lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MHPFGSQLLSSHYAAIGWDPDNDYAQLTKPTRALLDLNFLPGIHFSLGKLPAHQFANSASLSVLSPPSNISLAQRTLPQSSPYPTLTGSVSYVASSIQSFQLVPTRLAALTTVVDRFAVPSPPPNKSAEQHNGTFNTAQDYLLYGRFHIPTYRLDALYSYQFSPTLQALATLVSVPSSTSNSLGISGNGANQDGSPINHMSNGIGGPSIWNMMVSMNHDTGKWSQQYSYSTEDGLFGARVLHNFPATTTVRRRENNSALAHNAAQDSQVSLTSTDRKKLIDEDEVMDNVLKGRFSVGGELYFSAQRKSAGVSTGIRFCTIPDPPGAALTQQPTVINATLNPIMGQISTSYGTKIGPNLAMATRFDFNFFSFDSDITFGLELLQKKRAKDSHLNTHQPHELLVEGAEGKRDLKIMEKSYSNSTSMDKQDVNRAPGTANNYLIHSFWRTVSGLEDTLSILRARVSPVTGLTLMWEGRWKECLIGIGIQSEFLVSSPPLCLSATTHPSINEKQLPKVSSHPRQQSPLIKGICLELQYTTDN
The following text describes a protein:
Function:
Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody, Midbody ring.
Sequence:
MKKGSQQKIFCKAKMPSSSHSPIPSSMSNLRSRSLSPLIGSETLPFHSGGQWCEQVEIADENNMLLDYQDHKGADSHAGVRYITEALIKKLTKQDNLALIKSLNLSLSKDGGKKFKYIENLEKCIKLEVLNLSYNLIGKIEKLDKLLKLRELNLSYNKISKIEGIENMCNLQKLNLAGNEIEHIPVWLGKKLKSLRVLNLKGNKISSLQDISKLKPLQDLISLILVENPVVTLPHYLQFTIFHLRSLESLEGQPVTTQDRQEAFERFSLEEVERLERDLEKKMIETEELKSKQTRFLEEIKNQDKLNKSLKEEAMLQKQSCEELKSDLNTKNELLKQKTIELTRACQKQYELEQELAFYKIDAKFEPLNYYPSEYAEIDKAPDESPYIGKSRYKRNMFATESYIIDNAQAIQIKKMEPDEQLRNDHVNLRGHAPLDRQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAVQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAEKQKEIKDLQIAIDSLDSKDPKHSHMKAQKRGKEQQLDIMNKQYKQLESRLDEILSRIAKETEEIKDLEQQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLQDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDTEASQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLKLGAGEMNIHSPSDVLGKSLADLQKQFSEILAHSQWERNEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARINFDKRQHEARIQQLENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQFFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKEEQFRLEMEKTGVGTGSNSQVLEIEKLKETMERQRIEIARLQNVLDLTGTDSKGGFENVLEEIAELRREVSYQNDYISSMADPFKRRGYWYFMPPPPSSKVSSHSSQATKDSGVGLKYTASTPVRKPCPGQQDGKEGSGPPPASGYWVYSPIRSGLHKLFPNRDADSGGDSQEESELDDQEEPPFVPPPGYMMYTVLPDGSPVPQGMALYAPPPPLPNNSRPLTPGTVVYGPPPAGAPMVYGPPPRNFSIPFIPMGVLHCNVPEHHNLENEVSRLEDIMQHLKSKQQEERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAINLVKAHQELRLLQADAKDLEQHKIKQEEILKEINKIVAAEDSDFQCLSKKKEKLTEELQKLQKDVEMAERSEDHHLQVLKESETLLQAKRAELEKLKSQVTSQQQEMAVLDRQLGYKKEELHLLQGSMVQAKADLQKALRLGETEVAEKCNHIKEVKSLLEELSFQKGELNVQISERKTQLTLIKQEIEKEEENLQIVLRQMSKHKTELKNILDMLQLENNELQGLKLQHDQKVSELEKTQVAVLEEKLELENLQQIAQQQKGEIEWQKQLLERNKREIERMTAESRALQSCVECLSKEKEDLQEKCDIWEKKLAQTKRVLAAAEENSKMEQSNLEKLELNVRKLQQELDQLNRDKLSLHNDISAIQQQLQEKQEAVNSLQEELANVQDHLNLAKQDLLHTTKHQDVLLSEQTRLQKDISEWANRFEDCQKEEETKQQQLQVLQSEIEENKLKLVQQEMIFQRLQKERESEESKLETSKVTLKEQQHQLEKELTDQKSKLDQVLSKVLAAEERVRILQEEERWGESLEKTLSQTKRELSEREQQLVEKSGELLALQKEADSMRADFSLLRNQFLTERKKAEKQVASLKEALKIQRSQLEKNLLEQKQENSCMQKEMATIELVAQDNHERARRLMKELNQMQYEYTELKKQMANQKDLERRQMEISDAMRTLKSEVKDEIRTSLKNLNQFLPELPADLEAILERNENLEGELESLKENFPFTINEGPFEEKLNFSQVHIMDEHWRGEALREKLRHREDRLKAQLRHCMSKQAEVLIKGKRQTEGTLHSLRRQVDALGELVTSTSADSASSPSLSQLESSLTEDSQLGQNQEKNASAR
The following text describes a protein:
Function:
May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MVMRPLWSLLLWEALLPITVTGAQVLSKVGGSVLLVAARPPGFQVREAIWRSLWPSEELLATFFRGSLETLYHSRFLGRAQLHSNLSLELGPLESGDSGNFSVLMVDTRGQPWTQTLQLKVYDAVPRPVVQVFIAVERDAQPSKTCQVFLSCWAPNISEITYSWRRETTMDFGMEPHSLFTDGQVLSISLGPGDRDVAYSCIVSNPVSWDLATVTPWDSCHHEAAPGKASYKDVLLVVVPVSLLLMLVTLFSAWHWCPCSGKKKKDVHADRVGPETENPLVQDLP
The following text describes a protein:
Function:
Catalyzes the F420H(2)-dependent reduction of biliverdin-IXalpha at C10 position, leading to bilirubin-IXalpha, a potent antioxidant. As biliverdin-IXalpha is produced in high amounts in macrophages infected with M.tuberculosis, its reduction by Rv2074 may play a role in protecting mycobacteria against oxidative stress, aiding the persistence of M.tuberculosis infection.
Subcellular Localization:
Cell surface. Secreted.
Sequence:
MDTGEQHDADDEFVRFWQERRVCFLSTRRADGTPHLVPVGVTYDHATRTARVITSRDTAKARNVRRAAGAVVAVGQVDGRRWSTLEGVARVRDDAGAVRDAETRYAARYRQPRANPERVVIEIDVRRFLGTVRPSERRPQA
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA.
Subcellular Localization:
Nucleus.
Sequence:
MSHYGGGYRGDRGGDRGGDRSADQRNNYRPEPEQGYGYPPMRDEVWPAAGGGGRMDRGRERFDDRDRGREAGRRERSRDRAEREPRRRSRSRSRSGSPPVKQGRRRPTLFDVLPAGMAPGAPPPPAVLPGAQPNLAAAAAFAAPPPSIGLAPPAVAGFGAPPGGPPAVSQQATRHARRIYVGGLPPTATEQSISSFFSHALAAIGGNTAGPGNAVVNVYINREKNFAFVELRTVEETSNSMALDGIMFEGVSVRVRRPNDYNPAAAVSLGPSTPNPALNLAAIGLSNSNLGGGGGGGGGGGGKSNPNDNPDRIFVGGLPYYLTEDQCRELLGSFGAIKSFDLVKDRDTGNSKGYGFVVYQDTSVTDIACAGLNGLKMGDRTLTVRRATEGAPGGGAAPAMGPAGLGGLAGLGGLNPLAGVGGVVVNPLGLATATRIVVLTDAVSAEEIIDDQEYQDILEDMKDEASRHGLCNNVLIPRPTADNPTPAGMCKVIMEFNDVNGAMKARNAMHGRKFAGRVVNATYLTEAAYFGGRYDELAA
The following text describes a protein:
Function:
Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3 (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MNQTAILICCLVFLTLSGIQGIPLSRTVRCTCISISNQPVNPRSLEKLEIIPPSQFCPHVEIIATMKKKGEKRCLNPESKAIKNLLKAVSEKKSKRPP
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAATKAELLLPSLQISEPPASPLDGYSKLEELQMLLQNAAAGGSLLAASAADAAGLLSGESGDYGESLLDILDLQNFPPLTPRLQPLAYSGRFIFDPSSSGCSNLWAEPLLGLLGLGSITAPPSAAGSLTTSTPSVASSTPSQPSLGCSTIDVSSILSATPSYTSAAGSDSAHPPTDAFLAPQLYQSQAPPPAYPSSASRLGLQPVMAMLPDYTLPQQAPDGELSPSPDQKPLQPPFTPLSTIKAFSAQIQPQGPGGLLAKSCQSKKSPGGRQCRTPPHERPHVCPADGCERRFSRSDELTRHVRVHTGQKPFQCRICMRSFSRSDHLTTHIRTHTGEKPFPCSECGRKFARSDERKRHAKIHQRQRDRKPDGATATIPEAPASPDSSYSSPAHSCPAIGIQASSPCFTSSSACSSLSQVFPSSPSHHFYSSSCSSPLGSSLSELPSPHSSNLC
The following text describes a protein:
Function:
Part of the UDP-N-acetylglucosamine transferase complex that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharides are transferred from the lipid to nascent proteins by oligosaccharyltransferases. Functions as a protein-membrane adapter recruiting ALG13 at the cytoplasmic face of the endoplasmic reticulum, where the complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MVCVLTLAASAGGLAVLLIVRLWAVLRSHPVTPRQSLGLLIVAGSGGHTAEILRLVGSLSGAYSPRHYVIAESDEMSAKKIHSLELARAQNDSTTEHTEYYLHRIPRSREVRQSWLSSVFTTLYSIWFSFPLVHRIKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVETLSLSGKILWHLSDYFIVQWPTLKEKYPKSVYLGRIV
The following text describes a protein:
Function:
Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide. Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme is able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.
Domain:
The N-K motif seems to be a discriminant that could be employed as a fingerprint to identify beta-glucuronidases from the large GH2 family of proteins.
Sequence:
MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ
The following text describes a protein:
Function:
Acts as a calcium sensor for mitochondrial flash (mitoflash) activation, an event characterized by stochastic bursts of superoxide production (By similarity). May play a role in neuronal differentiation (By similarity).
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MASEELASKLQRRLQWEEGDSGLQPAPGAAPDPEPQPQPPAWAPTARADAELSAQLNRRLDINEGAARPRRCKVFHPYSEFPEFSRRLIKDLESMFKLYDAGRDGFIDLMELKLMMEKLGAPQTHLGLKSMIKEVDEDFDGKLSFREFLLIFHKAAAGELQEDSGLMALAKLSEIDVALEGVKGAKDFFEAKVQALSCASKFEAELKAEQDERKREEEKRKVRQAAFRELKAAFSA
The following text describes a protein:
Function:
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKPALLEVMRMNRICRMVLATCFGSFILVIFYFQSMLHPVMRRNPFGVDICCRKGSRSPLQELYNPIQLELSNTAILHQMRRDQVTDTCRANSAMSRKRRVLTPNDLKHLVVDEDHELIYCYVPKVACTNWKRLMMVLSGRGKYSDPMEIPANEAHVSANLKTLNQYSIPEINHRLKSYMKFLFVREPFERLVSAYRNKFTQKYNTSFHKRYGTKIIRRQRKNATQEALRKGDDVKFEEFVAYLIDPHTQREEPFNEHWQTVYSLCHPCHIHYDLVGKYETLEEDSNYVLQLAGVSGYLKFPTYAKSTRTTDEMTTEFFQNISAEHQTQLYEVYKLDFLMFNYSVPNYLKLD
The following text describes a protein:
Function:
Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner.
Sequence:
MSTPSETTTTTTSAPKLQLVVRSKTTAYQETSNGYGKNLTLPSFTNGDCRHVEYSKDGTLIAYVNINEIIICSSIDGSVHSKIERPNVGMISFSPQNSFLLTWERMSEYNNNENNLIVWDIKTKQILYKSSQKYCNQENWPLIKWTDDEVLAGKLNQNEVHFFNGRSIGVLAKKIKLADISSFDFAPGNAPYKVATFVPEKGSTPGSARIYVYPTVNEHVSHLTFFKASEAKVLWNKKGNAILVHTFTDTDKSGKSYYGETGLWFLSQDGSSFNLNIKGPIHDVQWSPTLDQFMVCYGNMPSQTTLFNLKGEPLVDFGLNPRNTIRFSPNGKLLCLGGFGNLQGDMDFWDLTRYRKICSTQSHCAVFTEWAADSIHFMTAVLSPRIRVDNGIKIQRYDNTVVYKEDIPELYQALWRPLNPLSFPNDKIIYPSVQQKEASPQPTKYTPPSLRNQQVASSAASPIRSPPGMELPPPPPGFKVYLTVNNKSAPKPKQPKGSNNTTTTTTTSPKPQSDEPKRELTPVEKKIRSVERKLKEVEILKDKLNSGEFIPPTAIEKINNESKFLEELRQLQQQL
The following text describes a protein:
Function:
Catalyzes the irreversible aromatization of 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate (cThz*-P) to 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate (cThz-P), a step in the biosynthesis of the thiazole phosphate moiety of thiamine. Cannot use cThz* as substrate, indicating that the phosphate group is essential. Has no thiamine phosphate synthase activity, despite a high sequence similarity with ThiE.
Sequence:
MELHAITDDSKPVEELARIIITIQNEVDFIHIRERSKSAADILKLLDLIFEGGIDKRKLVMNGRVDIALFSTIHRVQLPSGSFSPKQIRARFPHLHIGRSVHSLEEAVQAEKEDADYVLFGHVFETDCKKGLEGRGVSLLSDIKQRISIPVIAIGGMTPDRLRDVKQAGADGIAVMSGIFSSAEPLEAARRYSRKLKEMRYEKAL
The following text describes a protein:
Function:
Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MEASAPAGRLNSCLDVLSSSTARPELFLSVQEGLAGEFISLTKTLYDFHKALGSDVISGSPLKELVVENFDEEQIWQQLELQNNAALGHFQEAVAKSVKEEADISLLEPLEEEDEEEEKEESDEEQMDAEDQTEEEAEIQNDHLEEESDQSGKKGLKGTETHSFSDEDSDIDFDIDELEQRTKRLKSAVKKAGETSIVDDRFFKLYEMEAALDAAEKKESKAKDDKDEDDDDIDYFEEIISEDDEDDGEEEFGNASMMLTKSARDLKYKDYFDPVDDHEGFTGESKDNGEDEQSEGADDDDDGEEEDAIDEMEDDEDAIERAEKDNLSEPSKRVKFSLPYDSDGEEDTHTFQGKAEKSPEVKSSFEKRQEKLSEKIKKLESELLTEKPWQLKGEVTAQKRPENSLLEEMLLFDHAVKMAPMITEETTLELEDIIKRRIKDQAWDDVVRKEKPKEDPFEYKKRLTLDHEKSKLSLAEIYEQEYLKLNQNKTEEEEKPEHAEIKKMMDSLFLKLDALSNFHFTPKPPVPEVKIVSNLPAITMEEVAPVNVSDAALLAPEEIKEKNKGGEVKADAEKSSTDKKRERRKKKLARRIKLREKEKRQKLLEKKAEGNPRLSKKASAAELKKLTKEGRTSLLKDDGKDKALKSSKAFFSQLQDQVKMQITEAKKSQRKPKKRALSAQKLKL
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. Functionally redundant with CDC27A in the control of gametophyte development.
Subcellular Localization:
Nucleus.
Sequence:
MEAMLVDCVNNSLRHFVYKNAIFMCERLCAEFPSEVNLQLLATSYLQNNQAYSAYHLLKGTQMAQSRYLFALSCFQMDLLNEAESALCPVNEPGAEIPNGAAGHYLLGLIYKYTDRRKNAAQQFKQSLTIDPLLWAAYEELCILGAAEEATAVFGETAALSIQKQYMQQLSTSLGLNTYNEERNSTSTKNTSSEDYSPRQSKHTQSHGLKDISGNFHSHGVNGGVSNMSFYNTPSPVAAQLSGIAPPPLFRNFQPAVANPNSLITDSSPKSTVNSTLQAPRRKFVDEGKLRKISGRLFSDSGPRRSSRLSADSGANINSSVATVSGNVNNASKYLGGSKLSSLALRSVTLRKGHSWANENMDEGVRGEPFDDSRPNTASTTGSMASNDQEDETMSIGGIAMSSQTITIGVSEILNLLRTLGEGCRLSYMYRCQEALDTYMKLPHKHYNTGWVLSQVGKAYFELIDYLEAEKAFRLARLASPYCLEGMDIYSTVLYHLKEDMKLSYLAQELISTDRLAPQSWCAMGNCYSLQKDHETALKNFLRAVQLNPRFAYAHTLCGHEYTTLEDFENGMKSYQNALRVDTRHYNAWYGLGMIYLRQEKLEFSEHHFRMAFLINPSSSVIMSYLGTSLHALKRSEEALEIMEQAIVADRKNPLPMYQKANILVCLERLDEALEVLEELKEYAPSESSVYALMGRIYKRRNMHDKAMLHFGLALDMKPPATDVAAIKAAMEKLHVPDEIDESP
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MGGNKRAYYAVARGRNTGIYSTWDEASDQVKGYGGNRYKKFDSYEAAQEFCRTEGSRYSSSSGPYRRSTTSYGYSPYSSSSSNYSARHSDKYRKKISRSYSTEKDIEIFSNDTHEKSIACSDRQVVYADGSSLRNGKKGAVAGCGVFFGNDDPRNISVPLAGEEQTNNRAELQAIILALENTSGDLTIRSDSNYSIKSLTTWLPKWKKNDFKTSNSQPVKNLDLINRASDLMSDRNVSLEYVKGHSTDYGNQQADMLARRGASE
The following text describes a protein:
Function:
Has xylanase, avicelase and cellobiohydrolase activity.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
LYMGTATDNGATAMLNLVESLKYSWVPSTFSGQGAATPYDSNLVK
The following text describes a protein:
Function:
Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) (By similarity). Also binds the mitochondrial proton-transporting ATP synthase complex I and may play a role in the stability of its membrane-bound subassemblies (Probable).
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MLGLRAMLPKGKHFAVVLGNVSRQITLPHNCRCITSASWTRPQQSQPQNFQQNRWLSVKSTKTESDDALQRIYYGTLAPRMKMVKFFSLSTSLAGLAAQPILLEQGMKIGGTGMAVFLCTVGGFFTFVTPLLLHFITKKYVTELHYNPLTEEYTATTISLLLQKIKTTFRPNDVVVPEVPGMFTSFLVNKRPLFVDPALFDDPEHYVKIMGYDKPIDFKLDLTPNPEKSKTSEEKQ
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
Subcellular Localization:
Cytoplasm.
Sequence:
MVRLSPKDFIAQLDKLYGSAHGSVYITYKHFTGKYSVKKSGKGPIKTLPGVPEAGASMLLVRATDGNKIKISAIVSAHDVVSFQISLDKVMRKNMTGFKKDTPAPAKKAN
The following text describes a protein:
Function:
Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates. D,L-3-hydroxybutyrate, L-lactate, ethanol, L-malate and D,L-isocitrate are not substrates. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.
Subcellular Localization:
Cytoplasm.
Sequence:
MSFVTEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEECVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGNAGMRHFMAQFGPALQLPWTYLPAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIRETKARHGFAFAE
The following text describes a protein:
Function:
Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Sequence:
MSSSTTPAALKAAILIVSTTAAQDPATDSADVTLRQVFDEQQAQWEVHESKIVPDDVVQIQKQIIHWTNQATAASGDNNNNNNTNTINLIVTTGGTGFAVSDQTTEAVSALLHKNAPGLVHGMLAASLQVTPFAMMSRPVAGVRNGTVIVALPGSPKGAKENLQAVIKMLPHACMQAAGANSRALHKGGVKKLEQEAGVEGGGGRGHGHGHGHGHGHKHHDHGEHRGGGGGGCGAHGHGHNHGHGPGHGHAGLVRHTIPSENPKSNDPSLGPSRRHRESPYPMLSVSEALSQIAQHTPMPQIVTSKVDSSLIGAVLAQDVSARENVPAFRASIVDGYAVVVPQDGNMRGVFPVVSVSHAAPGDGEKMPTLKEGEIARITTGAPLPPGATSVIMVEDTVLVSTTSSKTEDAEDGKGVEEEKEVEILAADKVREGENVREVGSDIKQGQLILGKGDQVSAVGGEIGLLAAVGVGEVQVYRRPVVGVLSTGDEIVDHDRPGDLRLGEVRDTNRPTLISAARDWGYEVIDLGVARDKAGTLEETLRQALRQVDVVITTGGVSMGELDLLKPTIERSLGGTIRFGRVAMKPGKPTTFATVPVKDNDGERVSKVIFSLPGNPASALVTFHLFVLPSLHQMSGVSPPGLPKVPVTLGHDFSLDRSRPEYHRAIVSVSRDGVLTAVSTGGQRSSRVGSMKGANALLCMPCGPEPLRKGAKVEALLMGGLRSDVI
The following text describes a protein:
Function:
Functions as an E3 ubiquitin ligase.
Sequence:
MSSSSGVNLENYLIPLEEIKRATENFSQQRCIGGGGFGAVYKGQLSERWQNRTAAIKQLGQDSHQGEREFRNELEMISKFHHENIISFIGYCDEGNEMIIVYEYAMNGSLDHHLQDPHKIRCITWTERLMICIGAAKGLSYLHSGLGEHNRVIHRDVKSANILLDNNLVAKVCDFGLSKNGPRNQPDTQLYTRVAGTQFYMDPTYHESRILRKESDVYSFGVVLFEILCGMLVYHEKRFGGDGKQFLMTSVRRYYKKEPHKVIDPHIMEQIDSGAFDAFKEIAYQCISFNSIERPTMEKVVERIEEALTIQTNKRSACTPEVRSWIESAIHKLKSSSSYEQRMGAYEMNLLAKRNNDNRVAIAYAGVIPLLKNLLKSPDSQEQAVTTLLILSSHDNNKFIIVSSGAVPGIIHVLREGNMAAREDAAATLFSLSLIDENKVTIGSAEAIPPLVLLLREGTQKGKRDATTALFNLCIYQGNTIRAVRAGVVPVLIELVREPQGVLKDELLGVLFVLSTHPEGILAIGKAEAVPVLVEVIGSGSLKLKETAATVLGKLCFGDQKYLVEAQELGVVEKLKDLMYHGTDRGKRIVGQLLEKMTI
The following text describes a protein:
Function:
Catalyzes the asymmetric hydrolysis of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield AMP and ATP. Exhibits decapping activity towards FAD-capped RNAs and dpCoA-capped RNAs in vitro.
Sequence:
MALRAGGLIVFRRLAQAVPDTIQFLLLQTSYGEHHWTPPKGHVDPGEDDMTAALRETEEEAGLGPAQLRLVDGYRRELRYEVRGRAKTVVYWLAELRDPGAAVRLSREHQDYRWLGLEQACRLAGHTDMQDALRAAHHFLSTDVHKYRDL
The following text describes a protein:
Function:
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome; Forms part of the polypeptide exit tunnel.
Sequence:
MSKAIVLDSHLKEKGSVELPKRYESINSHNLYLYVKHYLSSARANTAKSKNRAEVSGGGRKPWAQKGGGRARAGSITSPVFVGGGVSHGATNNRNYNLKINKKQKRLALEYALEEKAQANKLFVVEKIAIKGVVEDNKRKHLTKEANQMFQALEQRDTLFVCMNMDEYTELAFSNLKKCLIVDVSELNAYLLAAFSSVVMEEAAFQHVVQDKTEE
The following text describes a protein:
Function:
Required for late and very late gene expression.
Sequence:
MAPCKYTPERVQMMWDAIAYNDSRRLAFMTDRPRWVHAHNFFDSAAQLFAYIVKNSISDVHVKPLEEGGREWVIDADFKDCADKAELMLKVNVGATAFMLFFEGKEDAVQRIMFSGNRGFHLWLKFCGKFKMDAPKSLREHWFNVFKQPAKLVSGDIRPGSFADCVRRAVHMYIGDAREDLVLRYWPDVDRDVFCNANKQIRAPFSYNYKGGDYSRCLTQQLQQRIKACSAGCLAGGTPPTSK
The following text describes a protein:
Function:
Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine. Attaches to the host inner membrane most likely through interaction with host yidC and forms together with chaperone gp40 an initiator complex to form the prohead.
Subcellular Localization:
Virion. Host cell inner membrane. Note=Located at a unique 5-fold vertex of the icosahedral capsid. Localization at the inner host membrane is likely due to interactions with host membrane proteins such as yidC.
Sequence:
MKFNVLSLFAPWAKMDERNFKDQEKEDLVSITAPKLDDGAREFEVSSNEAASPYNAAFQTIFGSYEPGMKTTRELIDTYRNLMNNYEVDNAVSEIVSDAIVYEDDTEVVALNLDKSKFSPKIKNMMLDEFSDVLNHLSFQRKGSDHFRRWYVDSRIFFHKIIDPKRPKEGIKELRRLDPRQVQYVREIITETEAGTKIVKGYKEYFIYDTAHESYACDGRMYEAGTKIKIPKAAVVYAHSGLVDCCGKNIIGYLHRAVKPANQLKLLEDAVVIYRITRAPDRRVWYVDTGNMPARKAAEHMQHVMNTMKNRVVYDASTGKIKNQQHNMSMTEDYWLQRRDGKAVTEVDTLPGADNTGNMEDIRWFRQALYMALRVPLSRIPQDQQGGVMFDSGTSITRDELTFAKFIRELQHKFEEVFLDPLKTNLLLKGIITEDEWNDEINNIKIEFHRDSYFAELKEAEILERRINMLTMAEPFIGKYISHRTAMKDILQMTDEEIEQEAKQIEEESKEARFQDPDQEQEDF