lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MADGKGDAAAVAGAGAEAPAVAGAGDGAETESMVRGHRPVSPAPGALGLRPCLWQLETELREQEVSEVSSLNYCRSFCQTLLQYASNKNASEHIVYLLEVYRLAIQSFASARPYLTTECEDVLLVLGRLVLSCFELLLSVSESELPCEVWLPFLQSLQESHDALLEFGNNNLQILVHVTKEGVWKNPVLLKILSQQPVETEEVNKLIAQEGPSFLQMRIKHLLKSNCIPQATALSKLCAESKEISNVSSFQQAYITCLCSMLPNEDAIKEIAKVDCKEVLDIICNLESEGQDNTAFVLCTTYLTQQLQTASVYCSWELTLFWSKLQRRIDPSLDTFLERCRQFGVIAKTQQHLFCLIRVIQTEAQDAGLGVSILLCVRALQLRSSEDEEMKASVCKTIACLLPEDLEVRRACQLTEFLIEPSLDGFNMLEELYLQPDQKFDEENAPVPNSLRCELLLALKAHWPFDPEFWDWKTLKRHCHQLLGQEASDSDDDLSGYEMSINDTDVLESFLSDYDEGKEDKQYRRRDLTDQHKEKRDKKPIGSSERYQRWLQYKFFCLLCKRECIEARILHHSKMHMEDGIYTCPVCIKKFKRKEMFVPHVMEHVKMPPSRRDRSKRKLLLKGSQKGICPKSPSAIPEQNHSLNEQAKGESHEYVTFSKLEDCHLQDRDLYPCPGTDCSRVFKQFKYLSVHLKAEHQNNDENAKHYLDMKNRREKCTYCRRHFMSAFHLREHEQVHCGPQPYMCVSIDCYARFGSVNELLNHKQKHDDLRYKCELNGCNIVFSDLGQLYHHEAQHFRDASYTCNFLGCKKFYYSKIEYQNHLSMHNVENSNGDIKKSVKLEESATGEKQDCVNQPHLLNQTDKPHLPEDLFCAESANSQIDTETAENLKENSDSNSSDQLSHSSSASMNEELIDTLDHSETMQDILLSNEKVFGPSSLKEKCSSMAVCFDGTKFTCGFDGCGSTYKNARGMQKHLRKVHPYHFKPKKIKTKDLFPSLGNEHNQTTEKLDAEPKPSSDTNSDSPDEGLDHNIHIKCKREHQGYSSESSICASKRPCTEDTMLELLLRLKHLSLKNSITHGSFSGSLQAYPSSGAKSLQSVSSISDLNFQNQDENMPSQYLAQLAAKPFFCELQGCKYEFVTREALLMHYLKKHNYSKEKVLQLTMFQHRYSPFQCHICQRSFTRKTHLRIHYKNKHQIGSDRATHKLLDNEKCDHEGPCSVDRLKGDCSAELGGDPNSNSEKPHCHPKKDECSSETDLESSCEETESKTSDISSPIGSHREEQEGREGRGSRRTVAKGNLCYILNKYHKPFHCIHKTCNSSFTNLKGLIRHYRTVHQYNKEQLCLEKDKARTKRELVKCKKIFACKYKECNKRFLCSKALAKHCSDSHNLDHTEEPKVLSEAESAARFSCNQPQCPAVFYTFNKLKHHLMEQHNIEGEIHSDYEIHCDLNGCGQIFTHRSNYSQHVYYRHKDYYDDLFRSQKVANERLLRSEKVCQTADTQGHEYQTTRRSFNAKAKKCGLIKEKKAPISFKTRAEALHMCVEHSEHTQYPCMVQGCLSVVKLESSIVRHYKRTHQMSSAYLEQQMENLVVCVKYGTKIKEEPPSEADTCIKKEENRSCESEHTEHSHSPGDSSAPIQNTDSCHSSERDGGQKGCIESSSVFDADTLLYRGTLKCNHSSETTSLEQCNIVQPPPPCKIENSIPNPNGTESGTYFTSFQLPPLPRIKESETRQHGSGQENTVKNPTHVPKENFRKHSQPRSFDLKTYKPMGFESSFLKFIQESEEKEDDFDDWEPSEHLTLSNSSQPSNDLTGNVVANNMVNDNEPEVDIPHSSSDSTIHENLTAIPPLIVAETTTVPSLENLRVVLDKALTDCGELALKQLHYLRPVVVLERSKFSTPILDLFPTKKTDELCVGSS
The following text describes a protein:
Function:
Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.
