lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Has both DNA primase and DNA helicase activities and may be involved in organelle DNA replication. Capable of producing RNA primers of 9 to 18 bases from a single-stranded DNA template.
Subcellular Localization:
Plastid, chloroplast. Mitochondrion.
Sequence:
MRFLLRLPQIHFRKLSCSMSVLMGSKQFLEFCLLPSFASYPSSPSYSSSRQVSSVSRRFRPVLASRPVSKNSPYYQRTNGLSSYNSIPRVPTPVDTEVEADKRVVLSRLVTLRRKLAEQGVDAENCPPGQHSGLICPTCEGGNSGEKSLSLFIAPDGSSATWNCFRGKCGLKGGVRADGGLASADPIEKVERKITVEGIELEPLCDEIQDYFAARAISRKTLERNRVMQKRIGDEIVIAFTYWQRGELVSCKYRSLTKMFFQERKTRRILYGLDDIEKTSEVIIVEGEIDKLAMEEAGFLNCVSVPDGAPAKVSSKEIPSEDKDTKYKFLWNCNDYLKKASRIVIATDGDGPGQAMAEEIARRLGKERCWRVKWPKKSEDEHFKDANEVLMSKGPHLLKEAILDAEPYPILGLFSFKDFFDEIDAYYDRTHGHEYGVSTGWKNLDNLYSVVPGELTVVTGIPNSGKSEWIDAMLCNLNHSVGWKFALCSMENKVRDHARKLLEKHIKKPFFDADYGRSVQRMSVEEKDEGKKWLNDTFYPIRCEMDSLPSIDWVLERAKAAVLRYGIRGLVIDPYNELDHQRTPRQTETEYVSQMLTKIKRFSQHHSCHVWFVAHPKQLQHWDGGAPNLYDISGSAHFINKCDNGIIVHRNRDENAGPLDLVQIGVRKVRNKVAGQIGDAYLCYDRTTGSYSDSPVTPGMPERRSPKRY
The following text describes a protein:
Function:
Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction. Instead, promotes autophagy by interacting with TUFM and subsequently recruiting the autophagy-related proteins ATG5 and ATG12. Also regulates MAVS-dependent NLRP3 inflammasome activation to attenuate apoptosis. Has no inhibitory function on NF-kappa-B signaling pathway, but enhances NF-kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species. Regulates viral mediated-inflammation and energy metabolism in a sex-dependent manner (By similarity). In females, prevents uncontrolled inflammation and energy metabolism and thus, may contribute to the sex differences observed in infectious and inflammatory diseases (By similarity).
Subcellular Localization:
Mitochondrion outer membrane.
Domain:
The LRRCT domain mediates homodimerization and LRRNT mediates trimerization of the dimers.
Sequence:
MRWGHHLPRASWGSGFRRALQRPDDRIPFLIHWSWPLQGERPFGPPRAFIRHHGSSVDSAPPPGRHGRLFPSASATEAIQRHRRNLAEWFSRLPREERQFGPTFALDTVHVDPVIRESTPDELLRPPAELALEHQPPQAGLPPLALSQLFNPDACGRRVQTVVLYGTVGTGKSTLVRKMVLDWCYGRLPAFELLIPFSCEDLSSLGPAPASLCQLVAQRYTPLKEVLPLMAAAGSHLLFVLHGLEHLNLDFRLAGTGLCSDPEEPQEPAAIIVNLLRKYMLPQASILVTTRPSAIGRIPSKYVGRYGEICGFSDTNLQKLYFQLRLNQPYCGYAVGGSGVSATPAQRDHLVQMLSRNLEGHHQIAAACFLPSYCWLVCATLHFLHAPTPAGQTLTSIYTSFLRLNFSGETLDSTDPSNLSLMAYAARTMGKLAYEGVSSRKTYFSEEDVCGCLEAGIRTEEEFQLLHIFRRDALRFFLAPCVEPGRAGTFVFTVPAMQEYLAALYIVLGLRKTTLQKVGKEVAELVGRVGEDVSLVLGIMAKLLPLRALPLLFNLIKVVPRVFGRMVGKSREAVAQAMVLEMFREEDYYNDDVLDQMGASILGVEGPRRHPDEPPEDEVFELFPMFMGGLLSAHNRAVLAQLGCPIKNLDALENAQAIKKKLGKLGRQVLPPSELLDHLFFHYEFQNQRFSAEVLSSLRQLNLAGVRMTPVKCTVVAAVLGSGRHALDEVNLASCQLDPAGLRTLLPVFLRARKLGLQLNSLGPEACKDLRDLLLHDQCQITTLRLSNNPLTAAGVAVLMEGLAGNTSVTHLSLLHTGLGDEGLELLAAQLDRNRQLQELNVAYNGAGDTAALALARAAREHPSLELLHLYFNELSSEGRQVLRDLGGAAEGGARVVVSLTEGTAVSEYWSVILSEVQRNLNSWDRARVQRHLELLLRDLEDSRGATLNPWRKAQLLRVEGEVRALLEQLGSSGS
The following text describes a protein:
Function:
Catalyzes the phosphorylation of a wide range of nucleosides to yield nucleoside monophosphates. Shows the highest activity for inosine, guanosine and cytidine, but very poor kinase activity with adenosine, thymidine, uridine and xanthosine. ATP is the best phosphate donor, but can also use ITP and GTP. Shows extremely low activity with fructose-6-phosphate.
Sequence:
MGGKMEKITCVGHTALDYIFNVEKFPEPNTSIQIPSARKYYGGAAANTAVGIKKLGVNSELLSCVGYDFKNSGYERYLKNLDINISKLYYSEEEETPKAWIFTDKDNNQITFFLWGAAKHYKELNPPNFNTEIVHIATGDPEFNLKCAKKAYGNNLVSFDPGQDLPQYSKEMLLEIIEHTNFLFMNKHEFERASNLLNFEIDDYLERVDALIVTKGSKGSVIYTKDKKIEIPCIKAGKVIDPTGAGDSYRAGFLSAYVKGYDLEKCGLIGAATASFVVEAKGCQTNLPTWDKVVERLEKHRI
The following text describes a protein:
Function:
Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MMKNLNGRTHNACYQPYYQQQLQLQQQHQQQQQLQQQQQLLQQQQQLQLPYAAPYNQLQQQQYTQQQYYQQQLQQQQQQQQQQQQQLLRQQQPTLSVYQQQQHAKQSYGHNNSNNNANMTQTARSNMQTASIATVSANGNNSSSSSSNANAANSATAAMAAMCQMQSFLSQQQQQQQQQQQQQQQQQQQQYHNNCAHINYNQQQQQQQQQLQQQQLSTAATTNGDKLALDNASEIANFLASELFMQQLVTFDGMQSAPTLTTPTLTPTTLRTIEETIYELTTEPQIVPFQAGFKPPPLTSLGAITNNNTVTPTTAAAAAAATLAVVNANPINANPQFDLLGLNCNSVRGSDTEDSNGSWNDGQLNDDQSTTDTSSAATDSTSYQNGGHMLGNGSNGGVNNFTVALAAVNNAGRASGQAGGNSTTSNSGTPARRGGGRRPNKAANMSPEEEEKRRIRRERNKLAAARCRKRRVDQTNELTEEVDALIKKGEDMKKEIENLNATKNQLEYVLQAHRPTCQKVRNDLLSVVTCNGLIAPTTLLSAGSCTGTGSQHSNNNNNNSSNNNNSNSSNNNNNNSNSNDSSSGGTITGFDATLNSTGRSNSPLDLKPVLTDEQLLQHIKNEPQDVGLDSSSSLDQDGPPPAKRCFALPNIAALTASLTTPTDPGSCSLNTPITSTAPNIFANFGGDLNSPTLNALNKLPKARPNTLNVQQLQRPFVVQQLGNDGNKAPPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPTCSSQNKHPLELPTPTSEPSKLVSL
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MALDSAIELVSQRSTSTSANNSYIFTGKRSEIDQYLQAVDIIQHSIASGSAHDHNTAKSAIQIAMPVLVNEMHNLLNINNNKSTHNPDSTTYSSTMSDTGSNSYIDDYEYRSTFSVTVINDIQSILKRMNAAGYMEDCKKAYVSNRKRCIDDSYQKLDVQKLSSNDARTMEWHTLELVIKVWMKSAKICFRKILPYEKHLCEIIFGDDMDDDCFIEMSSGCAIELLEIATSLSCVRIASDRLFRILELYKTFTDLLPEMNKMFNAQSSESFRTKAGQMVPKLAGVACMIVEKFEKDLFSADLSQHAPVDKIHSLCRYVMDYVYKLGQNKQTLMELSLSKPPLTPSVEMNFTVVEPQLQSKLPFHVIT
The following text describes a protein:
Function:
In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape.
Subcellular Localization:
Nucleus.
Sequence:
MVKAHKGVLVTCDPAAKQLILKLNDQPDHQISEFGLVTPFIIQELDDTHLMVTQECVNALKKQLEAELEKNTFTLDSL
The following text describes a protein:
Function:
Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Subcellular Localization:
Peroxisome matrix. Cytoplasm, cytosol. Nucleus.
Domain:
Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Sequence:
MTHNTMLQRFNGLLEPTHLYIVSVVAYSACNRPDKISGIAKEAMEHVGPSIYPKLREALVKSSPLVGFPRTINSLREMTTNIPPPFPDEFARAADADIDTGKRGKIYFEKTYGKVTQRVLRSMQSSSLDLANIALDYAYGKVLSFNEVVSPLETSLMIIAALVPQDVNPQLRGHLKGALNHGATKEQVMSARNIALEISKECGIQFKGDIETL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase involved in translation quality control. Involved in the rescue of stalled ribosomes by promoting ubiquitination and degradation of proteins on stalled ribosomes. Specifically required to resolve RNA-protein cross-links caused by reactive aldehydes, which trigger translation stress by stalling ribosomes: acts by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, leading to their degradation. Interacts with the translation termination factors eRF1 (SUP45) and eRF3 (SUP35); overexpression decreases the efficiency of translation termination.
Miscellaneous:
MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
Domain:
Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.
Sequence:
MALTQFENDLEILRDMYPELEMKSVKVEEEGEFPQRINGKLLFKISLLADVNIEFGEQHMLLSNLSNECVEFTIYSCHYPDIRRCVVMDIKSLWISTDEKKMLIDKALRLVEETVDMSIEFADSFTSILILIFGFLIDDTAILLFPNGIRKCLTQDQYDLFKQISEEATLQKVSRSNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKCGKKVSLSTDIIEEYLDDTVTSYERKRKLEAKYGRRVLELEVNDYLAEKMLDLAIKKEGSNLQRCPKCKVVVERSEGCNKMKCEVCGTLFCFICGVLLYPEDPYEHFREAYSGCYGRLFEGMPGTET
The following text describes a protein:
Function:
Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts. Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step.
Sequence:
MKKSQVKALLATKQQVQGHYQKQNQNPIQRPQSNLNKPHDLQLYGCLLKTLTHQTPPTPANLQSSIFNLRHTISASKSQNMSDEEHQFESKADAGASKTFPQQAGTIRKNGYIVIKNRACKVVEVSTSKTGKHGHAKCHFVAIDIFNGKKLEDIVPSSHNCDVPHVNRTDYQLIDISEDGFVSLLTESGGTKDDLKLPTDDSLLTQIKDGFNEGKDLVVTVMSAMGEEQICALKDIGPK
The following text describes a protein:
Function:
Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome. Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVGPAPSGPLLPLQSPVTIWMTTWGRSSSQPARDVIRSSLPSPAPPPGGPFGTSSNGPETPARVGLFLTLVFWSCVCCVCVCVCVSLSLIMGRSRRTGAHRAHSLARQMKAKKRRPDLDEIHRELRPQALPRPKRERDAEPDPDLPGGGLHRCLACARYFIDSANLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVQPQRLGVPTEVSTEIPEMDTST
The following text describes a protein:
Function:
Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
Sequence:
MGNASSSVHMQRERHKSTDLSTPSSPAHFRDSIGGGGAGQGGSAGAAALGAAAGAVGAAGGGGGGGGGQAFSFDKKHTAVLNEGSSQEDDDPYYTGTGTGSTRRGTAHDDATSAVTRDHSSMDNNEEEEEAAVGAEPATGSQLTGDEDDIRKTALPTVLRWDGGGKNVTISGTFSDWKPMAMVRSHQNFVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSVRESDFEVFQALAKDSENVTNYAEKEYSQEVPQVKPWEKVSGPPVLPPHLLQVILNKDTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLSATHRYRKKYVTTLLYKPI
The following text describes a protein:
Function:
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MGRASKDKRDIYYRKAKEEGYRARSAYKLLQIHEEFNILDPAEIRTGAVDLCAAPGSWSQVLAQHFKMISANLTAASEGDSLPAQTPRVVAVDLQEMAPIDGVTLLQGDITSEVTAREIIRLLNAPTSTGVVRTDDEQQQPQPASSSFSSSAPSPALGASPRKADIVLCDGAPDVTGMHELDEYLQHHLLLAALHITTFVLRAGGCFLTKIFRGPNTAFLVAKSQLFFQQVRVVKPKSSRNASMESFLLCQGFRMPLGYVPRFVGAAAPAAASSATTGCSRGAASASAGCGSRVEADNEEGVKGERSETAIGSGGPLRASGFTPEAPLYCYDTTASFSHASDGGAAAAATVHDVAHHNQRTSCTLADGVLAPFLSCGDLSGFDADMCYDRDEDADVLEPVQPPLQAPYLAAAAASPSQLAGVADGRDTEADASQKKKIRVESPTAIAGRDSSTGGEEQQ
The following text describes a protein:
Function:
Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
Subcellular Localization:
Cytoplasm, Stress granule. Nucleus, nucleolus.
Sequence:
MKNTMEEIKKNLDSLNSRVDNTEERISNLEDKNIEMLQTEEENELRLKRNEETLQELSGSIRRCNIRIIGIPEGEEKEKGAESLFKEIMAKNFPNLGREMELHVTEANKSPNFINVRRPIPRHTVVKLAKVNNKEKILRAARQKKITYKGTPIRLSADFSTDTL
The following text describes a protein:
Function:
Permease involved in the transport of the cationic amino acids.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MGGHEGFSNQRLSSATWFSHFRASALRSKSLPPPSSQTAVRSTSGDSLVRRLGLFDLILLGVGASIGAGVFVVTGTVARDAGPGVTISFLLAGASCVLNALCYAELSSRFPAVVGGAYMYSYSAFNEITAFLVFVQLMLDYHIGAASISRSLASYAVALLELFPALKGSIPLWMGSGKELLGGLLSLNILAPILLALLTLVLCQGVRESSAVNSVMTATKVVIVLVVICAGAFEIDVANWSPFAPNGFKAVLTGATVVFFSYVGFDAVANSAEESKNPQRDLPIGIMGSLLVCISLYIGVCLVLTGMVPFSLLSEDAPLAEAFSSKGMKFVSILISIGAVAGLTTTLLVGLYVQSRLYLGLGRDGLLPSIFSRIHPTLHTPLHSQIWCGIVAGVLAGIFNVHSLSHILSVGTLTGYSVVAACVVALRLNDKKDRESSNRWTSSWQEGVICLVIIACSGFGAGVFYRFSASVIFILLSVGVAVVASAVLHYRQAYALPLGSGFSCPGVPIVPSVCIFFNIFLFAQLHYEAWIRFVVVSVLATAVYALYGQYHADPSMLDYQRAPETESDA
The following text describes a protein:
Function:
Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 36 copies/encapsulin nanocompartment.
Subcellular Localization:
Encapsulin nanocompartment. Note=Probably lies against the interior face of the nanocompartment.
Sequence:
MAGPPDSDLDDVARIRLVLARELETINEYEAYARASSNPEVRAFFQHLAAEEKEHVSEAVHMLRMLDSGQNDHFAKPFVPGHFQAAEAPAPATVHVPTPDGPAFSVNGRNGRLPSEPPTSLPPQRLLYGLPAPPPAVESHPLTVGSLRRGGGGSGSGR
The following text describes a protein:
Function:
Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form dichlorochromopyrrolic acid (CPA), the precursor for the six-ring bisindolopyrrolocarbazole scaffold of the rebeccamycin. The hydrogen peroxide is provided together with iminoindolpropanoate by RebO. Due to the instability of indole 3-pyruvate (IPA), which is hydrolyzed in solution and exits in equilibrium with the predominant ketone form of IPA, the concerted functioning of the RebO/RebD system appears to prevent the buildup of significant amounts of IPA and its imine in solution, effectively shepherding the imine further down the biosynthetic chain.
Sequence:
MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGTTAAGERIVVSREREVTVHVDDASVFLEHPRGPGDSDQDAEIAVRTYVRGEPAAATIHIGQYFNPRAFPLDEHATAASATPEDLDVVALCVDGTRWSRHCVISTDENGDGRFLLRGARPGATRLLLSAEGATPFDGLTAAAAYDNDDSLGLWSGLASVAVRVLPDHWWMDDIPRDKVTFDLLYREVFAFYELLYSFMGEEVFSLADRFRVETHPRLIWQMCDPRNRAKTYYMPPTRDLTGPQARLLLAYLRAQNSDVVVPVIEPSHTRSGTPISTRTDLVRALRHGVAIELAVMLQYLYAAFSIPTHGAGQELVSRGDWTPEQLRLMCGDGGETTDGGVRGSLLGVAREEMIHFLVVNNVLMAVGEPFHVPDLDFGTINDTLMVPLDFSLEALGLGSVQRFIQIEQPEGLTGAVRLGDLPVPVREAEDFHYASLSELYGDIREGLQRVPGLFLVERGRGGGEHHLFLRESVNAVHPDYQLEVDDLSSALFAIDFVTEQGEGHVLTDEDTGEESHYDTFVRVADLLMKERLTAADTRRAQWSPAYPVARNPTVHGGGQSKELVTSPVARELMVLFNKSYFMMLQLMVQHFGGSPDASLRRSKLMNAAIDVMTGVMRPLAELLVTVPSGRHGRTAGPSFELDEKPAFIPRADVARRAISLRFRHLAESARTCALVPDKVVRNLDFLADQFATEGPR
The following text describes a protein:
Function:
Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.
Sequence:
LVTEIADTDNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALNDETSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSNRACDPLSGLTKNECGSDFAYFYFVSFIFLCSFLMLNLFVAVI
The following text describes a protein:
Function:
Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
Subcellular Localization:
Nucleus.
Sequence:
MSDAAVDNSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDNDVDTKKQKTDKDD
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MKTIHFDMNKYETHVDLEYLKEHGRVEKISDGVIFCSGLENAALHQAVLIDERHRGVILELNEEFVGIGLIDKTNDILEGMHVGVSGKFIEVDLFEEMAGRIIDTTGKMLYEESEEKPTATSPLFCVTPAIMTIDSVTRPLNTGLAVIDSITPIGRGQRQLILGNRQSGKTQIAVDTIINQHDQNVHCIYVAIGLKAAYIAEVIETLRNHGAMEYSTVVATAASDSLTAQYLTPYAGMALAEALRDQGKDVLIILDDLTKHADAYRAITLLFNRPPGREAYPGDSFYIHSSLLERAVQMNEEHGGGSITAIPMIETLSDDVTAYIPTNVISITDGQLFLKSDLFNRGQKPAVDVGVSVSRIGGDAQHPIIRKLSKNLTLILSQFEELKELLDFGNALDDGSMKMVSDGRLLTELFKQKILSPLSVTELIVILYAFQNGFLTKIPPANIQTFKGLLLEKAHMHKDFESFSAQIEAINELNESHVEMLEEIIRETGRLFS
The following text describes a protein:
Function:
Metalloprotease.
Sequence:
MRCSAALFLIGIFAVSLAAPVAEDPAPDEEPDRSEESESVEMEMLDPPEAPEPGDGEEYEGETDDDSEMYEPPPPPPEDEWEEDEEEESWDERWDAEGNLEEPVSSDDSEPPQEEDEEEPQPEGRSAVFPSAEEEGNSTEVDEEGSGDNLVPLPIGIELPPDPEFNSNYTIDETPPVDGNSTDEDGPSVLDSIIEINQNAGLFNGIPDGRSVCPEFECELSCMFGYETAEDGCPMCSCVPDGEEKLFEGDITLNADTKEYLRKVIDSDGRGASRRPLWTGRTVPYTFNRVVAYNSAKSNAINAAIRQFHSRTCIRFVRRTNQRDYIEFASLGGCFSNVGRNGGRQQVSIGNGCEQVGTVIHEILHALGFWHEQSRPDRDSYVRIQWANIPQSVRYNFQKYTSREVNSLGSAYDIGSVMHYGSYAFSFNRRPTITDTAGRPITTQRRGFSNSDLTQLAALYRCSNTGGGGTGTGGGGTGTGGGGTGTGNGNCVDRNNNCNSWSRQGYCASSRYRQYMQTNCRKACNLCSGTGTGGGGTGTGGGGTGTGGGNCRDSNNNCPSWSRLGYCRTGSYVQWMRTNCRRSCQLCSGGTGTGTRPNPTNNNCRDKSNHCGYWYRTGECTKNPTYMRDNCRKSCRLC
The following text describes a protein:
Function:
Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.
Sequence:
MTETKNMSSSRSSSQTVKASHILVKHQGSRRKASWKDPEGVRIKATSRDSAVQQLLMLKADIVSGKARFEDVASRYSDCSSAKRGGDLGSFGRGKMQKPFEDATFSLKVGEMSDIIDTDSGVHIILRTA
The following text describes a protein:
Function:
Probably part of the binding-protein-dependent transport system YcjNOP. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MATNKRTLSRIGFYCGLALFLIITLFPFFVMLMTSFKGAKEAISLHPTLLPQQWTLEHYVDIFNPMIFPFVDYFRNSLVVSVVSSVVAVFLGILGAYALSRLRFKGRMTINASFYTVYMFSGILLVVPLFKIITALGIYDTEMALIITMVTQTLPTAVFMLKSYFDTIPDEIEEAAMMDGLNRLQIIFRITVPLAMSGLISVFVYCFMVAWNDYLFASIFLSSASNFTLPVGLNALFSTPDYIWGRMMAASLVTALPVVIMYALSERFIKSGLTAGGVKG
The following text describes a protein:
Function:
May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region. In addition, at the cytosolic site, acts as a negative regulator of RcsB. In stationary phase, the FtsH-dependent degradation of YfgM ensures the release of RcsB from YfgM and thereby permits cellular protection by the Rcs phosphorelay system. May coordinate stress responses across the inner membrane via a dynamic protein-protein interaction network inside and outside of the membrane.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein; Periplasmic side.
Domain:
The first 14 N-terminal residues form the YfgM degron, which directs the protein to FtsH for proteolysis.
Sequence:
MEIYENENDQVEAVKRFFAENGKALAVGVILGVGALIGWRYWNSHQVDSARSASLAYQNAVTAVSEGKPDSIPAAEKFAAENKNTYGALASLELAQQFVDKNELEKAAAQLQQGLADTSDENLKAVINLRLARVQVQLKQADAALKTLDTIKGEGWAAIVADLRGEALLSKGDKQGARSAWEAGVKSDVTPALSEMMQMKINNLSI
The following text describes a protein:
Function:
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2.
Sequence:
MSSETVTNNPSTAPPTKRAPRIIRRKKKDSTTNDITSPTNEIPPHIQNNTQLNHIISTTLPQDYEFEIPKTIWRIEKSNAQHVGLQLPEGLLMYASTIGDILVKFATKTTAIKSLSILGDVTYGACCIDDLSARALGCDLLVHYGHSCLVPLTCTVIPCLYVFVEIRVDVQHLVDCVRMTFLEEERVRLLNEVTSSTSSDDSTNIRQVQFQAIVPQAKPLSPGEVLGCTAPSDATDDIDEPASNVEIAKERVMIFLADGRFHLEAAMISNPSLRALRYDPYSKTLTEERYEIVKMKRIRRDAIQSARKTMGIILGTLGRQGNPAILSRVRSLLHSRGIRSIIVLLSEIFPKKLEMLSSTNPDGGGRVCAWVQIACPRLSIDWGHYFCVPVLSPFELFVAFGEVVDTTDEGGYPMDFYSKGGGPWTNYYESNKARKAVSYGV
The following text describes a protein:
Function:
Multidrug efflux pump.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTTLPAPTISTTAELRALLRLAGPVVVSQFAANALALIATAVIGRLGERELAAAAYANAAYYLVFIMVVGVMLSVAPRVAQAHGAGDARGVARALGGGLRLALLLSAVMLPLMWALSFVLPNFAPAGVSRDLVAAYLRVYSLGMLPNLAFIALRGTLEGTGKPGAVTGVALTGVVWALLVAPALAFGWGPLPRLGLAGAAGASASAAWIMAALLWPLARRRVAYAGPLGPLGDEVRALFRLGWPIGLTLGAEGGMFSVTTLLMARFGPEVLAAHNVTMQTITAFFMVPLGIASATGVRVGTEAGAGRLAQARRAGLVGLGLSSAVMLTFAVIELAAPRTVFSVFVNVNDPANAGLIAAATGFLSIAALFQLMDGLQVTANGALRGLQDTRVPLLVSLVAYWVVGLGLGSVLSSVAGLGARGLWFGLTAGLTLAGLSLVGRFLYRTRAGRAA
The following text describes a protein:
Function:
Plays a role in mycobacterial fitness. Likely enhances survival of pathogenic strains. Considerably reduces the overall net negative charge on bacterial surface when bacteria are exposed to an acidic environment.
Miscellaneous:
MISCELLANEOUS: Expression in M.smegmatis increases cell resistance to human beta-defensin 2 (hBD-2) and to sodium nitrite. It also reduces the negative charge on the bacterial surface upon exposure to an acidic environment, enhances bacterial cell viability at lethal acidic pH and induces a slowdown in biofilm formation.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Unlike homologous domains of MprF and LysX that are positioned in the cytoplasm, the MprF-like domain of LysX2 is in the extracytoplasmic region.
Sequence:
MVAAAGEPLNCQRANPEVTVKLPSADVVPRLRGRQRVVVHVDSRTARCVGALALVCAACWLIALLAGDYRHAQWAVAGRLGWSLTVLAAVAFIARGIFLGRPVTAMHATAAGLFLLAGLAAHVLVADLLGEILIAGSGWALMWPTSAHPRPEDLPRVWALINATRADSLAPFAMQAGKSHHFSAAGTAALAYRTRIGYAVVSGDPIGDEAQFPQLVADFAAMCHMHGWRIVVVGCSERRLGLWSDPMVVGQSLRPIPIGRDVVIDVSNFEMTGRRFRNLRQAVKRTHNFGVTTEIVAEQQLDDQRQAELAEVLAASPSGARTDRGFCMNLDGVLEGRYPGIQLIIARDASGRVQGFHRYATAGGGSDMSLDVPWRRRGAPNGIDERLSADMIAAAKDAGVQRLSLAFAAFPDLFGANQLGRLQRVCRALIHILDPLIALESLYRYLRKFHALDERRYVLISMTQVFALALVLLSLEFVPRRRHL