lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasm. Rough endoplasmic reticulum. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Sequence:
MGIVIQHNKDRLVRPKQPLSEDITLLVKIYRLPGSKCSTAPFNKVVLRRLFMSRTHRPPMSVSRMIRKMKLPGRENRTAVVVGTVTDDVRIHEIPNLKVSALKITRRNRTRILKFVQIMRFVGLALAAPNRQKSVLLSAPRNARDVSRHFANAPSIPHTKPYVLSNKLRRRGSKLTYNN
The following text describes a protein:
Function:
Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.
Subcellular Localization:
Mitochondrion.
Sequence:
MEAMLKSSGLQKFYRKSDNLTIVDAYAGYGWFSTALYNSLQPKKLFLMDPSNYSKEPLSHLQAQDPEVITYSNYDPFQWRSYYPVYESISKAYNKPDRTEVSRDFLFVANLAYTRGESLLYQYLLCILHQNWLQRYGRVRMLIWISSASAEKLTHGSRRTKLQDKTVALKELDERIDKLKANIAKSELWLKRPNLSEKSENSHNKKLDKYRNTLEKLEKKRAESVSLIENRRFKSTVIREMTCDYRYLIGGNAKHTKRSKPVTTEAHRQVQIKKRLEGHKKRVPQMTCNPYDKDALVYYENDYENMFCPQKTTSLGGLVLLELTPKNVKLERLDEWFFVVTRLFVASILPIGRTLETLGPGATEWMSPHLSPAILSSKISEISIPDLEHIVEVFWRWPFKPQVLIDTYEERMVSTPDESTFDNPLFDIDDDVEGGGSDVDDDLM
The following text describes a protein:
Function:
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein.
Sequence:
MAMRLNENLDDNGEMHEINVTPFIDVMLVLLIIFMVAAPLATVDVKVNLPASTSTPQPRPEKPVYLSVKADNTMFIGNDPVTDDTMIAELTALTEGKKDTTIFFRADKTVEYETLMKVMDMLHQAGYLKIGLVGEETAKAK
The following text describes a protein:
Function:
Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP. Binds to and modulates the structure of the actin cytoskeleton.
Subcellular Localization:
Apical cell membrane; Lipid-anchor, GPI-like-anchor; Cytoplasmic side. Note=Accumulates near the inner, apical surface of highly polarized epithelium in tubules of nephrons.
Domain:
The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
Sequence:
MEIGVSVAECKSVPGITSTPHSKDHSSPFYSPSHNGLLTDHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSATKVEPIEKASGRQLPPHIELSRSPSDSMAEGERANGHSTDQPQDMLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEHEKEQFCIRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQKKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQLQQLQQQQQQQLSTSQLCTAPAAHEHLDSIEHTKEDVVTEQIDFSAARKQFQQMENSRQTLAKGQSTPRLFSIKPFYKPLGSINSDKPPTILRPATIGGTVEDSSTQAAKEQKALCVSESQSAGAGTGNAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPNALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEVHTSKEGSEQQEPGAMVEEAGSQAPGSEKPQGMFAPPQVSSPVQEKRDVLPKILPGEDKTLREKGPSQPPTAVQPSGPVNMKETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAQNAPSLPSRTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGAQRPKNLMQTLMEDYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYANQEEEDNE
The following text describes a protein:
Function:
Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Sequence:
MPLPDFRLIRLLPLAALVLTACSVTTPKGPGKSPDSPQWRQHQQDVRNLNQYQTRGAFAYISDQQKVYARFFWQQTGQDRYRLLLTNPLGSTELELNAQPGNVQLVDNKGQRYTADDAEEMIGKLTGMPIPLNSLRQWILGLPGDATDYKLDDQYRLSEITYSQNGKNWKVVYGGYDTKTQPAMPANMELTDGGQRIKLKMDNWIVK
The following text describes a protein:
Function:
May hydroxylate diterpenes.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MESLLAAGAGGIGVAAAAAVVAATLAVVPPKDRGNNPPPAVPGLPVIGNMHQLKEKKPHHTFTKWSKTYGPIYTIKTGASSVVVLNSTEVAKEAMIEKFSSISTKKLPKALSVISRKNMVSISDYGDFYKMAKRNIMLAILGFNAQKHFCDTRERMVSNVLSSLHKLVAVDPHSPLNFREVYTTELFGLSLIQNLGEDVCSVYVEEFGREISKEEIFHVLVHEILSCVVEPDWRDYFPYLSWLPNKSFETIVSSTEFRRDAVMNALIKRQKERIARGEARISYIDFLLEAKNSTQLTDHQLMLLLAESIAAAVDTVLVTTEWAMYELAKNPDKQEWLYREIREVCGGKAVTEEDLPRLPYLDAVLHETLRLHSPVPVLPTRFVHDDTTLAGYDVPAGTQVMINVFGCHMDEEAWESPGEWSPERFLGEGFKLADRYKTLAFGAGRRTCAGSQQAVSIACVAIARFVQELQWTLREGDGDKEDTMQYTALKLHPLHVHLKPRGS
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Domain:
The RING-type zinc finger domain is essential for ubiquitin ligase activity; The SBD domain (substrate-binding domain) mediates the interaction with substrate proteins. It is related to the TRAF family.