Sequence:
MASNSVLYRCSLVSYQYTSAATIIVGRRTVAISGNGFRACKPIRLARNCCSYSCSYPNPNDSAFVVANDEKYGNKQNISLTPRLYDYILSNVREPEILRQLREETASMRGSQMQVSPDQAQLLAMLVQILGAKRCIELGVYTGYSSLAVALVLPDSACLVACERDAKSLEVAKKYYELAGVSHKVDVKHGMAADILKSLILNGESCSYDFAFVDAEKRMNQEYFELLLQLVRVDGVIVIDNVLWHGKVADPLQVNDAKTVSIRSFNKNIMEDPRVSISMVPIGDGMTICRKR
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of flavin mononucleotide (FMN).
Sequence:
MRFYRPLGRISALTFDLDDTLYDNRPVILRTEREALTFVQNYHPALRSFQNEDLQRLRQAVREAEPEIYHDVTRWRFRSIEQAMLDAGLSAEEASAGAHAAMINFAKWRSRIDVPQQTHDTLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYFLAAEKLNVPIGEILHVGDDLTTDVGGAIRSGMQACWIRPENGDLMQTWDSRLLPHLEISRLASLTSLI
The following text describes a protein:
Function:
Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for the translocation of the substrate across the membrane. Required for full urease activity and plays a significant role in the virulence of S.aureus during urinary tract infection (UTI).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MHKIFSKNNLIFFVFVAFIFVVIVLQFFVSSENATKVNLSQTFEPISWLHLLGTDDYGRDLFTRIIIGARSTLFVTVLTLIAIVVIGVTLGLFAGYKKGWIERLVLRFIDVGLSIPEFIIMIALASFFQPSLWNLVISITLIKWMNYTRLTRSIVNSEMNKPYIKMAQLFHVPTRTILIRHLTPKIIPAIIVLMVVDFGKIILYISSLSFIGLGAQPPTPEWGAMLQQGRDFISSHPIMLIAPASVIAITILIFNLTGDALRDRLLKQRGEYDESH
The following text describes a protein:
Function:
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
Miscellaneous:
MISCELLANEOUS: Present with 1860 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSKFTWKELIQLGSPSKAYESSLACIAHIDMNAFFAQVEQMRCGLSKEDPVVCVQWNSIIAVSYAARKYGISRMDTIQEALKKCSNLIPIHTAVFKKGEDFWQYHDGCGSWVQDPAKQISVEDHKVSLEPYRRESRKALKIFKSACDLVERASIDEVFLDLGRICFNMLMFDNEYELTGDLKLKDALSNIREAFIGGNYDINSHLPLIPEKIKSLKFEGDVFNPEGRDLITDWDDVILALGSQVCKGIRDSIKDILGYTTSCGLSSTKNVCKLASNYKKPDAQTIVKNDCLLDFLDCGKFEITSFWTLGGVLGKELIDVLDLPHENSIKHIRETWPDNAGQLKEFLDAKVKQSDYDRSTSNIDPLKTADLAEKLFKLSRGRYGLPLSSRPVVKSMMSNKNLRGKSCNSIVDCISWLEVFCAELTSRIQDLEQEYNKIVIPRTVSISLKTKSYEVYRKSGPVAYKGINFQSHELLKVGIKFVTDLDIKGKNKSYYPLTKLSMTITNFDIIDLQKTVVDMFGNQVHTFKSSAGKEDEEKTTSSKADEKTPKLECCKYQVTFTDQKALQEHADYHLALKLSEGLNGAEESSKNLSFGEKRLLFSRKRPNSQHTATPQKKQVTSSKNILSFFTRKK
The following text describes a protein:
Function:
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Plays a role in the catalytic function of EntF. It is required for adenylation of amino acids in non-ribosomal peptide biosynthesis.
