lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a signaling pathway regulator involved in innate immune system response. In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis. Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription. In response to interferon IFN-alpha, associates in a complex with signaling pathway regulator IFI35 to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35. In complex with IFI35, inhibits virus-triggered type I IFN-beta production when ubiquitinated by ubiquitin-protein ligase TRIM21. In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries (By similarity). Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses (By similarity). Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion. Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Secreted. Note=Cytoplasmic NMI localizes in punctate granular structures. Nuclear localization increased following IFN-alpha treatment. Extracelullar following secretion by macrophage.
Domain:
The coiled-coil domain is necessary for interaction with TRIM21 and for TRIM21-mediated ubiquitination of NMI; The NID domains are necessary for the interaction with IFI35. The NID domain 1 is necessary and IRF7.
Sequence:
MSADEDNKEQVLKECEQAEEIMKDKQNQKLISEITKENIQLKEEIKKLEAELQETTRTSQINEDIPETKIKFTSVENPESDSEFSDISYSCQVSSKVPYELQKGQALITFEKEEVAQNVIRMEYHHVQVQNENVMLTANPVSLNSGVKFQVHVGVSKMKINVTDIPDELPESQMRDKLELSFSKSRNGGGEVEYVEYNKQTRSALITFVESGVADKILKMKDYPLYINQNCHRVTVYPYTETHLKKFQVFSGVSKRTVLLTGLKHLQTTDEEVVEDFISIHFQREKNGGGEVEVVKCSLGQPHTAYFEE
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity; Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MALAEICKISNAPYMRPNAWSSADVEEEQKGLMCNLANPYTLAAPPFENPLHNLNEIQANGDKTGVKINFDHGTTTLGFKFKGGVLLAVDSRATGGSYIGSQSMKKIVEINQFMLGTLAGGAADCVYWDRVLSKECRLHELRNKERISVAAASKIMANIAHEYKGMGLSMGMMLAGYDKRGPGLYYVDSEGSRTPGNLFSVGSGSLYAYGVLDSGYHWDLEDKEAQELGRRAIYHATFRDAYSGGIIRVYHIKEDGWVNISNTDCMELHYMYQEQLKQQAAK
The following text describes a protein:
Function:
Epoxide hydrolase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero-calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the hydrolysis of aromatic epoxide-containing substrates, such as the conversion of 24,25-epoxycucurbitadienol to 24,25-dihydroxycucurbitadienol.
Sequence:
MNEVSHRRIKTNGIWVHIAEQGRGPLVLLLHGFPEIWYSWRHQISFLANHGYHVVAPDLRGYGDSDSPLSPSSYTFMHYVGDIIGLLDHLGEQQAFVVGHDVGAAIAWHLSLFTPERVKASINLGVAYFDRNPNAKLGESLIRTFGDGFYISQFQEPGRAERTFARYDYLTVIKKFLLITQTDNLIAPPGMEIIDYLETPSRLPPWITEEELQVYADKFQESGFTGALNYYRALDLNWELTAPWQGSKIRVPVKFMVGENDIGFDINGIRQYIEGNVFRNLIPDLEVVMLDGHHYLQQEKHHQVSEEILSFLAKFPPE
The following text describes a protein:
Function:
As component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in cilia function and/or assembly. Essential for functional IFT-A assembly and ciliary entry of GPCRs. Associates with the BBSome complex to mediate ciliary transport.
Subcellular Localization:
Cell projection, cilium, flagellum. Cell projection, cilium, photoreceptor outer segment. Cytoplasm, cytoskeleton, cilium basal body.
