entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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O09131
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GSTO1_MOUSE
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Glutathione S-transferase omega-1 (GSTO-1) (EC 2.5.1.18) (Glutathione S-transferase omega 1-1) (GSTO 1-1) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (S-(Phenacyl)glutathione reductase) (SPG-R) (p28)
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MSGESSRSLGKGSAPPGPVPEGQIRVYSMRFCPFAQRTLMVLKAKGIRHEVININLKNKPEWFFEKNPLGLVPVLENSQGHLVTESVITCEYLDEAYPEKKLFPDDPYKKARQKMTLESFSKVPPLIASFVRSKRKEDSPNLREALENEFKKLEEGMDNYKSFLGGDSPSMVDYLTWPWFQRLEALELKECLAHTPKLKLWMAAMQQDPVASSHKIDAKTYREYLNLYLQDSPEACDYGL
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Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
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O09139
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E2F1_RAT
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Transcription factor E2F1 (E2F-1)
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MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQVPTGPAAPPAGPRDPDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSRTMVGIGQRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDIQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSAETFQISLKSKQGPIDVFLCPEESAEGISPGRTSYQETSGEDRNADSGTAGPPPSPPSTSPTLDPSQSLLGLEQEAVLPRIGNLRAPMEEDRLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEAVDYHFGLEEGEGIRDLFDCDFGDLTPLDF
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Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. Directly activates transcription of PEG10. Positively regulates transcription of RRP1B.
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O09159
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MA2B1_MOUSE
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Lysosomal alpha-mannosidase (Laman) (EC 3.2.1.24) (Lysosomal acid alpha-mannosidase) (Mannosidase alpha class 2B member 1) (Mannosidase alpha-B)
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MGTGPLTSGVRAGGGNTGWLWMSSCNLGSPVLPISFLFWLLLAAPGARAAGYKTCPPTKPGMLNVHLLPHTHDDVGWLKTVDQYYYGILSDVQHASVQYILDSVVSSLLEKPTRRFIYVEMAFFSRWWKQQTSATQDAVRNLVRQGRLEFVNGGWVMNDEAATHYGAIVDQMTLGLRFLQDTFGSDGLPRVAWHIDPFGHSREQASLFAQMGFDGFFLGRIDYQDKLNRKKKLRMEELWRASDSLEPPAADLFTGVLPNNYNPPKYLCWDVLCTDPPVVDNPRSPEFNAKTLVNYFLKLASSQKGFYRTNHTVMTMGSDFHYENANMWFKNMDKLIRLVNAQQVNGSLVHVLYSTPTCYLWELNKANLTWTVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGPEANVGPYGSGDSAPLQEAMAVLQHHDAVSGTARQNVVNDYARQLAAGWGPCEVLVSNALARLSHYKQNFSFCRELNISICPVSQTSERFQVTLYNPLGRKVDQMVRLPVYEGNFIVKDPHDKNISSNVVMVPSYYSETYQWELLFPASVPALGFSTYSVAKMSDLNHQAHNLLSRPRKHKSHHVLVIENKYMRATFDSGTGLLMKIENLEQNLSLPVSQGFFWYNASVGDEESSQASGAYIFRPNVGKPIPVSRWAQISLVKTALVQEVHQNFSAWCSQVIRLYKGQRHLELEWTVGPIPVRDDWGKEVISRFDTPMKTKGQFFTDSNGREILKRRDDYRPTWTLNQTEPVAGNYYPVNTRIYITDGQMQLTVLTDRSQGGSSLQDGSLELMVHRRLLVDDDRGVSEPLLETDTGDKVRGRHLVLLSSVSDAAARHRLLAEQEVLAPQVVLSLGGSSPYHSRATPKTQFSGLRQELPPQVHLLTLARWGPKMLLLRLEHQFALKEDSDRNLSSPVTLNVQNLFQTFTINYLQETTLAANQPLSRASRLKWMTNTGPTSYPEPSKLDPTSVTLKPMEIRTFLASVQWQEHRPA
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Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.
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O09160
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FUT1_MOUSE
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Galactoside alpha-(1,2)-fucosyltransferase 1 (Alpha(1,2)FT 1) (Fucosyltransferase 1) (MFUT-1) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.344)
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MWTPSRRQLCLAFLLVCVLSAGSFFFHLNGGNFFRNGLTLSVLCSDYHLLKSPVAMVCLPHPLQTSNGSPSCPEQSSSLSGTWTITPGGRFGNQMGQYATLLALAQLNGRQAFIQPEMHAALAPVFRISLPVLDPEVDSLTPWQHLVLHDWMSEEYSHLEDPFLKLSGFPCSWTFFHHLREQIRREFTLHNHLREGAQYLLSGLRIGPAGIRPHTFVGVHVRRGDYLEVMPNRWKGVVGDRAYLQQAMDWFRARHKDPIFVVTSNGMKWCLENIDTSHGDVVFAGNGQEGTPGKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFRPEAAFLPEWVGINADLSPLQAQFDPWKPDSLFRLV
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Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens. H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis. Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a.
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O09161
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CASQ2_MOUSE
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Calsequestrin-2 (Calsequestrin, cardiac muscle isoform)
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MKRIYLLMVGVYLLSLSGAEEGLNFPTYDGKDRVVSLSEKNLKQMLKRYDLLCLYYHEPVSSDKVSQKQFQLKEIVLELVAQVLEHKNIGFVMVDSRKEAKLAKRLGFSEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIVNNKLEVQAFERIEDQTKLLGFFKNEDSEYYKAFQEAAEHFQPYIKFFATFDKAVAKKLSLKMNEVGFYEPFMDEPNVIPNKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSIWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEDEDDDGDDNDDDDDDDDDNDNSDEDNEDSDDDDDDDE
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Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2 this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
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O09164
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SODE_MOUSE
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Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1)
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MLAFLFYGLLLAACGSVTMSNPGESSFDLADRLDPVEKIDRLDLVEKIGDTHAKVLEIWMELGRRREVDAAEMHAICRVQPSATLPPDQPQITGLVLFRQLGPGSRLEAYFSLEGFPAEQNASNRAIHVHEFGDLSQGCDSTGPHYNPMEVPHPQHPGDFGNFVVRNGQLWRHRVGLTASLAGPHAILGRSVVVHAGEDDLGKGGNQASLQNGNAGRRLACCVVGTSSSAAWESQTKERKKRRRESECKTT
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Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
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O09165
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CASQ1_MOUSE
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Calsequestrin-1 (Calmitine) (Calsequestrin, skeletal muscle isoform)
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MRATDRMGARAVSELRLALLFVLVLGTPRLGVQGEDGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSVYVFKGDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAYEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPMTIPDKPNSEEEIVSFVEEHRRSTLRKLKPESMYETWEDDLDGIHIVAFAEEADPDGYEFLETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSIWMEMDNEEDLPSADELEDWLEDVLEGEINTEDDDDDDDDDDDDDDDDD
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Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions (By similarity). Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1 this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity).
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O09171
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BHMT1_RAT
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Betaine--homocysteine S-methyltransferase 1 (EC 2.1.1.5)
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MAPIAGKKAKRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSLQTIKLMKEGLEAARLKAYLMSHALAYHTPDCGKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQQKEATTEQQLRALFEKQKFKSAQ
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Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
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O09173
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HGD_MOUSE
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Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase)
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MAELKYISGFGNECASEDPRCPGSLPKGQNNPQVCPYNLYAEQLSGSAFTCPRNTNKRSWLYRILPSVSHKPFESIDQGHVTHNWDEVGPDPNQLRWKPFEIPKASEKKVDFVSGLYTLCGAGDIKSNNGLAVHIFLCNSSMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICVIQRGMRFSVDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQGKLFACKQDVSPFNVVAWHGNYTPYKYNLENFMVINAVAFDHADPSIFTVLTAKSLRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIKGHYEAKQGGFLPGGGSLHSAMTPHGPDADCFEKASKAKLEPERIADGTMAFMFESSLSLAVTKWGLKTCSCLDENYYKCWEPLRSHFTPNSRSPTEPK
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Catalyzes the conversion of homogentisate to maleylacetoacetate.
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O09174
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AMACR_MOUSE
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Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA racemase)
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MVLRGVRVVELAGLAPGPFCGMVLADFGAEVVRVNRLGSTGENFLARGKRSLALDLKRSQGVTVLRRMCARADVLLEPFRCGVMEKLQLGPETLLQDNPKLIYARLSGFGQSGIFSKVAGHDINYLALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGIVLALFERTRSGRGQVIDSSMVEGTAYLSSFLWKTQPMGLWKQPRGQNILDGGAPFYTTYKTADGEFMAVGAIEPQFYALLLKGLGLESEELPSQMSSADWPEMKKKFADVFAKKTKAEWCQIFDGTDACVTPVLTFEEALHHQHNRERASFITDGEQLPSPRPAPLLSRTPAVPSAKRDPSVGEHTVEVLREYGFSQEEILQLHSDRIVESDKLKANL
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Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (By similarity).
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O09175
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AMPB_RAT
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Aminopeptidase B (AP-B) (EC 3.4.11.6) (Arginine aminopeptidase) (Arginyl aminopeptidase) (Cytosol aminopeptidase IV)
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MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQEQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFNRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWAASEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDHQEEFWKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKETFSATASQLHSNVVNYVQQILAPKGS
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Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4).
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O09185
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P53_CRIGR
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Cellular tumor antigen p53 (Tumor suppressor p53)
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MEEPQSDLSIELPLSQETFSDLWKLLPPNNVLSTLPSSDSIEELFLSENVTGWLEDSGGALQGVAAAAASTAEDPVTETPAPVASAPATPWPLSSSVPSYKTYQGDYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVNSTPPPGTRVRAMAIYKKLQYMTEVVRRCPHHERSSEGDSLAPPQHLIRVEGNLHAEYLDDKQTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDPSGNLLGRNSFEVRICACPGRDRRTEEKNFQKKGEPCPELPPKSAKRALPTNTSSSPPPKKKTLDGEYFTLKIRGHERFKMFQELNEALELKDAQASKGSEDNGAHSSYLKSKKGQSASRLKKLMIKREGPDSD
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Acts as a tumor suppressor in many tumor types induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.
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O09198
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MAL_MOUSE
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Myelin and lymphocyte protein (T-lymphocyte maturation-associated protein)
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MAPAAASGGSTLPSGFSVFTTFPDLLFVCEFVFGGLVWILIASSLVPLPLAQGWVMFVSVFCFVATTSLMILYIIGTHGGETSWITLDAAYHCVAALFYLSASVLEALATISMFDGFTYKHYHENIAAVVFAYVVTLIYVVHAVFSLIRWKSS
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Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Plays a role in the maintenance of the myelin sheath and in axon-glia and glia-glia interactions.
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O09460
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PCKA_ANASU
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Phosphoenolpyruvate carboxykinase (ATP) (PCK) (PEP carboxykinase) (PEPCK) (EC 4.1.1.49)
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MSLSESLAKYGITGATNIVHNPSHEELFAAETQASLEGFEKGTVTEMGAVNVMTGVYTGRSPKDKFIVKNEASKEIWWTSDEFKNDNKPVTEEAWAQLKALAGKELSNKPLYVVDLFCGANENTRLKIRFVMEVAWQAHFVTNMFIRPTEEELKGFEPDFVVLNASKAKVENFKELGLNSETAVVFNLAEKMQIILNTWYGGEMKKGMFSMMNFYLPLQGIAAMHCSANTDLEGKNTAIFFGLSGTGKTTLSTDPKRLLIGDDEHGWDDDGVFNFEGGCYAKVINLSKENEPDIWGAIKRNALLENVTVDANGKVDFADKSVTENTRVSYPIFHIKNIVKPVSKAPAAKRVIFLSADAFGVLPPVSILSKEQTKYYFLSGFTAKLAGTERGITEPTPTFSSCFGAAFLTLPPTKYAEVLVKRMEASGAKAYLVNTGWNGTGKRISIKDTRGIIDAILDGSIDTANTATIPYFNFTVPTELKGVDTKILDPRNTYADASEWEVKAKDLAERFQKNFKKFESLGGDLVKAGPQL
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Involved in gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA (By similarity). {ECO:0000250, ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}.
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O11436
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POLG_RGMVD
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Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
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MMNFGSLNVGLKQVDGTWVPRVFEEKEMARLLAEKQHARVMRATQEMMKAPNPFAEFDEMHQRGNPFAGRVRKCETREPKSAQKPIVTVDTVPVAIYTDVIWPENGKVHALSRRRAPRKHARRSKILACDLLTQVLNISRRAGKSVEVIGKRRCCLKPRRRDGKSCFGVITKHHKGVLSSRDMVKDLFVDSIIEHIAYTGHTPLIDAADIKPGDSGLIYREKKDGYVTRVVRGRHDGDIIDARDYVRAGIHTIKHYSDDGKSLVKYAPYCQPSHHTFGHMCRVTWSDTEILQFREMLSQAIMPQRDPRCDICAEVAGQRTKDEILQHARTSQMMQMLEFGKEDERWKAPRRVMETLLEESNWPSMDYSTSSEITTICCGNNDEPFRRIYSIMKVLAEPNLADVSAWQEANSSLLQLARYMKNREMSVQAGNSATFTNPFPPTVHTFGPTNNGADILQGPWDNWGDKQPIALAFFEKHFNKWQINEFSIDRRVRKHIRGTRKLALMDLNQSRSIKDLEDHVQEEEIPYERKTESCITMYKDQYLYSCSCVTARDGKPYLSMRYLQATGLIPIARGADVQHMPNSDSWQGFYYVAPEGYCYINIFLPMLALAPYYKVGKLSELIGKLIKVLGKWPKLKDVALACLYITEYHTYAQNALLPPILVHHSTRTMHVVDTLGSLSVGYHVLKAGTVKHLVNLASRLATGEMLDYNVGGSLGGIHAYDLLIRSTFDHVLLERALETDPYYILYSALSPTVLKQMYTSKSYANALRVFVRSNQSLFQVVCTLENLARRMTRAQSIEQQIMQLQSLYPQLLDMLADNIPDSPLSWLSHHVTTDSMQRAIELNNCDIELARGGYASINTSWRKKKEQYYADLIKEYYNALSPQAKIFVSRAYIGYLHATTPLFANARKISSEIASNICTQAYSRTIGRGISIVSSGGRKGKTWLTARGDSFYKTMISRAIKLYTPEVSAVIGVATVVGILLSTMTTLHTYLVKNKQTAQKTNEKFEELMYDKVALYIPKYDAEHSHLQGKDLDFEHFARWLMARDKKLSSFVQSHLVDTVTHQAKDDTNVWIEKCIATIVLMMMAIDSNKSDKLYQILCKLRTVFSTMGQTVVTHQSIDEILDIDESKRTTIDFERVEVMQPTQPILKTTFEGFWDMQIQMGRTVAHYRTTGRLVELTRENIAEVVATISSDTANAEFIVRGGVGTGKSTSLPTALCERGRVLMLEPTRPLTENVAQQLRGEPHFKSPSVHMRGLNTFGSSRITIMTSGYALHYYANNRQLLRDFEFIMFDECHVMDSSAMAFYSLCNDAKVAAKLLKVSATPAGRECEFKPMFPVRVSEAAQLSFESFVTAQGSKSTYDIIQYGNNILVYVASYNEVDKLAAMLLEKRFRVTKVDGRTMKLNTHGIELHGTAQVKHFIVATNIIENGVTLEIDCLVDFGTKVVAQLDTEGRRIMYMKVPISYGERIQRLGRVGRTKPGARLKVGHTMRGIVEIPEVIATEAAFQCFMYDLPVMTGQVSVSLLSKCTREQARTMAAFELSPFTMSNLVAFDGTMHPAIHDLLKKFKLRDSTVVLRRTALPLRASASWYTVREYETIIGDLHIENKDVRIPFVANDLSNSLLEGLWDAIQCNRSDVSTTKLTTVSANKIAYTLKTDTSSIQRTISIIDDLLAEERKKQEMFTHHLSTTSGGYTFGLNAIAMCIKSRYAKGYCIENIATLTNVRNQLTEFSGMSEDQYTSEIIQNYPDLTLVHHQSKQEIIRNLKLKAKYDQTLIASDLLLGTAVLIGGGAMLYKTFMTETNTRVHLEGDGKRQREKLQYRAARDSKQDYEVYADEREIQENYGEAYTKHGRKGPAHEKGTGSKTREFTNFYGFDPAEYDTVRLVDPITGKTCDKAVRDLLRMRDVADTFAEIRESMDEDMILQPGVNFAPALIEAYFMNSRTNAARRVDLVPHNPMQVGRLSNNIAGFPTHDGELRQSRPSRPIQKDQVPAANEYSVQHESKSIAKGLRDYHPVSSNLCALEYYCGDMRTSIYGVCYGPYILTTAHLIKEKGGWLKIRTKHGLFKLEAMDRVQIRELCGSDIIVIKGPKDMPPAPMRLKFRAPKSGERAVLVGFVDDNLDRQLVSDSSAVYRRENTGFWKHWITTKYGNCGLPMVSVDTMDIIGLHSLGAQNSNENYFAALTDDFSKQFFEPETDVPWQRKWSYNADKVNYGTMDLTSNQPSGAFKTTKLLEDLLEAVSHQSQEYTWLTKYCGANLLVIGKCPGNLITKHVIKGKSPTFDLFLSVDAQASDFFKPLMGDYAPSRLNREAFVKDITKYDTEIPIGNLSITDFENAVEDTYYILKDSGIEQCNYITDAIPIFDSMNMKAATGALYGGKKKDYFENYTDDMKQNILKESYIRLREGKMGIWNGSLKAELRSKEKVEANKTRVFTAAPLDTLLAGKGCVDDFNNQFYAAHLKGPWTVGITKFFGRWNDFLSELPPGWDYFDADGSRFDSSLTPFLLNAVLNIRKKFMINWAFGQRCLGNLYTEIIYTPIATPDGSVVKKMRGNNSGQPSTVVDNTIMVIIAMQYAISKAEFPAGRLRDQIRYFANGDDLVVAVEPSLSDKISSFSASFAELGLSYDFSNKVNDRSELQFMSHTGKLIDGMYIPMLERERICAILEWSRSDEPQFQLDAISAAMIEAWGDDELLYQIRRYYSWLLEQEPYKSIAELGHAPYLAEAALKALYTGKDPDAELIAIYERAMLNTPPTEDRPTKVVHEANVTAASSAATQTSTTSPTVTSTSGASTSTSSGTTSAPLASTTPPVSATTTPSTGTTAPTTPTVRAANLPDIAGHRKAKANGESQLNVRGENDDEDVPAASEFALPRLPTLGAKIRVPKFKGAIVLNKDHLIKYTPDQRDLSNTRATQEQFEKWYSGVRNEVEKTDEEMALLLNGSMVWCMENGTSPDLSGSWTMMEGEEQIAYPLEPFCRHAQPTLRSIMAHFSDAATAYVVLRNQKSRYMPRYGLKRGLNDYSLAPYAFDFYEITSTSPLRARERHAQMKAAAIRGKASRMFGLDGNVSAQSENTERHTVEDVNTRVHSLSGANML
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[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
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O11457
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VGP_EBOG4
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Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; Shed GP (GP1,2-delta)]
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MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETRYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTAVSNRAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSLRPPITKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNASTTSDTPPATTAAGPLKAENTNTSKGTDLLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF
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[Envelope glycoprotein]: Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Down-regulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation. [Shed GP]: Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4. [GP1]: Responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into dendritic cells (DCs) and endothelial cells (By similarity). Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity (By similarity). Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory (By similarity). Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap and allows GP1 binding to the host entry receptor NPC1. NPC1-binding, Ca(2+) and acidic pH induce a conformational change of GP2, which unmasks its fusion peptide and permit membranes fusion (By similarity). [GP2]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide.
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O12157
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GAG_HV192
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Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
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MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLLVQNANPDCKTILRALGPGASLEEMMTACQGVGGPGHKARVLAEAMSKVNNTNIMMQRSNCKGPKRTIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQVKDCTERQANFLGKIWPSHRGRPGNLLQNRTEPTAPPEESFRFGEETTTPSRKQETIDKELPLTSLKSLFGSDPLST
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[Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}. [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.
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O12158
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POL_HV192
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Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
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MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLLVQNANPDCKTILRALGPGASLEEMMTACQGVGGPGHKARVLAEAMSKVNNTNIMMQRSNCKGPKRTIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQVKDCTERQANFFRENLAFPQGEARKSSSEQNRANSPTRRELQVWGRDNNSLSEAGDDRQGTALNFPQITLWQRPLVNIKVGGQLKEALLDTGADDTVLEEIKLPGNWKPKMIGGIGGFIKVRQYDQILIEICGKKAIGTVLVGPTPVNIIGRNMLTQLGCTLNFPISPIETVPVKLKPGMDGPKVKQWLLTEEKIKALTAICDEMEREGKITKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTWDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEGFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPSIFQSSTTKILEPFRAQNPEIIIYQYMDDLYVGSDLEIGQHRAKIEELREHLLKWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIQLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGAKALTDIVPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQNQWTYQIYQEPFKNLKTGKYAKMRTAHTNDVRQLTEAVQKIALESIIIWGKTPKFRLPIQKETWEAWWTDYWQATWIPEWEFVNTPPLVKLWYQLEKEPIAGAETFYVDGAANREIKMGKAGYVTDRGRQKIVSITETTNQKTELQAIQLALQDSGSEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKERVYLSWVPAHKGIGGNEQVDKLVSSGIRKVLFLDGINKAQEEHEKYHSNWRAMASEFNLPPIVAKEIVASCDKCQLKGEATHGQVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFISNTVKAACWWAGIQQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIIDIIATDIQTKELQKQIMKIQNFRVYYRDSRDPIWKGPAKLLWKGEGAVVLQDNSDIKVVPRRKVKIIKDYGKQMAGADCMASRQDED
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[Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). [Reverse transcriptase/ribonuclease H]: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
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O12161
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TAT_HV192
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Protein Tat (Transactivating regulatory protein)
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MEPVDPNLEPWNHPGSQPKTACNNCYCKRCSYHCLVCFQTKGLGISYGRKKRRQRRSAPPSSEDHQNPIPKQPLPQTRGDQTGSEESKKKVESKTETDPFD
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Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}. Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
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O12164
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ENV_HV192
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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
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MRVEGIQRNWKQWWIWGILGFWMVMIYNVRGNLWVTVYYGVPVWKEAKTTLFCASDAKAYDAEVHNVWATHACVPTDPNPQEMVLENVTENFNMWENDMVEQMHQDIISLWDQSLKPCVKLTPLCVTLHCSNRTIDYNNRTDNMGGEIKNCSFNMTTEVRDKREKVHALFYRLDIVPLKNESSNTSGDYRLINCNTSAITQACPKVSFDPIPIHYCAPAGYAILKCNNKTFNGTGPCNNVSTIQCTHGTKPVVSTQLLLNGSLAEEEIIIRSKNLTDNVKTIIVHLNESVEINCTRPNNNTRKSIRIGPGQAFYATGEIIGDIRQAHCNISRTAWNKTLQEVGKKLAEHFPNKAIKFAKHSGGDLEITTHSFNCRGEFFYCNTSSLFNSTYTPNSTENITGTENSIITIPCRIKQIINMWQGVGRAMYAPPIEGILTCRSNITGLLLTRDGGTGMHDTEIFRPEGGDMRDNWRSELYKYKVVEIKPLGIAPTKAKRRVVEREKRAVGIGAVFLGFLGAAGSTMGAASITLTVQVRQLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQTRVLAIERYLRDQQLLGIWGCSGKLICTTAVPWNSSWSNRSQEDIWNNMTWMQWDREISNYTNTIYRLLEDSQNQQEKNEQDLLALDKWQNLWTWFGITNWLWYIKIFIKIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLTPNPRGPDRLGGIEEEGGEQDRDRSIRLVSGFLALAWDDLRSLCLFSYHRLRDLILIAARAVELLGRSSLRGIQRGWEILKYLGGLVQYWSLELKKSAISLFDTIAIAVAEGTDRIIEVIQGIWRAICNIPRRIRQGFEAALQ
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[Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}. [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}. [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
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O12165
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NEF_HV192
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Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
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MGNKWSKCSTVGRPAIRERMRRAPAAEGVGPASQDSDKYGALTSSSTPANNADCAWLEAQQEEEEVGFPVRPQVPLRPMTYKAVVDLSFFLEEKGGLEGLIYSKKRQDILDLWVYNTQGYFPDWQNYTPGPGVRFPLTFGWCFKLVPVDPREVEEANTGENNSLLHPMSLHGMEDSHREVLQWKFDSLLARRHMARELHPEYYKDC
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Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}. Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
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O12940
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TOM1_CHICK
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Target of Myb1 membrane trafficking protein (Target of Myb protein 1) (Tom-1)
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MDFLLGNPFSSPVGQRIERATDGSLRGEDWSLNMEICDIINETEEGPKDAFRAIKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHILVASQDFVESVLVRTILPKNNPPAIVHDKVLTLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPRRSVYSSNSQSGQNSPAVNSPQQMESILHPVTLPSGRDTSSNVPITPTQEQIKKLRSELEVVNGNVKVMSEMLTELVPSQAETSDLELLQELNRTCRAMQQRVLELIPRVQHEQLTEELLLINDNLNNVFLRHERFERVRTGQPVKAPSEAENNLIDLRPSTPPAVRQPEVTNNLSSQLAGMTLGSRSVSAGLHSLDTSGKLEEEFDMFAVTRGSSLAEQRREVKYEDPQATKGLAGALDARQQNTGAEESSASSDGAQLTNWMMRQGMVPVPQANFMEDIEKWLSTDVGESEDGKGVTSEEFDKFLEERAKVADRLPTLSSSSAGTPVSPAAASRHQKQAKEDDAMFAL
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Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1 CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation (By similarity). PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation (By similarity). Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity).
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O12971
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LFNG_CHICK
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Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase)
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MLKSCGRKLLLSLVGSMFTCLLVLMVEPPGRPGLARGEAGGAQRALQSLGAARAAGQGAPGLRSFADYFGRLSRARRELPAAPPSPPRPPAEDITPRDVFIAVKTTKKFHKARLELLLDTWISRNRDMTFIFTDGEDEELKKQARNVINTNCSAAHSRQALSCKMAVEYDKFIESGRKWFCHVDDDNYVNVRTLVKLLSSYPHTQDIYIGKPSLDRPIQATERISENKMHPVHFWFATGGAGFCISRGLALKMSPWASGGHFMSTAEKIRLPDDCTIGYIIESVLGVKLIRSNLFHSHLENLHQVPKTEIHKQVTLSYGMFENKRNSIHMKGAFSVEEDPSRFRSVHCLLYPDTPWCPSNVVY
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Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Essential mediator of somite segmentation and patterning.
