lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for stabilizing type IV pilus (T4p) in extended, nonretracted conformation on the bacterial cell surface.
Subcellular Localization:
Periplasm.
Sequence:
MKSKLPLILINLSLISSPLGANAAKIYTCTINGETVYTTKPSKSCHSTDLPPIGNYSSERYILPQTPEPAPSPSNGGQAVKYKAPVKTVSKPAKSNTPPQQAPVNNSRRSILEAELSNERKALTEAQKMLSQARLAKGGNINHQKINALQSNVLDRQQNIQALQRELGRM
The following text describes a protein:
Function:
Mediates transcriptional repression by certain nuclear receptors. Plays a role in development and neuronal function. May play a role in muscle-specific oxidative mitochondrial metabolism.
Subcellular Localization:
Nucleus.
Sequence:
MESFKELAREYDEKFKAFQDDLQKWEETSERKEYAEFHRVQAESEFPELKREREDRERWARAERIRGEDEKSMLAKEHADKKIRLGVAKIPRLLTESERKMDEFVERPGSILKDMKKEHRQSVLDRLEEWSPEERSLFKSRQADHVKIFHGLTEFFVDKTASDLVLFYYMNKKTEDYKKDFKPKKRVTKYKVGAFPSVEELAYFRMMPPLDFSSFPKNSLMCYFCCRTVNGIDLNGTFMPKEAYEIFAICPDEDRVVCSGCREEAAKLYKDNRCFGNRCSNQKKRANRVNRNIPLDFADFPVRTRAFIMDKLGSTRVAVKFCTPCKNALTRWINDVNNKEETIMAELLNYEGQVGWTDDEKTKLVTLINSSPTLDWVSISEGMNRRPNECKMQYDAMNGVKTQPMIEEVDEEDGNGQEEGGDALVNTPTTSSAAARRSGLARNAKKPVRTPRAPRSAGGRRTGGAVTRAQAVPKPVEDLGEEIDEMEIEDNDEDASRGSRGKDSKAPSDRDGSPADMEGDSPEGQDQDADQDQDQDQDVDEEEEEVIVRDIDSPVKTLLSPKILSGGHKPDFPPVPRIQKPSTSSQPPPPEPMDTKENESDDGEEDNDILEIDVDEPPAKRPTPTSSSSHLIGSSSVGGSERELGGRGLVQQQQQQQPQAQSAAPPVTVSTAAAATAERLVNATSPSPSVASQHLVPTETSTSVPPVTIVPPAIQQPVVVISGAAPQFTQQQTTHSPALIAQPIPQQLIPQRVSTPAQILTPTPVRPTAASTPSMDQFLGLFKQQQQQQQQQPQQSNLMQQLGNINPQFLALLLQQQQQQQQVQQAQVQAAQTQGSLTSGTPFQAQQRPDEALQKLFSSPEMLGTLLNAKYQFPQFPQAIQQNPLLMNAQHQLILQQQQLAMQHAQAQAAQAAQAQAAQAAQAQAQAQAEAKLKTQAAQAKAQADAQARVQTQQQAHLKAQAQAQYQMNRPQLIPASVQMPIGINTAYHQKSLTPSETSASATPPAHRPRAATTVGSKMPAGRSNVQEAELRTLKEELIKRIRLFRDRIAEDAHLKREEENIVTYTAQIQASRVQYNTEILGQMKQRYEQAAARRIEIVKELDEPAKFINGVQNKFNDFSVFKLDEIDRQTLHEILQRYAAEQKPDQLQQQQNDFHNLLRQNNIGIRQAQYPALQASPHQAAIIQHQQQQEAFKKLQQQHQDAQKRKLEAPVSSATPQVKRIALSQSSPVQRFSQHPNGTLPHNLAVVYQNKMPQDREKLLQEQQLNQYLFAAQQQHLQQQQQHHGTQPEQKSKRKSGIESITSMQGAPHRHIQLAGPSSSRIQSGRGVSPALSASRSVAPTISGAAGRSITAGTSGHSSTSDYNKELAERMNEVFKPTHPQLLQTKASAMNSNAVSPANTNNSDEIECVYQGPPKTPASIKRLQPTEGPRTLSGQRMKSILSVPAHQRRSSIPPVKTEDEAMECLSMMMYEEAKAPPSDRIVTKLISSSEAAAAANPSAKFSYLDIFNDVVKRDEERCQRMLQSTSVLQPSRELDAFLQQLQQNPQQYANLSAAEKLALQQYQIHSAHQKSQQQAQLQAAQQLQQQQQARPDHYEKFHLLRPNAEIVRPIPTTFSHFLNKATTSTVSSSASAPQFLQPPAAASIAAPTPISTPHAMPSPSVGVQTAPPTPQAVHHPVMPIIPGKPSSVNSNVSDVSSDDDDVRNPEKLPANRLPPLPGDKTAFRSVIDLRATGHVAVTKKIPVKYPLVVQAQNGIQPIKDYGPPCKNLVYEDLSDDE
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAAAVHPRVVRVLPMSRSSVPALAASVFHSPPQRQLHHAVIPHGKGGRSSVSGIVATVFGATGFLGRYVVNHLGRMGSQVIVPHRCEPYDTMHLRPMGDLGQIIFMDWNGRDKDSIRRAVEHSSVVINLVGREWETQNFDFEDVFVKIPQAIAQVSKEAGVEKFIHISHLNADIKSSSKYLRSKAVGEKEVRETFPEATIIKPAEIFGREDRFLNYFANIRWFGGVPLISLGKKTVKQPVYIVDVTKGIINAIKDPDARGKTFAFVGPSRYLLFDLVQYVFAVAHRPFLPYPLPHFAYRWIGRLFEISPFEPWTTRDKVERIHTTDKILPHLPGLEDLGVEATPLELKAIEVLRRHRTYRWLSSEIEDVQPAKTIPTSGP
The following text describes a protein:
Function:
Esterase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates; Esterase that catalyzes the release of covalently bound dihydromonacolin L from LovB during lovastatin biosynthesis.
Sequence:
MRYQASPALAKAPRALLCIHGAGCSPAIFRVQLSKLRAALREDFEFVYVTAPFPSSAGPGILPVFADLGPYYSWFESSSGNNNNGPSVGERLAAVHDPIRRTIVDWQTQHPHIPIVGAIGFSEGALVTTLLLWQQQMGRLPWLPRMSVAMLICPWYQDEASQYMRNEVMENHDDDHDSKDTEWQEELVIRIPTLHLQGRDDFALAGSKMLVARHFSPREAQVLEFAGQHQFPNRPRDVLEVINRFRKLCVTVQTLE
The following text describes a protein:
Function:
P cell-type specific protein which involved in agglutination during conjugation.
Miscellaneous:
MISCELLANEOUS: According to PubMed:16857197 the number of the intragenic tandem repeats for map4 is 9 rather than the 5 annotated in the reference sequence, producing a protein of 1092 amino acids.
Subcellular Localization:
Cell surface. Note=Localizes at the mating projection tip.
Sequence:
MNSYAILLSLFFSFERLLTLANANSLYSPFNNSSFVDSDTSFSDLSRNGLLSLLDSNTTSASVQTIAISQTDNAASCIPSASLLSSSVVLYSAKETVTVSSYWSLVSTSVTGTVYVPYTSSVACFPYATSDAPNPIPRGDSATSTSIAPTYSASDSSATTITSSSPSTSIIGTGSTDTSVSSTLTYHTPIASPTTSSNSDNEYTVDVITSSSLSSFVITNVDSTTTSVINYIGASTLESSSLTNTVSPTESTFYETKSSTSSVPTQTIDSSSFTSSTPVSLTSSSTSSSGSSQDSTTIDSTPSTIATSTLQPTTSSPITTSAPSLSSALPTTYPSSLSTEVEVEYFTKTITDTSSIVTYSTGVETLYETETITSSEISSIIYNFSTPISGSSFPDGFKPINPTSFPSLTSSTKKIPSTTLPTSSKMITTTTPSVSNNTQSSFLIISTFTSSYEHSEPFKVSSVPLTSNNFSSISHSSASSLPITPSSYLSNTTLHSSVQSSQSSQFTVSVPSSTQSYSTSSNFTTPITISTSLSSFPTTIVSSSFQYSSLSSNVTTTNAQSSSLSSSNSSALTHISSSIVSSGSSSALSSSTIVSSINSSSSVFISSVSSSLQYSSSYVTETTTSGSVGFTTTIATPVGSTAGTVVVDIPTPSWVTETVTSGSVGFTTTIATPVGSTAGTVLVDIPTPSWVTETVTSGSVEFTTTIATPVGTTAGTVVVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLIDVPTPTASSSPFPSCNTQCTNENSFRIQVINDDIYPSYVHLDSNNYAIAAARGDSDGENVFIYDSDIKRIVSCCGVKPIYRLDQDDTEGYSFEIYKDNDGQLQFKYPLNDALYPMELLTLTDGRIGITTNLTLYKPYYLNNVENERAANVVLRALEY
The following text describes a protein:
Function:
Sulfite efflux pump required for the secretion of sulfite as a reducing agent (By similarity). Plays a role in resistance to neutrophils during infection. Involved in transition to filamentous growth, which is believed to be central to the virulence of this human pathogen.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSSSSHNDNKIPPEKTTTPPLSSSNEDIYNPADSSNVLSSNQTLVSTNNNNNNNQNNNQNNNQNNDGKDTMDHLSYLSTIDSKRREQSYLKSFYQRFIIEDVVKNFTPAYFVSVMGTGISSSLLYNFPFPAYWLQICGYVMFGLTCTFFIGNIILLIMSCAYYPNRFRDYHVDPSRAVFMGAFSMGYITIVNFIALITKGEHIYFVWTLWWLAVFSAMYTSFLIVYLSFMSKLNESDVEAKLNATLLLPIVAITVVSSSGHSIELDLPHVHQTVLTMIVSFMLWSLSISMAFMVMTLYMGRLIIHKIPPTNLIMTSFLPVGFLGQSSYSIYLFGNNLNKFIPEELLYGKISLCLSGFVSVFLLSFGYFMCFVAVTSVLSKIRPFAKNPNPSHTNRFGLLKLEKSFWSMTFPMGTMSLSNTEIGHGGVGNYPLLTFKVMGSIFAAACIFITVGCSIGVVVYSFKKLREDMTNKNKYRNESMV
The following text describes a protein:
Function:
Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. Type II pseudopilus confers increased bacterial adhesive capabilities.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MKRARGFTLLEVLVALAIFAMVAASVLSASARSLQNASRLEDKTLAMWIADNRLNELQLEQTPPSSGRNQGELEFAGRRWEWRTQVDSTAEQDMRRVIVWVAAKPLGRERGSIEERAAARLVGFLGSQP
The following text describes a protein:
Function:
Might be involved in ligand transport (By similarity). A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse. Acts in host macrophages to modify the expression of different subsets of interferon-gamma-induced (IFN-g) genes, possibly by chromatin remodeling. Represses IFN-g induction of mouse macrophage MHC class II transactivator (Ciita), greatly enhances IFN-g induction of mouse macrophage inducible nitric oxide synthase (iNOS, Nos2). At least for Ciita repression, acts via mouse TLR2 and MAPK to inhibit IFN-g-induced enrichment of acetylated histones H3 and H4 at the host Ciita but not at Nos2 loci. Host Ciita regulates the expression of MHC-II and other genes involved in Ag processing and presentation, thus its repression contributes to immune envasion by M.tuberculosis. Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse, although TLR6 may play a redundant role, and a partial requirement for CD14 as an accessory receptor.
Subcellular Localization:
Cell membrane; Lipid-anchor. Extracellular vesicle, bacterial extracellular vesicle. Note=Found in bacterial extracytoplasmic vesicles both in culture supernatant and isolated from infected mouse macrophages: there is almost no co-localization of mouse and M.tuberculosis markers in the vesicles, suggesting they do not mix.
Domain:
Forms a U-shaped beta-half-barrel with a large hydrophobic cavity.
Sequence:
MKRGLTVAVAGAAILVAGLSGCSSNKSTTGSGETTTAAGTTASPGAASGPKVVIDGKDQNVTGSVVCTTAAGNVNIAIGGAATGIAAVLTDGNPPEVKSVGLGNVNGVTLGYTSGTGQGNASATKDGSHYKITGTATGVDMANPMSPVNKSFEIEVTCS
The following text describes a protein:
Function:
Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins. Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVVMSSFPPPTEGLLHVQADTQAFMQDRCLGNGVLYIAQERLSWSNEQGQGFSLEYPSISVHAICRDTAKFPHQCIYCMLDSPLEGNDDDEEAVGEVRFVPANISASRFLKHFDTILIIHFFVVQTPGFGGEEYFTNESEAVLTPEGQATLERLEGAFQMPSQQDFEEMTDPNGHVGNGTKIGDVDMEEEDSPGQFEDA
The following text describes a protein:
Function:
Acts as a signaling pathway regulator involved in innate immune system response. In response to interferon IFN-alpha, associates in a complex with signaling pathway regulator NMI to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35 and correlates with IFI35 dephosphorylation. In complex with NMI, inhibits virus-triggered type I interferon/IFN-beta production. In complex with NMI, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of the NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation when actively released by macrophage to the extracellular space during cell injury and pathogen invasion. Macrophage-secreted IFI35 activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Due to a polymorphism at the 3'-splice acceptor site of intron 4.
Subcellular Localization:
Cytoplasm. Nucleus. Secreted. Note=Cytoplasmic IFI35 localizes in punctate granular structures. Nuclear localization increased is stimulated by IFN-alpha. Extracelullar following secretion by macrophage.
Domain:
The NID domain 1 is involved in the negative regulation of p65/RELA transcription and the negative regulation of NF-kappa-B pathway activation.
Sequence:
MSAPLDAALHALQEEQARLKMRLWDLQQLRKELGDSPKDKVPFSVPKIPLVFRGHTQQDPEVPKSLVSNLRIHCPLLAGSALITFDDPKVAEQVLQQKEHTINMEECRLRVQVQPLELPMVTTIQMSSQLSGRRVLVTGFPASLRLSEEELLDKLEIFFGKTRNGGGDVDVRELLPGSVMLGFARDGVAQRLCQIGQFTVPLGGQQVPLRVSPYVNGEIQKAEIRSQPVPRSVLVLNIPDILDGPELHDVLEIHFQKPTRGGGEVEALTVVPQGQQGLAVFTSESG
The following text describes a protein:
Function:
In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Sequence:
MKEISVGLRTDTSGCFLHSRSRICNRVGGGLRQKARGNRDLHLLNSGNLSNCKTQRTMAFAGMLSEENIKAAVQACQAPGTFDFRSFFAQVGLIDSSEADRRKVFTVLDRDESGYIEEEELKLFLQNFFPGARELTGAETKALIAAGDKDCDGKIGMDEFCDLLE
The following text describes a protein:
Function:
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MSGTLLAFDFGTKSIGVAIGQRITGTARPLPAIKAQDGTPDWTLIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVTVTLHDERLSTVEARSGLFERGGYRALNKGKVDSASAVIILESYFEQGY
The following text describes a protein:
Function:
Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Sequence:
MEGAKDAGGDRSAITVQVKFCGRTLPVSLPMDATVADLKSLLQPVTNVLTRGQTLICKGKVLADKVSLKSVPVTNGSKVMLIASQGLHQGDGPITKDAATQSISPRKLIDTKQTQVSHTRTNVEKSRSERWKLTGVVALSECHLEAMPEEVWSCGHSVRVLDVSNNLIRDVPTKVGDLKLLNKLLLNANNITDESISWEGLSSLKSLTILSLSHNYLTTLPSAVGTLTSLCQLHIANNKITSLPDELGLLNQLQILKVANNRLSSMPSSIGNCRALVEIDLSCNLLVDLPETVGNLQDLKALILRNNGLKSLPPTLFKMCYQLSTLDLHGTEITNDFLRQIEGWEDFDERRRSKHQKQLDFRVGSSGVFDEGADDDRALK
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore.
Sequence:
MENPHEKDQSDALARIISGVSKLNSSIARVNEIQEEVYSRNLNLSVVSEIMQNYQASVDYYLRESGAMKEPFKNDD
The following text describes a protein:
Function:
Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGFGDFSTICTKAAIPLCALVGEQQINGGAGIQTNCYSRTIEIANTLIFQCANDFMHILAMVMTVIMIIHVRSKFTAVGRKEITSVFYIYLLLTIISLILDAGVTAPGSAPYPYFAAVQNGLVSALCTCLLINGFVGFQLYEDGTTLSVWLLRLCSLAMFVVSGAVSLLTFKNWAGLSSKNPIGIMIVTYIVNAIFLFVYVVSQIILVVGTLEDRWPLGDISFGVFFFVIGQVILYVFSDTICDNVQHYIDGLFFATICNLLAVMMVYKYWDSITREDLEFSVGVKQHNWEVKELLPDEDKRGTVYQDSDYTPSLYQQQYNGRHSHYSNLGH
The following text describes a protein:
Function:
Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEVDEFGLSKWFESSGIHVAGLVVGECCPTPSHWSAACTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQDGTEPSTLPFLDPNARPLVPEVSVKVPRVFNAGGAPRILALDCGLKYNQIRCLCRRGAEVTVVPWDHALDSQAYEGLFLSNGPGDPASYPSVVSALSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPASWLPLFTNANDRSNEGIVHDSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLAERLCLPGLPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTSGVLARYGVRVLGTPVETIELTEDRRAFASRMAEIGEHVAPSEAASSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNKEELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYNEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHTQLLEQHRGQPLPPDLLQQAKRLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIRQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELESPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPVIDAPALALAQKLAEAGARCDYTLFLGASSDNAGTLGPVAASAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAILMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSRDDLERLGPGKGEVRPELGSRQDVDALWENMAIIDCFASDHAPHTVEEKCGPRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKLKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLTPAAPATSEITTTPERPRRGIPVLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKAAEPDLMGTLDGTCYLPPPVPRQASPQNLGAPGLLHPQTSPLLHSLVGQHILSVRQFTKDQMSHLFNVAHMLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPDVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSAQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
The following text describes a protein:
Function:
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Sequence:
MSSFSFESSARLPLNPRFKQILHATVKSYIDTAEPVGSKMLTQQYNFGLSSATIRNAMAVLESWGLLFQPHTSAGRIPSDSGYRVYVDELISPPTELIQQMRAALAENLGERQDLESLLQGATRLLATLSGCVALITAPQSVFVSVRHLQIVHIGEGRALVIVVTDALQTRSFLLDLPQPEMAEQLETLNNFLNLQLQNRRLDDLNAAAVEAMGGEFHWYTDFLRGLIALLQRVLQPPTGQLYVSGVGEILKQPEFAEPERIQAIVQLLEVERERLGPLISPTQRHSRQIVVRIGAENPLGPMQFCSLVSSTYYLNEVPVGSVGVLGPTRLPYDRAIASVQAASDHLCQVMQAEDEPHRW
The following text describes a protein:
Function:
Acyltransferase; part of the gene cluster that mediates the biosynthesis of siderophore ferrichrome A which is contributing to organismal virulence. The first step of ferrichrome A biosynthesis is performed by the HMG-CoA synthase hcs1 which catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA and acetyl-CoA as substrates. The enoyl-CoA isomerase/hydratase fer4 then catalyzes the conversion of hcs1-produced HMG-CoA to methylglutaconyl-CoA. The acyltransferase fer5 then fuses the fer4-generated methylglutaconyl-CoA with sid1-generated hydroxyornithine to yield methylglutaconyl hydroxyornithine. Methylglutaconyl hydroxyornithine is then available for use by the NRPS fer3 to generate ferrichrome A.
Sequence:
MTAATSVQPSPAPRQPGLRATFNPRKEEKVFLARGAHAFTLPGRRASVNVEVDVEAESDEAALDAKETTITVSYAEKGQESSWSAAKWIKLDRLAKTSQHGVVNEDRATYQQAWSLELLDEAVEPARAIWSALYAFWIRHKRSDRLAVLLKGTQATKVRSYVFEAGLGFKSPCETDLILLDRNAFWQGAGAPAGLHWLQTPVPTRGLFPYVLDFTQSTSPPVLATHPLRPPKPAPGSVVYSRYVFSCSQHLELVHIDVSNPQHFDAYTRWQNSDRVNHGWREKGSDEKHRKYITEKNDDPHAMGVLVLWDGVPAGYGEMVWSKEDGMAAFVGGLGNYDQGTHLLIGEEQFRGKHRFTACMVSLKHACFLRDPRTEVVVGEPRYDLDIIPLLATFLPQEIRKEVELPHKRAVFFVLRRDRFLEEGILE
The following text describes a protein:
Function:
Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response. Modulates plant innate immunity against X.oryzae pv. oryzae (Xoo). Negatively regulates the basal defense responses to the compatible fungus M.oryzae.
Subcellular Localization:
Nucleus.
Domain:
The WRKY domain is required to bind DNA.
Sequence:
MAKMLPPPSQSVPSRPPSWLYIPPRRRHGTFTSSCAFRLSPSSPSSPPPPVLDFQYIQFMDSWIEQTSLSLDLNVGLPSTARRSSAPAAPIKVLVEENFLSFKKDHEVEALEAELRRASEENKKLTEMLRAVVAKYPELQGQVNDMMSAAAAAAVNAGNHQSSTSEGGSVSPSRKRIRSVDSLDDAAHHRKPSPPFVAAAAAAAYASPDQMECTSAAAAAAAKRVVREDCKPKVSKRFVHADPSDLSLVVKDGYQWRKYGQKVTKDNPCPRAYFRCSFAPACPVKKKVQRSADDNTVLVATYEGEHNHAQPPHHDAGSKTAAAAKHSQHQPPPSAAAAVVRQQQEQAAAAGPSTEVAARKNLAEQMAATLTRDPGFKAALVTALSGRILELSPTRTDPSLERR
The following text describes a protein:
Function:
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular Localization:
Plastid.
Sequence:
MAISSAAASTSKLSYPQHIHHSSPSPSSNCLFLKTHTPSTTHLSSSFIHPSTILPLPPAAATTLRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASLGNSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNIVVFLNKQDQFPGGRCSDYLRFRFACFGRLLMANPAIKRGENQWVDKIYELMDAVDNYIPIPQRCFTITGRGTVATGRVERGTIRVGETVDIVGVKETRNTTVTGVEMFQKILDEALAGDNVGLLLRGIQKTDIQRGMVLAKPGTITPHTKFSAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTAITNDRDEESQMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE
The following text describes a protein:
Function:
Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores. Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake (By similarity). Inhibits apoptosis and inflammatory response in cardiomyocytes via promotion of sphingosine-1-phosphate (S1P) and cAMP-dependent activation of AKT signaling (By similarity). Inhibits autophagy induced by nutrient deficiency in hepatocytes via promoting the phosphorylation of IRS1, AKT, and MTOR, and thereby subsequent activation of the AKT-MTOR signaling pathway (By similarity). Negatively regulates the differentiation of osteoblasts, potentially via sequestering BMP2, and thereby inhibits the activation of SMAD signaling (By similarity). The reduction in BMP2 signaling in osteoblasts also results in an increase in expression of the osteoclastogenesis-promoting factors TNFSF11/RANKL and SOST, thereby indirectly promotes bone resorption (By similarity).
Subcellular Localization:
Secreted. Note=Secreted when glycosylated at Asn-243 and Asn-295 (By similarity). Hydroxylation promotes secretion (By similarity).
Sequence:
MAPARRPAGARLLLVYAGLLAAAAAGLGSPEPGAPSRSRARREPPPGNELPRGPGESRAGPAARPPEPTAERAHSVDPRDAWMLFVRQSDKGVNGKKRSRGKAKKLKFGLPGPPGPPGPQGPPGPIIPPEALLKEFQLLLKGAVRQRERAEPEPCTCGPAGPVAASLAPVSATAGEDDDDVVGDVLALLAAPLAPGPRAPRVEAAFLCRLRRDALVERRALHELGVYYLPDAEGAFRRGPGLNLTSGQYRAPVAGFYALAATLHVALGEPPRRGPPRPRDHLRLLICIQSRCQRNASLEAIMGLESSSELFTISVNGVLYLQMGQWTSVFLDNASGCSLTVRSGSHFSAVLLGV
The following text describes a protein:
Function:
Required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis.
Subcellular Localization:
Nucleus.
Sequence:
MSKKITKKDEVEENILNLINKANRPYNYQMIEAAFPSMGKTQIVKTLKSLGEQGKLTFKEYNKAIIYWRIQDTGPKLDEQGYEIPQESIHDLNRKLDGINRQLEVEQDTLKSLISQSKQLNNQLSDEQIQKEVNQLSTENKELESKLLTFQTKEIMSDKDKQRLDDTIKKARSEWVKRKALFRDILDQVLERSNKKKKDLQEDIGWETDEDLKIQMIPDYSKPLSQQTLSSTNDESPFKKQKK