Sequence:
MKAVFTLPEKTHGPGPVFFTWQKAGGNYLVTTGYDQNVNVYDRHGNRKDQITLPGMCSGLGWEKDGDVLGIITDKSPILILWDANNRNVSQVDTGLRDVLTLLLWAKTGPFVAIGTSKGNLLVYNHRSCRKVPILGKHTKRITYGAWSQQNMLALVGEDNVLTVSNQEGDTLCQTSLKSEATLVQFSCMKRDEKNTVENTVSLVLNKRTLLLLDIYDPENPYVLAFQEMYGKIIEYRWYGDGYILLGFTNGYFVAISTSLKDIGQEMMQVRCHKQSLSHIAICLPQNKVASCSDNVIKVYDLSDLQEVQSVITVDDERRIEWLDWSDDGQLLGASGASGSLHVFLTKLPALGNSLGHRYAYLTSLYEVTVASVTEPELQMTVKVDIEPGFIALGPFHLVVGMNNRAWFYALGDKSMLPLQDKEYLGTVKSMKLNGDYAAALFDGKVQMQLIETEQSDMEERESKLFPDSSQGQAKITCHSVTEEFLMYGTDAGTIEFFFLEDWTIVNRYRHTNGIRQIHPDSSGTRLVVVDNKSEGFIYNPVNDHIVVIESFPTTTKGIFWDQYVENHGCFVAFDDHNISMYVYTPETVAGATVEPVRTISVPSGQNPLLLHCGSLTCQTQSGKTAVLLVSSQEEKGKITTAQQRQALSEHLKMRKFQDAWKICVELNSKKDWIEFGNAALANLDLDLATRIFRHIGDVGMVWSLQGIRHIEDKNLLAGHLAMFKGDFGLAQDLFLASSQPTAALQMHRDLLHWEQALQQAKRLDQQQMPFISREYAQQLEFSGDYANALVHFEKGITGELDHAEHDKACRAGIARMSVRCGDIRKGVHIAMQLENRVLQKECAEILESMKQHQEAAVLYEKGGYHDKAASLYIRLKNWTKVGNLLQNIASPKIYAQYAKAKEADGDYEEAAKAYESARDFENVIRIHLNHLNKPEEAVRLVKETKSVEGAKMVARFFQKLGDTISAVQFLVLSKCTDEAFQLAKTAKKMDAYADALGDSGSADDFYSIASYYEEARNNLEAGRFYLKAGQHKQAVKLLVKAASKDDDAAIGLAVQAAAEANDDQLTRQLIEFLMGETDGIPKDFKHLFRLYMGLRQYREAGKTAVVISREEQNAGNYRNAHNVLLSMYRELKKQHIKVPAEMHSNLMLLHSYILVKLHIRQGDHTQAARLLERVANSISRFPAHTVPILTSTVVECHRAGLGNSAFVHASTLLRPEYRGQLDPKYRKKVEGIVRKPHREQEPEPTAPCPFCESSVPEMELVCSHCKNTLPFCLVTGKHVLRHDLTLCPKCAFPAILSKFRALLETESSCPMCSETVVASELESQDFDPNLCGQD
The following text describes a protein:
Function:
Heme-binding sensor kinase component part of a two-component regulatory system involved in methyl sulfide metabolism. Does not act as a phytochrome-like photoreceptor.
Subcellular Localization:
Cytoplasm.