Sequence:
MASQLDRVIMCPICLDTMTKPIIQCQTGHSMCGDCVKDNLVKNCPQCRGPISTTRNYQLEQIIENMPRDLKCPCFFADKGCKYMLSPTEKADHEVECKNRKFLCEGRKFAKWKCEWFGNYGELEQHFKDVHRNSMEYKMQTEMDIRLDKDFRDVQIISFFNGAQYFWYKFVVDVALQRVFWVFQFIGPKKQAKNYYYEFEISNGPIRKFKVTEVCDNDVVKAEDLFRDEKCVSLSFNSVKSYLNDNGKLPIKFRIMAMRKHNEASK
The following text describes a protein:
Function:
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MPIDYSKWDKIEISDDSDVEVHPNVDKQSFIRWKQRDIHEKRMQRNIEIKSILIQLTMYAKLNERVDYLLEKLTSTELLDSEKVMSKLNSEFDPQEKFDYDKLIKDKGSTLRKGLKDLKFDREEIENTPCYNEMIEDLFVQIKDDHPETKTDGDKLIEYLKEHRNRIDDVLSKQTIKLDDLLYQKAQLIVSDDLHTGFDRSFLNKDKPEEKEENQDKPKAPEAKKTTVTTTETINSPKPVEENTDKEILDELEILPATKEFAKIPSDNLSKAAEFLIKHPSICTEQQKDALIMTAFDLQLENKSDEAKHIVHQSLLLQYVGQLSDNGKAAPANVINAIKLFFSKIAAESSPAKHAFLEDVNQTFNHIKGRCEIIKEEQKQNAANKEGTGEEEEEEALIQLKALDDNTELSVNIPQEGTKEYEIFTTKLPIEFQNAIKTESIDEVNKEFAKLKIEDAERILEIFNECGVIGISGYIEDEKEFEELKKEYAHETANQEEDQSASVEDTVD
The following text describes a protein:
Function:
Mediates cell growth arrest in response to cadmium exposure, which is essential to maintain cell viability. Regulates cadmium stress specific genes.
Subcellular Localization:
Nucleus.
Sequence:
MDFTPNSAINHLNLKFDDVPVSDDFSKDDLAEQLNVFTNPYFLDLEPSSMLSEGYYGFVSQPSGSSNSNKQEKNVQQQNPEKISTLQQVKEEEVSNTFSAPLNATGNFSSANPASIDLAYLDLQKLLTLPDHSKETQEKTSSQRELFEQKSSVASASKDNVSSSSILQGSASSKLLPDQSARQHQVLVGQTAIPTSEASSSINNTPLQAPVSSFADQNAFTNPLSTFASPDLASVSSPSLSSYKGAQSPNANSKRTKATSAIRTAAEEDKRRRNTAASARFRIKKKLKEQQLERTAKELTEKVAILETRVRELEMENNWLKGLIRPTSNF
The following text describes a protein:
Function:
Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release. Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via its binding to the substrate-binding domain (SBD). Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Colocalizes with HSF1 to the nucleus upon heat stress.
Domain:
The BAG domain interacts with the nucleotide-binding domain (NBD) of HSP70s and is essential for the nucleotide-exchange factor activity.