Sequence:
MAFSNPFDDPQGAFYILRNAQGQFSLWPQQCVLPAGWDIVCQPQSQASCQQWLEAHWRTLTPTNFTQLQEAQ
The following text describes a protein:
Function:
Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MGCFGSKEKEDPEKKTEEKKYSWDKREKIDPALYTVENLNDEFVIREPGSIDGQQFIIQNCKNTRIYLFDHIASITVDDCVDCCIIVGPVMGSIFIRDCENCKFIVACQQFRTRDCSKLDVFLSCATQPIIEASAKLKFGCYQLNYDGLKEQFEKSQLSLFCNNWCNIHDFTPVTEKSNSSLISEECSLNEMFPGITDSSTSKLNISTNRGDSVVLVSLGSRPKPSLDSCFVAVFPSNSSYQVARNIVTLLKDKCVLVQIREINLTVGDLKRIFPNSDLSVHHAAISSGSVIGIELNGDNCCNVCTDVVSTLPPEEQRSIYSSLNKDEVSGETERFFDFCDIQMNN
The following text describes a protein:
Function:
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Subcellular Localization:
Cytoplasm.
Sequence:
MRLIASDLRSGVERLGDMIAEAKTIVPFTGAGISTECGIPDFRSPGGIWTRNRPIPFDGFVASQEARDESWRRRFAMEETFAAARPGRGHRALASLYRAGKVPAVITQNIDNLHQASGFAHEHVIELHGNTTYARCVGCGQTYQLDWVKRRFDQDGAPNCTVCDEPVKTATISFGQMMPEEEMQRATALSRACDLFIAIGSSLVVWPAAGFPMMAKRAGARLVIINREPTEQDDIADLVIRHDIGETLGPFVGN
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Can participate in redox reactions and is able to catalyze dithiol-disulfide exchange reactions with other proteins, albeit with relatively low efficiency. May form transient disulfide bonds with nascent polypeptides in the endoplasmic reticulum and thereby promote efficient glycosylation.
Miscellaneous:
MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKWCSTYIIIWLAIIFHKFQKSTATASHNIDDILQLKDDTGVITVTADNYPLLSRGVPGYFNILYITMRGTNSNGMSCQLCHDFEKTYHAVADVIRSQAPQSLNLFFTVDVNEVPQLVKDLKLQNVPHLVVYPPAESNKQSQFEWKTSPFYQYSLVPENAENTLQFGDFLAKILNISITVPQAFNVQEFVYYFVACMVVFIFIKKVILPKVTNKWKLFSMILSLGILLPSITGYKFVEMNAIPFIARDAKNRIMYFSGGSGWQFGIEIFSVSLMYIVMSALSVLLIYVPKISCVSEKMRGLLSSFLACVLFYFFSYFISCYLIKNPGYPIVF
The following text describes a protein:
Function:
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular Localization:
Cytoplasm.
Sequence:
MGESIMKKAKEDAPSVDDSKKLAIEQAMSQIEKQFGKGSIMKLGSDSAKQTVQVIPSGSLDLDIALGIGGYPIGRIVEIYGPESSGKTTLTLSAIAEAQKRGGVAAFIDAEHALDPSYAKKLGVNIDELLVSQPDNGEEALEICESLVRSNAIDLIVIDSVAALVPKAEIEGDMGDSHMGLQARLMSQALRKLTGTIAKSKTVVIFINQIRMKIGVMFGSPETTTGGNALKFYCSVRLDIRKIETIKEKEESVGNRVRVKVVKNKCAPPFKQAEFDIIFNAGISREGSLVDLGVKHDIIHKAGAWYSYNTEKIGQGKEAAKEYLKNNPEIALTIENMVRDLNSLPLLVQENNKKSRKEEKLEQAAG
The following text describes a protein:
Function:
Bifunctional enzyme that possesses both UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities, and serves as the initiator of the biosynthetic pathway leading to the production of N-acetylneuraminic acid (NeuAc), a critical precursor in the synthesis of sialic acids. By catalyzing this pivotal and rate-limiting step in sialic acid biosynthesis, this enzyme assumes a pivotal role in governing the regulation of cell surface sialylation, playing a role in embryonic angiogenesis. Sialic acids represent a category of negatively charged sugars that reside on the surface of cells as terminal components of glycoconjugates and mediate important functions in various cellular processes, including cell adhesion, signal transduction, and cellular recognition (By similarity).