lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MILWRIVRPGAAMAYVQTGLVLIAEAMDTQQDSLKPRPAMRAAAFSVHVFTAFGAAIALLAMLEAVREHWAAMFQWLGVALIIDAIDGPIARRLDVKNVQPNWSGDVLDLVVDFVTYVFVPAYAIVASGLLLPVAAPLLGVAIIVTSALYFADLRMKADDNHFRGFPALWNAAAFYLFLLHWPPLWSTLLVAALVVLTFVPFHVLHPVRVVRLRWLTMSLIGIWAVLSLYTLDMDFRVGPGVTLALCAIALWISFSDALIRFARSFA
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MSAVNDPLELLTNKGTHEPSFLSPIWNPIACGVAGVGAAIFINWGFRKPVFSGIQKHIAFGAIGVGAGAYFDQKRNEYLAKRDAVLRHYIELHPDDFPVKERKTYGQVLESWVPVR
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MRLHSSNMAPIGEKSAKASSAEKENDDDEPQNLWTSILSEVSSHSSSKLPSCKSILVLGEDETGKTTLLSRLQGVEDPKKGYGLEYLYLDVRDEDRDDTTRCGVWILAGENEHEDLLRYALTADNLEHMLVIIAVDMCRPWNIMDSLQKWTQVIRRHVDSLRIPPEKLRELEQRLVQQFQAYTEPETGQDSSVTRRTSGVTKPTGAEDEEAVVLPLGETTLTHNLGVPIVVVVTKSDYVNTLEKEQDYSDEHLDFLQQNVRKFCLNYGAALFYVSVKENKNCDLLNRYLLHRLYDFPFNSAALVVEKDALFVPSGWDNLQKVSILYENMANIDPEKPYDEVIIKPVVRRLLQDNKEIIAEDEQVFLMKQQATIRNAAQGKPGQEASPRAADPRAMRTPEKRNPTNAPAASPITTQGKPKQIDPGKPGSANEGVLANFFNSLLSKKSVNSPAPGSPRTGNGGEKAVRNDAAAELDRMTRGRKPVAGTAPSSDVS
The following text describes a protein:
Function:
Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Localization:
Endomembrane system. Membrane; Multi-pass membrane protein.
Sequence:
MIADAVPAVTQVVFAICFCTGVSTFIPNLVETAKDMSVFVSHLLIPSLTFYNIATPLSVELLKKCSVLILFAALIVVLGVLIAQLASFFLFRVKNTGIPRDLQRSVHFKLLRRRGRRESDDGVSGKSTHILNIVVNGEREELPIEPRDVLERLEPPEEEYENEPFYCCAMTLALCVQNAVTIPLSLLQALAETLPWIDLEAGTAYIFMYSIVTICVVWGVGPVLVRRAKKTTDKRRIIRELMEQQRRLQNCHEATTQTEVSCTTSRLASPTFPMLSDPPANVDGSSGEARAGGPVHRSGVAPESSTSDRGAARYSIGEVNQSHDAARCPIVLLTTTPSTCQIFGCDLVETGQIRVISRSQFAREEAEANAGVSCLGSSMAWLKRTVVQLLRTPSFTSVILGVFVGIISPLKGLFVGGNLSPVMDILSALAKGSIPCSLFLLAANFMNPKATVPAPKPVRMRDAEQNTDFPLDDITVNRSFAETYYRERQDITFDIHASFTPAHLSQPGTGSAAGGRADFAPFATSTPATDPRKGFLTTLYDMFSLNGINKNFMFGVIVLRLIVMPAVGYGLVLAVLYISPSMLGGGSSQNVLLLVLLGQLASPSAINCNILFVAERYMPHVWAKMLFFQYVCCIVTLTGWYGLSIYIVR
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MKNTIVQQQRFLQSIHKPTYLQRPGSFALVYPYYAVMAGLGLYSLYASGRVIFGKKDAF
The following text describes a protein:
Function:
RNA-binding protein that is involved in oogenesis. Required for correct targeting of the migrating anterior follicle cells and the establishment of anterior-posterior polarity in the oocyte. May act as translational repressor of oskar during oogenesis. Function seems to be sensitive to small changes in expression.
Sequence:
MLSCASFNKLMYPSAADVAKPPMVGLEVEAGSIGSLSSLHALPSTTSVGSGAPSETQSEISSVDSDWSDIRAIAMKLGVQNPDDLHTERFKVDRQKLEQLIKAESSIEGMNGAEYFFHDIMNTTDTYVSWPCRLKIGAKSKKDPHVRIVGKVDQVQRAKERILSSLDSRGTRVIMKMDVSYTDHSYIIGRGGNNIKRIMDDTHTHIHFPDSNRSNPTEKSNQVSLCGSLEGVERARALVRLSTPLLISFEMPVMGPNKPQPDHETPYIKMIETKFNVQVIFSTRPKLHTSLVLVKGSEKESAQVRDATQLLINFACESIASQILVNVQMEISPQHHEIVKGKNNVNLLSIMERTQTKIIFPDLSDMNVKPLKKSQVTISGRIDDVYLARQQLLGNLPVALIFDFPDNHNDASEIMSLNTKYGVYITLRQKQRQSTLAIVVKGVEKFIDKIYEARQEILRLATPFVKPEIPDYYFMPKDKDLNLAYRTQLTALLAGYVDSPKTPSLLPPSLAGQLTPYANNNHLLLNANGLATPTGVCAPTQKYMQLHNSFQQAQNRSMVAGGQSNNGNYLQVPGAVAPPLKPPTVSPRNSCSQNTSGYQSFSSSTTSLEQSYPPYAQLPGTVSSTSSSTAGSQNRAHYSPDSTYGSEGGGVGGGGGGGARLGRRLSDGVLLGLSNSNGGGGNSGGAHLLPGSAESYRSLHYDLGGNKHSGHRAFDFDMKRALGYKAMERTPVAGELRTPTTAWMGMGLSSTSPAPAPLENGENGAAGGGASSGWRLPPGLGSPYGLSATTGLLDATPVNRRMQLAKHKDIQTLLTSLGLEHYIKIFVLNEIDLEVFTTLTEENLMELGIAAFGARKKLLTAIHTLLANEAACSTMPSSSSSQNSSSPRFSGSAAPGAERRPSNQW
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Subcellular Localization:
Nucleus.
Sequence:
MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK
The following text describes a protein:
Function:
Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.
Miscellaneous:
MISCELLANEOUS: The phosphatase activity of the PPP1R15B-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.
Sequence:
MEPGTGGSRKRLGPRAGFRFWPPFFPRRSQAGSSKFPTPLGPENSGNPTLLSSAQPETRVSYWTKLLSQLLAPLPGLLQKVLIWSQLFGGMFPTRWLDFAGVYSALRALKGREKPAAPTAQKSLSSLQLDSSDPSVTSPLDWLEEGIHWQYSPPDLKLELKAKGSALDPAAQAFLLEQQLWGVELLPSSLQSRLYSNRELGSSPSGPLNIQRIDNFSVVSYLLNPSYLDCFPRLEVSYQNSDGNSEVVGFQTLTPESSCLREDHCHPQPLSAELIPASWQGCPPLSTEGLPEIHHLRMKRLEFLQQASKGQDLPTPDQDNGYHSLEEEHSLLRMDPKHCRDNPTQFVPAAGDIPGNTQESTEEKIELLTTEVPLALEEESPSEGCPSSEIPMEKEPGEGRISVVDYSYLEGDLPISARPACSNKLIDYILGGASSDLETSSDPEGEDWDEEAEDDGFDSDSSLSDSDLEQDPEGLHLWNSFCSVDPYNPQNFTATIQTAARIVPEEPSDSEKDLSGKSDLENSSQSGSLPETPEHSSGEEDDWESSADEAESLKLWNSFCNSDDPYNPLNFKAPFQTSGENEKGCRDSKTPSESIVAISECHTLLSCKVQLLGSQESECPDSVQRDVLSGGRHTHVKRKKVTFLEEVTEYYISGDEDRKGPWEEFARDGCRFQKRIQETEDAIGYCLTFEHRERMFNRLQGTCFKGLNVLKQC
The following text describes a protein:
Function:
Involved in the nicotine degradation. Catalyzes the cleavage of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic semialdehyde.
Miscellaneous:
MISCELLANEOUS: The catalytic efficiency of HspA is lower than that of HspB.
Sequence:
MQRKLDSEPLRTRIYIDGYNFYYGCLRGTPYKWLDLLPLFEKHILPSILVTDNHGQIRAWRLLESPSIKYFTAKIIESVARAGDSVSSQARYHTALRKLHDGRIELIEGYYAVNKMKVKIVDPENPDKAPRECREIQAWKVEEKQSDVNLALQAYHDSITGQVDHAVIVTNDTDIAPALQMIRAHTDVRIGVVVPTSGQNRSANTDLIKFAHWKREHINSGELAACQLPRVIPGRKPTIKPESWYGQPELLQEILDLAIPVRGSRAAAFKWMEQPNQFLSGERPIELVETAEGATRVLQYIHSWIAQQEELP
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRLTTLWQNRSPGDRHLSTYFCFAAVRLLLVFVPQLGYVHPDEFFQSVEVMTGDHFRLEHTRTWEFNNSLPVRSIVLPFALLRIPWSFYEFVAECLKAWWQLELLGTYAYVVFPRLIYTLISFSNDYCLFRICRLYGLRFEIRLLAMGSSWILLVFGTRTFSNSLEMAMCSWLLCLVSECMLRTNTVVYKKEFLEEKYDKAESISERVRIWKLKNSLPAHNLQHLMAMSTICVAGVFNRPTFLLFGAPMVFFWLLRGMGTRSITFRDFNLRIALFCLCALPALVLFIFCDSLYYQHLTLGELHMMHLSIDNFVFTPWNFIKANLDSAQTASHGVHPCYVHLMVNMPMLFNVLALASLGAFAQLLLRFFRAEYQVLPRFQSIVSLMSGAIFVPLFFLSLINHQEPRFLLPVTFPLILLHAPKLITGFSAKYPFQKDHPLLRLFYDKLLSSKASGPYLLKIWYVSNVALTLFFGFIHQAGVYPLAADISHVIATKPAATHVHLITSHIYSLPLHLINIPSSRVLHFNRLTHQRYRRPRDFYMYEYGGLPLDSLLQKVKLISGSCEVKKSGPSRRRYKLYLAIPASLSADLHEALVHSNASSYLNFELLKVFYPHLSTEAFPHLQGRHPCDVDAPHWAHDDLRGTCSAEQLPAFSFAYLNKQFSSFVHQLGLALYEIDVTRNKPRSVVIKKASMTETAA
The following text describes a protein:
Function:
Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
Subcellular Localization:
Endoplasmic reticulum. Membrane; Multi-pass membrane protein.
