lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
FQTPPPITRHMFSVLALATQILANVNLAAQTVEPIDLAPPPKVRQIRIPGDILIGGVFPVHSKSLNGDEPCGEIAETRGVHRVEAMLYALDQINMQNDFLRGYKLGALILDSCSNPAYALNQSLDFVRDMIGSSEASDYVCLDGSDPNVKKQSQKKNVAAVVGGSYSSVSVQLANLLRLFRIAQVSPASTNADLSDKNRFEYFARTVPSDDYQAMAMVEIAVRFRWSYVSLVYSADEYGELGADAFKKEARKKGICIALEERIQNKKESFTESINNLVQKLQPEKNVGATVVVLFVGTEYIPDILRYTAERMKLTSGAKKRIIWLASESWDRNNDKYTAGDNRLAAQGAIVLMLASQKVPSFEEYFMSLHPGTEAFERNKWLRELWQVKYKCEFDTAPGTTATRCEDIKQSTEGFNADDKVQFVIDAVYAIAHGLQSMKQSVCPDDAIENHWISRYSKQPEICHAMQNIDGSDFYQNYLLKVNFTGKMLLLLQSSSLAFLDIVGKRFRFSPQGDGPASYTILTYKPKSMDKKRSMTDDESSPSDYVEIGHWSENNLTIYEKNLWWDPDHTPVSVCSLPCKTGFRKQLIKDEQCCWACSKCEDYEYLINETHCVACEQGWWPTQDRNGCFDLSLSQLKYMRWRSMYSLVPTILAVVGIIATLFVIAVYVIYNETPVVKASGRELSYILLISMIMCYCMTFVLLSKPSAIVCAIKRTGIGFAFSCLYSAMFVKTNRIFRIFSTRTAQRPRFISPISQVVMTAMLAGVQLIGSLIWLFVVPPGWRHHYPTRDQVVLTCNVPDHHFLYSLAYDGGLIVLCTIYAVKTRKVPENFNETKFIGFSMYTTCVVWLSWIFFFFGTNSDFQIQTSSLCISISMSANVALACIFSPKLWIILFEKHKNVRKQEGESMLNKSSRSLGNCSSRLCANSIDEPNQYTALLTDSTRRRSSRKTSQPTSTSSAQDTYL
The following text describes a protein:
Function:
Major selective outward-rectifying potassium channel of the guard cell membrane. Involved in regulation of stomatal movements according to the water status. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by depolarization. Conductance of the channel is modulated in a potassium-dependent fashion. May interact with the cytoskeleton or with regulatory proteins.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity; The KHA domain (rich in hydrophobic and acidic residues) present in the C-terminal part is likely to be important for tetramerization.
Sequence:
MGRLRRRQEIIDHEEEESNDDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYKAWEMFILVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRTVYKPTRIAFRYLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRINYLFTRILKLLFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTTALYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLISFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTEFINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISIICNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQEAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVNLKDKFGHTPLFEAVKAGQEGVIGLLVKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMNPNSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDVKNAQSSIYPSSLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGLSDGASFVLLSEDQGRITDIDMISDGHKLYMISDTTDQT
The following text describes a protein:
Function:
Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL.
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein.
Domain:
The DBB domain is required for dimerization.