Sequence:
MSAATQSPMMQMASGNGASDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPPEGPKDTASSANGPSRDGSRLLPIREGHPIYPQLRPGYIPIPVLHEGSENRQPHLFHAYSQPGVQRFRTEAAAATPQRSQSPLRGGMTEAAQTDKQCGQMPATATTAAAQPPTAHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYIPIPVIHEQNITRPAAQPSFHQAQKTHYPAQQGEYQPQQPVYHKIQGDDWEPRPLRAASPFRSPVRGASSREGSPARSGTPVHCPSPIRVHTVVDRPQPMTHREPPPVTQPENKPESKPGPAGPDLPPGHIPIQVIRREADSKPVSQKSPPPAEKVEVKVSSAPIPCPSPSPAPSAVPSPPKNVAAEQKAAPSPAPAEPAAPKSGEAETPPKHPGVLKVEAILEKVQGLEQAVDSFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEAEQPLQEIMGAVVADKDKKGPENKDPQTESQQLEAKAATPPNPSNPADSAGNLVAP
The following text describes a protein:
Function:
Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Sequence:
MFSKLYNFVRQHKKKIFFSVGLTGGAYLLNRYVQRKLHEWESRTTQNYLDQIKHQHHFESILQTSDSTVLSLLPKIREPLLTILETDSLLEKLKTRPPNRLELWEEMKARILTFAVCSVYAESLLAALLRVQLGVVGGYVYVNSQRSQQTSGGVLPALTSQEIHQRYLSLIQHFFEGGIEELVHVVKAAVVAAFGHVSLKERVSVNDFVVAFDYIKGYVSRGSKPLPGFMRFLLPPLNVESDSQEATVLNTMILETRDILETDDFSKVLATCIDIGFGNLRGEVEESFHIMQMAEGSGDQVATSFALAKLLPVLKNGLVAGRADSFLKQILQVELLRSMLANVYEAFCQTEDVDRLNHNLAPFT
The following text describes a protein:
Function:
Required for the maintenance of viability of cells in stationary phase and in starvation conditions.
Subcellular Localization:
Cell membrane; Lipid-anchor. Cell tip. Note=Also localizes to the site of cell division.
Sequence:
MSAQQFYGDKGYAPAPPQQAYGGPNYYPPQQNYPQQGYAPPQGYPQGGYPAQQPMYVQQPQASDPGGDLCCGLLTGLACCCCLDAMF
The following text describes a protein:
Function:
Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them (By similarity). Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis (By similarity).
Sequence:
MTRTNLITGFLGSGKTTSILHLLAHKDPNEKWAVLVNEFGEVGIDGALLADSGALLKEIPGGCMCCVNGLPMQVGLNTLLRQGKPDRLLIEPTGLGHPKQILDLLTAPVYEPWIDLRATLCILDPRLLLDEKSASNENFRDQLAAADIIVANKSDRTTPESEQALQRWWQQNGGDRQLIHSEHGKVDGHLLDLPRRNLAELPASAAHSHQHVVKKGLAALSLPEHQRWRRSLNSGQGYQACGWIFDADTVFDTIGILEWARLAPVERVKGVLRIPEGLVRINRQGDDLHIETQNVAPPDSRIELISSSEADWNALQSALLKLRLATTA
The following text describes a protein:
Function:
Required for regulation of peroxisome size and number. Also promotes peroxisome division and biogenesis.
Miscellaneous:
MISCELLANEOUS: Present with 382 molecules/cell in log phase SD medium.
Subcellular Localization:
Peroxisome membrane; Peripheral membrane protein.
Sequence:
MTSDPVNTNISSPTLTDRNADESWELLKREFNTLFSNLKTDSKEEGNFTDNKGVIAKKPIVLQDNDDSDFTQNQGKVATATSTTSDRSFKRTLGSIEMKKRYVKKNCQAKFVFNTLEGKEVCSKILQHTLGLLSLLLLTRKIRLLNFSSKLRLVIQQLSLFRYYLRFGNFAINLYKIIKRFRWLREMKKLHYKDQSILFYFKNFRFFDIIEAFYNLTDELILFHKLQSMFGKKNTSHANTNRLMTFVKEQHYILWEVLNILAINKNIEQWRQLIRDEIYLSIYNTSGNAIKEYELKYKLPTNDKVNLELRKNNITLDFYKIILNLLSNLINIKGKRDKYNSELAYEIISVGSGVTELLKLWNRAKVTSANEHTSAV
The following text describes a protein:
Function:
Involved in the biosynthesis of the O-methyl phosphoramidate (MeOPN) group found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the ATP-dependent phosphorylation of the amide nitrogen of L-glutamine to form L-glutamine phosphate, the first committed step in MeOPN biosynthesis. Also catalyzes the phosphorylation of D-glutamine, gamma-L-glutamyl hydroxamate, gamma-L-glutamyl-hydrazide and beta-L-aspartyl hydroxamate. Does not phosphorylate L-glutamate or L-asparagine. Does not act on L-glutamine derivatives with removed alpha-amino or alpha-carboxy groups.