Sequence:
MIGVDMKLETLVNNGPAVIFLCRAETGWPVETVTANIVRFGYSPKDFISGGLGYADIIYPADLEIAVSQFFSYVEKDYIGKDLDYKVEYREYKGEAGEHKRNGKGNIGKDRGGYDSFTQQYRLLNKSGDVLWVEAEIKVLEEEEGKAGLFQVTVFDISRWKHTEKAMPAALDTENELKRIINSGHVIVFLWRAEPGWPVDFVSENISELGYTPEDFTSGRIVYTDIIHPDDLDNVRAEVSKNTEEGRDYFSKEYRVLAKSGEVRYVDERTLIRRNEKGEITCYQGILLDITQRKEAEELILSQNRVLERIASGASLDEVLLLLVNYAEEMKPGLLCTVMLLDREQKRLFYGACPSLPKLYSKAINGIQVQVNSETAGTAAGTGKRVIVGNIMKDPFCEECREIAQKVGLKACWAEPIFSSGGEVLGVFTIYLRETRKPREEELEFIRTNAYLAGIAIEHVQAADALKESENRFRTIFDNINDQLYIREPDGISYMDVNQVVVDRLGYSKEEILNMKAEEIIPSEYWASVRENMQKIKAEGSRIFEAGAVCKGGTVIPLEVSARIIDYGGKKTIFSVSRDITERKKAEVAQRLNGSRLEALVKLDQMAGASLKEITDFAREEAVRLTGSKLGYLAFMDAYESTLVMHSWSDSAMEECSIEDKQFVYPVKSMGLWGEAVRQRKPIITNDYPAPNPLKKGYPKNHVHLIRHLNIPVFDGKRIVAVAGVGNKEENYDESDVRQLTLLMQGMWQLIQRKQLEEALRTYSGELSRANEELRSVNMMKTEFVEEMMFPEKAEYGEIMDYETLYAIDSQQQKAVNTFIHYSEKLRRLVDSLLYQSLEKAGKIDYSFEETQLKDVLSDAFLNNVFLIGEKALEVKKEVSASLSEIKGDREKLTALFTALIDHAIKFTPQGGKLALEVKEEAGNVHIVIADSGKGISKELIPYLFDRLYQVNDSITRRYQGLESGLYICKNIVDAHKGEIWFESEEGLGNLMHVKLPK
The following text describes a protein:
Function:
Probable mitochondrial mRNA stabilization factor.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MLRAGRYSKASSVLRAVGGKRPSVCMASRVLTRLYSNGKEDDQVASSSSPSSKPWYLQGTGKPEIDVTSPFVGKIKLPATPVPDTVVNVTEYMRDKLGVTDITCFNTHEAHRPCVKNGYVILGCVKSTRHGARSMIELMRFLKTEYGVLPQKEGGISVQELRKRQKRLQRKGNLTSASAELAGESDWYLIDSKLYDGNGSGVFVHLLTKEKREDLNLEGLYCTSEERGLYQKKVLSPSNDHLPNDDDDNVLAGLKRLALQNSRRYYSSTSSATADYARSSLQGGSNMENSDAPLFSLVDSLAQLPETEELDPQEWIRSLDAKWAFIDLTEKHWQARWLMYRLLYVNRLHALQRAQDGDSANLDHLKRDLTFCYKTLLEYFTLKQAMNGRLNKEELVGMLDIMLTQKELNGGYSKLVKHNRVLQQLLDHYKFHEPELFRDEQITIRTLKLMVSSQAKLNVLSEFVRFLRDTGYTNRNVAIKCIEILAEAKEWRELKTFMFRDTTAALLSDPMVWAHFLRSILAHGEPLLWRSLIDDGSILWLVRCGVDVRACEELHSALLELFQRAGYDAVKADSLLRDYIQDGACS
The following text describes a protein:
Function:
Catalyzes its autophosphorylation, which is needed for enzymatic activity and phosphorylates myosin II heavy chain at a threonine in the C-terminal tail region. This phosphorylation is critical for regulating the assembly and disassembly of myosin II filament, affecting myosin localization during an array of cellular contractile events, including cytokinesis and capping of cell surface receptors as well as chemotactic cell locomotion.
Sequence:
MFNIKKRKESITGIPPINVNSPQSVPLSGTLQSPLITPNSPNFVSRQCPFKKFGCSSFLVSKAEFDNHLKDDAQFHLQLAVEKFDHQFDLHTQLMAHFTEQMEDQLEKTMKVVRNHTDSLGGNVQTKLDEGIEKCMAFAKKVEQQQQQLAKRLITQQIQEKKSTSSPLVKGGISGGGGSGGDDSFDGANISSMSTSKQELQQELQSLSIKMKKELTELSDELSQKLERSTGNIDIKIKRIEGEVNEKIDKRQLVSTIDDSIGKKTDSIGYTLESSIIKKVEEKEKKKSEQNQLLFDSKIESLKDKIKIIETQQLDTSSEVRKLKLESTSSGNLMAGLNGTSGRPSSSSHFIPSSVSAAANNINKNEIMEEVKKVEEKLQKKIREEIDNTKSELSKVERSVKDNRSEIEGLEKDCKNQFDKQDNKIKQVEDDLKKSDSLLLLMQNNLKKYNEFVDRERDRESERLKLQDSIKRLEQNQKKIEAEIQEGNEQVERVLREEASISPISSVPKSPITTKRSSIILNSPPMTSQQSSPKIQDLLSSSGSSSVSGINISSETGEMGILWEFDPIINKWIRLSMKLKVERKPFAEGALREAYHTVSLGVGTDENYPLGTTTKLFPPIEMISPISKNNEAMTQLKNGTKFVLKLYKKEAEQQASRELYFEDVKMQMVCRDWGNKFNQKKPPKKIEFLMSWVVELIDRSPSSNGQPILCSIEPLLVGEFKKNNSNYGAVLTNRSTPQAFSHFTYELSNKQMIVVDIQGVDDLYTDPQIHTPDGKGFGLGNLGKAGINKFITTHKCNAVCALLDLDVKLGGVLSGNNKKQLQQGTMVMPDILPELMPSDNTIKVGAKQLPKAEFSKKDLKCVSTIQSFRERVNSIAFFDNQKLLCAGYGDGTYRVFDVNDNWKCLYTVNGHRKSIESIACNSNYIFTSSPDNTIKVHIIRSGNTKCIETLVGHTGEVNCVVANEKYLFSCSYDKTIKVWDLSTFKEIKSFEGVHTKYIKTLALSGRYLFSGGNDQIIYVWDTETLSMLFNMQGHEDWVLSLHCTASYLFSTSKDNVIKIWDLSNFSCIDTLKGHWNSVSSCVVKDRYLYSGSEDNSIKVWDLDTLECVYTIPKSHSLGVKCLMVFNNQIISAAFDGSIKVWEWQSK
The following text describes a protein:
Function:
NADP-dependent D-xylose dehydrogenase catalyzing the oxydation of D-xylose into D-xylonolactone (By similarity). May also display activity with other sugars. May play a role in the regeneration of NADP(+) in the presence of these sugars (Probable).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTSMSGASPVIHWGFLGAGSIAAVFAKDLVGVPERHKVQHEIVAVATRDSEHRASSFAKNHCAPCKPKAYGSYEELVKDDKVDIVYISSTHPQHYEVVKLALLNDKAVLCEKPLTINYPEALELVELARARNLFFAEGFWIRFYPIVKAAKTLLHEDRVCGDHFRLFVDFSQDFRFRELPSESRLRTVSLGAGVLLDMGVYPLTWSRLLLYDDPKNEKQEPTVSSNALTFEDHNGDIGDYTTAVTLVFPKTESIAMLCTSMDRGKMSDDFLKLDGENGNQLFISGDCYRPQSIKLIRASGETEVFDFSFDDATGFFYEQDAVAECLLKNMKEAPEIPHEETLKMMQLTDQIRRQINVTYPADLRYTTA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDMAQEPVTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWVEDRERPEFQAVQRGPRPGARKSADPKRPCDHPAWAHKKTHVRRERAREGSSFRKGFRLDTDDGQLPRAAPERTDAKPTAFPCQVLTQRCGRRPGRRERRKQRAVELSFICGTCGKALSCHSRLLAHQTVHTGTKAFECPECGQTFRWASNLQRHQKNHTREKPFCCEACGQAFSLKDRLAQHRKVHTEHRPYSCGDCGKAFKQKSNLLRHQLVHTGERPFYCADCGKAFRTKENLSHHQRVHSGEKPYTCAECGKSFRWPKGFSIHRRLHLTKRFYECGHCGKGFRHLGFFTRHQRTHRHGEV
The following text describes a protein:
Function:
Required for male fertility. Plays a critical role in sperm capacitation and acrosome reactions during fertilization, and also plays a role in the regulation of proteins involved in spermatogenesis. Regulates protein pathways that promote chromosomal synapsis formation, double-strand break repair, formation of the inner mitochondrial membrane cristae and apoptosis in developing sperm. Required for normal sperm motility and binding to the zona pellucida, potentially via a role in ADAM3 protein maturation.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Expression in the acrosome decreases after acrosome reaction.
Sequence:
MASWALSAALLCLGGAFAYSELHSLSLREGSALGQATVPGPPEEEQPVTKDCGIAPLRGAVEGSRIIGGSQADTGAWPWQVSLQVQDGDILMHVCGGALVRDRWVLTAAHCTKEARDPLKWRAVMGTNDLTRSPYHSRNIRITDIIIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPFGVFQKLDQNTACFISGWGRTREEGNGTTILQEAKVHFISREVCSSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCYLPEHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEWMTHYLSQGNINRLFNMDIVLGQVLTALGSVILLGVT
The following text describes a protein:
Function:
May be involved in cell wall metabolism, related to senescence.
Sequence:
ADAIKAGLDLDCGPFLAIHTEAAVRRGLVSQLEINWALANTMTVQMRLGMFDGEPSAHQYGNLGPRDVCTPAHQQLALEAARQGIVLLENRGRSLPLSTRRHRTVAVIGPNSDVTVTMIGNYAGVACGYTTPLQGIGRYTRTIHQAGCTDVHCNGNQLFGAAEAAARQADATVLVMGLDQSIEAEFVDRAGLLLPGHQQELVSRVARASRGPTILVLMSGGPIDVTFAKNDPRISAIIWVGYPGQAGGTAIANVLFGTANPGGKLPMTWYPQNYVTHLPMTDMAMRADPARGYPGRTYRFYIGPVVFPFGLGLSYTTFAHNLAHGPTLVSVPLTSLKATANSTMLSKTVRVSHPDCNALSPLDVHVDVKNTGSMDGTHTLLVFTSPPDGKWASSKQLMGFHKIHIATGSEKRVRIAVHVCKHLSVVDRFGIRRIPLGEHKLQIGDLSHHVSLQTNLGEIKV
The following text describes a protein:
Function:
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MRGDRVRLIVVLLVLAGALLAIFWPSKGGWISNIRLGLDIKGGARIEYMVEVQQGTENPSDVVDDVWTVLRNRLDAAGYTEAAVKKVLRDNKYYIVVEIPGATDTVQAEKLIGSTGVLYFAQVLDEYLGEDPSKVPELSLEARRENAVWLKGRDGKWYLVKKEIMGRKDLVLEAPRIVYARPEVETRTGRYGYKVSFELAKEYVDIFKKITQALYVPEGTYDPKKRLAIVLDDVVQFVGQVVAIITDGKAEITGNFSLEEAKQLAAILRSGALPARLVKTSSGWVAPLLGRDVIDASLKAGIIGLILVLVYMIIYYRTMGIVADLALIYNTVLLLGVMAAGKFILTLPGIAGIILTIGTTVDGNVIIYERIKEEMRLGKPVKTSIAAGFDRSLSTILDANITTILTGLILYYFGTGTIKGFAITLIIGVLGSIFVNLVFSRLLLDALARFIKPLRADEAQGGTGQ
The following text describes a protein:
Function:
Involved in DNA repair and RecF pathway recombination.
Sequence:
MSRTYQTLGIVVKGMAFGESDRLVTIFSPEYGLIRAIAPGARKPKSSLRGRTELFVVNQFLLFAGKSLDRINQAETQYSYPGLGQNVCNLAAGQYLIELILALGTEASAQTSLYELFTEHLRRLETEATVENIYGHLAQALFHCLGAEGIAPQFHHCAITAQTISPNFYDRQWRVGFSPELGGIVDLRSSRDMGPIPQMRRLTAMELSLLQQLNQPALPDPQQYLPVIARKNFRLWDWVKAENLMRYYAQRQLGKSFRAAVLLDSMWEVDF
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MNLSAVTVQPVPFRPLEREKHIESLFRAFTRGRRHAPEPQDTPVSRSLGDGLSPRLTEDHEHENSQGGTEKRAALELHTLKEAELRAGLSSIQEPVMAVAGEDQGLALLETVSQLRIMARPELQGPHCKPGRSYSITTGTRSQIYVAVEESSCLCLQCCGPARSCSIRGYSRQAQEVFLLERPLRADACCLGCCLMEMRAFGADRQLIGTVRQRWSMFTPLLEICDLDGTSNIRILGPCCPCRCYSNQEFQVVSKTGEKLGKIWKKWPGYNEDYNIDHEYFGVDVPPEMNPKSKLLLLAATFLLNHMFFEMS
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:
MAEARYRPAPLASLPATLDPAEYNVSPEDRRLQARRLAIRARLKRQYLLQYDNPHRRALIDDPALYRWTYARSTNVYPNFKPTPKTSLLGAIAGIGPLFFWYYIFKTDRDKKEKLIQEGKLKRPLSLLS
The following text describes a protein:
Function:
This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular Localization:
Mitochondrion matrix.
Domain:
Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the transient carboxylation of the biotin covalently attached to the C-terminal biotinyl-binding/biotin carboxyl carrier (BCC) domain.
Sequence:
MLRAASNFRAVANREFACAKRQLSKTTRKNATAAATRPGVPRDEREGKEIYTTVGIDHNEPKFDKILIANRGEIACRVIKTAKAMGIKTVAVHSDVDSNSLHVKMADEAICVGEAPTAKSYLRVDRILQAVEDTGAQAVHPGYGFLSENTKFAAELEKAGAKFIGPNSKAILDMGDKIHSKKIATAARVSMIPGYDGEIPEEDFCVKVSREIGYPVMIKASAGGGGKGMRVAWNDKQAREGYRLSKQEAASSFGDDRMLVEKFIDNPRHIEMQILCDKHGNALWLNERECSIQRRNQKVIEEAPSSFVPPEMRRKMGEQAVQLAKAVGYDSAGTVEFLVDSQRNFYFLEMNTRLQVEHPITECITGIDIVQQMLRVAYGHSLPLTQEQVPLNGWAFESRVYAEDPYKGFGLPSVGRLSKYVEPRHVDGVRCDSGIREGSEISIYYDPLICKLVTHGDNRQQALDRMQEALDNYVIRGVTHNIPLLRDIVQEKRFRSGDITTKYLPEVYPEGFQGTVLTHAEEKTVIAFAAALNARKLARANQFLNQNRQRSTHVASFSKTYKFVSSLPAKEGQRPTEHAVEVSFVDGDANKAKVSIGGKVIDISGNLSLSLPVNSIEVNGEHITTQIVGKRAGEITVLYKGTPFKVQVLPEQAVKYLQYMKEKAKVDLSTVVLSPMPGAIKNVNVKPGDMVSEGQELVVMEAMKMQNSLHAGKTGRVKAVNVKVGATVDEGEVLVELE
The following text describes a protein:
Function:
Involved in gametogenesis and steroidogenesis.
Subcellular Localization:
Secreted.
Sequence:
MRMRVLVLALLLPVLMSAESECRCSCRLTNISITVESEECGSCVTIDTTACAGLCWTMDRVYPSSMAQHTQKVCNFKNLMYKSYEFKGCPAGVDSVFVYPVALSCECNQVNSDTTDWGAISPQTTSCSIH
The following text describes a protein:
Function:
Probable inactive histone-lysine methyltransferase that acts as regulator of transctiptional gene silencing independently of histone H3K9 methylation. Contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci.
Subcellular Localization:
Nucleus. Chromosome.
Domain:
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Sequence:
MAPNLRIKKACDAMKLLGISETKTRAFLRKLLKTYENNWDFIEEDAYKVLLDAIFDEADAQSTEKNKKEEEKKKKEEEKKSRSVATSRGRRKAPEPLVQDEEDDMDEDEFPLKRRLRSRRGRASSSSSSSSSYNNEDLKTQPEEEDEDDGVTELPPLKRYVRRNGERGLAMTVYNNASPSSSSRLSMEPEEVPPMVLLPAHPMETKVSEASALVILNDEPNIDHKPVISDTGNCSAPMLEMGKSNIHVQEWDWETKDILNDTTAMDVSPSSAIGESSEHKVAAASVELASSTSGEAKICLSFAPATGETTNLHLPSMEDLRRAMEEKCLKSYKIVHPEFSVLGFMKDMCSCYIDLAKNSTSQLLETETVCDMSKAGDESGAVGISMPLVVVPECEISGDGWKAISNMKDITAGEENVEIPWVNEINEKVPSRFRYMPHSFVFQDAPVIFSLSSFSDEQSCSTSCIEDCLASEMSCNCAIGVDNGFAYTLDGLLKEEFLEARISEARDQRKQVLRFCEECPLERAKKVEILEPCKGHLKRGAIKECWFKCGCTKRCGNRVVQRGMHNKLQVFFTPNGKGWGLRTLEKLPKGAFICEYIGEILTIPELYQRSFEDKPTLPVILDAHWGSEERLEGDKALCLDGMFYGNISRFLNHRCLDANLIEIPVQVETPDQHYYHLAFFTTRDIEAMEELAWDYGIDFNDNDSLMKPFDCLCGSRFCRNKKRSTKTMQILNKA
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. Probably involved in early steps of spliceosomal assembly.
Subcellular Localization:
Nucleus, nucleoplasm. Nucleus speckle. Note=Moves from nuclear bodies to nuclear speckles upon interaction with SR proteins.
Sequence:
MTKKKNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGKSTGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGETSQIRAHDAAEREKGKSKKSNKNFSPGDVSDREAKETRKKESNEKRIKRKRRYSSSDSYSSSSDSDSDSESEAYSSSSYESSSSSDGKHRKRKSTTRHKGRRGERKSKGRSGKKKARPDRKPSTNSSSDTESSSSSDDEKVGHKAIKSVKVDNADQHANLDDSVKSRSRSPIRRRNQNSRSKSPSRSPVRVLGNGNRSPSRSPVRDLGNGSRSPREKPTEETVGKSFRSPSPSGVPKRIRKGRGFTERYSFARKYHTPSPERSPPRHWPDRRNFQDRNRDRYPSNRSYSERSPRGRFRSPPRRRSPPRYNRRRRSTSRSPDGYRRRLRDGSRSQSPRHRSRSQSPRKRQPISQDLKSRLGPQRSPIRGGRTSPAESLSPSHSPSPPGKRGLVSYAD
The following text describes a protein:
Function:
Required for vacuolar assembly and vacuolar traffic.
Sequence:
MSVDESNSDSEIDSISSSDEDEEPKLIYERITEKFQGCFMNDTISACAISKEHFFFGSHNGAIYIYQKNGILLRKMILHSASVVDLSVDLESENLASCSMDGKMIISNITTRETTVHDFKRPLLSVAIDPYYSTRSSRQVLSGGRAGKVVLSEKGWLGNKDTVLQADCGAVYKISWYTTYIAWASDLGITVYSTEFGKVLGRLEPPKRLPNDEIFPYQLFWQSESRLVIGWSDQIMIVSIQRSNVANELPKISLQALLEIDSIVSGVLMLGFNILTLAYIANVEDFTSAIPSQRIEGCRPELRLIDSSFKELCGDAIGLANYSRLQPSDYHLLPDPSSNSHSFVISPNDIVYVRERNQIDHVKYLVSKEMYAEAIDAVKKLPEIPPSLQISELAKKYIFHLLGKGQYKEAGMVIPSLYNDNLAEWEQWVFVFAENDHLEDIADFLPTGENHLSPLVYEMILAQYLATDERTFNKKLHEWPTMLYSVSTIRNATLKKFKENQKSSTLTESLAFLYLEDNMPIDAFHLYLKLHSELCIDLILQHNLYDEARASVLLLMLISSKGKSSDTKSAMSSMLVQHVHSFPPQEVIMQIHSVPQFLYEYFCEFELMYPNSLMEYGDLKLDVFAEFDRKRFFDFLVNTQCYSLDHAAQICKQYNYLDELVYILGRMGNNKEALMLIINELLDIGRAIRYVKEQADRELWDDLISYSLDKPEFICTLLENIGTDENARNLLSKIPPGTKLPHMKKSISKLLADHQSQVQLYQSCYKLFKNESISMAIKYREQEQSGLEFLVKDNPFNSFGDEQLDYNYRKRIPMIYDLRTKKYIRPEDVRIDTDDVFKDDKIAYFKTRMHLKPEVQMRNKLDLLMMLYKQT
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity).
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MSSYYNKGDAPSWEALDQDGLDDVIDTSEYAYASRDHILFCIDAAQSMHKPYPDTTDESGQLVRGRSALHQALDVAQQIQRAKVLSGPDDSVGLLLYNVDPSAVAEDPGNYQPGNYVFQTLRTINAEEMKRLVKLMQTAKEQYEAQDDDETVETTEPEILRKTFPPIEESHEMNIANVIQTCNFLFRDGGTQLRGNKRVFWITDNDMPPGMNNRQPARTSYGDLTTYGVTAETFFIDRPDHRFNPNIFWNDILDREAIDYNDDQPDPEGLSSLADLMKDLVIKTSPKRTHFHVPLKLGKDGEIVIGVSGCSMVSEQGKGASRYVKMRGQVVEEVQSKTEYTSAETGAVLKDSEIGQAYEFGNEAEVRNILEPNPWEAHVKERAKNQNAVDHVLEDDKERRQREDEGEDLEEEEEDDKKGVEKWMGKQKAALPKIVARTRLQFSNEEVSQFRSMGIEPQIKVLGFQAASQLRFQDNLKHPFFIYPNEEEYTGSTRTFAALLNSCLKYNRHALALCRLRSNHVPEFCVLIPQEEKTSSNGQEYPPGFHLIILPYKDSIRPPPKKVAEFLQSPPIATDEQINAMKAVIKRTRFKAAAYRPEIYPNPSLAYHYDQLQALAFEEDWDPEDPAKQALDKTMPLYGGMHSRAGEFMEEFNKEIENDERAVEKLAAPTKRGKAEKETTVNEWDLRNIPDMWKKGTLSQCKVQELKDWAKHYHVPLQGKTKKADIIDVVSEHLSTSEDDLAGASSKKAKK
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
MHCLFIKQMRGLVKVRHSLAKKHFVIGVAYSSFKMRPTRPSAADGTERLPFQWLKLRAPEFRVSGEQITVLQEPSEFYNAIKDNIGLSKKSIVLASLYLGDGPMEEELVKSIHDACERAESEGEELSIHVLLDCVRGSRGVKNSRTMLQPLLKDFRDQVTVSLYHTPELRGAKKALIPERFNEAIGLSHLKVYTFDDTLLMSGANLSEMYFTNRQDRYILIKNCPELVNFFNELVLAVSSLSFQLHPDNSLTLHSADSIHPFEGDLEEFKLRAFNKIQNVLESHEHDHSLGSLKKWQRTVTGSSKSDCAMNNQRECRTDQSKLGHATTDHKTVQSSLGSVLVAQESGGVHYVFDASANERTSKCNEGDVTDGSVESQGDGCHGDLRQGRTDHNSVEETVDQVKVQLQDEDAIHVRGQDAHPFVGNSRQRTLDDTKATASQGTKSLEDCTKDIKEADTVIYPLVQMGPLGITVDQEVTRQLLGEGDPEAVCYLASGYFNLTSEYMDTILQSNATFEMLMASPQVNGFYGSRGISGYIPHSYTFIAREFFRAIHQGRQQRRITLYEFYRVAWTFHVKGLWYYLPEESLPSLTLIGSPNFGHRSVHRDLEAQLAIVTQNASLREQLHNEHERLYARSEKVTADTFTQPERRVPLWTRLVTIVTRNFF