lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection.
Sequence:
MAIEVGRPAPDFTLDGSQGPVTLSQYRGKNNVLLAFYPGDFTPVCTKELTCFVEDWSKFQGKDTVILGISSGSVDSKSKFAQSLGAQFPLLSDGEKRVAGLYDVSGFLGVARAYFIVDKQGVLRYKHVEALPFFKREDEELLGVLAEL
The following text describes a protein:
Function:
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Has a preferred substrate specificity towards the photosystem II (PS II) D1 polypeptide.
Subcellular Localization:
Plastid, chloroplast stroma. Mitochondrion. Note=Reported to be localized to chloroplast and mitochondria based on transient GFP expression in a heterologous system.
Sequence:
MAVCNCFLQAPPLSRILLPVLSRRATTLSAGYGRLKSTVTFCSTVNRTSPLTSSVRAEVKRVSRKDDKVASATDVQFETPLKIVEYPDPILRAKNKRIDIFDENLKNLVDAMFDVMYKTDGIGLSAPQVGLNVQLMVFNPAGEPGEGKEIVLVNPKIKKYSDKLVPFDEGCLSFPGIYAEVVRPQSVKIDARDITGERFSISLSRLPARIFQHEYDHLEGVLFFDRMTDQVLDSIREELEALEKKYEEKTGLPSPERVEARQKRKAGVGFGKR
The following text describes a protein:
Function:
Component of the centrioles that acts as a positive regulator of centriole elongation. Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity or RAB8 activation. Required for primary cilium formation. Required for sonic hedgehog/SHH signaling and for proteolytic processing of GLI3.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.
Sequence:
MKQRKGQGPGGSRGRKKRGLSDISPSTSLPPLVEGQLRCFLKLTINRVIWKIAKPPTCVLVRVRWWGETSDGTLFCPRDALQTEPKAVRTTTRYAIRCGPKQFTSYLTDMAVLVLEVITKLDHLPIGRVQINGLAQLSPTHQINGFFTIVSSTSKKLGELQVSLALEPLSETYDSYHPLPTTDMTENVLLSKQGFRENTEPSSTQFQVPSRPRDIHTIKIDGKELGANSSRSTTPRGKDHVYFAENPDTIKDSSFGLQHHLNSGQSLESVTLKGRAPRKQMSLLSSSEFQPQIRTVAKSHSDSCILSSNNPPTKDLLSALLEQGNKLRNAMVISAMKSSPETSVLLDQVHPPINEDSLRASTQIRAFSRNQFKDHIEDHLLPSTENTFWRHDTKADTRAIQLLLGSAELSQGNFWDGLGSPPDCPSPGSDVYCSSELNDPQYDQSLLENLFYTVPKSDTSISDFLSEEDDVVPSKKISQSTALARSSKVLESSDHKLKKRSTGKKNRNLVEQQMLSETPEDTQTMTLSVDRLALLGRTHSVRIIIETMGIPPDNHQMTPDKKSYAGPPPKVTTAKKRTFFVEYHFPVGFSESGLGKTALITEVVRLASSKITNGKVKFQQRFVFPVQFGGPMIEHWWNSNLTFQIYAKKTPQKKPEVIGSASLSLRAVIQSELLSFSDQLPVQQENDQTVFGPLKVTMELVTDNKDITGVNTKLSGNTHYTPLCAPTSPNKALPELNQDMTYTKNPQNLNQIHEETAKKAQNLVLPTRKSPSPLAPHPSTFMAMPASHNLVIQTNGSTKESALLLHVLLMVPDGKDFISGESEKQSPCNVYLNCKLFSTEEVTRSVIAWGTTQPVFNFSQVIPVSLSSKYLERLKNNVMVIETWNKVRSPGLDKLLGLVKLPLHQFYMSFKDPKISRLLLDAQYPVVAVDRYMPVIDVFSGHQNGSLRVFLAMGSSDQIMALQRLKHEEGTLPPFSPRPAHFLDQPTVASVAMAEDRGNALMEHCFEIHVEMVKGLAPLQATVWGEADCYVQYYFPVQHSQSSVLKGPEFLENGITLKPFRTATTLCVPDPIFNSEHHHSLLLPAEVPVQRLLLSAFSAQGLVPGGAVQFEIWCRYYYPNVRDQMVAKGTLPLSRICAMVTTQHREDVGIQTFNLPLTPRIENRKQLRNQSSGLLDVGLRYRRSPRTAEGVLAARTVSISVQIIRACGLQAAAKALAEQEPALQFSATVGVNASVTTHLSFLPQGEQRRTHPVACSFCPEFSHHVEFTCNLVTQHCSGEACFLAELLEFAEVIFAVYHENTKSASDIISIESCKEYLLGVVKVPTKELLIKRSGITGWYPIILPEDGGLPHGLELMQKIVGGLELSVSFTHRGDRERVLEAAELLGWSFENSLKDFVRMDEGEPATVTISTPRLWLPIHCVLLAGHNHIHKNTYCYLRYKFYDHEAFWTPLKKPKESVNKKQIIVTFKASKRAEVTRGPSLLWYFREERLEIQVWQAYGNDSVERPHQTDSWIGSAYVDLARLGERSARTLTVSGVYPLFGRNASNLSGAALRVHVVLSSLSSHLEPTHELDSMDCSSHSESEQLPRRNDEVQLSPPEEVSCHQKSPASTQVPCSSTTAEVCLTQEGPAELDGTFAVSILVERAMHLSLKGSPLTERKVLIPSCCVSFATADESSPVYTQVVENTDSPIWNFQQQSRLSKELLLDPQQTLVFKVWHKGDEERVIGFASVDLSPLLSGFQFVCGWYNITDFSGECQGQIKVAVSPLESLIHFKEERQARRGVETSKSLIPIYSPFSFPASDMYAAFSSHMARQTLDQLAHASSKELDFSSPGRSGTTRNQASRHEEHVQNIRRFHESLHLQGEALLPCDDKLTTSPLSSQTSILTSLRKNLSELDQIQRYFSQKLTKPFLPLSPQTQTAISQHQESCRDHLEPGASSLDPGSQCILEKSNNLVLQVSSLITDLQTITRDSQAALSSHRARSRNNKATTLPDARDTEALQEQCTMPDEPLAKAPDKGTDSPPPPPLEETSNGGRMLHESLRHTVPITRMQSSEDTEAGPAYSDEDYEEDIIEPRTLNEITTVTDKTSPWSSFISDTSDVISPQPDEVQREGPSCPSPGPFYREELTVKSSFLSSSERAVNSHLPREGSPSQSLVACEGEASKAKISGESASANPQPIPCPTLSGAQQSRTFVGWSSPQADQNKEPKSEAPAENEAATSELSDSADSFKKLPLNLASQSRREKHKGPPIDSSDIRQRQVTTGSETSTKHSLLLPEPIVVPNFFLPPQQLEASLRMLSLSATLPPAATTDQDKSEATRGALSQRPCRPRPNSLPPNLPEEETRRIARIFSSRYSQKD
The following text describes a protein:
Function:
ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL also acts as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR.
Miscellaneous:
MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity; MISCELLANEOUS: The tightly bound ADP participates in a double displacement phosphoryl transfer reaction and thus plays the same role as histidines, cysteines and aspartic acids in other phosphoprotein intermediates.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPVALEAASSIAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQMLALAAKE
The following text describes a protein:
Function:
Required for spermiogenesis.
Sequence:
MNKSLIFLLSFAYSCYSTKTENNFDINDVENKACQYGCGFENVRRTSFRKTYDILYTCSECSTLFDLCIKYRTCQDGCVPEMPVLPYDQAKDVSARIRPPMNPCLDLVTACNYESMDSYEILRSENPFLYI
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MIELRNFSYTYGTAAIPALKNINLEIRKGELLLVTGHSAAGKTTLALAMAGILHHEIGGKIEGNISFQSRDVKEFDGIKELSRHIGVVFDDAESQLIFTTVEEEIFSGLENRGHPEKEMVRRSKEAMDFCAISHLNNRAPHMLSGGQKQKVALAATLALDTEVLILDEATAELDSQAVRKVFSVLKRLKDAGKTIIIIDHNIEDFLEIGDRVVLLEKGEIKAIKSPSEFTSKSSDLTSTNLTSTSALQTDLPLSRTAEQPIISVKNLTQRYGEILALDNIDLEIYPGELVAILGENGSGKTTLVKHFNGLLRPYSGKVTVKGLETSTTPINELVKHTGLVFQNPDNMLFEDTVEAEINFGLNNIGVKGPEAVGAILRSLELVNLNDKQKVFPRHLSRGERQRLAVACIIAMKPELIVLDEPTTGLDAEESDRMMQLMRKLQQEGHTIVMVTHNLQIVRDHVERVIRMESGKVVEDSANRKFSGKGSVKEESDYKGHVSKEIVSEEIVSEEIVSEESVSEECVRGGTCA
The following text describes a protein:
Function:
High-affinity uptake of glycine betaine. Does not mediate either carnitine or choline uptake.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLKHISSVFWIVIAITAAAVLWGVISPDSLQNVSQSAQAFITDSFGWYYLLVVSLFVGFCLFLIFSPIGKIKLGKPDEKPEFGLLSWFAMLFSAGMGIGLVFYGAAEPISHYAISSPSGETETPQAFRDALRYTFFHWGLHAWAIYAIVALCIAYFQFRKGAPGLISSTLSPILGDKVNGPIGKAIDCIAVFATVVGVSTSLGLGATQINGGLNYLFGIPNAFIVQLVLIIIVTVLFLLSAWSGLGKGIKYLSNTNMVLAGLLMLFMLVVGPTVLIMNSFTDSIGQYIQNIVQMSFRLTPNDPEKREWINSWTIFYWAWWISWSPFVGIFIARVSRGRTIREFLIGVLVTPCILTFLWFSIFGVSAMDLQQKGAFNVAKLSTETMLFGTLDHYPLTMVTSILALILIAVFFITSADSATFVLGMQTSYGSLNPANSVKLSWGIIQSAMAAVLLYSGGLAALQNTAILAALPFSIVILLMIASLYQSLSKERREIKKAEKLDKPRSPRVKKAY
The following text describes a protein:
Function:
Required for determination of left/right asymmetry in nervous system. Acts together with unc-40 to control an initial left-right asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may control the asymmetry in Wnt signaling response by restricting posterior polarization to one of the 2 Q neuroblasts. Involved in left-side QL posterior migration. In right-side QR, unc-40 and mig-21 pathways mutually inhibit each other in posterior migration, allowing anterior QR migration.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYSIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW
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; Peripheral membrane protein. Mitochondrion intermembrane space.
Sequence:
MGNVFGNMTTLNATSMMTVMTPEVENFKPSFDPMLGFPNGRKRREMVATEAELESARIPPKSRNYCAHKLIEFKACRKDHFPLVYRCQHEKHEYDDCLYQDYLIRYKEYERERRLRAREEQRRRKQAAENLE
The following text describes a protein:
Function:
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSSNTAHICVVGSLNIDFAVSTSRCPGPGETLTANSLSVTAGGKGANQAVACGRASHTSSDASKVTVSMIGAVGADDVYYATLIRPTLEDSGVDTKYVEEKTDSRTGSATIIVEDSAHGENRILVVPGANHAGMDDVSKILATIQSYPQAPALIVLQGEIPRHTTLDLMRHFNQPGNQTHMLFNPAPVFADGVPVDALSNTSVLVMNETEAVQMQASISPESAISTQTTDELKPEDLASQFHALANVRIVLITLGAKGVFFSTRTGRKGFVAGVRVQKVVDTTAAGDTFVGYFAAAFAEFIATSAPLEEFDKTIEQAVRRANCAAALCVQRPGAMQSIPTASEVDGLDSR
The following text describes a protein:
Function:
Regulates arginine biosynthesis genes.
Subcellular Localization:
Cytoplasm.
Sequence:
MKEYDDYSAKEQQQLAVCQRLISEKSYLSQEEIRRDLQNEGFEGISQSTVSRLLKLLGAIKIRNTKGQKIYSVNPQRRPSPDAGRSIAEMVVSVEHNSEFILIHTAAGYGRAVARILDYHALPEILGVVAGSSIVWVAPRVVQRTALVHKQINYLLKMNLNS
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex. Binds to the 7-methylguanosine cap of RNA molecules (By similarity).
Subcellular Localization:
Nucleus, nucleoplasm. Nucleus, gem. Cytoplasm. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
Domain:
The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA. The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules. The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially. Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit.
