lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MALINWIMDLIHLKLSTIFSLLPSNNGRKICNLVHRTSTIVCLLLICAINLYARQTTYYNHIQNLRKMVDVLIHVFTTLSNINSVVLAFLRSEVWSVLVAKTEIRNRGNVIFYALTFLYLFYGYCEISFYAKINPFIVIFLFPELVNNFLILLSILNINYFANQLKDMLVVFRQGLENEKFKLNFLAKNEANPFIVSRIFGLQSRCDYHLNYFIKICTKIDAFNKIYGWQILIFAATLLVFMYDSLNQVFTEVARSNHMSDIVPIKLFKCFSFIYGILLIRPCFKFNGEMDKIVTILRKILIDLPQTQNTDFCHHLKIKLIFLLKQIEMKKPYFTAGGFFQVNYVMLVHILNGLTSYLLVTQQAS
The following text describes a protein:
Function:
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MRMAVSMEDVKKLREMTGAGMLDCKKALEEAGGDIEKAKEILRVKGLAKAEKKAGRETKEGLIYVIVSEDRKKGAMIELNCETDFVARNEEFRKLAERITRHILEKDENKNKSGEGSEILSQELYDEPGKTVETLIKEAIAKIGENIRLSRYCRYDTEDYLHSYVHGGGRIGVLLDFKAPELNDQVLRLVQDVAMQIAAMRPEYVRIEDIPQEVLERERRILREQALQEGKPEHIVDKIVEGKLKKFYQEKVLLEQPFIKEEKKQVKDVIKESGLNVEIKRFCRFELGGL
The following text describes a protein:
Function:
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Sequence:
MKVYIATPYGFCSGVKKSISLAEKILSLKGEVYTLGALVHNPKVIEELSKKGIKVLGKDEIVEGKALIVRAHGLPQRDIDFYKSLGNEIYDATCPLVKKVQVLAEYLKNNKYKVIIIGEKNHPEVIGILSYTDNQGIVIEYESDIEKVEYYPKIGIVFQTTQSFDNAIQKVNLIMNKGKEIRIFNTICPETIERQEKAKKLSKIVDVALVLGGKNSANTRRLYITLSLKVPTYHIENLEEIDKNWFKEDSKVGIITGTSTPNNFVEEVLALLKSLYPLEIHLV
The following text describes a protein:
Function:
Transcriptional regulator that binds DNA independently of its methylation status. Required during plant organogenesis and development.
Subcellular Localization:
Nucleus.
Domain:
The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Sequence:
MGGEEEVVSVELPAPSSWKKLFYPNKVGSVKKTEVVFVAPTGEEISNRKQLEQYLKSHPGNPAIAEFDWTTSGTPRRSARISEKTKATPSPDKEPPKKRGRTKSPVSKKDAEGEKSEGGGEENSHVKDTEMNPPEGIAENENVTDKNGSGETERVNDAKENIVAEETPNAAPVQEEGESMKEKALDSVDDKSKETDKEKDTGSIEKNSVDVEKKTVEASDEKKNSEAETRNHEENGLTTEAEGKEKTAEGEATG
The following text describes a protein:
Function:
Scaffold protein in the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex.
Sequence:
MAERISYLGYNIPPEVKNMIPVVQKFEQSFYRDILSMVALYMKTKKITLNKKEENDRLEQITDSIHNKLTISANDNKVDPNLSSIVFTGLYYILKIAIKKKVNNQTFLADITDLKLPQPLITDLSNIYNNQGKDLAEKSNNDKILFPKLETFKWRVDVIISSSFTSRVLIPVILMEMADNNGKTRVFEVSVDTFHKLRYNVAKVLKDLEDLEQNQIISKLENKLN
The following text describes a protein:
Function:
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA (By similarity). This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (By similarity).
Miscellaneous:
MISCELLANEOUS: A single active site specifically recognizes both ATP and CTP and is responsible for their addition.