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O12976
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PSN1_XENLA
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Presenilin-1 (PS-1) (EC 3.4.23.-) (Presenilin alpha) (PS-alpha)
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MNDTSERRSNENSESQSNGQTQSSSQQVLEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRFDGQLIYTPFTEDTESVGQRALNSILNATIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSYIYLGEVFKTYNVAVDYITLALLIWNFGVVGMICIHWKGPLLLQQAYLIMISALMALVFIKYLPEWTTWLILAVISVYDLVAVLSPKGPLRMLVETAQERNETLFPALIYSSTMIWLVNMADGDPGLKQSASTKTYNTQAPTAHPRSDSAASDDNGGFDTTWEDHRNAQIGPINSTPESRVAVQALPSNSPPSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
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Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins.
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O12990
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JAK1_DANRE
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Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1)
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MPELAVMDLGRQLCVKMKKQRKAEMTIPTAMKGLEIHFYLADTHQLEFFKACYTAEDLCVEAAKRCRISPLCHNLFALYEESQDLWYAPNHVFKVTDETSIKLHYRMRFYFTNWHGTSEIESPVWRHTLSKQKSVLNSQKTTEGTPLLDAASLDYLFAQGQYDFLRGLSPVRPTQTDEEHHEIENECLGMAVLAITHHAKSNNLPLSGAGAETSYKRFIPDSLNRTIKQRNFLTRIRISNVFKNFLNEFNSKTIQDSNIGLYDLKVKYLSTLETLTQGVGREIFKPKNLKVTGESEGSPAQMLPLGDNGMGYEVQVYGTTGISWRRKPAPNQLILKDKPKSKKIKGDKQWNDKKKDSGWTLFSDFHEITHIVIKDCCVTIYRQDNKTMELDLFYRDAALSFAALVDGYFRLTVDAHHYLCTDVAPSSVVQNLENGCHGPICTEYAIHKLRQEGNEEGTYVLRWSCTEYNFIIMTVVCIELDLCESRPVPQYKNFQIETSPQGYRLYGTDTFRPTLKELLEHLQGQLLRTDNLRFQLRRCCPPQPREISNLLVMTTDREPVPQKKTQVSQLSFDRILKEEIVQGEHLGRGTRTNIYAGILKPKSDDEDDLGGYSQEVKVVLKVLGSGHRDISLAFFETASMMRQISHKHTALLYGVCVRHQENIMVEEFVQYGPLDLFMRRQTTPLSTAWKFQVAKQLASALSYLEDKKMVHGYVCSKNILVARDGLDGEGGPFIKLSDPGIPITVLSREECVDRIPWIAPECVKDTANLTIAADKWSFGTTLWEICYNGEIPLKDKKLSEKERFYAAQCQLATPDCDELAKLMTHCMTYDPRQRLFFRAIVRDIVMVEKQNPSIQPVPMLEVDPTVFEKRFLKKIRDLGEGHFGKVELCRYDPRGDRTGELVAVKSLKPENREEQSNNLWREIHILRELYHENIVKYKGICNEEGGRSIKLIMEFLPAGSLKEYLPRNKAHINLKTLHNYSVQICQGMDYLGSRNYIHRDLAARNVLVENEGTVKIGDFGLTKSIKDNEGYYTVKDDLDSPVFWYAPECLIHCKFYRASDVWSFGVTMYELLTYCDASCSPMSVFLKLIGPTHGQMTVTRLVKVLEEGKRLPRPDDCSEQLYNLMRRCWEATPEKRIDFKSLIANFQQMLDNL
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Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (By similarity). Appears to be required in early development for specific cell migrations (epiboly), expression of homeobox protein goosecoid and formation of anterior structures.
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O13010
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PI42A_PIG
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Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(5)P-4-kinase isoform 2-alpha)
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MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSXARSGARFHTSYDRRYVIKTITSEDVAEMHNILKNYHQHIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNXKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPNIDVYGIKCHENSPRKEVYFMAIIDILTHYDAKKKAAHAAKXVKHGAGAEISTVNPEQYSKRFLDFIGHILT
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Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (By similarity). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (By similarity). May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P (By similarity).
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O13012
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ESR2_ANGJA
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Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
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MAGSPGNELPLLQLQEVDSSKVGESGGSSGLLPTMYNGALPALSMESHAVCIPSPYTDSSHDYAALTFYSPPILSHGGPAVPESPAARQSLSPSLFWPAHGHHGHVSPLALHFQQPLVYREPAHSPWAEPKPLEHGQAQTSKLAGKRMAESEEGTSSVGGCFAGKGDMHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNGYICPATNQCTIDKNRRKSCQACRLRKCYEVGMMKCGVRRERCTYRGARHRRMPHIRELAGTGGGARTQRRGEGVVPQTQEAQSSALTPEQLINRIIEAEPPEIYLMKELKKPFTEDSMMMSLTNLADKELVLMISWAKKIPGFVELDLSDQVHLLECCWLEVLMLGLMWRSVDHPGKLIFSPDLKLNRDEGSCVEGILEIFDMVLAATSRFRELKLQREEYVCLKAIILLNPNLCTTSSENREELESRNKLLHMLDSVTDALVWTIAKKGLTFQQQSARLAHLLMLLAHIRHLSNKGMEHLSNMKRKNVVPLYDLLLEMLDANTMHSSRMSASYSSQPSPWSQAAQSQPGPPPSCSGECPCPPKESSTI
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Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.
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O13016
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PTN1_CHICK
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Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) (CPTP1) (Protein-tyrosine phosphatase 1B) (PTP-1B)
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MEIEKEFHRLDQAASWAAIYQDIRHEASDFPCKVAKHPRNKNRNRYRDVSPFDHSRIKLNQGDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSIKCAQYWPRKEEKEMFFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPEYGPVVVHCSAGIGRSGTFCLVDTCLLLMDKRKDPSSVDVKQVLLEMRKYRMGLIQTADQLRFSYLAVIEGAKFIMGDASVQEQWKELSNEDLDPPPEHTPPPPRPPKRTSEMHNGRMHEHAEFFPKHQVVEEEIRCSVSTAEETVSDGRVFSSVPLITDSTSQDTEIRRRTVGENLHVTAHKEESKSESVEEDDENMMTTWKPFLVNICMFTFLTAGAYLCYRVCFH
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May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity).
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O13023
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HHEX_XENLA
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Hematopoietically-expressed homeobox protein hhex (Homeobox protein hex) (XHex) (Hhex-A protein)
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MQYQHPSSSALGLSVPLFAPTPLQHPTPFYIDDILGRNSASNGTPALPTPTLPSPNSSFTSLVATYRTPIYEPTPIHPAFTHPGAALAASYGASTYASPLYPFSRPVSDYTHALIRHDSLGKPLLWSPFIQRPLHKRKGGQVRFSNDQTIELEKKFETQKYLSPPERKRLAKMLQLSERQVKTWFQNRRAKWRRLKQENPQGNKKDETESLENICEESQERCLSAEQKSRESSLDDPTSSPTSQGNLDSEVSDDSDQEVDIEGDKGYYNCAH
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Recognizes the DNA sequence 5'-ATTAA-3'. Transcriptional repressor. Regulates the differentiation of both endothelial and blood cells (By similarity). Probably plays a role in the proliferation of vascular endothelial cells during blood vessel development. Establishes anterior identity at two levels acts early to enhance canonical wnt-signaling by repressing expression of tle4, and acts later to inhibit nodal-signaling by directly targeting nodal/nr1 and nodal2/nr2. May play a role in liver development. Induces heart development.
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O13024
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INCEA_XENLA
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Inner centromere protein A (XL-INCENP) (xINC) (xIncenp) (Mitotic phosphoprotein 130)
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MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRQSNASWSSSVRRLSVRNQNKANDDSIQEEPAQLKRMTRARAQASIKSTPVLETALPESPSQICQKNAQVKISEQERRSAEQKLIESDFELKTVPEITKDNVSETVNSAVPAVPVTPENKSRAAGKLKIAASSTPEQKAEMVDLTCESPRPANEQQLNLSNQSATPTGSKSDRRSVRRSLVVRKSSSRRASLASQFSLASKRESMTREAVRKSIRQSISQKKAAMEISSTSSQRSYQSSIEMVDDEITIKIRPETVPSETVSEEAPAAESPRRSLRSRAFKKIAISNLPDSEEPPRKVTRQMVAGNAEPTPETTEDAQNIRRKSYKRAVDELSDDERPSEEERSPPRKKTPSPPCPPSKIVRPPPHMKSFLHTVQKNQLLMMTPGSIGKNIIMKSFIKRNTPLKTDPKTEEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKVRREERLRKVLQARERVEQLEEEKKKKIEQKFAQIDEKSEKVREDRMAEEKAKKKMTAKKQEEVECRRKQEEEARRLKVKQMEEEERRHQELLQKKREEEELERQKKIAEAKRLAEQERERQLLAEKERLRAEREKERIEKEKALQLQRELERAAQEKEQQRREAEERKKREQQERLEQERLRKEQEAKRLQEEEQRKAKEQAAVAASAPVMNVTVDMQNSPACESYEMTPKSCKVPSVKVNEDNYGMDLNSDDSTDDESQPRKPIPAWASGNLLTQAIRQQYYKPIDVDRMYGTIDSPKLEELFNKSKPRYFKRTSSAVWHSPPLSSNRHHLAVGYGLKY
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Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with aurkb/aurora-B, the N-terminus associated with cdca8/borealin and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs aurkb/aurora-B toward substrates near microtubules. Activates aurkb.
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O13033
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RAG1_DANRE
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V(D)J recombination-activating protein 1 (RAG-1) [Includes: Endonuclease RAG1 (EC 3.1.-.-); E3 ubiquitin-protein ligase RAG1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAG1)]
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MEKGRWSSEDAPRASMPDELSHPKFSEWKFKLFRVRSMEKAPVQNETPVEKENQPELAMEKTSSQGSVMRLCFGGKSKENVESARGRVDLKLQEIDTHMNLLKNMCRLCGIAIQKAKGPSHEVQGVLEESSRCALRRMGCKLVTWPEVILKVFKVDVTTDMETVHPSLFCHRCWTAAIRGGGFCSFTNTRIPDWKPHTSQCNLCFPKKSSFQRVGRKRTKPLKSAHILPKRFRRDSSESSRVWRQTTENPDGKEWLKLSVQRGQWVKNITRCQRDHLSTKLIPTEVPADLIRAVTCQVCDHLLSDPVQSPCRHLFCRLCIIRYTHALGPNCPTCNQHLNPSHLIKPAKFFLATLSSLPLLCPSEECSDWVRLDSFREHCLNHYREKESQEEQTPSEQNLDGYLPVNKGGRPRQHLLSLTRRAQKHRLRDLKNQVKTFAEKEEGGDVKSVCLTLFLLALRAGNEHKQADELEAMMQGRGFGLHPAVCLAIRVNTFLSCSQYHKMYRTVKATSGRQIFQPLHTLRNAEKELLPGFHQFEWQPALKNVSTSWDVGIIDGLSGWTVSVDDVPADTISRRFRYDVALVSALKDLEEDIMEGLRERALDDSMCTSGFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTIMSISIRLEGEDDGITIFQEQKPNSELSCRPLCLMFVDESDHETLTAILGPVVAERKAMMESRLIISVGGLLRSFRFFFRGTGYDEKMVREMEGLEASGSTYICTLCDSTRAEASQNMVLHSITRSHDENLERYEIWRKNPFSESADELRDRVKGVSAKPFMETQPTLDALHCDIGNATEFYKIFQDEIGEVYQKPNPSREERRRWRSTLDKQLRKKMKLKPVMRMNGNYARRLMTREAVEAVCELVPSEERREALLKLMDLYLQMKPVWRSTCPSRDCPDQLCQYSYNSQQFADLLSSMFKYRYDGKITNYLHKTLAHVPEIVERDGSIGAWASEGNESGNKLFRRFRKMNARQSKTFELEDILKHHWLYTSKYLQKFMEAHKNSVKAMQATFNPEETPEEADNSLDVPDF
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Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity).
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O13034
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RAG2_DANRE
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V(D)J recombination-activating protein 2 (RAG-2)
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MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGGSLGKGTALVAIPSEGNPTPPEAYHFYQVSFQKEQDGEATAQGCSQESTDFEDSAPLEDSEELYFGREPHELEYSSDVEGDTYNEEDEEDESQTGYWIKCCLSCQVDPNIWEPYYSTELTRPAMIFCSRGEGGHWVHAQCMELPESLLLQLSQDNSKYFCLDHGGLPKQEMTPPKQMLPVKRVPMKMTHRKAPVSLKMTPAKKTFLRRLFD
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Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex, rag2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity).
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O13076
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AA2BR_CHICK
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Adenosine receptor A2b (Adenosine receptor 2b)
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MNTMKTTYIVLELIIAVLSIAGNVLVCWAVAINSTLKNATNYFLVSLAVADIAVGLLAIPFAITISIGFQVDFHSCLFFACFVLVLTQSSIFSLLAVAIDRYLAIKIPLRYNSLVTGKRARGLIAVLWLLSFVIGLTPLMGWNKAMSGCPNSTNETGADHGAGHHGCFISCLFENVVTMSYMVYFNFFGCVLLPLIIMLGIYIKIFMVACKQLHQIELMGNSRTTLQKEVHAAKSLAIIVGLFAFCWLPLHILNCITHFHEEFSKSKPEWVMYVAIILSHANSVINPIIYAYRIRDFRYTFHKIISKILCKTDDFPKCTTDNNQHLTVTNVNAPAASVTI
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Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
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O13097
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EFNB1_XENLA
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Ephrin-B1 (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) (XlERK)
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MEGLRRLLGLLLVLYRLCSALGKNLEPVTWNSQNPRFISGKGLVLYPEIGDRLDIICPKGDSSQPYEYYKLYMVRRDQLEACSTVIDPNVLVTCNQPGKEYRFTIKFQEFSPNYMGLEFRRNQDYYITSTSNSTLQGLENREGGVCQTRSMKIIMKVGQDPNAVPPEQLTTTRPSKEADNTGKIATFGPWNGPVENPGKSDTNLSDKPTAGGGVDGFFNSKIAVFAAIGAGCVIFILIIIFLVVLLIKIRKRHRKHTQQRAAALSLSTLASPKCSGNAGSEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
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Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity). May have a role in the developing mesenchymal and nervous tissue.
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O13146
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EPHA3_DANRE
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Ephrin type-A receptor 3 (EC 2.7.10.1) (EPH-like kinase 1) (Tyrosine-protein kinase receptor ZEK1)
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MALFRIYSFLAPFHILVLCQALRNYPDNEVTLLDSMSAPGDLGWEAYPSEGWEEISVMDERNIPMRTYQVCNVMEANQNNWLRTGLIQREGAQRVYVEIKFTLRDCNSLPGVPGTCKETFNVYYHESNNAVAAPLRHIRESQYIKIDTIAADESFTQTDVGDRVMKLNTEVRDISGLSKRGLYLAFQDLGACIALVSVRVFYKRCPLAVLNLARFPDTVTGGDSALVEVRGTCVEDAEELEGPRMFCSADGGWLVPIGRCVCRPGFEEVDGHCQPCRSGFYKASAMDAYCVKCPPHSYSHQDKASECVCERGFYRAESDPRSMACTRPPSAPGNPISMVNETAVTLEWSPPRDSGGRGDVSYSVHCRKCSGETGASERCVPCGSGAHFNPRQFGLTHPRVLVTELQPHTNYTFSVEALNGVSDLSPSPRQLVSVNVTTSQTVSVILKERKGTDSVTLAWQGPEPVDGTVVEYEVTYYEKNQQDQNYTVLKTKSNSMTVDGLKPGTTYIFRVRARTDGGYGNYKGEIELETSHEDMLAVGDPNQQTILAISVAGGAVLLVLLVACFIVSGRRCGYIKAKQDPEEEKMQFQHGRVKLPETRTYIHPHTYEDPNQAVRDFAKEIEVSNIRIERVIGAGEFGEVCSGRLRLPSKREIQVAIKSLKAGYSEHQRRDFLSEASIMGQFDHPNIIRLEGVVTRCKPVMIVTEYMENGSLDTFLKKHDGQFTVIQLLGMLRGIAAGMQYLSEMNYVHRDLAARNILVNRNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVISYGERPYWEMSNQDVIKAVDEGYRLPAPMDCPVVLHQLMLDCWEKNRSDRPKFGQIVNTLDRLIRNPSSLKQLANSAVWEDPVTPEAAVNTVEDWLDLIKMGQYKEHFSSAGYVTLDSVLYVSSSELDKMGVELAGHQKKILSSIQCLQAHHGTQVQV
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Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially efna5. Upon activation by efna5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation probably through activation by efna1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).
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O13147
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EPHB3_DANRE
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Ephrin type-B receptor 3 (EC 2.7.10.1) (EPH-like kinase 3) (Tyrosine-protein kinase receptor ZEK3)
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PLLVLDLIIQERGESFSHTVTAQHTSAKVEGLKAGTVYSVQVRARTVAGYGRYSNPVDFSTSLYVCPVSSSSTSMHLRRREELTTTTTGLKSREERFQKSDDPERSVQDLLPLIVGSASAGFVVILAMIVIAVVCLRRQRTGSELEYTEKLQQYVSPGVKVYIDPFTYEDPNEAVHEFAREIDISCVKIEEVIGAGEFGEVCRGRLKQAGRKETTVAIKTLKAGYTEHQRRDFLSEASIMGQFDHPNVIHLEGVLTRSCPVLIVTEFMENGALDSFLRLNDGRFTVTQLVGMLRGIAAGMKYLSDMNYVHRDLAARNVLVNSNLVCKVSDFGLSRFLDDNSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVMNAVEQDYRLPPPMDCPAVLHQLMLECWVKERNMRPRFGQIVSTLDKFLRNAASLKVLTSTHSGDLCRIGGTLPGHQRKSIGDAQDIKQQMSQTLPIRV
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Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. May control other aspects of development through regulation of cell migration and positioning (By similarity). May play a role in early pattern formation within the developing nervous system.
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O13148
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EPA4A_DANRE
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Ephrin type-A receptor 4a (EC 2.7.10.1) (EPH-like kinase 2) (Tyrosine-protein kinase receptor ZEK2)
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IGIGEFGEVCSGRLKMPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIRLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGILRGIASGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEEDPDAAYTTREITGTYQSQGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPVSLHQLMLDCWQKERAERPKFSQIVNMLDKLIRNPNSLKRTGGEIARPNTTLLEPSSPE
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Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including efna1 and efnb3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections (By similarity).
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O13154
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PACN2_CHICK
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Protein kinase C and casein kinase substrate in neurons protein 2 (Focal adhesion protein of 52 kDa) (FAP52)
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MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ
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Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. {ECO:0000250, ECO:0000250|UniProtKB:Q9WVE8}.
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O13186
|
GCR_SAIBB
|
Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
|
MDSKESLTPGKEENPSSVLTQERGNVMDFCKILRGGATLKVSVSSTSLAAASQSDSKQQRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLQLLEESIANLNRSTSVPENPKSSASSSVSAAPKEKEFPKTHSDVSSEQQNLKGQTGSNGGNVKLYTADQSTFDILQDLEFSSGSPGKETNQSPWKSDLLIDENCLLSPLAGEEDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSSSNVTLPQVKTEKEDFIELCTPGVIKQEKLSTVYCQASFPGANIIGNKMSAISIHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPANKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSTVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQASSNLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQLPKYSNGNIKKLLFHQK
|
Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression.
|
O13282
|
TAF5_SCHPO
|
Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 72 kDa subunit) (TAFII-72)
|
MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTFHHTNNNMNCAEFSPDSTMIACGFQESYIRLWSIKADKKSLPKSTSVEDSDGSVRLLSHSGPVYGTTFSPDNKYLLSCSEDASARLWSVDTKTALVAYKGHTGPVWDVAFGPFGHYFATASHDQTAQLWSCDHIYPLRVFAGHLSDVDCVTFHPNSAYVLTGSSDKTCRLWDVHRGHSVRVFNGHTQPVTAVAIAPDGHTMASADSEGLIHLWDIGTGRRIKTMRGHRGNIYSLSFSRESTVLVSGGSDCTVRAWDVFKTNYNNPVSSSLTGSVVTPFSAKTSTFNEVNWSTSPDQMVALYTKQTPIFNVSFTRRNLCLAISVS
|
TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis.
|
O13286
|
SRW1_SCHPO
|
WD repeat-containing protein srw1 (Suppressor of rad/wee1)
|
MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDAATCKKTRTMSGHTERVGALSWNDHVLSSGGRDNHILHRDVRAPEHYFRVLTAHRQEVCGLEWNSNENLLASGGNDNALMVWDKFEEKPLYSFHNHIAAVKAITWSPHQRGILASGGGTADRTIKLWNTQRGSMLHNIDTGSQVCNLLWSKQTNEFISTHGFMENEVALWNYPSVSRVGTLKGHTDRVLYLAMSPNGENIVTGAADETLRFWKLFDSKSKHSASTMSSPFDPTMKIR
|
Has a role in cell differentiation and cell cycling by negatively regulating cig2 and cdc12-associated cdc2. Down-regulates the level of cdc13, particularly in a nitrogen deprived environment. Regulator of cell cycle G1 phase progression. Prevents onset of mitosis during the pre-Start G1 period. Required for degradation of cdc13 mitotic cyclin B during G1 arrest but not during mitotic exit.
|
O13289
|
CATA_CANAL
|
Peroxisomal catalase (EC 1.11.1.6)
|
MAPTFTNSNGQPIPEPFATQRVGQHGPLLLQDFNLIDSLAHFDRERIPERVVHAKGSGAYGVFEVTDDITDICAAKFLDTVGKKTRIFTRFSTVGGELGSADTARDPRGFATKFYTEEGNLDLVYNNTPVFFIRDPSKFPHFIHTQKRNPETHLKDANMFWDYLTSNEESIHQVMVLFSDRGTPASYREMNGYSGHTYKWSNKKGEWFYVQVHFISDQGIKTLTNEEAGALAGSNPDYAQEDLFKNIAAGNYPSWTAYIQTMTEAEAKEAEFSVFDLTKVWPHKKYPLRRFGKFTLNENPKNYFAEVEQAAFSPAHTVPYMEPSADPVLQSRLFSYADTHRHRLGTNYTQIPVNCPVTGAVFNPHMRDGAMTVNGNLGSHPNYLASDKPVEFKQFSLQEDQEVWNGAATPFHWKATPADFKQAQELWKVLKRYPNQQEHLAHNIAVHAAGADAAIQDRVFAYFGKVSQDLADAIKKEVLELSPRK
|
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Required for hyphal growth.
