lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in output regulators CikA and SasA. KaiB switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from KaiC, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation; Component of the oscillator and circadian clock in this organism, enhances fitness in a rhythmic environment. The homotetramer reduces the ATPase activity of KaiC3 by 35%; A metamorphic protein which reversibly switches between an inactive tetrameric fold and a rare, thioredoxin-like monomeric fold (KaiB(fs)). KaiB(fs) binds phospho-KaiC, KaiA and CikA. KaiA and CikA compete for binding to KaiB(fs), and KaiB(fs) and SasA compete for binding to KaiC, thus the clock oscillator and output signal pathway are tightly coupled.
Domain:
Has 2 forms, fold switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC.
Sequence:
MSPFKKTYVLKLYVAGNTPNSVRALKMLKNILEQEFQGVYALKVIDVLKNPQLAEEDKILATPTLAKILPPPVRKIIGDLSDREKVLIGLDLLYDEIREREAEDQ
The following text describes a protein:
Function:
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Nucleus matrix. Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton.
Sequence:
MFQPCCSKSTMSRSGVAVNDSALQAFNELKLGKKVTFIIYKINDAKTEIVVEEEGTTDSYDTFLGKLPENDCRYAVYDFEYEISSGEGKRSKLVFFTWSPDTAPVRSKMIYASSKDSLRRALTGISTEIQGTDFSEVAYESVLERVSRGAGSH
The following text describes a protein:
Function:
Endolysin that degrades host peptidoglycans and participates with the holin protein(s) in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin(s) has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Subcellular Localization:
Host cytoplasm. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane.
Sequence:
MSKLVWLDAGHGGKDSGAAANGIKEKDIVLKIVKKVKSILTSRYEVAVKLTRDSDVFYELIDRARKANAAKADLFVSVHINATPGGKGFETYRYVKTSASSSTGQQQKVLHDAIYKRIKKYGIKDRGEKAADLSVLRNTSMPAVLTENLFIDNKDEAALLKKDSFLNDVAEGHAEGIAEILNLKKKSGGSAPKKEDKPSSGKTKMVIVKDNPDGFLWVYNKADWNARYKKVKPDEAFTIDKTVTVNGSKMYKLKSGLYITAASKYVTVKEK
The following text describes a protein:
Function:
K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties. In pancreatic islets, conducts K(+) countercurrents for Ca(2+) release from the endoplasmic reticulum (ER) and regulates the frequency and duration of cytosolic Ca(2+) oscillations coupled to secretion of pancreatic hormones. In pancreatic beta cells, drives ER Ca(2+) efflux, which in turn activates Ca(2+)-dependent plasma membrane K(+) slow currents and cytosolic Ca(2+) influx, overall contributing to synchronous cytosolic Ca(2+) oscillations. Limits glucose-induced cytosolic Ca(2+) oscillations coupled to second-phase INS secretion. Contributes to beta cell adaptation to acute inflammation by maintaining normal cytosolic Ca(2+) levels and INS secretion (By similarity). May regulate beta cell mitochondrial Ca(2+) levels either indirectly via ER Ca(2+) efflux or directly by hyperpolarizing the mitochondrial membrane potential. Limits mitochondrial Ca(2+) oscillations and ATP production involved in glucose homeostasis upon metabolic stress (By similarity). In pancreatic delta cells, limits Ca(2+)-induced Ca(2+)-release involved in somatostatin secretion and modulates islet paracrine signaling involved in glucagon secretion. Permeable to other monovalent cations such as Rb(+) and Cs(+) (By similarity).
Subcellular Localization:
[Isoform a]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein; [Isoform b]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The pore-forming domains 1 and 2 assemble to form a single pore in which M2 and M4 transmembrane helices line the central cavity and M1 and M3 face the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 carrying a signature sequence TxTTxGYGD that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation.