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEPVGALHLIQAAKLGNVKAQNILRTAGTALGLGVVNILHTMDPSLVILSGVLASHYIHIVKDVIRQQASSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIH
The following text describes a protein:
Function:
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MTDSVTVGSDAYEQYVEAGDILTTVLSEAADRVTVGATHLEVASFAEERIRELGGEPAFPVNISVNEEASHAAPGADDDTEFGEDMVCLDVGVHVDGHIADAATTVDLSGTPELVEAAEESLAAAIDMVEPGVQTGALGAEIQDVVEAYGYNPVVNLTGHGMDVFDAHTGPTVPNRGVDSGAELAVGDVVAIEPFVTTGTGKVTEGAATEIYEVVSSGTVRDRRARQLLDDLEQFDGLPFAARWLDGARAEMSLTRLERADIVRSYPVLKEADGELVGQDEHTLIVTEDGCEVVTA
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MPSAPWKAYCNTFLGEISSLSFDPYTDLLWTANPSGTVVSHFLPTTTLPPSDQDRRITRYTSFKSHTYRSPSTELLLAERGVLSLADKSLKFTNRRGIPYWFLSTAFQDACSMAFTAPKSAELIIGGAKPELVLLNASTGALVRRIDISQSGKSTLNSAQPSTGFSPTTHLRRSQSLICCGARSGTVTLRDPVTLKEEHSMMTHYAGLEQMETEGNYLVTCGYSLKQGHPVRDPLVKVFDVRALRPLAPITFSSSPAHVRFHPRMSSTLFITSSTGQLQIIDLAHPIPNSSFYQLDVGTFITDMCISSSGDGLAYAEADGVVHLWTTAVGEMDLGDESVRSNTKPIKWSRGNMPIALPDSVEESAPVQWTDETPLSSIGMPYYSTELFSVLPSENYITPYSPLYQRRALPDTDLSVRASHHQSSNTTHEVFDGGGQKFEVQYISNPKKTKRYQASLPTQPIVSSSGRSATARVGSPSQNLGQLIPNSKRKLSIPLFRSEKEKEKAKTLGRGKAHMEANLVGNESERDDEISFDMSLDDFHEMPKWYRQVEIKYSKFGIEDFDFGFYNNTQYSGLETHIVNSYTNSLLQVLYHTLPVRKVAESHIALSCTTQNCMLCELGFLFKMLDDAQGVNCQTSNFSRAFSINQRAIALELMDHQHQEFCLHQSQIMPRLGDQSTNTQKIPISSKSYSSLIQLCHHFLLDQIAEDASKISTDYPFESLRSHPINTQIRTTNSTTSVATISNHLLPSPIGDIYTTRWQTTQSCPSCHHQISRTSFTKVIEMTYPRKALSNEPKPSTDFCSILKNSMIRETTAKSLCSNCNQYTHQRWRRQPDDLGAGNKALPTVLALNTGVTNSEQFEIWLDRRAKSAFVSSSSTKPANLEDDSSSVNEHFLQPEIGISIEPLPDLPQETNTSSSCRISIGDNHPIKIPQNAVIYELRGLIVQIQSDDETPHLVSLIKVNNHHKITSPSTTSTTLNLDDKPQSENGAGAGAWYLFNDFLVKKVSQEEALSFPACWKVPCVLYYVRKDFDEVLDFTKLPANTVDKSILLKEINLSKCRDVNKIRHEVLKEDELPKKGDLVAIDAEFVSLQQEEVDYKSDGTRLVRRPSQMTLARVSVLRGEGSKTGVPFIDDHIQTFEPIADYLTEFSGIRPGDLDLNASPHTLVPLKVAYKKLRLLVDLGCIFIGHGLSKDFRIINIHVPPSQIIDTVDLYYIASRQRKLSLRLLSYLILRHDIQNAGTHDSIEDARTALQLYDIYRQLNNEGVWKDELESVYRKGKEMGWKVPADKLRSPLPAPAIPPAPSPCTSATPKPPSSTTSSTVSGRNTAVQAPRFTPSTLSAASATYFPPAGIAASKPPNSRSLQPVVRQTLSSTSTPAADQGHAEPAASFYRSIPQNSQTKASPPAPNFGHSILGTLNQTGPSAYNNNNSNNSRTVTTTTVFQRYTTAPPPVFEPKKKPPAFNPMAPSFVHSSSSSSSSSATSTNRPLMSTTSSGPSSSTYTHNGAQHEKKSHTGLPYHHHHTSLSHSSLGSASLPGSSIDTHSSGSSLEFFPSNNNTLIGHPPRPNNNNNSNNSNELYSFHPLPHHHPHQQPQLPHQPLPLPASHVYSNPNPLPPHSPHNALHHHQHHQQHHHQVSNEFVYHHPHHHHPHPHHPHLFHQEQHFPIHSSSSSSSTSTPSNPTTSSNTTAALSNHHQLHSPITSSTHSPSSNPNLSSLLSGSHNEFNFIG
The following text describes a protein:
Function:
Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also has a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.
