lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Enzyme involved in the ethylene biosynthesis. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
Sequence:
MVLIKEREMEIPVIDFAELDGEKRSKTMSLLDHACDKWGFFMVDNHGIDKELMEKVKKMINSHYEEHLKEKFYQSEMVKALSEGKTSDADWESSFFISHKPTSNICQIPNISEELSKTMDEYVCQLHKFAERLSKLMCENLGLDQEDIMNAFSGPKGPAFGTKVAKYPECPRPELMRGLREHTDAGGIILLLQDDQVPGLEFFKDGKWVPIPPSKNNTIFVNTGDQLEILSNGRYKSVVHRVMTVKHGSRLSIATFYNPAGDAIISPAPKLLYPSGYRFQDYLKLYSTTKFGDKGPRLETMKKMGNADSA
The following text describes a protein:
Function:
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Subcellular Localization:
Secreted. Bacterial flagellum.
Sequence:
MRLSHNLASLNAFRNYSKVLREQSTALDKITSGYKVRRSKDDPNVMAQSEKTKIQIRGLQVASRNAQDGVSMLQTAEGGLENIGNMLMRIKELTIQAANGTNNLDDQEVIQNEINELIAGIETTAKGTEFNGVKLLSQGNKFSDQTNVMTKSVPIGANVGDLEDIPFYNLTTEGLDIKGKINVTDASKLGESLDAVNNAIETVLSVRSEYGSLENRFEECINNIGEISFKMEGANSELVDADVAEEMMIYAKSDILYQSSLAIMRQTNNFPMDVLKILENVKSK
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that negatively regulates IL3-dependent cellular responses through IL3RA ubiquitination and degradation by the proteasome, having an anti-inflammatory effect.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MWLFTVNQVLRKMQRRHSSNTDNIPPERNRSQALSSEASVDEGGVFESLKAEAASPPALFSGLSGSLPTSSFPSSLVLGSSAGGGDVFIQMPASREEGGGRGEGGAYHHRQPHHHFHHGGHRGGSLLQHVGGDHRGHSEEGGDEQPGTPAPALSELKAVICWLQKGLPFILILLAKLCFQHKLGIAVCIGMASTFAYANSTLREQVSLKEKRSVLVILWILAFLAGNTLYVLYTFSSQQLYNSLIFLKPNLEMLDFFDLLWIVGIADFVLKYITIALKCLIVALPKIILAVKSKGKFYLVIEELSQLFRSLVPIQLWYKYIMGDDSSNSYFLGGVLIVLYSLCKSFDICGRVGGVRKALKLLCTSQNYGVRATGQQCTEAGDICAICQAEFREPLILLCQHVFCEECLCLWLDRERTCPLCRSVAVDTLRCWKDGATSAHFQVY
The following text describes a protein:
Function:
Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine. Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon. AtoC acts by binding directly to the promoter region of the target genes. In addition to its role as a transcriptional regulator, functions as a post-translational regulator that inhibits polyamine biosynthesis via regulation of ornithine decarboxylase (ODC).
Subcellular Localization:
Cytoplasm. Note=Membrane-associated in the presence of AtoS.
Sequence:
MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEVKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGIDPADV
The following text describes a protein:
Function:
tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Sequence:
MVEDRPPPEPEPGRCAFWLGARKARHCRSLALPSQRYCGNHLHLDPAAQSQASGAAAAARAARVPCPIDPTHTVFASELDIHVKRCPALIIAQREKAQPHFLEDVNAGSDDEPNLPPPPQPRAPRPDATAGPEPAQGVSEKAAGTTAGTAAGTAAGVGAAAVGAAGFGAGAAAAGAAAAQGGHQGGPARPQGQEQQQAPAQNVEPGEEGEVAEEWTPALGPFVKGRAAQRAALARRLGEAAFLAILDKVEAAFGAACGGAAPPAVVLRPAECEGMLSAPSDQRPFDLKHGLQQASIMGNMQRVGLIRPGPQGGAGVAVVELGAGKGYLGGTLAACGGVGRLVATDIVAGLRLKADRHLRHILFGRHRVDLKDYVPAATPELTMRRQTQPQQQKQPQQQQQPAEGPEAKGQARQQKQRQQKQKHPHPSSAPTTSAGSRGDSPAAKRPALDGHVPPPSQPLPVQGPSGGSGCAGAGPAAAAAAVAERAPSGPSPMEGAEAGEGVPALEAAGAPGVAAPPQGPPQEPPQGAPAAVAASATAAEVPAAECWVAVAKHLCGAATDYGLRACLLPHDEPARRSNTDANTTNPDTTNNNSQEGWGPGSSQSSAAHKHPQPHPHPQPHPQPPFRGLAVAPCCHHRCGWRAYTGKRLFRRLGLSPTEFELVSWMTGWALCGHDTPAGSAAAAAECGEAGGEIEGEEGQEGAGCRSAGAQTQPQGLQQEPVRGQAAGQQEQQQQQNQQQEGADAKAPAPFDPATRLPRARRMAVGQMCKQLIDRGRLEWLCERYERAELVCYIGPEVTGENRLLLAVGPRAGARAGAGEGAGQGAGEGAGEGAGAGATERKDV
The following text describes a protein:
Function:
Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis. Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form following the recruitment of caspase caspa. Its subsequent activation causes the cleavage of the midformed pro-il1b and results in il1b maturation and secretion in the extracellular milieu. Activated by direct binding to bacterial lipopolysaccharides (LPS), which causes non-canonical inflammasome activation and results in the pyroptosis of infected cells and their extrusion into the gut lumen, as well as in cytokine secretion. Plays a crucial role in the restriction of bacterial infection to intestinal sites. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (By similarity). Promotes pyroptosis by bacterial infection by E.piscicida.
Subcellular Localization:
Inflammasome. Cytoplasm. Note=Co-localizes with pycard, caspa and nlrp1 in the cytoplasm. Co-localizes with pycard at large cytoplasmic aggregates, known as specks.
Domain:
The Pyrin domain mediates LPS recognition and homooligomerization.
Sequence:
MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQACRGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL
The following text describes a protein:
Function:
Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD.
Miscellaneous:
MISCELLANEOUS: Present with 3530 molecules/cell in log phase SD medium.
Sequence:
MFSGFSSFGGGNGFVNMPQTFEEFFRCYPIAMMNDRIRKDDANFGGKIFLPPSALSKLSMLNIRYPMLFKLTANETGRVTHGGVLEFIAEEGRVYLPQWMMETLGIQPGSLLQISSTDVPLGQFVKLEPQSVDFLDISDPKAVLENVLRNFSTLTVDDVIEISYNGKTFKIKILEVKPESSSKSICVIETDLVTDFAPPVGYVEPDYKALKAQQDKEKKNSFGKGQVLDPSVLGQGSMSTRIDYAGIANSSRNKLSKFVGQGQNISGKAPKAEPKQDIKDMKITFDGEPAKLDLPEGQLFFGFPMVLPKEDEESAAGSKSSEQNFQGQGISLRKSNKRKTKSDHDSSKSKAPKSPEVIEID
The following text describes a protein:
Function:
Receptor for the neuropeptide CAP-3/pyrokinin-1 (TGPSASSGLWFGPRL-amide). Also activated weakly by other neuropeptides terminating in the sequence PRL-amide including pyrokinin-2, Hug-gamma, and ecdysis-triggering-hormone-1. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSAGNMSHDLGPPRDPLAIVIPVTVVYSLIFITGVVGNISTCIVIKKNRSMHTATNYYLFSLAISDFLLLLSGVPQEVSYIWSKYPYVFGEYICIGRGLLAETSANATVLTITAFTVERYIAICHPFLGQAMSKLSRAIRIIVLVWIMAIVTAIPQAAQFGIEHYSGVEQCGIVRVIVKHSFQLSTFIFFLAPMSIILVLYLLIGVHLYRSTLVEGPASVARRQQLKSVPSDTILYRYGGSGTAMSFNGGGSGAGTAGLMGGSGAQLSSVRGRLNHYGTRRVLRMLVAVVVCFFLCWAPFHAQRLIAIYAPARGAKLRDQHEFVYTVMTYVSGVLYYLSTCINPLLYNIMSHKFREAFKAVLFGKKVSKGSLNSRNNIESRRLRRALTNSSQTQRFSIESAEQPKPSIMQNPTNKPPVAAQYAMIGVQVN
The following text describes a protein:
Function:
Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.
Subcellular Localization:
Nucleus.
Sequence:
MADVAAASLFGADRRLCSADVLSPPEVRARIEVAVLNFLAALSSPSSPAISVLPLIARKSSNCSLRSGLLSDVSSVYLSYAFCKRSLTRENDAKSFVRVWKVMEMCYKILGEGKLVTQRELFYKLLSDSPKYFTCQRHVNQTIQDVVSLLRCTRQSLGIMASSRGALIGRLLLHEPEGEHIDCSILGPSGHAITGDLNQLSKLNLYSDARYLILVEKDAVFQRLAEDRLYNQLPCIVITAKGYPDIATRFILHRLSQTFPNMPIFALVDWNPAGLAILCTYKYGSISMGLESYRYACNVKWLGIRGDDLELIPQSAFQELKPRDLQIAKGLMSSKFLQDKHRAELALMVEMGKRAEIEALYCHGFDFLGKYIARKIVQGDYI
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, (R)-adrenaline/epinephrine, (R)-noradrenaline/norepinephrine and serotonin) and phenolic and catechol drugs. Catalyzes the sulfation of T4 (L-thyroxine/3,5,3',5'-tetraiodothyronine), T3 (3,5,3'-triiodothyronine), rT3 (3,3',5'-triiodothyronine) and 3,3'-T2 (3,3'-diiodothyronine), with a substrate preference of 3,3'-T2 > rT3 > T3 > T4.
Subcellular Localization:
Cytoplasm.
Sequence:
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
The following text describes a protein:
Function:
Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins. Involved in activation of the JAK/STAT pathway. Catalyzes ubiquitination of methylated RBM15. Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA. As part of the PINK1-regulated signaling, upon mitochondria damage, ubiquitinates ABCE1 and thereby recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSCSSDDQSDKECPLCMEQLEIDDWNFYPCKCEYQICRFCWHRLRTDENGLCPACRQPYPEEPLNFKPLSTADMAKMKSEKKMKQQAEKQRISESRKHLASYRVLQKNLVYVVGLSARVADPEMLKKPEYFGKYGKITKVAVGTTTSGVVGSASHTAYVTYMRVEEALRAVQGVQNALVDGRVVKASLGTTKYCSSFLRSQSCYKPECMYLHDMADADISFTKEDMHAGKHADYEKRLMDTLLKCTVSHTPAPQSIVPSQLLISSTLTSTLPAVSRKKTDVNGSVRDIKSMEEDDMKLEDEFPPVSAVIRQNVHPPVPIPSNPVPSTSEEKPNGITKSVMAKKEKKEKTVMPSCTSTRIPRDVLTLPRELSASPPDDWTSRDDGPSCSPPPGLPAPPHLVATNSSTTMTPPSESSVSPPRRDVPSVSSASSTPQWQTLLGLAPRPISPPSNGFFSDDDLGFDPFHESSRELAALVEEERNAVPPSSFLPPPPALPHPHLMQHQHRQHHQHNGGYAPYNSLYGAVMKGGHIPAPAEGRIAMECDDHYSAVMREGKRVGMDSMGSGNLSSVGGLASLFSGGLSGLDSSPLDTYSFSSNGLAGGYSFPSLSSHSLSNGFPTHDMVNQSLSSRQTHDASSFARSSMMPPPPPGLGVPHGLNAPPPPGLGPPRSMMTGTTHGLVPPSSVPQGLAALTALRHTPSTNCSTSSNTRTPLMSKAEWQEGFKSLLPNINVRFSAELERELK
The following text describes a protein:
Function:
Crucial regulator of cellular iron homeostasis. May play a role in regulating the function of the thioredoxin system. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.
Sequence:
MANTINTNEEFENILKDNKFLVVMFWADWSKPSTQMRDVFDQLAKQATNQANNKLLFLKVEAEKVHQISGRYNVKSVPTCIFLNQGKLVQSVVGANPSELALQTNNFSKTCDTLPLEEQQQQQQSEEIINKIKLDQEQEKKLLNERLEKLVNQSPVMLFMKGNPEKPQCGFSNKTVTILKENGFEFGSFDILQDQAVRNGLKEYSNWPTYPQLYINGKLVGGYDIIKDLNEEGELIDLKP
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSIIHGDVKRVAFGYDSAGNTCNQKTNKPIENLTNSGMSTDGKPYVFFMSTLYPKNALQICIEKCPNKKLTTEQDIVDFYNTEKIFQLDDFMTKTLNDLSLCWRELIGLTVIAVVIAFLMVVLMRFLAAVIVWVIVVLSVVGSIVGSVFLWWCFVVHLKAEEQEEFLVPLVGSSLKKKWTFLIFAIVASVLTVILLLMLLIMRKRISLVVALFHEAGKCLADVPMLLIQPIWTFLFCLVKFQKNTFEKQFWWIHLIGWIWTTEFTLACQEFVITSTVAIWYFTTTYDNINNNTTTNINDHTNNNINNTTTNINDHINNDNNDNNIINININDRCKGSENACARCCLKCCICCLWCLEKVLKFLHQNAYTIIAIEGTSFCTSARKAFEIISSNALRVLAINSVGDFVLFLGKVAVMCLTGVFAVLWLRTIPSINYLAVPVFLVCVFAFVIAHCFLSVYKMVVDALLICFCEDCQKNDGTPGREYFMSHSLMQFVTDSSAKISNTAGAVVGSGDATEGTVLKPALGP
The following text describes a protein:
Function:
Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions weakly as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has no wax synthase activity.
Sequence:
MRRLNGVDALMLYLDGGSAYNHTLKISVLDPSTDPDGWSWPKARQMFEERAHLLPVFRLRYLPTPLGLHHPIWVEDPEFDLDAHVRRVVCPAPGGMAEFCALVEQIYAHPLDRDRPLWQTWVVEGLDGGRVALVTLLHHAYSDGVGVLDMLAAFYNDTPDEAPVVAPPWEPPPLPSTRQRLGWALRDLPSRLGKIAPTVRAVRDRVRIEREFAKDGDRRVPPTFDRSAPPGPFQRGLSRSRRFSCESFPLAEVREVSKTLGVTINDVFLACVAGAVRRYLERCGSPPTDAMVATMPLAVTPAAERAHPGNYSSVDYVWLRADIADPLERLHATHLAAEATKQHFAQTKDADVGAVVELLPERLISGLARANARTKGRFDTFKNVVVSNVPGPREPRYLGRWRVDQWFSTGQISHGATLNMTVWSYCDQFNLCVMADAVAVRNTWELLGGFRASHEELLAAARAQATPKEMAT
The following text describes a protein:
Function:
Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.
Miscellaneous:
MISCELLANEOUS: The final C-region domain is deleted from PubMed:115869 chain. It was isolated from a myeloma protein that contains 1 light and 1 heavy chain per molecule, linked by a disulfide bond. In contrast, normal mouse IgA molecules contain 2 light and 2 heavy chains and lack a light-heavy chain disulfide bond; MISCELLANEOUS: M511 chain was isolated from a myeloma protein that binds phosphorylcholine; MISCELLANEOUS: M511 sequence was compared with that of mouse MOPC 47A, and a genetic mechanism for the deletion of the CH3 domain of the mutant chain is proposed.
Sequence:
ESARNPTIYPLTLPPALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGRYTMSNQLTLPAVECPEGESVKCSVQHDSNPVQELDVNCSGPTPPPPITIPSCQPSLSLQRPALEDLLLGSDASITCTLNGLRNPEGAVFTWEPSTGKDAVQKKAVQNSCGCYSVSSVLPGCAERWNSGASFKCTVTHPESGTLTGTIAKVTVNTFPPQVHLLPPPSEELALNELLSLTCLVRAFNPKEVLVRWLHGNEELSPESYLVFEPLKEPGEGATTYLVTSVLRVSAETWKQGDQYSCMVGHEALPMNFTQKTIDRLSGKPTNVSVSVIMSEGDGICY
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:
MTVSTPSKPHICRFPPGADPDVINQAFREDGVVILEGFLTPAQVDKVNCEMKPHLAKVRGGNMRYGPMDTSLETTLEPERRRIHNLAGLSETFRQDILNHPLMHELSRRVFSEFGDYWQYAGSVIDCAPGTPDQFLHRDQPAQKLFNVGPDAPEGFINFLTALTDFTKTNGATRFVWGSHRDWIDKSDENHPIVVAEVKAGDSLFFSGKIVHGGSFNGTNDTYRSSVALPIVPCIMTPYEANIHIPRSTVETMTPLAQRMIGWRSACLPDPYAIGTWTLNMNELGEQMGLKSKGYLEN
The following text describes a protein:
Function:
Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). No activity with L-proline, trans-4-hydroxy-L-proline (t4LHyp), cis-4-hydroxy-L-proline (c4LHyp), trans-3-hydroxy-L-proline (t3LHyp), D-proline, cis-4-hydroxy-D-proline (c4DHyp), trans-4-hydroxy-D-proline (t4DHyp) or L-serine as substrates. Involved in a degradation pathway that converts c3LHyp to L-proline, which would allow A.fabrum to grow on c3LHyp as a sole carbon source (By similarity).
Sequence:
MSSAVSTTAAPEARSILAGAAEGKVIATTEALSFWGGVDPATGKVIDVHHPLHGICLTGGVLFMPTSRGSCTGSGVLLDLILTGRAPSALVFCEAEDVLTLGALVAAEMFDKALPVIRLDAETFSRFSRAAHVSIDQNTIKADGVSLAIAPPATAHLDLNDDDRAMLVGRDGIAVRQAMRIIVAMAAQQGASALVDVTQGHIDGCIYASPANLTFAEKMADMGGKVRAPSTMNAISVDKANWRAQGVPEDFGDPAARLADAYVRMGCKPTFTCSPYLLDSAPSAGESIAWAESNAVIFANTVLGARTAKHPDFLDLCIAMTGRAPLSGVYIEENRRPQRIVDVALPAGIDDAFWPLVGYLAGKAAPDCIPLLRGLGAAKPSRDDLKALCAAFGTTSASPMLHIEGATPEAGLAPLETAETVTISLQDMAAAWSLLNDGPEEVQLVAIGSPHASLEECRALAAVFAGRKRRADVAVIVTAGQQVIDAAGKDGTLQSLKDSGVQVLPDLCWCSISEPVFPTKTRALMTNSGKYAHYGPGLSGRAVRFGSLADCVESALTGRAVSRLPVWLS
The following text describes a protein:
Function:
Part of a complex with bicd-1 and dlc-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells.
Subcellular Localization:
Nucleus envelope. Note=Probably recruited to the nuclear envelope by unc-83.
Sequence:
MEEAKNMALLFFMDHLMQKNGRRTIHDLSCQFGARGFSEEMRNAVGTTQEGLTEFLQGHPSLFTVEGDQVILNGHNDLNAKNNPLLQSGIRSRNYEKEAVDFFVTKLTKFGPELQIKSLLGHRSQAAPEVRLVSGRHLKEFCEFLQSQVDYFVVEGDRVRLKNMPEPDENAIEMDDEGRPLAGVKAKQAAVEYLKSVLEQNEDQPIPLDQFYQNFCQRFSHTIRQDVATNPKELLQFLKLNRGLFFIRSNKVSLVKNRLNEDGSENGSDEGEETNNNGMFPLDQSALTRIHFVKALKPAQDLISRLWQDINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATTSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKFNKSLNEMRPISFINLQRVYYPQSIMLSDVTPRKMSMCPNWGVRPITEEFQLTIVEEAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPEVLLASPNRPPPQPFISSPYRASTRRDVRNGGSIMQSFSPAPYAAAPRPQMSDACTQTFSTGDIEVLNVFYE
The following text describes a protein:
Function:
Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Sequence:
MRIRLGRHNAPDFPQGAAVTIGNFDGVHLGHKHILQKLRLEADARGLPVVTVVFEPQPKEFFALRTGRMPPCRISPLRTKLELLEGTGCVDAVWVLRFDQNFSEISAQGFIDRLLRQTLNTRYLLVGDDFRFGAGREGCFELLAQQPDMQTERTPSVIVEDIRTSSTAVRQALSDGNLAYAKKLLGHDYVLSGRVVHGRKLGRTLNAPTANIRLPRHRYALGGVFVVEADGAFGTRRGVASFGFNPTVDSGCSQKLEVHLFDFQGDLYGQGLNVRFLHKLRDEEKFDGMEELKRQIEADMEAARRW
The following text describes a protein:
Function:
Hydrolase highly specific for thiamine triphosphate (ThTP).
Subcellular Localization:
Cytoplasm.
Sequence:
MSTDTTNNSDASSQTTSSSPSEYEIEKKFPISKSSASSIEQTLTKLGFQQTHKEEFTDWYFDLPSPHWYFSTLNDTWIRYRETKVKLGSSWGWRGVWQVKRGKSTRRDQEDDDDSAGLRLRGREDDGMTVYEEFQGKVAKAMVLDMLSRLDLDEAMMAETSGSSAPRDALYEGHDVPRLDGDEILAPFARFKTFRTSWQIPPTSTTDEIDVTAMFTGLKVDIDSTDFGYSVGEVEAVIANEDGNEASIEAEKEKIRTLVGMLNCDDTSKDDNDPSMARGKLEWYLINNRRDHYDACVEAGVMMA
The following text describes a protein:
Function:
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEYLPDGDGVSFTQGNILCCQCGVPIQPNPANMCVACLRTQVDITEGIPKQGVLHFCRNCERYLQPPNQWLACALESRELLTLCLXXXXXXXQVHLIDAGFVWTEPHSKRIKLKLTIQKEVVNGAILQQVFVVEFVVSNQMCEDCHRVEAKDWLEWLSIKKYKTSEKLLSHDVKSNTYNYKSTFSVEIVPVCKDNIVCLPPKLAQQLGNLNQICVCLRVSTTVHIIDPSTLQIADVTAPVFWRTPFQSLCEPRQLTEYMVLEVEPIRHHERVHVAGEGAKSHKHLLADVWVARSSDLGMNDNQYHCRTHLGHLLRAGDLVHGFDLSNANVNNDFLDKMKADRLPDVVLVKKVFDKSKRHRRRNWKLKRLAKELETMDTDSMERDYNEFLEDLEEDPLYRKDVNIYRDAEKLAVESDTDDDDAPRISLQEMLEDLHISEDATGGEGADMMTD
The following text describes a protein:
Function:
Involved in cell wall synthesis where it is required for glycosylation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MISSAVILVGGPSRGTRFRPLSFDVPKPLFKIGGREMIYHHLAALSKIESVKDVFLVGFYDESVFKDFINEVASHFPSFNRIKYLREYNCLGTGGGLYHFRDQILKGHTSNVFVMHADVCCSFPLQELLNVHHEKKALVTLMATKVSKEDASNFGCLVEEPSTGRVLHYVDKPSSYLSNIISCGIYIFDASIFDEIKKAYERRLEEVEKQLRSLDEGMEDYLSLETDVLAPLCSDSSKAIYAYNTPEFWRQIKTAGSAVPANSLYLQKAYHDGTLPKPDTEAEIIQPVFIHPNAIVSKGAKIGPNVSIGARVRIEDGARIRNSIIQEDCEISANAVVLHSILSRHCKIGKWSRVEGSPTLPSQHSTTIMRNSVKVQAITVMGADCIVHDEVRVQNCLVLPHKEIKVGLVGEIVM
The following text describes a protein:
Function:
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAARVVAARCRNIYGLKKKPHGLRNFCSSGDPGSVPLSQPLPSLPVPQYATVTNQTYDTKITTLENGLKVTSENKFGQFCTVGVLVDSGSRHEVAFPSGISHFLEKLAFNSTARFGNRDDILQQLEKYGGICDCQSSRDTIMYAVSADRKEVDPVVSLLSDVVLKPNITELEIEDTRRAIQFELEDLNMRPDPEPLLTELIHAAAFRDNTVGLPKLCPPDNILQIDQSTLFNYLSLKYILLSCMVHFFTILFIFYSQPSETTQWAFPNSVRQTTSCKSTSPPCLTTYNTVGLPKLCPPDNILQIDQSTLFNYLSLHYVPSRMVLAGVGVKHEALVEAANKYIVGGNASWEGQGRYPVKAVDESIAQYTGGMRQAVLNMMMGGGGSFSAGGPGKGMYTRLYLNVLNRYHWMYNATAYHHSYEDTGLFCIHASAHPTEVRELVGVLVREFVRMAGPVGGVELARAKTQLQSMLMMNLEARPIVFEDIGRQVLNNSARKTPQEFCNMIAAVTEEDIRRVARRMLETKPSVAALGDLRQLHSYEDIQTGLASRDGQMPRRFTLFR
The following text describes a protein:
Function:
Involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MSTNHRPQLESKRGKVIKIKDTIQHARGLPQQTSIKYRQDIKNEKTINKFDDLQKHDNNKITSLESISPPTKKLKIESTKEITTEPLNQEIDKQSKLSLKNDDQSDIQPNEKSESDEEDSKDEEDDESSDDDDSDDDDTALLLKEIENIRREKEKQNSDSTNNSINNSLTLQTHDSSTKKKSWRSSTTFNNKSKKESTNDRNNNYTTDTLNSQHHQKFMSKYIR
The following text describes a protein:
Function:
Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits. Also required for maintenance of normal cell surface levels of APP and LRP1. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome.
Sequence:
MHFSIPETESRSGDGGGSAYVAYNIHVNGVLHCRVRYSQLLGLHEQLRKEYGANVLPTFPPKKLFTLTPAEVEQRREQLEKYMQAELIHRQTQPERTSSPPAKDLLRQDPLLGSSETFNGFLRRAQQETQQVPTEEVSLEVLLSNGQKVLVTVLTSDQTEDVLEAVAAKLDLPDDLIGYFSLFLVRELEDGAFSFVRKLQEFELPYVSVTSLRSQEYKIVLRKSYWDSAYDDDVMENRVGLNLLYAQTVSDIERGWILVTKEQHRQLKSLQEKVSKKEFLRLAQTLRHYGYLRFEACVADFPDKGCPVVVSAGNSELSLQLRLPGQQLREGSFRVTRMRCWRVTSSVPLPSGGPNSPGRGRGEVHLELAFEYLMSKDRLQWVTITSPQAIMMSICLQSMVDELMVKKSGGSIRKMLRRRVGGALRRSDSQQAVKSPPLLESPDAAREPIVKLSSKLSAVSLRGIGSPGPAPDPGTSDVHGNFAFEGIGDEDL