wanglab/gogpt-training-data huggingface dataset:
Protein: Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Fatty acid activator 1) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Long-chain acyl-CoA synthetase 1) (P30624)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activates long-chain fatty acids (LCFA) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids. Also facilitates the transport of LCFAs into the cell, either by active transport or by decreasing the intracellular LCFA concentration. It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities. Also involved in long-chain base (LCB) uptake of sphingolipids. In contrast ot LCFA uptake, LCB uptake does not require ATP, suggesting that the enzyme is directly involved in active LCB uptake. Involved in the sphingolipid-to-glycerolipid metabolic pathway, converting the shingolipid metabolite hexadecenoic acid to hexadecenoyl-CoA, which is then further converted to glycerolipids.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Cell membrane {ECO:0000269|PubMed:27136724}.
Interaction partners:
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Long-chain-fatty-acid--CoA ligase 4
- Very long-chain fatty acid transport protein
- Acyl-coenzyme A oxidase
- Triacylglycerol lipase 3
- Monoglyceride lipase
- Long-chain-fatty-acid--CoA ligase 2
- Diacylglycerol O-acyltransferase 1
- Triacylglycerol lipase 4
Sequence:
MVAQYTVPVGKAANEHETAPRRNYQCREKPLVRPPNTKCSTVYEFVLECFQKNKNSNAMGWRDVKEIHEESKSVMKKVDGKETSVEKKWMYYELSHYHYNSFDQLTDIMHEIGRGLVKIGLKPNDDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSLIKPVQAAQDVKYIIHFDSISSEDRRQSGKIYQSAHDAINRIKEVRPDIKTFSFDDILKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGACIGYATVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKLNMQRLHIPGGGALGNLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEQKDSSINIENYLEDAKLIKAVYSDLLKTGKDQGLVGIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDILNAVKDKVDAVYSSS
Protein: (2Z,6E)-farnesyl diphosphate synthase (EC 2.5.1.68) (Short-chain Z-isoprenyl diphosphate synthase) (Z-FPP synthase) (Z-FPPS) (Z-Polyprenyl diphosphate synthase) (Z-isoprenyl diphosphate synthase) (A0R2W4)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11004176, ECO:0000269|PubMed:4741910}.
Interaction partners:
- Polyprenyl synthetase
- Decaprenyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Isopentenyl-diphosphate delta-isomerase
- Bifunctional short chain isoprenyl diphosphate synthase
- Transmembrane protein
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Phosphatidate cytidylyltransferase
- Cysteine--tRNA ligase
- Ribosome-recycling factor
Sequence:
MDIIPPRLKEPAYRIYEMRLRHELVRSKAQLPRHIAVLCDGNRRWARDAGYDDVSIGYRKGAAKIAEMLRWCQAAGIEMATIYLLSTENLQRDPDELTALIEIITDVVEEICAPYNKWSVRTVGDLELLGDEPARRLREAVESTTTKGANFHVNVAVAYGGRQEIVDAVRSLLSKELANGATAEQLIEAVTVDGISENLYTSGQPDPDLVIRTSGEQRLSGFLLWQSAYSEMWFTEAYWPAFRRVDFLRALRDYTARHRRFGK
Protein: Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) (P46664)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}. Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}.
Interaction partners:
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Trifunctional purine biosynthetic protein adenosine-3
- GMP reductase 1
- AMP deaminase 1
- AMP deaminase 3
- AMP deaminase 2
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MSISESSPAATSLPNGDCGRPRARSGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLDGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLRMCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQQLKGYMERIKPMVKDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVSLKYAHMINGFTALALTKLDILDMFTEIKVGVAYKLDGETIPHFPANQEVLNKVEVQYKTLPGWNTDISNARTFKELPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Protein: Uncharacterized membrane protein C6F6.04c (O14237)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVALVNNMRKITIPSVGGKLVSSGQFQNFIASCILFCCPGIYLAVTGLGAGGGHPDAYHMADVTNSLLYALFTVCGWAGGPILKYLGPRWALALGATGYPIYIGGLWYFDNTGKQGFTIFTGAYEGIAAGLLWASTAYISLSYSCANQKSQFIATQWTILAFGSTVGSFIAFGINYHSTSTGVPMAVYIIFIIIMACAVLLAILFIKSPSDVRKSDGTSALSPSNKTFGQELWGLFEAAKDWRLLCLLPASFASQSTIAWQSHLNSYYFSLRTRSLNNVLFWVIQFFVPYLFTLILDAKALKRRTRGIIGLTIQAVVIMATLSGELGWIVSKHIDLHDTSPDLDWTQRGYGGALVLYLLMGIQYGSSIVSVQWCISLLSSDPDKYARYAGLYKGTQAAGMCVSFGIDAAGVSFLGQGIIYFIFLFVMCASQLIMTSIFGKETDRLSTKEHFTDDKSYIDGVMPSTDTYMNEKTSDELDKKSLPSDQVYV
Protein: Probable transmembrane sensor (Q9I647)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable sigma-70 factor, ECF subfamily
- Probable sigma-70 factor, ECF subfamily
- ECF sigma factor, FemI
- ECF sigma factor FoxI
- Probable sigma-70 factor, ECF subfamily
- Probable sigma-70 factor, ECF subfamily
- Metal-pseudopaline receptor CntO
- Sigma factor PvdS
- Probable sigma-70 factor, ECF subfamily
- Probable sigma-70 factor, ECF subfamily
Sequence:
MSADDRHSPVRARVLDEAIAWQLLLDSGEAHPDDHRAFHRWYAAHPEHERAWEQLGGLDRHLARAANGPARNALLSGNARFKRRLRRLGGSALGLVLALGVGLGVANRYVPVRYLLADAYSATGEQRELTLPDATHVRLNSRSAIDVRFDGERRQVVLLAGEILVETAHGDPRPFVVSSADGDMRALGTRFLVRREEPGTRLTVLQSAVAARAETLSEERVIKEGQQVLILPQGLQASEAAPALAGAWAQGMLVVENARLADLVAELGRYSPALLQVDPSIADLRVTGSFPLKDTRLALQALEPSLPVRSVRHNAWWFEVVPR
Protein: Lysosomal thioesterase PPT2 (PPT-2) (EC 3.1.2.-) (S-thioesterase G14) (Q9UMR5)
Organism: Homo sapiens (Human)
Function: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.
Subcellular location: Lysosome {ECO:0000269|PubMed:9341199}.
Interaction partners:
- Palmitoyl-protein thioesterase 1
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Long-chain-fatty-acid--CoA ligase 4
- Long-chain-fatty-acid--CoA ligase 1
- Long-chain-fatty-acid--CoA ligase 6
- Fatty acid CoA ligase Acsl3
- Long-chain-fatty-acid--CoA ligase 5
- Long-chain-fatty-acid--CoA ligase ACSBG2
- Long-chain-fatty-acid--CoA ligase ACSBG1
- Battenin
Sequence:
MLGLCGQRLPAAWVLLLLPFLPLLLLAAPAPHRASYKPVIVVHGLFDSSYSFRHLLEYINETHPGTVVTVLDLFDGRESLRPLWEQVQGFREAVVPIMAKAPQGVHLICYSQGGLVCRALLSVMDDHNVDSFISLSSPQMGQYGDTDYLKWLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALINGERDHPNATVWRKNFLRVGHLVLIGGPDDGVITPWQSSFFGFYDANETVLEMEEQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPWLS
Protein: Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)] (O95760)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury. Induces rapid UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819012, ECO:0000269|PubMed:17185418, ECO:0000269|PubMed:18787100, ECO:0000269|PubMed:18836528, ECO:0000269|PubMed:21734074}. Chromosome {ECO:0000269|PubMed:17185418}. Cytoplasm {ECO:0000269|PubMed:32272059}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:22215666}. Secreted {ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:35794369}. Note=Secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore following cleavage by CELA1 (PubMed:35794369). Associates with heterochromatin and mitotic chromosomes (PubMed:17185418). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:35794369}.