Miscellaneous:
MISCELLANEOUS: The reductase activity of YfcG is unique in that no sulfhydryl groups in the protein appear to be covalently involved in the redox chemistry; MISCELLANEOUS: Glutathionylspermidine (GspSH) binds YfcG about 10 times more tightly than GSH. Moreover, GSSG binds 100 times more tightly than GSH and 10 times more tightly than the GSH analog, GSO(3-).
Sequence:
MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLAEKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS
The following text describes a protein:
Function:
Polycomb group (Pc-G) genes are needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (Bx-C) complexes, and hence for the maintenance of segmental determination. Can act as a modifier of position effect variegation (PEV) (By similarity).
Subcellular Localization:
Nucleus. Note=During S-phase in early embryogenesis.
Sequence:
MEELCKQPPPPPPLPPPPSSPSVAIEDPLPNGKGGGAVVVPSIAKLPEEELLGSVTMHNCPGTRASARVIQKMKQDQTRPMTPPPSEREPNKKEEKAAQKTPSQLKTGSGKTTWTNVERNCFFDALNEFGKDFEAVANCINAKLKRRNANSDYSFKTKDQVRQHYYQTYHKICKYVRFSEELKKPAQELYTLINYGEMRRKLQFLTEKHFMKLKQLVYQGQITVRCKGKNIRIKTPSCKALRRLNQLDDSLEDIRLPSKVEVLVTPANMEAFGRVQSLAQNPRGRIIVPLHKKLISFIKTFEYKWRSANQRLHEEKSAIFPSSLPSTATNNNNNNNETEPMQPSVASLDPSMCFQPRPGVAIHRPLLSITAYLSSISICLTAYEERMGFKVRSETLGNLAGMPVAASKRLRTESGSEKRSPETKKPKPSASPPLEKTLDDGPLEGNLMKMENSSGDELAEEIHEFLGDILEAMPHPQAVTIPALSTTTGDTTTVAVALETSHDPVLQAYPASADLSHAMVTSVIQTTCAAAPAPSTLVSGSLTAPSVARSKRKEAKEAAAAAQARNFKPLLSDDILKRIRKGWTQANAADITIGDLYVVFGQDSKLELEYYWCEVDSSTAMASSILTINTVAPSSSSVATQTGTSASNAIQTSASSNCYVSATSTSSTSLPYNPNDCDSVERVRAVTTSSVSNKLKHLLLVANLSERVRKRQCNCGHTCDRKRDLMTKAQQLAEATATGVVDGNFRTPMLPVRRPISNIDPVRQLSALTRQKINRQVLVQRRLLPPTSVGDRPYDLLSVRQLHSGLFEPIDRVDGTSSGGISSSGSKPDSSMGATAASQDQEPGDQRALDFLNDEATQASNRDMPNLDICVATSRTDVSGSLNEAVQDESTNQSFFHGSMSPMHLLRDSTSNARWLEDNINDFSLTSLLGHLDEIDATRDILDPSSSMSIISESSVDFRHKFQEIAALLQQQEKD
The following text describes a protein:
Function:
Transcription factor. Transcriptional activity probably positively regulated by phosphorylation. Modulates expression of target genes, acting by binding to regulatory cAMP response elements (CRE). Acts downstream of the calcium-triggered CaMKK-CaMK1 signaling cascade, consisting of the protein kinase kinase ckk-1 and the protein kinase cmk-1. Plays a role in learning and memory, feeding behavior, stress response, entry into the dauer stage and modulation of lifespan. Involved in commitment to the developmentally arrested larval state known as dauer, acting by positively regulating the expression of dauer-inhibiting TGF-beta-like daf-7 in the ASI neurons. Plays a role in both associative and non-associative long-term memory (LTM). Involved in modulating feeding behavior, acting by regulating transcription of tryptophan hydroxylase tph-1 in serotonergic ADF neurons. Regulates transcription of genes involved in endoplasmic reticulum (ER) stress. Involved in modulation of lifespan, in response to raised temperature, but independently of the heat-shock response pathway, acting by regulating transcription of FMRFamide-like neuropeptides flp-6 in the AFD neuron; [Isoform c]: Plays a role in associative long-term memory (LTM) and learning; [Isoform e]: Plays a role in associative long-term memory (LTM) and learning; perhaps required at the time of acquisition and/or the consolidation phase of memory formation.