Miscellaneous:
MISCELLANEOUS: The reaction mechanism comprises three steps. First, a histidine residue of the enzyme attacks ATP at the beta-phosphoryl group to form AMP and a pyrophosphorylated enzyme intermediate. Next, the pyrophosphorylated enzyme intermediate is hydrolyzed to generate inorganic phosphate and a phosphorylated enzyme intermediate. Finally, the phosphorylated enzyme intermediate transfers the phosphate to the amide nitrogen of the acceptor substrate L-glutamine. In this mechanism, the gamma-phosphoryl group of ATP is converted to phosphate and the beta-phosphoryl group is utilized in the phosphorylation of L-glutamine.
Domain:
Contains an N-terminal ATP-grasp domain, a specialized central substrate-binding domain for L-glutamine and a C-terminal phospho-histidine domain.
Sequence:
MAELKFKTKAQNLKNLQTKLKKAKVLPLVLTSLEELISNEDKVLQDIQTLKANRLIIRSSSLSEDSMKNSNAGAFLSLANIKADSKDELLKALYEVANSMPSKSDEILVQPMLENITLCGVGFSVDKDNFSPYFCLQYDENGSNSSITDGSSKSAKTYYHYRNYLEFKDIRLQKIIELIKELEVLYDCHFLDVEFAFAIQDDKEELFCLQVRPLVMHEKNNLFHSLPKEALYRFYKRFESLKESRSRVLGDKAIFGVMPDWNPAEIIGLRPKRLAFSLYKEIITDNIWAYQRDNYGYRDLRSHPLIHSFLGIPYVDVRLSFNSFIPKKLDENIAQKLVNFYLDKLNKNHELHDKIEFNIVYSCYDFNSSKKLEELLNHGFNENEIKRLEFSLLELTNKIINPRSGFYLKDIQKAYKLKERYDGIINSNFSLIDKIYWLIEECKRYGTLPFAGVARAAFVAMQLLNSLVEIDFITKEEKDDFLNSLNTVSKNLSKQTNHLNFHNKDQFLKDFGHLRAGTYNILSPRYDEDFELYFDADQKDSKVYLQDKAFVFSKEKTRALNALLKEHGLEINACEFFDFLKQAIEGRELVKFEFTRLLSKAIVYIEELGKYYDIEKEDLAHLDIKSILNLYSSLYSINPKEQFIEEINRNKKEYELTQAIKLPSLLCNADEIFSFYNHSIIPNFITQKSITAFTAKENDKDLEGKIVLIYAADPGYDYLFTKNIAGLITCYGGANSHMAIRASELGMPAVIGVGEENFEKYLKAKKINIECESEQIFCL
The following text describes a protein:
Function:
Transcription regulator that modulates expression mediated by transcription factors of the GATA family. Cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The CCHC FOG-type zinc fingers probably directly bind to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC FOG-type zinc finger is probably essential for the interaction with GATA-type zinc fingers (By similarity).