Interaction partners:
- Interleukin-1 receptor accessory protein
- Interleukin-1 receptor-like 1
- Interleukin-1 receptor type 1
- Caspase-1
- Myeloid differentiation primary response protein MyD88
- Cytokine receptor-like factor 2
- Interleukin-5
- Interleukin-13
- Interleukin-17 receptor B
- Thymic stromal lymphopoietin
Sequence:
MKPKMKYSTNKISTAKWKNTASKALCFKLGKSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLKTGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSSITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKDEKKDKVLLSYYESQHPSNESGDGVDGKMLMVTLSPTKDFWLHANNKEHSVELHKCEKPLPDQAFFVLHNMHSNCVSFECKTDPGVFIGVKDNHLALIKVDSSENLCTENILFKLSET
Protein: Without children, isoform A (Q9VB55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEEISSLDSFGADSNARPESATPRSEEQQDQDRQQTAPAASETLDTPASPPAEDAAAQESKPPPSKEADDDFEQISEGSLDADDNQSRDKAASTPADPVDAEEPAEEPTPNEEPQGGEDEQPQTEAVRVDPQEEPEEAEEETDALQATAEEVEAAAAEADAVDGGPASPEAMDVDEGEVDAEGEAEQEAEDDAALDREATDDVDMQSVGADSHQAEDAEPPEGRDEVDTSLEEQENGQDPDEREKDAAADEDDPDAEGDAESEQVDENAEETGEAEHGDDTVENVLEPEESDVCLIPDDQETEVTEAEKELARENAEKAAEEEEAEERQAKTPDNDRKSPADAAADPEDDSAAAVDATDVSPTTPTADGVAAAANEEEAGGDVPDPDEPTAEESSSAGAGEPGSTPKIIISWIVGSVQKCKQCGDEKNCGFRYRSPEESEEMDKEKENDKAEENAEEGEEEEARQKPAAPSGFEYICDTACVDALLEDQPGKYFVRRKKFLVEEVVREEGAAEAEASADGEGGDAEEEATPANTQDCLQCKDKTRCKYFIKQDQDCFYICNDDCFNLLNAEEPDKFKLKRHSIRVRNIGATTLQPPQNSPTKRTDGSVVARTVEEAETARLDRIESFRRRCADCEADINTDEKQLMWETMDFCNEVCLGSYQRTIGSTCETCKQEVSSIALGKYCVRFGFDVRQFCCAGCLNTFKKGLKTCSCCQKDISGGQEGFLAPVGDKDQFKDFCSQSCLRRYESMCNPRRKLRTDVCGVCNNQKPVRVEMLLEDREHYFCSNPCFSAFKFVSNVNADPCAMCSKYFERRSAESYTIYNEQQSPKVFCSRVCINVYIIVNRHIVSCQWCKVKKYNFDMIYQIGGPHDQETLTCSINCLTMHGVSCNISARAVTKCDNCSNFNTPQYHLTMSDASMRNFCTYQCVMQFQNQFARAPLTLDSDLPPSSAGSSKSQQQSNRGNKNAAPFPTGLPKRVKLKLSHTGKGGVGGKKSGSGTMLPVISTVQSLASGETEARIGNLTVRRKRGRPRESGTSSPPLSMPGVHPPAQRGRPRKHAVDYSARSPSPTMSGGSSHMGIPVRRNTTTTMDFGPATVTETKIITVPPYPKAVRNVNISCKPLTVTQGEQCSPDVRDCATQTEKDYSNKVLIPVPVPIFVPQPMYMYSAPFPVPVPIPLPIPVPIFIPTTRNTAQGILKEIKKIQDKMPEDPLEAELLMMAEMVAEEKHESDSDSDNEIKPDPGLVALQYQNSLESVAQQQQQQQVVDVSGAGHNPYGDDMLQIALKMATGDYDNHHQTSTVDLETSMTANTISSQSPMGHDGMGQMGVHHLDQQHHMLDATQRTARGRKRGVGVVMDPPNRNSRSPVKRQRGGEMDHSALQQQSQQAQQPQEKPDAQMFLKYTFGVNAWKQWVMTKNADIEKSSMRRRPFKTELLQMTADELNYSLCLFVKEVRKPNGTEYAPDTIYYLVLGIQQYLYVNGRIDNIFYDPYYERFTECLDEVARKFSVLYNDSQYIVTRVEEEHLWECKQLGAHSPHVLLSTLMFFNTKHFNLTTVEEHMQLSFSHIMKHWKRSSQNSKVPGSRNVLLRFYPPQAGLDANPRKKKVYEQQENEENPLRCPVRLYEFYLSKCPESVKTRNDVFYLQPERSCVPDSPVWYSTQALGQDALQRMLHRVKMVKEINIALLTT
Protein: Hemolymph clottable protein (Q9U572)
Organism: Penaeus monodon (Giant tiger prawn)
Function: Forms stable clots in the presence of calcium.