Sequence:
MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDVDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDRAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLVIYYGSFRKVLEAASKWKHPIKIELTKPMRAFSEPLIIPDPVDPRRNVTAAVSLKNIATFSVAAKYYLKNPSMEFFFPSKKVEEKIKGDVLILRLNLDEKSSEDIIWGQIKRSVNKIERALKQSGFRVIDIQAWGDTSNIVIAVQLESKNIGQYYLNIGPQYYSETIDDFIQKNDNIWVGEDGRLYSIKERKEYNAEAIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MQRLQELLLRHRFTAADSSSGGEIWVLGICYKVSADANDEAVSAHAFEEFLNDFSSRIWITYRKGFESLGESKLTSDVGWGCMLRSGQILLAQALVCHYLGRTWRRNACQECLQEYLQILQSFGDSESCSFSIHNLLEAGRPFGLAAGSWLGPYALCRTLEALAKADEDQNAKKGGKRALPFAVYVVSGETEGDRGGAPVRCVEDAAVLCSKWGEATEEWSPLVVLVPLVLGLDKLNPRCLFFYWRSRIFQIEHVIFRLHRCPRVSKLKYLPSLRATFTLPQSLGVAGGKPGASTHLIGVQGDQAMYLDPHENQQVFAVTPENLELDTSFYHCSVVRRLPLDSIDPSLAIGFYCRDRAEFDDLCARSSELVKQYNGAPIFTVAEKSAPSKLQNSSDMGLEESFSKDPSSEDDWQML
The following text describes a protein:
Function:
Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex. As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. Required for optimal Pol-delta activity. Stabilizes the Pol-delta complex and plays a major role in Pol-delta stimulation by PCNA. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. In this context, POLD3, along with PCNA and RFC1-replication factor C complex, is required to recruit POLD1, the catalytic subunit of the polymerase delta complex, to DNA damage sites. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS, as a component of the tetrameric DNA polymerase zeta complex. Along with POLD2, dramatically increases the efficiency and processivity of DNA synthesis of the DNA polymerase zeta complex compared to the minimal zeta complex, consisting of only REV3L and REV7.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Partially colocalizes with PCNA and POLD1 at S phase replication sites. Recruited to DNA damage sites within 2 hours following UV irradiation.
Domain:
The PIP-box mediates the interaction with PCNA.
Sequence:
MEDELYLENIDEFVTDQNRIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVTYLVAGNLIQNGHTCHKVAVVREDKLEAMKSKLATVTSVHVYSIQKALLKDSGPLYNTDYDIIKANLHNCSKFSAIRCADAVPRTPAEVAQARTLARSSSQTPSDTSAVSTPPLNGHGPTAAKQSSQPPKGIMGMFAAKAASKAQDANKEPKAKEAPSVSAASSKPSAKGNIMNNFFGKAAMNKLKVNSVPGQPKEEKEAVKTSVPATEPESSPNTIVEKPGRKTEPAKIQQKDKKSKMKRMDKSDNEEEREPENQKKKRKRIKQLESDSSDEEDVLASPTLEEEKAPSPPPLVPALKAELEPASTEASAGGKKRKRKRVLKSKMFVDEEEGCMVTEKVYESESCTDSEDDFAKTKPPAVPKQPALPVKKEPKEERKNQKKGAATASRANKQISIMGFCQKK
The following text describes a protein:
Function:
Phosphorelay intermediate protein that is part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to oxidative stress and probably to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound histidine kinase SLN1 to two distinct response regulators SSK1 and SKN7.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSEDKLQKLQDSGLVDWAVFSEIVTMDEDEEGFSKSLVEVFVSQVEETFEEIDKYLKEKNLEKLSSSGHFLKGSAAALGLTKISNQCERIQNYGHKINFDNFQLEDIKTKGDSAVSAENVAVNDGETNPENGSNGNETSNNKTNTSNIPDESSDDFWIALIEDALAKARDGFDQSRRALDEYYE
