lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm. Nucleus speckle. Chromosome. Note=Shuttles between the nucleus and the cytoplasm (By similarity). KAT5/TIP60 inhibits its nuclear translocation (By similarity). Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity). Preferentially localizes across the entire gene coding region (By similarity). During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorylated POLR2A/RNA polymerase II and helicase DDX23 (By similarity).
Sequence:
MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS
The following text describes a protein:
Function:
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
Domain:
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence:
MSLPEPYYNDDKSSFAYPTVRKRWPTIIDGAIEDVQQTIENHQEEASIGHKIIQQLLNTKEDFVNDAIVRPFTDEEITINPHLKHYNESLENLNKIKPVTWQTGPWLYLECYLYQYINNFFIVNTNEFWNHYDVFQNLKDKTFKQSELGVLELCKRYETLSKQLDQANDEVLHLLFKEFIDISLWGNATDLSLLAGNVTLEDIKSVQGAEVRKKNEEKILVNDLSQAWKQLHNDGNDSGTKRVDIVLDNSGFELFADLILTLFLLDSKLVQEVHLHCKEIPWFVSDTMPKDFQDLLNQLVDPEFYPQIHSDEPSSIKLVHDKIQHYYDKHALIINHDPFWTLDYNYWYIPKFDSLYSELQHSNLIIFKGDLNYRKLTGDLQWPKTTPFKTAIQELSTSNLPVLSLRTCKADVVVGLPEGVNEKLIKEYENMGNENGQLWSSSGKWAVISFNK
The following text describes a protein:
Function:
Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Sequence:
MPKHVFSVDMTCGSCAEAVSRVLDKLGGVKYDIDLPNKKICIESEHSVDTLLATLKKTGKTVSYLGLE
The following text describes a protein:
Function:
Required for arbuscular mycorrhiza (AM) development during AM symbiosis with AM fungi (e.g. Glomeromycota intraradices).
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MAIKSIIPATYFLLFLHLLLPLASCIKTKQVYVVELFGDHTSDDKTLHEVENSHHSYLLSVKETEEEARASLLYSYKHSINGFAALLTPKEASKLSEMEGVVFVHKNQPKIYSLHTTRSWNFVGLDGPLNPWEEESDHTDGNLLARAQYGKDIIVGMIDSGVWPDSKSFSDEGMEPVPTKWKGVCQNGTAFDSSQCNRKIIGARYYLHGYQSAFGPLNEKEDYKSARDKDGHGSHTASIVAGRVVPNASAIGGFAKGTALGGAPLARLAIYKACWPIKGKSKHEGNICTNIDMLKAIDDAIGDGVDVLSISIGFSAPISYEEDVIARGALHAVRKNIVVVCSAGNSGPLPQTLSNPAPWIITVAASTVDRSFHAPIKLSNGTIIEGRSITPLHMGNSFYPLVLARDVEHPGLPSNNSGFCLDNTLQPNKARGKIVLCMRGQGERLKKGLEVQRAGGVGFILGNNKLNGKDVPSDPHFIPATGVSYENSLKLIQYVHSTPNPMAQILPGTTVLETKPAPSMASFSSRGPNIVDPNILKPDITAPGVDILAAWTAEDGPTRMTFNDKRVVKYNIFSGTSMSCPHVAAAAVLLKAIHPTWSTAAIRSALMTTAMTTDNTGHPLTDETGNPATPFAMGSGHFNPKRAADPGLVYDASYMGYLLYTCNLGVTQNFNITYNCPKSFLEPFELNYPSIQIHRLYYTKTIKRTVTNVGRGRSVYKFSAVSPKEYSITATPNILKFNHVGQKINFAITVTANWSQIPTKHGPDKYYFGWYAWTHQHHIVRSPVAVSFP
The following text describes a protein:
Function:
Probably involved in exporting SapB from the cell (Probable). Expression of the ram locus (ramA, ramB and ramR) induces rapid aerial mycelium formation in S.lividans.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTSTEAGALRRLAPPARRFLAHRKGVLVRLALWSLAESGQAFLVGHAVARSVDEGFLAGDPRRGLLWLGVALVAVLSGARVVRGVFAQLAGVTEPLRDGLVRHAVDRSMARAAPGGPGGTDRAAVSRLTNQVEIARDSFAGLVLTLRSFVFTAAGALLGLLSLHPALLVVVLPPLAAGLALFLVTLRPMAAAQRRALAADEALGEHAASARAALRDLTACGTGPGAERHGADLVADAAAAARTLAGWAAVRTAALGVAGHLPVLALLVAVEWLRGHGVSVGALLGAFTYLVQSLLPALHTLMTALGAAGSRLLVVLDRILGPEPEPEPEPEPEPEPELGSGLEPEPEPASEPESGPSTASASAAAFAVHTAAAPAVELRSVTLSYGVRAEPVLDALDLRVAPGEHLAVVGPSGIGKSTLTRLVAGTLAPSRGEVRVAGRVVTGRPAAELAALRVLVPQDAYVFSGTVGDNLAYLRTDPSPAELDAAVEAFGLAPLVERLGGLDATVRPAELSPGERQLVALVRAYLSPAPLLLLDEATCHLDPASEARAEKALAGRSGTLVVVAHRLSSAVRADRTLVLDGIRAQSGTHAELLGRSPLYRDLTGHWNS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Domain:
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MSNTVRAISPDITLFNKTLTFQEISQNTREAVIYIHGGAWNDPENTPNDFNQLANTIKSMDTESTVCQYSIEYRLSPEITNPRNLYDAVSNITRLVKEKGLTNINMVGHSVGATFIWQILAALKDPQEKMSEAQLQMLGLLQIVKRVFLLDGIYSLKELLVEYPEYDCFTRLAFPDGIQMYEEEPSRVMPYVKKALSRFSIDMHLVHSYSDELLTLRQTNCLISCLQDYQLSFKLYLDDLGLHNDVYKNGKVAKYIFDNIC
The following text describes a protein:
Function:
Cation/chloride cotransporter that mediates potassium-chloride and sodium-chloride cotransports. Involved in plant development and Cl(-) homeostasis. May be involved in long distance Cl(-) transport. Does not function as an H(+)-dependent cotransporter.
Miscellaneous:
MISCELLANEOUS: Cotransport is inhibited by the loop diuretic bumetanide.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDSGDIEEAGGNGEEEFRSGPRLGGSKYRPVVAHDRAVVEMSSIDPGSSSSTLKNIKVVAPGDVGAGVRGPEDGVNGHQKESKLELFGFDSLVNILGLKSMTGEQIQAPSSPRDGEDISITQGHPKPPALKMGTMMGVFVPCLQNILGIIYYIRFTWIVGMAGIGQGLVLVFLCGLCTFLTTISLSAIATNGAMKGGGPYYLIGRALGPEVGISIGLCFFLGNAVAGALYVLGAVETFLKAFPAAGIFRETITKVNGTAVSESIQSPNSHDLQVYGIVVTILLCFIVFGGVKMINRVAPAFLVPVLLSIFCIFIGIFLAKTDDPDNGITGLRLKSFKDNWGSAYQMTNDAGIPDPTGGTYWSFNELVGLFFPAVTGIMAGSNRSASLKDTQKSIPVGTLAATLTTTSLYLISVLFFGAVATRDKLLTDRLLTATIAWPFPAIVHVGIILSTLGAALQSLTGAPRLLAAIANDDILPILNYFKVADTSEPHIATLFTAFICIGCVVIGNLDLITPTVTMFYLLCYSGVNLSCFLLDLLDAPSWRPRWKYHHWSLSFVGASLCIVIMFLISWSFTVVAIALASLIYKYVGLKGKAGDWGDGFKSAYFQLALRSLRSLGANQVHPKNWYPIPLVFCRPWGQLPENVPCHPKLADFANCMKKKGRGMSIFVSILDGDYYECAEEAKEACKQLATYIEYKRCEGVAEIVVAPNMTEGFRGIIQTMGLGNLKPNIVVMRYPEIWRRENLTEIPSTFVGIINDCITANKAVVIIKGLDEWPNEYQRQYGTIDLYWIVRDGGLMLLLSQLLLTKESFESCKIQLFCIAEEDSDAEALKADVKKFLYDLRMHAEVIVVTMKSWDIRSEGNSQEDSLEAFDAAQRRISDYLGEIKRQGSNPLLANGKPMVVNEQQVEKFLYTMLKLNSTILSYSRMAAVVLVSLPPPPLNHPAYFYMEYMDLLVENVPRMLIVRGYHRDVVTLFT
The following text describes a protein:
Function:
Sodium-dependent amino acid transporter that mediates the uptake of the L-enantiomers of various amino acids, including L-proline and L-methionine, and also of acidic amino acids such as L-glutamic acid and L-aspartic acid (Probable). May additionally have a role in potassium-dependent amino acid absorption. In response to the availability of amino acid nutrients, may play a role in dauer formation. May play a role in promoting fertility.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MADSGSNEEAMKRQAPSVKFDSPSKPDPQQVSQQSNQLSSQKSIQQSTQSKIDPSRIDTKNTTVTTTRPTLDTPPEEEEEKRDGFGNSFEFVLTSLGLAVGLGNIWRFPTRAYNNGGSAFLIPYLTCAFLFGLPAVYFEFLTGQYQGKSPPVIFRRVRPILEGVGWMGVFVAALVAIYYIVIVSWISIYMINICRGHFALWSHCNNDWNNGTSCITMADQYLCKNHTKVMANSTLWNSSLPIPDKMVYFNGACQDANGTDVSTATEQYFMTYIVQPSSGMLDFGGFNWPVFAAMSVCWLLTGLGILKGAKIMGKISYVSVLVPYVLVVVLFINGVFQDGSGVGLEMYFGTPNYTKLYEQDTWTEALKQLCFSLSVGHGGLISLSSYSPKRNNIFRDALIVIIGDTTMSLVGGGAVFATLGYLAKATGQDVKDVVKSGLSLAFVVYPEAMTRMPVPWLWCFIFFLMLFLLGASTEIALVDVFCSCIYDQYPRFRNRKWIVVIAWCSVLYCIGLVFSTRAGYYWFEMFDEYAAGFSSVCTVVCELLVMMYIYGFRNVRDDITEVVGHARNKFTGAIGAHSWYFTANWMVISPSIALILVGLSFVREYPYMGRHDIYPAVFDIFGWFLSFLPVIIVPIFMLLNFIRCRNRGHSYRTLFMLQKQHASYRRIAANYSKDQLALQDQLPDKEPWDEENVDLTDSESESRNAASGDVPIDDVATIDTSSTYHQVY
The following text describes a protein:
Function:
Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).
Subcellular Localization:
Nucleus.
Sequence:
MQEVSAGLERFTFTFEEDVELQRGTGLLPFQGMDRSGSAVCSFFAKGLCHKAVSILTRPRGDAGVCKPRLRGLCKTGDQCKFPHQYDVTTSPECYFCSKLGFSVDCNKECPFLHVTPDFKNQDCLWFDQDFCKDGEPQQKGALGGTGEQDGAGGGSPAREGCPLGRNGQQPLPQIPQAPCSGTRPAVPGRLLGAGSLGFTSQRLPDLEHTTELLVSSL
The following text describes a protein:
Function:
Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin (By similarity).
Sequence:
MWRPLENTPEVLEPYLQKIGVQDASVFDLFSLEEIPEYIPRPVHALLFVFPSSGTKTIYKGSRILPKDSDKVLWYPQTIPNACGTIGLLHAVSNGELRRKVNENDFIKSLIRTAEGSSIEERAKLIEDSKELEALHAAFAGPPLEVEGSEEDVETDLHFICFVKGKSKDDNHFYELDGRQEGPVQHSEIESDLLNAEVLSVIKNYIQSIDSPFFSLVAITTP
The following text describes a protein:
Function:
Hydrolase highly specific for thiamine triphosphate (ThTP).
Subcellular Localization:
Cytoplasm.
Sequence:
RRAFIEVEQKFIFGPGTAEKLTALGATLQSDHSFRDQYYDALDLRLTLADHWLRHREGAGWELKCPPKPRERNGVPDGISKSPGGSDAPGDNHPLQPLESLGQTHGAVQYLEVTCPQEIVARVCGLLGIDPATVGHENMAQAVEDLGLKGFASFVTRRCQYRLGDLNVDLDQADFGYAVGEVEALVKRQEDIPTALESIQKLGNQLGFDEKTRIPGKMSAYLHQFRPTHYEALTRLGRLRKMGDGVHGQKENNV
The following text describes a protein:
Function:
Probable DNA helicase that may play a role in DNA repair during meiosis.
Subcellular Localization:
Nucleus.
Sequence:
MDSKEADEVKPLAEFLIRHHSEQLRSIVLSSDPKLHYPLYIDFAELMDENPQLAHLVFSQPTEYLRHFDQAALWAHKIVLENLNFGEKGIQKKYIHVRINVCGSPLEYPETFPSIGRVRVKHRGILLTLKGTVIRSGTIKMYEGERMYQCRKCKHEFPVYPELESRNSITLPSFCPSMRSKPCEGMRFDCVDETVIRHDYQEIKIQESTQALGVGAIPRSIPVILKDDLVDIVKAGDDVIVSGILTAKWSPDLKDVRCNLDPVLVANHVRRTNGLKSDINIPNDIIMKFNQFWSDFKDTPLKGRNAILRGICPQIFGLFTVKLAVALTLIGGVQHVDASGTKIRGESHLLLVGDPGTGKSQFLKFAAKLSNRSVITTGLGSTSAGLTVTAVKDGGEWMLEAGALVLADGGLCCIDEFDSMREHDRATIHEAMEQQTISVAKAGLVTTLSTRTIVFGATNPKGQYDPDQTLSVNTALSGPLLSRFDIVLVLLDTKNPEWDAVVSSHILAEGESDNGDSNDDLANIWTLDMLRRYIHYVKGYFRPVLTKEAEKVISSYYQLQRRSATDNAARTTVRMLESLIRLAQAHARLMFRNEVKRLDAIMAILCIESSMTTSAIVDSVGNALHSNFTENPDQEYTKQETLILEKLRSIDEFSDMHIIEELPR
The following text describes a protein:
Function:
Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Sequence:
MSQPGKGKRPAASPRPKRAAAAGAAEAHVYEKSSRIPSKAEEKKKAETSEEKAASHSSKYPSRISTSGMNSSKTSTSSPASVSTLSMNPTETKYQATPINKETKGLHYHNKKKKTPQAKKSGTEEKPQATKATDPPGKDAHGKNSEEDKKQKGPAKQVMATESKDSLAGKETLKPVEQPTPGKPTEGSQNKEKKSQPLSGPVKAESTKPSKESSFSDALDDLVDTLGGPEENKPESPKYSGPQVSDPFSSTYIEELGKRESTIPPEYRHLLDRHEGAAIGPPDSEKQMGADEAIDSLSSGFTCSPAATGKTTDKEKASGGEVLKASSTKPVKSAAPPDEKKRRVEVMHHYPQSSNRGLEDLGKLLADPVPESLPTTPSHIEVIKTPSSSDPIDSLSETLGHPEEEPLQTIPPSEEVDEAKAREERLKKCGEDEDTLPADYQLKPATDKDGKPLLPKPEDKSKPISESKLIDELSKDFESSEPQQKKLESAKKTKDSETPAHAPVKEVVSKTSMCSVQNAPPEPSLRRGIEALGQIFAHPGLEPLPTTHSHIEVIEKEQVSDDAVEALVGSLEKKEIDPEETKPSVDKIKEKSKEEKREKVGEKEETVPPEYRLKAAKGKDGKLLEKKQSEKTSLMSDDDILDALSEGFSCSKAPVTCAEISAAQQKDEGLDDAFDELSKTLGERKPDPDDNKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDNDKDGKPVKPPPKDPKNSKDSGDPIDELSEGFDNCSQIPSSEGTKKSAKKKDEKEASSTKPAKNGGKSKSKEKSSRSKTDGEKTS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Nucleus.
Sequence:
MSTPPQPSFKGQLYCIAAAGQTVPGAPTARRFTVDDFEIGRPLGKGKFGNVYLARLKKNHFIVALKVLFKSQIEKEGLEHQLRREVEIQAHLQHPNILRLYNYFHDARRVYLILEYAPKGELYKALQRSHTFDEQRTATIIEELADALIYCHERKVIHRDIKPENLLLGLMGEVKIADFGWSVHTPSLRRRTTCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGNPPFESASTSETYRRILKVDLRFPPSMSSGARDLISKLLRFQPLERLPLVRVLEHPWIRAHSQRVLPPSVPMAF
The following text describes a protein:
Function:
Probably participates in a plant defense mechanism.
Domain:
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Sequence:
SIPCGESCVWIPCTITALAGCKCKSKVCYN
The following text describes a protein:
Function:
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
Sequence:
MLHNDLYQINMAESYWNDNIHEKMAVFDLYFRKMPFNSGYAVFNGLKRVIDFIEHFGFSESDLEYLKSIGYKDDFLSYLKDLKFTGSIRSMQEGELCFGNEPLLRVEAPLIQAQLIETILLNIVNFHTLITTKASRIRQIASNDKLMEFGTRRAQEIDAALWGARAAYIGGFDSTSNVRAGKLFGIPVSGTHAHAFVQTYGDEYVAFKKYAERHKNCVFLVDTFHTLKSGVPNAIKVAKELGDKINFVGIRLDSGDIAYLSKEARRMLDEAGFTETKIIASNDLDEETITSLKAQGAKVDSWGVGTKLITGYDQPALGAVYKLVAIENEDGSYSDRIKLSNNAEKVTTPGKKNVYRIINKKTGKAEGDYITLENENPYDEQPLKLFHPVHTYKMKFIKSFEAIDLHHNIYENGKLVYQMPTEDESREYLALGLQSIWDENKRFLNPQEYPVDLSKACWDNKHKRIFEVAEHVKEMEEDNE
The following text describes a protein:
Function:
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Subcellular Localization:
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Domain:
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence:
MDYKTKKNSNATVDIKLTFEASDIEKAFDKTYEEKQKNVKIPGFRPGKAPLNMVKRHLGDSVASDAINTLIVDGMTSILSKLEHPMIRFPKFEIQDYQPGKNLIATAIYETNPEITLGKYKKIKIKLPEVSVSDLDVSEEVEKVRKNLARKQLKEEGQAAVAGDIIDMEYTVCEKGQESKNSGNTSNDYHLGHENNLKGFDENLYGMKSGEKKDFVHTFPEDYSQNEVAGKTFEYSVTIKALYANILPAVDDDLASEFDGSESLNVLKDKIRKNLKEGFEDRVKNKKLDEIYKEIIDDSKYVFPESYLREESEHVFHNMIHEFKLPHMTMEKYANMVQKDLKEVQESFQKLAETRLKHYFTRQKIAEIENISYSEQDFDADLEKLASSYQISLSDLKKELEKGKLMEQYRENFFAKKIDNILFDLVEKKYTDKLNIGQIKDYLNQKEEVKA
The following text describes a protein:
Function:
May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (By similarity). Plays a role in apoptosis by tethering caspase ced-3 to the nuclear membrane preventing its autoprocessing in absence of ced-4.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein. Note=Cytoplasmic side of the nuclear pore complex (By similarity). Co-localizes with caspase ced-3 to the perinuclear region in germ cells.
Sequence:
MSNEDVAEDVSQVTDFHFHTCRKFRLFSSKSDGYSQNEINIRNRVATSSQLGVTFVTVNSNQLSCFHTKSLLGYKITRENMNVEVTDLPIKTIRLHGVVLINDMGVNSDGTVLGVLHTKNNDVSVDVFDIKKICTSSSIEPFKPLCTTRVGTEQINQGSCLEWNPAFPDTFAASSTDRSILVAKINVQSPANQKLVGIGKFGAVTTAISWSPKGKQLTIGDSLGKIVQLKPELEVVRSQHGPENKPNYGRITGLCWLATTEWLVSLENGTDQDAYLMRCKKDKPTEWIQFHELSYSSSKWPLPPQLFPATQLLVDWNVVIVGNSKTSEISTVGKRDDWQTWVPVEGESIYLPTTSSGKDTVPIGVAVDRSMTDEVLLNPDGSQRHRPSPLVLCLTNDGILTAHHIISTFAAHIPCQMSSQNLAINDLKKLQFDSQKPISAPPSDQTPVTKPSTVFGQKPEAETLKSSLVGSPSSVQTPKPSSSLFNPKSIASNIETSQLTESKPSTPAAPSSQPKIASTPKSEAIPKISDKTLEHKKAELIATKKQVLIERMDKINDSMAGAKDATMKLSFAVGKVKTTIMECADVVRASLGDSKEVMDELKNLILSIERMSDRTQHTVKEMDFEIDEKMELVAGVEDGNQVLEKLRNMSETEKLMRFNKLETAADLLNGKYEECSDLIKKLRMSLSEKESLRKQAILSPLRLSSNLNQLRSGSETELALKVMRNVSKIIMDTREQIQRTELEFVRFQRDVKFQNFKKGKENLNFTQPLEMSSLDGDAPQGKSLTDAESIKVRQALVNQIQKRGIVKTRNVIVESYKKSENSAAMKNDLLDTSNLSNAILKLSMTPRRVMPSSSLFSASPSTPSTKSDAATQADEPPIVKTVVVTVESPAKPIASAPAVSSPLIKLNTTTATTTMTTPKVTVPKEEANKTQDQKPIISTPASSSIFSSGSLFGTKTQTPLVSKEESTLTTGVPSLINSSLSISPQEIEKASSKVETLNKTEEVKDEKSENEVTPDLKSEEPKSLETKVKEEPKPAVQTPVKEEETGSNIQKTPSFSFNSTTTPKSTSSTSSIFGGGLKTQTPSSSNSTNIFGARTTTTATPTPASNTSSIFGGGSKAASSPFGSFGQAGCQPAKTSNPATSTASVTFSFNTGATSASAKPAGFGSFGAGASAKPSSVFGGSVTAPTVPNVDDGMEDDSMANGGGSGGFMSGLGNARTSNTSGGNNPFAPKTSTGTSASSSSWLFGGGGNQQQQQQQKPSFSFNTAGSSAQQASAPATGTSSVFGGAPKFGSQPAFGAKPFGGGANAGLSKNASIFGGATSSTTNNPATGGFAQFASGQKTSSLFGGGATPQTNTSIFGGGANTTPAPTSSVFGGGASANANKPTSFTSWR
The following text describes a protein:
Function:
Involved in the synthesis of both phthiocerol dimycocerosates (PDIMs) and phenolic glycolipids (PGLs), which are structurally related lipids non-covalently bound to the outer cell wall layer of M.tuberculosis and are important virulence factors. In vitro, TesA has both thioesterase and esterase activities. Exhibits thioesterase activity on acyl-CoA derivatives such as palmitoyl-CoA and decanoyl-CoA. Also displays hydrolytic activity on ester substrates, being more active on pNP esters with short carbon chain lengths (C2-C5) than with those bearing medium and long carbon chain lengths (C8-C18).
Sequence:
MLARHGPRYGGSVNGHSDDSSGDAKQAAPTLYIFPHAGGTAKDYVAFSREFSADVKRIAVQYPGQHDRSGLPPLESIPTLADEIFAMMKPSARIDDPVAFFGHSMGGMLAFEVALRYQSAGHRVLAFFVSACSAPGHIRYKQLQDLSDREMLDLFTRMTGMNPDFFTDDEFFVGALPTLRAVRAIAGYSCPPETKLSCPIYAFIGDKDWIATQDDMDPWRDRTTEEFSIRVFPGDHFYLNDNLPELVSDIEDKTLQWHDRA
The following text describes a protein:
Function:
A potent inhibitor of RNA polymerase (RNAP) probably involved in viral defense. Destabilizes the transcription pre-initiation complex of TBP, TFB, DNA and RNAP, inhibits abortive transcription initiation, productive initiation and transcription elongation. Increases the RNAP KM for NTPs about 50-fold. Overexpression of TFS1-tip4 (TFS1 with the active tip of this protein, phenocopies this protein) in S.acidocaldarius MW001 leads to severe growth inhibition. When bound to RNAP induces conformational changes that widen the DNA-binding channel, probably destabilizing the interaction of DNA with RNAP.
Miscellaneous:
MISCELLANEOUS: Strain 2-2-12 is a substrain of P2 that is highly susceptible to infection by Sulfolobus turreted icosahedral virus 1 (STIV-1).
Domain:
Has 2 zinc-ribbon domains (ZR-N and ZR-C); functionally important residues Lys-76, Lys-77 and Lys-78 are probably located at the tip of a domain that extends from ZR-C into the RNAP active site. The nature of these residues determines if the protein is involved in stalled transcript cleavage and thus activation (Asp and Glu residues in TFS1) or in RNAP inhibition (Lys or Arg residues in this protein TFS4). Increasing numbers of Lys residues lead to an increased ability to inhibit transcription. ZR-N interacts with Rpo1C and Rpo2 while ZR-C binds in the NTP entry funnel to sites in Rpo1N without reaching the active site.
Sequence:
MRFCPKCGSFLKVKGNKMVCSKCGYSDHDVEKVILKENVAHENDKTIIADGETIEGRVAISLCPRCGSVRAILLNKKKRLYRCMTCNFVYNI
The following text describes a protein:
Function:
Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity; The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.
Subcellular Localization:
Mitochondrion. Cytoplasm.
Sequence:
MSPNPVNTASLDAWKTQAFKSDKNRLAQAAISRGNFQDMIIDRSALNKNIGVFNTQIQLEGTPITYQRSSGRCWIFASLNVLRIALQQKLKIPSFQFSQTYLFFYDKLEKSNWFLDNVIDTADEELDSRLVQELLKEPVNDGGQFDMIINLVEKYGLVPLDVFPDSWNSENSRNMCYLITEKLREYALTLRELVKAGKKDEALAMKADFLQEIHTILCITLGTPPAVDEKFTWDFQTRDKVSDDKELEISAKKVETLQLTPKELYELIGIDFKKYFSLINDPRNEYNKRYTVDRLNNVAGGAKAHVDYVNTDISELKKAAIKAIQNNEAVFFGSDVGKFGDRKSGVLDTQAWDYNLGFNTSMKLNKKQRLQTGSSMMTHAMAITAVHLDESGKPVRWRIENSWGKDNGKDGYYQMSDAWFDEYVFQVVTTDKYVEPEVLEILKQEPKVLPLWDPMGALARL
The following text describes a protein:
Function:
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Sequence:
MSFSIPPLSSIGSHNNNKNNNNNNNNNSNNNNSHAPRTSIKKSHKESIIGTNDDAASCKLSAVNVGYYSDPFVKYFVKHPIRRQPLINRGFFSRVECIEQLVSQFFTQYKDINKKQIISLGCGFDTYYFRLMNNKDIKKDFIYFEVDYDQVISNKIKIIQNHKELQSMIDQEWDSKYDTNEKLASMVNHQRVSSKSYRLGSIDLTNLETFKIFDELEIDYNVPTLFLSECVLVYIPTKCGNDVIQWASNKFSESCFITYEQIKPNDEFGRMMIKNIEMKGCPLLSIESFPEIDDQRKRYNNLGWNKTEILDMRHVYSDFINKNRIKETEKLEIFDEFEEWDLIQGHYVYVFAMKSNSPSILDSYYFENSKNK
The following text describes a protein:
Function:
Member of the two-component regulatory system CreC/CreB involved in catabolic regulation. CreC may function as a membrane-associated protein kinase that phosphorylates CreB in response to environmental signals. CreC can also phosphorylate PhoB.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MRIGMRLLLGYFLLVAVAAWFVLAIFVKEVKPGVRRATEGTLIDTATLLAELARPDLLSGDPTHGQLAQAFNQLQHRPFRANIGGINKVRNEYHVYMTDAQGKVLFDSANKAVGQDYSRWNDVWLTLRGQYGARSTLQNPADPESSVMYVAAPIMDGSRLIGVLSVGKPNAAMAPVIKRSERRILWASAILLGIALVIGAGMVWWINRSIARLTRYADSVTDNKPVPLPDLGSSELRKLAQALESMRVKLEGKNYIEQYVYALTHELKSPLAAIRGAAEILREGPPPEVVARFTDNILTQNARMQALVETLLRQARLENRQEVVLTAVDVAALFRRVSEARTVQLAEKKITLHVTPTEVNVAAEPALLEQALGNLLDNAIDFTPESGCITLSAEVDQEHVTLKVLDTGSGIPDYALSRIFERFYSLPRANGQKSSGLGLAFVSEVARLFNGEVTLRNVQEGGVLASLRLHRHFT
The following text describes a protein:
Function:
Potent suppressor of cytokine production that acts as a regulator of innate immune signaling and inflammation. Acts as a key negative regulator of select cytokine and chemokine responses elicited by TRIF-independent Toll-like receptors (TLRs), thereby limiting inflammatory cytokine responses to minor insults (By similarity). Has ribonuclease activity (By similarity).
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Nucleus, PML body. Note=Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies.
Sequence:
MSTTRPLLGMKRITEVTCTEPPGGRQSPTASRAQPDSLTVDEFTVHEDKQTELKCSKPKVEQVFQVTFTIIGLLDHTGAHGSKASRQIWLQLKGKKEDVYKAKEYVKGLCDPELQKEEWYPVDMHCIFAGARGLFLDRLLRDTSAEVQVLEPGRLKLSGCAEAVVMAQSRVQQFVALFQEKRSLPADREPSVKRKFKTFVEDRADKYAMELLLLPSALKEELLGLAQSPTQPIVIIDLEQDRSQTSTPVTDLSNRILDTTFEDKTSPITPEVMPGLNGRPCNKRRSSESEQRDTKRQYSLERREEEQCEEREREPTKTWTVKSAKGTLAASEMTNESEAVSPETNLRCLVNFFRTMGYQQDVVERVVRETGQTEDTFLLLERIVEETQKTQSTQGAQRTSRTPDPSPCANASSTSTSNRLKEKERVQMRALAEIKCKENIRPPSTNGIGQKNQTSSVPLASATLKRNNGAQTDLCEVIIIDDEEDFTETERKPRLTPLDLKPESRFDYLPRGSSQTMVPVRMETVTNLRSSSQGPPLRTSDTRPGCSYQTLPGRAPLPRSEAQYTSKAAPLTGMSRFQQSLRTPYRLILQNEPGSPNLRHIIIDGSNVAMAHGLHRVFSCRGIAIAVEAFWRRGHREITVFVPQWRQKKDPNITEQHFLNQLENLRLLSFTPSREVCGHRISSHDDRFLLHLAEKTGGVIVTNDNLRDFVSQSEAWRRIIHERLLQFTFVEDHFMIPDDPLGKHGPHLDEFLLKDSRGSPIIPPLRTDLRATPSVYSQAAQSTAHPSSPSHWPHSGPPDWHLPRPSPSPPPQRSPSETTELKRKLYDIFPDQKQRIDRILSDNPYMRDLNALSGLLLG
The following text describes a protein:
Function:
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKILLIGYGAMNQRVARLAEEKGHEIVGVIENTPKATTPYQQYQHIADVKGADVAIDFSNPNLLFPLLDEDFHLPLVVATTGEKEKLLNKLDELSQNMPVFFSANMSYGVHALTKILAAAVPLLDDFDIELTEAHHNKKVDAPSGTLEKLYDVIVSLKENVTPVYDRHELNEKRQPQDIGIHSIRGGTIVGEHEVLFAGTDETIQITHRAQSKDIFANGAIQAAERLVNKPNGFYTFDNL