Subcellular location: Secreted. Note=Secreted in hemolymph.
Interaction partners:
Sequence:
MKALILLLLGACQALQPGLEYQYRYSARVASGIPSINRQFAAAGIQADVTVQMAADYSVVVQFSNIEVGDLNKVLDCDLRAPLPIEYHPLEDYVDLLEKPFRVIMNESHVPSYMEGPEEPIWISNVRKGFVNIFRVPLFWSTELHSTKLNYGAVEETLVGRCQNWYTSMKLPVNLAEEVNVQREHFMEEDIQRDAYSSSYTTKTKSKTSSKTSSKTSSKTSSKTSKTGKTSPGQLANVPHIEDTLWSVRRTTDFDMCENLVSLQIHSSKYTEDIIQRSSVASYLIRGDTHRRIEQVVVEGTITVLTNKEQHEHVDTFTNQTLELKAVREVGEPITVTYDVHPHYDWQYDIERPQGDQFIPLEQVLTGRPVTDQIVNSIMEYIKKTVDDLSHRMEHYPAKPENLAYIIGRLVEAVANLDYPYIQTLYTHFDGKGTMQKYIFVQLVIHAGTEPAVNFAVDNLSDILFYVTFYESIGVSLRTPAPIPKIMHSLINGEEGLHHSLGLMNFATLAHDACLSEDRKHFYFDYSCGPKTTCDPELIITNFIPYLVRELGNQGKDVWQRLIYLQALSNLGTPQTINVLKPIILGVTETNIFMRTNAIWSLSAYNMHKTALSQIYEILMPIIENKGEQFEIRNIAFLTLATWGPGHAWWQQLAVSTWHDPSPQFANFVTTTIYSISDSHTKLAETVSRIKHLCKPAAPASILHSTNFFLHEYLFSEEHGSRVNFAWFASVHGAIPEEVFLRIQREFFYGYTKVLKIDGQQRGLYNLMQLMKQKMTKPQKRPQSSAQEIVSGMWEELKEKIGFTSPESASDATLWLKLDRLIYVALQYHFMEGAPIPYGMYSGKPFYDKDLNTLIAFPTEIGIPFSVLYVAEDATWLNINGNPETSMTSGKMKVNVDFIFETSQVQFVDARAHVPWSKRPAVASGVYADTQLVLPLNVHASFDMYSQEIQLSIEPTNTQKIDVIKFEFIPYTVLENNYPGDVLVIENEYKPILHGEVPLFNDKHQAFPSDVGLWIQVATEGDIHHTPSIYEIITQLFSAHTSTHIWEQSIVFDPTLSTTKTVSFTFNYVSTGGSGSLVDRGDYDDGQISQGSFDEDFGQFSQVAGGSDQDIMEVDSFGTQSQTIERIMRLQQALISSGGHVRTISVEVELQGTPTRNYEASLTWAISSSASTRSSKVQVTLIKHPAVGVLEDPYTICLNAQIVKPHFNPFFTTEDVLTANYHSTVKAELFEGETCEEAPVLLLEASFDVSSNVKERVKEAIEKGCDYSTYAPGIDIITSPLYDHSHITATWTPDFPDNLKNITYYVDDIIKASLSKKIEFDHTSAHHASRVEIDATKCIETGLWTVRTEKPYAVSIINELELPAWANPIFTPAPLATTLLYGLTVGRTPVSCTIDETKVRTADGKVFAYEPSECWNAMTLDTTFDQRGAMLVRNTGQWEVRIIWQKEGLVIDMSPTNFLVNGEPAKGTDNRYTVLHHDDSHTIVFESGTSVKVSDKVEVLLGLDHRGHTTGICGNFDGEPSNDMVGPKGCYYTDGPLFALSWASPGEGCASFMYKNLKRDVVWYQENCPHFTYEPTGVTHADALYDCTEWVYHQRTEGQYHCKALSPMPVCRPECVASHPITTSVEYECRFSGHQQQAQQQQQQQVQGTQWEECFPHFYTLTYPSSCIPQ
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (P00349)
Organism: Ovis aries (Sheep)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate 1-dehydrogenase
- Ribose-5-phosphate isomerase
- GDH/6PGL endoplasmic bifunctional protein
- 6-phosphogluconolactonase
- Transaldolase
- Transketolase
- transketolase
- Gluconokinase
- Mannose-6-phosphate isomerase
Sequence:
MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVLGAHSLEEMVSKLKKPRRIILLVKAGQAVDNFIEKLVPLLDIGDIIIDGGNSEYRDTMRRCRDLKDKGILFVGSGVSGGEDGARYGPSLMPGGNKEAWPHIKAIFQGIAAKVGTGEPCCDWVGDDGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGLGHKEMAKAFEEWNKTELDSFLIEITASILKFQDADGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQNIPFEGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPGLQNLLLDDFFKSAVENCQDSWRRAISTGVQAGIPMPCFTTALSFYDGYRHAMLPANLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGSVSSSSYNA
Protein: Brevinin-1OKc (C0HL10)
Organism: Nidirana okinavana (Kampira Falls frog) (Babina okinavana)
Function: Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=6 uM) and against Gram-positive bacterium S.aureus (MIC=12.5 uM).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P86027}.
Interaction partners:
Sequence:
FFGSIIGALAKGLPSLISLIKK
Protein: Aquaporin 9, putative (Q388I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQSQPDNVAYPMELQAVNKDGTVEVRVQGNVDNSSNERWDADVQKHEVAEAQEKPVGGINFWAPRELRLNYRDYVAEFLGNFVLIYIAKGAVITSLLVPDFGLLGLTIGIGVAVTMALYVSLGISGGHLNSAVTVGNAVFGDFPWRKVPGYIAAQMLGTFLGAACAYGVFADLLKAHGGGELIAFGEKGIAWVFAMYPAEGNGIFYPIFAELISTAVLLLCVCGIFDPNNSPAKGYETVAIGALVFVMVNNFGLASPLAMNPSLDFGPRVFGAILLGGEVFSHANYYFWVPLVVPFFGAILGLFLYKYFLPH
Protein: Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (X5D8S6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL
Protein: Short-chain dehydrogenase/reductase family member NovK (Novobiocin biosynthesis protein K) (Q9L9F7)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: Non-catalytic subunit of the NovJ(2)K(2) heterotetramer that catalyzes the NADPH-dependent reduction of the tyrosyl moiety of L-beta-OH-Tyr-S-NovH intermediate to yield the tethered beta-ketotyrosyl-S-NovH in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Interaction partners:
Sequence:
MTRVAVVAGGGEHTGPAVALRLAAGGFDVALLGSEFTSADKTVRRVEEYGRQCVTVRAELSDARSVAVAFGRVRTALSGPAVLVTCVGPQPLPDGLPEDESADEQRYTAVRRALRPVFVCCQAGAGQLLRHRWGRIIIVTEPADADGNTWRTSRPVLDGLIGFTRSAALELARSGTTVNLVAPADRAADSRAPAHRAAGDDSAGSYADGVAHVTEFLVDERAVGITGQAIRVAARADVPLLRER
Protein: serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (Q9VQL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phosphoseryl tRNA kinase, isoform A
- Asparagine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- Glycine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Serine--tRNA synthetase-like protein Slimp
- Lysine--tRNA ligase
- leucine--tRNA ligase