Sequence:
MSEMVHSRLKQGQGPAAAQQSFYPPGSPASVHKGATCFECDITFNNINNFYVHKRLYCSSRHQQGETGGLVKEGAVTAAAPPVSHAASPQARPVSRAASASPSCPDPAPGGTASEPKVVEVKIEDPGLKDATCSSSSEGEGPGGGQASEGSQSPSGSAEDQDDDPTRTFCQACNIRFSRHDNYIVHKRFYCASRHDPTNQRPHSGKAAFLPQPIRTRKRKKMYE
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MESLINPSHGGGNYDSHSSSLDSLKPSVLVIILILLMTLLISVSICFLLRCLNRCSHRSVLPLSSSSSVATVTSDSRRFSGHRVSPETERSSVLDSLPIFKFSSVTRRSSSMNSGDCAVCLSKFEPEDQLRLLPLCCHAFHADCIDIWLVSNQTCPLCRSPLFASESDLMKSLAVVGSNNGGGENSFRLEIGSISRRRQTPIPESVEQHRTYSIGSFDYIVDDVDSEISESNFNRGKQEDATTTTATATAVTTNPTSFEASLAADIGNDGSRSWLKDYVDRLSRGISSRAMSFRSSGRFFTGSSRRSEELTVMDLEANHAGEEISELFRWLSGV
The following text describes a protein:
Function:
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MRPVSKYGQNFLIDLNLVELIARSAEIGPSDIVLEIGTGVGSLTSIMASQAGAILTVEIDQNLFQLASEELAPFPHVKMIQGDALKNKSTFRDDIMESIREAKSRLPDDSKFMLVANLPYNVATPIVSNLLHQDPPPDRIVVTIQKELGERMVAGPGSKDYGALSIWIQATCRAEIVRILPPTVFWPRPKVDSAIVRLDVDHERGNAIPDLKYFHQTVRALFFHRRKFLRSVVISAMKGRLDKPAIDEILGRLGHGETARAEELNLEQISDLVEALRQAELANE
The following text describes a protein:
Function:
May have a role in processing of pre-rRNA or in the assembly of rRNA into ribosomal subunits. May be involved in pre-mRNA splicing (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSMRLTFKGDKKIQKKKKKNTKSLQSSLESAENDPFWTDANELNELEGPAVIYKIDDDAGVSLGIEEVKESCVLLPLDKVSLEPELTRQVFLLSILNNTILLKSCLGKYMSCSKSGDLYCTQEAVGSQEQWIAENLGSGFWAWKSVSTKKYLTLSREKQDQAIACVSDTVIPEAKWRIRVQTRFLKKNKSSLFDNPTIHSRQLESMAGRKLSTDEKKTLKKAFKEGVLHEALLDLRVSSRSDKYG
The following text describes a protein:
Function:
Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B.
Sequence:
MDLQQELEQEACWKLELDKVTKLDPSKKKKKKKKKRPFIREDATYDSEPDYGYAELLSRVFDMLREEEVSTQRPRTVMMRRPQLLAQGTHITVCLDFAHLCTMMHRKPGHVITFLLGQMETKGWLNKQHQLEMKGLVSSQHFQAVFQRYIDAFVICSCCKSSDTALAEANGISTLSCEMMLQTKTKQKVVL
The following text describes a protein:
Function:
Nutrient-regulated protein kinase that promotes the activity of at least 6 distinct transport systems for nitrogenous nutrients under conditions of nitrogen catabolite derepression. Under poor nitrogen growth conditions, required for post-Golgi sorting of the general amino acid permease GAP1 and the three known ammonia permeases, MEP1/2/3, to the plasma membrane. Also contributes to the stability and the retention of GAP1 at the plasma membrane. Inversely, promotes the degradation of tryptophan permease TAT2 under the same conditions. Activity is regulated by the TOR signaling pathway via phosphatase SIT4. Although thought to be involved in regulation of GLN3-dependent transcription by nitrogen catabolite repression, this seems to be an indirect effect from the reduced uptake of the nitrogen-repressing compound.
Miscellaneous:
MISCELLANEOUS: Present with 284 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Note=Appears to be more concentrated in punctate structures reminiscent of the Golgi or of an endosomal compartment.
