lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MDYFSVDLFYNFVFAFLASVCRVIALIIYENQSEPYMDEIFHVSQARQYCNGNFSHWDPMITTLPGLYLASIGSLKPIDVLFDVKTCGNLYWLRCINLIFCLATLYIISIIVVKLQKQNEIISSWHTSLLALNITTFPVLFFFNFLYYTDAGSTFFVLLSYYFHLSNVHSLAACMGAVSIIFRQTNVVWVVFLFWLTLIPVLNGQRRVIGRNLNGSKYELEFTSDPVSNIKLILKNIIHTNMKFMLALVEDFVDHLFPYCIVIIAFLIFLWFNNGIVVGAKLDHEASFHCSQLLYFFAFSFFFFLPLISVSNTLSDFLKHIKKRTTFIVASVIAITTIIHYTTMSHKYLLADNRHYIFYIWKNVFQKHWCIRYLLAPVYLFAMYSLWRLFKSINVLWKFGFICCLAAALVPASLIELRYFIIPFLFLRLNVPYSQSYFKILVEFMFYNVINACTLTIFVKKTFKWPDSDEIQRFMF
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB; this reaction does not require ATP in vitro. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. Displays ATPase activity in vitro, which is modulated by the oligomeric status of the protein.
Miscellaneous:
MISCELLANEOUS: The four proteins YwlC, TsaD, TsaB and TsaE are necessary and sufficient for tRNA(NNU) t(6)A37 threonylcarbamoyladenosine biosynthesis in vitro in B.subtilis.
Subcellular Localization:
Cytoplasm. Note=Localized predominantly at the cell poles and at the periphery of the bacterium.
Sequence:
MKQLKWRTVNPEETKAIAKLTAAFAKPGDVLTLEGDLGAGKTTFTKGFAEGLGITRIVNSPTFTIIKEYNDGVLPLYHMDVYRMEDESEDLGLDEYFHGQGVCLVEWAHLIEEQLPQERLQIVIKRAGDDEREITFTAVGNRYEMLCEELSRHDNISN
The following text describes a protein:
Function:
Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Subcellular Localization:
Cytoplasm.
Sequence:
MKTLFIDRDGTINKDCPYCHNPSDLFIYPDAVDLLQRYQDDGFRIIIVTNQSGIGRGYFTESQFKEFSDFMNDKLKENGIVISAIYYCPHKPEDSCNCRKPETGLFSEVLEDYKVDIPSSIVVGDRNEIDGEFARRIKLPFRLLRH
The following text describes a protein:
Function:
Appears to function during host infection, and may play a role in suppressing the host immune response.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Host nucleus. Host cell membrane.
Domain:
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (By similarity). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
Sequence:
MRVLKFLSLMAMLGCTIGQSGSATPGSLHLLGGPTTTDWYPECALRCWENTKYVTKCSEDQQCLCSDVNYQNSVFQCIYSQCDTVHFGSALHHAIAQCLGTDNEVFFAIPPIPDRDALRRREDEYAAGAKLFGSGSAAGYPTESAAFPVQSANYPTDSVGGPYSPSPTASVPFPYFSLTSVTSPAAKSATTTEATRNTVPASTTAPSPSPQLYTGNASTSRATVSLTVVLTVAAVYLVL
The following text describes a protein:
Function:
Catalyzes the CTP-dependent phosphorylation of phytol to phytylmonophosphate (PMP). Can also use UTP as an alternative phosphate donor, but not ATP or GTP. Is involved in tocopherol biosynthesis, via the utilization of phytol generated by chlorophyll degradation. Also plays a significant but not critical role in the recycling of phytol for the biosynthesis of new chlorophyll molecules.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGIEQNNPMALPLWIAVGLAATYLGAVVLTAELLNRLSLSPAEVTRKIVHIGAGQVVLIAWWLSIPGWVGAIAGVFAAGIAVLSYRLPILPSLESVGRHSYGTLFYALSIGLLVGGFFSLGLPIFAAIGILVMAWGDGLAALVGQRWGRHRYQVFGFRKSWEGTLTMVLASFLVTVVFLSYTFGFTVIVLVVAGTVAIASAGLESFSRWGIDNLTVPLGSALIAWAGSYLWLG
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.
Miscellaneous:
MISCELLANEOUS: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin; MISCELLANEOUS: Present with 16228 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL
The following text describes a protein:
Function:
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Miscellaneous:
MISCELLANEOUS: In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Subcellular Localization:
Nucleus.
Sequence:
MPSLISLKSIRPFNRDFLFSNTLHIRRTLKELLEVTHKPMLDMVNMDLPTNGVVADERKFEAYIYKLNDRLTQCGMHSRIPPNSSDVTSGGPCPRNLAISLGHIAYRFAIPDANELRHYAAGSSTIYGEINLEQMASFVDELNIGPNDHFMDLGSGVGQLVSFVAAYAQTKKSVGVEIMPNLAQMARANEQFSKSLLRHFGKTVNPTRLVHGSFTSPDIVHEIQNEATVICVNNIKFSAELKLELKMILSKCADGTRIISSESIAPRPRSQNSTSSRVDEFVRISTERPLLLVESNTSWTGNTVPFYLTEIKHNQ
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MVHLLQCSGSSHMPLPLFFLSVLLLLPSVESAHSDAGRLPLMLLEIGSSKEEEGGRRGEMMKMERRGLIGSRPPRCERVCMSCGHCEAVQVPIVPQDHKQRAGREHHDAASDIGAAMLAAYRVNGGISDYKPLSWKCRCGGMILDP
The following text describes a protein:
Function:
Component of clathrin-coated vesicles. Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle.
Sequence:
MELAHSLLLNEEASNQLGDVQKAEFVFEWLRYLEKLLLATNRDDVREKQKALVEQLLSLLSSSPGPPTRKLLAQNLAILYSIGDTFSVYETIDKCNDLIRSKDDSPSYLPTKLAAVVCLGSLYKKLGRILANGFTDTVGNILKAVKSAESQGRYEIMLSLQSILTGLGAAAAPCHRDVYKAARSCLTDRSMAVRCAAAKCLLELQNEAIFMWSTDLDSVATLCFKSFEGSNYDVRISVSKLLGTVLAKAVIAKHPGGASRQSTRRVSLEEVLELLGAGFLRGSSGFLRASGDMLKGSSSVSRDVRVGVTQAYVVFVSTLGGAWLEKNLAVFLSHILSLVSQSNPKATQTQIDAVCCRRCVSFILRATIGGLLGEKAQIAAAKDICQAIWKLKKVMDAVLSDGNLETRLSSTDVAASQHMLVCALQELGNLIHSLGTTAAPLLQDSSTGLLDSVISVVLHPSISVRLAAAWCLHCIAVALPSYLTPLLDRCLERLTTLKSSPEAVTGFSFAVAALLGAVTHCPLGIPHGKGKIIMTLAEDLLCSAAQNSRLSLQRTQAGWLLISALMTLGPAVVSHHLPRVLLLWKCVFPVSPKDLETERSRGDSFTWQVTLEGRAGALCGRLTAISLLPGLPSHFVCPVGFMLSSILKTYGSSLKTPSVVYRQRLYELLILLPPETYKGNLCAILKEVAAELTAPDSQVAASACLLPALCHPDDLLILSPLLQETDHRFIEEQLLFGNGIACGSLEYDPYSIYEKDVEGDSVPKPLPPALSVISSASKLFGVVCANVDEAQRVLILDQLLNSIKHTKGARQQTVQLHVVSAISNLLKYVAGSKQSLGPEVRRLVLTLVLGALESPNPLLRCAAAEAWARLAQVVDDGAFTAGLAQVSFDKLKSARDVVTRTGHSLALGSLHRYLGGIGPQHLSSCIGVLYTLSQDSTSPDVQTWALHSLSLTIDSAGALYHVHVESTLSLIVMLLLNVPPTHAQVHQSLGRCLNALITTLGPELQGNNTSVSALRTSCLLGCAVMQDHPGCLVQAQAISCLQQLHMFAPRHVNLSSLVSCLCVNLCSPYLLLRRAVLACLRQLVQREAAEVSEHAVMLARDNRDNNPAADTNLREVGLEGALLALLDRETDGSLCQDIRETLHHMLTSMAVEKLSLWLKLCKDVLAASADFTAVTCVDTMQEEEGDRGDDASVLTRGDDKPHPFSNPRWGTRVFAADCVCRIISQCENANSAHFDIALAQEMKKSDSRNDFLVLHLADLIRMAFMAATDHSDQLRLSGLDTLLVVIRRFADIAEPEFPGHVILEQYQANVGAALRPAFTSETPPDITAKACQVCSAWIASGVVSDLGDLRRVHQLLVSSLMKIQAGKEALSQLYNESASTMEVLAVLKAWAEVYIIAVQRHKNHKQTLKTTINSEDSVRSGSASAAGLLDLVCTDLATLSRLWLAALQDFALLTLPAEFASQLPVEGGAFYTAETSKSATPHYHNSWALILHAAALWLTSTGFADPDEGGANLSRPVTPTSMCQGSSSSGPAVKSPEDVYTDRFHLILGISVEFLCSLRSDATLESITSCLQALQALLDAPWPRSRVGSDQDLGIELLNVLHRVILTRESPAIQLASLEVVRQIICAAQEHVKEKRRSAEVDDGASEKETVPEFGEGKDTGGLVPGKSLVFATLELCVCILVRQLPELNPKLTSGPRDKASKPKTLSEEGSRLVAAALVILAELPAVCSPEGSVSVLPTILYLAIGVLRETAVKLPGGQLSSTVTASLHALKGILTSPMARAEKSHEAWTSLLQSALATVLDCWSPVDGAHQELDEISLLTAITVFILSTSPEVTAVPCLQNRCIEKFKAALESKDSVVQMKTCQLLHSIFQYPKPAISYPYIYSLASSIVEKLQEMDRRRPGDAAELQLCQEGIKLLEALVTVADEEHRAQLVACLLPILISFLLDENALGSATSVTRSLHDFALQTLMQIGPRYSSVFKNVMASSPALKARLEAAVKGNQESVRVDPSSKQAKNLGRNSSIQLKTSFL
The following text describes a protein:
Function:
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Also plays a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand.
Miscellaneous:
MISCELLANEOUS: Interaction with FSFFV envelope-like membrane glycoprotein gp55 results in constitutive tyrosine phosphorylation and activation of isoform sf-Stk; MISCELLANEOUS: [Isoform sf-Stk]: Lacks part of the extracellular domain, oligomerizes and is constitutively activated. This isoform confers host susceptibility to Friend disease.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MGLPLPLLQSSLLLMLLLRLSAASTNLNWQCPRIPYAASRDFSVKYVVPSFSAGGRVQATAAYEDSTNSAVFVATRNHLHVLGPDLQFIENLTTGPIGNPGCQTCASCGPGPHGPPKDTDTLVLVMEPGLPALVSCGSTLQGRCFLHELEPRGKALHLAAPACLFSANNNKPEACTDCVASPLGTRVTVVEQGHASYFYVASSLDPELAASFSPRSVSIRRLKSDTSGFQPGFPSLSVLPKYLASYLIKYVYSFHSGDFVYFLTVQPISVTSPPSALHTRLVRLNAVEPEIGDYRELVLDCHFAPKRRRRGAPEGTQPYPVLQAAHSAPVDAKLAVELSISEGQEVLFGVFVTVKDGGSGMGPNSVVCAFPIYHLNILIEEGVEYCCHSSNSSSLLSRGLDFFQTPSFCPNPPGGEASGPSSRCHYFPLMVHASFTRVDLFNGLLGSVKVTALHVTRLGNVTVAHMGTVDGRVLQVEIARSLNYLLYVSNFSLGSSGQPVHRDVSRLGNDLLFASGDQVFKVPIQGPGCRHFLTCWRCLRAQRFMGCGWCGDRCDRQKECPGSWQQDHCPPEISEFYPHSGPLRGTTRLTLCGSNFYLRPDDVVPEGTHQITVGQSPCRLLPKDSSSPRPGSLKEFIQELECELEPLVTQAVGTTNISLVITNMPAGKHFRVEGISVQEGFSFVEPVLTSIKPDFGPRAGGTYLTLEGQSLSVGTSRAVLVNGTQCRLEQVNEEQILCVTPPGAGTARVPLHLQIGGAEVPGSWTFHYKEDPIVLDISPKCGYSGSHIMIHGQHLTSAWHFTLSFHDGQSTVESRCAGQFVEQQQRRCRLPEYVVRNPQGWATGNLSVWGDGAAGFTLPGFRFLPPPSPLRAGLVELKPEEHSVKVEYVGLGAVADCVTVNMTVGGEVCQHELRGDVVICPLPPSLQLGKDGVPLQVCVDGGCHILSQVVRSSPGRASQRILLIALLVLILLVAVLAVALIFNSRRRKKQLGAHSLSPTTLSDINDTASGAPNHEESSESRDGTSVPLLRTESIRLQDLDRMLLAEVKDVLIPHEQVVIHTDQVIGKGHFGVVYHGEYTDGAQNQTHCAIKSLSRITEVQEVEAFLREGLLMRGLHHPNILALIGIMLPPEGLPRVLLPYMRHGDLLHFIRSPQRNPTVKDLVSFGLQVACGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARGVLDKEYYSVRQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYPHIDPFDLSHFLAQGRRLPQPEYCPDSLYHVMLRCWEADPAARPTFRALVLEVKQVVASLLGDHYVQLTAAYVNVGPRAVDDGSVPPEQVQPSPQHCRSTSKPRPLSEPPLPT
The following text describes a protein:
Function:
Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.
Subcellular Localization:
Cytoplasm.
Sequence:
MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFETA
The following text describes a protein:
Function:
Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs.
Sequence:
MTEDRNFDDIAHKFAKNIYGSDKGEIRQVIVWEDLEQLLSQLDTQKVPLHVLDAGGGLAQVSQKIARLGHRVTLCDLSSEMLQLAEQDIANNGLLEQYRFVHSPVQTIQAHLDAPVDLVLFHAVMEWLAEPKPALQNLLAQVRPGGMVSVMFYNYHGLVYKNAVCGNIPHVLEDMPHRKRFKLQPQKGLLPEEVYQWIEESSFEICGKSGIRCFSDYIGNMKNMGEYQYEDLVALERKFCRQEPYLSLGRYIHVWAKKKQ
The following text describes a protein:
Function:
EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
Sequence:
MAAFPNPNSNAGLKKLDEHLLTRYYITGHKASKDDITVYAALSKHPPSQYVNVSRWYNHIETLLGISGISCQGSGVSIDGLVSTSEHAVAGSNDGVAVVDNDKDVDQDVDLIREDTQKEKKSAEERATSTKKKICWESVLIVIIPQDCQTNMKKLEERLRTIQMEGLIWGASKLVHVGYGVELLRIIATMPRNEKIDVFDVLVGDYISFLGRFNVATAGLHQSLVLINPNDEETDMKKLEETVRSIQVAGLFWGASKLVSIGYGIKLLGIECTAVGHLAHLGRRVGFNTIFKEKIMDHPYVQSCQTLSLNIISGKSGLVLRKLFGDNPDIKKTEETVRSGQMEGVVWGASKIYNVGYGFKYMRTIFTIVDDQLSLDTVTRNTGGIPLNRICKRQKPFLNSLKLLM
The following text describes a protein:
Function:
Required for normal DNA replication. Phosphorylated in response to DNA replication stress. Phosphorylation allows it to mediate the activation of RAD53.
Miscellaneous:
MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Note=Associated with chromatin during S phase.
Sequence:
MDDALHALSSLTAKKRTTTYKKVAVPILDENDNTNGNGPNDIDNPPELTGNGFLFANATLNRVKNRLEGKKAPEQNHNNGKDRSENSLPTQLISNLYDGGEELEKSEVKDNSYSEKNVSSSFTQTQRIPVSIQQDKVFNVPIHSVNDGKPTQLIKEDGLVNETSQALKTPLTTGRPGATQRIDSSGATSQTQPIKSIEPQSQIITTSSNHSNALSPKIPIIPTELIGTSPLFQSIQNRGPDTQMDVPPQTAHDEDKTQAIGIPQATHQEQKTQIDTVAQTLQDEVPHTLKIREIQSELASEDSKREKARNVEYKKPQKPIPTKKFFSKESFLADFDDSSSNEDDDIKLENAHPKPVQNDDELHENKSVELNLTDETRINEKRVPLLSSYANNLKREIDSSKCITLDLDSDSDEYGDDDMDSIKLSKDESVLPISQLSKATILNLKARLSKQNQKLSQRPNKSKDPKVDHNVLLNTLRKASRKQILDHQKEVIETKGLKLEDMAKEKEIVENLLEQEILRNKRIRQKEKRREKLEENDFQLNAHDSGSDSGSESSGFALSGNEIADYESSGSENDNRRESDSEKEDDEIILKQKKSHHVKHIINESDSDTEVEAKPKEKADESLPKRIAINLGHYGDNIGEDTDKFQETNVLDTQNIEEVMAERNTIENEVKDDVYVNEEADEAIRRQLIDKEKLQLKQKEKEHEAKIKELKKRGVTNFFEMEAEESEDEWHGIGGADGEGSDDYDSDLEKMIDDYSKNNFNPHEIREMLAAENKEMDIKMINKILYDIKNGGFRNKRAKNSLELELSDDDEDDVLQQYRLKRRELMRKRRLEIGDDAKLVKNPKSSAFFESMVEDIIEYKNPFGAEEEYNLDITSTATDLDTQDNSINVGDNTGNNEQKPVDQKNKKVIISEDFVQKSLSFLKSNNYEDFETDKELSRIQHGNDEAIEDLYTLKQNSSIKSFTNSQTDSTTSKTVNTIIDLEKRPEDEDEVENGDTSLVGVFKHPSIIKSFASRTDINDKFKEGNKTVKILKSYKTVGSSKASITYMGKTRKLIAPKRKTEGSHRYHHDHHNKKMKMKTKTKSNKLFESGQDSFDN
The following text describes a protein:
Function:
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MGTDGLDDKQARPPRRARRSLRWVLAAPLLFAAASVLQVLALRIIDPPISTVMVGRYLEAWGEGEAGFSLHHQWRDLDEIAPSLPISVVAAEDQQFPSHHGFDLQAIEKARDYNARGGRVRGASTISQQVAKNVFLWQGRSWVRKGLEAWYTLLIELFWPKQRILEMYVNVAEFGDGIYGAQAAARQFWGKDASRLTPTESARLAAVLPSPRRYDARRPGAYVQRRTAWIQRQARQLGGPGYLQAP
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts on the folding of rhodopsin RH1 and RH2 (but not RH3) and is required for visual transduction.
Sequence:
MFWFTSVVVLLIALSANDVDAAKRFGKKKNKPWEDSDRDSENDLLVTKKVFFEMEIDDEPAGRVVIALFGDTCPVTVQNFAAIVRGNWRQDKRLSYNNTQVHRIVPDFVIQMGDVTEGDGTGGKSIYGNFFADENFYLRHWGPGWVAMANSGPDTNNSQFFILLTRARWLDGKHVVFGKVIEGMDIVDKMAEVDADDNGFPLEPIRIVDCGIIPVPTPYLIANPDAEPSQEKKKDKKKQ
The following text describes a protein:
Function:
Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).
Sequence:
MMGCFALQTVDTELTADSVEWCPLQGCRHLLACGTYQLRRPEDRPAGPQNKGGMEVKEPQVRLGRLFLYSFNDNNSIHPLVEVQRKDTSAILDMKWCHIPVAGHALLGLADASGSIQLLRLVESEKSHVLEPLSSLALEEQCLALSLDWSTGKTGRAGDQPLKIISSDSTGQLHLLMVNETRPRLQKVASWQAHQFEAWIAAFNYWHPEIVYSGGDDGLLRGWDTRVPGKFLFTSKRHTMGVCSIQSSPHREHILATGSYDEHILLWDTRNMKQPLADTPVQGGVWRIKWHPFHHHLLLAACMHSGFKILNCQKAMEERQEATVLTSHTLPDSLVYGADWSWLLFRSLQRAPSWSFPSNLGTKTADLKGASELPTPCHECREDNDGEGHARPQSGMKPLTEGMRKNGTWLQATAATTRDCGVNPEEADSAFSLLATCSFYDHALHLWEWEGN
The following text describes a protein:
Function:
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MFIMSSISHAQLGWNDAGTPVSDQFDDVYFSNVNGLAETRYVFLEQNHLPQRWHNDDQRRFVIAETGFGTGLNFLAVWQAFVAFREANPDAKLKELHFISFEKYPLSKSDLIQAHQAWPELAQFAQKLHKHYPLAIPECQRIVLNDGLVTLDLWFGDIKDCLPKVATQEQGLVDAWFLDGFAPSKNPEMWNQNLFAGMAKLAKHGCTCATFTSAGFVRRGLIDAGFAMKKVKGFGTKREMIAGSLSEKVPYTNIAPEFRFEATHGLQEVAIIGGGIASATLATTLARRGVAVTLYCADEKPAQGASGNRQGAVYPLLSGDHNAVSRVFAPAFLFARQWIEQAAEQINFDHDWCGVTQLMWDEKATDKLKSMLEGNFPTQLVHGLSAEQTNQQVGVPVDKASVHYPLGGWLSPAELTQGLIHLLEQQGKLTAHYQTPIDALTWQPETQLWQLRSGDTLMSHQCVVIASGHQFDSLSQTAELPLGKVKGQVSHIPTTETLSKINSVLCYDGYMTPVSQQNGYHCIGASYDRQHLDATFDPQAQHENAQKLIHCLPEQTWPLEVDVSGNQSRQGVRCVSRDHLPFVGNVGEFSKITEQYRDLAQQHQAEPIALYPQLYALVGLGSRGLSSAPLMAELLASQMCGDPMPLGVDLLEQLHPSRMWVRKLRKGKALTQKV
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAGTSGLLNAVKPKIQTIDIQAAAGWGIAAAAGAIWVVQPFGWIKKTFIDPPPTEEK
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:
MENIKLEEIIKAVNGELVITGEKDEYNSVSTDTRKIEKGDIFIALKGENFNGNNFVEMAIEKGAALCIVSEINFSEGKVSKSSYVIKVENTNKALLDLAKYYRSKLDIKVVAITGSTGKTSTKDLVAAVLSEKYKVFKTEGNFNNEIGLPLMIFKLDKSYDIAVLEMGMNHFNEIHNMAEAAKPDIAIITNIGISHIENLGSRENILKAKLEITDFFCKDSILIINGDDDLLSNFESDKFKVYKIGTDKKFDFNGDNLNLEAESIKFDILERGKTAYRCFSVNVPGKHNVLNSLTAIACGRVLDINYRDIQTGIKNLKATSMRLDIVKEKGFTIINDCYNASPDSMKAAIDVMKNIKGKRTIALLGSMRELGSEGYRAHREVSEYAREKGIDLLFSIGEFSEAYREGFEEINKENYKSFLNNEEAAKYIKNIIKDGDIILIKASRAMKLEEIVKELRIKQEK
The following text describes a protein:
Function:
Cytokine which promotes survival following infection by Sindbis virus by suppressing the immune deficiency pathway. Following infection by the enteropathogenic bacteria E.carotovora limits intestinal stem cells proliferation. When secreted from muscle or adipose tissue, can attenuate age-related intestinal tissue degeneration by inhibiting apoptosis.
Miscellaneous:
MISCELLANEOUS: The name 'Diedel' is the German translation of Tweedle and is based on the fictional Lewis Carroll characters Tweedledum and Tweedledee due to the presence of two subdomains within the protein.
Subcellular Localization:
Secreted. Note=Secreted into the hemolymph.
Domain:
Contains two subdomains, SD1 and SD2. SD1 is composed of an antiparallel beta-sheet covered by an alpha-helix and displays a ferredoxin-like fold. SD2 displays a new protein fold made of loops connected by four disulfide bridges.
Sequence:
MASPVVSLLLVGICALAFVHVARSECCTSRELVEFKMDRGDCEAVRAIENYPNGCEVTICADGVAQLGAYCGQGSCNIFGCNCDGGCLSGDWSQEFVRRNQQYGIQIIKVTRLPF
The following text describes a protein:
Function:
May be involved in rRNA-processing and ribosome biosynthesis.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVLKSTTAGNVSVYQVSGTNVSRSLPDWIDKKRKRALKHDLEYQNRIELIQDFEFSEASNKIKVTNDGQYCMATGTYKPQIHVYEFANLSLKFDRHTNVENIDFLILSNDWTKSVHLQCDRSIEFQTAGGVHYRTRIPKFGRCLTYNPINCDLIVGSSSDELYRLNLDQGRFLSPLKLDMTDGGNIDSGCNAVDINSMHGLISAGLDDGTVEFWDPRSKQRAGKLFVSDQLINSTNNTEQSSCGITSLAFRPQDALNFACGTSNGQTLLYDLRASEPYQIKDQGYGYDIKKIIWCQDSLKPEMILTSDKRIVKIWDHTNGKSFASMEPTVDINDICHIPQSGMFFMANEGMPMHTYYIPNLGSAPNWCSFLDNVTEELEEKPSDSIYSNFKFITRDEVVKLNLTHLIGSKVLRSYMHGFFINTELYDKVNLISNPNSIYDQRKREIANKINEERKSRILTSSNGNDLPTKIKVNKDLVNKLQTKFAENGTPDGNANGATDYVESIVNDDRFREMFENPDFEIDEESHEYKQLNPVKSTKDITTTNTGTTNSRGRGLTAAEESDEERLNMKDSHHTGLDSDESDEESDSESEEQSEDEAKSAETRERVGKELNKIRQSKQKQQQQDSKKFQNEMKILSQQSSSSSSSLANTEKASVSFGSQVNKLNKISKQNKNNNSISNAKDARLRRHARGEAELTFVPQKSKSKSTKSKFNNNHSDDEKSDSGKTKDSGRTKQRFEGRRIASKNKFRGM
The following text describes a protein:
Function:
Mediates homophilic cell-cell adhesion (By similarity). Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MASLLSSSLPSCLPSLLFLLLQLTSSSAGQFRVIGPGHPIRALVGDEVELPCRISPGKNATGMEVGWYRPPFSRVVHLYRNGKDQDEEQAPEYRGRTQLLKETIGEGKVTLRIRNVRFSDEGGFTCFFRDHSYQEEAAMELKVEDPFYWINPGVLVLIAVLPVLLLQITVGLVFLCLQRRLRGKLWAEIENLHRTFDPHFLMVPCWKITLFVIVPVLGPLVALIICYNWLHRRLAGQFLEELRNPF