|
O13290
|
DYHC_SCHPO
|
Dynein heavy chain, cytoplasmic (Dynein heavy chain, cytosolic) (DYHC)
|
MDKNDNSQCQLSTVSDEILIFLKKLLSLSVSDNLDDICETIALQSTFVDTFRSFINDEYYTVIYLYGSPCLTSSPTSPDSCTFGNMTFQWTSLLQDVFSGTSAFAIFKRFPLTDTPLTLQNMLYINQLPILKGGHKSNEIPERPINAIFLYTKYVMSCYFTAYLAMESVDDRSTIDLNSPSKGKELELTCQKFADFERSFTFFCREYQNSDTILQHHPLILSTIKHAEENNLDLSVRLLPSKVLSDSEFYKSLSNLVNVWLKTTRSLIKLFHDQISKTALEEFNFWQFYYRSLSRLNDQLHSRPVLFVLDILAFGKRFHTIASFNSETNIQCFVDKVGKIDALFKEISLDIFLSSSTLESLQLSAALLYSTFSKKWRNTGYPETRVLDFINFITEDLLKLISRLLPALGALSLSNVDFSHRTAVSSDILSLCYIRLKDFLRISGSLKEEQSYYGLKNSIKQIKAFENKLKYIQSFHEKHQQLIGALSEVYGLTHLTELEILEHLNKKEHVFNILTVFKDLQSLNVLDISLKGVNAWNSLETSYYNCMTVLEDEVIAQLKSLLQYSKTSSQMFTTLMRFQPLFFRTRVRTSISDCLHLLVNRIKQELDLLKTRFTEDVSDTELIAMNELRNLPMASSAIIWATQLKNRLHEYTKNINIIFGEDWNNFPDGFELKVECITLQKRLDTNLIFTNWINDVSSRNLNFDFDSKIFYLTQSESAESPLRLSVSIDFDPCSFCKEIRTLAHLGYNIPSQLMELASCLQRIQLIAMCLIDSVQSFNDVSFEISKTEEERFLLQEYELAVRQHIVTGLFISWNDFIVGNLSTPPKCAIGKRNFLKNIHPNVENYAYQFSSLTSLLMNKRNAISHTYMQIQEQLFQLDICEYSGDIFLTIQRKLQDLIDLLYVNGYSNLPPFVRALNLRFQDLLISRCRKFLSFFKTTILTSGNENNDLKSKFSSDMYEKLRGFLKPTNLTIQRNIIEFDPPVYRKKEDSIYLLDMCLQSVVNIPLLSIKTTAQRNCTLIGFFPVINRLESEILGIFESLLFHFDSILGYQNYWKKVEPFLNLNSLNLLLKSELFQLDQCYSLSLYLIHLKSEVDEIGKVTDFKIFSVNNTEFKSQVYLYLREWINALFDRFTFLLGKESEHLLNELDDTHSSLSTVDFTVNNTESLINSLKIFKKAGCYKLNVEHKIITYQNYEMTFNDCDAFSEFNFSLLKDITSKWKDLLESFECRRLKLENNKDEILRNFSEFAKRVNTETLSLISEWCASSLSLIKANYDEFSSTVDDFLFRFSKATEQCLMVKYIKKDLEIEIEESCDFSIQTEEIHLYKKFKDVISSNLEFIVEIKNTRWKLFDTATLSVQTTHQINALESVHTSFQHFKLFTNTKQSLNQLKDCTLLLQKLKSCPLKPVHWISLFEITKSTEQLDFEKLLVSDILGIDLQAHESFITTLLNSAVVEANLENQFNEVHSFWKNSYFSFKSFKGRNYIVVGCQELIDAVEKNMDSLNLIKTSRHFKDGDMNITDLQSKMKIIVKFLNIWKEIQQIWTHLSAIFYESTYIQQLLPELAASFFNSSKTYMHLVTLLKERSYLYKVSNIPSLLESAAKLSTTLEDSKKSLLKYFELQRHKISRLYFLGDDDLMELISNPCDPFVINKQIIKLYPGIRSLIVDTENTNINGCTTNEGNELLFDNPICLLDNTQPLHWISSLEPFLKATLFQLFSTSFQQIRDFYYNKSRNVFCKEWFLRYPSQITLLSLRCTLCHEIETGIADCCLDAVFNFINDGISSLVLLADENELSIKKKVTLMFNELLHFKETVGLLCKNSFNNYFWSREVKAFYREDHDDEAVVIKMFSLEFIYAFEYSELDDPIVYTDLTRNCFSVLLHSIASNLGGSPIGPAGTGKTETVKAVSAYLGKNVFVFNCDNAFNYKTIQRILSGLAQIGTYICFDEFNRLDSGTLSAISYDIQRIQSLVSHSDGLCQSPILLDAPTIFVTMNPGYLGRFKLPSNLKKLFRPIWMGSPDNKKICEILFLSFGFKESSLLSQVLDSFFLCCSGSLSNCLHYDFGLRAMKVVIKAAKRIKGFLKKKNTICQELEILWYAIREVLYPSLIYQDIPLFFKAEESYFNFPAVKANAFIDPDNFEVNIEQTLSKNFFGNNQYLKLKIMQLYQMSEAYNGIILLGKTGSGKSQIFRILQSALLNIGIDCIVYVISPKALTKESLFGSMNMDTREWTDGVFTKLLRKTRDSCYYKRYMFVFDDELSPEWVEAMNSLLDDNKTLTLSNGERIALQPYVKIFFEADSVASLTRATISRCGLICISNIDDNILSSTDKMLSFTSGATNYPLGSSNDEFSTVFSKVLTDEVMMNLISSCYKFSVDLQHIMNFTKQRFFTTFYSLLDQTKLFTRSSNITESLSFKELCNYLKKKICYILAWCCTGDTDAKSRERFTHWLMQNASVDLPEIKDFEHVSILDFDVSLETQSWYPIAGKTLKSSALKYAGNTVIPTLDTVRYAEFLNFSLTKNRCVIFCGPPGSGKSMLMLGTLRSRQDVEVIALNFSISTSSKSVVSFLEQSTVYYRSTGMTIMCPKNHEKVLVLFCDEINLPRSRNCLAEDVICFLRHMLEHQGFWHPLHKEWVTIKNIFVCGACNPSTDIGRNDFPERFLRRTVLIFVDYPESYSLVTIYNALLEKSALINQYKTIILNIVKASVKFYQVLRENFKSSTQGYVYTPRDLTRWLISFKNYAESYAETNNLSLIKVWYHEACRVLLDRLVSQKECSWGMTELQKVIVTDFGEFEVSVIFEKQIIFTDILKNGLEFLDFASLRPKLESLYKKFYSSHPNNTLVFVDETITHILRFHRILNNSGMHALLQGSVGLGQKAVVEFVCWLNSFSLFELQKNQTYSIEDFEDNLKSILILAGTTNCKACLAINESIAGVPGFLDLLNNLLTNSEVSNFFDQNDWAEIKKNLNKLNEFQPLKFDSEESVTEIFMNNVFQNLCVVFYVYTSADVDFQTNSLSPALLNRCTIDYYHSWDYHSMLQIANEVLQETISLNALDHDNPNLKNIKGSSIYDAVAQAVVNTHTSIVWEFKHLGKTSYFSCLHFIRFLNTFCLIFGRDANKLSKEKSRIENGFKKIKETSQGIDKFKEALSDQQNVLFSKTKTANDRLQCIIQTKQAVEAKKVYSLQAEASLQKKSFLLNEKKNSVMKEVSYAKPAVIEARKSVSDIKKAHLIELRSLSRPPMAIRITMEVVCKLLGFSATDWKNVQQLLKRDDFIPKILNYNLEKELSINLRRKIEQDYFSNPIFTFDSVNRASKACGPLLLWIKSICNYSKVLEKLEPLNSEVDRLKLEQKNAEECIQETIAACKDLDEKLLQLQEEYASMISEIHSMELQMDEVKCKMQRSIEVITDLSIERNEWSGFLNLYPKRMWNLVGESLMEASFVVYAGNLDPSMRIFLRNKCEPIISSFGFPISKSAVRTNIERCVQTSIESKYYKNLTDYSLENIYIIQENKSPLLIIDPSSQILDILPSLYKGKASDLISFSNKSFQNQIKLALLSGSAIIIKDAELWDVSIEPLLKPEFFTGSGEVQTTFAKDTITITLPLNIIFFSEVQSNELENKASKFMNVVNFTLSISLLETQMLKSVISVQEPGVFKQKDNCFTLKLSIERQIRSLQEQLLKTLCSSNENIVGTDEIVVLLKNLKEKHETIRLAYSESQSINRKVDELIRRYKLSIKSFLSVVVVFQHFISLKKSYSFSFNFIWSTFHQMLNVVLENRNQDFKSLIMDALRDLIRRCFLYIFPEDRVLFLFLLMFFFFPKETESLRKLLIVNGKTLELEQSYLNFFETCSDSNERGGLESLFFKTHASNIQNFCTEVLANTHCEEDCLKLLYDLWSSAFKVEFSNIKYDFLKIINDESESRMPTIVYLMENCEIDSLLQNAKIPQNIKKLTVSLGSAENESLADSYLKLASTEPLWLFINNIHLSTPWAEKLPSKMSNHLHKNSRIVCLSEIHNQLPHQLLCISRSIVFNKQTSFKNNLLNLLELLPTMTHTLPHNRFRLFFFLSWLHATLAEIYCFTCSSWKEPCYFDDSDFYFGTKILCNILYRNVHLEEFSWGTFKDLLLNVVYGPKVSASSDFIALDKILKRLIAQFKTQISSNILLTDNFKFILPYEITFSSAKEVIGQLPDEIPPGWLDIPENSKRKRTDIYFSMCI
|
Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity the force-producing power stroke is thought to occur on release of ADP. Required for nuclear movement during meiotic prophase.
|
O13297
|
CET1_YEAST
|
mRNA-capping enzyme subunit beta (EC 3.6.1.74) (mRNA 5'-phosphatase) (mRNA 5'-triphosphate monophosphatase)
|
MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM
|
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
|
O13298
|
PHD1_SCHPO
|
Histone deacetylase phd1 (EC 3.5.1.98)
|
MDTPETSTPYEQVEKGSFFSFRPQKKRVTYHLDEQVGNYHYGDKHPMKPHRITITNHLVMGYGLHNKMSVFSPRMATFGEMSEFHREDYLDFLKRVTPDNAEQFADKFQQFNIGDDCPVFDGTYEFSQRSAGASLDASRKLVQGQTDIAINWSGGLHHAKRGEASGFCYVNDIVLAILNMLRFFPRVLYIDIDIHHGDGVQQAFYESDRVLTVSFHKYNGDFFPATGNFDENGVKGGKYFALNVPLEDGIGDEQYTSLFKSIIEPTINTFQPSAIVLQCGADSLGYDRLGVFNLSIHAHGECVRFTRSFNIPMLVVGGGGYTLRNVARAWCYETSICVNEQIPSELPRETLYYEFFAPDYTLHPRLTTKIENKNTPKALEDLRIRALEQLRYLGGAPSVQMQQIPPDLTGHLEEEDERLNDEYLDKAVDVRVRG
|
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Is not essential. {ECO:0000250, ECO:0000269|PubMed:9781677}.
|
O13310
|
ORB6_SCHPO
|
Serine/threonine-protein kinase orb6 (EC 2.7.11.1)
|
MDKNDYLHFERNPSLFPKSTLDKVQKTKKYIEHYYKVAVDHAVERNQRRINLEQRLATERGSEERKNRQLRASGEKESQFLRFRRTRLSLEDFSTIKVIGKGAFGEVRLVQKLDTGKIYAMKSLLKTEMFKRDQLAHVKAERDLLVESDSPWVVSLYYAFQDSLYLYLIMEFLPGGDLMTMLINYDTFSEDVTRFYMAECVLAIADVHRMGYIHRDIKPDNILIDRDGHIKLSDFGLSTGFYKQDQSASYMKPRTGNTVKRGQMVDAIWLTMSSKDKMATWKKNRRVMAYSTVGTPDYIAPEIFLQQGYGQDCDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLTFPNDIHLSIEARDLMDRLMTDSEHRLGRGGAIEIMQHPFFTGIDWDHIRETAAPFIPNLKSITDTHYFPVDELEQVPEQPVTQQPASVDPQTLEQTNLAFLGYTYKKFNYLTMKGAL
|
Interacts with pak1/shk1 and coordinates cell morphogenesis with the cell cycle. It is essential for maintenance of cell polarity and is involved in mitotic control.
|
O13318
|
PHR2_CANAL
|
pH-responsive protein 2 (pH-regulated protein 2)
|
MLLKSLFPSILAATSFVSSVAAEDLPAIEIVGNKFFYSNNGSQFYIKGIAYQQNNLDSNESFVDPLANPEHCKRDIPYLEAVDTNVIRVYALDTSQDHTECMQMLQDAGIYVIADLSQPDESINRDDPSWDLDLFERYTSVVDLFHNYTNILGFFAGNEVTNKKSNTDASAFVKAAIRDTKAYIKSKGYRSIPVGYSANDDSAIRVSLADYFACGDEDEAADFFGINMYEWCGDSSYKASGYESATNDYKNLGIPIFFSEYGCNEVRPRKFTEVATLFGDQMTPVWSGGIVYMYFEEENNYGLVSIKDNTVSTLKDYSYYSSEIKDIHPSSAKASAESASSISRTTCPTNTNNWEASTNLPPTPDKEVCECMSASLKCVVDDKVDSDDYSDLFSYICAKIDCDGINANGTTGEYGAYSPCHSKDKLSFVMNLYYEQNKESKSACDFGGSASLQSAKTASSCSAYLSSAGSSGLGTVSGTVRTDTSQSTSDSGSGSSSSSSSSSSSSSSGSSGSKSAASIVSVNLLTKIATIGISIVVGFGLITM
|
Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism (By similarity).
|
O13326
|
CYSD_SCHPO
|
Homocysteine synthase (EC 2.5.1.49) (O-acetylhomoserine sulfhydrylase) (OAH SHL) (OAH sulfhydrylase)
|
MPVESEHFETLQLHAGQEPDAATSSRAVPIYATTSYVFRDCDHGGRLFGLQEPGYIYSRMMNPTADVFEKRIAALEHGAAAIATSSGTSALFMALTTLAKAGDNIVSTSYLYGGTYNLFKVTLPRLGITTKFVNGDDPNDLAAQIDENTKAVYVESIGNPMYNVPDFERIAEVAHAAGVPLMVDNTFGGGGYLVRPIDHGADIVTHSATKWIGGHGTTIGGVIVDSGKFDWKKNSKRFPEFNEPHPGYHGMVFTETFGNLAYAFACRTQTLRDVGGNANPFGVFLLLQGLETLSLRMERHVQNAFALAKYLEKHPKVNWVSYPGLESHVSHKLAKKYLKNGYGAVLSFGAKGGPDQSRKVVNALKLASQLANVGDAKTLVIAPAYTTHLQLTDEEQISAGVTKDLIRVAVGIEHIDDIIADFAQALEVA
|
Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Can also use O-succinyl-L-homoserine and L-homoserine as substrates. Has also cysteine synthase (O-acetylserine sulfhydrylase) activity in vitro, but in S.pombe, it seems only to be involved in the alternative pathway of methionine biosynthesis under cysteine deficiency conditions.
|
O13329
|
FOB1_YEAST
|
DNA replication fork-blocking protein FOB1
|
MTKPRYNDVLFDDDDSVPSESVTRKSQRRKATSPGESRESSKDRLLILPSMGESYTEYVDSYLNLELLERGERETPIFLESLTRQLTQKIYELIKTKSLTADTLQQISDKYDGVVAENKLLFLQRQYYVDDEGNVRDGRNNDKIYCEPKHVYDMVMATHLMNKHLRGKTLHSFLFSHFANISHAIIDWVQQFCSKCNKKGKIKPLKEYKRPDMYDKLLPMERIHIEVFEPFNGEAIEGKYSYVLLCRDYRSSFMWLLPLKSTKFKHLIPVVSSLFLTFARVPIFVTSSTLDKDDLYDICEEIASKYGLRIGLGLKSSARFHTGGILCIQYALNSYKKECLADWGKCLRYGPYRFNRRRNKRTKRKPVQVLLSEVPGHNAKFETKRERVIENTYSRNMFKMAGGKGLIYLEDVNTFALANEADNSCNNNGILHNNNIGNDNFEEEVQKQFDLTEKNYIDEYDDLAHDSSEGEFEPNTLTPEEKPPHNVDEDRIESTGVAAPMQGTEEPEKGDQKESDGASQVDQSVEITRPETSYYQTLESPSTKRQKLDQQGNGDQTRDFGTSMEL
|
Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB.
|
O13339
|
TERT_SCHPO
|
Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit)
|
MTEHHTPKSRILRFLENQYVYLCTLNDYVQLVLRGSPASSYSNICERLRSDVQTSFSIFLHSTVVGFDSKPDEGVQFSSPKCSQSELIANVVKQMFDESFERRRNLLMKGFSMNHEDFRAMHVNGVQNDLVSTFPNYLISILESKNWQLLLEIIGSDAMHYLLSKGSIFEALPNDNYLQISGIPLFKNNVFEETVSKKRKRTIETSITQNKSARKEVSWNSISISRFSIFYRSSYKKFKQDLYFNLHSICDRNTVHMWLQWIFPRQFGLINAFQVKQLHKVIPLVSQSTVVPKRLLKVYPLIEQTAKRLHRISLSKVYNHYCPYIDTHDDEKILSYSLKPNQVFAFLRSILVRVFPKLIWGNQRIFEIILKDLETFLKLSRYESFSLHYLMSNIKISEIEWLVLGKRSNAKMCLSDFEKRKQIFAEFIYWLYNSFIIPILQSFFYITESSDLRNRTVYFRKDIWKLLCRPFITSMKMEAFEKINENNVRMDTQKTTLPPAVIRLLPKKNTFRLITNLRKRFLIKMGSNKKMLVSTNQTLRPVASILKHLINEESSGIPFNLEVYMKLLTFKKDLLKHRMFGRKKYFVRIDIKSCYDRIKQDLMFRIVKKKLKDPEFVIRKYATIHATSDRATKNFVSEAFSYFDMVPFEKVVQLLSMKTSDTLFVDFVDYWTKSSSEIFKMLKEHLSGHIVKIGNSQYLQKVGIPQGSILSSFLCHFYMEDLIDEYLSFTKKKGSVLLRVVDDFLFITVNKKDAKKFLNLSLRGFEKHNFSTSLEKTVINFENSNGIINNTFFNESKKRMPFFGFSVNMRSLDTLLACPKIDEALFNSTSVELTKHMGKSFFYKILRSSLASFAQVFIDITHNSKFNSCCNIYRLGYSMCMRAQAYLKRMKDIFIPQRMFITDLLNVIGRKIWKKLAEILGYTSRRFLSSAEVKWLFCLGMRDGLKPSFKYHPCFEQLIYQFQSLTDLIKPLRPVLRQVLFLHRRIAD
|
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
|
O13345
|
AFLQ_ASPPU
|
O-methylsterigmatocystin oxidoreductase (OMST oxidoreductase) (EC 1.14.14.117) (Aflatoxin B synthase) (Aflatoxin biosynthesis protein Q) (Cytochrome P450 64) (Cytochrome P450 monooxygenase aflQ)
|
MIYSIIICAGALLGFLILQKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHHERYGPMSSLEVMGQTIIMINDAHLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNKQAWKTIRANMKQEIGTRRAIATFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCTRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALYPEVQHQAREELDRVVGPTTLATFEHRSQLPFIDALVKEVFRWHPASPLGAPHITQEDQIWDGYLLPKGALLLPNIWTFTHDPSVYHDPMVFKPERFLERQSSPPETDPMKFVFGFGRRICPGRFVTDEKLFLIACHAISCFLISPKDPGAPEPDWLPGVISQPGPFDLNVVPRSPAHEELIRSIETDHPWKNADATDISQFMARNQMI
|
O-methylsterigmatocystin oxidoreductase part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the O-methylsterigmatocystin oxidoreductase aflQ is involved in the last steps in which OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2. The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1.
|
O13351
|
PMT3_SCHPO
|
Ubiquitin-like protein pmt3/smt3
|
MSESPSANISDADKSAITPTTGDTSQQDVKPSTEHINLKVVGQDNNEVFFKIKKTTEFSKLMKIYCARQGKSMNSLRFLVDGERIRPDQTPAELDMEDGDQIEAVLEQLGGCTHLCL
|
Required for chromosome segregation where it may be involved in microtubule assembly. Loss of smt3 leads to an increase in telomere length.
|
O13370
|
DED1_SCHPO
|
ATP-dependent RNA helicase ded1 (EC 3.6.4.13) (Multicopy suppressor of overexpressed cyr1 protein 2)
|
MSDNVQQQVDSVGSVTEKLQKTNISRPRKYIPPFARDKPSAGAAPAVGDDESVSSRGSSRSQTPSEFSSNYGGRREYNRGGHYGGGEGRQNNYRGGREGGYSNGGGYRNNRGFGQWRDGQHVIGARNTLLERQLFGAVADGTKVSTGINFEKYDDIPVEVSGGDIEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQEANQECPSFLIAMARESSFGGNGRGGRYSGRGGRGGNAYGARDFRRPTNSSSGYSSGPSYSGYGGFESRTPHHGNTYNSGSAQSWW
|
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Inactivation of ded1 blocks mitotic cell cycle progression at G1 and G2/M. Induces sexual development and ascus formation. {ECO:0000250, ECO:0000269|PubMed:10725227, ECO:0000269|PubMed:11711540, ECO:0000269|PubMed:16273369}.
|
O13426
|
GLYC_CANAL
|
Serine hydroxymethyltransferase, cytosolic (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (SHMII) (Serine methylase)
|
MSAYALSQSHRQLTEGHLKDTDPEVDQIIKDEIDRQQHSIVLIASENFTTTAVFDALGTPMCNKYSEGYPGARYYGGNEHIDRMELLCQERALKAFGLTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLDLPHGGHLSHGYQTDSRKISAVSTYFETMPYRVDLETGLIDYDMLEKTAVLYRPKVLVAGTSAYCRLIDYKRMREIADKVGAYLVVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSVNPKTGQEILYDLENPINFSVFPGHQGGPHNHTIAALATALKQANTPEFKEYQEQVLKNAKALESEFTKKGYKLVSDGTDSHMVLVSLKDKQIDGARVETVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGLGEEDFKKIVSYIDFAVNYAKEVQSQLPKDANKLKDFKNAVSGDSEKLKAVRDEIYQWAGSFPLAV
|
Interconversion of serine and glycine.
|
O13437
|
FDH_CANBO
|
Formate dehydrogenase (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase)
|
MKIVLVLYDAGKHAADEEKLYGCTENKLGIANWLKDQGHELITTSDKEGETSELDKHIPDADIIITTPFHPAYITKERLDKAKNLKLVVVAGVGSDHIDLDYINQTGKKISVLEVTGSNVVSVAEHVVMTMLVLVRNFVPAHEQIINHDWEVAAIAKDAYDIEGKTIATIGAGRIGYRVLERLLPFNPKELLYYDYQALPKEAEEKVGARRVENIEELVAQADIVTVNAPLHAGTKGLINKELLSKFKKGAWLVNTARGAICVAEDVAAALESGQLRGYGGDVWFPQPAPKDHPWRDMRNKYGAGNAMTPHYSGTTLDAQTRYAEGTKNILESFFTGKFDYRPQDIILLNGEYVTKAYGKHDKK
|
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms. {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:9226256}.
|
O13516
|
RS9A_YEAST
|
Small ribosomal subunit protein uS4A (40S ribosomal protein S9-A) (RP21) (S13) (YP28) (YS11)
|
MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
|
O13527
|
YA11B_YEAST
|
Truncated transposon Ty1-A Gag-Pol polyprotein (TY1B) (Transposon Ty1 TYB polyprotein) [Cleaved into: Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
|
METFTGYLKSTCFHQISPYPPSIMSIQVKVHANILILSFIECLRMPMHRQIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKLRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
|
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).
|
O13535
|
YH11B_YEAST
|
Transposon Ty1-H Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
|
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENLHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQQSNDLNIESDHDFQSDIELHPEQLRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQSNTHESSHASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQLLMMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDPGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
|
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).
|
O13547
|
CCW14_YEAST
|
Covalently-linked cell wall protein 14 (Inner cell wall protein)
|
MRATTLLSSVVSLALLSKEVLATPPACLLACVAQVGKSSSTCDSLNQVTCYCEHENSAVKKCLDSICPNNDADAAYSAFKSSCSEQNASLGDSSSSASSSASSSSKASSSTKASSSSASSSTKASSSSASSSTKASSSSAAPSSSKASSTESSSSSSSSTKAPSSEESSSTYVSSSKQASSTSEAHSSSAASSTVSQETVSSALPTSTAVISTFSEGSGNVLEAGKSVFIAAVAAMLI
|
Component of the inner layer of the cell wall.
|
O13563
|
RPN13_YEAST
|
26S proteasome regulatory subunit RPN13 (Proteasome non-ATPase subunit 13)
|
MSMSSTVIKFRAGVCEYNEDSRLCTPIPVQGEIEIKPNEEEELGFWDFEWRPTEKPVGRELDPISLILIPGETMWVPIKSSKSGRIFALVFSSNERYFFWLQEKNSGNLPLNELSAKDKEIYNKMIGVLNNSSESDEEESNDEKQKAQDVDVSMQD
|
Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins.
|
O13601
|
RSP1_SCHPO
|
DnaJ-related protein rsp1
|
MARTAFHDEFVDYYTILGAESTSSYVEIRQQYLKLVLRYHPDRNPGREAEVLPQFQLIQKAHEVLKDPKLRELFDQRRLLEAGRPDGVLRFRPKKSGPKNDISTKVASKVSVTMATKFAEKKKKQDRENVDSKDNNITNFSLHRSFSASGKMEKNNSFKEVSTSKSYISSGYLHPKTSPIFKKNGYATENVVDPISSSPRFKGPNYNKFNAKLYLESLREKRRTYTPLSEISNGLNSNGVENSSITKSSPRSSSSSNNERFKDTSEESIIFTSPNTPEHPSVYQTDITPEIKLEHSDNNSPSKPEIPFRHPTSKPLPPKPLSRSKSSSLSRNQTRSQLNDLSAENDSTSNSTEYDDQLQSILRSLAIEGDDDEVAKVLPKPPSVPTIQAPIPPEAPRNLTNASVDSYLNSFEMYQRRWSSYSIIYTQYAFQWQIFKNKCFQLDLMNTPGQSRLIDNWKEGSQAIQLFYAYEQMHLRALEELQSLKESLFASFGI
|
Has a role in the proper organization of the interphase microtubule cytoskeleton. Required for equatorial microtubule organizing center (eMTOC) disassembly into satellites, contributing to the dynamic redistribution of MTOC components for organization of interphase microtubules.
|
O13648
|
ANM3_SCHPO
|
Ribosomal protein arginine N-methyltransferase rmt3 (EC 2.1.1.-)
|
MLVKPMACYFEIWTRKVTTIEDFSLAIANRFKQMGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPVGKVDIIISEWMGYALTFESMIDSVLVARDRFLAPSGIMAPSETRLVLTATTNTELLEEPIDFWSDVYGFKMNGMKDASYKGVSVQVVPQTYVNAKPVVFARFNMHTCKVQDVSFTSPFSLIIDNEGPLCAFTLWFDTYFTTKRTQPIPEAIDEACGFTTGPQGTPTHWKQCVLLLRNRPFLQKGTRVEGTISFSKNKKNNRDLDISVHWNVNGKADSQSYVLN
|
Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in ribosomal protein rps2.
|
O13666
|
ERG3B_SCHPO
|
Delta(7)-sterol 5(6)-desaturase erg32 (EC 1.14.19.20) (C-5 sterol desaturase erg32) (Ergosterol Delta(5,6) desaturase erg32) (Ergosterol biosynthetic protein 32) (Sterol-C5-desaturase erg32)
|
MDVVLQYADKYVFDTFYGKIAESFDSSSSFANTAVNSTTLGLAEKVNFAITSGLLDRNNVWRQFTSLFLITWIMGTLSYFLSASFAYYVYFDREEARRHPKFLKNQEHLELMVALKNLPGMAILTAPWFLAEIRGYGYVYDKLDEYGYFYLFFSIALFLLFSDFLIYWIHRALHHRWLYAPLHKLHHKWIVPTPYSSHAFHYLDGYSQSLPYHMFPFFFPLNKYVYLLLFGSVNYWTVLIHDGKYFSNNAVVNGAAHHAAHHMYFNYNYGQFFTLFDRLCSSYRQPDQELFDAELRNEKLQEQRIRFMETVQYTVEGKDDRTYASKKDN
|
C-5 sterol desaturase part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway. Erg31 and erg32 catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable).
|
O13684
|
PCS1_SCHPO
|
Monopolin complex subunit pcs1 (Chromosome segregation protein 1)
|
MRKNNMQTSKDSELKEQAKGKSSKLIHKLPKQRTRISQGQMHSTQDFVNNEDQDAYSVRENENELHINNSGMSELNKKLQLPNVELSTLSHTQEQEFNELNKLIRKINELQEFYLLEDLAKPVTNAGADADDTIVKDLKKELENEKKANHSLKNELLKTREQIKNYSKINILIKELFGLEVADCIEDEDGYRFNCKNTGRRGTLEYQLLLDDQNFTFTPRLNVQTDEELMKHLPDYLLEEIIFTKEQGKLFSARLMKALQD
|
The monopolin-like pcs1/mde4 complex is essential for accurate chromosome segregation during mitosis and meiosis II. May clamp together microtubule binding sites on the same kinetochore, preventing merotelic attachment of microtubules. In contrast to its S.cerevisiae ortholog CSM1, is not required ofr mono-orientation during meiosis I.
|
O13685
|
UBC13_SCHPO
|
Ubiquitin-conjugating enzyme E2 13 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 13) (Ubiquitin carrier protein 13) (Ubiquitin-protein ligase 13)
|
MALPKRIIKEIETLTRDPPPGIVAAPTEDNLRYFKITMEGPQQSAYEGGKFHLELFLPDEYPMMPPNVRFLTKIYHPNVDKLGRICLSTLKKDWSPALQIRTVLLSIQALMGAPNPDDPLDNDVAKIWKENEPQAIANAREWTKKYAV
|
Has a role in the DNA error-free postreplication repair (PRR) pathway. The ubc13/spm2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
|
O13688
|
NSE6_SCHPO
|
Non-structural maintenance of chromosome element 6 (Non-SMC element 6) (Core protein 1)
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MNASNNISKFPDLDNSSKLIDHILDSDDSEELDELPDISSLVPSARAQSRKQYLKNDSSNSSTYRWNIDLLSSTATIDDSVAKRRKLAVQNLLQYDSTQTFQTGDEIDELIGKSVGSNVLNVLRSNPIYDDDLRYEYCSNSKARVPDWNTLKAECLKDNDLEFNEGIIPTTFGDLLSAKLVPLDIALSICSLQFFRSLGDTTCSEWIANLEKIFYSYKSSSNNLNQIVRFIFETTADMIGIDLAKRQVPIQLERTSASENLKSNLKIKVINFLKCCGTLYRFSDDTVRFEMIQDACRILIDNQVGSFCKWQFSQFMELPISLNPDFLISNIHKVSESPRVWVTILSSLSRSCQKFRKKIAFTLFVGKQSKNDDSDFSSLCQRLDEISASCNNDYTTLLYQIRTFGYAVDEKHFKTNERLECLLEKLRKIDLTISGSTDHLLLSRCEVKDCIHRLFMVLYYLNTNSAPELERIIESDLPNNNKQKDRYFKDKTSNLSMKENKSFSAKKVKKGKKKNKRQAYKR
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Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. May prevent formation of excessive Holliday junctions or assist in their resolution.
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O13692
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GAS5_SCHPO
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1,3-beta-glucanosyltransferase gas5
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MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA
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Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
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O13710
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SMC5_SCHPO
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Structural maintenance of chromosomes protein 5 (DNA repair protein spr18) (SMC partner of rad18)
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MDGLRPSKRRKSNPLYSDYALGSIVRIKLVNFVTYDYCELFPGPYLNLIIGPNGTGKSTIVSAICIGLGWPPKLLGRAKEAREFIKYGKNTATIEIEMKYRDDETVTITRQISQDKSSSFSINREACATSSITSLMDTFNVQLNNLCHFLPQDRVAEFAQLDPYSRLMETERAIDHEGLLPAHEKLIDLRKREREILQNKNQGQSTLNSLKDRQQALEKEVNIFKEREKIKSYIEMLGLAKMLVIYREKTNVFNQLRADKKKLKKDLKDLVEEFQPILDKGEELRSDLKLKDDTFNDYSSASMELNTSNLRARASFSNFMENEKKLYEKVNTNRTLLRNANLTLNEAQQSVKSLTERQGPRPSDNGVQDLQEKMQEVNAEKLQHENEKLESSHELGSIRTLKAQKLIDLDNIKRELSYYNDATKRKLDFMSSAPGWEDAYQTYQLLKEYESAFEAPAYGPIYMNLKCKEKGFAALIEGFFRTDTFRTFIMSNYNDYLKLMDLITSKTKYTPTIREFSSERKKKIEDFEPPCSREKLQSFGFDGYVIDFLEGPEVVLVALCHMLKIHQIPIAKRELPPASVNALNNFRLANGDPVLKTYLAGSSIHLVFRSAYGDREITRRTDPLPSRSIYFSENVEMDLVKRKEEQLNAQLSQLENLQNEERKLQEKVNEHESLLSRTNDILSTLRKERDEKLIPIHEWQQLQERIEHQTLLLRQREKVPEQFAAEIEKNEDIRKENFEALMNSVLKVKENSIKATNNFEKMLGSRLNVIEAKYKLEKHEMDANQVNARLTEVQDRLKDITDKLASAREDAMSLYGSVVDSLQTQSSDRQTAITELNEEFATSSEVDNKISIEETKLKFMNVNSYVMEQYDARKKEIEELESKMSDFDQSVEELQDEMNSIKEDWVSKLEENVQCISDRFSKGMSGMGYAGEVRLGKSDDYDKWYIDILVQFREEEGLQKLTGQRQSGGERSVSTIMYLLSLQGLAIAPFRIVDEINQGMDPRNERVVHRHIVNSVCDNAVSQYFLVTPKLLPDLTYHRNLKVLCICNGAWLPATFRTSLSTYFEKLKKSALISSS
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Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
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O13712
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MUG61_SCHPO
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Meiotically up-regulated gene 61 protein
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MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGVTNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPFETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNTTSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLVGLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKFDSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWHQEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFGLKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVYLKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAAITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSIQLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL
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Required for correct meiotic chromosome segregation.
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O13716
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AGN1_SCHPO
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Glucan endo-1,3-alpha-glucosidase agn1 (EC 3.2.1.59) (Endo-1,3-alpha-glucanase agn1)
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MKLVLFLVLLFSALINLTNADKMVVAHFIVGNTYPYTVSNWEEDIQDAIAVGIDGFALNMGSDAWQVERIEDAYDAAASVSSDFKLFISFDMSIISADADFIEGVVRRFADKPNQLYYDGKVFVSTFAGETDTFGYSDVSTGWDSAVKEPLASAGYPIYFVPSWTSLGQGALEESVADGFLSWNAWPTTDADMNDNDDIGYQNLANSLGKLYVAPVSPWFYTHLSYKNWAYKSDWLIIDRWNEMLSVQPDMIEVLTWNDYGESHYIGNIQGALPAGSEGYVDGFDHTAWRYLMSPYISAYKLGLSEPYINFESLFYWYRPTPKSATATADSLSYPSGGDYMEDEIFVLVYLLQSAEVTVTCGSTTQTFSGVPGVNQFTIPMETNASPSFTVARQGGTLASGTGPEIVDSLSIYNFNAYTGVLYF
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Has a role in cell separation where it is required for the degradation of the cell wall material surrounding the septum (the septum edging) which must be hydrolyzed before full separation of the daughter cells can occur. Hydrolyzes 1,3-alpha-glucan predominantly into pentasaccharides.
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O13734
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SGO2_SCHPO
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Shugoshin-2
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MSKASLSPNVEDLKKKQIRQYKEIIRISKAQSIRIKELQLENERLLSENIDLRTTAINLEEQLETVQNENEENKTKLAALLNRFHEETDNFLSKLSLCQQEIQDTFKPVEANLAYDVDTDSEDLDEESVVKDTEEIIEQAQHDVSLRNLSGIEDENIIDDGETAINEQKKREANVFSDTQSAPQLKSGKALPADFENPYNLSNSKPVNNNNEDRVEAVTSENKSIDSAPQEKNHEYEIVSPKSLSNKINNQAAAQRRTEEDNANGVAQEENEGSQEAHFHSRIQSDTVIQSTPTKRKWDVDIQNKQINLASAATNVTGYVSETDSRPNRANSLDSAVLLVQSSNKSNRNGHHISDPNLNSSISLKFAPEDTAHNSLTSQENVGPQVTTTSLSNMTVAESPRTDTPREINGLVDSSVTNGNEKFSVEIMNDSNKIGLNPKSFTDEEREILTLFRNPPMRLSSEPPSSNGFSIAHPNNSPLRPPSLQGILNAEDRPYEIEPSRSSFATNDTGSYNNLELLSSVTNLKSPNENDRVTKTQSRRETKVKRRRKARIQETSEESTVVNEPNEKPDGRSRRERKKVNYALPGLRTKLRRNFDLPSDHVKAKKTRRAPKNSENDSATKTETANITSEAPTTSEVTLENSETLNL
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Involved in chromosome cohesion during mitosis and meiosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. Required for faithful mitotic chromosome segregation and proper kinetochore orientation during meiosis I. In contrast to sgo1, it is dispensable for centromeric protection of rec8 during meiosis I as well as protection of rad21 during mitosis. Required to sense the lack of tension at centromeres during mitosis.
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O13736
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SLA1_SCHPO
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Actin cytoskeleton-regulatory complex protein sla1
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MANLPIIGIYKVLYSYEPQEINPGEEIPENEREISIVEDEIVCLLEKGEDDWYLVKRNVNSNDDDEEIGIVPSNYITEAEPSTKMKALYDYTQQSVDEISFQADQTLDCYGDTDSDWILVGFNNNFGLAPRNYVEGMDASSAPASQEPSASGVNAPTVSAPNSMVSPPPSFQPPSAAAPATSLPSDYNPPPPPPPPPAVEDQAADANEPDDYYSSGRAVSPEIPPTYTPKQADPLPAPPPPPPPTLPPQSTNTSQLPMPSRNVNNLGSQVNIPPPPATPSQPPRPPTNASTRSTGTSSSMAHSYDSPPSPSSPSDAYGDPNQHLKLRTDSHDDSRAYDSSSSMGNPAYEKWEVREVVGKKKKRTGILAINNKSIVLTFTKTMDAAQVWPVTDLVNYSSERKHVFIEFNSDSGITSLHLHASSNTNADNIIRALGDVAGSARAAGLREIAAASGSPMPKLPSDSALHRLNAASDAAGVNGGRTGDYEMSTVYGDRSARAEDHKPKDSSAGQKMGTVLYDFIAEAADELTVKANMRVVIVNDTASSDWWKCSVDGKEGVVPSNFIKPDTEGDAKSPPSSSKSGQGSSLSRRASKHESKHKRDSKHEARPESKHESHRESKSAEKDKKDKKDKKEDSKRSRSHSVSKPDSSKLRTWTDRTGAFKVEAEFLGYSDDKIHLHKTNGVKISVPSAKMSYKDLDYVELMTGKKVYSRTERKKDTQKQSHDHGHSHSKSHDREKEKEKKKDREHRKHRETEEEDEGPPPQPARPESTRPALAPPSSSHSNDKYDVIQERPKISYDWFDFFLRCGVDFTVCNRYTHNFNNEHLDEACIPSLNPDTLRTLGLKEGDIIRVMNHVNELNGVSTKPASAITPETKSTVNQIMSGGEALAAPVAVPAPIPAPVAEPAPPAAPAKEVVEKAPSPPATRPKSTTPQKFDDDAWANKPVTEPPVRASSVTVEPARVTESMNKMNISEEAKKPEAPSRPRTAPIPEPEEQKKAPVEKKDAEKSVQAPIPAQPTGNITIQNAYFTAPQPMAADPFQSPLYVQPTGFQPPPSALPIQPTGYMQPIPVQATGYQPLMVQPTGLQPHMTGVMPQVTGVMPQMTGVVPQMTGVMPQMTGVQVQKTGAMPQQPVNYGYQVAGMQPQATGIISQPTGIRAQATGIMTQPTGLHTQATGMMQPTGMQPQATGIMPQATGMMQPTGMQPQVTGIMPQSMPMQPQMTGVQVQKTGMVAQPMLSQYTGYQQNYTPTAMPAADGYGMQPSMNDTQAYYNMNAQTPVNYGFAGGQDTSFGYEQQQMYSPMQQQQQQYYGTEMQPDMGYQQPMMSNYYDPMQMQQQTPYGYNQTGMEGYSEYGYAQPAGNMANPMSYDPVSNASLYMPSDYNQQTQPANYYDSSFGGAQGANEAGKKASIYQATPDNPFGF
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Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity).
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O13759
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CSX1_SCHPO
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RNA-binding post-transcriptional regulator csx1
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MSIDCLYRRSSLFDTSFVPLHSSIPATSKMSASNSDVNAPISPVVDEGKSELVSPTLERLVAPFNCSPSSTPLQDVAGVGSKMSDTLWMGDLEPWMDATFIQQLWASLNEPVNVKVMRSKASSSETLISYCFVQFSSSAAAERALMKYNNTMIPGAHCTFKLNWATGGGIQHNNFVSRDPEFSIFVGDLLPTTEDSDLFMTFRSIYPSCTSAKIIVDPVTGLSRKYGFVRFSSEKEQQHALMHMQGYLCQGRPLRISVASPKSRASIAADSALGIVPTSTSNRQPNQDLCSMDPLNTTVFVGGLASNLSEKDLQVCFQPFGRILNIKIPFGKGCGFVQYSEKSAAEKAINTMQGALVGTSHIRLAWGHNTLPVSALSQSQSQVSDEGFDRTLSANQIFGMNQSVIGANSGSSNSSGSSLKSAPVSPRTAAAQSLLPNSVVSSINGMNSVNFSTISPPPLSRSASISPTLSGSGSGLTPLSSHFPSAATGLVGGQVYPQSSVLQSSKINGSAKVQPSVKLPEWLQPFSGNNHNSFATQDLLTRVSSLKLVDDEQPASLNGSAFQARASRPWNLGRERQSSLIDLRHELEQNENGLEKSGFGLNLRGRLPPRSYSTFNCTGQYLQPSLRLSRDS
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Regulates global gene expression after oxidative stress. Interacts and stabilizes atf1 and pcr1 mRNAs after oxidative stress, thus controlling their turnover.