Sequence:
MSSLTRLLQEKRKNETSNSSPRTSADTLTTTPESQSLDLHSRNKSSSHIGSVSNSSSSDRNRANVPVPGSVTTVTQIYSEEDSSSTAGSSLDDRNQFSSSFLNANFAHTASFYGTSAQSRDRFGSLINDQGTAGLSSHGGSFAAQNRITSRLSTTSHTSGRAIPSLSSSIPYSVPNSNKDNNSSNSNSSSLSSSWLETYAGGMPNNISAIDSNVISSPKVDSVEPRFVISKQKLQKASMDSNNANATQSRSISRSGSFSSQLGNFFFSKNSKESSNSNSAGMSFSANSNGPSPNIKNPNVTNGSTPIPKPIRARQSSIYSASRQPTGSYTDNFYGSPSSVHDHLPPSQSVPRSQHSSIGDLKRFFKKSSNSNLSSNSNNVIPNGSPLSSGIAVPSHSHSSSHFAAGNNSYSTSYNGNGDTIYSHSHGGSGIPFSKRYIKTGADLGAGAGGSVKLAQRISDNKIFAVKEFRTKFENESKRDYVKKITSEYCIGTTLNHPNIIETIEIVYENDRILQVMEYCEYDLFAIVMSNKMSYEEICCCFKQILTGVQYLHSIGLAHRDLKLDNCVINEKGIVKLIDFGAAVVFSYPFSKNLVEASGIVGSDPYLAPEVCIFAKYDPRPVDIWSSAIIFACMILKKFPWKIPKLRDNSFKLFCSGRDCDSLSSLVTRTPDPPSYDESHSTEKKKPESSSNNVSDPNNVNIGPQRLLHSLPEETQHIVGRMIDLAPACRGNIEEIMEDPWIRSIDMCHLVEDGLSFKVVRGEDHHHTQVDQSEAHIAGLEKKKKKQNNQ
The following text describes a protein:
Function:
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Subcellular Localization:
Nucleus.
Sequence:
MPEGLLVRTFHHSVSPFVGKQVVKTGSNSKNLQSLWLQDTQVHGKKLFLRFDPDEEMGPAGNSSPPEPPQKEAQMEGTVDSNGQKTLDASSRSAELECLKGDTPTGDAGRRLRVSSCLFGSVWVNDFSRAKKANKRGDWRDPAPRLVLYFGGGSFLALYNCQMPWSSSPEVTPTSLEALGQAQPVSYTPLNQKYFSGLGNVIKNEVLYRTGIHPLSLGSVLSEALVDHVVEFSTAWLQGKFQGKPQHMQVYQKEQCPAGHQVMKKPFGPSGGFQRLTWWCPQCQSQLLEEPEQWTQGALHGTLPLGEPDV
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
MPALLVYLIILAIAAGVTFALFGEVGEADVAPADALALFAAATPTASGATSCSLEAAAETTAGADDCGARKSHAAPGDASGIEHIKSLLMKCGVPPQQQEMISFLGRHCCVLPVKSHTVRVLNRPADFYEELKARVMAAQRSITLSALYIGDGPLSRAFVACLEERVRWAAAGGRPFSITILLDYNRMQDRKNLVSLKTLMELAQQTASTASLPVDAAIVGASASSPTTHSPSTLGSSSIVADGERDAEEDEVVRGNSSDDASSATTTTAAAASTGVRVRLFLYQNPSKWNRLFAPFGRAKEVLGVQHTKVFVFDQRHTILTGANLSDDYFATRMDRYMIVKDNALVARWFTQLVRTANRMSHPVVCRKEFAEQLIGGGDTCASRTPNKRGALGHSSSAASPSSCMAAATANGSAPEPLQSPLRWVVEKVSRAVSPPLTSLVSQREGSPTLHRKSNLVILANALQMDPSVDTEAFCARANALLHDFAAWARRLCAVATVDWSCYDTFLFPTVQAGRAGVYHDSVIVKQLLRLSTAEDHIFLASPYLNMHASFVDEVLHGTSYVDCITASVQTNGWNGHNGVAGRIPLFYLQLERSFYYLMKAYSCLRRVHIREFSVKGLTFHAKGLWFMGRRCCPAAAAAASPPGKDDEGDARQHHDGHGADAAAADPCPLESISAPYLVAYGSTNYGYRSVHKDVEAEAFLLTTNDALRETLRQELLFLLQQSVPVTEAQFVGTAMGRFQPVISLLAHLGHDFL
The following text describes a protein:
Function:
The dimeric enzyme acts as a SUMO/pmt3 E1 ligase. It mediates ATP-dependent activation of pmt3 and formation of a thioester with a conserved cysteine residue on aos1 (By similarity).