Sequence:
MAASGWGRGCDILIFYSPDAEEWCQYLQDLFVSCRQVRSQKTQTYRLVPDASFSAQDLWVFRDARCVLVLLSAGLVGCFGQPGLLPMLQRACHPPQRVVRLLCGVQPGDEDFQAFFPDWAHWQEMTCDDEPETYLAAVRKAISEDSGCDSVTDTEPEDERELPFSKQTNLPPEISPGNLMVVQPDRIRCGAETTVYIIVRCKLDEKVSTEAEFSPEDSPSIRVEGTLENEYTVSVKAPDLSSGNVSLKVYSGDLVVCETTVSYYTDMEEIGNLLSSAANPVEFMCQAFKIVPYNTETLDKLLTESLKNNIPASGLHLFGINQLEEDDMMTNQRDEELPTLLHFAAKYGLKNLTALLLTCPGALQAYSVANKHGHYPNTIAEKHGFRDLRQFIDEYVETVDMLKTHIKEELMQGEEADDVYESMAHLSTDLLMKCSLNPGCDDELYESMAAFAPAATEDLYVEMLQASAGNPVSGESFSRPTKDSMIRKFLEGNSVKPASWEREQHHPYGEELYHIVDEDETFSVDLANRPPVPVPRPEASAPGPPPPPDNEPYISKVFAEKSQERLGNFYVSSESIRKEPLVRPWRDRPPSSIYDPFAGMKTPGQRQLITLQEQVKLGIVNVDEAVLHFKEWQLNQKKRSESFRFQQENLKRLRESITRRRKEKPKSGKHTDLEITVPIRHSQHLPEKVEFGVYESGPRKSVLPARTELRRGDWKTDSMSSTASSTSNRSSTRSLLSVSSGMEGDNEDNEIPEITRSRGPGPTQVDGAPVVTGTPVGTLERPPRVPPRAASQRPLTRESFHPPPPVPPRGR
The following text describes a protein:
Function:
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MVVTKLATQRPKLPSVGRLGLVDPPAGERLAQLGWDRHEDQAHVDLLWSLSRAPDADAALRALIRLSENPDTGWDELNAALLRERSLRGRLFSVLGSSLALGDHLVAHPQSWKLLRGKVTLPSHDQLQRSFVECVEESEGMPGSLVHRLRTQYRDYVLMLAALDLAATVEDEPVLPFTVVAARLADAADAALAAALRVAEASVCGEHPPPRLAVIAMGKCGARELNYVSDVDVIFVAERSDPRNARVASEMMRVASAAFFEVDAALRPEGRNGELVRTLESHIAYYQRWAKTWEFQALLKARPVVGDAELGERYLTALMPMVWRACEREDFVVEVQAMRRRVEQLVPADVRGRELKLGSGGLRDVEFAVQLLQLVHARSDESLRVASTVDALAALGEGGYIGREDAANMTASYEFLRLLEHRLQLQRLKRTHLLPDPEDEEAVRWLARAAHIRPDGRNDAAGVLREELKKQNVRVSKLHTKLFYQPLLESIGPTGLEIAHGMTLEAAGRRLAALGYEGPQTALKHMSALVNQSGRRGRVQSVLLPRLLDWMSYAPDPDGGLLAYRRLSEALATESWYLATLRDKPAVAKRLMHVLGTSAYVPDLLMRAPRVIQQYEDGPAGPKLLETEPAAVARALIASASRYPDPERAIAGARTLRRRELARIGSADLLGLLEVTEVCRALTSVWVAVLQAALDVMIRASLPDDDRAPAAIAVIGMGRLGGAELGYGSDADVMFVCEPATGVDDARAVKWSTSIAERVRALLGTPSVDPPLELDANLRPEGRNGPLVRTLGSYAAYYEQWAQPWEIQALLRAHAVAGDAELGQRFLRMVDKTRYPPDGVSADSVREIRRIKARIESERLPRGADPNTHTKLGRGGLADIEWTVQLLQLQHAHQVPALHNTSTLQSLDVIAAADLVPAADVELLRQAWLTATRARNALVLVRGKPTDQLPGPGRQLNAVAVAAGWRNDDGGEFLDNYLRVTRRAKAVVRKVFGS
The following text describes a protein:
Function:
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU (ISU1, ISU2 or ISU3). In a second step, the cluster is released from ISCU, transferred to a glutaredoxin, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MMLRVAGRRLLGAASGVGGGEAAPAVAAAGAASRGYHERVVDHYNNPRNVGSFDKDDADVGTGIVGAPSCGDVMKLQIRVDEGSGRIVDARFKTFGCGSAIASSSVASEWVKGKQMEEVVAIKNTEIAKHLSLPPVKLHCSMLAEDAIKAAVKDYEAKKGKLAKADE
The following text describes a protein:
Function:
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB3D may be involved in the insulin-induced exocytosis of GLUT4-containing vesicles in adipocytes.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MASANDTRHQTQVQKDVADQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVYRNEKRVKLQIWDTAGQERYRTITTAYYRGAMGFLLMYDITNQDSFYAVQDWATQIKTYSWDNAQVILVGNKCDLEDDRLVAREDGQRLANELGFQFFEASAKDNINVKQVFERLVDIICDKMNESLDTDPSILTNQKGPSLQDTPPDGQSGGCGC
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MERDDCRRFQDSPAQTTERRVKYKPKKKRAKDDDDEKVVSKHPNFRGVRMRQWGKWVSEIREPKKKSRIWLGTFSTAEMAARAHDVAALAIKGGSAHLNFPELAYHLPRPASADPKDIQAAAAAAAAAVAIDMDVETSSPSPSPTVTETSSPAMIALSDDAFSDLPDLLLNVNHNIDGFWDSFPYEEPFLSQSY
The following text describes a protein:
Function:
E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location. Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAQESDDRYRPKLFYEDVVSRQKVGLIQYGVVVASFLESDEEDDEEFEPQVKLKRGHVRVTWYPDGQREVVPEAKLHLVDRSLMPRDFVRRHTAGQDSQGGTVLNTDITVDLQIIGTNKVIPGVNSKKLKPLQRILPYEYVVYGVWLGRVRDVNAHLILRLSNGARCSMWVGDAAQLEDIRVQSDAFWEEEHAFYPGQTLMGPAKAFKDVEWLSGRQPILSSKAKFKVTVEDLALKEVNVEWQTRGFSPPKKQPSELDEDLKPPEAAIQGDNINNLRKPEHFMYTHITFGDRAVYRLTEEDLGKVQILAPPSMTKEPAAQPDESVDDVAKEKTKGAAAAYELAKLLSEEAAKAIDFAEKKTREASQANDRIKEITKEAFELIQQAKDKASDVPAMQDSISKLAEDFSGNKTFTEEALQQFLTTKSTLENVYSTMEEAQRKSAEIAEAMEITKVKSKEAAAANEAAKIKSREASEASKVVKQMSQEARKAVEKMEGEIRASKRKIEKSKEERVGAETSGRVQGRRERRQNENKHDHDTQESGPSKAGTDNEDESASVQSGATVANTSLNRVDLSDNLKTECSELEERDKKNARVELESESVINDKKDLALEGASGGPMNDTVMDHPELFSQACELSSSIVAKCDTLGGAVSEFCSGLNGIMADISGTLELVNKVEKDLSPQAQNNSISESDRLKSDATHTNRLSESQTTTVKLLNGEVDSDGQLLTNGASVGSGKTIPSSGKAAEDSSKPSVLEDKDFIADDEEDLLTDDDNADSECSSSTASSRSSKGGRSKRLGVTLGVKTLKKAHRRVKKRKKRGAQQEWIPGDVVPVEVVNVSTLVDVMWQDSTIEHGIPANELAPIQHCDEHEFCPGDFIVDKRVVPKKDMYGFVRTVDHKARTCQIQWQEAAPGHPQGFLTHEEEEVSAYDLGDHPDYTYRIGDLVVRIADSTQAACRTPTSEKPCIGQVLRTNGDGSLAVVWIDNSVSSVPPQDLYRVDSEDEGGWSGDDSEWESVDSDEDWETDSDPASGDEVDGKLKSAEKPKEKKKDKKESTSSPATKPSHEQKGTTRTQEPVEEVTSPEEEVMSPEEEVMSPCSQVQEAKWVSAKGEGFSVSETCPVCHKFRDLDFGPANMKSFFSNIKKELTLLSTSLPEGILVKTFEDRMDLFSVAIKGPHNTPYEDGLFLFDLKLPDAYPLIPPLLHYLAYHSGRLNPNLYEDGKVCVSLLGTWQGKGTEKWTKDSNLLQVLVSIQGLILVSEPYYNEAGFEKDKGSQEGLENSRCYNEMVLLKMVQTMSKMTLNPPDIFKEEIIEHCRQHGHRMIQRLESWLELSETDSPNGAETKANSDSTVSSINKETTTSEHQQASAASNQPLTRQSSTTVAPSGGNDQPKTTMLPKTDHSVVGENQSSTNRDQPTTSSKQAAVTSISQQPACATSSKNHSSTSANQSGLAEVSSNQLGINFNSSEQTDSNQSSVGASKLPPTTDSMCMSEVFDGSGASQVSGVTLSPNPPGFPLFPLSKGFRMSLRSHLVAYRSVLHKLGIQES
The following text describes a protein:
Function:
Catalytic part of CAK which activates cyclin-associated CDK1/CDK2/CDK4 by threonine phosphorylation, thereby allowing MPF activation.
