lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May act as a component of the auxin efflux carrier.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MITGKDIYDVLAAIVPLYIAMMLAYGSVRWWKIFTPDQCSGINRFVAVFAVPLLSFHFISSNDPYAMNYHFIAADSLQKVVILVALFLWQAFTKHGNLEWMITLFSLSTLPNTLVMGIPLLKAMYGDFSGSLMVQIVVLQSVIWYTLMLFMFEYRGAKLLINDQFPETAGSITSFRVESDVVSLNGREPLQADAEIGDDGKLHVVVRRSSASSMVSSFNKSHGLNSLTSMTPRASNLTGVEIYSVQSSREPTPRASSFNQNDFYAMFASKAPSPKHGYTNSFQGAVGDVFSLQSSKGATPRTSNFDEEMLKVAKRRGGRSMSGELYNGGGGGGVPSYPPPNPIFAGSTSGGSKKKESGSMPNKELHMFVWSSSASPVSEGNLRHAVNRAASTDFDSSKPTYQQENAASKAMHELIENMGKSSGGDKDLEILEEGSKFPTGGSPLSCQKKLNMEEGEVAKKQQMPPASVMTRLILIMVWRKLIRNPNTYSSLFGLTWSLISFRWNIQMPTIVSGSIAILSDAGLGMAMFSLGLFMALQPKIIACGKSVATFSMAVRFLTGPAVIAATSIAIGLRGVLLHVAIVQAALPQGIVPFVFAKEYNVHPDILSTAVIFGMLIALPITILYYVLLGL
The following text describes a protein:
Function:
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monooxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Sequence:
MPSAAVSVPEVPSSDRKTVYLVTGASRGLGRGLVQAFLLRPNSIVIAGLRNRTSQAGALDALPRGENSSLIAVQLDSGSKSDPADAVSILQRDYGITHLDVVIANAAIAANYGPASTMPLEYLETHMQINAYAALLLFQATRVLLQAAKSPQFICVGAPISTITEMESCARAPLTNYALSKLAACYLVRKIHFENKWLVAYIVDPGHIQSDMGAQAARLFGRKEAPTTIEESVAGICARMTEADKNTTSGRFILFSDGSDVPW
The following text describes a protein:
Function:
Has a role in the establishment of anterior-posterior polarity in tissues during embryogenesis. Required for the alignment of the mitotic spindles and division planes. May have a role in cell death events. Required for normal defection and oocyte fertilization. Involved in sperm function. Operates in pharyngeal pumping during feeding.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The GPS region of the GAIN-B domain is required for signaling.
Sequence:
MRRNKTTYSLLQTILVACLLTVTPTFASNKPTTDESGTISHTICDGEAAELSCPAGKVISIVLGNYGRFSVAVCLPDNDIVPSNINCQNHKTKSILEKKCNGDSMCYFTVDKKTFTEDPCPNTPKYLEVKYNCVVPATTTTTTTTTSTTTTDSSLIVDEEEEAQKDALNSDVIKPVKKKEDVFCSATNRRGVNWQNTKSGTTSSAPCPEGSSGKQLWACTEEGQWLTEFPNSAGCESNWISSRNSVLSGVISSEDVSGLPEFLRNLGSETRRPMVGGDLPKVLHLLEKTVNVIAEESWAYQHLPLSNKGAVEVMNYMLRNQEIWGSWDVTKRKEFASRFILAAEKAMVASAKGMMTSAESNVIVQPAITVEISHKIKMSSQPTDYILFPSAALWNGQNVDNVNIPRDAILKINKDETQVFFSSFDNLGAQMTPSDVTVAIAGTDQTEVRKRRVVSRIVGASLIENGKERRVENLTQPVRITFYHKESSVRHLSNPTCVWWNHHELKWKPSGCKLSYHNKTMTSCDCTHLTHFAVLMDVRGHDLNEIDQTLLTLLTYVGCIISIICLLLTFFAYLIFSRNGGDRVFIHENLCLSLAIAEITFLAGITRTEDSLQCGIIAVALMYMFLSALTWMLLEGYHIHRMLTEVFPSDPRRFTYLLVGYIPPAIITLVAYLYNSDGFGTPDHCWLSTQNNFIWFFAGPACFIFCANSLVLVKTLCTVYQHTSGGYLPCRHDVDSGRSIRNWVKGSLALASLLGVTWIFGLFWVEDSRSIVMAYVFTISNSLQGLFIFLFHVVFAEKMRKDVGHWMYRRGCGGSSNSSPNHKRHNVQRDLMSPGVNSSTGSDFLYNTNDKYLTNSDTTNRLVYNGIMNHPNQMSVYQQHPHHQIYEQQPGTYDYATIAYGDMMPGHRVAAPPAYQRLAVAEGRYGSQHQLYQGWHHRPPPEFSPPPPPLSTGPPNSRHYGTGSSGRRPPSSKMSDDSAYSDGSSSMLTTEVTPQGQTVLRIDLNKPSMYCQDL
The following text describes a protein:
Function:
Esterase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step. The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA. The roles of dbaB, C, E and F have still to be determined (Probable).