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MRSKIKLSLIANKTSRRTTFRKRKGGITNKLHELTTLCGVKACAVISSPYENPVVWPSTEGVQEAVSMFMERPATEQSKLMMSHETYLQDKITKETKKLESLRRENRESQLRQFMFDCVEGKMSEHQYGARDLQDLSLYIDHYINQLNSSVMLLTNNGASSSSFPPPLHTSVAGAGAGAGAAPLVVAGAGAAPLAVAGAGASPLAVAGVGAAPLAVAGAGPPMAQNQYEPIQPYIPTAFSDNIQYQAPVDFNHQIQHGIYDNLSLDPNHQYPFQDDPFMEMLMEYPYEQVGYAAEHAHIPFMNGNYYNYHQPPTVGLTTTGHMPSNNATTTTTTNTTVV
The following text describes a protein:
Function:
May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Sequence:
MRFSSKFFSPCSTDILENLKTEATMYFHWPFCKNICTFCSFNKYKKVENSFSKIIDERMEKCLIKETETILGFTGIKKINSIYFGGGTPSLAPTTTISRIINCVKQLTNVDEQAEITIECNPSSLSMTKTLEEYFKFGINRVSVGVQSLDDGTLKVLGRDHSANDSVMLLKSALDVFGSDAVSVDLLFRKPGDTIQSWKNELNEILSYKPHHISLYELTPERGTPLFRQLQSGTVVLPNEDDAASMYILALELLKEYGFERYEISNFARAGSCAQSSHNMSYWNGTQYVGIGPGAHSRFFPLGANSRESRVQALDPKSWQDLVERNGHATRLCRQQSQIDVLSELVATSLRTTKGIQPKRWLIFQPEYSLVDVFEQAPSIQMLFLSGNLQWSVDGSLQATEKGLNVVDSILPNILTVLNEFYETNKLKV
The following text describes a protein:
Function:
Neuropeptide ligand for the CCHamide-1 receptor CCHa1-R. Neuromessenger mediating signaling between neuronal cells of the circadian clock network involved in regulation of sleep latency (the time required to fall asleep), amount of sleep and depth of sleep (arousability). Together with PDF, involved in regulating intensity and periodicity of daytime activity. In subsets of clock neurons modulates the rhythmic expression of PDP1 and PDF, and together with PDF modulates the rhythmic expression of circadian protein PER/period, but not TIM/timeless. Mediates signaling from DN1a (anterior dorsal neurons 1) clock neurons to s-LNv (small ventral lateral neurons) clock neurons through CCHa1-R, contributing to regulation of activity rhythms by the circadian clock, particularly in the morning. May be involved in signaling between clock neurons and non-clock neurons, such as the fan-shaped body, involved in sleep homeostasis. In response to a high protein diet mediates hormonal signaling between the gut and a CCHa1-R expressing subset of dopaminergic cells in the protocerebral anterior medial (PAM) cluster of the brain. This suppresses arousability by mechano-sensory stimulation (but not thermal stimulation) but is not involved in regulation of sleep patterns.
Subcellular Localization:
Secreted.
Sequence:
MWYSKCSWTLVVLVALFALVTGSCLEYGHSCWGAHGKRSGGKAVIDAKQHPLPNSYGLDSVVEQLYNNNNNNQNNQDDDNNDDDSNRNTNANSANNIPLAAPAIISRRESEDRRIGGLKWAQLMRQHRYQLRQLQDQQQQGRGRGGQGQYDAAAESWRKLQQALQAQIDADNENYSGYELTK
The following text describes a protein:
Function:
Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.
Sequence:
MQNTLQQISIYGRLLGAVFYYEPNDARLTDILTFFRQPNWMQEWEISFDVKTHKKITALIEKGLQQNITEQYQYLFIGPNELPTPPWGSVYLDPECVIFGNSLLALRDFLQQHQIAFQTQQDEPEDHIGLMLMLAAYLAENRPHLLTKFLREHFLTWAYHFLEQLSKIENSDFYQALALLTIKTLQQWQVDLHINVPTVRFYR
The following text describes a protein:
Function:
Mediates dephosphorylation of MAPK substrates such as SLT2, acquiring enhanced catalytic activity under oxidative conditions.