Subcellular Localization:
Nucleus.
Sequence:
MATMASTSNCSPVATSPLMMLLFKALQEGGDSEDEARRRREQLNRRPSYRMILKDLETADKVMKKEPEETPPSSVDASPLQFQSVMRPPPTAPPTSAATPNRILPSSNAASPYGSPLGSSILSNQPLVLPFAPINGDFDFSAAIAAASQPKVFPGGPQQNGLGGGGGGGGVPGPSSGIAGMSVQPPTSSTPSQQQSVQSLEGTSGLIGSAMKPMLGIDAVSFPEFGTTDWQSPMLSGGYSSSPSPTMTGGSMRMGGGPLHGEDESNRKRQVRLLKNREAAKECRRKKKEYVKCLENRVSVLENQNKALIEELKTLKELYCRKEKDGM
The following text describes a protein:
Function:
Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body (By similarity).
Sequence:
MQHNTFLPNDAVEEQKQNPYYGILRAVETDLRLGQRWCELKVHVLDIDLKTKRPLLSGIPVNGQLKDKLQYVLPLYLQETISIEFLSSVFDSMKKLSLPLVKDARGLSGDEFFLYLGIMCSDSTIVYYKITDGLIKPRQNDEE
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MEFCPSCANMLQYELPNMHDARFFCPTCPYVAYVDRKVKIKRRQHLVKKEIQPIFTLDDYKNAPKIEEPCPRCGFPEAAYRTQQTRSADEAETRFFRCMNNNCGHTWVDYS
The following text describes a protein:
Function:
Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Subcellular Localization:
Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEISREYFPNNYSSHGRPNIKDVLREGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALSSLQLPDGMGLIVRTAGVGKSADALQWDLSFRLKHWDAIKKAAEGRPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKVLELAKEHIAALGRPDFSSKIKLYSGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDTTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTHEVHAIVPVQIASYLLNEKRESVNAIEKRQGGVRAVIVPNDQMQTPHYSVLRVRKGEEVPSLSYLLPQLHEAEMAQPLEEATIERKRPEQPALATFSLPTEVPPEEAPTVAKAKPAVATPAAVSTDVEQPGFFSRLFSGLKNMFGASAEAEVQPAEVVKTDTSENRRNDRRNPRRQNNGRKERNDRTPREGRDNSSRDNTNRDNTNRDNTSRDNANRDGANRDNSNRDNSGRDNVSREGREDQRRNNRRPAQPTTTSQGQTEVVEADKAQREEQPQRRGDRQRRRQDEKRQAPQEIKADVAEAPVIEEVQPEQEERQQVMQRRQRRQLNQKVRIQSANDELNTLESPVSAPVAQVVVAEVQEEVKLLPQITAQTDDDSANERTTNNENGMPRRSRRSPRHLRVSGQRRRRYRDERYPAQSAMPLAGAFASPEMASGKVWVRYPVTPVVEQVVVEQIAIEQTTTVEQTAIVEQVSVANIVTAQLPVEQVQNTVAEQESSATPSVMTTPTVAVATAAVTLAPQHKPGGSSSSAAAVPGRAPIVAAVPVVAETTAAETVVAKTEAAIDAVAVVEPMAAVESIAAVETATVEPVVTEEPNVTEPAVAEPAIETDPVEETTSVVEIAPTVEPTPMIEDTAVVVAATVVDTTPETASTVQDDIVEETAVEAVNISETVAEETAITEPAAEAIATQQTTIAQETIAEPTVETAIDVVAVVKQPAVAHPEGVVFKHFASAPMTKAPAPDYAPESPTKGHWERPTFDFSGKGSAGGHAAATQATAPATKPQSVE
The following text describes a protein:
Function:
Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
Subcellular Localization:
Peroxisome.