Sequence:
MTIRIPSGEEADYTLHLPRILCLHGGGTNARIFRMQCRVLERFLRSTFRFVYAEAPFAAQPGSDVTSVYKDHGPFKAWLRCTAADPDRSAQEVVKKINLSIATAMYDDDMRGATGEWIALLGFSQGAKVAASILYAQQTIQQRLGERAATRPRFRFAVLMAGRGPLVWLLPETSSGPGSIPMGLVDAASPSMLDSEPELPTDSTEHMLRLPTLHVHGLRDPGLSLHRRLLRSYCQSDSVSLVEWEGEHRVPLKTKDVTAVVDQIYALARDTGVLDSWC
The following text describes a protein:
Function:
May be involved in the regulation of mesenchymal cell differentiation through transactivation of NOTCH1 target genes.
Subcellular Localization:
Nucleus.
Sequence:
MNASVEGDTFSGSMQIPGGTTVLVELAPDIHICGLCKQHFSNLDAFVAHKQSGCQLTTTPVTAPSTVQFVAEETEPATQTTTTTISSETQTITVSAPEFVFEHGYQTYLPTESTDNQTATVISLPTKSRTKKPTAPPAQKRLGCCYPGCQFKTAYGMKDMERHLKIHTGDKPHKCEVCGKCFSRKDKLKTHMRCHTGVKPYKCKTCDYAAADSSSLNKHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHTASVLENDVQKPAGLPAEESDAQQAPAVTLSLEAKERTATLGERTFNCRYPGCHFKTVHGMKDLDRHLRIHTGDKPHKCEFCDKCFSRKDNLTMHMRCHTSVKPHKCHLCDYAAVDSSSLKKHLRIHSDERPYKCQLCPYASRNSSQLTVHLRSHTGDTPFQCWLCSAKFKISSDLKRHMIVHSGEKPFKCEFCDVRCTMKANLKSHIRIKHTFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSNPAALRVHSRVHCTDRPFKCDFCSFDTKRPSSLAKHIDKVHREGAKTENRAPPGKDGPGESGPHHVPNVSTQRAFGCDKCGASFVRDDSLRCHRKQHSDWGENKNSNLVTFPSEGIATGQLGPLVSVGQLESTLEPSHDL
The following text describes a protein:
Function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular Localization:
Nucleus.
Sequence:
MQTLTDRLVHRLKELGVTFLQAKCTHLNHKPDCIQVQLNNGLTLDADHVVSAVSSQVLAQLLLPSDMTDIMTYNPSVTVGVVNLVYKGADALPVQGFGYLVPRSETANTDIIGCIFDSSALPDQDSPQDFTRLTVMMGGHMFAKKFGFAPNDKENADLVSGNQLSRKLEKIAVETVQAHLNIPVEKLDAVKAVVLKECIPQYQVGHADRVARLIKYMESDYSGRISLCGSSYYGVGVNDCVHGSRMAPVRVTILFIAVPIDCIGMDSDMHQTIDSSFYKNEVSSNPTIHYSHMADLIRPSTRHTYVADISMSDDPKWTIQPNLMSILTEEFTQESDSGDHTAMLENIQITSPSPVVIALNPQLQSASSLQIHITFKKPVCLEWVQIMQSASRIQELYLDGLYQCTAKAELLSDSDDEESNSRNDHWYLLSIENLDKEISTCTIKFLGLNPTTEFCIASIVVGGSLSSNYTARSIYTSMIEHQPKIQSVVNPDQDSVQVHNNDCTFQATVVLMPITRKSVNFKMNFFVLHEELLLWQEVSTVSTNSFDYEVPVPALSLDETEHILDELVVLLQDDPSSLLQPRPFDTCKSYIKHMRCLTPASADKFSDILISAFGQAIASITLDLAENASHNFEADRILAEKFAFLLVSWIQTATAISKEETTQTSTTVKSLKSKSKLSSLAQDNQQWDWIGQRERIITHLEHLVELELDRLILATSERDVLTSMICKSISLILESPEVLKREPVCIALIDTLCIIATRYETPAQFGGVRSRIEDFLREDNLADFVANLLNSMIANHNNAAFVEIILKDIADRHFTEKDLKAAKTISKLLVKFSEMRPKEFLKSMAFMQCQFDSEIYAIRCAMIEVVGNLIHLHLVNDTSESAAKSLHSYYDILEERLRDVNYYVRAKVLQVIMKLSERRQDAPAVTDIPLDTRHQLVALTINRLQDKASIVRKNAIKLLAHFIETSPFIAIEEDQGRLSLKYFETHKADLLRVMESKYPTEVLEMLIHGTNTTIEEATKGNANDDVSMDASASESDTDAMTIVNEADADTTAQDSSNSNAVNAIDPIQLNDIELQRLRVLLKYYDDGIQFINQINGAVSLLCDLLSSSIKTEVIETMRFFVVAFRFEMESSWEGVRRMVHKIWDKDTTDNESSGIREHVIRCYESLFLDPPEGPRAVEDVIADNLVALTQRMNLAELTSLEQLISTMVQTDRFNMKAVNLLWSIFCKYLLYLCSKHANVPIAKRQGAVMILGMIGKSRKDILLQNIDRLVRNGLGEGDKISLVLSRHTCLTLQHAAANKRQKGSIATRFDRLNVDHAMFQRLSTIILTPTMSLDWFGFCEQAINTIYALAEQPDMIVGSLVKQLACRVFGSMNTATSVPSISTDIMSELSNAISSKLVIGETQSNPPTTATTNSIHLAQLCFLVGHVAIKQIVHLEIIENEWKRRCHSVKNNQTPSKHGATSDLEQTTGTVEDEFTDRVIYVREHELLFGPKSLLGVFGPLLTHICLNNRTFQNPTLQIMSTLALCKFMCVSSQFCESHLPLLFTILERSDNPTIRSNTLISLGDMTISFNFLIDQSIAHLYQRLTDSDLSVRKNTLMVLTFLILNGMIKVKGQIFEMAKCLEDKDKRISDLAKLFFTELSTKDNAIYNNLPDMISNLECVEEDKYRRIMKFLFEFIKQDRQSESIIDKLCARFCNANTERQWQDIAFCLSLISFSTEKSLKKLVDALPMYQDKLHPEKVYKYFTDIIKKVKKIPGKPELKQMVDEYEKTLQELHVKCVENHEAVIKAEQDKKITSHLPKAMVINKQFNRRDELEHSSDEEDKSAEPEVQKELEENDKIENSDSETETVVFDAFPKRTRSVVSKLPKHIGGSPVTRRQINAMGDN
The following text describes a protein:
Function:
May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.
Miscellaneous:
MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIFLNTFARCLLTCFVLCSGTARSSDTNDTTPASAKHLQTTSLLTCMDNSQLTASFFDVKFYPDNNTVIFDIDATTTLNGNVTVKAELLTYGLKVLDKTFDLCSLGQVSLCPLSAGRIDVMSTQVIESSITKQFPGIAYTIPDLDAQVRVVAYAQNDTEFETPLACVQAILSNGKTVQTKYAAWPIAAISGVGVLTSGFVSVIGYSATAAHIASNSISLFIYFQNLAITAMMGVSRVPPIAAAWTQNFQWSMGIINTNFMQKIFDWYVQATNGVSNVVVANKDVLSISVQKRAISMASSSDYNFDTILDDSNLYTTSEKDPSNYSAKILVLRGIERVAYLANIELSNFFLTGIVFFLFFLFVVVVSLIFFKALLEVLTRARILKETSNFFQYRKNWGSIIKGTLFRLSIIAFPQVSLLAIWEFTQVNSPAIVVDAVVILLIITGLLVYGTIRVFIKGRESLRLYKNPAYLLYSDTYFLNKFGFLYVQFKADKFWWLLPLLSYAFLRSLFVAVLQNQGKAQAMIIFVIELAYFVCLCWIRPYLDKRTNVFNIAIHLVNLINAFFFLFFSNLFKQPAVVSSVMAVILFVLNAVFALFLLLFTIVTCTLALLHRNPDVRYQPMKDDRVSFIPKIQNDFDGKNKNDSELFELRKAVMDTNENEEEKMFRDDTFGKNLNANTNTARLFDDETSSSSFKQNSSPFDASEVTEQPVQPTSAVMGTGGSFLSPQYQRASSASRTNLAPNNTSTSSLMKPESSLYLGNSNKSYSHFNNNGSNENARNNNPYL
The following text describes a protein:
Function:
Delta(6)-protoilludene synthase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols. The first step in melleolides biosynthesis is performed by the delta(6)-protoilludene synthase PRO1 which catalyzes the cyclization of farnesyl diphosphate to protoilludene. The orsellinic acid synthase armB produces OA by condensing acetyl-CoA with 3 malonyl-CoA units in a three-round chain elongation reaction folowed by a C2-C7 ring closure (By similarity). ArmB further catalyzes the trans-esterification of OA to the various sesquiterpene alcohols resulting from the hydroxylation of protoilludene (By similarity). The melleolides cluster also includes 5 cytochrome P450 monooxygenases, 4 NAD(+)-dependent oxidoreductases, one flavin-dependent oxidoreductase, and one O-methyltransferase (By similarity). The cytochrome P450 monooxygenases may be involved in protoilludene hydroxylation to elaborate melleolides with multiple alcohol groups, such as melleolide D, which carries alcohol functionalities at C-4, C-5, C-10, and C-13 (By similarity). The role of the NAD(+)-dependent enzymes remains unknown (By similarity). Numerous melleolides, including arnamial, show 5'-O-methylation of the aromatic moiety which may be catalyzed by the methyltransferase encoded in the cluster (By similarity). The flavin-dependent oxidoreductase might represent the dehydrogenase yielding the aldehyde in position 1 of arnamial and other melleolides (By similarity). Finally, several halogenases, localized outside of the cluster, are able to catalyze the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product (By similarity).
Miscellaneous:
MISCELLANEOUS: Armillaria species are both devastating forest pathogens and some of the largest and oldest terrestrial organisms on Earth (Probable). They forage for hosts and achieve immense colony sizes via rhizomorphs, root-like multicellular structures of clonal dispersal (Probable). One genetic Armillaria gallica individual localized in Michigan's Upper Peninsula stands out as exceptionally large, covering hundreds of tree root systems over approximately 75 hectares of the forest floor. Based on observed growth rates of the fungus, the minimum age of this large individual can be estimated as 2500 years.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MSQRIFLPDTLANWQWPRHLNPHYAEVKKASAAWAKSFRAFQTKAQEAFDRCDFNLLASFAYPLADEARLRSGCDLMNLFFVIDEYSDVATEEEVRAQKDIVMDAIRNTEKPRPAGEWIGGEVSRQFWDLAKKTASTQAQKRFIDTFDEYLESVVQQAADRNNSHVRGIESYLEVRRNTIGAKPSFALLEFDMQLPDEVINHPVIKELENSCIDMLCLGNDVVSYNLEQARDDDGHNIVTIAMNELRTDVAGAMIWVDEYHKQLESRFMENFKKVPRWGGPIDLQVARYCDGLGNWVRANDQWSFESERYFGKKGPEIIQRRWITLMPKMVSEELGPQIVDGSHL
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
METHSSEILETDTELVNSVNPRETLDRSSPNSPENSANSNKFEGLQMEEEELDSSPVRRYTPYSSYTSHWSQPWGPITNSKPLGSQLTSTAEPDDDEPSASGWPDGPNKVETTKSVSVGSLWNCHRDDDAKSFMLGAGLANLGNTCFLNSVLQSFMHTVSLIQGLKLNDHATPCDSYLKGFCVICALKELIDALLVSETGVVSPCKFVNNLSYFSSTFHRFQQEDAHEFLQCFLDKLEQCCDVSRPKGSPTLETENFVKQAFGGRLVSKLRCCNCGHCSDTYETLIDLSLEIEDVDSLATALESFTKVEKIEDSEIKFTCEKCKEQVSIEKQLVLDKAPSVAALHLKRFKTDGSLVEKIDKYVSFPLELDLHAYADNNQSDNEEMKYDLYAVIRHVGFSYTSGHYYSFIRSAPNEWYKFDDSKVIQVGEDFVLSQEAYVLFYAKRGTPWFSDFIEVQKPFIDPSILNTSPKSVLDNTDVVCVTSPRPPNPRALCVKGSNDAANELSPNSLNKVQDSDGKENVQTRSAPGPHGASNILHPKSPEVDKVSFPSILKENCSTLDPGAPSRTIYITPKTPSRSPSPEIYREDPPADWVSCKKQLPKELEQNMERKQACTLIKKSMRGSRAQQLPAAMGGSHSGSSVNKKRRRMDVSPSRDDSSSTGRRRSSLGSVFRTVTAGSLR
The following text describes a protein:
Function:
Highly specific D-xylulose kinase which participates in the catabolism of xylose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway.
Sequence:
MTDYSNSKSLFLGFDLSTQQLKIIITDENLTPLDTYNVEFDSQFKSKYTKINKGVITGDDGEVISPVAMWLDAINYVFDEMQKSKFPFDKVVGISGSGQQHGSVYWSGEANELLNDLIPCKELSSQLQDAFSWGYSPNWQDHSTVKEAEDFHKAIGKEHLAEISGSRAHLRFTGLQIRKFITRSHSKEYESTSRISLVSSFVTSILLGEIAPLEESDACGMNLYDIQKSQYDEELLALAAGVHTEIDNVSKEDPKYKKSIDQLKQKLGEISPITYKSSGKISKYFVDTYGFNSDCKIYSFTGDNLATILSLPLQPNDCLISLGTSTTVLIITSNYEPSSQYHLFKHPTLPDHYMGMLCYCNGSLAREKARDQVNKKHNVSDNKSWDKFNEILDHNKDFNGKLGIYFPLGEIIPQAPAQTIRAVLEDNGEITPCELDSHGFTVDDDASAIVDSQTLSCRLRAGPMLSKSSTTKNGKTNSSEELQQLYDNLVDKFGELSTDGKKQSFESLTARPNRCYYVGGASNNTSIITKMGSIFGPTNGNYKVEIPNACALGGAYKASWSYKCELENKMIGYDEYIGKLFDTNDELESFKVDDKWEEYFTGVGMLAKMEETLLKQ
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MYLQRWLFSTNAKDIAILYFIFSTFCGLAGTAMSFIIRMELSAPGQQYLQGQNQLFNVLVTGHTILMVFFLVMPMLIGGFGNYYLPLMIGASDMSFARLNNISFWTLPPTLICLLTSTMVESGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLTTISSLLGTINFIVTALNMRTNGMTLHKMPLFTWSILITAVMLLMSLPVLSAGVTMLLMDRNFNTSFFEVQGGGDPILYQHLFWFFGHPEVYIMIVPTFGMMSHIVSTYSKKPVFGEISMIYTMGSISLLGFLVWSHHMYVVGLDTDTRAYFTSATMIITIPTSIKVFSWLTTIYGGSLRLTTPMLYTLSFLFLFTVGGLTGVVLANTSLDVAFHDTYYVVTHFHYVLSLGAVFSMFAGYYYWSPTVLGLNYNEKLSQIQFWLIFLGTNIIFFPMHFLGINGMPRRIPDYPDTFTGWNLVSSFGSMMTIMSLMLFTYIIYDQLMNGLTNKVNNKSINYMKTPDFIESNNIFLMNTTKSSSIEFMLNSPPTIHSFNTPTIQS
The following text describes a protein:
Function:
Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
Subcellular Localization:
Fimbrium.
Sequence:
MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ
The following text describes a protein:
Function:
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. May be involved in Mg(2+) transport.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein.
Sequence:
MASTIYRLITIVSLLSLLHCAYSAAQHRFYLRLTEQPFINLPSDVVAQTVISLIALIYGTSFLANPFLFIKKDQHHDRSCDEALNCPSFITFDNRAKAMSPEFAMLRTLKQQQRQRQNSSRGTHSGRVSEVIQTEEDSADDSQE
The following text describes a protein:
Function:
Catalyzes the transfer of a sulfo group from 3'-phospho-5'-adenylyl sulfate (PAPS) to the 2-OH position of iduronic acid (IdoA) or glucuronic acid (GlcA) within the heparan sulfate (HS) chain and participates in HS biosynthesis. Required for metanephric development of kidney formation, suggesting that 2-O-sulfation within HS is essential for signaling between ureteric bud and metanephric mesenchyme.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MPIWLTPTAKETNRDTHQERSAGVLRSNKLNRKGVGGGASGCRAAIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRSKLERAIARHEVREIEQRHTMDGPRQDVALDEEDDMVIIYNRVPKTASTSFTNIAYDLCAKNKYHVLHINTTKNNPVMSLQDQVRFVKNITSWKEMKPGFYHGHISYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATELYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
The following text describes a protein:
Function:
Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Sequence:
MHHQRSSGKILCVILQHIMYESEWLKLKQQKWVLSRLWKNSALILPLLCGYLLAMTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES
The following text describes a protein:
Function:
Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis (By similarity).
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target; MISCELLANEOUS: The poly(P)- and ATP-dependent glucokinase reactions both follow an ordered Bi-Bi mechanism, with glucose being the second substrate to bind and glucose 6-phosphate being released last. The mechanism of poly(P) utilization is not strictly processive and is most likely nonprocessive, where there is dissociation of poly(P) prior to complete utilization.
Sequence:
MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH
The following text describes a protein:
Function:
An adapter protein that specifically links the 26S proteasome to its substrate CDC4 which is one of the substrate recognition subunits of the SCF E3 ubiquitin ligase complex. Required for turnover of cell cycle regulatory proteins CDC4 and GRR1. Required for synthesis and nuclear export of 60S ribosomal subunits. Required for vegetative growth.
Miscellaneous:
MISCELLANEOUS: Present with 45900 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAKKSNSKKSTPVSTPSKEKKKVIEKKSSTAIPRERVIKAVNELIKFTSKPQDENNEEGNNGKKNLLEDDEEELKKDLQLIVVNNKSFTGTSKSFKLKLLNVKHSFYKPWKEASATAVKDFKVLLILKDSDIKKVSEDDLFDQLDSEGIKVDEIICGKDLKTVYKAYEARNAFISQFSLILADDSIVTSLPKLMGGKAYNKVETTPISIRTHANKEFSLTTLTNNIKKVYMNQLPVKLPRGTTLNVHLGNLEWLRPEEFVDNVELISEQLIKAYQIRSIFIKTNRSPVLPLYYNQDVLDELEAKKDKIEETHEDDMVTIDGVQVHLSTFNKGLMEIANPSELGSIFSKQINNAKKRSSSELEKESSESEAVKKAKS
The following text describes a protein:
Function:
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MAPIELSSLSSNWKKLQASLQSSKPAESSKHKKFDQGTEQSLKRKRPQTNGSSAHAPSTVVNGNGIHTPRKSSASRKRQKMEEPTSVGASVKHHDTKSLERSVSMPSLKKRPLLTDPTEIVEPVSILEPHPDFPDIENEGVSETALPGKYVAVDCEMVGIGPEPNRDSALARVSLVNFHGHQVYDSYVQIPRKIEVTDYRTAVSGIEPRHLRPDVARPFDEVREDLKTLLTGRILVGHAVKNDLDVLILKHEPKFIRDTSKFSKFRQLALRPGHTPGLKLLADKLLGVQIQVGAHSSVEDARATMALYRLEKAEFEKEIRQKYGNIRLDTADVVKDDGDEEKKKRNRKKSKKKKKH
The following text describes a protein:
Function:
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSWKFLIASITVHLVLIYSIFDVYYTSPLVHGIPPQFINSQEAPAKRIFIISADGLRYDTFNKYPDKSPYLHSIMNERKGIYGLSRSHIPTESRPGHVAIFAGITEDISAVAKGWKKNPVQFDSVFNRSSYSWMWGSPDIVNLFDDLPNAESFSYSADEEDFASKDASNLDKWVFEHFENFLETAKTDEALNDKMREQKSIFFLHLLGIDTNGHGNKPMSRQYIDNIKVVDSGIEKVQHLVDAFFGDHKTAWLFTSDHGMTDWGSHGAGSDDEVLTPFVAWGAGVKQGGPKLDLNQIDLAPLISALIGCPIPVNSMGILPVQMMNSKGSSYEFKAIEANFKQLKEQIIFLKNAKSRRLWFRQFEKFGDKAMESLRTTLAQLGRDRRFSVATSLFADNAHLMKEAIVFYHRYDRQMLGAAVSCSFVAWIALVVSFLHNSTSKENLSLLVPHHLFIIPLACSLLFTAYCSLSMTQTIYIILPIYLISILENHSKLTQRIREHVKALSAQPDWLNKVLSVEVFVKPFLGFVGFSITICIFVLTFMDRAFLAAVFVLLMALPQFYSHPIVSYWSKTWLTLCLVLCIFPFLPAVGVSTHIPLCILSPIITAFLCHRLSRRSCLTRIQRMLELMIYVQSATAFMIAVVNYGFEKFAATVNCSMDLLDLNPTFCDCSVVAHGSISCGSSNCIRLMLLCEKIVPYSLLSISYESLFMLIFLVLLTLFVRFEFGHLSDVELLQLKVDSTKISTGEYVELRRTVVCVSFVLCPLFGTGNFASINSFNPSTLNLFISVFSPFTMAILLILKLLIPILLVTSAFASIVRFDQESIQRLCCFSLIFTDFMSMCFFHQLRDEGSWLDIGMSISQFIVSMCISLALLLLLSISSHLMAFEFRKFPGKRNHQEIESISSRKLSDDESA
The following text describes a protein:
Function:
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Localization:
Nucleus.
Sequence:
MSFITAFRERVFIASGDLIRTFRISEETELKNFISWSKINPERIQKPSFDIEKELKAVEKRVILCLAHSNVLTTHGRRLVAVGTNEKQIHVFEYFVNDKGDIVTAEHIVTSVVPKAPTAIVFDKEDAYVVVGDRAGDVHRFSVLNGSAIEMAGAISMILDVAFSPDGKRLLMADRDEKVRALRYPATSVIDSFFLGHTEYVKTLAVQDNDSLWSSGGDKNLYNWSIAKCSAPRRTLDLSQFDAPIRKISINLQHKKIAVIFEKIETVVIVDLNQESLQTTSVSIVGESQCLDIASTKDYFAVLGRSTVHLIDLNNMEQKFVPIDEELTITLTSTNDAIDNLFKNVTHNNQQEYEKRKADKFEQIEKKKRRLNEDINGDDGEGPGPSNS