Sequence:
MVLDLDLFRSDKGGNPDLVRENQKKRFKDVALVETVIAKDTEWRQCRHRADNLNKVKNVCSKVIGEKMKKKEPVGAMSEDLPADVTKDLTEIVAETLQPLTVNQIKQLRVLIDDAMTENQKSLELAEQTRNTSLREVGNHLHESVPVSNDEDENRVERTFGDCEKRGKYSHVDLIVMIDGMNAEKGAVVSGGRGYFLTGAAVFLEQALIQHALHLLYARDYVPLYTPFFMRKEVMQEVAQLSQFDEELYKVVGKGSEKAEEVGIDEKYLIATSEQPIAAYHRDEWLPESSLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKVEQFVLTSPHDNKSWEMMDEMIGNAEQFCQSLGIPYRVVNIVSGALNHAASKKLDLEAWFGGSGAYRELVSCSNCLDYQARRLLVRFGQTKKMNAAVDYVHMLNATMCAATRVICAILETHQTETGIKVPEPLKKYMPAKFQDEIPFVKPAPIDLELAAAEKQKGKKEKTKKDPAAG
Protein: Heat shock protein SSB1 (EC 3.6.4.10) (HSP70 chaperone SSB1) (G4NAY4)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Chaperone that interacts with the histone acetyltransferase HAT1 and mediates its translocation from the nucleus to the cytoplasm during germination and starvation conditions. Within the cytoplasm, HAT1 regulates autophagy via acetylation of the autophagy-related proteins ATG3 and ATG9.
Subcellular location: Nucleus {ECO:0000305|PubMed:30776962}. Cytoplasm {ECO:0000305|PubMed:30776962}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- SIS1
- Zuotin
- Stress-induced-phosphoprotein 1
- Hsp70-like protein
- Chaperone dnaJ 2
- Chaperone dnaJ 3
- Heat shock factor protein HSF24
- Small ribosomal subunit protein uS5
- Hsp88-like protein
Sequence:
MSTEVYDGAIGIDLGTTYSCVATYEGSNVEIIANEQGSFTTPSFVSFTADERLIGEAAKNQAAMNPANTVFDVKRLIGRRFDDPTVKKDMESWPFKVVDEDGNPKVEVEYLGTTHKFSPQEISAMVLVKMKEIAEAKIGKKVEKAVITVPAYFNDNQRQSTKDAGAISGLNVLRIINEPTAAAIAYGLGSGKSEKERNVLIYDLGGGTFDVSLLNIQGGVFTVKATAGDTHLGGQDFDTNLLDHCKKDFQRKTKKDLSGDARALRRLRTACERAKRTLSNGTQTTLEIDSLFDGEDFSLQITRAKFEELNQTAFKGTLDPVTQVLKDAGVDKAAVDEIVLVGGSTRIPKIQKLLSDYFGGKKLEKSINPDEAVAYGAAVQAGILSGKATSAETADLLLLDVVPLSLGVAMEGNIFAPVVPRGTTVPTLKKRSFTTVADQQQTVQFPVYQGERTNCSENVSLGEFTLAPIPPMRAGEPVLEVVFEVDVNGILKVTATEKTSGRSANITIANSVGKLSTSEIENMISEAEKYKTNDEEFTKKHEAKQQLESYIARVEDIISDPTLALKLKRGQKEKIENTMSEAMAQLELGESTADDLKKKELALKRAVTKAMSSR
Protein: Apoptosis-related protein (Q8I359)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S19
- 40S ribosomal protein S28e, putative
- Small nuclear ribonucleoprotein E
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S11, putative
- 60S ribosomal protein L30e, putative
- 60S ribosomal protein L35, putative
- 40S ribosomal protein S3
