDAFQGVEAQTVANAFAAMEHDLTIVPVINKIDLIHARPDEVAEEMMNSLGTDPDECKRVSAKTGEGVAALLDAIVDSVPAPTGDPKAVLQAMVFDSNYDDFRGAITYIRVMQGTVRKGQKIKFLRAGSVHDVVELGQFAPSRVPCDELVAGQVGYLICNIKSLGDVHIGDTISIAGNDPAPALPGYDRPKRMVYCGLFPSDGQDFSELRDA... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
Q88T65 | MKQSHIRNFAIIAHIDHGKSTLADQIMSLTQTVSAREQHAQLLDDMTVEQAHGVTVKARTVRNYYQADDGQEYEYNLIDTPGHVDFNYEVAKSLAATEGAILLVDATQGVQAQTIANYRIAKQRQLTLIPVLNKVDLPSADIDAALAQLNDLDSAFTPEQVLQISAKTGQGVPAVLEAIKQRLPAPQGDLHQPLKALVFDSLYDPYQGVIAYVRLIDGQLKSQQALCLMQGQQDFNGKAIGVFAPQMHPQESLSAGDVGYVVTGIKDPRKVRVGDTLTSVATPTQRPLAGYQPAKSMVFAGLYPKNNDYPALKEAVQKLN... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
A9KF98 | MTTISQKFIRNFSIIAHIDHGKSTLADRFIQLCGGLSEREMKAQVLDSMDIERERGITIKAQSVTLNFKSQDGHFYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAAQGVEAQTVATCYTAIEQGLVVLPVLNKIDLPQADPERVIQEIEDVIGIEAHDAIRVSAKEGRCVKELLEQLVVAIPPPVGDPEAPLQALIIDSWFDSYLGVVSLVRVKAGTLRKGDKIRVMSTGKDYYADQIGHFTPKRQPLEELSAGAVGFVVAGIKDIFGAPVGDTLTHAKQSAGSPLPGFKQVKPQVFAGLFPINSEEYEPFREALA... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
Q6A9B2 | MSAPQPGSTDPAVIRNFCIIAHIDHGKSTLADRMLQITGVLDERSARAQYLDRMDIERERGITIKSQAVRMPWEVDGVTHLLNMIDTPGHVDFSYEVSRSLQACEGAILLVDAAQGIEAQTLANLYLALEADLEIIPVLNKIDLPGAESDRHAAEIAGIIGCDESEVLRVSAKTGEGVSDLLDTIVAKVPAPEGVADAPARALIFDSVYDTYRGVVTYVRVVDGALRHREKILMMSTGAAHEVLEIGVISPEMVPAQGLSVGEVGYLITGVKDVRQSRVGDTVTNASKPSEKDLGGYQHPKPMVYSGLFPIDAKDFPDLR... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
Q0JEU6 | MAHLLFLPILQLLLLYCTKSAQAQLNISIGSSLTPQGVNNSWISPSADFAFGFLAVDGNSSSYLLAVWFNKIADKTVVWYARTSSNGKDDTIPVQVQSGSVLKLADGALSLRDPSGNEVWNPQVTDVGYARMLDTGNFRLLGTDGATKWESFGDPSDTILPTQVLSLGTALHSRLLATDYSNGRFQLKVQRDGNLVMYPDAVPSGYLYDPYWASNTVDNGSQLVFNETGRIYFTIINGSQVNITSAGVDSMGDFFHRATLDTDGVFRQYVYPKNIHARPLWPEQWTAVDVLPENICQSIQTMVGSGACGFNSYCTIDGTK... | Function: Involved in resistance against the herbivorous insect brown planthopper (N.lugens, BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I me... |
A0R758 | MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELER... | Function: Kinase that has a preference for L-erythrulose, producing L-erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro.
Catalytic Activity: ATP + L-eryt... |
Q6D8V6 | MTYLFNQPSSFARELTEGFVAAHADKVRQVPGGVVRSTRSREGGVAIVVGGGSGHYPAFAGLVGQGLAHGAAMGNLFASPSAQQICSVARAAHNGGGVLLTFGNYAGDVLHFGQAKARLNAEGIPCELLAVTDDISSAPLNEWQKRRGVAGDLMVFKAVSAAAEAGYDLAAVLEVAERANQRTRSLGVAFSGCTLPGAEHPLFTVPEGMMAVGMGIHGEPGIRDVPISTADELAELLVSSLLKEVPHGITTLSGQRISVVLNGLGGVKYEELFVVYRRVSQLLVEQGLTVVEPEVGELVTSFNMAGLSLTLFWLDEELER... | Function: Involved in catabolism of D-apiose. Catalyzes the phosphorylation of L-erythrulose to L-erythrulose 1-phosphate . Can also phosphorylate D-erythrulose and dihydroxyacetone in vitro .
Catalytic Activity: ATP + L-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate
Sequence Mass (Da): 61435
Sequence Length: 590... |
O95214 | MAGIKALISLSFGGAIGLMFLMLGCALPIYNKYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGIVVSAFGLPIVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW | Function: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14428
Sequence Length: 131
Subcellular Location: Membrane
|
Q9CQ74 | MAGIKALISLSFGGAIGLMFLMLGCALPIYNQYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGIVVSAFGLPVVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW | Function: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14414
Sequence Length: 131
Subcellular Location: Membrane
|
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