Sequence:
MPSAGLCSCWGGRVLPLLLAYVCYLLLGATIFQLLERQAEAQSRDQFQLEKLRFLENYTCLDQWAMEQFVQVIMEAWVKGVNPKGNSTNPSNWDFGSSFFFAGTVVTTIGYGNLAPSTEAGQVFCVFYALLGIPLNVIFLNHLGTGLRAHLAAIERWEDRPRRSQVLQVLGLALFLTLGTLVILIFPPMVFSHVEGWSFSEGFYFAFITLSTIGFGDYVVGTDPSKHYISVYRSLAAIWILLGLAWLALILPLGPLLLHRCCQLWLLSLRQGCGAKAAPGRRPRRGSTAARGVQVTPQDFPISKKGLGS
The following text describes a protein:
Function:
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing.
Sequence:
PDPDVRRLEPAGRHARHPILASRDFFIVVPPAEKDDDEDLFKVPQCSCQALQLQEGYINSSRNAGWGAFNSCRWQVNGSGQFCGVAEMIGPVDFDRSVDYWQQDKWSGQFPVKWHIIKDVPNNLLRHIILENNDNKPVTNSRDTQEVQLGWHDAGTYDKNIIEWPKCSGANGSLRFKVELKHGANADLVNAMKLIPPSTTSEPHPRSMSAAPSSPFHLSAPIRA
The following text describes a protein:
Function:
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA); CasE is required to process the pre-crRNA into single repeat-spacer units, with an 8-nt 5'-repeat DNA tag that may help other proteins recognize the crRNA. This subunit alone will cleave pre-crRNA, as will CasCDE or CasCE; cleavage does not require divalent metals or ATP. CasCDE alone is also able to form R-loops. Partially inhibits the cleavage of Holliday junctions by YgbT (Cas1). Yields a 5'-hydroxy group and a 2',3'-cyclic phosphate terminus; A component of Cascade, which participates in CRISPR interference, the third stage of CRISPR immunity. Cascade binds both crRNA and in a sequence-specific manner negatively supercoiled dsDNA target. This leads to the formation of an R-loop in which the crRNA binds the target DNA, displacing the noncomplementary strand. Cas3 is recruited to Cascade, nicks target DNA and then unwinds and cleaves the target, leading to DNA degradation and invader neutralization.
Sequence:
MYLSKVIIARAWSRDLYQLHQGLWHLFPNRPDAARDFLFHVEKRNTPEGCHVLLQSAQMPVSTAVATVIKTKQVEFQLQVGVPLYFRLRANPIKTILDNQKRLDSKGNIKRCRVPLIKEAEQIAWLQRKLGNAARVEDVHPISERPQYFSGDGKSGKIQTVCFEGVLTINDAPALIDLVQQGIGPAKSMGCGLLSLAPL
The following text describes a protein:
Function:
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MAPNLLLESYNRIVYARVLEKLTTEGGIKKGLKEKLADFNQSIWYIERTKEKMTISVSTPCWKQLKENRSLEFLQKVYGSDLVEADSNSEYNLILTIPEKHDKPEEFAMNAAKLLTNMLIGPAVVLADEVKNNKADEKLVQIDYRPGESYWLKPNGDRLTVIFSIKFDDKDDAVFGRVFINEFSKSAAGCPSCDVVTRKNAPPPSELKTVEGLAEDNCYISFLLEKRHLNNPQKTLEVLMSCRNYINFHIKCSKAFLHIRMRNKVSHLQLVLNRAKPEREVEKKTASGRTFKK
The following text describes a protein:
Function:
High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores. The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores. In astrocytes, the calcium released into the cytosol allows the Ca(2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation. May play a role in platelets activation and in vascular development. Mediates up-regulation of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, triggered by coagulation factor Xa (F10) in cardiac fibroblasts and umbilical vein endothelial cells.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
ASKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKPLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYLSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSTVANRSKKSRALFLSAAVFCIFIICFGPTNILLIAHYSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIYKKLLT
The following text describes a protein:
Function:
Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cartilage and bone formation or neurogenesis. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathway such as MAPK p38 signaling cascade to promote chondrogenic differentiation (By similarity). Promotes the expression of HAMP, this is repressed by its interaction with ERFE.