Subcellular Localization:
Nucleus.
Sequence:
MDKYNIEALIGEGTYGVVSRATVKATGQIVAIKKIRKILIQNQTDDGINFSAIREIKILQELKHDNVVNLLDIFAHKSNVYLVFELMQWDLQEVIEDKSIILKPADIKSYMKMLLQGIEACHRNWVLHRDLKPNNLLMSINGDLKLADFGLARQYGSPNKVFSPQAVTIFYRAPELLFGAKSYGPSVDIWSIGCIFAELMLRTPYLPGTGEIDQLRKICSALGTPNESNWPGVTCLPNYIKFTDHPATPFKQLFTAASDEAIDLISKMLLFNPSNRISAADALNHPYFTSGVKHTNPADLPVPFAKKASLLQQRQVLAQVQQQLLQKQQQQQQQQQQQIQSQPEPIQVDNVEQTQQAQQV
The following text describes a protein:
Function:
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Cytoplasm.
Sequence:
MTFSAPAPTQLDPVVRHLYVHVPFCPSICPYCDFHVLTRQAGLVERYLERLEQEAAELAAAYAVDLDTVYLGGGTPSFLRDHELRALVESVQRHLGWGRAENTLEINPGTVSTERAALWRSLGFDRASVGVQSLDDATLKFLGRRHDARQARDAVSRLIAQDFRVSGDLITAVPGQPLDSDIHGLVELGVGHVSAYTLTIEPGTEFARRGVQVDEDAEREGFERTEELLAGHGFSRYEVSNYARAGQESRHNLSYWQGKTYLGLGPGAAGHYPVPTPGADALTLRRTNPHLHDWLVGQQGETLLVDPHEYVTDALFMGLRLRRGLDLADLTRRSGVDVAGRYGLVIERQVRLGLLEHSGTNLRATAQGWWVLNRIVREFMEVDAAETA
The following text describes a protein:
Function:
Seems to inhibit myoblast differentiation. Transcriptional repressor of E-box-dependent transactivation of downstream myogenic bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-CAGGTG-3' and 5'-CACCTG-3'.
Subcellular Localization:
Nucleus.
Sequence:
MVAGEKRQDFPKASCLVEANGSCSACEELVGSCHLPDKEASSNPSDPLQPWDSTSAIACVSLPLLPHHGETLGTSGPEPQETSLVGPRAGQAPSVTLKDSFNLPPVLVLPTRWPPILGSDGALDEHLRAEGTSRVPGSFECIHCHRPYQTLAGLARHQQLHCHLPTGCAFTCRYCDKEYASLGALKMHIRTHTLPCVCKVCGKAFSRPWLLQGHIRTHTGEKPYTCSHCSRAFADRSNLRAHLQTHAGTKKYRCALCPKAFSRMSLLVRHEDAGCCPGP
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis.
Subcellular Localization:
Cell junction. Cell projection. Cytoplasm, cytoskeleton.