Sequence:
MNIYTSPTRTPNIAPKSGQRPSLPMLATDERSTDKESPNEDREFVPCSSLDVRRIYPKGPLLVLPEKIYLYSEPTVKELLPFDVVINVAEEANDLRMQVPAVEYHHYRWEHDSQIALDLPSLTSIIHAATTKREKILIHCQCGLSRSATLIIAYIMKYHNLSLRHSYDLLKSRADKINPSIGLIFQLMEWEVALNAKTNVQANSYRKVP
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity). Plays an important role by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone. Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (By similarity). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (By similarity). Displays no reductase activity towards retinoids (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Apical cell membrane.
Sequence:
MASCVLLHTGQKMPLIGLGTWKSNPGQVKAAIKYALSVGYRHIDCAAVYGNEIEIGEALKENVGPGKAVPREELFVTSKLWNTKHHPEDVEAALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNDDGTIRYDSTHYKETWKALEALVAKGLVKALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVVCIPKSITPSRILQNIQVFDFTFSPEEMKQLDALNKHWRYIVPMITVDGKSVPRDAGHPLYPFNDPY
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MTSKDDSVRAKATHKFREELEQLTVNQEESEFLIEFFLHKLSDPQSLLDTTYILLKLSKSSKSIHPSFIKMIQNKQIIIPTFSREARINFYQIFLAFPITFELAAIILQSIIGEKDPRNILVAFQLCDAILEVKNIGTQYKREIFEFLDCYYPIEFNEKADPRFQIKKVEIEHILNKCLFSEVLLNDSILLLQDKIVSAYDRAQGSALKSVMWIIKNQNKITALQIEEIYESIQKLAEQVIMDDDVIEQIPITLIEICNNERFQKVKTKIKTISLKTLEEIPATQQGFIYFNFLKLLVQNHGETIFRDIVQIFNKKFDTKNINVTQKRLENVISAIAEYKKYNREFVSELDNNQKSLLYDKLQQGITHKMQNVFILTLKCLADIMKYYQDYQKDLELYLYNQINNRELIEQQCILDYFAKNGIVDIKQYQQLLAFWSENNQLLYDYSLTCSLYNIQDYFSQFTLGLINNQNYQIKSEQISALKGYLDNNSISNSIRQDQAQLVINHIYNPLNKNRKNKLIKQLIQFILKQFALNQNIIKQITLDYVLHLEDDQIYYYIPLMEQELNENLIQSILEIIYKQDFKQRDVQITNRKYAYKFIYTCLSKYQKELNLDFPQLSTMETQFNDHQLNQLQLYIVLLRQQMLFNNEIALEKLKEISQSHPQLLSQIIKHKDLENKPSLQKSIGEMIKQLNHKQTLNYLINQVDEEFITGLANPELLQLIIEHFNDTKIDKLKSLALIVNWCPILKKQTISRFCTLQLIL
The following text describes a protein:
Function:
May be involved in proliferation and apoptosis in myeloid precursor cells.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVKQTKAKTFQAYLDSCHRRYSCVHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERLLLTGLHAVADIYCENCHTTLGWKYEQAFELSQKYKEGKFIIELSHMIKDNGWD
The following text describes a protein:
Function:
Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex.
Subcellular Localization:
Chromosome, centromere, kinetochore.
Sequence:
MDNFEENSHALCLVLNNIISQEVIDDNFKEAFFETIPEDEDGSTKMFNISFVSPGVKHPLQNIITKTEYGFFLVSKAILEVSHDEDGEETYQFTHSKLSRKTIEHVLVGTPISMEVYYINGREPLHRVSTGSDESTSTFDVQLTNLASVNPVQKDEARYLISLFDYALANNHEISEEVKNIPLCVMVSGENSANEMSLAHLASIPKHSTINHVIVSSRGPFIDPNALPNINFFKKWHAGSTSGPIQTCGYAIFELLGLSHASSEPQGDTLSSVLIEFAWENVSDVLQMPPLSCNSVLHVQNIPGSMELCALKLNMEVEQLKILSEMLNEQEKEWPFDSEDLESAFDRTAKLLEKQNSVDTETPASEKEMDDTNDCLPFDQDTFAARKELDFTESLWMVLKDAADFEDVAASIQSAFFATLSGKQQPILYGSNTSSIAELMRAVLTCDTNEEKHKLRMRMEEIISDKSEILRCLVEIGVEKLLRDLTTYFLSEELVTQEQLSYYTDTSPDLVSRVSMVGKMHNILDLILTTKSVIDVGHSNLQLLTQSSLTYYKHHTVGDHPVFSLSLPAFGMSSSSAIKQIIASQKPSTWCVSLKSKTKKGEIVSVVHISTTMLTGKAENSVLDISALNEDGDCTINGLPRSKLPYYLTFAKQTLLPLIPCKLNIK
The following text describes a protein:
Function:
Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Inhibits root growth.