Sequence:
MNIDSNIIKNENLINANNHTDRRDVHDSLAEAPEKITELKKNHWEELLPSSSNWYCTSVADCNENQIYIYACKSNVSIFNIKSKKFIGELNGHTDRVTSVGFFKRFESKNDESYKWCITGSDDKTVRIWKFNSNDDDHNEDTEIGDDFKHGSGGGGSDGGGGDDVNNFYGNKSSNFCIYYHQEHKAGVTCVVASPLVPDLVLSGDKAGALVIYRTLTNHVFPIPPIIGNNISISTLAFSPNHSDLVAIGYLNGIVLIYNFVIRSTVCKISAHSADVLSIVWFDSTIIQKNNIFHDNNINDQDDNNSNHRNRIFLATCSKDKAIKIWKQVGEKIESGFTNIYQFNPSKYSIQHSSSSGGGGINQNDKQRVWLTLSWSPESPQYLLSNSLTADVLIWDLINFKSPPEKFQSSHQRLIFNITQIPNSDGSLAKTTATTETTTKNKIKNKDKKQSQIKLNNKVITVSLDRQIIIWENLKAKIKIQGLGGFVYSIDTCSYSPNTFAIGCGDNTIRLWSPTENSKDAYESKTLWKGIQSKVTSLSICKDYGFSNSNLIAFGMDDGRVGVYNINTNQSKIFPGGHKNEIYEIIWKPPPTPTPQKNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNNNSNNEQQPNKLYSIGNNEIYEWDYNDFNKSFTNMTPIIQQLNPKETFSKHKTDINFNLNGDMISIGYSDGTIDIFTSEFLFLTRIREHKKLINRVQWNHFKENEMILASASTDKKVIIYKLSKIGNQNENEKKIDNEKGKENENEKGKENENENENENENENENENENEIENIVNNNNENDTEIEIKNINKNENVDKEEMVENNNNNNIKYKIEILHQFIGHKNNVCSVSWSNVDPNLLGSASADGTVQVWNIKSKEAISNMRGHDGRVFTVCWSLLDPNLLVSGGEDQTVRLWNYSTQPFKTVTESQIKKSPQPELSISLNKKITEQQQQQQQPQSPIKSNPDQSNNPSLVPPILLTSVTSTSNTTATATTITQITESLPKKRPIFLLNKDIVQRQDSSQYVVPLAKYFTTNDQDSINTNETKQEYEFGSNSENNNSKIEAIFSEKKEIINKLVQKESLELLKIDDVENYISLNSWNPANLKQALYQVIKNGKLTGNIVSLSIQAGREIFESICNLYSQQLICIGDYHLAVSYLLMIGKVNEAIEVYRNTLLFQEAIILAKSRFLPDDPIINKLFTEWAKQTETSHPIHSIKCYLATINDQSLNSKQELLKLLSSVQTKQIIKIQSDLEQILK
The following text describes a protein:
Function:
Binds to spermatozoa upon ejaculation and may play a role in sperm capacitation. Displays heparin-, gelatin- and phospholipid-binding activities.
Subcellular Localization:
Secreted.
Sequence:
MAPLVGLFLIWAGASVFQQLHPVNGGDIPDPGSKPTPPGMADELPTETYDLPPEIYTTTFLPRTIYPQEEMPYDDKPFPSLLSKANDLNAVFEGPACAFPFTYKGKKYYMCTRKNSVLLWCSLDTEYQGNWKFCTERDEPECVFPFIYRKKSYESCTRVHSFFWRRWCSLTSNYDRDKAWKYC
The following text describes a protein:
Function:
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes to the plus ends of microtubules and the mitotic spindle poles.
Sequence:
MESLLTDKQRSDLETSIFGYVSRLTNDEALLSQLAAVLSQPSGSEPVPADTLKANALLLEKKWLSVIRLQRKVMDLETRLEAAEREASSTHKANGLGAGDPKTWLPKTSRFSLLHKQPVNAVSFHPFHSTLASACEDGNIRIWDYELGEIETTIKAHTRGVLDVDFSQPDTGASRDKSHDKPRADVSHAQPRALLVSCSSDLTIRIWDPQNEYANVKTLTGHDHTISAVKFTASGNHVISASRDKTVRVWSVQSGYCVRTVHGHTDWVKSCAALNEEFIFSAGIDHVTRVSEFVSGDGKMTLLGHEHVIEGVAVYPKSAAGCLAKLDKTSSYFVVSWSRDKTIRVWSSRGDPLLILRGHDNWVRGVVLHPAGRYLVSVSDDKTMRCWDLEQGGRCIRVVDAHGHFVTCVAWAPNDVNGRVRCLVATGGVDGQVKVWQ
The following text describes a protein:
Function:
Involved in endocytic trafficking by stabilizing organelles of the endocytic pathway. Probably acts as a cytoskeletal linker protein required to tether endosome vesicles to the cytoskeleton. Involved in modulation of endocytosis at stages required for down-regulation of membrane proteins that control synapse size. Not involved in synaptic vesicle recycling. Required in R7 cells for boss endocytosis into multivesicular bodies (MVBs). Has a role in regulating adult longevity.