- 60S ribosomal protein L34
- 40S ribosomal protein S4
Sequence:
MNIEKAEAKSKLIEMSKQNIENKTKKELELKQKQEELLEKRRLILKSLLTPEAHARLSRIAIVKEEQARKIEDIIIRNSQMGLIYNKIDDDHLIKIIEQINDKIYKKDPVIEIRRRKQFDDDDDFNEEDYM
Protein: Probable protein-export membrane protein SecG (P9WGN5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein translocase subunit SecE
- Protein translocase subunit SecY
- Protein translocase subunit SecA 1
- Protein translocase subunit SecA 2
- Membrane protein insertase YidC
- Sec translocon accessory complex subunit YajC
- Signal recognition particle receptor FtsY
- Protein translocase subunit SecD
- Signal recognition particle protein
- Probable cell division protein WhiA
Sequence:
MELALQITLIVTSVLVVLLVLLHRAKGGGLSTLFGGGVQSSLSGSTVVEKNLDRLTLFVTGIWLVSIIGVALLIKYR
Protein: Carnation, isoform C (M9PF72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFPHLKGHGQRVNLQLLQEAACRELLQQLDRIEGSKVIVLDETMIGPLDLVTRPKLFADRGIRLLALKPELHLPREVANVVYVMRPRVALMEQLAAHVKAGGRAAAGRQYHILFAPRRSCLCVSQLEVSGVLGSFGNIEELAWNYLPLDVDLVSMEMPNAFRDVSVDGDTSSLYQAAVGLVQLQRLYGRIPKIYGKGEFAHRVWEHAKQLGRDERTLYNGDKGVVDQLILLDRSIDLLSPLATQLTYEGLIDEFYGIRQNKLTLPAENFPSDGALPGGGGSGPRVEESQSLLGDTEKKTILLHSGEQLYAELRNKHFNEVTKLLARKAREIHVQMHATSQDKSVQEIKSFVENLLPQLMAQKKATSEHTAIAGLLHEQVNAVRFADDLAAEQEFMVCADIDKPSAYIEDLIACRVELNRVLRLICMQCHAASGFKEKLLNHYKRELVHVYGLEVLLTISNLEKSGLLHLQTESRAYSVLRKTLHLTVDDNVEIEPKDISYVHSFYAPLTARIVEHSLKPLGWQTLKSQINNLPGPTFEDFQAQLVGIGGRHTVTTVSEGSLLNVPRVVLVCFVGGCTFAEIAALRFLAAQEDNNVEFLIATTKVVNKHSFLDSLMSSXGRRLSRLEAYRLSNAHGLARG
Protein: Probable oligoribonuclease (EC 3.1.15.-) (O94626)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: 3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA exonuclease 3
- Uncharacterized exonuclease C637.09
- RNA exonuclease 4
- Uncharacterized mitochondrial carrier C12B10.09
- mRNA degradation protein pet127
- Uncharacterized nucleolar protein C2C4.08
- Uncharacterized protein C25H2.10c
- UPF0612 protein C337.02c
- Probable transcriptional repressor C1348.12
- Uncharacterized transcriptional regulatory protein C11D3.11c
Sequence:
MQGAFLNNRIILQSYHIKKRLYSKRTSSLHSRFLQPTYRKNICQISKPIFQQDLSTNTNFISKLKSPFSNLKMSNLKQPLVWIDCEMTGLEVGKHVLMEVAAIITDGNLRPVEEKFDAVIKLDEKQLSEMNDWCIEQHGKSGLTERCRQSNLTVKDVENQLLAYIKKYIPKKREALIAGNSVHADVRFLSVEMPKIIEHLHYRIIDVSTIKELAKRWCPDIPAYDKKGDHRALSDILESIGELQHYRSYWLS