Subcellular Localization:
Cell membrane. Secreted, extracellular space, apoplast. Note=The precursor of SCOOP6, PROSCOOP6, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP6 in the apoplasm.
Sequence:
MGTKCYSKLRYVVVLVLLLFVFPCSLSQSAPSSVTGRRLMGIYMPNGGIIAGSSPSGQAPNINNNYHGRRLMISEARPSKSKKGGGREPESPG
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:
MDDEKRPRVGDTAESPRKSPRLVHRIPTTTDQAESGVGLKSLLGLIKNNPSKELDDPNAASLGVIDVEKKAARPGDTAATALDVNDWWEKVVALQWMASVGGDCRARRCRHVLYGEDDINLAIALIKTCDDTPMCNADNCGNTEGREISACLDCESRFCTTHGKWHASVNKHWVALVYKKPHVAYCFACEECYFIRTEHFGVVMDNEDDYFISLREEDEKGMRVDNVAGDHASGSVIGHACPIKGIPNLGNTCYLNSLLQCLLVLGRLRAGILGLDAPLGLLGSSLRSLFDDADSVNNAGGLLDPEKLLACVRMLNPEFKGNGMHDSQEALCILRTGLDKEERAMKLSNMQAGAPSAVAPTVIDSIFGGQLSVTSSCKHCSVRSLSHDVFHDLSVPLPQESPAKSDELSPWTKGRRSPRKIRINLLSAIDKHKSDNEKTQSPASELEDVFLVKRSKPLKVDSTKVEQISHSMDAGGPLQTRKDKVQGKVVDVLPRIPEDPASPSFVSPLSEEKNDSAVQPEVSTEAKMTASSAKVTTKDKGKTQISDVVYDKAHDINSLASIEKCLELYLETEIEWTCENCSKVLKKPGIMSSTKEDTTAGDQSEQLEKSAHQVEENQNEQKDKNECPIQTRLIRKLPPVLTIHLMRYLEDLTKVIGHVSFKEILDVGQFMDPSSEDRDNSRYRLVGFVEHLGPSMYAGHYVAYVRPSPPQQTNGSSSWFRASDTDITEVSLEEVLKREAYLLFYERIEG
The following text describes a protein:
Function:
Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity.
Subcellular Localization:
Nucleus.
Sequence:
MYYRKEYTKVQGLVYLNQNLCITITMKCIIPGRHTKVFGKAVHSLSRIGNELWFDPVEKGLALRVVNSSRSAYACIFFSPLFFHKYHRTAFLEQAAGCTQLNFKCKFSVKSVLPVFRSLSTLEKNVDKCTIYANINDGYMNFQLFYKNGLTKTYQLAYEDCEPLQAVFANNTCPNVLRIQPRVLSDVVVHFPTCQEEITLCVTPLRVSFKTYCEEAFEFSKSVHTEMHLSPEEFHYFQIGVDSEVTFCLKELRGFLAFADTTSSYISLYFSKPGKPVAFSMDNMFFEANLILATLAETEMRNSSQISKSNIAGSKLCSPPPATELSNATSVAENLASQHIISLPQAENQSPMISNSTLLTACGNAKEDHPDMVEETPTHSSYSKFCTLFFGAVSSETHENADGTFCSLATASEDEDEDFCSRKLSQTF
The following text describes a protein:
Function:
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Subcellular Localization:
Cytoplasm.