Subcellular Localization:
Cytoplasm, cytoskeleton. Endosome. Synapse. Note=Enriched at neuromuscular synapses, in both presynaptic and postsynaptic regions.
Domain:
The coiled coil domain mediates homodimerization.
Sequence:
MSAPKNEMYYSLLEWFKTLNLNAPHADAESLADGVALAQALNQFAPESFTDAWLSKIKASAVGSNWRLRMSNLKKVTQSVYDYYSDVLNYSLSDFSKPDLQRIAEKCDLGELERLLQLVLGCAVNCAEKQSYITEIMCLEEELQANIMRALQELEATRQASTPEGGVASSLSRGSRTGLLDSKAVQEDRDALAQKCFETEKKMLLLIDEKTNLQQELHKLQQEFARLEQHSTVIGDDGVSLGPVQTGSVRYNELRRQLDLLKEELLQSEGAREDLKIKAQQQDTDLLHMQMRIEELMKSSAEVTTLKDEVDVLRESNDKLKICEAQLDTYKKKLEDYNDLKKQVKILEERSADYVQQNAQFEEDAKRYANTKGQVELFKKEIQDLHAKLDAESSKNVKLEFDNKNLEGKNLALQRAKDSLLKERDNLREAVDELKCGQLSSNTALTGTTVSRELQPSATVEKLQRLEAENKALREGQGGQTALAQLLDDANKRCENLREQLKTANERILSLSHASQSDDPILKESEFGKQIKQLMELNEQKTLQLEEAVTQSTSLQCKVTQLETNLSAREQEILVYDAKYRKCVEKAKEVIKSIDPRIASALDASVLEKSADLVEAEPKPKMSVMEEQLMTSAFYRLGVNAQRDAIDSKLAILMGSGQTFLARQRQSAPRKSLSAMKSK
The following text describes a protein:
Function:
Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLKRRSNALITLSRTKLFPITTVAYYHRRLLNQQRRAVSTSPKKEIKSLEDLANLDSLDGVDTELIRDLINEHTTKLNIKKELDMLKKFSQEEESGHEIPVKRFIRPLWMFILMGSSVYLLLHFSWWKLEHEERESQLKKEVEILEHQLNELIVQDKTHNTSRGKGSNESTHMKPWYRRWFW
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular Localization:
Cytoplasm.
Domain:
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence:
MATDYYAVLGVRRDASQDEIKKAFRRLARELHPDVNPDPKTQERFKEINAAYEVLSDPQKKQVYDLGGDPLSQAAGGGAGGFGAGGFGNFSDIMDAFFGTASQRGPRSRTRRGQDAMIRIEVELDEAAFGTTKDIQVDTAVVCNTCNGEGAAPGTSAQTCDMCRGRGEVSQVTRSFLGQVMTSRPCPQCQGFGTVVPTPCPECAGDGRVRSRRTLTVKIPAGVDNGTRIQLAGEGEVGPGGGPAGDLYVEIHELPHSTFQRRGDDLHCTVTIPMTAAALGTKVPLETLDGMEEVDIRPGTQSGQSIPKHGRGVTHLRGGGRGDLIVHVEVTTPGKLDPEQERLLRELAKLRGEERPTGQFQPGQQGLFSRLKDAFNGR
The following text describes a protein:
Function:
Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.
Subcellular Localization:
Membrane; Single-pass membrane protein. Lipid droplet.
Sequence:
MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF
The following text describes a protein:
Function:
May act as a carbohydrate transporter.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MSELKNISILFIVVFAASMLRSTEAIDHIVGSRNGWIIPVDGHSFYSDWASNITFKENDVLVFNFVTGRHTVVELNQTYFENCNVNQNIQFLDTSPSPVRFTLNRTGVFYFTCSIPGHCASGQKLIVNVSASSPALSQGPSSPTSSVSSDIHIDLVATFSILIAAVAVNFLF
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system. Degrades total E.coli RNA, which is partially inhibited by cognate antitoxin VapB15. Upon expression in M.smegmatis inhibits colony formation, which is neutralized by coexpression with VapB15.
Miscellaneous:
MISCELLANEOUS: In this enzyme the conserved residue Asp-4 binds Mg(2+) via H(2)O.