Sequence:
MDQTVSENLIQVKKESGGIAVITINRPKSLNSLTRAMMVDLAKAFKDMDSDESVQVVIFTGSGRSFCSGVDLTAAESVFKGDVKDPETDPVVQMERLRKPIIGAINGFAITAGFELALACDILVASRGAKFMDTHARFGIFPSWGLSQKLSRIIGANKAREVSLTSMPLTADVAGKLGFVNHVVEEGEALKKAREIAEAIIKNEQGMVLRIKSVINDGLKLDLGHALTLEKERAHAYYSGMTKEQFRKMQEFIAGRGSKKPSSKL
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
MGAAAVEVEAARPRNGSAGILEKKHRMGADAASQSGPWLASAGAAPRRVNFRPALNKDQGMLLPYQHPSSSSLPRPLNSVMAAKSNNRACPTAASPPIHEPLSWTPAPRIGAGLSNLGNTCFLNSVLQCLTYTPPLAGYLDSGQHKATCRAAGFCAMCALQEHVRQALASSGGAVSPSTLVKNLRCISKSFRMWRQEDAHEYLRCLIEGLHNCCLPPGVKSNSAVSQERSLIHKIFGGRLRSQVKCTVCLTCSNTYDPLLDLSLEIVRADSLTKALNRFTAVEALEGDNKYHCSHCNKKVRALKQFTIDKPPNILTIQFKRFSSTGSSGGKIDKKIEFGRTLDLKPYISNPQATDAKYSLYAVLVHAGWSTHSGHYYCFVRTKGDMWHALDDSRVKQVSEKSVLDQKAYILFYIRDSPTRSSVVTDQRLQSTLPAFKKLLSDGAAEVADDSSADDLDNNSTHRGSNAGNADGSLNRTNGIAQVAPDSGLPAAPNANLPSVKPAGNSQIPSESNTADTTNVAKNIAIDTYGPITTNNSLDVKMKTDNATEKLTKIASIEKKDVLKANVNGLAAVENLVKEIHSNGLEASAPSTGNADVATAVSDKLSSAEEFKNQEDEDIDCSTSGEDEDEDWNEYTKPLNSCTSHSYMRLLYAMPHTRRYFMARALPVQRDRKRSACKKVRGQVENGHCEGMPNGLSSNDKISKRLCCTPGDGGFSKRQKLVDHREESRSSDEMTAVVSTSAKTNGLIYSGASSSHGGKSNGHANKSESDDVTVLRERLQADGSCQAEDLGGSAPATVATGDPGKTGLDVPTKDGSRKSTAALQHSSPDSSKKSKCNGLGVSNPVDGCLKGAVSSPKSSTRLQPNGLYDFEVPRWGEVEANENGSLKDVDRLLRMHKTVVPERDAWDEEYDRGKAKKVRIKATFDVGNGANPFQMMAEAAKNSKQRLHAPIKNYVDE
The following text describes a protein:
Function:
MFS transporter involved in the basal level of azole susceptibility. Confers resistance to voriconazole and, to a lesser extent, to fluconazole.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MATEKGDQNAEKIEQSLPQKIPYWRLVVDQGVLTQQIIDYPYKGSGTEEDPYEVVWMENDPRNPMTWTQLRKWSLTMTVAVSTLAVALVSSAYTGGVREIEAEFHIGSEVATLGVSLFVLGFAIGPLLWAPLSEMFGRQIIFTVTYCALTAFNAGSAGAQNSWTLIILRFFAGAFGASPLTNAGGVIADMFHAKQRGIAMSLFAAAPFLGPVLGPIIGGFLGMNAGWRWVMGFLGAFSGAVWIICTIFVPETYAPVLLRRRAEKLSKHTGKVYVSKIDIDQGRVTLKDAFKTALSRPWILLFKEPIVFLLSLYMAIIYGTLYMLFSAYPIVFQGVRHWNQGVSSLPFLGIMVGMMFAVTYSVWDNKRYVQVQAKHGGFAPPEARLPPTLIASVAIPIGLFWFAWTNYPSIHWIVCILAGAPFGFGMVLVFLGIMNYLIDAYTIFAASVLAANSVLRSIFGAVFPLFTTYMYEDLGIHWASSIPAFLALACVPFPFLFYKYGATIRKRCEYAAKSDAFMRKLAEQMKQAPEPESEETEEPVFDRTEAPAPDVSDVSETESNVEELPDVRQMRSRASTRTASSLRRVVSYEGNPYDIDRVNTRESFTKK