Domain:
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Sequence:
MDLKKTLLMPKTSFAMQANLSTSEKNFHDFWKDKKVFQKLKKQNKGKQIKILHDGPPYANGSIHVGHALNKILKDFILRSWLYEGYDVVFIPGWDCHGLPIEHAVSKKNPSSYSNLSTVEKRKLCHQFALSQIAVQKEQFQRLGLLNDFQNCYYTIDESFQFKELELFLQAIKKGLIFQDLKPTYWSPISRTSLAEAEIEYKEVNSIALYLTFKVSKSDFLDENANLLVWTTTPWTLPTNQAIAIHPDFDYLLFEYNQQKFVILEKLFEVFTNKLNWTNAIKLKKFKGSNLKNSSYSHCFYNKVLPVLMGIHVVDNEGTGIVHSSPAFGIDDFYLCQKNKIKEVLISIDEKGVFNNLLNDKELENCFYLKANDLIINRLKQNNSFIFSEVISHREPHDWRSKTPVIYRASKQLFIKTKSIKKQLKKQINQVNFLNSKNQLRLKEMLLQRDEWCISRQRVWGLPIPIVYANNKPLLDFSTIQYTIKQLKKHGIDSWFEKDVTCFLKPDKTKKWVKYHKEIDTLDVWFDSGSSYNVLEINKYGSIADLYIEGSDQYRGWFNSSSNCGIIQNDLIPFKSLVSHGFTLDENGNKMSKSLGNIVDPLKICDQYGADILRLWVANTDWQIDNKIGVNILKQVAEQYRRIRNSLLRFILGNINGFNFTSMDDYKFSLEDKIVIHKTNSLVEQIEKFLEKYNFLGCLKVINKFVLWLSSWYFEIIKDTLYCDAKNNPNRLAKQAVLNYIFTQLISFLNIFIPHTAEDAWKNYSFNKKPISVNLFTKPTVFKVANSKNLENIYKTFTSIKNAAFKEIEKLRKEGLISKNNQIELTVGINKKIPKKLKDNLALWLNVNSVNLTNNENEIKVKKTKKTMCERCWNFQTIIKQKLDHNLCSRCFKVC
The following text describes a protein:
Function:
Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus; tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm.
Sequence:
MDKQALLGLNPNADSDFRLRALAYFEQLKISPDAWQVCAEALAQRTYSDDHVKFFCFQVLEHQVKYKYSELTTVQQQLIRETLISWLQAQMLNPQLEKTFIPNKAAQVLALLFVAEYLTKWPKGVDLYLRILMAINSELVDRDVVHTSEEAHRNTLIKDTMREQCIPNLVESWYQISQNFQYTNSEVMCQCLEVVGAYVSWIDLSLLANDRFINMLLGHMSIEVLREEACDSLFEVVNKGMDPVDKMKLVESLCQVLQFSKPVNGMGQSWIVSWSKLIKNGNIKNAQEALQAIETKVALMLQLLIHEDDDISSNIGFCYDYLHILKQLTVLSDQQKANVEAIMLAIMKKLTYDEEYNFENEGQDKAMFVEYRKQLKLVLDRLAQVSPELLLASVRRVFSSTLQNWQTTRFMEVEVAIRLLYMLAEALPGMMRTLVTSGVSSYEHTSVTLEFFETVVRYEKFFTVEPQHVPCVLMAFLDHRGLCHSSAKVQSKMAYLFSRFLKSLNKQMNPFIEDILNRIQDLLKLSPPENGHQSFLSIGVMIVNSEYAAERKEALMRNLLTPLMEKFKILLENLMLAPDEERQASLADCLNHAVGFASRTSKAFSNKQTVKQCGCSEVYLDCLQTFLLALSCPLQKGILRSGVCTFLHRMIICLQEEVFPFIPSASEHILKDREAKDLQEFIPLINQITAKFKVQVSPFLQQMFMPLLHAIFEVLLWPAEENDQSAALETDFFRGPGVGSISLQLVVPKSAQLWLKWGLLWASKGRKCTLIGPWAAMGGLGKAPLFPILVCGTGSQAPSLQALPSTQEPVCLPLLSMAPRLSCQGTPAGQCQASLGPSLASLPFSLVPQIQRGPRQQGTVMSTLPQVYAHTAGL