lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase MAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of MAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of MAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active MAP1.
Miscellaneous:
MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
Sequence:
MSALRNIKFNEEEDGELPCLVTGEENNLQEILENVSYDGGNIVSDAKVERVNKQVENTSAGATDVHEKKRIPVSIITGYLGSGKSTLLEKIALKGADKKIAVILNEFGDSSEIEKAMTIKNGSNSYQEWLDLGNGCLCCSLKNIGVKAIEDMVERSPGKIDYILLETSGIADPAPIAKMFWQDEGLNSSVYIDGIITVLDCEHILKCLDDISIDAHWHGDKVGLEGNLTIAHFQLAMADRIIMNKYDTIEHSPEMVKQLKERVREINSIAPMFFTKYSDTPIQNLLDIHAYDSVRISDILDSGSGNGTIHDDRMGTIMLTFRPLKNEEEYNNKFIKQFLQPLLWKNFGAMTVLGGRRRDDGRDWEVQRTKGLILIEGENPIARVIQGVRDTYDVFPGKYDGSNKECKIVLIGKYLEKESIEELLRKTLE
The following text describes a protein:
Function:
Probable methyltransferase.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MGILKKTIFIGGIYGLGVYIGAVAWRLRKDVLNYESRQKSDLLIPNSNSISIYNQIADKYSRKITREEIFSGIYFLRYFLLRNAKGDVLEVGSGPGTNFPFYKWKKINTLTLVEPAEKMREIADARAKKKVPPNVLYRQFADLRQLPPNQSYDTIIQTFCICSQEKAVEQLNNYRSLLRSDGRILLIEHGKGKYKFLNRILNAYAESHYESWGCVWNRDIEQLLEDSELTIDSCKRFNFGTTYVIEAH
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular Localization:
Cytoplasm.
Sequence:
MPFLENCLKLQNVAVVSKVGNKESEKAAIDVAKKLLAKKSKVYTISPIQVEGAKQIETLEELKKVKLDLVVTLGGDGTTLRVFRNLENETPILTINVGGNRGILAEITIEEIDDALNQIQKDKFFLDKRTRVVASCGGKEFPPALNEIFINRANLTKTAEIEIKFQNDTVKQKMDGVIVATPSGSTGHSFSLGGPILHESLDVLIITPVAPVYRLESIVVPDEKIEIISSHDCNIVMDAQVVKSAGFEEPITIKKYKKPAVFIRLKKRGLRQMSKLGF
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPVRKMDLQVVDLIFKVGKIFTITPSSLLQTSPNKIHSCFIVVTYIVVTSLTYKISHVTYKQLTSVQYILAIFSLVAVYTHDFYVFIFVRCWRNFWLDLSRGLRKVNNRKNRRKVHYFWFIMSQLFLLVECVFGLVYYTYFTNYQLAFLMFVNFFRRYFQMFFLILRCILLDIILGKYRQQLWTLESKVPQTRKVGRDLYVLKKTIDVFNDIFGWPCFTNIFSASITVLITLDVFIKSNGHFTYDTRTMTEVLNQMLHMIGICSYWICITINILLCDAVLKEFDKIEELVSELKLRKNRFGHKFILLNRIILHNRPEFKAADFFSLHKSTLFGITYSITNFLLIMIQFKPS
The following text describes a protein:
Function:
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Sequence:
MEAKSRSLSLEGFTFEESWEEKKKRAEKIVEILMKTHPREKLLIGDPYRTLVHCIISQRMRDEVTYRVWEELFKKYKDIETIANTPVEEMQEFLRKQGVGLWKTKGEWIVKASKIILERYGGKVPDDIHELMKLPGIGRKCANIVLAYGFGKQAIPVDTHVNRISKRLGLAPPRVAPEKVEEYLTALIPKEKWIYVNHAMVDHGRSICRPINPKCEECPLREFCPYAKGLVTDEDIKGNARKPTRR
The following text describes a protein:
Function:
Represses the expression of the alkB-rubAB operon, which encodes the alkane hydroxylase AlkB and the rubredoxins RubA and RubB. Acts by binding to the promoter region of the operon. In addition, EMSA analysis show that AlkX can bind to the promoter region of mmpS1 and mmpL3 and to the intragenic region of mmpL11, suggesting that it may participate in the regulatory network that controls the expression of MmpL lipid transporters.
Subcellular Localization:
Cytoplasm.
Domain:
Contains an N-terminal DNA-binding domain and a C-terminal ligand-binding regulatory domain. The C-terminal regulatory domain can bind saturated fatty acids.
Sequence:
MSTPSATVAPVKRIPYAEASRALLRDSVLDAMRDLLLTRDWSAITLSDVARAAGISRQTIYNEFGSRQGLAQGYALRLADRLVDNVHASLDANVGNFYEAFLQGFRSFFAESAADPLVISLLTGVAKPDLLQLITTDSAPIITRASARLAPAFTDTWVATTDNDANVLSRAIVRLCLSYVSMPPEADHDVAADLARLITPFAERHGVINVP
The following text describes a protein:
Function:
Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MNEFEDIIYPGPSHVTTNIEFEDENIENNENYLNLVQILKELVDNNLKEEIEFKPMVGGVTNTLFKSSFITGQGSNKSVIIRLYGKGSEQFIDRKTEANIQYLLSKNGVGPKFYGTFENGCIYGYVEGDQLQLEDLYQNNILSLIAKETGRWHSLKLDINSNSQLLLSSSSDSSIKESTTISTSTSTSTSTSSTSPSTSPSLENSTLSPRNMNTQTSSTSLFKNLNSWINNAMTLTSKESKGSMISKINLNRYKEEAMSLMSFIEEHYSGEEYINFCHNDLIPRNMIYNKEKGQVKFIDFEYSGYNFRGYDIGNFFCEFSGLDLDYTKYPSIEIQKRFIKNYLISINNCKNIQQKQKQKQQQQQIQNSINDENMDIENDELLYEPSKEEIHNLYIESNHLTLGSHLMWGFWGIIQHFSSSIDFDYIDYAIKRFKQYDLVKNKVLSLK
The following text describes a protein:
Function:
Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6.
Subcellular Localization:
Cytoplasm.
Sequence:
MDESVRYDRCHQVQLGVFNESQLSSVEEDVQNLPQQGTGNILFTHDGVLLKKASAEHIADLNTSGSLSLVEYSRSIAEMPRRRLLLEWQPNDSIMIADDSQDQGDWALVDRISGRTRTTSECRAFNTRPIEPSGGATTRSRVMRAQLEDLSSVEVRHRGQTIRFMRKGANGVHSEFFFQHGNADLFVRSMRDQHLIENAETSRSGGEVYAILTTENQKLKKTFAELDIGQIKASQLPRESWLPNKLAGILGNIPDYVQPPFQRSPKSRPGVLISGDRQTSPDNYQIIGLSGSTNSACSSNGQSRGGSAEKSPADSELETLNAQDEKIVNNLPDRQRVERGHPLTETQWLEFQTPDGRISDSARIKELIFRGGVVQSLRPEVWKFLLNYYLWSDTHVERIERRKQKSIEYYNMKAQWLAMTTTQEANFCGYRERKCQIEKDVKRTDRSLQFFAGEDNPNLTLLQGILMTYVMYNFDLGYVQGMSDLLAPILEIQVNEVDTFWCFVGFMELVFTNFDIDQAGMKTQFAQIRRLIEFANAPLFNYMRSHDSDNMYFCFRWLLVWYKRELNSEDVLKLWECLWTRLPCPNFHLLFSVAILDQETRVIIDSQYEFTEILKHVNELSGNIDVQKTLQVAEGIYLQLKGSETLPNDIRSIIGEPLLPAAAGEEIDGGMVDEEPTYSDDGFDELVKELTPEEKVRQQALLEEACERSLFLQFH
The following text describes a protein:
Function:
Minor protein component of the vitelline membrane. Involved in vitelline membrane biogenesis during late stages of oogenesis. Required for efficient disulfide and non-disulfide cross-linking of several vitelline membrane components.
Miscellaneous:
MISCELLANEOUS: The name 'palisade' was given because of the disruption of the palisade-like arrangement of vitelline bodies and follicle cell microvilli within the perivitelline space during vitelline membrane secretion.
Subcellular Localization:
Secreted. Secreted, extracellular space, extracellular matrix. Note=Secreted into the perivitelline space by follicle cells and becomes incorporated into the vitelline membrane.
Sequence:
MMMHSRNRSWTLTLLALGVVLATSAEDLPRSNRIAVPGEPLYYLMADAGPVVTPNEALKRTNRSLLKWWDDLFPRNNNNCCNNNNNNLLYPTAPLLPAPAVPNNCNGLQLQDLDPFKQMKLFKKLPELFPTASPCGQCGGGCGQNNYVAPAPQSPSYGGDGYGVLPNGGYIKPDTEYNGPGDGDAGYVAPAAPAYEAPAPPAPAYEAPAPPAPAYEAPAPAAPAYEAPAPAAPAYEAPTTDYSAPAPPAPAYEPPASSYTQGYSQPAQPSYVGAPPAQIVYQPIIYLSTPLASKSSTSQVEYDDQKYVTPTAPPPPPPPAPVYEAPSQNCYQPAAPPAPNYATPSCQTPIRLSLIDQPYRVAPELFEEYNYRLALASQNIL
The following text describes a protein:
Function:
Acts preferentially on the c-Jun N-terminal kinase (JNK) and p38 MAPKs. Plays an important role in the heavy metal stress response and in axon regeneration by negatively regulating the kgb-1 (JNK-like) and the pmk-1 (p38-type) MAPK signaling pathways.
Sequence:
MTVLDTVTISTCGLAALIREAPDTTLVVDCRGFTEYNESHVRHSMNAFFSKLIRRRLFENKLDDNCLIHQLMSCSSGCTKMDEKLDLVLYAEEDKPRGNKRRIASCNAPESTAKIMRVLRERLEDTDKFRSVMVLEGGFKQFAQQYPQLCESSEGMTRLPQSLSQPCLSQPTGDGITLITPNIYLGSQIDSLDETMLDALDISVVINLSMTCPKSVCIKEDKNFMRIPVNDSYQEKLSPYFPMAYEFLEKCRRAGKKCLIHCLAGISRSPTLAISYIMRYMKMGSDDAYRYVKERRPSISPNFNFMGQLLEYENVLIKDHVLDYNQASRPHRHMDYYGPSDLCPPKVPKSASSNCVFPGSTHDESSPSSPSVSEGSAASEPETSSSAASSSSTASAPPSMPSTSEQGTSSGTVNVNGKRNMTMDLGLPHRPKALGLPSRIGTSVAELPSPSTELSRLSFNGPEAIAPSTPILNFTNPCFNSPIIPVASSSREVILTLPTPAASSSSSTSSEPSFDFSSFESSSSSSIVVENPFFASTEVPAGSSSISTPSGSQSTPASASSSAASRCRMKGFFKVFSKKAPASTSTPASSTPGTSRAARPECLRSSGIIISAPVLAITEEEDAESPESGFNEPEVGEEDDDSVSICSTSSLEIPCHQ
The following text describes a protein:
Function:
Transcriptional repressor of a subset of early mesodermal genes including myod1 and t/bra. Binds DNA on N-box motifs: 5'-CACNAG-3'. Acts as a negative regulator of myogenesis, mediating Notch signaling to repress expression of myod1 (By similarity).
Subcellular Localization:
Nucleus.
Domain:
Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG); The bHLH, as well as cooperation between the central Orange domain and the C-terminal WRPW motif, is required for transcriptional repressor activity; The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins.
Sequence:
MPADLMEKNSSSPVAATPASMSNTPDKPKTASEHRKSSKPIMEKRRRARINESLGQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRVQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTDVRTRLLGHLANCMNQINAMNYPTQPQIPAAAAPHPAYGQPLVQLQGAAPQSSPAPIACKMGGPPVEAAKVYGGFQLVPAPDGQFAFLITNPAFPHNGSVIPVYTNSNVGTALPPSVSPSVMPSVTADSVWRPW
The following text describes a protein:
Function:
May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Mitochondrion.
Sequence:
MNRLSPRAAVLCQGAVRGLCVSSRQGRESVAKPCSEEEAALYVHWPYCEKRCTYCNFNKYIPRSDNEAAIRSCLVQEARTLIRLSQVHRITSVFFGGGTPSLASHGTIAAVLEAVSQTALLPQDAEITLEANPTSAERSRLQQFQKAGVNRLSVGVQSLDDQELLLLGRTHSTSEAQKTLEEACNLFPGRTSVDIIFGLPGQSLASWHRTLRQLLDICDDHVSLYQLTLERGTSLFKMVQDGRLSTPDMEVASQMYEDARRTLSESGFRQYEVSNFARNGALSAHNMSYWLGKQYIGIGPGAHSRFVPRGSGGQQRQARIQTLEPEPWMKEVMHYGHGTRKVTELNDLDVLSETLVQGLRTDIGITHERWQQIVPSLSLYHVFGASQEIGELRQAGLLVLDERGLRCSWKGLAVLDSLLLPLLTQLQEHWAQRETGTF
The following text describes a protein:
Function:
May regulate transcription elongation by RNA polymerase II. May enhance transcriptional pausing at sites proximal to the promoter, which may in turn facilitate the assembly of an elongation competent RNA polymerase II complex.
Subcellular Localization:
Nucleus.
Sequence:
MGGGHHHAAQVPASLGRDLRACLRCRLVKTYDQFNKNGCENCKFFHMEQEHDRILECTTVNFSGLISSMDPTGSWAARWLRISKFVPGCYALAVSGVLNEDMQNICEDNNIKYVPR
The following text describes a protein:
Function:
Could serve either a nutritional or an osmotic protection function.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKKDTRKYMIYFFGALGGLLYGYDTGVISGALLFINNDIPLTTLTEGLVVSMLLLGAIFGSALSGTCSDRWGRRKVVFVLSIIFIIGALACAFSQTIGMLIASRVILGLAVGGSTALVPVYLSEMAPTKIRGTLGTMNNLMIVTGILLAYIVNYLFTPFEAWRWMVGLAAVPAVLLLIGIAFMPESPRWLVKRGSEEEARRIMNITHDPKDIEMELAEMKQGEAEKKETTLGVLKAKWIRPMLLIGVGLAIFQQAVGINTVIYYAPTIFTKAGLGTSASALGTMGIGILNVIMCITAMILIDRVGRKKLLIWGSVGITLSLAALSGVLLTLGLSASTAWMTVVFLGVYIVFYQATWGPVVWVLMPELFPSKARGAATGFTTLVLSAANLIVSLVFPLMLSAMGIAWVFMVFSVICLLSFFFAFYMVPETKGKSLEEIEASLKKRFKKKKSTQNQVLNERTL
The following text describes a protein:
Function:
Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform 1; MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
Subcellular Localization:
Nucleus envelope. Cell membrane; Single-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region.
Sequence:
MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS
The following text describes a protein:
Function:
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions (By similarity). Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MASGQMAPSLLRRPITFVSSCPPALRSFGALCPPTGSTDLIGGTGRDILIAAAPARRAPLHATLPLLRSLHTSPAPQLSASHQHQAQQQQQQTKQPQQPYDPQQDQVPSTSTASSSKPAADPVYNLPNAVSVARLVSGPLIGYWLVQGHYEAATLALAVSGASDWLDGWLARRLGASSVFGSYLDPLADKVLIGCVAAALLMNGAMPGWVAGVVVGRDVLLVAGSFVFRLRGFGWRWPGAAAFFRTVDTSAAAAGAATGAANGVASGGGGGGEGVSFMRPLLISKANTVLQLLLLGGYLLRGMDGGAGLQLLLPGGGGEELIMGLELATAATTVASGLAYGTMAVQGKLFK
The following text describes a protein:
Function:
Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity).
Sequence:
MVRVMVVIRIFGTGCPKCNQTYENVKKAVEELGIDAEIVKVTDVNEIAEWVFVTPGVAFDDVIVFEGKIPSVEEIKEELKSYLEGK
The following text describes a protein:
Function:
Catalyzes the 14-alpha demethylation of obtusifoliol to 4 alpha-methyl-5 alpha-ergosta-8,14,24(28)-trien-3 beta-ol.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MDLADSQQQRLIAGAALLVATVAFFRFLLRSRSGGKRLPPTIPGAPVVGGLVKFMRGPIPMIREQYARLGSVFTVPIISRKITFLVGPEVSAHFFKGNEAEMSQQEVYRFNVPTFGPGVVFDVDYSIRQEQFRFFTEALRANKLRSYVDQMVVEAEEYFSKWGESGTVDLKYELEHLIILTASRCLLGREVREKLFDDVSALFHDLDNGMQPISVLFPYLPIPAHKRRDRARARLAEIFATIIKSRKASGQSEEDMLQCFIDSKYKNGRPTTEGEVTGLLIAALFAGQHTSSITSTWTGAYMLRFKQYFAEAVEEQKDIMRRHGDKIDHDILAEMDVLYRCIKEALRLHPPLIMLLRQSHSDFTVTTKEGKEYDIPKGHIVATSPSFANRLPHIYKNPDSYDPDRFGPGREEDKAAGAFSYISFGGGRHGCLGEPFAYLQIKAIWTHLLRNFEFELVSPFPENDWNAMVVGIKGEVMVNYKRRKLAVDN
The following text describes a protein:
Function:
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair; ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin by shifting nucleosomes. Regulates transcription upon recruitment by YY1 to YY1-activated genes, where it acts as an essential coactivator. Involved in UV-damage excision DNA repair. The contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Involved in DNA replication. Required for microtubule assembly during mitosis thereby regulating chromosome segregation cycle.
Subcellular Localization:
Chromosome. Cytoplasm, cytoskeleton, spindle. Nucleus.
Domain:
The DBINO region is involved in binding to DNA.
Sequence:
MASELGAGDDGGCPELAKPLYLQYLERALRLDQFLRQTSAIFNRNISSDDSEDGLDDNPLLPQSGDPLIQVKEEPPNSLLGETSGASNSGMLNTYSLNGVLQSEPKSEKGNLYNFSKLKKSRKWLKGILLSDESSDTDSPSEEDGDDEINLTREELHNMLRLHKYKKLHQNKYSKDKELQQYQYYSAGLLSTYDPFYEQQRHVLGPKKKKFKEEKKLKAKLKKVKKKRRRDEELSSEESPRRHHHQTKVFAKFSHDAPLPGSKKKHLSIEQLNARRRKVWLSIVKKELPKANKQKASARNLFLTNSRKLAHQCMREVRRAAIQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNYYKAQALKNAEDAYQIHQARTRSFDEDAKESRAAALRAANKSGTGFGESYSLANPSIRAGEDIPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFSRFVPRFKVLPYWGNPHDRKVIRKFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRRIKKDVENELSDKIEIWMYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTQQAQNTTSSLMNLVMQFRKVCNHPELFERQETWSPFHITLKPYQISKFIYRHGQIRVFNHSRDRWLRVLLSPFAPDYIQQSLFHRKGVNEESCFSFLRFIDVSPAEMANLMLQGLLARWLALFLSLKASYRLHQLRSWGEPQGESQQSPQYLRNKDFLLGVDFPLSFPNLSSCTLLQSLVFSSHCKAVSGYSDQVIYQRRSATSLIRCCQVTELPSFLCVASPRVTAVPLDSYCNDRSAEYERRVLKEGGSLAAKQCLLNGAPELARDWLNRPSQFFPQPPGGLWSIRPQNGWSFIRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQNRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRANEKSEIQQMVISGGNFKPDTLKPKEVVSLLLDDDELEKKLRLRQEEKRQQEETNRVKERKRKREKYAEKKKKEDELDGKRRKEGANLVIPFVPSADNSNLSADGDDSFISVDSAMPSPFSEISISSELHTGSIPPDESSSDMLVIVDDPASSAPQSRATNSPASITGSVSDTMNGISLQEMPATGRGHSGRSRGRPKGSGSASKGTGKGRSRKSTAGSAAAMAGAKAGAAAASAAAYAAYGYNVSKGISASSPLQTSLIRPAGLADFGPSSASSPLSSPLSKGNSVPGTPKSLNVTSSLTPDPLIRKQGKGPNPPGGR
The following text describes a protein:
Function:
Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Miscellaneous:
MISCELLANEOUS: Lacks the EAR-like motif (Domain I) which is one of the conserved features of the Aux/IAA family.
Subcellular Localization:
Nucleus.
Domain:
The N-terminal half of the protein contains the conserved domain II which is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Sequence:
MNSFEPQSQDSLQRRFHQDNSTTQQPRDTTTPFIPKPASKNHNNSNSSSGAAGRSFQGFGLNVEDDLVSSVVPPVTVVLEGRSICQRISLDKHGSYQSLASALRQMFVDGADSTDDLDLSNAIPGHLIAYEDMENDLLLAGDLTWKDFVRVAKRIRILPVKGNTRQVKRNE
The following text describes a protein:
Function:
Component of a complex that acts as a quorum sensing protein regulating discoidin gene expression during growth and development. Its function in the complex is unclear as it has no ability to induce discoidin during growth and development by itself.
Miscellaneous:
MISCELLANEOUS: According to PubMed:15947191, it is secreted in the conditioned medium. However, prediction tools clearly predict a transmembrane domain. In some conditions, it may be cleaved and secreted in the conditioned medium, which would explain the discrepancy.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Secreted.
Sequence:
MNKKIIILIYLIFIKSIVGQNPVWIGGSGCNLFTDSSCWSPSTSPLTTDIVTMGVDSTQTVVDGDITITTLINNNLTLGGVEMSSTISLEIIDTSLIVSGAFSMATNSRLSLSLSDSYANSLVSGSATRNAVNVLMNLQSMQTLMVGSSFTMTGNSVLDVNRSISTINGVFTMNDDTSLFMYSKQNGDSKFTVGNSVLNDASSLNFQGQSFIFFNQTNLPSGLVLNDQSKIVAIDADNVKISGVVTLNDQSSIQLTSSRLYLDSLVTATTSSILVNNSTLSILQSIPTTFSPASAVFKGSVFTIKSNCTIQSPITMIDSVYSFNQSHTLASQFTGSNVYMIMDAAILNAGNYYDCSGCSLSMRNSIANFDSYENQGDLILSSSKLNSNAPITSNTGSIFGYYGELNQALTVESGSLGVYNEKTRLFVNGNVIVESGAKIQFYLSSPLDFSWLNTSGSLDVQSGTIIEIYVYIEILNNGSMEVIKTSNGFVTPLSTDNVKLYTYDPDNDVITDFSTTGGCEYSISITNTSVLVHTDYACQQAIITLGTDGISKGSLAGISVSMVALACFVSLGVWWKTSKKNDQRNDSQVLTNFSQNKSDDIDVERKL
The following text describes a protein:
Function:
Acyltransferase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics. The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain. EasB produces several polyketides that can be further processed by the downstream enzymes. The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD. The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA. EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues. A last step of cyclization leads to the production of emericellamides.
Sequence:
MEETNVKLSVPLSEDVIKLSALDQQIMRFYAKAVFIFERDSSKTSIDIVHHLKQGLAVTLSEIPDLAATIAPVPNSHRKDLELRIGPNSGVPFKVVDQTKQESWVYGTYPDLAAKHFPTSDIPHDILFIPQPQPSADGLPAAFLQVNIIDGGVIIAISWHHSVCDARGISILIDAWARHTATSLANGKPDLPATPAEGSRDRWRLDHGLREVTIDQLPEYTIDSSAREDPSGSYLLDRENPVTVPYSVSTWYFSASSLKALRDALAQVENDESTQFTKVEAVSALVWKHMSIARQLDRSNPDGSSLFTTRLDFRARTKPPFPDTFIGNINEPTARVRLPIAEICRASTPESLTTLAEAVRAATENTTEQSMRTLIGLVNDAPAVTDVAWKYNYFPGPDLGVTDISNIDAMKKNWGAGLGTPTCVRSYSRETGLLYLFPQDDDGGFEIQVQCEVEAVERLKADETFTRYCEFKRASAYNA
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Sequence:
MAKKSIEKKKPVQTTPQQKEEDGSINLKLNYTIDEIVVDFESFDKKYECNVCCNYILDTNIRVARQCPKGHYVCMECWERILKSKKECPHCRTKVESVPALSRNIFLENEFNELLVHCPFSKEGLVKNGLSFNITTSTNDNIKINKICDCKVKFKDLDNHLRNKCHRIIKCCCGAYFKKENHPDHIKQCPESKISCENCLKPISKSLYENHKTECSEFFIGQIKALQKCNFPDCNIELPMYQMGKHMESHVNSLYTMIKDLSIRIDENKLDHQKFPDEYSYQNEEKYLQIVKENKILREKIENNEMVGVWTIQDYRISNFITSKSFNMSDLRFKVKLG
The following text describes a protein:
Function:
Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly.
Sequence:
MPPEMEIIEATNEELLLGFKLIKSPTDGFTDSVKFELKQTFADSSYARSITSLAVQWPWVASGGTDGRIFVYDMRTRKQSQIILSHAGRVNTLKFTPDLSLLLSGSDDGHMIATRVGSWTKEYDWQKAHAGQAVTHVSCHPSSKLALSLGGDQVLNTWNLVNGCVAHKTNLKNKATLDFQTGCLSWSKQGDHFTLSGPLVLEIWGIENAHVMRRIEMPSKPICITWLDGNECLTGLDNGNIAWISLKDEDDTPPTFILAHEVRVKAIAYLNEFLATVSIAGQIKVWKIDMETRKLEEIARSFMDCRPTDLGLLDLRQFGNVRPVEQRTKVEEKPKAKVESDQSAKPAAPRGFVTIEYEQDKKLDAEKKKEKKKNKKDEESSEESNSSEDKENDDFSDSDSDVSSDHGHRKRKPMKREQQPTPASKGKAKQQKKK
The following text describes a protein:
Function:
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Miscellaneous:
MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MSRIDDLQQDIESLLSEINSLEESREKLKAKIKDKRKNEESANPIVQEFEDLFDQFPQLNNFLFNEHPELEETDDKDISRAQADIPATPIPYEPKKRAKLENEEILPEQEWVLKTQPMVQHQMFDPGVADLLDTDILTSPSKRKRKLKIDDISTSDRSELEDYIVLENVYRMFGITFFPLVDPIDLKIKDASGEIFVDREMLGIRLEVFSERTSQFEKPHYVLLKKRIKSNSWFLFKHTIPSFIDVQGIFDDTNGGLVISHDDAYLFAKRVFLQLVEVQKRRQIFKDLEAKKIIHDLDLDLESSMVSFFVKDIKVELFVKQNEIVSCSILDDIHDFSQNNKSKWEIALLGSLDDLELKLNHSFATIFK
The following text describes a protein:
Function:
Mediates 1-deoxy-D-xylulose (DX) phosphorylation in the cytoplasm prior to the translocation of 1-deoxy-D-xylulose 5-phosphate into plastids. Can also phosphorylate D-xylulose (Xyl). Uses preferentially ATP as cosubstrate.
Sequence:
MPELSLPQDSYFLGFDSSTQSLKATVLDSNLNIVASELVRFDSDLPHYKTKDGVYRDPSGNGRIVSPTLMWLEALDLMLQKLSKPNFDFAKVAAVSGSGQQHGSLENAFSIKESPIWMDSSTTAECRAIEKAFGGALELVHVTGSHAYERFTGPQIKKIFDTRPEIYSSTERISLVSSFMARMNLMDIKSWSKVALEATAPGLESKLGELAPAYAVAGNIAPYFVERYHFNKDCLVVQWSGDNPNSVAGLTLNIPGDLAISLGTSDTVFMITKDPNPGLEGHVFPNQVDAEGYMVMLVYKNGSLTREDVRNCYADKSWDVFNKFLQQTQPLNVGFHRYIIENFSGTPDGLKEKEVRALIEGQLLSMWAHAERFGMPSPPKKIIATGGASANHCILSAIASIFGCDVYTVQRPDSASLGAALRAAHGWLCNKKGGFLPISDMYMHKLEKTSLSCKLSVSAGDQELVSKYATLMNKRIEIENQLVQKLGRC