Subcellular Localization:
Secreted.
Sequence:
MHWTVFLLRGIVGFLWSGWVQVGYAKGGLGDNHVHSSFIYRRLRNHERREIQREILSILGLPHRPRPFSPGKQASSAPLFMLDLYNAMASEDNPEEYLVRVSLAGEAKETRKGYPASPNGYAHRLHLPPRTPLTTQSPPLASLHDTNFLNDADMVMSFVNLVERDKDFSHQRRHYKEFRFDLTQIPHGEAVTAAEFRIYKDKGNHRFENETIKISIYQIIKEYTNRDADLFLLDTRKTQALDVGWLVFDITVTSNHWVINPQNNLGLQLCAETGDGRSINVKSAGLVGRHGPQSKQPFMVAFFKASEVLLRSVRAASKRKNQNRNKSNSHQDPSRMPSAGDYNTSEQKQACKKHELYVSFRDLGWQDWIIAPEGYAAFYCDGECSFPLNAHMNATNHAIVQTLVHLMFPDHVPKPCCAPTKLNAISVLYFDDSSNVILKKYRNMVVRSCGCH
The following text describes a protein:
Function:
Ammonium transporter that mediates the import of ammonium in prespore cells. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development. May function as an ammonia sensor that relays information concerning ammonia concentrations to the signaling pathway involved in the slug versus culmination choice and regulates prestalk gene expression.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein.
Sequence:
MEQFSTSSSESSDSSSEYSLEFYMDTSWVLDAANLVFFMQAGFGMLEAGMVRAKNTKSILLKNLINTAICAISYYCVGHSFAYGKVNPNSFVGFGNFFLMDYTHYAYWMIQWAYAATATTIATGAMAERLQLHCYILFTLVQTILIYPFVAHWIWSQNGWLFDLGIVDFAGGAVIHIVAGITGACGSFLLGPRIGRFNQESGKPKNLPGHSVVLMSLGAMILWYSWYGYTAGASLGMTRSRVLPASRVSVVVTLSGATGLITVLGIGKIFNGHYDLVKGINGLIAGLVSSTSSCAYIEPWAAIIIGFIGGIVYWFSSWALLNWLRLDDPVDSTAIHLFGGCWSLISVAFFATHGRVRNPDIILPGGIFYGGGISLLWVQLVGMVLAILWAGFLSGIFFFTMDYFGKLRVDVDTELAGLDNSNHGGSAYIFD
The following text describes a protein:
Function:
Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system.
Sequence:
MGMNENQNKGISVENLTLSYEKNLVLNNINFSIKKGSVVTLVGPNGCGKTTLLKIINGFLRQNEGTVYIDSRNIEGIANRELSRILGHVSQMHKSSFPFSVLDVVLTGRMPYISMFSTPGKEDIEKAYQVLEFMGIAHFARRQYTRISGGERQMVMIAKALAQEPDFLLLDEPTSFLDLKNQIHVLKTIINLAKTRNITVLMTLHEPNHALLFSDEIILLRKLHGPENENISSRHDPNTGASPEKENILTYPVENIVSSGAPEKVMTPEKIKEAYGIDVEILEHKGKRMIIPEI
The following text describes a protein:
Function:
May be required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase (By similarity).
Subcellular Localization:
Periplasm.
