lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating.
Miscellaneous:
MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Nucleus membrane.
Sequence:
MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIYYKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDVSVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNSDASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDTNFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCKKSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSESTNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFKMNFGL
The following text describes a protein:
Function:
Plays a role in cell adhesion. May play a role in cell-collagen interactions.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MINRWIHPKVYSRVSRPGEVPTRGGQRGGRAAGVRRARAPRPRSFAARMRRVCGLRERRPGGARRAEPPPPAPPPRGRAGAEEGESAAGSGARVRRSPGGPGGAGRGGAGGAGRRASPPLAAAAYLTGPAAAALSLAQVPAGRSMALLVRLLPVALALALGPAATLGGPARSPYQLVLQHSRLRGRQHGPNVCAVQKLIGTNKKYFTNCKQWYQRKICGKSTVISYECCPGYEKVPGEKGCPAALPLSNLYETLGVVGSTTTQLYTDRTEKLRPEMEGPGSFTIFAPSNEAWASLPAEVLDSLVSNVNIELLNALRYHMVNRRVLTDELKHGMALTSMYQNSGIQIHHYPNGIVTVNCARLLKADHHATNGVVHLIDKVISTITNNIQQIIEIEDTFETLRAAVAASGLNTLLEGDGQFTLLAPTNEAFEKIPAETLNRILGDPEALRDLLNNHILKSAMCAEAIVAGMSVETLEGTTLEVGCSGDMLTINGKAIISNKDVLATNGVIHFIDELLIPDSAKTLFELAAESDVSTAVDLFRQAGLGVHLSGKERLTLLAPLNSVFKDGTPTIDARTKNLLLNHMIKDQLASKYLYHGQTLDTLGGKKLRVFVYRNSLCIENSCIAAHDKRGRYGTLFTMDRMLTPPMGTVMDVLKGDNRFSMLVAAIQSAGLTEMLNREGVYTVFAPTNEAFQAMPPGELNKLLGNAKELANILKYHIGDEILVSGGIGALVRLKSLQGDKLEVSSKNNVVNVNKEPVAEVDIMATNGVVYAISSVLQPPAVRPQERGDELADSALEIFRQASAYSRAAQTSVKLAPVYQRLLERMKH
The following text describes a protein:
Function:
Involved in combinatorial activation of gene expression in pharyngeal muscle. Specifically binds a site necessary for activity of the B subelement of myo-2 enhancer; [Isoform b]: Regulates distal tip cell fate.
Subcellular Localization:
Nucleus.
Domain:
The homeobox domain is required for the induction of distal tip cell fate.
Sequence:
MFNVSALRAATPSIASVSSVASPSEQHGLSTSVGVGVNDTTSRTGDGGAASSASSASAAPQQQSQSALHNKLEAKWDTLLPTDTNLQCSTWPDSIPLLAGYSATPTFSFDPCTYGSYDPSAYFASNGIAGSMYTLPDQFPRSENDMLDNSNTSNGNKSDKDGIKLEDEDEILEDEENDEEDDGTGKRKKRKRRVLFTKAQTYELERRFRSQKYLSAPEREALAMQIRLTPTQVKIWFQNHRYKTKKSHTDKPINAALLTTMPNAFSSQSTAASFPTRAMPIPMLVRDSSARSSDISSTSPYTVAFGSANSGYLPTPSAYLPATSGYFSNGPSAASSYMTNTQWWPS
The following text describes a protein:
Function:
Stimulates feeding behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MRSPYSLPYLLFLPLGACFPVLDTEEPVDAVGGTGREMSWMDPARGRPFPWGSPGWPRAPYPHALLVTAKELRASGKARAGFQLRLGRQDDGSEATGLLLGEAEKVGGLLGTLAEELNGYSRKKGGFSFRFGRR
The following text describes a protein:
Function:
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Sequence:
MVACRSLVRQWPRYLRHPSSLRALSRLSQPRVQTQFVRRGYASISAAELKFGQPLHETHPHLLDPGELTPGITALEYAHRRSRLANKLPKHAIAVLAAAEVTYRASGIFNVFRQDSNFFYLTGFNEPDALAIIINDGSGDNHLFHLYCREKDAKAELWDGARSGTQAAMDVFNADESGDIERISDILPKVLADATEIYTDIPAFNPGRSSLHRFLYGPTGTSEKLKKLVDHSKVKPLRPILNEMRAFKSEEEVVQLRRVGQASGRAFTEAMRHSFTGEKDLSSFLEYNFKLNGCDGSAFVPVVAAGSNALSIHYTKNDDIFKDGDMVLVDGGGELGTYISDITRTWPVNGKFSDPQRDLYNAVLNVHRSCVSLCRESAGLSLDRLHGIAENGLKDQLTQLGFDLSGDALRTLFPHHLGHYIGLDVHDCAGYSRGYDLKAGQCITIEPGIYVPDDDRWPAKFRGVGIRIEDSVCVGDDNPIVLTTEAVKEVLTWCNSQVDDIEALRD
The following text describes a protein:
Function:
Fe(II)/2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Sequence:
MVGSRTWCESEMLFVQPDAGTKEELYYRVTPKPGQTQANFNWTPHKVRFHDARPQRDSFDLNTHGFTFVEDAISPQLIERIRADDTAAVEGDYFASVAALVKRVTGADHVVCFSPYTRKENSEKGIFGQPARTVHCDHTPAAAIELTHKLCGEDAVRLLQSRFRAFSVWRPLVEPVLDWPLAVVDGRTIAPDDLHPVHWLRYEKKDTEPPFQLSFSETQKWYYLSRQRSDEVSIVKNYDSEVVPSPRSAHCAFKHPFVPKDAPPRESIDVRCLVFGGR
The following text describes a protein:
Function:
Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Sequence:
MSSIGKEDIYESDGAASQVQKSEPENDNPTHPDIELISVDVDEALKKYKNRVLNLTSSDFSDSIAKKRRHAFGNNQYVLEVTGAGFSGTETAAEKLNRILYEVADLNEQIRADENLKTDLLNAEVLENLEKEVKTLQVAQSNGKTARVEHDVELPNVRTDSKVATLENRLRRIEQVIGSSVIPSAPVLDTIEDLKLRCETLNHSYVSGLEQRLNMMLTKLEKIDETRANNDIDENLDKKVDEILELMQKWDVACSSLPSNVNKVKALNRLHEQVQHFAGGLSHLKTIREKLEKEVAQGREAIIEYESQGKQEIGSVVEKLKLLEAKVADLK
The following text describes a protein:
Function:
Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to the SPB and also to the equatorial MTOC.
Sequence:
MSEIHVKTALSRLADKYLQNSKNPSVPYTIETIVSFFQEIIHSISPDTFQLDIDDILYKIYSKIPPEENNDALFSKLSNLVSRLKSQTVIHNKSQILYFLYLLSPISQSSRDVSSHLLDESISNPINIPSTEVESSNFGQTRYDQVPENPQITDWDEGLENESSISIAHDSSRLNRSTETSSVQHTLITEADLLSSISYVLQGISTEYVQFKNELALLSKRIPVQYLLQMRALSETGLLYQELKVFSNYDPSVSQSIDGDNVSKAFINDQSLALQSLKSVISKELTNFLALIASLDSQIRADASLEKPMVTIRRCIAWTQVAKLKLRILSSVVNDNMNQENKKRLIQVVSKYNVHGDPLIQELSDKILTEITGPLYEMIENWIYKGELVDPYQEFFVKEKNGSESHDHQGQGDVVWKGKYFLDKELIPSFLSEELVDKIFLIGKSLNFARYGCGDFDWAQEHYQKLVKKLSYRDPHSLETVVDKAYTESINHLVYLMEEVFHLTDHLKAIKKYLLLGQGDFVDLLMESLGNSLDQPANTLFRHNLTASLESAIRSSNASYEPEYVLKRLDARLLELSHGETGWDVFTLEYKVDSPINVIITPYCSRQYLKIFNFLWRLKRIEFALAHSWRRVNLGERNVFRNLDYTKFEWHFVSCHLAEMIHFVCQLQYYILFEVIEISWQELQLAMEKPNATLDTYIEAHEKYVTSITHKGLLGGGKSRNEDSFLHQLHDILKVILNFHDAIELLYNFSCSLSNRIRINVPISTDALAAQYTPIKNELSNFTEEFQVRLQKLLHGLASHKDPEMRFLSVRLNYNEFYVSHRRRHDKDVTSQ
The following text describes a protein:
Function:
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Subcellular Localization:
Nucleus.
Sequence:
MSSTSTASLTPSDPGQDLDIEADLLTTESGFSLAKCPPIYVLPTHLDLDALHQTEETLIQHGARLTYDVAEATLILGKVRQKKRAALELRSRGVWTEEVESTSSHTSGPPAKRRRLESGRNGSAVSEIYLSTEDESEEDGRRLTAHLEHPQLSESKRSERTSVSKLLSKDEGVIRVVRLDWLAQCAEAQTLLPLASFVVYHARKIERPATRGDDETANSQAILDRAKQDAAFKAPFPPSTDKHDRVASHRAPPKLYRQTTSENEEAEPLPPPPEWVRDGVMYACMRSSFLNTPNNAFINQLVKIRTIRELNLDEIGVRAYSTAIAAIAAYPYEIRRGSQILSLPGCDSKIANLFVEFKASESGTLAAAEALDKDPDLRTLHTFYNIWGVGSKTAREFFYARQWRDLDDIVEHGWHSLSRVQQIGVKYYDEFLLDIPREETEAIGKIICQHANSASVRPTAQYDGHGVECIIVGSYRRGKPVSHDVDIILSHRDEAITHNLVVDVVASLESEGWITHTLALHLTTSKRDQQTLPYRGDDDDRNHFDSLDKALVVWQTPKDKLGSGTQASSANTNPHRRVDIIVSPWRTVGCAVLGWSGDTTFERDLRRYAKKAHGWKFDSSGVRERVTGGQVIDLEARGETWQERERMVMEGLGVGWRPPEERCTR
The following text describes a protein:
Function:
Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL5, CCL7, CCL8, CCL11, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL21, CCL22, CCL23, CCL24, CCL25 and CCL26 with nanomolar affinity. Binds to CCL3 and CCL5 with 1:1 stoichiometry. Although binding to CCL25 is observed, does not inhibit CCL25-induced chemotaxis. Has been shown to reduce cardiac injury and inflammation in mice through its anti-CCL5 activity.
Subcellular Localization:
Secreted.
Domain:
N-terminus residues are involved in complex formation with CCL5. A N-terminal derivative peptide composed of residues 37-54 inhibits CCL5 activity in monocyte migration assays, suggesting that Evasin-4 derivatives could be used as a starting point for the development of anti-inflammatory drugs.
Sequence:
MAFKYWFVFAAVLYARQWLSTKCEVPQMTSSSAPDLEEEDDYTAYAPLTCYFTNSTLGLLAPPNCSVLCNSTTTWFNETSPNNASCLLTVDFLTQDAILQENQPYNCSVGHCDNGTCAGPPRHAQCW
The following text describes a protein:
Function:
Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Sequence:
MINSIKTLLLIATLAILSACGWHFQQSVTMPSEWRTLALESDDSYNDFTVIMRRKLQENQVNVVNLEQNIPILRINKQITSDQVASIFKHGREAEKLLMLEVEATFRLANGESYPINAKVNRTFFDNARAALAKSEEREVIWNDMREQVARQLIVKIIALQNQIKRK
The following text describes a protein:
Function:
Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). EJC core heterodimers play essential roles in plant growth and development, and pollen and seed development. The MAGO-Y14 heterodimer selectively binds to the UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript and regulates the splicing of UDT1, a key regulator in stamen development.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA.
Sequence:
MATGGAAGEDVPGGGEFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDTMIRKEVFVSPSVLREARRIIQESEIMKEDDNNWPEPDRVGRQELEIVMGNEHISFTTSKIGSLVDVQTSKDPEGLRIFYYLVQDLKCFVFSLINLHFKIKPIQS
The following text describes a protein:
Function:
May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MELSSRKPYFIEEEEEENLASSLSEMEAGFSGNNNNSNNHGNPQNGVVSSSRFSYGRLNSLRNSQSYYYNQYSVSSPRSVVSGRFHDFRFDIQQPHFLDSCFLCKKPLGDNRDIYMYRGDTPFCSEECRQEQIERDEAKEKKQNLSHSVKSAMRRKEQSSPTRSRDYAFHNGTVAAA
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:
MASQSPTARIYLLLYNSINALLWLRILITVLRAYSQNLDVISLPTLYTVLEPQVRWTQTLAVAEILHAAIGLTRSPVFTTFTQIFARSVQVWAINYGFPAVTASSRAYAAMLFAWAVADAVRYSYFVVLLAGLHVPSVLRWLRYSLFIVLYPIGISAEWWLMYRAAGVTSSSLVAGIFYFCLGLYAPVFYPADKSGSIMMYSYMLRQRRKTLAK
The following text describes a protein:
Function:
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Sequence:
MRRFTVLSLFSLAACSLLNYEDIFAYPKYSFVWSTDELTKERAEQLVQETPETQNTQYLRVGNEEFLCTYPQWKGVIETFNNGASHSTDDEVVEQGLQAIRTLGGVCLLDPNGYWTYEYCHDTSIRQFHYEDDKQAAQNYYDLGIAPVIERSSIGAWTVRKSGTKRSLQIEWINGTKCDLTGKPRQTLVQYECVDDGDAPRIAWYTELSTCSYSMTIHVPALCGLEPFRRSDLSDVQNIVCHPVVEVATSTKEEDDEKEEKESAPNEDAVTNVDESKPVSTSISSVSLPSSSSVSIDEL
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of quinones. Exhibits a low enzymatic activity with beta-naphthoquinones, with a strong preference for the ortho-quinone isomer (1,2-beta-naphthoquinone) over the para isomer (1,4-beta-naphthoquinone). Also displays a low reductase activity for non-quinone compounds such as diamine and 2,6-dichloroindophenol (in vitro). Involved in the generation of reactive oxygen species (ROS).
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Major isoform under normal light conditions; MISCELLANEOUS: [Isoform 2]: Major isoform under UV light exposure. Undergoes rapid proteolytic degradation by the proteasome.
Sequence:
MLAVHFDKPGGPENLYVKEVAKPSPGEGEVLLKVAASALNRADLMQRQGQYDPPPGASNILGLEASGHVAELGPGCQGHWKIGDTAMALLPGGGQAQYVTVPEGLLMPIPEGLTLTQAAAIPEAWLTAFQLLHLVGNVQAGDYVLIHAGLSGVGTAAIQLTRMAGAIPLVTAGSQKKLQMAEKLGAAAGFNYKKEDFSEATLKFTKGAGVNLILDCIGGSYWEKNVNCLALDGRWVLYGLMGGGDINGPLFSKLLFKRGSLITSLLRSRDNKYKQMLVNAFTEQILPHFSTEGPQRLLPVLDRIYPVTEIQEAHKYMEANKNIGKIVLELPQ
The following text describes a protein:
Function:
Controls the pigmentation pattern of the adult cuticle and larval mouth parts.
Subcellular Localization:
Secreted.
Sequence:
MNPLGMLSLGLMVCLIGAFSRIASAKLEEKFSWKQLAFDWPTPEAEAEAKSNGHYIVENNLPLGVERWQNRIFVTVPRWKAGVAATLNYIDINSTEKSPKLHPYPSWEANKLPIDVQPQDQKTPSGGRLDADKAQDAGIQLKDNSTVISTFRIQVDVCDRLWVLDTGLADILGSPKQITPNSILVFDLKTDTLLRRFTIPADQTKEDSFFANIVVDADRSECQDAFAYIPDLGAYGVIVYSLRNDKSYRVKHNFFHFDPLHGDFNVGGVNFQWTDGVFGLAVGPMNPDHSKDIYFHALASTKEFKVSNRVLQNESHVTAGDSYYDFKYVGDRGMNGQSTAEVFDPETGVIFYTQVNKDAIACWNIKRPYTPDTQGLIDSDSHTLVFPNDMKIDNEGTIWVLSDKMPTYLYKELDPSAVNYRILMGQNRDLIKGTPCEM
The following text describes a protein:
Function:
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MKITKIINYNNFKITNVWGGIISKASHFSTQHGQYDKSERICNFGFQKVSEEIKSRLVYNLFSNVCNKYDIMNDMMSLLVHRFWKDQFVKELDILLKYHSYNIQDYVYQHYKDHSSNNEKIQKKNENTSDTNGYSNNYSVYSDIPNYKILDLAGGTGDIAFRILEKSKFYLKKNNQSIPFDHISYQQYLPHIIVCDVNNDMLNVGKKKAATLGYDQNLTWLVQNAENLESVESNSIDVITLSFGIRNFTNIPQALKEIHRVLKPGGRFLCLEFSKVQCHIFNIFYKFYLNNVIPIIGKVVANDMKAYKYLAESIQTFLTPDELAQLFHQANFKNITYTTMTMGIVSIHSAYKLV
The following text describes a protein:
Function:
Transcription factor that plays a critical role in response to various stresses and reduces the stress through transcriptional activation of its target genes including multidrug transporter FLR1.
Subcellular Localization:
Nucleus.
Domain:
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD and c-CRD, respectively (By similarity). A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD (By similarity).
Sequence:
MAEVDNGGAQKSSASRKKRYQELDPETRMKRVAQNRAAQKAFRERKERKMKELERKVVDLENLTKLNEVETNFLRDQLSILVKELRKYRPETKQDHKVLKYLEKHKGGAAGAGNGAATGSVSTSTRHTDLAASNANRVSKDSSILPGAKIIRQDLESFNENRHFNVTGQLTPPGNTSSSTTANSVAANAKKQSIPHSDSSDSNESKNTWNTDPTSSEDWLDDVMTSHKQISRGQSGSGIDFNNFFDEQVSEFCTKLNQACGTKACPIPQSKSAATTPLPGTSSNGNSNSPMIINDTMGDVSLNMQGNEHGNATNNLVTDPAFLSNTWDDMSPASNQHSTGGAPGFGQLGFGDNLLGNDILFSPNSPAYSPSVLGSGRTQEVYRSPAVQKVVEKENESKSVNFPFINSSLAFPGDYDNNFFRETTDLNFDDNDQDDNFTNSNDLVNDYFTTNIPDTDNSDSALIANGLVKEEPSMQTEDTFKVQNTNDMLNSSRMKETIDNQNIGEKTTKDDNEDDDEDDENDNTVVPSRDDGLLRCSEIWDRITAHPKYSDIDIDGLCSELMAKAKCSERGVVINADDVQVALNKHMS
The following text describes a protein:
Function:
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Subcellular Localization:
Nucleus.
Sequence:
MAENQAPPKGARVDDATRRELRRELHQACQDVHRQKEVLCDISTNRLVEVIRHSETLLDKAEGIQKAKEVAVSAEIFRNLADCNNELANKLVQKQGRGPMDLIVKLRAAFVHTANPQVDGAEDPTAFNWGELGAFVEHLRRPARGASCMFGPMLVQPKERKAPAQRQKRQAPAELVRPEEKDCMVEGSEEKQDTDRNMEVMWGVIKAQNSPLVGFPELVLNAASFAQTVENMFTLSFLVRDNRVALVEDEERGWCVQPLEGGKAKGAQQPPQQQQQHAPQLQFIMSFHLKDWEAMKCYVRPSECLMPHRDKAAQHERDKAAAAAEERATKKARQHERAA
The following text describes a protein:
Function:
Component of the type III secretion (T3S) injectisome that translocates effector toxins into host cells, facilitating the establishment and dissemination of infection. Polymerizes into flexible and regularly twisted fibrils and plays an essential role in needle assembly.
Sequence:
MDISRMGAQAQITSLEELSGGPAGAAHVAEFERAMGGAGSLGGDLLSELGQIRERFSQAKQELQMELSTPGDDPNSLMQMQWSLMRITMQEELIAKTVGRMSQNVETLMKTQ
The following text describes a protein:
Function:
Nucleoporins may be involved in both binding and translocation of the proteins during nucleocytoplasmic transport. In S.pombe it is required for the nuclear localization of retrotransposon tf1.
Subcellular Localization:
Nucleus, nuclear pore complex.
Domain:
Contains F-X-F-G repeats.
Sequence:
MPPVSKNTRTSSKTVKKPYDPPQGSSRPFFTVLKRAFSSVLHPFTSGLDEKASGTASKDRKSGRAGTKSLLTPELTPHYLGKSPRIIRVSNRSHVRTIDGIEEKVHTNTFEPRKPKQKQDYTNSPTLFKRHDELSLKSLNSLHPSSALSKKLGSTSQHQIATPKSSASLLNILRSLHDEQKNTLNISSVKQDRITEANPTCEKRKPSRSPSPMLSKKKSVARASENEPSAKQNKSFSGNDSHKSLTDIRDKENGETEVSAKNHVPHRSSRRRRRHQRLIPIIYETLEQMDLRKPVLVNAEVQTDSNPGNTMFIDKQDIYHRLSTPTSRKRQTLEKGHIKAFSAVDEDLDEIFACEDDVHYTALPKQNPKSERILEPIIASPKDNTSDKGLLTKSAPTFEELQASITPKPVKTSPNDTALTLANAEDNKTFEHQPLSKDTEAPKSQFSSSPTKESTTRKSEVEPPSPSKEIKSSHFSVPEFKFEPKTEATTDKKLNVPKFEFKPTATADVQTNRLKENEPKPTFFAQLPSKTQETPSITENKPSFFSQLSPKREETEKKDNAPSAPASTSGFSFGGFAPKTLEEKEETKAPTFNFSLNNASSTQDTTKPTLQFNFGSSFGKPTSNIFNDKKTSENGLASSTVASESKPSAPESKPSSGFGNTAGSSPFSFNLTKESKEVPPTNSFSFAKKGKDEANDSLSAKASTPFSFAKPNTENVTTTAPQFSFNFTKPNTDAKTNLLPEKTFNEEAVKQKETEKEVPPTGPKASEIKDSVSSNNAVPSSTFNFVSPFAAVSEKTNENNIPNDTTKTNGNATKRTLEQTEDAKPFAFSFGSTTEQANKKASTSNETTKPQLDTSSKTDGVTANAPFSFASAFNAPKPSTNTADGKDSASNLTTPSPAFSFGNNSGVKASSNNNPSTNSSTAPFSFGTSNKPAFSFGSATSKTTSEGTAPAASASAPAPTTSAFSFGASNSSMNKEENTPMAKDAGDTAPASGFKSGFSFGANNSPQPASMFGTSTPAPSSAFAFGNQSGTNPAAPAGFGGITNTATNNPPSTGFTFTPSNAGSTAAPMFGAGNTPNPSGSINNASQAFAFGSGEPSNPASNPPSTGFSFGAATPSAFNASASQSPAPNGIQFNLGSSNSQTNAPPGRKIAVPRSRRKR
The following text describes a protein:
Function:
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Subcellular Localization:
Cytoplasm.
Sequence:
MITLSLAEIAEVVGGRMHDIPDASAEVTGPVVRDSREAGPGSLFVAFVGERADGHDFAARVVEAGAVAVLGSRPVGVPAIVVDDVQAALGALARHVVRRLGTTLVALTGSAGKTSTKDLIAQVLRRKAPTVFTPGSMNNEVGLPLTALTATDETKFLVLEMGARGIGHIRYLTELTPPKIGAVLNVGSAHIGEFGGREQIAQAKGELVEALPPAEEGGAAILNADDPLVRAMASRTKAKVILFGESGEADVRAENVRLTDTGQPSFSLHTPSGASDVTMRLYGEHHVSNALAAAAVAHELGMSADEIATALSEAGSLSRWRMEVTERPDGVTVVNDAYNANPESTKAALRALVAMGKGRRTWAVLGKMAELGDEALAEHDAVGRLAVRLNVSKLVAVGGREARWLQLGAYNEGSWGEESVHVSDAQAAVDLLRSELRPGDVVLVKASRSVGLESVATALLETGAEGEVAAR
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSATQDRHGPGTSNLAPLPLNSALLSPWDFLRPTKKLRTEVLDTAKIFLDSLASSVCDSQNTRQRNSKKRKRPDDDHHAASILRLRQLYVDGFTSDQVWEQALRIFNSADQEIQRDYTVCANNRQPGSSEESPSEDGINSLRDASDEPEDILEDFSDDNEQGGERDGEAEDSSQSDLEESEDGVHQTEEDPYDEEDENLGTYIEDRFGLNDGFFSIDDFNKQTELFEQRDARGDVEDESDEEDINWHANPLDARGPSTLSQKQEKAVGVDDDLSGSDDDASEEEGPTFDNMAELDSEDEDVTAAAGAGFSNTSDIMYADFFAPPPRKASAKKSRPLPKTQPRITDNDIDRAMADVRRDLFDDDEASVQDSDNEPGVGRTHQSTHEKQRARIADEIRRLEAANVAKKEWMVSGEARAAERPVNSLIEEDLDFERVGKPVPVVTTELSESIEELIKRRIIAKEFDEVIRRRPGLLDRQLTQKARVEIEDSKPQQGLAELYETDHIRTTDSNYVDPKHQKLLKEHTEITNLWKEISSQLDTLSNWHYKPKAPQASINVVTDVATITMEDAQPTAGGAIRASAALAPQEIYAPSETTRATGEIVMRDGVPVTKEEMTREDKARFRRRQKKMAQASANSNQPRSRKALEKQQIVSDLKKAGVKLIGKEGDMMNINGSKIVGTVDRNGAHAIKL
The following text describes a protein:
Function:
Low affinity sodium-dicarboxylate cotransporter that accepts a range of tricarboxylic acid-cycle intermediates with 4-5 carbon atoms. There is no interaction with monocarboxylates.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MARKRGISSLLLIYKQSFVIWGALLIFSPLLMFVGDSHGLQAKCLYCVAVMGSYWVFEALPLAITAFIPMILFPLFGIMRSEEVARAYLPDTCFLFMGGLMVALAVEKCELHARVALFVLKTVGSEPARVMAGFMGVTGFLSMWISNTATTALMVPILQSVITELVSNHRMEDLVALCEAHHNSSRKHSVGMRRLSLPNENNEIKREEMDTAMSPREQKMAKGLMLSVCFSANIGGAATITGTASNLVLVGQLNELFPGADTGVNFLSWLIFAFPMVFCCLIYCWCVLYLLYLRDAPKGSIIVTRKLQQKYNELHAFSFAEMAVIFCFALLLVLWILREPQVVPGWGEMFKDEFVSDATSAMFIVILLFTLPEKLPSSRGSSEQRKASSGLLDWATVQDRFPWSVLFLLGGGFALAAGVKESGLSHDIGAIMRYLDVFNHNIIMLICIIISVTLTNVCSNTVIASIFIPIVAELARSLEIDPLNFMLPVTISASFAFLLPVATPPNAIVFSSGYLKVFDMFVSGLCVTLGCVVLSMLNMLLWAGFVFNLHLFPQWAANPSPPLDVQDWAVENNITFVGTSKL
The following text describes a protein:
Function:
Regulates the expression of several genes involved in acid resistance. Required for the expression of gadA and gadBC, among others, regardless of media or growth conditions. Binds directly to the 20 bp GAD box found in the control regions of both loci.
Sequence:
MIFLMTKDSFLLQGFWQLKDNHEMIKINSLSEIKKVGNKPFKVIIDTYHNHILDEEAIKFLEKLDAERIIVLAPYHISKLKAKAPIYFVSRKESIKNLLEITYGKHLPHKNSQLCFSHNQFKIMQLILKNKNESNITSTLNISQQTLKIQKFNIMYKLKLRRMSDIVTLGITSYF