Sequence:
MSLKLPRNWDFNLKMDAAKIARSRSVMSGEAVTTRPGSPSSMERPLKLGWLKKQRSIVKNWQQRYFVLRGQQLYYYKDEDDTKPQGCLSLQGSTIKEVSGNPEEGGKFIFEIIPGVSGDQNRAGQDTCVLMANSQSDMEEWVKSIRRVLGSTSGAVFGQCLAETMAYEQKFGQHQVPILVQKCAEFIREHGVNEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRELPEPVVPWIQYEDFLLCGQTLDMDQKKGHQDLLKQLSLLPRDNYNLLSYICRFLYEVQLNSAVNKMSVDNLATVIGVNLIRPKIEDPATIMRGTLPIQKVMTVMISNHADLFPPSKDVLPSPTAQQNDKKTPILRSSVGWDSAEDSTLPRAESSVQRQMKDHPSASRAPGLAVSSRAPSEDTGLQPSKDTVGMWKMQARKRTQTLPNRKSFLTAASPGEKGSSDRNDIFNSDFWKGSTQSNPHSVLTEGHKRTLSHDLFKLLDLHRASAYDNVPTSHLESSSSSPSPASSCSDKEFQPCPSPCHHPQDPTSPASSPSEVFQPASESKESLQSMVLKLQREMDEQKETYEEQIKSLEKENYDVWAKVVRLNQDIEREKKKSEELELKLKNMERLQEDLEKKNKMLEEEIKTIAKSRSKSDAKTN
The following text describes a protein:
Function:
Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular Localization:
Cytoplasm.
Sequence:
MAKQAIKRAKILAVKNNNKIGVLLINLGTPDEPSVPAVRRYLRQFLSDPKVIDVPSLVRWIIVHLCILPFRPKRSAKLYQKIWMPEGSPLLVYSEMLRERVGETLGDDFCVALGMRYGKPSIETALKKLQEAQCRQLIVLPLFPQYSTSTTASALEEVRAKNSFKEMTVIDRFFEEPHYIDSMTTLIHENLNEFQPDYFLFSYHGLPERHLVKSGCQLAICNRKNNCSPISSSNENCYRAQCFETSRLIAKKLNLTDQQYGVAFQSRLGRAKWIEPYTDKYLIELSKKGIKKLMVVCPSFPVDCLETLEEIGIRAQSQWQRLDGETLKLIPSLNAHPQWVNAIAKMAKKSLQLF
The following text describes a protein:
Function:
This methylase recognizes the double-stranded sequence 5'-CCWGG-3', methylates C-2 on both strands.
Sequence:
MQENISVTDSYSTGNAAQAMLEKLLQIYDVKTLVAQLNGVGENHWSAAILKRALANDSAWHRLSEKEFAHLQTLLPKPPAHHPHYAFRFIDLFAGIGGIRRGFESIGGQCVFTSEWNKHAVRTYKANHYCDPATHHFNEDIRDITLSHKEGVSDEAAAEHIRQHIPEHDVLLAGFPCQPFSLAGVSKKNSLGRAHGFACDTQGTLFFDVVRIIDARRPAMFVLENVKNLKSHDQGKTFRIIMQTLDELGYDVADAEDNGPDDPKIIDGKHFLPQHRERIVLVGFRRDLNLKADFTLRDISECFPAQRVTLAQLLDPMVEAKYILTPVLWKYLYRYAKKHQARGNGFGYGMVYPNNPQSVTRTLSARYYKDGAEILIDRGWDMATGEKDFDDPLNQQHRPRRLTPRECARLMGFEAPGEAKFRIPVSDTQAYRQFGNSVVVPVFAAVAKLLEPKIKQAVALRQQEAQHGRRSR
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAPLSEAREREIEEWRQARAKIRADRHAFLKDQVLAPNEPLPPKNPGFSARWSGWWATQGAKFVPMVVQTPVRKGGMFFLKWVLPLWVGHYLFKYNFLGKDDGMTGVVYRRPRVYPNDSKFNPPPAPGEA
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin; The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSFKVNWNSLETEPLTNWTKELLTSALNSGKSPNILALNITIKDLNFGKIAPDFEILEIGELDRDRFRGIFKIDYQGDFHLTLHTKVQANPLNIYYHNSLEKEVCNYSQDEFITPNFLLSNEQFAIPLDLKLSDIKINGIGIIVFSKSKGLTLVFRNDPLDSIKVSSTFDTVQVLANFLQKQIENQIRDLFRETLPTLIHQLSLKYLSLDNNINEIKSKLSQQDSVSMTNNELASSLKLFDDEENEFPLIYSSKNLQKNMQLFKSRETFRLSAPKFKNIVQRTRLDKFTKSYPNLLNSLYANNADLQHRFVNNINHGHNNNSNTSSTGIPIELLVSHDDKQHYGKTDNLLKDISSIQANNFYKYSNKDAPNKPKRRRIKVHKKSKVKQDDNTVKASELQNVDSTFMESRSISPQETIDTTSTLIESAPMTRNVSTNIKSPTLETMSTGSSSSASSQVIAHPTPKRAHQPADSTVSTTTINKENHIDYIKARNLYQDFIQMSQSPGYYDKVISNGRGIGLGNSGGNYFGFNGNGNGLERTMSASPIKHLNKDKKSINYIDTSKINEKLNQFRLDGGKNSANTNNSSGGKNFRPGFTRNESNGQQGILFEAFNFPSVAPPPPPYC
The following text describes a protein:
Function:
Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3.
Sequence:
MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE
The following text describes a protein:
Function:
Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side. Mitochondrion.
Sequence:
MAEKTITVEEVLKHNTRDDLYIVVKDKVYDISKFLDAHPGGEEVLVDLAGRDASGPFEDVGHSEDAQELLEKFYIGNLLRTEDGPQLPTTGAAAGGSGYDSSQPVKPAMWLFVLVMVVAYFAFRKYVLK
The following text describes a protein:
Function:
Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 which are related to motility. Regulates specific signaling activities in the cilia, such as the daf-2/insulin receptor-like transduction pathway.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Note=Moves along the axoneme.
Sequence:
MATENPQTWALWLILSEMASDMQEDKKVAKILVLGPPKAGKTTLCTFLADFMEDGDTLKKGEDSGERERKFEFEFTSVYRPTKGVRIQEFETHEFFTEQEQNELGGTRRLEDSEIQLWDVSGDKKYEDCWPAIKENAEGVILVVNPEEHKGSDLQQWFYEFVEKENIDLSCVMVILNEQGAKKTNHEQISGFEILPKLRGVHHVAHHFGSEAMQVKMEVNSFMASVLKMDQRQMGSGVDHGLGYADEQEDDF
The following text describes a protein:
Function:
Probable aminotransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Sequence:
MPSETITPLLAHRARTNIQWFTHKHMRQVSRLNAKQHRVNMMTAENWSIRDELVDQYKTLFAQHLSPRHLSYADGMGGDAELLQAAADFFNRVFAAHSRVQPAHLVVGAGCSSLLENLLYDICEPGEGVLIETPFWGGFETSFVLRSNVTAVHVRPPCHGNGSADLDRLVSAYIEAYERALRQAPCRIKAILVCNPHNPCGHIYPPRVIQALLQFAQRHDLFYISDEIYALSTLDEQTAFTSVLSIDVAALGVDLARVFTLYSISKDLGSSGLRLGFGITQAHPDLRLSLAISNHSRVSTFTSLVITALLHDPEAATAILHQNRAALQRSAKLISDFLAFHQIPFVPPAAGVYVWARLGWRSSSRPGDEPSWDEEARLNDRFEAAGVSVGAGQGYCASEPGWFRITFAIPREELVAGLRRIEQVVGMEGQKWTAI
The following text describes a protein:
Function:
Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Sequence:
MRRYSANVGTLWSHLPLLERIEAAARAGFRAVEMHFPYAVPPGEVRDAIQKFDLTLLGINSPPGDIARGELGIAAIPGREDEFAESLHMALNYCQVAGAQALHIMAGNTFGYWRTACLETFKSNVALAADLAISNNVRLLFEPLNRALHPAYFYHEVDQLARLLDDVGHPWLKIQFDMYHVGMHHRRVRDVLKRNWSRIGHIQIAAVPDRGEPRAGDVDIMEVLDEAELRGYGGWIGCEYKARGNVEEGLAWREMARFSETG
The following text describes a protein:
Function:
Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on eukaryotic initiation factor 2 (eIF2) gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHHWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTTENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL