lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dose-dependent activator of the defense response against virulent pathogens, including bacteria, fungi and oomycetes, that acts in a positive feedback loop with the defense signal salicylic acid (SA). Regulates the salicylic acid (SA) signaling pathway leading to cell death and modulating cell fate (e.g. cell enlargement and/or cell division). In response to SA signaling, triggers the accumulation of FLS2 at the plasma membrane, thus priming defenses. Involved in SA-dependent freezing signaling and tolerance.
Miscellaneous:
MISCELLANEOUS: Sequence variations impacting defense responses are observed between cultivars. Enhanced resistance is correlated with a substantial reduction in vegetative biomass; MISCELLANEOUS: The dominant gain-of-function mutant acd6-1 and over-expressing plant ACD6-o is dwarf and shows spontaneous cell death and increased disease resistance, as well as increased defenses and better responsiveness to salicylic acid (SA). These symptoms are SA-dependent. In acd6-1, constitutively high free and total SA levels leading to collapsed dead cells with adjacent enlarged cells in the palisade parenchyma cell layer. This phenotype is absent in NahG background, in which SA is degraded. Strong accumulation of camalexin (an anti-fungal compound) and SA in acd6-1. The mutant acd6-1 exhibits freezing sensitivity, this sensitivity is suppressed in nahG background.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Constitutively undergoes endoplasmic reticulum-associated degradation (ERAD), via ubiquitination and subsequent degradation by the proteasome. During salicylic acid (SA) signaling, the soluble pool decreases, whereas the plasma membrane pool increases.
Sequence:
MDSSGADLDRIEAQRSMLVSHDQRKDFSHSGGVGTTSPTGDTEPVPKFRTNLKLSDLFALPGEDVEMTPEIFGGMSNGEKECLEKLRSNGTPMERVKSNTGDSILHIAAKWGHLELVKEIIFECPCLLFEQNSSRQTPLHVATHGGHTKVVEALVASVTSALASLSTEESEGLNPHVLKDEDGNTALYYAIEGRYLEMATCLVNADKDAPFLGNNKGISSLYEAVDAGNKFEDLVKAILKTTDDNVDREVRKFNLDSKLQGNKHLAHVALKAKSIGVLDVILDEYPSLMDEQDEDGRTCLSYGASIGYYKGLCNILNRSTKGVYVCDQDGSFPIHSAAKNEHYEIIKEFIKRCPASKYLLNRLGQNILHVAAKNEASLTAYMLMHDKDTKHLGVGQDVDGNTPLHLAVMNWDFDSITCLASRNHEILKLRNKSGLRARDIAESEVKPNYIFHERWTLALLLYAIHSSGFESVKSLTIQSVPLDPKKNRHYVNALLVVAALVATVTFAAGFTIPGGYISDSKKPNLGRATLATNPTLFIFLLFDILAMQSSVATICTLIWAQLGDLALILKSLHVALPLLLFSLLCMPVAFLFGVITAIAHVKWLLVTISIISGGFFLFAIFILGPHVMLQRSHLPPSSGIFLKTFMLTIDISELFVILIKACFGCVACSE
The following text describes a protein:
Function:
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MMNANRLPTRILGLDPGLRRTGWGVLAVEGSRMTHIAHGVITPDEKAEFADRLLHLFEGITAVIEQHRPDEAAVEEVFLNTNAQSTLKLGHARAAALIAPARAGLLVAEYSTRLVKKAVVGTGAADKAQIGFMIARLLPTAGKTTADCADALAVAITHANLRVANRRVA
The following text describes a protein:
Function:
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIGIVGVGNMGSIFAEKFSKEAERILLVEKDSEKLSRFNAPPYEIADLEKVREADLIVLAVKPQDAPIVLSALKGFDGILLSIVAGLKIEEIRKYGIHKVARIMPNVAVRVGEGVLATAFSADMSLEERELVKSLLEKLGFVVEIEEKLFSAVTALTGSGPAFIFVVVEAFLDAALKMGIPLDTAKELVYRLFKGSAELLTETGEHPALWKHRVSSPAGTTIEGLITMERFAVRSGVIESLISSYRRALELEEK
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Sequence:
MKQDGAARRRGEKAKAPPDGPPPAPPDVEMQEETAAVPAGEAGGERQPQRELDAITLEDIKEHVKQLEKAVAGKEPRYVLRALRALPSTSRRLNANVLHKAVNGFFTSNGAVRDFLLGFLEEPMDTEAELQFRPRMGKAASAPLLPEVEAYLQLLLVIYLMNSKRYPEAQKVSDDLMQKISSQNRRALDLVVAKCYYYHSRIYEFLNKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRNYLHYNLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKAIQLEYSEARRTMTNALRKAPQHTAVGFKQTVHKLLIVVELLLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQVLDQFGDKFQADGTYTLIIRLRHNVIKTGVRMISLSYSRISLADIAQKLQLDSPEDAEFIVAKVAVQEASSLCLPGLPTTPARPLLPRPQRAPFPGLLISGCAALGVLRAPTPISVHSLSPPLPAPSFALNCCLHPGRWWCPDHAPRGSQAIRDGVIEASINHEKGYVQSKEMIDIYSTREPQLAFHQRISFCLDIHNMSVKAMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDGFP
The following text describes a protein:
Function:
Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in 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.
Sequence:
MVNLSLRPRPAKAKFKGLPANLEVSPEDTVASVVAKLSAATKLSKSRIRLTVADEENGGAPGAKKKHIVLKPEHAVGDYLFSDSPVVFVKDLGPQIPWRTVFILEYLGPLLAHPIIFFGQKFFYRQSFEYTFAQKLVFTLCMLHFLKREIETIYIHKFSSATMPLFNLFKNSGYYWFIAGFNLAFFVYAPASFSSPQAPLWKRFLFSTGFFERTPLFLNLMAALWLWGETSNFWTHFNLASLRNDGSKDHKIPFGYGFNLVSCPNYFFEVVSWIAIALMCGNWSAYVFTAIGFGQMYVWAVQKHRRYKREFGDRYPRNRKVMVPFLL
The following text describes a protein:
Function:
Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and are delivered to lysosomes enabling degradation of membrane proteins (By similarity). Thought to be a cofactor of SKD1/VPS4, which catalyzes the disassembly of membrane-associated ESCRT-III. Target of pathogen-responsive mitogen-activated protein kinases (MPKs) that plays a critical role in plant basal resistance to Pseudomonas syringae in a SKD1-dependent manner by promoting multivesicular bodies (MVBs) trafficking upon plant infection.
Subcellular Localization:
Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus. Endosome, multivesicular body. Note=Localized in multivesicular body when associated with SKD1.
Sequence:
MSNPNEPARALLPYLQRADELQKHEPLVAYYCRLYAMERGLKIPQSERTKTTNSILMSLINQLEKDKKSLTLSPDDNMHVEGFALSVFAKADKQDRAGRADLGTAKTFYAASIFFEILSQFGPVPPDIEQKHKYAAWKAADIRKAIKEGRKPTPGDPVDDDTDLSIPSSGPSGSYDHSASDTNTTSHHRTELDPPHDSNDDSSHHQFPEVPQHPLPPRFYDNPTNDYPADVPPPPPSSYPSNDHLPPPTGPSDSPYPHPYSHQPYHQDPPKHMPPPQNYSSHEPSPNSLPNFQSYPSFSESSLPSTSPHYPSHYQNPEPYYSSPHSAPAPSSTSFSSAPPPPPYSSNGRINIAPVLDPAPSSAQKYHYDSSYQPGPEKVAEALKAARFAVGALAFDEVSTAVEHLKKSLELLTNPSAGAGH
The following text describes a protein:
Function:
Has a broad role in development, specifically in the genetic pathway SynMuvB that negatively regulates specification of the vulval cell fate. Required for fem-3 3'-UTR-mediated repression in the regulation of the sperm/oocyte switch. Acts by regulating the translation of fem-3 mRNA, by binding to its 3'-UTR.
Subcellular Localization:
Nucleus.
Sequence:
MGEVGANATESTAPPPPPAADSNSNSSSSTSEPKENGEVNGTATDKTAVTDNAAVAEEDNDDEEELLHEEADKNGTNSEAANGEKSATEPQANSDVAPSGEEKLHSNAADRLGKKEAAEPTESSSDATNPSSRSGEGDACGKTELSKQATEEKKLSTSRESDEIETMDVDEEEDDGDVVAVDAENGTANGSPGGDEEPPVVAAKQPQQQVTEVDDDEPMEVDGGDEQDAAAAAPTNGHKESNADEDGATVRSEKLTSSKTAAEKDKSEPPTHPPSKQPADDDAEEEEEDDDKPVSINSDSEGEESPQKRDSGEPVAVADKATKPATNSKLILVDEGGLAKLNEAVPAAAASTVAGGDASAGKKSDTVPSNGVVVDGAAATATRTQNGDCDGDLTILSDKEDDCVVIEDDDGESDASVPAVPANNARRSGSIRATGGRKSDGGVGGGAASLMAGSAINPLAAAAAALQQQQLNQSIVSSMDDDDEDEDDDDDDIEEIIDDPLALGTQATNLSMGGRGYQPNTPVNLKGQKSLLMNNAAGGAAGGKEPTLVIIDTNTMMNNGGGAQRGATNLASAGVTSPNVNSNAANLLAKASSAGILSNASASPGAQFNSRSLLNSPGVVGNSPVATAAGAAMLNQGGMLGKSAAAGSALAPVTPLLPALTDDMFVLEAPSFIVPYIYEKPPADNLRDIVDELEVTIKEMRKKLEESGAVPPAASKQQGGDTAEQAKEDGAKNAAAAAAVAASLYGDKESDKSKNNKKRKRNNDDDDDWDELETSTDDEASDEEQKTKVLIKEARADIEAIKEHIISPSDKDDLTGVGGGGGSSGGANGSDPKKSENYFENPLGKFFMNIGINLVQEFVQTDLLRQQKRKRDREGKPSPSTQLAINSLMKNLEQSKENNKPYKFEMKRCEYCPFKSESALVMAHHYETPHMRNFIYKCNFCAYETRPPHDILYHMEAVHNIKGRMEKALSYHHCPNCPFEDNGKSKLARHAVACAKKFRPELNLNPPMDWEPPAKIPRIKPKHGLVGTATAYQAMTAQQQKNIALANQQRLNQQQVASSAVHLQQQQHLSQLQQQQLVGQQHLGLAGTNAAAATLNNVALANLSPAAQAVAIRARAAAAGLGGAGSGGVGGLGAGGGVGGAGGGRAPAIIPSPTGITGAGSGVRGAGAVAGLGGGLNATALAASAAAIRNTLAGAGMVIPNNLQLSASALAAAAAAGGFSKYLPKSINNAGRSLLTNSNASITIQNASSMKATKTAQAPSISITPLPRQSASNSSSAAANMSNIAGALSKLQAQGTSAVKPGQNPSGGKMAFVVCEICDGYIKDLDQLRNHMQWIHKVKIHPKMIYNRPPLNCQKCQYRFFTDQGLERHLLGSHGLVTSSMQEAANKGKDAGRCPVCGRVYQWKLLNHVSRDHNMTLKPAHLSYKCTVCTATFGMYKQFESHVYSAHSTVAKKTGEGKGSKGGGGSGGGGMGQQQTSSGMGSSGGSSSSGGAGGLRNPFVGGGDSLLKPLKINDEITIIPQPTSNSKMAKTIELESHVID
The following text describes a protein:
Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence:
MNQFTLFAVVAFFSSSVLAQEMTVVMTDLSSGQSVGTVTVTDSEYGTVFTPQLTGLPAGLHGFHVHANGSCETSSKDGKTVLGGAAGGHYDPQNTGKHGYPWTNDNHLGDLPALYVDAQGQANQPVLASRFKMAEVKGKALMVHAGGDNHSDHPMPLGGGGARIVCGVIGL
The following text describes a protein:
Function:
NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MAATFTLDDVRKHNSKDDVWMVIHNKVYNVTTYLEDHPGGSIILREVAGTDATEQFVEIGHSVEATDILEELYVGDLAEEEHAEEVEIFRPTYEKVAMEAAVKVEKATVSKVKKNVRRTIAMSSVIASVGAVGLAKGWWTGPEWALAAVTTAQKPINQLADFIRSKFAQNGSSSKLFWWGVGIATVVELSLTTAATTWALSKFEAQKEFTHFPRSRPAKKERKVAILKIPTNSTSGPAVKPPVKVMDPADWRKFKLVRKVLVSPNVYHLVFALPHPTDVLGLPTGQHVALRALIDGKSVSRSYTPVSNNSDLGRVELLIKVYDQGLMTKHLERMEIGDQIEMRGPKGAMQYVPNSYAKEIGMIAGGTGITPMYQLIRAICEDESDKTKISLLYANNTEADILLREELDGFVKAFPDKLSVQYVLGQADENWTGLRGFVTADMIKDFLPPAADTTKMLLCGPPPMVAAMSKNLVSLGFTAPGTLSKATDQVFLF
The following text describes a protein:
Function:
Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival.
Subcellular Localization:
Mitochondrion.
Sequence:
MDPPPHDVWTQSEHFHGFLLVHREKHQRVWRGGGGLSSLDGWRCVSPAGFDPRRSWGHTPPAEPWRLRLSEAAYEKLAEETLDALAEFFEDLADEDVAGEELDVLFSSGVLTVKVGGDYGTYVINKQTPNKQIWLSSPTSGPKRYDWSGERWLYYHDGVSLHQLLSQEFSLIFKRNINLLDLPHS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDQPINSFDQVTFEDVAVYFSEREWASLLDAQKDLYKSVMRDNYEAVTSLGFPVVRPKAWGRMCQGVTVKLEGTEQMDIGDSAQNMKDVMKCLNKCLSPLPISTEPGSRCTTWAAPDPMDQLVGNVSVKEEEFQAFGALGSMPPHVPNPQSRLDSDRQRQNGSAQHQAPPSAPDAERLHAPFQCTKCQRTFTNPYDLQSHSNVHIREIRYTCRDCGRGFSRSDFFKAHRHVHTGEKPFKCPECKKSFSAVSILKKHLRSHQPKMSRRAKKMKRKNKQNVPDVLADPDYERRHLCTVCQKTFSKSYNLKVHERIHTGEKPYKCPKCDKCFSQNARLRVHRTTHAEWAHEAVWLRKRKPSAPAEKLHVCNVCEKGFSKSYSLKVHLRTHTGEKPYSCPECHKSFSKNNLLTVHKRIHSGERPYQCSECLKSFSVISHLRVHRRTHTGERPYKCTECVKSFSDYSSMVRHQRIHSGAKPYQCNICGKPFREKSHLTVHQRTHTGERPYKCGECHKTFSDCSSYVEHRRHHTGARPYQCELCHKSFTKAYTLKIHQRVHTGERPYKCPLCPRSFSINYHLKVHEKTHADNQPETLSRK
The following text describes a protein:
Function:
Catalyzes the synthesis of activated sulfate.
Sequence:
MSTVGNPANIFWHENPVGKAEREKLLNQQGCVVWITGLSGSGKSTLACSLGRELQSRGKLSYVLDGDNLRHGLNKNLGFSAESRAENIRRTGEVAKLFADAGLICIASLISPYRKDRDACRALLSDKKFIEVFLNMPLQLCEERDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEIEIQQKDGLVPAPNEMAGQVVSYMEDRGFLEA
The following text describes a protein:
Function:
Calcium sensor of the mitochondrial calcium uniporter (MCU) channel, which senses calcium level via its EF-hand domains. MICU1 and MICU2 (or MICU3) form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. At low calcium levels, MICU1 occludes the pore of the MCU channel, preventing mitochondrial calcium uptake. At higher calcium levels, calcium-binding to MICU1 and MICU2 (or MICU3) induces a conformational change that weakens MCU-MICU1 interactions and moves the MICU1-MICU2 heterodimer away from the pore, allowing calcium permeation through the MCU channel. Also required to protect against manganese toxicity by preventing manganese uptake by MCU: mechanistically, manganese-binding to its EF-hand domains does not induce any conformational change, maintaining MCU pore occlusion. Acts as a regulator of mitochondrial cristae structure independently of its ability to regulate the mitochondrial calcium uniporter channel. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG.
Subcellular Localization:
Mitochondrion intermembrane space. Mitochondrion inner membrane. Note=Recruited to the mitochondrial inner membrane by EMRE/SMDT1. Also localizes to mitochondrial cristae junctions.
Domain:
The EF-hand domains have high affinity for calcium and act as sensors of calcium levels; The polybasic region mediates interaction with EMRE/SMDT1 and association with the uniplex complex; Lysine and arginine residues in the K/R-ring mediate electrostatic interactions with MCU and play a key role in MCU inhibition in absence of calcium; The C-helix plays a key role in mitochondrial calcium uptake, probably by mediating interaction with MICU2.
Sequence:
MFRLHSLSALAELAVGSRCYHGGSQPTQMKRRLMMVAFLGASAVTASTGLLWKRALAESPPSVNNPKSELGDKGKNKDEGEVCNHEKKAADVCLEPHPEEKKKKRSGFRDRKVMEYENRIRAYSTPDKIFRYFATLKVINEPGESEVFMTPQDFVRSITPNEKQPEHLGLDQYTIKRFDGKKIAQEREKFADEGSIFYTLGECGLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEFEQASCPGNIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQRKLQHDVLKLEFERHDPVDGKITERQFGGMLLAYSGVQSKKLTAMQKQLKKHFKEGKGLTFQEVENFFTFLKNINDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRLMRGLEKPKDMGFTRLMQAMWKCAQETAWDFALPKQ
The following text describes a protein:
Function:
Acts as a transcriptional regulator. May mediate transcriptional activation by binding to the E-box motif 5'-CANNTG-3'. Required for the correct morphology, terminal identity and function of the ADL sensory neurons by controlling the expression of the ADL-specific gene repertoire, including chemoreceptor encoding genes, ion channel encoding genes, neuropeptides and the neurotransmitter eat-4. Regulates the expression of the srh-234 chemoreceptor encoding gene in the ADL neurons under feeding conditions. Plays a role in the chemorepulsive response toward ascaroside pheromones mediated by the ADL sensory neurons.
Subcellular Localization:
Nucleus.
Sequence:
MPMVVAKRNARERTRVHTVNQAFLVLKQHLPSLRQFTKRVSKLRILNAAITYIDTLLKLIQSSEAVPQSVISATLGPIVPTPVRAVHKISKPDTVISQPIRPLAPVLPRHETYLPAPIAATCAPDHSLVDYRSTFASSLAPPVPMQMPSVFSPQPTFPYMKSLLDYPTYFYQPSTAPPPPPAPTAPQSHLIVNNQLVPMPSYQCF
The following text describes a protein:
Function:
Beta-mannanase likely involved in the utilization of carbohydrates in the human gut. Catalyzes the hydrolysis of different beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan, as well as carob and guar gum galactomannans, to a mixture of oligosaccharides. The dominant product from ivory nut mannan is found to be mannotriose; mannobiose and mannotetraose are produced to a lesser extent. Does not hydrolyze mannobiose, and hydrolyzes mannotriose at a significantly lower rate than the longer oligosaccharides.
Subcellular Localization:
Secreted, cell wall; Peptidoglycan-anchor. Note=Is likely to be cell attached, either by the sortase mechanism (LPXTG motif) or via a C-terminal transmembrane helix.
Domain:
The carbohydrate-binding modules (CBMs) are responsible for the affinity to carob galactomannan.
Sequence:
MKTTVTKLLATVAAASTIFGMSTLPAFAAEGKSASNGNSVNISDVNATAETRALFDKLKNSGKGDLRFGQQHATDENISSSASQGDVYETTGKYPAVFGWDAGLALRGAEKPGSGADKNANAKALAQNITDADSKGAIVTLSAHWCNPGTGKDFNDTTAVASELLPGGKYSGTFNKELDAIAATAQRAKRSDGTLIPIIFRPLHENNGSWFWWGATHASASEYKELYRYIVDYLRDVKDVHNLLYAYSPGGVFNGDSTDYLATYPGDQWVDVLGYDEYDSDDSADDSSAWINTVVKDMKMVSDQASQRGKIVALTEFGRSGDRKFKESGTGDKDTKFFSELAEALAENVPSTAYMMTWANFGGGGDNFQAYTSWKGSDGEADFKAFADSNKNLMASKDNVDYSNAPAAAMQNGSARIVTPVDGNRVTDTKVVVRVKTEGVKYSDLDLNSAIVTTDRGQNVKLKYSCNGYFTGILDLNAAGINLDQSKLTLTPQVKTKDGKTLAAADGNGSVTVKLGAKPEQTVDNVEDFDSYDNEAELQSVYSPSHSTKSNLTLVDSPEDNGTKAGNIHYDFVSYPEYNGFQRSHTPKQDWSGFSKLNMFLKADGSDHKFVVQVNAGGVTFEAYPKIDGTDGHVVSLNFGDADGNGGDFAPASWDTAHAGMKLSQKLLSKVGSFALYINDNGGNRPKSGDLTLDSIKLDGKRDAYAPNTNPTPGNTAKAQSVDDFSGYSDDAAAQSAWGNRGHTEVLSLDEGPTDGSKALRFKYDFSNGGWYDVAKYLDGANWSGESVLAFQVKGDGSGNAIGLQIGTSDGKYFLASVKLDFTGWKQIEIPLVDNANLTQSWPEDANKDNPMTEDDLASIKELVFASQQWNSESDGLDSSIADIKVEPAENTSNEQTPKDESKTEVKADKEQEQSEDTSADVTAQDPATCPISDEDSKGSTGNTTVTVKPTPDTKEPADNTGKDGLSRTGSNIISAIAAVAVLLLGGCAVLIARKRKGGDIE
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Within the pathway, FUM2 performs the C-10 hydroxylation present in FB2 and FB4 and which occurs early in the biosynthesis. The biosynthesis starts with the FUM1-catalyzed carbon chain assembly from one molecule of acetyl-CoA, eight molecules of malonyl-CoA, and two molecules of methionine (in S-adenosyl form). The C18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by the pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate is then stereospecifically reduced to a 3-hydroxyl product by reductase FUM13. Subsequent oxidations at C-10 by the cytochrome P450 monooxygenase FUM2, C-14 and C-15 by FUM6, FUM12 or FUM15, tricarballylic esterification of the hydroxyl groups on C-14 and C-15 by acyltransferase FUM14, and C-5 hydroxylation by 2-keto-glutarate-dependent dioxygenase FUM3 furnish the biosynthesis of fumonisins. The tricarballylic moieties are most likely derived from the citric acid cycle, and their addition to the carbon backbone may involve FUM7, FUM10, FUM11 and FUM14 (Probable).
Sequence:
MYNIFFHRASKFPGPTIAGATSFRYHWAMSTGNVAPWLREQHARYGEVVRIAPDMISYVSPDAWKDIYAYKPGEKEQNGIDWTIPSRDDDVPSMFSEPNDAEHNRVRRLFLPAFSDRALKQQEPLLSKYSDQLVHLIRRGIDDNRDQEFDAVKLYNFTTFDIMGDLTFGEPLGLLKNSSYSEWVQNLFRDIKTAGIFLFIFDFPPLPWLVKKFSPPSIQRAHEIHKQHTVDRVNRRLEKGLDRPDIWNLVLSQPEGRGLTHPQMHANADIFMIAGTETTATLLSGLTYLLLKNPEKLQRLVEEIRGSFGSIEELTVENLARLPYLSACLSEGLRCYPPVPIGPSRVTPKTGGQVLGERVPGRVRLTIPQCAAYYSDLNFKDPYSFIPERWLPGTGYESDRKGILQPFLIGPRNCIGQNLAYHEMRLILCKLLWHYDIELCPDKGNWLLDQKMYIFWEKRPLMVKFTKARK
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSSLRNAIPRRAHKERSQPSSRKKFGLLEKHKDYVQRAKAFHKKEGTLRVPFYSFLFLQLLIPSTVNNFLQKLREKAANRNEDEFYFKMVRTKTVDGVHKPESEANKYTQQELMLMKTQDMGYILQKIQSERNKIERLTASLHSIDKQPVNKHVLFAEEREEAKELESQYQKSKIPFTSEDIPAGIKRKTAQSYQELEARRSRLNQLEKIYMDMAMQKELQKKGRKRKLGEDEIVCPTSKPVYKWCAERKR
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular Localization:
Nucleus.
Sequence:
MESLDQTPNPHFQTPEDQSNPPPPPPPPPPPPETLDFIPVCPNSPPPPPAEEPQFPDPQNPHKTLISNPPQIAPENGHNPQTTTPKPEIPKSLLSENGVANTNSGDRDCSGGEEETTSRRRRRSRWDPPADAGADGSNNNDSGSGTRKRKSRWADDEPKPVIQLPDFMKDFTGGIEFDPEIQALNARLLEISRMLQSGLPLDDRPEGARSPSPEPIYDNMGIRINTREYRARERLNKERQEIISQIIKRNPAFKPPADYRPPKLQKKLYIPMKEYPGYNFIGLIIGPRGNTQKRMERETGGKIVIRGKGSVKEGRLQQKRDLKPDPSENEDLHVLVEAETQEALDAAAGMVEKLLQPVDEVLNEHKRQQLRELAALNGTIRDEEYCRLCGEPGHRQYACPSRTSTFKSDVLCKICGDGGHPTIDCPMKGTAGKKMDDEYQNFLAELGGTMPESATKQTATLALESSGSGNNPPWAGSNTGGLGSANQAGLGANGLKPKEYDDTNLYIGYLPPNLDDDGLIGLFSSFGEIVMAKVIKDRITGLSKGYGFVKYCDVQMANNAIASMNGYRIDGRTIAVRVAGKPPQPTVPPGPPTSTMPAYPIPTQPLGGAYPSQQFTAGGPLPNGPPTSYVGAHASYRGTPVPWGPPVPSPYGPYAPPPPPPPPGSTMYPPIPGQPIPPYGVQYPPPVQPVPSGTLTQTVASSEAQQSYPPGVPSENSLSAPLAASNVYGHSIGYSSYYSAVPPPPPPPATDHSQGMGNVPWASNSTMPPPHSSSAEKARYGADAEYAKFMAEMK
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVYTAEDLIKNAQVVAIIAAPQVSAEADLLAQLGSRNCIPVLSFSCVSPTLHLHTVPYFVQTSPKESSQVAPIVDIVTSFLGREVVIVYEDSPYGIGILQPLTEALQSSSVHTIDSVVVPIGVTDDHFDQMLYRLKNMSARLFVVNMRTALAVHLFSRAKDAGMVTEDYVWIATVALGNVVDGLSPDDIDNLQGILTLRPYVQGTSLARFKARFHLENLNTDRVHTPSVLLFRAYNTAWATCIAAEIAGVSRLAIRVAEIDLSRHGLSANRRVFLDSILNTTFDGLTGDFRMVNREVQPPSYEIVHVNRKGALGVGLWTPPLSLQPQKLSRKGYSFDNSRRSVFWREDTVRTSKGREKTGFPLNLDTKHSLNLESKRRNARKLVGGRSGKLCRSYNEKLLRIGVPQKDGFKAFVNVSRPYFFCKDNATRPSTTKQVTGYIIDVFETAMEKLQHPPCYDFCVFDGSYDELVGNVSLGILDGAAGDVTITANRTGQVDFTMPYTQSGVSLLVLSESDLEPIQWTFLAPLTKELWFATVGFFFFTGFVVWVIERPRNPEYQGSSLRQFSNASYFIFSTLTFSHDHIIRSLLSKIAVVIWCFLVLVLVQSYTASFSSILTAERLHPTVTNLDQLLVNGDYVGYQHNSFVYSMLRDRGFSKHRLIPYSREDEYADALRKGSMNGGVSAIVDEVPYLTSFLFSDARYQNEFQIVGHIYKTPGLGFVFPQGFPLLHNISTAILNITEGNEGSQFEEKWFGTAATTPTVSNKPSTPLTLQSFSGLFLTSGFFSSLMMLISIMRLAHARWTELRHGDADPMDNISGDEEFRQLHPEA
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-formimino-L-glutamate to N-formyl-L-glutamate and ammonia.
Miscellaneous:
MISCELLANEOUS: There appear to be two competing pathways for the degradation of N-formimino-L-glutamate in P.aeruginosa: the two-step degradation of N-formimino-L-glutamate to ammonia, formate, and L-glutamate (via HutF and HutG), and the direct hydrolysis of the formimino functional group of N-formimino-L-glutamate to produce formamide and L-glutamate (via PA3175).
Sequence:
MSAIFAERALLPEGWARNVRFEISADGVLAEIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRMVARLSPEQIEVIACQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKEVDDCQAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD
The following text describes a protein:
Function:
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Sequence:
MTIELLTPFTKVELEPEIKEKKRKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERKGISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYPVIWVDVPLMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY
The following text describes a protein:
Function:
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVKSARQGAGGFWRDFKDFILRGNVVDLAVAVVIGGAFTSIVNAFVAWLMAVLLQPVLDQAGVSQLQDLPLGLGELVIAIINFLIIAFVIFLIIKAIEKMQRKKAVEEEIVAEAQPDPVLEAQTNLTDSINRLITTLENQQSSSQ