Sequence:
MIAELVSSALGLALYLNTLSADFCYDDSRAIKTNQDLLPETPWTHIFYNDFWGTLLTHSGSHKSYRPLCTLSFRLNHAIGGLNPWSYHLVNVLLHAAVTGLFTSFSKILLGDGYWTFMAGLMFASHPIHTEAVAGIVGRADVGASLFFLLSLLCYIKHCSTRGYSARTWGWFLGTGLCAGCSMLWKEQGVTVLAVSAVYDVFVFHRLKIKQILPTIYKRKNLSLFLSISLLIFWGSSLLGARLYWMGNKPPSFSNSDNPAADSDSLLTRTLTFFYLPTKNLWLLLCPDTLSFDWSMDAVPLLKTVCDWRNLHTVAFYTGLLLLAYYGLKSPSVDRECNGKTVTNGKQNANGHSCLSDVEYQNSETKSSFASKVENGIKNDVSQRTQLPSTENIVVLSLSLLIIPFVPATNLFFYVGFVIAERVLYIPSMGFCLLITVGARALYVKVQKRFLKSFIFYATATLIVFYGLKTAIRNGDWQNEEMLYRSGIKVNPAKAWGNLGNVLKSQSKISEAESAYRNALYYRSNMADMLYNLGLLLQENSRFAEALHYYKLAIGSRPTLASAYLNTGIILMNQGRTEEARRTFLKCSEIPDENLKDPHAHKSSVTSCLYNLGKLYHEQGHYEEALTVYKEAIQKMPRQFAPQSLYNMMGEAYMRLSKLPEAEHWYMESLRSKTDHIPAHLTYGKLLALTGRKSEAEKLFLKAIELDPTKGNCYMHYGQFLLEEARLIEAAEMAKKAAELDSTEFDVVFNAAHMLRQASLNEAAEKYYDLAARLRPNYPAALMNLGAILHLNGRLQKAEANYLRALQLKPDDVITQSNLRKLWNIMEKQGLKTSKT
The following text describes a protein:
Function:
Catalyzes strongly the dephosphorylation of 6-phosphogluconate (6P-Glu) and slightly the dephosphorylation of dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates.
Sequence:
MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVARLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKARGWDITA
The following text describes a protein:
Function:
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEFLMTLVFLVLLVEIVFCTFFMLPVSMHLRKNVYNKLDKLFGGQNAKIFLKVLALLVIIVFCDSIVNSYNINKKLHTPELTGAKFDRQNEYTRMFRYQRNSYICGFCLYLFFLIYRSQGIISQLSNVEASKTAIEKQTKNNLNTVETLLSENEKLKTEIKDLKKMEKEHKAMKSQAENTTKEYLKLQEEYNQLLGKKPKTQKKDD
The following text describes a protein:
Function:
Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione conjugates.
Sequence:
MPSGAVTSEQIRASDIGTTILKAGGSAADAIIATVLAVNTLSPYHSDIGGGGFAIVKEPGDSGQVKCLDFRQCAPEGATPELFKTSNTSTSVGGLAVAVPGELKGLEELHKAYGTLPWSRLFKESIELAEGGMEVRGDLYDFITQEANPAGSSNMRGTWMMEDPTYTSLITKDGQAIPIGSIWKRPEYATTLRKIAAEGAAAFYQGEIAEGLVKAVRARDGVMTVDDLKNYKLKWREPLSTKFKDYTLYAPPAPASGAIWLSVMGMLSQFEPAGYGSVTDLHRLTEALRLAYGQRTALGDPAYIDGVEEKQRDWLTEKRIKARARMIDENHTKEPDYYKPPKVALDFDNGTSNITATDSSGLTISITTTVGLGWGSRIMVPGYGFVLNGSMDDFSVEGRPNGFGYEPQVTNYVAGGKRPLSSSCPYIITNSTGKVIASGGAAGGSTIISSNAQVALFVLVYGFSASQALAANRLHNQILPNVTKVERGSNVRGVRVEGFSEEQVEGLKQKGHVIEWVDKSFSTPCVMVWTDDGWEGDGDPRKHDSGGSVYHE
The following text describes a protein:
Function:
Molecular chaperone that may interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAGSLVQSAILPTVAVNRIQSHLRGSGKVKRGSKMMCQPRKHSLRLQGFAGLRRSDNVEFSSRNQRDFHSVVSGYISYSRGKASRGVAKAMFERFTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGRGSGFVAVEIPFTPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLESLGADPSNIRTQVIRMVGETTEAVGAGVGGGSSGNKMPTLEEYGTNLTKLAEEGKLDPVVGRQDQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGKKVITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALERRFQPVRVPEPTVDETILILRGLRERYEIHHKLRYTDEALIAAAQLSYQYISDRFLPDKAIDLIDEAGSRVRLRHAQLPEEARELDKELRQITKEKNEAVRSQDFEKAGELRDREMELKAQISALIDKGKEMSQAESEAGDSGPTVTEADIQHIVSSWTGIPVEKVSSDESDRLLKMEETLHKRVIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALASYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEKGGRRIGFDLDYDEKDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEVFDRLKVKDIELQVTERFKDRVVDEGYNPSYGARPLRRAIMRLLEDSLAEKMLAGEIKEGDSAIVDVDSDGNVTVLNGGSGVPEPIPPAVSV
The following text describes a protein:
Function:
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular Localization:
Cytoplasm.
Sequence:
MSVSNDLIWQVIRDNNRFLVKRPEFGGIQFNREPVNVSGKNAQRFSGLCNDKAVGVQANSPRGVVLITKTNPKNAQKPAKLFRKDVIANASSRKTYKSIAGRIGRTGYRDDLVKVSVARASAILSSQRPKKTVA
The following text describes a protein:
Function:
Promotes matrix assembly and cell adhesiveness. Plays a role in spinal cord formation by regulating the proliferation and differentiation of neural stem cells.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MGIFVVLTMKASVIEVLLVLLVTGIHSNKEPAKKVKRPKFTVPQINCDVKAGKIINPEFLVKCPAGCQDPKYHVYGTGVYASYSSVCGAAVHSGVLDDSGGKILVRKVAGQSFYKGSYSNGVQSLSLPRWRESFVVSESKPQKGVTYPSTLTYSSPKTAAANAGETTKAYEKPSLPGTTAQPVTLSQALATPVAEATHRATSKPFAASVTSSSRPQPVGHRSQEMEEMATWKPEPVLLDSGFVPKEELSTQSSEPVLQGDPNCKIDLSFLIDGSTGIGKRRFQIQKQFLVDVVQALDIGPGGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSNVGRAISFVTKNFFSKANGNRGGAPNVAVVLVDGGPTDKIEEVSRVARESGINVFFVTVEGAAEREKQHVVEPNFASKAVCRTNGFYSFNVQSWLSLHKTVQPLVKRVCDTDRLACSKTCLNSADIGFVIDGSSSVGTSNFRTVLQFVANLSKEFEISDTDTRIGAVQYTYEQRLEFGFDKYNSKADVLSAIRRVGYWSGGTSTGAAIQYALEQLFKKSKPNKRKVMILITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVIATHPARDHSFFVDEFDNLYKFVPRIIRNICTEFNSQPRN
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.
Sequence:
MKFTHISAFTIVALTTSVHAILPQPSETIDSVDPSPSPSLNSQSVPQATGGPEFPSTSTTQGPGGSQGDHSNQTPRVRLKSSKLSKFLCGIGQGRKSGHRKYKKRPQDGQNDSIDLFLESLLNIPQFSGLGYQGGDYGLADHVEENSRQQQLIEVIAKGINAETSKFKKHLLSFSAYLGEYEVWVKNILNFLDGFEAISKLSSEFINGLGKIFKEFLEIIHVLYESIYQILVKSFGSVETFKQQFTAAALGVFGSGWVFLTWTPSSSTMSIVTTANQDHPEFAPQFAGTGAMTLLALDVWEHAYYVKYRNVRANYVAA
The following text describes a protein:
Function:
Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIQWFPGHMAKARREVTEKLKLVDVIFELVDARIPLSSSNPMLEEIIHQKRRVIILNKADTADEKTTKEWIDYFAEKGLPAVAVNAQEGKGLFKIEQAAEKLMAEKFDRLRSKGMKPRAIRAMILGIPNVGKSTLINRLAKKNIARTGNKPGVTKAQQWIKVGKTLELLDTPGILWPKFEDQEIGYKLALTGAIKDDLLQMEEIAGYGLRFLENHYPDRLQTWLKVETVSEDPIETLAFIAEKRGLLDRYNDPDYSRAAETVVREIRQQKLGRMSFDFPNWEDEVE
The following text describes a protein:
Function:
Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
Subcellular Localization:
Secreted.
Sequence:
MLLSAPLRHLPGLLLLLWPLLLLPSLAAPGRLARASVRRLGTRVPGGSPGHLSALATSTRAPYSGGRGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHVFYVETYGVIEKLSARFQETFCALDQCMLGTHQCQHVCVSDGDGKHHCECSQGYTLNADGKTCSAIDKCALSTHGCEQICVNDRNGSYHCECYGGYALNADRRTCAALDKCASGTHGCQHICVNDGAGSHHCECFEGYTLNADKKTCSVRNKCALGTHGCQHICVSDGAVAYHCDCFPGYTLNDDKKTCSDIEEARSLISIEDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQVHR
The following text describes a protein:
Function:
Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. However, is less efficient than Hsp31 and YhbO, suggesting that YajL might be preferentially dedicated to protein repair. Displays a covalent chaperone activity with sulfenylated thiol proteins by forming mixed disulfides with members of the thiol proteome, and preferentially with sulfenylated cellular proteins, upon oxidative stress; these mixed disulfides can be subsequently reduced by low-molecular-weight thiols to regenerate YajL and reduced proteins. Involved in biogenesis of ribosomal proteins, probably as a ribosomal protein-folding chaperone. Confers resistance to oxidative stress. Plays an important role in protection against electrophile/carbonyl stress. The chaperone activity reported for YajL is probably recruited to execute its deglycase activity, to interact with non-native glycated proteins and gain access to partially buried glycated sites. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity.
Sequence:
MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLAITCSRGVKLLADAPLVEVADGEYDVIVLPGGIKGAECFRDSTLLVETVKQFHRSGRIVAAICAAPATVLVPHDIFPIGNMTGFPTLKDKIPAEQWLDKRVVWDARVKLLTSQGPGTAIDFGLKIIDLLVGREKAHEVASQLVMAAGIYNYYE
The following text describes a protein:
Function:
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The selectivity filter, in which calcium ions are arranged in single file, is composed of two acidic rings separated by one helical turn along the central axis of the channel pore.
Sequence:
MPPSLLPRVSLALLVTSSSSSSAGCSSTSPLWSNYIKRHSTTATVRRFVTTTSVGAASGTKIVVQFRNGVPTLTVPLPSRREELCLFPMRPLTENVGILCENMKTEDRGIDFAAVYTNDGIRLSSSSSLEHVLQMKTFRLRINDVLYDVTVEKPYGKEMNTDEGLSKLDSLRETISALHATLCLDEYKEERERRLAKALEDAERQLEPMEQEKNRIALECDAHANRVMWGLFAVMGVQTGLFARLTWWEYSWDIMEPVTYFSTYLTVIGSAAYYLHTKQSFDYPLAKNRIFTKRFHKKAAIEGFDIDLYMAMIGRVERLREELKRLRDPLFHHLPIPTLEKLEQTLIQESSKNVITKK
The following text describes a protein:
Function:
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (ssc1) (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Domain:
The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Sequence:
MSSAILLGVGIAATAAAGKIGVDAFRKYRNLNGGVKAFLKGGFESKMSRAEAIQILSLNNRTLTRQKIKEAHRRLMLANHPDRGGSPYVASKVNEAKSLLDADRSIRKFSSWALPVSKQRSMPSVLEAVKWLEYSSIPKA
The following text describes a protein:
Function:
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
Sequence:
MTIPEKPQGVIWTDAQWQSIYATGQDVLVAAAAGSGKTAVLVERIIQKILRDGIDVDRLLVVTFTNLSAREMKHRVDQRIQEASIADPANAHLKNQRIKIHQAQISTLHSFCLKLIQQHYDVLNIDPNFRTSSEAENILLLEQTIDEVIEQHYDILDPAFIELTEQLSSDRSDDQFRMIIKQLYFFSVANPNPTNWLDQLVTPYEEEAQQAQLIQLLTDLSKVFITAAYDALNKAYDLFSMMDSVDKHLAVIEDERRLMGRVLEGGFIDIPYLTGHEFGARLPNVTAKIKEANEMMVDALEDAKLQYKKYKSLIDKVKSDYFSREADDLKADMQQLAPRVKYLARIVKDVMSEFNRKKRSKNILDFSDYEHFALQILTNEDGSPSEIAESYRQHFQEILVDEYQDTNRVQEKILSCIKTGDEHNGNLFMVGDVKQSIYKFRQADPSLFIEKYQRFTIDGDGTGRRIDLSQNFRSRKEVLSTTNYIFKHMMDEQVGEVKYDEAAQLYYGAPYDESDHPVNLKVLVEADQEHSDLTGSEQEAHFIVEQVKDILEHQKVYDMKTGSYRSATYKDIVILERSFGQARNLQQAFKNEDIPFHVNSREGYFEQTEVRLVLSFLRAIDNPLQDIYLVGLMRSVIYQFKEDELAQIRILSPNDDYFYQSIVNYINDEAADAILVDKLKMFLSDIQSYQQYSKDHPVYQLIDKFYNDHYVIQYFSGLIGGRGRRANLYGLFNKAIEFENSSFRGLYQFIRFIDELIERGKDFGEENVVGPNDNVVRMMTIHSSKGLEFPFVIYSGLSKDFNKRDLKQPVILNQQFGLGMDYFDVDKEMAFPSLASVAYRAVAEKELVSEEMRLVYVALTRAKEQLYLIGRVKNDKSLLELEQLSISGEHIAVNERLTSPNPFHLIYSILSKHQSASIPDDLKFEKDIAQIEDSSRPNVNISIVYFEDVSTETILDNDEYRSVNQLETMQNGNEDVKAQIKHQLDYRYPYVNDTKKPSKQSVSELKRQYETEESGTSYERVRQYRIGFSTYERPKFLSEQGKRKANEIGTLMHTVMQHLPFKKERISEVELHQYIDGLIDKHIIEADAKKDIRMDEIMTFINSELYSIIAEAEQVYRELPFVVNQALVDQLPQGDEDVSIIQGMIDLIFVKDGVHYFVDYKTDAFNRRRGMTDEEIGTQLKNKYKIQMKYYQNTLQTILNKEVKGYLYFFKFGTLQL
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA.
Subcellular Localization:
Nucleus.
Sequence:
MTDYEGGRYEGNGTDFDNDNYGSADGGGSSPPARPDDHSDSKSQHGSRDHERESSKSREKEREKGRDKERDRDRDRDRDKDRERDKDREKSRDRDRDRERDRDKDRDRHHRDRDRHRDRSERRERGRDRDDDDYHRSRDYDRDRRRDYDRDREERHKRRSPSPSRGRSERRSKSRSRSRSRSKSKRISGFDMAPPPSAMLTGAAAVAAAAGQIPGTAPAIPGMFPNMFPLGTGQQFGTLPVMPVQAMTQQATRHARRVYVGGLPPTANEQSVATFFSHVMAAIGGNTAGPGDAVVNVYINHEKKFAFVEMRSVEEASNAMALDGIIFEGAPVKVRRPSDYNPSLAATLGPSQPNPNLNLGAVGLTPGSAGGLEGPDRIFVGGLPYYFTEAQIRELLESFGPLRGFDLVKDRETGNSKGYAFCVYQDLSVTDIACAALNGIKMGDKTLTVRRANQGANQPKPEQETVLLHAQQQIALQRLMLQPVPTKVVCLTQVVTADELKDDDEYEDILEDMRTEGGKFAFCSATFCYKESGLTYTDRRHHYPLFIFT
The following text describes a protein:
Function:
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Sequence:
MATEKKPPITCHVLDTTIGKPGANIPVTLTLHPSSPSSTSTPQSFQSTTNSDGRVASWTPTPPPFTAPTPLETLFHQPGDQRWSLTFNTEEYFKGRGVETFFPEIEVKFVVREAQKGEHFHVPVLVGGFGYSTYRGS