Sequence:
MKKTWLFLTALLFSSVAFSAIDALNFSSPQQESDYHQLTQSLRCPQCQNNNIADSNATIAVDMRGKVFELLQEGKSKNDVVDYMVARYGNFVTYDPPITASTLVLWIAPLLLVLLGVVFLLRRKPKTQSAVKSQEILTDEDNARLAELLNKDKXMNFTLIFILTTLVVALICFYPLLCQFKAKHGQKRDDLNKALYFSRLEEIEQDNSQGLVENVEQLKQELQKTLLDDVPSKVQENVDYSGKSYGKIWFISGVLALGIIAGPSYFMVGSWQAESMLEQTYAKLPYFFDRMKNEDKNPFSDTEMQQFSTALRIDLQKNPTDAKKWWMLGQIGMNLGDARLAFDSYQKANKLEPDNVQYKLGYARILMFSEDATDKLKGGNLLREVIRQEHTNIEALSLLAFRYFETEDYKMAAVTWAMMLRLMPKDDERVPLIEKSIRTARDALEAQNEEKSKSITPEK
The following text describes a protein:
Function:
Involved in the biosynthesis of the siderophore pyochelin. Adenylates L-cysteine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety (By similarity). Then forms a peptide bond between the salicyl-thiazolinyl intermediate bound to the second carrier domain of PchE and the cysteine bound to its own peptidyl carrier domain to form the salicyl-thiazolinyl-cysteinyl-S-PCP2 intermediate. It subsequently cyclizes the C-terminal cysteine to form the second thiazoline heterocycle in the salicyl-thiazolinyl-thiazolinyl-S-PCP2 intermediate (By similarity). When this intermediate is released by the action of a thioesterase, it produces the tricyclic acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid (HPTT-COOH), an advanced intermediate containing the aryl-4,2-bis-heterocyclic skeleton of the bithiazoline class of siderophores (By similarity).
Domain:
Modular protein that contains a condensation/cyclization domain involved in the cyclization of the cysteine, an adenylation domain which activates the cysteine residue into an aminoacyl-AMP ester, a peptidyl carrier protein (PCP2) domain which bears a phosphopantetheinyl arm to attach the activated cysteine and a thioesterase domain (TE) that may release the newly synthesized peptide from the enzyme.
Sequence:
MSLGELLETCRSRRIELWSEAGRLRYRAPQGALDAGLAERLRAEREALLEHLEGGPGWRAEPDMAHQRFPLTPVQAAYVLGRQAAFDYGGNACQLYAEYDWPADTDPARLEAAWNAMVERHPMLRAVIEDNAWQRVLPEVPWQRLTVHACAGLDEAAFQAHLERVRERLDHACAALDQWPVLRPELSIGRDACVLHCSVDFTLVDYASLQLLLGEWRRRYLDPQWTAEPLEATFRDYVGVEQRRRQSPAWQRDRDWWLARLDALPGRPDLPLRVQPDTRSTRFRHFHARLDEAAWQALGARAGEHGLSAAGVALAAFAETIGRWSQAPAFCLNLTVLNRPPLHPQLAQVLGDFTALSLLAVDSRHGDSFVERARRIGEQMFDDLDHPTFSGVDLLRELARRRGRGADLMPVVFTSGIGSVQRLLGDGEAPRAPRYMISQTPQVWLDCQVTDQFGGLEIGWDVRLGLFPEGQAEAMFDDFVGLLRRLAQSPRAWTDGDATEPVEAPPQALPGSARSIAAGFAERALLTPDATAIHDAAGSYSYRQVAQHASALRRVLEAHGAGRGRRVAVMLPKSAAQLVAVIGILQAGAAYVPVDIRQPPLRRQAILASAEVVALVCLESDVPDVGCACVAIDRLAADSAWPPPPAAEVAADDLAYVIYTSGSTGTPKGVMLSHAAVSNTLLDINQRYGVDANDRVLGLAELSFDLSVYDFFGATAAGAQVVLPDPARGSDPSHWAELLERHAITLWNSVPAQGQMLIDYLESEPQRHLPGPRCVLWSGDWIPVSLPTRWWRRWPDSALFSLGGATEAAIWSIEQPIRPQHTELASIPYGRALRGQSVEVLDARGRRCPPGVRGEIHIGGVGLALGYAGDPQRTAERFVRHPDGRRLYRTGDLGRYLADGSIEFLGREDDQVKIRGHRIELAELDAALCAHPQVNLAATVVLGETHERSLASFVTLHAPVEAGEDPRTALDAVRQRAAQALRRDWGSEEGIAAAVAALDRACLASLAAWLAGSGLFASATPLDLATLCQRLGIAEARQRLLRHWLRQLEEGGYLRAEGEGWLGCAERPAQSPEDAWTAFAGCAPAALWPAELVAYLRDSAQSLGEQLAGRISPAALMFPQGSARIAEAMYSQGLHAQALHEAMAEAIAAIVERQPQRRWRLLELGAGTAAASRTVIARLAPLVQRGAEVDYLFTDVSSYFLAAARERFADQPWVRFGRFDMNGDLLDQGVAPHSVDILLSSGALNNALDTPALLAGLRELLSADAWLVIQELTREHNEISVSQSLMMENPRDLRDERRQLFVHTGQWLEWLAAQGGDLACGVVPPGSALDLLGYDVLLARCKTDRARLEPAELLAFVEARVPRYMLPAQLRVLERLPVTGNGKIDRKALTGFARQPQADLRHGVAQAPADELENALLALWREVLDNPSLGVEQDFFGAGGDSLLIAQLIARLRERLESARRHPFDRLLRWALSQPTPRGLAERLRSAPEEGRGPALAAARGVAPAPAGMSRAPLAEGAVALDPLVRLVPGEGVPRVLVHEGLGTLLPYRPLLRALGEGRPLLGLAVHDSDAYLAIPAEHLNACLGRRYAEALHRAGLREVDLLGYCSGGLVALETAKSLVQRGVRVRQLDIVSSYRIPYRVDDERLLLFSFAATLGLDTAALGFPAPERLGQAVQAALAQTPERLVAEALAGLPGLADLVALRGRVLQAASGSADAVSVERDTLYRLFCHSVRASQAEAPEPYVGALRLFVPDAGNPLVPRYAEALETQWRAAALGACGIHEVPGGHFDCLGEALAQSLSKPMPEEASR
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDVEQLTSSKLGTKQYWDEFYNLEKNNYAENPNDSGECWFSDSGAEEKMVDFLVDEEEQGQGESLISLDCKMCDLGTGNGRLLFSIREGGFTGHLTGLDYSQPAVEFSTKIAEQEEMENITFEHADFLGDAAMWSTGNRQWDVVLDKGTLDAIALSDIKYEGKTGVQTYPHVVQHMVKTRGVVLITSCNFTSDELVKIMTTDTCLKEWKHVKYPSFRFGGTDGSTVCTIAFKKE
The following text describes a protein:
Function:
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
Subcellular Localization:
Cell projection, cilium.
Sequence:
MAIRGHKGLQQLLSMATSVNSFLGPMKSYKFIFDQITHESILTSSSFRLLENLDLTSAIGQLLNETIQAHHKSYKTGTTTLFFMVGAWSSAVQECLHLGIPVSLIVSVMLDGLNSCIGHVHSLQVSLVSQVTSDCTNIKTNGINHSNYSASGDQGNCSSELENNPLPRVSNMRTASEFPVAFHKKPLPLCTGTNLYKTQRRRLFHSRHLAEDLSFFQDVPERPQTTTLNNETLDGLAKGLAHGYQPVMNLVKNAVCLHCAEIKENSLDKSSFNISRLETCSLPGLSEEHTTVSFGYTTLVPTESAAVITHLNGKPLRILLVDGELTESHRHLGFDNPDNVKMVFEHAGNEKHNLEDSWISRAYEKIIQANINLILVRGDVCPFLLKQCIHRNILIVTQVKQNILQAFSECTGAEPVTYLTQINCCSVGNEAFVTLCTRANSIIEVSQKIVISITAKKLNLITATLSSRIPSTMQSIEDQFLTCAYRLHHALQEGNVFYGGGAIELLCIHHLQKLVQESSSSFYAYDNAQFHCLSSWMTESATFYRAAIIGCLAKGWYKYISVLLCNMGGFLSELDAVTFIENELQNISHHSSPIDYVRDQYSKKDLFNDEMGISISHHSLPVYDNVTPKLEAWRRALHLVLTVLQTDAEVITNSATQNQILMSETSNGEYLFL
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MPSSNTDVDGLTGEETTINKFSTLRPSYRPEEIHLVVETVDRYNPQNMAILEEYISSQLKTNNYDRTACLALLKLYQLNHADANVYVIASVLALALSALPESDFTLCMYLLREEWLADPLIAHLVHMHELLGQAQFSEFWAYLESEESVREFTGDYSLFDDNIREFIAQTLSITYQTISIESLEKMLDLSDEDLADWVKMRESWSVNADDDSLIDLPITSWNQAKEIVMQEDVKFEQLGKILNRSRLVV
The following text describes a protein:
Function:
May regulate the transcription of the frlABCDR operon, involved in the utilization of fructoselysine and psicoselysine.
Sequence:
MSATDRYSHQLLYATVRQRLLDDIAQGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQSQKVENALLTVSGFTDFGVSQGKATKEKVIEQERVSAAPFCEKLNIPGNSEVFHLCRVMYLDKEPLFIDSSWIPLSRYPDFDEIYVEGSSTYQLFQERFDTRVVSDKKTIDIFAATRPQAKWLKCELGEPLFRISKIAFDQNDKPVHVSELFCRANRITLTIDNKRH
The following text describes a protein:
Function:
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Sequence:
MTEKKIKKVVIKEEENELEMVAAGMGPAKGAVKREGDENKAALLANEEGGGNDGETEWWTQGTLTTTKKGEKRWDTLLHNGVLFPPAYVPHGIPILYNQQKFEMTPEEEEVATMFAVLREHDYYRNEVFRRNFFQSWREILDKRKHPIRCLELCDFSAIYEWHQREVEKRKSRTREEKKELKRIADEEAEPYKWCIWNGKKEQVANFRVEPPGLFRGRGEHPMRGKLKKRILPEDVVLNIGKEAPIPQAPAGHKWKGVVHDQNVTWLAMWYEPTIGQCKYVMLAPSSTLKGQSDYAKFETARELKNHIDDIRESYTKDFSSTDEMERQRAVATYFIDKLALRVGHEKGEEEADTVGCCSLRKEHIELRPDNVVRFDFLGKDSIRYVNEVTVLPEVYKLLGSFIKRTDSEIFRKVTPTTLNNYLKSFLKDLSAKVFRTYNASITLDEWFREKPVDPKASLSDKLVYFNKANTEVAKLCNHQRSIPKTFHVSVQSIKYKLEDIKRTIDTLRRAQSVSENGSVEEAATQFFKEQDEVQYQWLNTYGTPEEIQAYEEFVKKRVIPTALTGSASSTKNKSGKKTANGKSKKSGGAKRSTKKASGTKKKKTRSKKSAAKTGKKASGKKKKQKKRGGSKRGSRGKNGAGAASGDENDEDAPLVNIIAK
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MASDNESITQLKPPMRFMLPHEIFHVTKPAHQWYEHRDNHDYDDDYYDDDDDEDYDGDGDEDDSVCSLLEDEIDQHEFDSPESDDYTLSLDGSNPTLHQDHDQDDDYDEDYLTEPLSSPPRSASFFDCNMCMKMAREPVVTSCGHLYCWPCLYSLLSQRECLVCKSKVFDSLITPIYNSKPQLRLQCATKSKGAFSSTLKISINLAQIVFWLFIMQSFM
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.
Miscellaneous:
MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MQPIIKGAVSSTFKRALYNFGIKEKKSVNIEMGRTQQTKKIDQSLSKKLPKGTIYDPFDFSMGRIHLDRKYQANKNSNRNDIMKSGANPLEFYARPRILSRYVTSTGRIQHRDITGLSAKNQRRLSKAIRRCQAIGLM