Sequence:
MPTLMQLSNDMKPLTFVEALRNFKSAKVLLVGAGGIGCELLKNLLMSGVKEVHIIDLDTIDLSNLNRQFLFRKKHVKQPKAIVAAKTASSFNPNVKLEAYHANIKEDRFNVAWFRQFDLVFNALDNLDARRHVNKQCLLASVPLIESGTTGFLGQVQVIIHGKTECYDCNPKEPPKTYPVCTIRSTPSQPIHCVVWAKSYFFPQLFSNDQESDGIIDNVSANEMERREIAELARETTELNELRSSIGQSDNGFEKIFTKMFTKDIVRLREVPDAWTYRSPPKELSYSELLENAEKATSPWLNEQNVWNVAESFAVLRDSIRRLALRSKSSKDDLSFDKDDKDTLDFVAAAANLRAHVFGIQQLSEFDIKQMAGNIIPAIATTNAVIAGLCITQAIKVLQGDLNDLKNIYLAKRPTRVLHCEKTCKPNPYCPTCSFVLLQLGVNDKNMTLRVLVDDILKSRLHYSEEVSVLNDKLIYDPDFDDNLDKTFDDLGINPAKNTILTVLGDSAVEKDDDGEEATRVPLLIEVTFIDSNSTEGLPYQILSNATSIPLKQQPPSNSPEDSQVLTDEINEVNDFSSSERIVINLDEYDIIVDSKTSSHNKQLKRRPSNDTLTQEAKSKKQAKIHTM
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MSSKLPTTLLRRPSALPSTTTYTAYSASRPTPPSCTAHGAQGQQIRNATFVPRHRRPYQFTQLVQLSDGSTFTVRTTMPTALYKSAKDSRNHLLWQPSDKSLKNVELDEAGKLAAFRERYGRGWDLDAKMTPEEEAAAAAALAAGGGAGVPGGKAAKKAAEEALLAKKKKEEEEAAKKAAEAEEADPFDSLTDLISGYATENMNPGLNFKETRHYGKKK
The following text describes a protein:
Function:
Acts as a corepressor of recombining binding protein suppressor hairless (RBPJ) and inhibits Notch signaling in neural stem cells, thereby opposing their self-renewal and promoting neurogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MQKILQTDDITDNQVLRKRKRKRTETANSENANSALEKAQRDPYSGNAFLPGESSSDEETPLMELSKEELCNKIESLKEKLRSIRKENSRLRQSLVMLQVLPQAVTQFEELVGMAETLLKSGGAVSTPASTLWRATNNSSPDSFASLCSNSNSTSSSPSSVKAEEEQHPGEKQFTIERWQIARCNKSKPQKFINDLMQVLYTNEYMATHSLTGAKSSTSRDKVVKPAMNQNEVQEIIGVTKQVFPSADDVSIRRMIGQKLNNCTKKPNASKAPNSQDGILK
The following text describes a protein:
Function:
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Sequence:
MTLFCEQVPYPRLAEAFGTPLYVYSQSALTEAFEHYQTAFAALNPLVCYAVKANGNLSIIKHFASLGSGFDIVSGGELARVLAAGGDAAKTIFSGVGKSEAEIEFALNAGVKCFNMESIPEIDRIQKVAARLGKTAPVSLRINPDVDAKTHPYISTGLKANKFGIAYADALEAYHYAAQQPNLKIIGIDCHIGSQLTDLSPLVEACERILILVDALAAEGIVLEHLDLGGGVGIVYQDENVPDLGAYAQAVQKLIGTRRLKLILEPGRSLVGNAGSLLTRVEFVKYGEEKNFVMVDAAMNDLMRPALYDAYHHIEAVETKDIATLTANIVGPICETGDFLGKDRTIACEEGDLLLIRSAGAYGASMASNYNARNRAAEVLVDGNEYRLIRRRETLEQQMANELACLQAEHQNAV
The following text describes a protein:
Function:
Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress. Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression. Activates BaeR by phosphorylation which then activates the mdtABCD and probably the CRISPR-Cas casABCDE-ygbT-ygbF operons.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKFWRPGITGKLFLAIFATCIVLLISMHWAVRISFERGFIDYIKHGNEQRLQLLSDALGEQYAQHGNWRFLRNNDRFVFQILRSFEHDNSEDKPGPGMPPHGWRTQFWVVDQNNKVLVGPRAPIPPDGTRRPILVNGAEVGAVIASPVERLTRNTDINFDKQQRQTSWLIVALATLLAALATFLLARGLLAPVKRLVDGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEKNQQMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPETVASLQAEVGTLTKLVDDLHQLSMSDEGALAYQKAPVDLIPLLEVAGGAFRERFASRGLKLQFSLPDSITVFGDRDRLMQLFNNLLENSLRYTDSGGSLQISAGQRDKTVRLTFADSAPGVSDDQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQREV