ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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A0A1Z3GBK8 | MGIVALILIKAAMSLILSSFPLFRSSRSSPASASLAGSGLPKTTPPKTASLQSHSPMFEETKGRIAKLFKKNEVCISTYDTAWVGMVPSPFSSDQPCFPDSLFWLLDNQCPDGSWAQPHHHSHSHSPSLLNKDVLSSTLASILALHKWGLGQHHIAKGLHFLELNFASATDNSQITPLGFDIVFPAMLDHAADLSLNLRLDPTTLNDLMNRRDLELQRCTENGSAETEVYMAYIGEGMGKLHDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSALNKFGSAVPAVYPLDIYSQLCIVDNLERLGISRFFSTEIQSVLDETYRCWLQGDEEIIMDASTCGLAFRTLRMNGYKVTSDSFIKVVQDCFSSPGHMRDVNTTLELYRASELMLYPHEIELEKQNSRLRSLLEQELSGGSIQSSQLNAEVKQALDYPFYAALDRMVKKKTIEHYNIDDSRILKTSFRLPSFGNKDLLSLSVQDYNRCQAIHREELREFDRWFVENRLDELEFARHKSAYYYCYFAAAATFFAPELSDARMSWAKNALMTTMVDDLFDVTGSVEEMKNLIQLVELWDVDVSTECCSHKVQILFSALKRTICEVGDRAHQLQGRSIRSHIIVIWLDLLHSMMKEVEWTRDKFVPTMDEYVSNAHVSFALGPIVLPALYLVGPKLSEEMVNHSEYHNLFKLMSMCGRLMNDIRGYEREHDDGKLNAMSLYIMNNGGEITPEVAILEIKSWNDRHRRDLLRLVLEEKSVIPKACKDLFWHMCSVVHLFYNKDDGFWSQELIEVVNQVIHQPILLNHF | 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-CPP) to ent-atiserene .
Catalytic Activity: ent-copalyl diphosphate = diphosphate + ent-atiserene
Sequence Mass (Da): 91743
Sequence Length: 806
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.185
|
A0A1D6KUI6 | MASLSFASSHASLFCCQQSSSAIILRPAGALLRLSRRQPSSHTISTTDQLFPRRSRMPRNVDTHAAAERNSPSTMSSLEAVDELETNGDSAVVVVREQQQQQHLLMGATDDGLPPSPYDTAWVAMVPAPGNPLVPRFPQCVDWILQNQRSDGSWGPDGGSGDHPSSPLGKDALMSTLACVLALKTWDAGEEHVRKGLSFVGNNSPSCVMTGDERDAPVGFSVIFPGMLARAIDMGLDIPMMTQANVDAFIRLRDTELNRMAATTGSKAFMSYVAEGLGDVLDWDEAAMVYQRQNGSFFNSPATTAAAAIHGNNDRALRYLDSLVNMFGSSVPTVYPRSTYSRLHMVDTLQKMGLSRSFVSEINEMLDMTYRSWLANDDEEMMLDMSTCAMAFRLLRMHGYDVSSDGLAQFSSESSFRDSVHGQANDTEALLELYKASQIQITEDELVLVDIRSWSAKLLKEQLGSDKVSRSVDAQEVQQVLKFPFYTTLDRLEHRRHIEQFKAGGFHMLKSAYRFCKEDEELVSLAVQGFHSSQALYQQELQFLTRWAKEARLHDLEFARIMPMNTFFPNAALMYAPELSEARILCTKNCMLATAVDDLFDVGGSREEMENLVRLIDMWDEHEEVGFCSERVEILFRAIYDTSKELAAKAMAVQNRSVINHVAELWADLVRAMMTEAEWSMRGHVPSSMEEYMQVAETSFALGPIVLMPLYLIGPELPEAVVRCPEYKQLFHHMNVCGRLLNDLQSYEREAKQGKINSVLLVAPRHGGSIEAAKSEVRRAIEASRRELLRMLVAEADATVPRPFRQEFWNMCKMVHLFYMEDDCYSSPKELVHAANMVVFDPLRVREL | 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-copalyl disphosphate (ent-CPP) to dolabradiene .
Catalytic Activity: ent-copalyl diphosphate = diphosphate + dolabradiene
Sequence Mass (Da): 95121
Sequence Length: 848
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Plastid
EC: 4.2.3.196
|
Q0JEZ8 | MASPMEAVARSSLVLAPRRRRALGLLPAAAAAAPFVLDCRRRHNGGMRRPHVSFACSAELDTGRRQLPSTGTRAVMSSCPGYVEGRMVGENTSQINMGWEARILRHLENPEFLPSSYDIAWVAMVPLPGTDHLQAPCFPECVEWILQNQHSNGSWGVNEFDSSASKDILLSTLACIIALEKWNVGSEQIRRGLHFIAKNFSIVIDDQIAAPIGFNLTFPAMVNLAIKMGLEFPASEISIDQILHLRDMELKRLAGDESLGKEAYFAYIAEGLEESMVDWSEVMKFQGKNGSLFNSPAATAAALVHRYDDKALGYLYSVVNKFGGEVPTVYPLNIFSQLSMVDTLVNIGISRHFSSDIKRILDKTYILWSQRDEEVMLDLPTCAMAFRLLRMNGYGVSSDDLSHVAEASTFHNSVEGYLDDTKSLLELYKASKVSLSENEPILEKMGCWSGSLLKEKLCSDDIRGTPILREVEYALKFPFYATLEPLDHKWNIENFDARAYQKIKTKNMPCHVNEDLLALAAEDFSFCQSTYQNEIQHLESWEKENKLDQLEFTRKNLINSYLSAAATISPYELSDARIACAKSIALTLVADDFFDVGSSKEEQENLISLVEKWDQYHKVEFYSENVKAVFFALYSTVNQLGAMASAVQNRDVTKYNVESWLDYLRSLATDAEWQRSKYVPTMEEYMKNSIVTFALGPTILIALYFMGQNLWEDIVKNAEYDELFRLMNTCGRLQNDIQSFERECKDGKLNSVSLLVLDSKDVMSVEEAKEAINESISSCRRELLRLVVREDGVIPKSCKEMFWNLYKTSHVFYSQADGFSSPKEMMGAMNGVIFEPLKTRGN | 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 Mass (Da): 94956
Sequence Length: 842
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Plastid
EC: 4.2.3.35
|
A0A1Z3GCD1 | MFSSSLKLKTNPLMDNKIHRSSSDRDFRGSTISSVKCSLNNSEDLIVKVRERVKGKVEISPSAYDTAWVAMVPERDYSGQKPRFPECLDWIVENQNADGSWGVQSSSMLKHSLSCTLACLLPLRKWNVASPQLLRNGVEFIRSSSSAATDKNQISPIGFDIVFPMMIQYANDLNLELLLNQDLVNILFQNREAQLTRNKNLEYVAEGLGSSIDWNKVLMHQRSNGSLFNSPATTAAALIHRHDKKCLEYLNSLLSIYKTWVPTIHPMDVYARLCLVDHLQGLGVDRFVHPEIEVVLQETFRLWQQKDDKIFTDATCRAMAFRLLRMQGYHVTPDELGGYVDEESFFATVSFESSGTDTVLELYKASQVRLPEDDDTLEKLHDWTSKFLKQKLQSKTILDQQLERKVEFNLKNYHGILDAVKHRRNFDLYDIDHRRILKTAYRCPTVYNEDILLLTAQDLMTRQVQNQKELQIMERWLEDCRLDKVSGRNAVLVSYFLNANNFPDPRLSEARLAYAKTVTLITFLDDFFDHHGSREDSLLIMELINKWTEPLTVSYPSDEVEILYSALHATITDTAEKVYAVQGRCIKSLIIELWMEVLTAMLGEMDSCNADTPPDFDEYMAFAPKSLGCSLSILPSLHLMGETISEEMVTSLECFELDKHVSIAIRLLNDQQTFERERKERTTNSVTLLMDADQISEEEAVSRIQKLIEHHTKELLKLVVQKEGSVLPRKCKDIFWNTIKVGYCLYRFSDEFTSPQQMKEDMKLLFHDPVLKTTP | 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 ((+)-CPP) to isopimaradiene .
Catalytic Activity: (+)-copalyl diphosphate = diphosphate + isopimara-8(14),15-diene
Sequence Mass (Da): 89113
Sequence Length: 775
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.-
|
A4KAG8 | MMLPMSSACSGGQFPGASPHGIIPKQFSRAPRIRVSIRGAAGVEKSLGLGRNAGSQQGMHKNELHDKIRKQLRDVQLQPSSYDTAWVAMVPVQGSHQTPRFPQSIEWILQNQYDDGSWGTNLPGLVVNKDILLCTLACVVALKRWNTGRDHISRGLNFIGRNFSVAMDEQTVAPVGFNITFSGLLSLATRTGLELPVMQTDIDGIIHIRKIELERDAYGTASSRRAFMAYVSEGLGNLQDWNQVMAYQRKNGSIFNSPSATAATIIHGHNYSGLAYLDFVTSKFGGPVPVMYPQNAYSQLCMVDTLERMGISESFACEISDILDMTYRLWMHNEEELMLDMRTCAMAFRLLRMHGYDITSDGMAQFVEQSSFDDSIHGYLNDTKALLELYKSSQLRCLEDDLILEEIGSWSARVLLEKISSKMIHISELPEVEYALKCPVYAILERLEQKRNIEQFKTKEQLKIEGFKLLKSGYRGVIPNDEILALAVDEFHSSQSVYQQELQDLNSWVAHTRLDELKFARLMPSITYFSAAAVLLPSESARIAWTQNCILTTTVDDFFDGEGSKEEMENLVKLIEKWDDHGEIGFSSECVEILFYAVYNTSKQIAEKAMPLQKRNAVDHIAESWWFTVRGMLTEAEWRMDKYVPTTVEEYMSAAVDSFAVGPIITSAALFVGPELSEEVFRSEEYIHLMNLANTIGRLLNDMQTYEKEIKMGKVNSVMLHALSHSGGGRGSPEASMEEAKREMRRVLQGCRFELLRLVTRDAGVVPPPCRKLFWLMSKVLHFVYMEKDRYFTAEGMMASANAVILDPLQVTLPPSDSGTL | 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 (Da): 92408
Sequence Length: 821
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.103
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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 | MELDPDDVFRDEDEDPENDFFQEKEASKEFVVYLIDASPKMFCSTCPSEEEDKQESHFHIAVSCIAQSLKAHIINRSNDEIAICFFNTREKKNLQDLNGVYVFNVPERDSIDRPTARLIKEFDLIEESFDKEIGSQTGIVSDSRENSLYSALWVAQALLRKGSLKTADKRMFLFTNEDDPFGSMRISVKEDMTRTTLQRAKDAQDLGISIELLPLSQPDKQFNITLFYKDLIGLNSDELTEFMPSVGQKLEDMKDQLKKRVLAKRIAKRITFVICDGLSIELNGYALLRPAIPGSITWLDSTTNLPVKVERSYICTDTGAIMQDPIQRIQPYKNQNIMFTVEELSQVKRISTGHLRLLGFKPLSCLKDYHNLKPSTFLYPSDKEVIGSTRAFIALHRSMIQLERFAVAFYGGTTPPRLVALVAQDEIESDGGQVEPPGINMIYLPYANDIRDIDELHSKPGVAAPRASDDQLKKASALMRRLELKDFSVCQFANPALQRHYAILQAIALDENELRETRDETLPDEEGMNRPAVVKAIEQFKQSIYGDDPDEESDSGAKEKSKKRKAGDADDGKYDYIELAKTGKLKDLTVVELKTYLTANNLLVSGKKEVLINRILTHIGK | 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 length. Acts as a negative regulator of telomerase. Required for maintenance of the telomeric C-rich strand.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 70291
Sequence Length: 621
Subcellular Location: Nucleus
EC: 3.6.4.12
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A5V2F7 | MRNDIADPEGPPRKGRLREEGMAALTLGALGVVFGDIGTSPIYAFREALGQAAEDGIVAGEILGVLSLALWALILVVTCKYVLFLMRADNNGEGGVLALMTLAQRSTRRRRTLVMALGAIGAALFYGDGVITPALSVLSAVEGLKTIPGLEHSVSRGEILLITSAILIGLFLMQARGTRIVGRLFGPVCLVWFVTIGGIGLIHIADQPAILAALLPHNGVLFMANHGVAGMFVMGAVFLTVTGAEALTADMGHFGAKPIRTGWLAIVFPALALNYLGQGAFALHRLEVASARGVEFVNQDWFFLMAPGLARIPLVILATCATVIASQAVITGAYSLTRQAIQLGLLPRLKIRQTSEHAAGQIYLPTITMLLFVGVMVLVLGFGSSSAMAAAYGVSVSGTMVVTTCLAFLVVRRSWGWGWPLTVAVIVPLLLLDLFFFGANILRIYEGGWVPLIVAGGVGLLIVTWVRGRKLLLAIDQSQAIELEELARMLRARPPERVPGMAIFLSSGMEAAPSALLHNLKHNKILHERNLALTINTVNQPAVPAAQRLDMTNIDENFTRAVLNYGFMESPDIPRDLAFALRHGDNKLEPMQTSYFIGRSTLRPSKHSGMPFWQDLLFIFLYRNASDPTDFFRIPPNRVVELGSQTTI | 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 | MSQLSAPGAENTRRLLAMALGSVGVVYGDIGTSPLYAFREALRPVSHDGVTDVEIVGLISLMIWALTIIVTIKYVLFLLRADNQGEGGTLSLLALLMKTANGHTAILFFMGIAGAALFIGDAMITPALSVLSAVEGLKLVTPALSDYVVPIAVVILLFLFAVQSKGTAAVSKFFGPITLVWFLVMGAVGFMHIADDLSIFRAFNPYYAVAFLFNEGYVGIVVLGAVFLTVTGAEALYADLGHFGRRPIQWAWFTVVFPALTLNYLGQGAFVLKNPEAMSDPFFLMFPKWALLPAVILATAATIIASQAVITGAFSLTRQAIHLGFLPRMAIFHTSETHTGQIYLPNVNTLLMFGVMALVFIFGSSESLATAYGISVTGAMVVTTVLAFEFLRMRWNWPAWWAAGVLLPLFALELVFLGANMLKIHDGGYVPILIAATFIVIMWTWKRGTAILHTKTRHIDIPLERFIKSIERQSEHAPVSVPGTAIFLTSDPESTPAALLHNIKHNHVLHQQNFILTIRTANTPKVPREERVSARRLSERFTLMEVRFGFMETQNVSQALGLFRKSGLKFDIMSTSFYLGRRKLVPDAQSGMPHWQDRLFIALANAAIDPSDYFRLPTNRVVELGSHVII | 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 | MAIVALGVVYGDIGTSPLYTAQTFLAGQGGLGSVDREAVLGMLSLVFWSITLITTVKYVLIAMRIDNNGEGGIFALYSLIRKYGAWLAIPAMLGGAAFLADSVLTPAVSISSAVEGLQTLPPLEGLFDENPSLTLMITVVIIVILFSVQSRGTESIGKVFGSMVLVWFGFLAIVGVTNLSNDWSVFEALNPVYGIKFLFSPNNAAGIALMGTVFLSTTGAEALYSDMGHVGRGNIYFTWPFIKVALVLNYFGQGAWMLANSDNPQYTAMESLNPFFQMMSPNVRYLAVILSVSAGVIASQALITGAFTMVSEATRLNWMPHLQVRYPARTRGQLYIPVVNGVLCVSTLAVLAIFKDSEHISAAYGLALTITMITTTVLLGVYLWHSGKRVGAIVFTVLFLAIQAMFFIASMAKFLHGGWFTMLLTAAILFVMYTWNEGTKLERAQRRHMRPNDFLPALDKLHSDFRIPYFADNIVYLTSDSETKRLDTDIFFSIFADHPKRARAWWAVSVETTDEPFTREYSVEDFGTNYIYRVRFRLGFKVSQSIPAYIHQIMHDLSKTGELPKQKSIYPKVDADPDIGTIRYVLIHKALMPESKVSARGALSLQAKYAIRHMAGSPVKWFGLAPYNPLVEVQPLFVSTRRPPRLKRTDTAKTIPTPTPTRAVADPAAVPDPMDTTSGLGRLVQELDAAVSAEARKTAEAAAADAPAEQGDKGDKGKAENGKPAAKPQRSAKQKR | 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 | MKTEAQSYWGGIIKSMGLVFGDIGTSPIYTLTVIMTLTKPDAEHVLGILSLIVWTLIILVTVEYAWLAMSLGRKGEGGTIVLKEILIRLLKSGRQMAFAGFLAFLGVSLLLGDGVITPAISILSAVEGMRLIPGLEDLAQGGLILVAAVIAVFLFIFQFKGTDKVASAFGPIMVVWFSALTVSGLVSIIGTPTVVQAISPHHAVLFLKHNGLAGFFVLSEVILCATGGEALYADMGHLGRKPIIRAWYFVFCALVINYLGQGAFILRNPEAKNILFSMVKSQVPMLYIPFLLLTISATIIASQALISGVFSIVYQGITTRILPLMKVDYTSTHLKSQIYIGSVNWSLLVAVIFIMILFQRSENLAAAYGLAVTGTMFITGIMMTMIFSRTTKKWKVPIALAVTVIDFAYLTANLHKLPHGGYWSLVLASIPLAIMVIWTRGQRALYRSLKPLDLDTFLLSYEQIYAKGHNIPGTGLFFVRETPVVPPYVIHCIIRSNIIYERNVFVSLTRTDEPFDVRTKLTRGIGTGLDAFEVNAGYMERLDIEKLLKKHGVEEKVIFYGIEDIDTSNPVWRIFATIKRQSANFVQFNKLPVSKLQGVVTRVEM | 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 | MGSGPADEEHTVDTEPGVSPPRRTVGGRETVRAAVVVGALGVVFGDIGTSPIYTIQTVFNPEDPHPVPISTNNVYGVVSLIFWSVMLIVTATYVLLVMRADNDGEGGVMALITLLRRMGAVRGSRVTAVLAGLGIFGAALFFGDSMITPAISVLSAVEGLKVVEPGLEEWIVPITAVIIVALFSVQRRGTAAVGRLFGPVMIVWFVSIGACGVSGIARHPEILKALSPTYALSFFFGHFGIAFFALAAVVLAVTGAEALYADMGHFGRRAITRGWLVLVLPACVLSYLGQGALLLGDQSAVSSPFFLLAPGWARWPMVLLATAATVIASQAVITGAYSVASQAAQLGYLPRLRVAHTSESTIGQIYVPWINWVLMVSVLTLVFAFRSSAALAYAFGMAVTGTITITTLLFFYIVRTRWGTPLWLVVCGAGCLLAVDLLFLAANLTKLVHGAWLPLLIALTAFTVMTTWQRGRAIVTRARERAEGSLGDFVGQLHDYRPPLVRVPGTAVFLNRGKQTAPLAMRANVEHNRVLQQHVVIMSINTLPVPRVPDTERTEIDKLGYAEDGIVHVTAFFGYMDAPNIPDVLRLLDPAETEGPIAVDSASYFLSKIELTMGTAPTMATWRKRLFIATSYITADAAEYFGLPGERTVIMGSRIDV | 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 (Da): 9713
Sequence Length: 84
Subcellular Location: Secreted
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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 increase in swimming speed on zebrafish larvae, as well as death which occurs between 2 and 18 hours later (By similarity). Also paralyzes swimming crabs (C.danae) when injected at the junction between the body and the walking leg .
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 5718
Sequence Length: 50
Subcellular Location: Secreted
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Q8PM33 | MTDPLSRAHAAALDAADPLRNLRDAFVFPQHGDDDQTYFVGNSLGLQPRAARAMVDEVLDQWGALAVEGHFTGPTQWLTYHQLVGDALARVVGAQPGEVVAMNTLSVNLHLMMASFYRPTAERGAILIEAGAFPSDRHAVESQLRLHGLDPATHLIEVEADEPNGTVSMSAIAEAIAQHGPHLALVLWPGIQYRTGQAFDLAEIVRLARAQGAAVGLDLAHAVGNLPLTLHDDGVDFAVWCHYKYLNAGPGAVGGCFVHARHATSDLPRMAGWWGHEQQTRFRMDPQFVPSPGAEGWQLSNPPVLALAPLRASLALFDQAGMAALRAKSEQLTGHLEQMIHARVPQVLQIVTPVEPARRGCQLSLRVAGGRARGRALFEHLHAAGVLGDWREPDVIRIAPVPLYNRFSDLHTFVEQVEAWAAA | 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 degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
EC: 3.7.1.3
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Q05979 | MEKALELDGEYPESLRDEFNIPTFKSMGLSSDDKPVTYLCGNSLGLMPKSTRNSINAELDAWSDCAVESHFKHPEEARGKVPWVSIDLPILPLLAPIVGAQENEVAVMNSLTANLNSLLITFYKPTEKRFKILFEKGSFPSDYYAFYNQCKIHGISEPENVFIQIEPREGETYIRTQDILDTIEVNQDELALVCLSGVQYYTGQYFDIGRITSFAHQFPDILVGWDLAHAVGNVPLQLHDWGVDFACWCSYKYLNAGPGGIGGLFVHSKHTKPDPAKESLPRLAGWWGNDPAKRFQMLEVFEPIPGALGFRQSNPSVIDTVALRSSLELFAKFNGINEVRKRSLLLTNYMTELLEASKYYKHPLRIEKLPCFFTILTPTSTDEEHGAQLSLYFDSDTGKEDIMPKVFQYLHDHGVIGDARRPNVIRLAPAPLYNTFSDVYIAVNALNEAMDKL | 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 degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.7.1.3
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Q8C8H8 | MELKKDSNAVAIDMLLIVHSEKRRAAQATHLDPQANPGALLQNRGGFQGVRNGIRKWQELEENSFQGNLPEKQCLQQPQVITSYDNQGTQLTVEIHPQDAMPQLLKKFSLAKRLQGDKNGNMRPRQPGGKDAHAYPWDRSSLKSMPLDLRLFEKLDASASQVTVKSGLNELVSDLLQEAHSDLERVRAIWIWICHHIEYDVEAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRVAGVQCVTVPGYSKGFGYQTGQSFSGEFDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKFTFLYNEFYFLTHPALFIEDHFPDNKNWQLLKPPQSLRQFENSMYHKSEFYNKGMLSAHPETSMIRTVNGKATITIESRAPTLFMFMLNGKQEHGLLSLRKNGMKLEVYPPTMGTHKLQIFAKGNSEIYSSVLEYTLKCNYVDFSVQLPSELHQPVGPSWFSEQMGITKPSHSDPIIHTSDGRCAISFSVEEGVSVLASLHGDDGPITEETQRRYIFQLNRGKRTELKVQLPHAGKFALKIFVKKRQEQGNFIFVFNYLLCCANTKVNWPMFPESFGNWGQDNELLEPLSGVLPANRNVAFKLKLHGIAKALVKGQDTWPLTLNPEGYWEGSCNTAGCQEVYVMVLENANHNFYSYILKYKVNDQ | 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 viability.
Sequence Mass (Da): 32419
Sequence Length: 287
Subcellular Location: Mitochondrion matrix
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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 | MSQQKKYIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLIAIANPNQHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTINAKFASRG | 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
Sequence Length: 666
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 6.2.1.3
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Q9T009 | MTSQKRFIFEVEAAKEATDGNPSVGPVYRSTFAQNGFPNPIDGIQSCWDIFRTAVEKYPNNRMLGRREISNGKAGKYVWKTYKEVYDIVIKLGNSLRSCGIKEGEKCGIYGINCCEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHAEVSIAFVEEKKIPELFKTCPNSTKYMKTVVSFGGVKPEQKEEAEKLGLVIHSWDEFLKLGEGKQYELPIKKPSDICTIMYTSGTTGDPKGVMISNESIVTITTGVMHFLGNVNASLSEKDVYISYLPLAHVFDRAIEECIIQVGGSIGFWRGDVKLLIEDLGELKPSIFCAVPRVLDRVYTGLQQKLSGGGFFKKKVFDVAFSYKFGNMKKGQSHVAASPFCDKLVFNKVKQGLGGNVRIILSGAAPLASHIESFLRVVACCNVLQGYGLTESCAGTFATFPDELDMLGTVGPPVPNVDIRLESVPEMNYDALGSTPRGEICIRGKTLFSGYYKREDLTKEVFIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLAQGEYVAVENLENVYSQVEVIESIWVYGNSFESFLVAIANPAQQTLERWAVENGVNGDFNSICQNAKAKAFILGELVKTAKENKLKGFEIIKDVHLEPVAFDMERDLLTPTYKKKRPQLLKYYQNVIHEMYKTTKESLASGQ | 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
Sequence Length: 666
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 6.2.1.3
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Q8LKS5 | MEFASPEQRRLETIRSHIDTSPTNDQSSSLFLNATASSASPFFKEDSYSVVLPEKLDTGKWNVYRSKRSPTKLVSRFPDHPEIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIINGRTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAEIAASNPIPSKL | 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 mobilization for beta-oxidation during seed germination, which is essential for postgerminative growth and seedling establishment .
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 77353
Sequence Length: 700
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Peroxisome
EC: 6.2.1.3
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Q9SJD4 | MEDSGVNPMDSPSKGSDFGVYGIIGGGIVALLVPVLLSVVLNGTKKGKKRGVPIKVGGEEGYTMRHARAPELVDVPWEGAATMPALFEQSCKKYSKDRLLGTREFIDKEFITASDGRKFEKLHLGEYKWQSYGEVFERVCNFASGLVNVGHNVDDRVAIFSDTRAEWFIAFQGCFRQSITVVTIYASLGEEALIYSLNETRVSTLICDSKQLKKLSAIQSSLKTVKNIIYIEEDGVDVASSDVNSMGDITVSSISEVEKLGQKNAVQPILPSKNGVAVIMFTSGSTGLPKGVMITHGNLVATAAGVMKVVPKLDKNDTYIAYLPLAHVFELEAEIVVFTSGSAIGYGSAMTLTDTSNKVKKGTKGDVSALKPTIMTAVPAILDRVREGVLKKVEEKGGMAKTLFDFAYKRRLAAVDGSWFGAWGLEKMLWDALVFKKIRAVLGGHIRFMLVGGAPLSPDSQRFINICMGSPIGQGYGLTETCAGATFSEWDDPAVGRVGPPLPCGYVKLVSWEEGGYRISDKPMPRGEIVVGGNSVTAGYFNNQEKTDEVYKVDEKGTRWFYTGDIGRFHPDGCLEVIDRKKDIVKLQHGEYVSLGKVEAALGSSNYVDNIMVHADPINSYCVALVVPSRGALEKWAEEAGVKHSEFAELCEKGEAVKEVQQSLTKAGKAAKLEKFELPAKIKLLSEPWTPESGLVTAALKIKREQIKSKFKDELSKLYA | 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
Sequence Length: 720
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 6.2.1.3
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Q9CAP8 | MIPYAAGVIVPLALTFLVQKSKKEKKRGVVVDVGGEPGYAIRNHRFTEPVSSHWEHISTLPELFEISCNAHSDRVFLGTRKLISREIETSEDGKTFEKLHLGDYEWLTFGKTLEAVCDFASGLVQIGHKTEERVAIFADTREEWFISLQGCFRRNVTVVTIYSSLGEEALCHSLNETEVTTVICGSKELKKLMDISQQLETVKRVICMDDEFPSDVNSNWMATSFTDVQKLGRENPVDPNFPLSADVAVIMYTSGSTGLPKGVMMTHGNVLATVSAVMTIVPDLGKRDIYMAYLPLAHILELAAESVMATIGSAIGYGSPLTLTDTSNKIKKGTKGDVTALKPTIMTAVPAILDRVRDGVRKKVDAKGGLSKKLFDFAYARRLSAINGSWFGAWGLEKLLWDVLVFRKIRAVLGGQIRYLLSGGAPLSGDTQRFINICVGAPIGQGYGLTETCAGGTFSEFEDTSVGRVGAPLPCSFVKLVDWAEGGYLTSDKPMPRGEIVIGGSNITLGYFKNEEKTKEVYKVDEKGMRWFYTGDIGRFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSISPYVENIMVHADSFYSYCVALVVASQHTVEGWASKQGIDFANFEELCTKEQAVKEVYASLVKAAKQSRLEKFEIPAKIKLLASPWTPESGLVTAALKLKRDVIRREFSEDLTKLYA | 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
Sequence Length: 691
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 6.2.1.3
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P83111 | MYRLMSAVTARAAAPGGLASSCGRRGVHQRAGLPPLGHGWVGGLGLGLGLALGVKLAGGLRGAAPAQSPAAPDPEASPLAEPPQEQSLAPWSPQTPAPPCSRCFARAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDIPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMMKENVAFEQEKEGKSNEKNDFTKFKTEQENEAKCRNSKPGKKKNDFEQGELYLREKFENSIESLRLFKNDPLFFKPGSQFLYSTFGYTLLAAIVERASGCKYLDYMQKIFHDLDMLTTVQEENEPVIYNRARFYVYNKKKRLVNTPYVDNSYKWAGGGFLSTVGDLLKFGNAMLYGYQVGLFKNSNENLLPGYLKPETMVMMWTPVPNTEMSWDKEGKYAMAWGVVERKQTYGSCRKQRHYASHTGGAVGASSVLLVLPEELDTETINNKVPPRGIIVSIICNMQSVGLNSTALKIALEFDKDRSD | 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 it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein . Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of breast cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism .
Sequence Mass (Da): 60694
Sequence Length: 547
Subcellular Location: Mitochondrion
EC: 3.4.-.-
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Q9EP89 | MYRLLSSVTARAAATAGPAWDGGRRGAHRRPGLPVLGLGWAGGLGLGLGLALGAKLVVGLRGAVPIQSPADPEASGTTELSHEQALSPGSPHTPAPPAARGFSRAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDLPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMVKGTPPPSDQEKELKEKGGKNNEKSDAPKAKVEQDSEARCRSAKPGKKKNDFEQGELYLKEKFENSIESLRLFKNDPLFFKPGSQFLYSTFGYTLLAAIVERASGYKYLDYMQKIFHDLDMLTTVQEENEPVIYNRARFYVYNKKKRLVNTPYVDNSYKWAGGGFLSTVGDLLKFGNAMLYGYQVGQFKNSNENLLPGYLKPETMVMMWTPVPNTEMSWDKEGKYAMAWGVVEKKQTYGSCRKQRHYASHTGGAVGASSVLLVLPEELDSEAVNNKVPPRGIIVSIICNMQSVGLNSTALKIALEFDKDRAD | 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 similarity). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (By similarity). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism .
Sequence Mass (Da): 60705
Sequence Length: 551
Subcellular Location: Mitochondrion
EC: 3.4.-.-
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P02920 | MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA | 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 directed toward the galactopyranosyl moiety of the substrate .
Catalytic Activity: H(+)(in) + lactose(in) = H(+)(out) + lactose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46503
Sequence Length: 417
Subcellular Location: Cell inner membrane
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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 inner membrane
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P22733 | MKKKLVSRLSYAAGAFGNDVFYATLSTYFIVFVTTHLFNAGDHKMIFIITNLITAIRIGEVLLDPLIGNAIDRTESRWGKFKPWVVGGGIISSLALLALFTDFGGINQSKPVVYLVIFGIVYLIMDIFYSFKDTGFWAMIPALSLDSREREKTSTFARVGSTIGANLVGVVITPIILFFSASKANPNGDKQGWFFFALIVAIVGILTSITVGLGTHEVKSALRESNEKTTLKQVFKVLGQNDQLLWLAFAYWFYGLGINTLNALQLYYFSYILGDARGYSLLYTINTFVGLISASFFPSLAKKFNRNRLFYACIAVMLLGIGVFSVASGSLALSLVGAEFFFIPQPLAFLVVLMIISDAVEYGQLKTGHRDEALTLSVRPLVDKLGGALSNWFVSLIALTAGMTTGATASTITAHGQMVFKLAMFALPAVMLLIAVSIFAKKVFLTEEKHAEIVDQLETQFGQSHAQKPAQAESFTLASPVSGQLMNLDMVDDPVFADKKLGDGFALVPADGKVYAPFAGTVRQLAKTRHSIVLENEHGVLVLIHLGLGTAKLNGTGFVSYVEEGSQVEAGQQILEFWDPAIKQAKLDDTVIVTVINSETFANSQMLLPIGHSVQALDDVFKLEGKN | 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 PTS EIIA type-1 domain may serve a regulatory function, through its phosphorylation activity.
Subcellular Location: Cell membrane
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Q90617 | MAPPRCPAGLALLLLLLGACGFFQSYAVEVDVKDASNFTCLYAQWMMKFLIKYETNSSDYKNASLDLTSTVTHNGSICGSDTQAALLAVQFGDGHSWSINFTKNNETYRAEFITFTYNTNDTAVFPDARRQGPVTIVVKDAMHPIQLNNVFVCHHTTSLEAENVTQIFWNVTMQPFVQNGTISKKESRCYADTPTAAPTVLPTVANVTTASTTISPAPTTAPKPAENPVTGNYSLKTGNKTCLLATVGLQLNISQDKPLLINIDPKTTHADGTCGNTSATLKLNDGNRTLIDFTFIVNASASVQKFYLREVNVTLLNYQNGSVILSADNNNLSKWDASLGNSYMCRKEQTLEINENLQVHTFNLWVQPFLVKENKFSIAEECFADSDLNFLIPVAVGMALGFLIILVFISYIIGRRKSRTGYQSV | 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 for lysosomal degradation (By similarity). Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity).
PTM: Extensively N-glycosylated. Contains a minor proportion of O-linked glycans.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46715
Sequence Length: 425
Subcellular Location: Cell membrane
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P13473 | MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF | 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 targeting them for lysosomal degradation . In the chaperone-mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 . Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy . Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes . Required for normal degradation of the contents of autophagosomes . Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits . Is not required for efficient MHCII-mediated presentation of endogenous antigens .
PTM: O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 44961
Sequence Length: 410
Subcellular Location: Cell membrane
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Q9UQV4 | MPRQLSAAAALFASLAVILHDGSQMRAKAFPETRDYSQPTAAATVQDIKKPVQQPAKQAPHQTLAARFMDGHITFQTAATVKIPTTTPATTKNTATTSPITYTLVTTQATPNNSHTAPPVTEVTVGPSLAPYSLPPTITPPAHTTGTSSSTVSHTTGNTTQPSNQTTLPATLSIALHKSTTGQKPVQPTHAPGTTAAAHNTTRTAAPASTVPGPTLAPQPSSVKTGIYQVLNGSRLCIKAEMGIQLIVQDKESVFSPRRYFNIDPNATQASGNCGTRKSNLLLNFQGGFVNLTFTKDEESYYISEVGAYLTVSDPETIYQGIKHAVVMFQTAVGHSFKCVSEQSLQLSAHLQVKTTDVQLQAFDFEDDHFGNVDECSSDYTIVLPVIGAIVVGLCLMGMGVYKIRLRCQSSGYQRI | 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 hepatocellular lipogenesis through activation of the PI3K/Akt pathway . May also play a role in dendritic cell function and in adaptive immunity .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 44346
Sequence Length: 416
Subcellular Location: Cell surface
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Q7TST5 | MPGQISAVAVLFLSLTVILHGYQIREKEFPKARGYLQYTATSAEQITTKPLLQLINQRSHITLASRFKDDYIQMAAETSAIENTAHITMKTVTPVTTKSLPPISSASYTFVRSNNAHMTASSTDDTIGSGSIAHLPVPTTRASLAIVNYITGRATQLGGQTTLPKTFFTASHKSTTNQRPTLSTNVLGTSTPTHKDRSTTSPVPLVPRPTLVTWSSPAKIGTYEVLNGSRLCIKAEMGLALIVQEKDLDSATQRYFNIDPSLTHASGKCDSQKSNLFLNFQGGSVNITFTKEENLYYISEVGAYLTISNTEKTYQGKKNTLMMFETVVGHSFKCVSEQSIQLSAQLQMKTMNIHLQAFDFEGDSFGNVNECLSDYTVVLPMVAIIVVVICVVGLSVYKIRQRHQSSAYQRI | 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 hepatocellular lipogenesis through activation of the PI3K/Akt pathway. May also play a role in dendritic cell function and in adaptive immunity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 45129
Sequence Length: 411
Subcellular Location: Cell surface
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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 | MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAIMECILTEHFGENILDPLFEIYTKNLQENFHVFDKEIRKDADLYLVLKRKGN | 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 on deoxyloganic, dehydrologanic, epiloganic and loganetic acid .
Catalytic Activity: loganate + S-adenosyl-L-methionine = loganin + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42018
Sequence Length: 371
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.50
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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 not secreted to influence other bacteria (Probable).
PTM: Cross-links are proved in vitro, when coepressed in E.coli with the ProcM lanthionine synthetase.
Sequence Mass (Da): 8708
Sequence Length: 81
Subcellular Location: Secreted
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P14789 | MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYAGNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL | 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 proteolytic activity of elastase (lasB) and elastolytic activity of other proteases . Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate .
PTM: Processing of pro-LasA can occur extracellularly and requires elastase (lasB) . Secretion and processing may be linked .
Sequence Mass (Da): 45517
Sequence Length: 418
Subcellular Location: Secreted
EC: 3.4.24.-
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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 = an N-acyl-L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine
Sequence Mass (Da): 22691
Sequence Length: 201
EC: 2.3.1.184
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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 types (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 3517
Sequence Length: 30
Subcellular Location: Cytoplasm
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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 types.
PTM: Phosphorylated.
Sequence Mass (Da): 29970
Sequence Length: 263
Subcellular Location: Cytoplasm
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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 | MNKKHGFPLTLTALAIATAFPAYAAQAGGATPDAAQTQSLKEITVRAAKVGRRSKEATGLGKIVKTSETLNKEQVLGIRDLTRYDPGVAVVEQGNGASGGYSIRGVDKNRVAVSVDGVAQIQAFTVQGSLSGYGGRGGSGAINEIEYENISTVEIDKGAGSSDHGSGALGGAVAFRTKEAADLISDGKSWGIQAKTAYGSKNRQFMKSLGAGFSKDGWEGLLIRTERQGRETRPHGDIADGVEYGIDRLDAFRQTYDIKRKTREPFFSVEGERESKPVAKLAGYGKYLNNQLNRWVKERIEQNQPLSAEEEAQVREAQARHENLSAQAYTGGGRILPDPMDYRSGSWLAKLGYRFGGRHYVGGVFEDTKQRYDIRDMTEKQYYGTDEAEKFRDKSGVYDGDDFRDGLYFVPNIEEWKGDKNLVRGIGLKYSRTKFIDEHHRRRRMGLLYRYENEAYSDNWADKAVLSFDKQGVATDNNTLKLNCAVYPAVDKSCRASADKPYSYDSSDRFHYREQHNVLNASFEKSLKNKWTKHHLTLGFGYDASKAISRPEQLSHNAARISESTGFDENNQDKYLLGKPEVVEGSVCGYIETLRSRKCVPRKINGSNIHISLNDRFSIGKYFDFSLGGRYDRKNFTTSEELVRSGRYVDRSWNSGILFKPNRHFSVSYRASSGFRTPSFQELFGIDIYHDYPKGWQRPALKSEKAANREIGLQWKGDFGFLEISSFRNRYTDMIAVADHKTKLPNQAGQLTEIDIRDYYNAQNMSLQGVNILGKIDWNGVYGKLPEGLYTTLAYNRIKPKSVSNRPGLSLRSYALDAVQPSRYVLGFGYDQPEGKWGANIMLTYSKGKNPDELAYLAGDQKRYSTKRASSSWSTADVSAYLNLKKRLTLRAAIYNIGNYRYVTWESLRQTAESTANRHGGDSNYGRYAAPGRNFSLALEMKF | 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) storage, and thereby plays a role in the endocrine regulation of organismal growth and survival . Likely functions by enhancing the activity of the JH hydrolase enzymes Jheh1 and Jheh2 . Required for lipid droplet positioning and fat storage .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35736
Sequence Length: 307
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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Q9H6V9 | MDSELKEEIPVHEEFILCGGAETQVLKCGPWTDLFHDQSVKRPKLLIFIIPGNPGFSAFYVPFAKALYSLTNRRFPVWTISHAGHALAPKDKKILTTSEDSNAQEIKDIYGLNGQIEHKLAFLRTHVPKDMKLVLIGHSIGSYFTLQMLKRVPELPVIRAFLLFPTIERMSESPNGRIATPLLCWFRYVLYVTGYLLLKPCPETIKSLLIRRGLQVMNLENEFSPLNILEPFCLANAAYLGGQEMMEVVKRDDETIKEHLCKLTFYYGTIDPWCPKEYYEDIKKDFPEGDIRLCEKNIPHAFITHFNQEMADMIADSLKDDLSKM | 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.
Sequence Mass (Da): 37319
Sequence Length: 325
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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Q8BVA5 | MASEVEEQIPVREEFFLCGGVETKIIKCGPWTNLFEKQDVSKPKQLIFIIPGNPGYSAFYVPFAKALYTLMKSRFPVWIISHAGFSVTPKDKKVLAAPQEESNAQKIEDVYGLNGQIEHKIAFLRAHVPKDVKLILIGHSVGTYMTLHVMKRVLELPVAHAFLLFPTIERMSESPNGKFATPFLCQFRYLLYATSYLLFKPCPEVIKSFIIQKLMGQMNIKLELPLTDILQPFCLANAAYLGSQEMVQIVKRDDDIIKEFLPKLKFYYGKTDGWCPVKYYEDMKKDFPEGNIYLCEKGIPHAFVLDFSQEMATIVAEWINNRPPRK | 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 .
Sequence Mass (Da): 37374
Sequence Length: 326
Subcellular Location: Lipid droplet
EC: 3.1.1.-
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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 | MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPTRQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ | 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 synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state.
PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome.
Sequence Mass (Da): 46533
Sequence Length: 411
Domain: The dimerization domain is located in the N-terminus.
Subcellular Location: Nucleus
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P70662 | MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ | 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 synergistically with LHX1/LIM1 in axis formation and activation of gene expression . Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state .
PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome.
Sequence Mass (Da): 46503
Sequence Length: 411
Domain: The dimerization domain is located in the N-terminus.
Subcellular Location: Nucleus
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P70060 | MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKESFHNNFVSLDCDQCTMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ | 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-mediated ubiquitin-proteasome-dependent degradation.
Sequence Mass (Da): 42825
Sequence Length: 375
Domain: The dimerization domain is located in the N-terminus.
Subcellular Location: Nucleus
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Q6NVL6 | MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKESFHNNFVSLDCDQCTMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPNKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ | 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: Undergoes rnf12-mediated ubiquitin-proteasome-dependent degradation.
Sequence Mass (Da): 42656
Sequence Length: 373
Domain: The dimerization domain is located in the N-terminus.
Subcellular Location: Nucleus
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O43679 | MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQYDAANGMDDEEDFNNSPALGNNSPWNSKPPATQETKSENPPPQASQ | 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
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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
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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
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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: Secreted
EC: 3.1.27.-
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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 apparatus.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26789
Sequence Length: 230
Subcellular Location: Cell inner membrane
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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 release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24754
Sequence Length: 228
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32850
Sequence Length: 287
Subcellular Location: Cell inner membrane
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O30387 | MTHSSLPGYFGPLFAVFLFVLGLCVGSFLNVVIARVPLDQSIVRPRSRCPRCGHVLAWYENIPLLSWLALRARCRGCGVPISVRYPLVELLTGLLFFACLRRFGWTYELVPALVLVSLLVPLAFIDLDHWILPLSMTVPGMLAGIALAFPLGMDAFRDALMGAAVGFLSFRMMEYVGWKVFQREALGAGDKYLVAMLGAFLTWRALLGVLLFASMQGAVVGILMLLATGRAGPRTENTQDEPAGDAPPLTMTWEFTQPGLPLWKRLLLVPVCLLVQPIPDAPLDEEGEEEEWVPERTSIPFGPWLALAGLELLLLGPWLSRVLPADIAMMLGGLP | 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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36768
Sequence Length: 335
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31332
Sequence Length: 286
Subcellular Location: Cell inner membrane
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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 apparatus.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31131
Sequence Length: 279
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine . Substrates include proteins required for pilus biogenesis PilE, PilV, PilW, and PilX as well as some components of the type II general secretory apparatus GspG, GspH, GspI and GspJ .
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31870
Sequence Length: 290
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31818
Sequence Length: 289
Subcellular Location: Cell inner membrane
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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-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29767
Sequence Length: 269
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29337
Sequence Length: 253
Subcellular Location: Cell inner membrane
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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 group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32295
Sequence Length: 289
Subcellular Location: Cell inner membrane
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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 release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31843
Sequence Length: 287
Subcellular Location: Cell inner membrane
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Q7UX15 | MASKSSRSQEHIRNFCIIAHIDHGKSTLADRLLESTGTVDNRGKKTQMLDDLALEQQRGITIKARAVAMRYKRDGIEYELNLIDTPGHVDFQYEVSRSLACCEGALLLVDAFQGVEAQTVANAFAAMEHDLTIVPVINKIDLIHARPDEVAEEMMNSLGTDPDECKRVSAKTGEGVAALLDAIVDSVPAPTGDPKAVLQAMVFDSNYDDFRGAITYIRVMQGTVRKGQKIKFLRAGSVHDVVELGQFAPSRVPCDELVAGQVGYLICNIKSLGDVHIGDTISIAGNDPAPALPGYDRPKRMVYCGLFPSDGQDFSELRDALERLAVNDPSFEFEPETSDALGFGFRCGFLGLLHMEIVQQRLEQESDIDLVQTAPNVTYEITDKRGVTKNIHKPQDVPDPGDIEKFCQPIVRCNVIVPEEYIGPVMKLCQERRGIQKGHEVLGASRAMLTYDIPLAEVIYDLHDRIKSCTRGYGTLDYEMVGYEEADLCRLDILVNGNRVDALSVVCHRADADRRGRAVAKKLKSEIERHMFEVAVQAAIGSRVIARETVPAMRKNVTAKCYGGDITRKRKLLQKQKEGKKRMKAVGNVEISQKAFMAVLTDGE | 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 to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66781
Sequence Length: 604
Subcellular Location: Cell inner membrane
EC: 3.6.5.n1
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Q88T65 | MKQSHIRNFAIIAHIDHGKSTLADQIMSLTQTVSAREQHAQLLDDMTVEQAHGVTVKARTVRNYYQADDGQEYEYNLIDTPGHVDFNYEVAKSLAATEGAILLVDATQGVQAQTIANYRIAKQRQLTLIPVLNKVDLPSADIDAALAQLNDLDSAFTPEQVLQISAKTGQGVPAVLEAIKQRLPAPQGDLHQPLKALVFDSLYDPYQGVIAYVRLIDGQLKSQQALCLMQGQQDFNGKAIGVFAPQMHPQESLSAGDVGYVVTGIKDPRKVRVGDTLTSVATPTQRPLAGYQPAKSMVFAGLYPKNNDYPALKEAVQKLNLNDPSFTYVEERSEALGVGFRCGFLGTFHLQIIRERLHDEYGVDVLTTAPNVTYHVTLTNGQQVIVNNPVQFPAFSLIKEVTEPFMKAEITMPADNLNAVLKLAEQHKGTLIDLANSGDLIVASLKIPLSEIAYHFFSELKSVSHGFASLSTAFMANEVSDLVKVEVDINYAPVDALTFIVHREDAPNMTQQLVANLKTTVPRQLYPTPVQARVEGKVIARVDVPPLRKNAAVNGEQHSTSKKAALLRRQSANKRRASKNTIKLPQSVFNAILSL | 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 to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65272
Sequence Length: 595
Subcellular Location: Cell membrane
EC: 3.6.5.n1
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A9KF98 | MTTISQKFIRNFSIIAHIDHGKSTLADRFIQLCGGLSEREMKAQVLDSMDIERERGITIKAQSVTLNFKSQDGHFYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAAQGVEAQTVATCYTAIEQGLVVLPVLNKIDLPQADPERVIQEIEDVIGIEAHDAIRVSAKEGRCVKELLEQLVVAIPPPVGDPEAPLQALIIDSWFDSYLGVVSLVRVKAGTLRKGDKIRVMSTGKDYYADQIGHFTPKRQPLEELSAGAVGFVVAGIKDIFGAPVGDTLTHAKQSAGSPLPGFKQVKPQVFAGLFPINSEEYEPFREALAKLQLNDAALFYEPESSEALGFGFRCGFLGMLHMEIVQERLEREYNLELITTAPTVSYEILTKQGEMLYVDNPSHLPEPGKIGEIREPIAVANILVPPTYLGAVITLCVEKRGVQKKLLYLSNQVSMTYEIPLSEVVLDFFDRLKSASRGYASLDYSFNHFQAADLVKLDILISGQKVDALATIVHRDLAYTRGRELTERLKDLIPRQMFEVAIQAAIGAKIIARTSVKALRKNVTAKCYGGDITRKRKLLEKQKAGKKRMKQVGKVAIPQEAFLAVLRVKNE | 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 to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66557
Sequence Length: 602
Subcellular Location: Cell inner membrane
EC: 3.6.5.n1
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Q6A9B2 | MSAPQPGSTDPAVIRNFCIIAHIDHGKSTLADRMLQITGVLDERSARAQYLDRMDIERERGITIKSQAVRMPWEVDGVTHLLNMIDTPGHVDFSYEVSRSLQACEGAILLVDAAQGIEAQTLANLYLALEADLEIIPVLNKIDLPGAESDRHAAEIAGIIGCDESEVLRVSAKTGEGVSDLLDTIVAKVPAPEGVADAPARALIFDSVYDTYRGVVTYVRVVDGALRHREKILMMSTGAAHEVLEIGVISPEMVPAQGLSVGEVGYLITGVKDVRQSRVGDTVTNASKPSEKDLGGYQHPKPMVYSGLFPIDAKDFPDLRDALDKLQLNDAALVYEPETSTALGFGFRVGFLGLLHMEIVRERLEREFDLDLISTAPSVVHHVLMEDGSTVAVTNPSEYPTSGRIAEVREPIVDATILSPAEYIGTILELCQQRRGVQQGLDYLSSDRVEIRYRLPLSEIVFDFFDQLKSRTKGYASLDYHEAGEQAADLVKVDILLNGDPVDALSSIVHRDKSYSYGVAMAAKLKELIPRQQFEVPVQAAIGARVIARETIRAVRKDVLAKCYGGDISRKRKLLEKQKAGKKRMKVVGSVEVPQEAFVAALRTGESTEKK | 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 to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66868
Sequence Length: 611
Subcellular Location: Cell membrane
EC: 3.6.5.n1
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Q0JEU6 | MAHLLFLPILQLLLLYCTKSAQAQLNISIGSSLTPQGVNNSWISPSADFAFGFLAVDGNSSSYLLAVWFNKIADKTVVWYARTSSNGKDDTIPVQVQSGSVLKLADGALSLRDPSGNEVWNPQVTDVGYARMLDTGNFRLLGTDGATKWESFGDPSDTILPTQVLSLGTALHSRLLATDYSNGRFQLKVQRDGNLVMYPDAVPSGYLYDPYWASNTVDNGSQLVFNETGRIYFTIINGSQVNITSAGVDSMGDFFHRATLDTDGVFRQYVYPKNIHARPLWPEQWTAVDVLPENICQSIQTMVGSGACGFNSYCTIDGTKNTTSCLCPQNYKFIDDKRKYKGCRPDFEPQNCDLDETTAMLQYDMAPIDRVDWPLSDYEQYNPIDQTECRRLCVTDCFCAVAVFDKASSTCWKKRFPLSNGKMDVNVPRTVLIKVPRSTNSPSVFSSGSSKWKEDQKYWILGSSLLFGSSVLVNFLLISVMLFGTYCSITSRKKTQLSQPSNNSGLPPKIFTYSELEKATGGFQEVLGTGASGVVYKGQLQDEFGTNIAVKKIEKLQQEAQKEFLVEVQTIGQTFHRNLVRLLGFCNEGTERLLVYEFMSNGSLNTFLFSDTHPHWSLRVQVALGVARGLLYLHEECNKQIIHCDMKPQNILLDDNFVAKISDFGLAKLLPVNQTQTNTGIRGTRGYVAPEWFKNIGITSKVDVYSFGVILLELVCCRKNVELEVLDEEQTILTYWANDCYKCGRIDLLVAGDDEAIFNIKKVERFVAVALWCLQEEPSMRPTMLKVTQMLDGAVQIPTPPDPSSYISSLA | 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 membrane protein
Sequence Mass (Da): 90376
Sequence Length: 811
Subcellular Location: Membrane
EC: 2.7.11.1
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A0R758 | MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELERLWTAPVETPAYRRGAMPAVDRTPRTTTWDAAETTIPEASEGSRECARNIVAVLETFQQVCADNEAELGRIDAVAGDGDHGQGMSFGSRGAAQAARDAVDRNAGARTTLLLAGQAWADAAGGTSGALWGAALTSAGGVFSDTDGADEQAAVDAICAGIDAILRLGGAQPGDKTMVDAAVPFRDALVKAFDTQAGPAITSAARVAREAAEKTADITARRGRARVLGEKSVGTPDPGALSFAMLMKALGEHLTR | 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-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate
Sequence Mass (Da): 59357
Sequence Length: 571
Pathway: Carbohydrate metabolism; L-threitol degradation.
EC: 2.7.1.209
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Q6D8V6 | MTYLFNQPSSFARELTEGFVAAHADKVRQVPGGVVRSTRSREGGVAIVVGGGSGHYPAFAGLVGQGLAHGAAMGNLFASPSAQQICSVARAAHNGGGVLLTFGNYAGDVLHFGQAKARLNAEGIPCELLAVTDDISSAPLNEWQKRRGVAGDLMVFKAVSAAAEAGYDLAAVLEVAERANQRTRSLGVAFSGCTLPGAEHPLFTVPEGMMAVGMGIHGEPGIRDVPISTADELAELLVSSLLKEVPHGITTLSGQRISVVLNGLGGVKYEELFVVYRRVSQLLVEQGLTVVEPEVGELVTSFNMAGLSLTLFWLDEELERFWRAPADAPAFRKGSMSPGEPLAERTFVAELEVIPNATAASKAAAHCVAAALNAARDIVLANVTELGRIDAIAGDGDHGIGMERGVIAAADKATEMLERQAGAGTLLQRAADAWADQAGGTSGAIWGVALNALGTVLGDEQRPDGRRVADGVRQAKESVMHFGKAKPGDKTLVDALIPFSLALTQRVETGMSLPEAWQQAAQCAQQAADDTAQLLPKIGRARPLAEKSLGTPDAGAISLAMILDAVSAVLNSDTTSTSSHQTATQAESER | 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
Pathway: Carbohydrate metabolism.
EC: 2.7.1.209
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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
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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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