Sequence:
MIVDTSVWIAYLSTSESLASRWLADRIAADSTVIVPEVVMMELLIGKTDEDTAALRRRLLQRFAIEPLAPVRDAEDAAAIHRRCRRGGDTVRSLIDCQVAAMALRIGVAVAHRDRDYEAIRTHCGLRTEPLF
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MVMGGRHGLTRKPRAVGIMTIFLGFCLVSSLWLTLYSIVRARHLSVEEPLDFTSGLQNCQDAKISKLVALSLQDPTLGGLLPALKEYEPGQCISRTEEGPIRIPSRFTPSPYLVAKLRLYENRHRKCAPKAVKLSKNGTNSRKELGDCQFVIWIGNSGLGNRMITILSAFVYALLTDRVLLLDNTSTDIDGLFCEPFPGTSWLLPENYDYNWMNTVTWENTNRLGRLLQMSGFGNITIPSPVPNDYIFLNLMHDYDEHDRRFFCSRIQKQLKKVSLLYWRSNNYVVPGLHFDHSFHCKLDLMFPERATAFHHMARYLFRPSNSMWGMILRFRQPYLDGARRQVGLQVRILESNVTIPIVADQRARPPDLLKHRSSSYETLIPSFRDFQLLACVLEKEILPKGSSSAEDMLLSSKTRSTSVLVTSLDSAYYETLRNYYLEHPVEGTDYIGVYSPSEELYQQYGSDHDKKAWADMYLLSLSNTLVTSPRSTFGYVAQALAGVIPWFLTKIDSLETANETFQAHGPCNRGVSLEPCFHAPPALDCEGYGNGLNSSNIFSFIKPCEDVIGGIKIMPSYANDITAEGKTESRSERKT
The following text describes a protein:
Function:
Dioxygenase that specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA. N(6)-methyladenosine (m6A) DNA is involved in epigenetic transgenerational inheritance. Plays an essential role in DNA replication and repair in the germline during meiosis. Binds to components of the DNA replication machinery such as top-2, and directs their localization to DNA to control DNA replication.
Subcellular Localization:
Nucleus. Note=May co-localize with top-2 on DNA.
Sequence:
MGSAEQACGCKGARFCALCETTERVKKLRVVEDKHVNYKVFIYDHIRQIAIPTTNLNSQSSLEDIIDESTSCQSVSTDGSIEIDGLTLIHNFLSESEESKILNMIDTVEWAQSQSGRRKQDYGPKVNFKHKKVKTDTFVGMPEYADMLLNKMSEYDVKKLGNYQPFEMCNLEYEEVKKSAIEMHQDDMWIWGNRLISINLINGSVMTLSNDNKSFLCYVHMPHRSLLCMADECRYDWKHGVLAHHIRGRRIALTMREAAKDFAEGGELYEKYGAELIRLGNIRVPLSKTSV
The following text describes a protein:
Function:
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Subcellular Localization:
Cytoplasm.
Sequence:
MLNQIKKDAQDRMEKSLEALKGHISKIRTGRAQPSLLDAIQVEYYGAATPLRQLANVVAEDARTLAVTVFDRSLISAVEKAILTSDLGLNPSSAGTTIRVPLPPLTEERRRDLIKIVKGEGEQGKVAVRNVRRDANDKIKALLKDKEISENEQHKAEEEIQKITDIYIKKVDEVLADKEKELMDF
The following text describes a protein:
Function:
Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.
Sequence:
MGVFQKGEDQKGESANMKPIPLLSSYDMGKFNLSHRVVLAPLTRSRSYDNLPQSHAMEYYSQRATKGGLLIAEATGVSSDAQGMSVIPHTPGIWTKEQVEAWKPIVDAVHAKGGIFFCQIWHVGRASDMEERPISSTDKPIEKTEENYFLGFSTPRSLTVEEIPDVIKHFTLAAKNALEAGFDGVEVHAANGFLLDQFMKDGVNARADEYGGGVAGRCRFALEVVDAVAAEAGAGRTGVRLSPYSRCLDCADSDPDALAAHMARELGSRGVLYCNVVEPEMVATPAEGGSGGETMRIPHRLRAVREAFAGTLMVGGGYDREEGNWAVAGGYADLVVYGRLFLANPDLPRRFRLGAPLNGYDRATFYTADPVAGYTDYPFLDDDGDDGLAASAASASSNKSGDQDGV