lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MAVKATYLVVYNFLQALGWLYVAVLLLDNYFKTGSFDQSYSVVKDVVGFLLLGAFLEVIHAAVGLVRSGTLNTLLQWLGRLHVYYAVIGSVPELQSEPALAIMLLAWSLIEIIRYPQNALATIKASPRWLVWLRYTAFIPLYPAGVLGEVILMYKALPYIKDRSLHGEYFKHLPFGYHEFLWGVLLVYPFLWLNLYLYLFRQRKARLAGQKKPVKRTSKRE
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MMTAESREATGLSPQAAQEKDGIVIVKVEEEDEEDHMWGQDASLQETPPPDPEVFRQRFRRFCYQNTFGPREALNRLKELCHQWLRPEVNTKEQILELLVLEQFLSILPKELQVWLQEYRPDSGEEAVTLLEDLELDLSGQQVPGQVHGPEMLARGVVPLDPVQESSSFDHHEAAQSHFKHSSRKPRLLSPRALPATHVPAPQHEGNPRDQAMASALLTADSQAMVKIEDMAVSLILEEWGCQNLARRNLNRDSRQMNLGTVFSQGSENRNGSESTSKAEVKGDSTSHGEIAGRFQKEFGEKREQQGRVIERQQKNPEEKTGKEKKAPGPPTAKEKKPTTGERGPREKGKGLGRSFSLSANFNNTPEEIPSGAKTHRCDECGKCFTRSSSLIRHKIIHTGEKPYECNECGKAFSLNSNLVLHQRIHTGEKPHECNECGKAFSHSSNLILHQRIHSGEKPYECNECGKAFSQSSDLTKHQRIHTGEKPYECSECGKAFNRNSYLILHRRIHTREKPYKCTKCGKAFTRSSTLTLHHRIHARERASEYSPASLDTFGAFLKSCV
The following text describes a protein:
Function:
RNA-binding component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Sequence:
MSTSLGFLAKKSKRNCLILQWVHMKNGHKTRHDSKGRLWRRTRLDLRTANTMMHIFILYQVQHP
The following text describes a protein:
Function:
May be involved in non-photochemical quenching, a process that maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage (By similarity). May play a photoprotective role in the thylakoid membrane in response to light stress (Probable).
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MALSQVSASLAFSLPNSGALKLATITNPTSTCRVHVPQLAGIRSTFASGSPLLPLKLSMTRRGGNRAASVSIRSEQSTEGSSGLDIWLGRGAMVGFAVAITVEISTGKGLLENFGVASPLPTVALAVTALVGVLAAVFIFQSSSKN
The following text describes a protein:
Function:
DNA-binding transcription factor that can both act as an activator and a repressor.
Subcellular Localization:
Nucleus.
Sequence:
MPFSGLVALLGSLVFLWNGSEACIPLGAPELLEVKVLGGGELHTDLVWRRCEAGNLPGESQRPEGGGGDGVTLFALHFPSVPPSGQWPPLSGVTLCVHWAGGGAAHSVKVSRASTVTLAPKAQDSGLLGSSVSGPLQEDLATKALCPRVLAPKESEEPRKMRSPPGENPSPQGELPSPESSRRLFRRFRYQEAAGPREALHRLWDLCRGWLRPERHTKEQILELLVLEQFLAILPREIQGWVRAQEPESGDQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGEGPPDQEQERLPPEPQSDLAKSQDAQPVALAQGPGLPNRLPGQLSGDQVLQDASLLPEVSLRDVEQKASLQLPPNRVSPFKDMIFCFSEEDWSLLDPAQTGFYGEFIIGEDCGVSLPAHDPAAQLDVSQGEEDGPRGAQLQDLQGKDTAQVSYLNFSSLQPFQVDERRKREEPPMPEFQTCQQTALMQSTCPAAGNAPSLERSLDEEVTIEIVLSSSGDEDSQLGSYCTDEPRSPPEKPHSLPASPRSGAEGAEVQTSSRKSYVCPNCGKIFRWRVNFVRHLRSRREQKPHECSVCGELFSDSEDLDGHRETHEAQKPYRCGACGKGFRLNSHLLCHRRVHLQPDGLAPVRKRERAEPGPTGGGPGTLLGKGPAKLGFQCCDCGRGFQRPDHLARHRSAVHEKSRARPLQCRYCVKSFSHNSDLLRHQRLHMKRRSKQALNSY
The following text describes a protein:
Function:
Exerts an anti-apoptotic effect in the immune system and is involved in responses to infections.
Subcellular Localization:
Cytoplasm, cytosol. Endoplasmic reticulum. Golgi apparatus. Mitochondrion.
Sequence:
MLIGRSGAGKTTIGNAILGEEVFKESRTRESEIQRGRVEARNISIIDTPGFFNTHLTDEELQMQMKKSLDLCSPGPHVFLLIINLENFTDNVANTVKTIHQHFGRSAFRFTMVLFIGKEAMSKREWIEFRLSRKTRELLSFFEEKCHVIIHRNKRDKKQIASLMENIEEVVRKNRREHYVKEICLENGEDEVKIQHVQVEQKKEENRLDLHVGEDENNDKSEQKEQTAENDGEKSSSGGSEISRTFKVSLIPEEKKEMTEKCSITGSDLRIVLLGKSRSGKSSTGNTILGKSDALKINKINKTCEKQEANTRGRNVSVIESPILCDPSMPREQMKDEIQKCAELSAPGPHVFLLNIRLDEMFTEDKKNTVKWIQANFGEKALRYTIILFTHADYLKGKPLNEYIRENKDLQAIADEFGGRFHSFNNEDVNNQTQVTELMEKIEKMVEENGGKHYSIVKMSYKSEKVNQNSFNWWKAVFILLIGALAAAAVAQSGLDR
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MGAEQQAASAKAGGSRFAATCGLLRQFMKEQGAAAAASPAVTIDFMPAAADGFGAAPQERRTMELFPQQAGTLKDSQDLRMWPEKAQLTIFYGGRTMVFDDFPAEKAKELLQLAGSFEASDAGSEPVNYHNSQAEPFLSEMPMARKASLQRFLEKRKSRLAAADPYYPGPYFAPKENGIGGKPVEAADHGAPWLAVSSPVLHLN
The following text describes a protein:
Function:
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Miscellaneous:
MISCELLANEOUS: In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Subcellular Localization:
Nucleus.
Sequence:
MSEADAGRIEESPSREVGEPVDAMPVNDRRSSSVEVVNGDMLLLHSIFYQGKTLKLAGTHTHIYNVVFRILKHVCKKVAQLTVAFPAGWDNDKPDSAKVASLCKIYNRVAKPFASAWSGSYNTDTLDDWGERNCTQKVAIDITTYAYELAVPRPADLNHYYKSFTSETYGETNLEQMASIIDELNIGPQDVLVDLGSGIGQLVCFTAAYAKCRKTVGIELSQTPANYANDLGDYFKKLMNHFGKTYGRFEHYQGDFLNPKFKKLICEEATVIFINNFAFSPELMFRITNELLQDLKHGTRIVTTKPFGDHKKELTVRSVGDINAISHTVELKSLDYGVSWTAKQVTFWLTTMDHTKLIRYYEEERRKKLEPSGSRERSQVTEKRKLDHKERDNRDTSNLNRGG
The following text describes a protein:
Function:
Promotes normal hermaphrodite (XX) development, in concert with zinc finger protein tra-4 and histone deacetylase hda-1, perhaps as components of a complex. May act redundantly with nasp-2. Involved in innate immune response to B.thuringiensis strain DB27 and S.aureus bacteria. May play a role in the uptake or spreading of dsRNA.
Subcellular Localization:
Nucleus.
Sequence:
MDTENIADASDIRVKDASGDSDEKGNGTTTEEETVEQKEKRLAELLAAGRRALKVNDIDKASDSLSEATELSSEIYGENHENTFDSLYYYGMATLELAKEESQLLKGPGEKESGDEEQAGNSDDKTDEENGETEKEDGEESGEEEDDDDDTMKLSWEILETARCIAAAKIEALEAEQSGISAIEEWNLKLADVLVLLGEHGISDGKYTQAFEDLDRALNIQRNVLPPSSRKIAQTYILIGNACASDANYDETVQYFGKTKDVLIARQTELKHELERGVDDKEKKSEFENELKELEEMMPGVEEMIADAVHSAAQVEETKKAIKAQFEGFTQVLAKLPQEAGDQKEANDISSLVRRPAKRAVDAPTDNQAVKKEKEEEGTTSI
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. Plays a role in salicylic acid-mediated negative feedback regulation of salicylic acid (SA) accumulation. May be involved in the overall regulation of SA, benzoic acid and phenylpropanoid biosynthesis. Involved in defense response. May act as negative regulator of resistance to the necrotrophic fungal pathogen Plectosphaerella cucumerina by modulating the accumulation of the phytoalexin camalexin and the salicylic acid- and jasmonate- dependent defense pathways. Controls the adaptability to nitrogen limitation by channeling the phenylpropanoid metabolic flux to the induced anthocyanin synthesis. Involved in the regulation of inorganic phosphate (Pi) homeostasis in a nitrate-dependent fashion. Directs the ubiquitination and subsequent degradation of the plasma membrane-localized inorganic phosphate transporters PHT1-1 and PHT1-4, to maintain phosphate homeostasis. The ubiquitination of PHTs triggers their clathrin-dependent endocytosis and trafficking to the vacuole through the endosomal pathway for degradation. Functions cooperatively with UBC24/PHO2 to regulate the abundance of PHT1-1, PHT1-2 and PHT1-3 in different subcellular compartments. Regulates Pi homeostasis by mediating, cooperatively with UBC24/PHO2, polyubiquitination of PHT1-4 and its targeting for degradation. Directs the polyubiquitination and subsequent degradation of the plasma membrane-localized nitrate transporter NPF2.13/NRT1.7, to help plants to adapt to nitrogen deficiency by regulating the source-to-sink remobilization of nitrate. Regulates leaf senescence during nitrogen deficiency by mediating, cooperatively with UBC24/PHO2, polyubiquitination of NAC92/ORE1 and its targeting for degradation.
Miscellaneous:
MISCELLANEOUS: Is the target of miR827, a Pi starvation-induced microRNA.
Subcellular Localization:
Nucleus speckle. Nucleus. Cell membrane. Note=Localizes at the plasma membrane, where it interacts with PHT1-1 and PHT1-4. Localizes at the plasma membrane, where it interacts with NPF2.13/NRT1.7. Localizes in the nucleus, where it interacts with NAC92/ORE1.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MKFCKKYEEYMQGQKEKKNLPGVGFKKLKKILKRCRRNHVPSRISFTDAINHNCSRECPVCDGTFFPELLKEMEDVVGWFNEHAQKLLELHLASGFTKCLTWLRGNSRKKDHHGLIQEGKDLVNYALINAVAIRKILKKYDKIHESRQGQAFKTQVQKMRIEILQSPWLCELMAFHINLKESKKESGATITSPPPPVHALFDGCALTFDDGKPLLSCELSDSVKVDIDLTCSICLDTVFDPISLTCGHIYCYMCACSAASVNVVDGLKTAEATEKCPLCREDGVYKGAVHLDELNILLKRSCRDYWEERRKTERAERLQQAKEYWDYQCRSFTGI
The following text describes a protein:
Function:
DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Also associates with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination.
Subcellular Localization:
Nucleus, nucleoplasm. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks.
Sequence:
MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESATMAVVKGAEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKAENGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEKRGNKPSDKATLLAFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPAAITKKLDALERSSSWSKTCIGPSQGNGFDPELYEGGRRGYGGFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMSLRKGKEPKIEEFTPPDEDCPLREASSRKIPKLTVKAREHCLRLLEEALISNHQAAGSTHGADLQAKAVELEHETFRNAKMVNLYKASVLKKVAEIHKASKDGQLYDMESGTKSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDEDRSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGSAKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRSEDASPSCGDVPGKCTQEVGAQGHLVAVFQTEGPRERPSTCSLRDQSFPEGQPSPLKETQAEKRPRPQQGNPERRAQKRLRPSTKSSILAEAKDSTLASDRSTENKVAQEPCQLSASGTSLREAADIVVRHLTPFYKEGRFISKDLFKGFARHLSHLLAQQLSPGRSVKEEAQSLIKQFFHNRARCESEADWHSLRGPQR
The following text describes a protein:
Function:
Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MGSIDTVGMGQRAIDQIISELSLNEKVALLSGVDAWHTFAIPRLGIPSIRTTDGPNGARGTRYFNGVPSACLPCGTALGATFDRDLIFSLGQLLAAECRAKGAHVLLGPTINIQRGPLGGRGFESFSEDPVLSGLAAASYCSGVQDGGVVPTLKHLVCNDQEHERVAVSALVTPRALREIYLLPFQLAIQGARPGAVMTSYNKVNGLHASENPGLIRDILRGEWGYEGAVISDWFGTYSVADAVNAGLDLEMPGPTRFRGPALMHALTSNKVSEKTLNERVRKVLELVQLASRAGVPEYAPERKLNRPEDRALLRRAAGESVVLLKNDKNDSTNSPILPLDREKTTLVIGPNADLAAYCGGGSASLLAYYTVTPRQGIADKCGAEQVVFSQGCYGHKELPLLGEHLRTIETGQPGYTFRVYTEPPPASGSFKGSDSRTPVDELHMTNSSAFLMDYSHPQISGDTYYATLEGTFEPPESGVYEFGLTVAGTGLLYIDGVLVVDNKTVQRAGTSFFGIGTVEERGERYLEAGKKHHVFVEFGTAPTSNLQHHHGVVSFGPGGLRLGGCRKLDTDTAIQQAVQSAAQADQVVVCVGLSGDWESEGFDRPHMDLPPGTDELVNAVLAVQPNAVIVVQSGTPVTMPWADKAKALLQAWYGGNEAGNGIADVLFGDVNPSAKLPLTFPRELAQNPSYLSYRSERGRVLYSEDIYVGYRYYDTTGQPPLFRFGHGLSYSTFHLRDLTVRETAPYAANIKESSLRVSVTVSNTSARPGAEVVLVYVRPPAAACSVGRPVRELKGYEKVMLQPGETREVSITIPLGLATSFWDEGCDAWLSEKGLYFVEAVGTGEGNTLVAPLTVQVSRVWNGL
The following text describes a protein:
Function:
SUMO-targeted ubiquitin ligase that plays an essential role in nuclear antiviral defense evasion triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML, SP100 and MORC3. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells. Interestingly, the E3 ubiquitin ligase activity associated with the RING finger domain does not seem to be directly required to inhibit the activation of IRF3 but instead plays a critical role in modulating the cellular localization of ICP0. Upon reactivation of latent genome, suppresses the silencing of viral DNA by dissociating either HDAC1 or HDAC2 from the HDAC-RCOR1-REST-KDM1A complex localized at the ND10 structures and causes their dispersal. Two cellular histone ubiquitin ligases RNF8 and RNF168 are also targeted by ICP0 for degradation, leading to a loss of ubiquitinated forms of H2A, a relief of transcriptional repression, and the activation of latent viral genomes. Enhances the localization of host CCND3 to ND10 bodies that serve as precursors of replication compartments to enable efficient viral replication. Like many RING-finger E3 ubiquitin ligases, ICP0 can induce its own ubiquitination, an activity that promotes its instability due to its targeting to the 26S proteasome for degradation. ICP0 restricts this process by recruiting the cellular ubiquitin-specific protease USP7 that cleaves the anchored ubiquitin chains from ICP0, thereby promoting its stabilization.
Subcellular Localization:
Host cytoplasm. Host nucleus.
Sequence:
MEPRPGASTRRPEGRPQREPAPDVWVFPCDRDLPDSSDSEAETEVGGRGDADHHDDDSASEADSTDTELFETGLLGPQGVDGGAVSGGSPPREEDPGSCGGAPPREDGGSDEGDVCAVCTDEIAPHLRCDTFPCMHRFCIPCMKTWMQLRNTCPLCNAKLVYLIVGVTPSGSFSTIPIVNDPQTRMEAEEAVRAGTAVDFIWTGNQRFAPRYLTLGGHTVRALSPTHPEPTTDEDDDDLDDADYVPPAPRRTPRAPPRRGAAAPPVTGGASHAAPQPAAARTAPPSAPIGPHGSSNTNTTTNSSGGGGSRQSRAAAPRGASGPSGGVGVGVGVVEAEAGRPRGRTGPLVNRPAPLANNRDPIVISDSPPASPHRPPAAPMPGSAPRPGPPASAAASGPARPRAAVAPCVRAPPPGPGPRAPAPGAEPAARPADARRVPQSHSSLAQAANQEQSLCRARATVARGSGGPGVEGGHGPSRGAAPSGAAPLPSAASVEQEAAVRPRKRRGSGQENPSPQSTRPPLAPAGAKRAATHPPSDSGPGGRGQGGPGTPLTSSAASASSSSASSSSAPTPAGAASSAAGAASSSASASSGGAVGALGGRQEETSLGPRAASGPRGPRKCARKTRHAETSGAVPAGGLTRYLPISGVSSVVALSPYVNKTITGDCLPILDMETGNIGAYVVLVDQTGNMATRLRAAVPGWSRRTLLPETAGNHVMPPEYPTAPASEWNSLWMTPVGNMLFDQGTLVGALDFRSLRSRHPWSGEQGASTRDEGKQ
The following text describes a protein:
Function:
Potent antimicrobial peptide against most of Gram-negative bacteria, some Gram-positive bacteria (Bacillus) and some fungi. Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells.
Subcellular Localization:
Secreted. Target cell membrane. Note=Forms a helical membrane channel in the prey.
Sequence:
MEGFFWKTLLVVGALTISGTSSFPHKPLTYEEAVDLAVSVYNSKSGEDSLYRLLEAVPALKWDALSESNQELNFSVKETVCQMAEERSLEECDFQEAGAVMGCTGYYFFGESPPVLVLTCKSVGNEEEQKQEEGNEEEKEVEKEEKEEDQKDQPKRVKRFKKFFKKLKNSVKKRAKKFFKKPKVIGVTFPF
The following text describes a protein:
Function:
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
Subcellular Localization:
Bacterial flagellum basal body.
Sequence:
MDKSIKILEKVMDICTYRQKILASNIANADTPNYKAKDINFQEELKKAAESHNAEYKVIEAPTTMPNRDGNTVNIEVEMTKLAETMLMYNGATQLFSTRIRMLKDAIKGGR
The following text describes a protein:
Function:
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Sequence:
MAEEIKLTPLETFAQAISASAKTIATYCRDSGHPQLSDDNSSGLTGDVLPPSAPQAVTAARQTILEASYRLQQLVTEPSQYLPRLTVYPQHLAALRWLCHFRIPELIPVQGTRTYYELATEAKVPLHQLQSIARMAITGSFLREPEPNIVAHSRTSAHFVENPSLRDWTLFLAEDTAPMAMKLVEATEKWGDTRSKTETAFNLALGTDLAFFKYLSSNPQFTQKFSGYMKNVTASEGTSIKHLVNGFDWASLGNAIVVDVGGSTGHASIALAESFPDLKFIVQDLPMVTSTSKDNREKTPLPETVASRISFESHDFFKPQPVQNADVYLLRMILHDWSFKEAGEILANLVPSVKQGARILIMDTVLPRHGTVPVTEEALLRVRDMTMMETFNSHEREIDEWKDLIQGVHTGLRVQQVIQPAGSSMAIIEVVRG
The following text describes a protein:
Function:
Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome.
Sequence:
MGNVYRKKATRYLWMWWFDAAGARQYASTGEEDEVKARAVLKATEKRVAAEKDQGLGASGPVTVEAYAAKWMEGRVTLRSVMDDRSRMQHHVLPSLGDKELGVLTRRHVLALVREVRAKGLAPRTVRHVYALVRTMLSDAVVDGLLERSPCDLRERRGEIPAIRDADPRWRDSAVYSRAEVVALITDERIPLERRVLYAVAFVGAVRIGEASALQVRDWDGTVNPLGKLWVTKTFNHKVGEVYETTKTDTPRQMPVHPWLSTMLASWLAYGWARMYARTPRQDDLILPSPTGMHQRPQGVLRRLHADLDLLGFRRRRTHDARRTFISLARADGADKYLLQWVTHGRRSDMVDAYTTPPWDALCREVAKLKLELPKQEEETMACRVPSCDSGVTADAGKEKPQQVRELAGAGVARSTGLEPVLLGSFYANPRQLPTKSEGLDAESAKLARTGAVDWHKPVTAPHPLAVVRQQMGVLKSGAGRERKVLASQLVDASLMALERLAAALHRTHAADDRWSDCPACRAVADGESPSAT
The following text describes a protein:
Function:
Involved in defense response to powdery meldew fungus; Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
Subcellular Localization:
Secreted.
Sequence:
MASSRAILAMGLLAAVLSPALSKRSFISMPADVSSPVTLANGLSYGYHANSCPQLQDIVWPIVESAVLGEVAIAAGLLRIFFHDCFPQGCDASVLLTGPNSERDLPPNQTLQPRAMQLIEDVRVKVHAACGATVSCADIIALATRDAVFVVRAHVGRCSCTVQQKHLPTSLAKEPMQAGESEMFYFYDLPLGRFDSLEPANSSAVFDLPQSTADANTLINVFKSRNLEPIDLVALSGAHTVGKAQCSSFNNRFSEDADFARRLAANCSSDPNRLQDLDVETPIVLDNQYFKNLMEGKGVFTSDQVLISDGRTDWAVKGLAENKYWFYSQFRDSLVKLSQYQPGGNVGEIRRNSCFTPNGQSIPATAGDEGFAASA
The following text describes a protein:
Function:
Specifically methylates the N7 position of guanine in position 518 of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MSPIEPAASAIFGPRLGLARRYAEALAGPGVERGLVGPREVGRLWDRHLLNCAVIGELLERGDRVVDIGSGAGLPGVPLAIARPDLQVVLLEPLLRRTEFLREMVTDLGVAVEIVRGRAEESWVQDQLGGSDAAVSRAVAALDKLTKWSMPLIRPNGRMLAIKGERAHDEVREHRRVMIASGAVDVRVVTCGANYLRPPATVVFARRGKQIARGSARMASGGTA
The following text describes a protein:
Function:
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSPREIVLKETNQIDFISNQSIFDISPISGWKPFAPTDQILGIFIVFVLLLTFFIFYKLKLKKADSLKNNSYFLLLFQMLFVWVQDTTADLLGEENKKFAPYFLMLLLYIVSSNLVSLLGGISPPTSSLTFTFSLGLATFIGIVVMGIRYQRWNFFKEFAFGITVKGKKYSTFIPNPFSILSGFAPLFSISLRLWGNILAGTVILALFYNFWIFIFSSINNQPLALSLGTVFAGLITPVLHIYFDVIAGVLQGYVFVMLTYNYWAKMRNQGLENNNASELHFKGIKVIQENI
The following text describes a protein:
Function:
HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA). Hmg1 and hmg2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (Probable). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (Probable).
Miscellaneous:
MISCELLANEOUS: Mutations of Phe-262, Ser-305, Pro-320 or Ile-412 are associated to acquired resistance to azoles, clinical drugs used to inhibit the activity and kill Aspergillus fumigatus cells during infections.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MATSLITRKLRSAEATNDVEPGWLKRQVTGVLQSISSHACQHPIHTIVVIALLASTTYVGLLEGSLFDSVRNSRNIAGQVDVDTLLQGSRNLRLGESTSWKWQVEDSLASQDYTGVNHLALTTFIFSDSLSKSSSIAPAATELPIPSNASAQPVPFTPNLFSPFSHDSSLAFTLPFDQVPQFLKAVQEIPDTSSDEDDGEQKKWIMRAARGSAYGSGGAIKLWLADAWGSFVDLIKHAETIDIVIMTLGYLSMHLSFVSLFFSMRRLGSNFWLAATVLFSGVFAFLFGLLVTTKLGVPINVLLLSEGLPFLVVTIGFEKPIILTRAVLTAAADNRGRAGQASSSTTKSIQDSIQTAIKEQGFEIIRDYCIEIAILIAGAASGVQGGLRQFCFLAAWILFFDCVLLFTFYTTILCIKLEINRIKRHITLRKALEEDGITHRVAENVASSNDWPLTESESSNKTSIFGRKLRSSSVRRFKILMVGGFVLVNVVNLSTIPFRDSSQGAGLPLLSRVSNVFAPTPIDPFKVAENGLDSIYVSAKSQMMETVVTVIPPIKYKLEYPSVYYAALGESRTFDIEYTDQFLDAVGGRVIESLLKSIEDPIISKWIIAALTLSIILNGYLFNAARWSIKEPEVAPVPAAPTVAVVEAKKEYPKIDLNPDTPKRSLEECEAFLKEKRAAYLSDEELIELSLRGKIPGYALEKTMENEDLMSRVDAFTRAVKIRRAVVARTPATSAITGSLECSKLPYKDYNYTLVHGACCENVIGYLPLPLGVAGPLTIDGQSYFIPMATTEGVLVASTSRGAKAINAGGGAVTVLTGDGMTRGPCVGFPTLARAAAAKVWIDSEEGRSILTAAFNSTSRFARLQHLKTALAGTYLYIRFKTTTGDAMGMNMISKGVEKALHVMATECGFDDMATISVSGNFCTDKKAAAINWIDGRGKSVVAEAIIPGDVVRSVLKSDVNALVELNTSKNLIGSAMAGSVGGFNAHASNIVTAVFLATGQDPAQNVESSSCITTMRNLNGNLQIAVSMPSIEVGTIGGGTILEAQSAMLDMLGVRGSHPTNPGDNARQLARIVAAAVLAGELSLCSALAAGHLVRAHMAHNRSAATTRTSTPVSAAVSAARGLTMSSSE
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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 (By similarity).
Subcellular Localization:
Mitochondrion inner membrane. Note=Matrix and cytoplasmic side of the mitochondrial inner membrane.
Sequence:
MLARLAAKRLLEIRQVFRQPTSQVTRSLSTALNYHLDSPDNKPDLPWEFSEANQSKVKEILSYYPSNYKQSAVIPLLDLAQQQNGGWLPVSAMNAVAKVIEVAPIRVYEVATFYSMFNRAKVGKYHLLVCGTTPCMIRGSRDIESALLDHLGVKRGEVTKDGLFSVGEMECMGCCVNAPMITVADYSNGSEGYTYNYFEDVTPEKVVEIVEKLRKGEKPPHGTQNPKRIKCGPEGGNKTLLGEPKPPQFRDLDAC