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O13766
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MDE10_SCHPO
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Zinc metalloprotease mde10 (EC 3.4.24.-) (Meiotically up-regulated gene 139 protein) (Sporulation protein mde10)
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MRLVLLFSCVLAVSSYAEIILAHSDENLLSRTKNNLSKWNENRLYDYGSKSTMSLPVSSLFPALQTLWIGVVADCSYVTHFTSRMEAKKHIFQEFEGVSTLYEDSFNINVQIHSLILPSAHDCSANVVDRPEISMSPRISIEEKLEIFSKWKYESPGNNVFEAISPHERESFPSEPQVSVLFTSSVKRSPHGVSWFATICSETHIENEWHVGPLSVVSAYPNDRLVVAHEIGHILGLIHDCNKKSCGDHSEACCPLSSSLCDAQELYIMNPSNSYTYANLRFSDCSILQLHSLVEKKYVSLSCLSKPSEKSVLRLGTCGNGIVEDGEECDCGEDCENNPCCDGKTCKLTKGSLCDDQQDACCYQCHFKNAGTLCRQSTNPCDKPEFCTGISSKCPVDENWDDGRICQDSLGMGSCASGVCTSASRQCKKLTNFSSLSCHSDSCKVSCQNEDGTCFISAKDYIDGTRCRGGLCYNGVCVPIEGSSASWSKQPSLFCASGTMLISLAVIAWFFW
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Has a role in the development of the spore envelope.
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O13768
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ERCC3_SCHPO
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General transcription and DNA repair factor IIH helicase subunit XPB (TFIIH subunit XPB) (EC 3.6.4.12) (DNA repair helicase ptr8) (Poly(A)+ RNA transport protein 8) (RNA polymerase II transcription factor B subunit ercc3) (TFB subunit ercc3)
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MSLKRKNNAREGTPDEDLEEYSDYSDVDNYGEEDDDSYKPAPRIRINNNKTKAQTTTNSNEARQSGISAMFGQNDFSNLLGLKLDHTARPLWINPIDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDNVEDKKDITNDSSKETAEKSSSDELFSAVVGLQEEEDDEDAVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRNDNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSANKQLKKDSKEHHALFRKHLYTKRR
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ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ptr8, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ptr8 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription (By similarity). Plays a role in mRNA export.
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O13788
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SSR1_SCHPO
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SWI/SNF and RSC complexes subunit ssr1
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MSNVTENKHDLHENGVPDSAQPMELDVSKKEDTEPEVRDEAKEFLLSQLPQVEVPEWAQWFDFSKVHEIEKKQNPEFFDGKNTSKTPEVYKEYRDFMISTFRLNSKVYLTFTACRRNLAGDVCAVLRVHRFLEQWGLINYNVNPDTRPSKIGPPSTSHFQILADTPRGLVPLLPPPSSSIPRSKAVTIEDPSIVRTNIYDPSLDDVLKGKGSTPNQKPSLSNLHENNIDQSDSPQHCYCCGNKFNESYYQSQTAQKYNVCISCYQQNRFPSPTTIADYKEVAIQNKIEDDDTWTAQELVLLSEGVEMYSDDWAKVASHVNTKSVEECILKFLNLPSSDKALFKMDKVHTNPVVDSLQGKNPILSVVSFLAKMVPPSSFTQKSSAKEEESDKVKGESVYPKPESESYDVEMNGKSLEDSDSLSELYLTNEEKKMASIIKDSVNVQIKLIESKLSHFDYLDQHIRLKSQELDAFAQATYREKLYMKRECQNARKKIEQQLQSKDTAANGLPVQSSAETSVIPASSMSPS
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Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
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O13790
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CUL1_SCHPO
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Cullin-1 (Cul-1) (Cell division control 53 homolog)
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MTTLNTNDKDLPIVKKYDSLNGTWDFLKTGVSQIFERLDEGMTITKYMELYTAIHNYCADASKTITVDNFNDQTANVLGEALYNNLVLYLEEYLARLRKECISQTNHEEQLAAYAKYWTRFTTSARFINHLFGYLNRYWVKLKNRFTETLVYDIYTLCLVSWHHHVFSHIRDSLLQNLLYMFTKKRLYEPTDMKYVEVCVDSITSLSFDKTDMTKPNLSSYKTFFETNFIENTKNFYAKESSEYLASHSITDYLKKAEIRLAEEEELVRLYLHESTLKPLLEATEDVLIAQHEEVLHNDFARMLDQNCSEDIIRMYRLMSRTPNGLQPLRQTFEEFVKRSGFAAVAKIVPQVGGEADVDPKEYMEMLLSTYKASKELVNTAFHGDTDFTKSLDTAFRELVNRNVVCQRSSSRSPELLAKYADSILRKSNKNVDIDDVEDCLSSIIIIFRYVEDKDVFQNFYTKLLAKRLVNGTSNSQDAESSMLSKLKEVCGFEYTSKLQRMFQDISLSQEITEAFWQLPQSRAGNIDFSALVLGTSFWPLSPNNVNFHLPEELVPLYEGFQNYYYSCHNGRKLSWLFHLSKGEIKARINPQTNVTYVFQVSTYQMGVLLLYNHRDSYTYEELAKITGLSTDFLTGILNIFLKAKVLLLGDNDKLGDPNSTYKINENFRMKKIRVQLNLPIRSEQKQESLETHKTIEEDRKLLLQSAIVRIMKARRTLKHVVLVKETIDQIKSRFTPKVSDIKQCIDMLIEKEYLERQGRDEYIYLA
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Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(pop1-pop2) is required for the maintenance of ploidy and directs ubiquitination of cig2.
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O13795
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POF8_SCHPO
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La-related protein 7 homolog
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MFVPRQLNVRKIKAFTGKENNSIADGNNNKLKDEHYKHNEASKEPSHSISGGLMLNQQDRQLIEPLNPDFLSAVDSILEIYFHRERQKEKVHLAFLIQQDDFWKGIRPNPTQNNLKYALSYVTNALFHFDNSSHMVIRNENIVLPLDIPLYDRIIYVEPVPATLSNKSLLLAGKLRKYLKEFLPYVDAIGTPEGYAFVILYKKVDQSALSKLPVPPGWVLLTRKEWTNREEKYFENQLHLVKASSSDVSNSSNSFPENRYPKLTKVEKQMTKSVSKTSQTDKDEDNLDFTKNLLTRIKNLHPLTNKSTIHSLLSYVFSRQTQNIACEPMYIDYRKDETEAIIRWKTPLHAETCINAFRTQERKQNSHDDIRAHRKKGSSRPFLIAELITGEEEKNYWRMLKK
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RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex. Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1. Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division.
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O13801
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DRI1_SCHPO
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RNA-binding protein involved in heterochromatin assembly dri1 (Dpb4-interacting, RRM, and IDR-containing factor)
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MSKLPSPTMPLPESVGDLVVLHFETNLDDHGISIGRAPCEIHEICWVILDGKTLEKQHCESCSIREDSSRHGICGSASSLTEAIFTLDNSIQERLNFQGKPFTFVVMNGRELRVLLPKEARDQGITLPSYMRHPRLFDLSSEYAKWQIRMGAVPPYTITLSHIFGKLDVDSLPPITESKAIELSPSDAPYITKGLTQCWRLANATTLLLRKAEKDSRGHSLPSVLTQPINCQADARSFYAERSKIVHVAGLTNDVTQLELESWFTNHGVHPVALWTLKTPEPYKSTGTGFVLFASHEDAADALAFNGYCLGDRMLEIIPSSTKVLDKASDILIPFPSSKNRPRPGDWNCPMCGFSNFQRRTSCFRCSFPGPTHVSAATGSNTFSPDFPYGNSYGNGSSHFIANYGGSVHHSNENTMQSDLQHQNGNNAVNHHHSSRSFGGNVPFRAGDWKCGSEGCGYHNFAKNVCCLRCGASRATAAVVADHASGPVNGSYSHNSYSHIPPVMSTSPPNHSVYPYSQLSINSVTANHGQNFGGQNGGNVSRFDDHGRFKEVSRPSVTTDQGDWLCECGFTNFRRRSNCLRCNAPHYSNMQIPASLPSDFNAYV
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Mediates heterochromatin assembly by promoting RNAi-mediated heterochromatin silencing and histone deacetylation. Binds pericetromeric transcripts and recruits the RNA-induced transcriptional silencing (RITS) complex to heterochromatin. Recruits sir2 to chromatin to promote deacetylation of 'Lys-9' of histone H3.
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O13807
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DDB1_SCHPO
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DNA damage-binding protein 1 (Damage-specific DNA-binding protein 1)
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MTYVTYLHKPSSIRNAVFCKFVNASSWNVIVAKVNCLEVYSYENNRLCLITSANIFAKIVNVKAFKPVSSPTDHIIVATDSFRYFTLFWDANDNTVSNGIKIQDCSERSLRESQSGPLLLVDPFQRVICLHVYQGLLTIIPIFKSKKRFMTSHNNPSLHDNFSVRIQELNVVDIAMLYNSSRPSLAVLYKDSKSIVHLSTYKINVREQEIDEDDVVCHDIEEGKLIPSENGGVFVFGEMYVYYISKDIQVSKLLLTYPITAFSPSISNDPETGLDSSIYIVADESGMLYKFKALFTDETVSMELEKLGESSIASCLIALPDNHLFVGSHFNNSVLLQLPSITKNNHKLEILQNFVNIAPISDFIIDDDQTGSSIITCSGAYKDGTLRIIRNSINIENVALIEMEGIKDFFSVSFRANYDNYIFLSLICETRAIIVSPEGVFSANHDLSCEESTIFVSTIYGNSQILQITTKEIRLFDGKKLHSWISPMSITCGSSFADNVCVAVAGGLILFFEGITEVGRYQCDTEVSSLCFTEENVVYVGLWSADIIMLTYCQDGISLTHSLKLTDIPRSIVYSQKYGDDGGTLYVSTNNGYVLMFNFQNGQVIEHSLRRNQLGVAPIILKHFDSKEKNAIFALGEKPQLMYYESDKLVITPLSCTEMLNISSYVNPSLGVNMLYCTNSYISLAKMSEIRSLNVQTVSVKGFPRRICSNSLFYFVLCMQLEESIGTQEQRLLSFLRVYEKNTLSEIAHHKFNEYEMVESIILMNDDKRVVVGTGFNFPDQDAPDSGRLMVFEMTSDNNIEMQAEHKVQGSVNTLVLYKHLIVAGINASVCIFEYEHGTMHVRNSIRTPTYTIDISVNQDEIIAADLMKSITVLQFIDDQLIEVARDYHPLWATSVEILSERKYFVTEADGNAVILLRDNVSPQLSDRKKLRWYKKFYLGELINKTRHCTFIEPQDKSLVTPQLLCATVDGSLMIVGDAGMSNTPLLLQLQDNIRKVIPSFGGLSHKEWKEYRGENETSPSDLIDGSLIESILGLREPILNEIVNGGHEGTKLDISVQDLKSIIENLEKLHP
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Component of an E3 ubiquitin-protein ligase that includes cul4 (By similarity). Required for ubiquitination and the subsequent degradation of the DNA replication licensing factor cdt1 and of the ribonucleotide reductase inhibitor spd1. Also required for transcription-coupled nucleotide excision repair. {ECO:0000250, ECO:0000269|PubMed:12857752, ECO:0000269|PubMed:14701809, ECO:0000269|PubMed:15805471, ECO:0000269|PubMed:16252005, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:17039252, ECO:0000269|PubMed:18794354}.
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O13816
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SCC3_SCHPO
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Cohesin subunit psc3 (SCC3 homolog)
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MSESVTTGSDDDGGDRESSPVMLSQSFDPMSSSSNSSSEENSDDDYEKTISSKKRHPRPNSKGVNVKRSRRNAIVEEDPQEEIFNNLFAFLLDQKVDTMDIAVSWFADYAKDNQSALANLINFILKCCGCNRAINVFDVQDQDSASATLSQIQLSVERTSTRDYPLNSKNLKFRNFRKRLTGLLSNFVSQLSIRNYLYNSTVFEDIMSWVVAMSSSTMRPIRHTATVFCLNIMTFLCEKSKELLNEHAIATKQLEKEEKRSRVNRNRINELNNSLGEIVKQQDTLTTYLNDYFDSVFVHRYRDVEPKIRVDCLQELGVWINTVPSIFFSGSYLRYLGWMLSDINTTVRLTVVKVLRKFFETDSFIGGLRHFSSRFKERILEMSCVDADIGVRVASIRLCNAMRTCGFLENSEILKVLKLILDINPRVQREAVLFLCKVVDESVNEKIDLWGEEDYILKAFSQTSLTTFSVHWIKFSQMCKLLEEVRLSYQSSFDYDTLLRIFQKNGNFITPITQALLNACEIDSIYQSWEDISNFVLFDNYTSTLKDPIDSILSFCKLNDFQESILLQLLSASIQTVCNNNFITPKTVHNKQAAETTNDQNKDKDLLYLNLLPYINSITERNSASPTLLHDSLRLLFSMDLTEMTDPQLSRHFELLINNLKKFFLTNNDLQIIQGCTILFLRLDSIPALKEDLKLLVTDICDQTVTEFLKNFGSFNIQDAVITKDEFVIFEACLTRIEGCTSLKDFSDYPEFDIIYERLVSLLSRVPNSYEDTLKFSAINTLQSLLFWFFLRKDNPADEEKKKDDETKVFNCLINIMNNDSSKILQLQAARTFLETVIMKEGVKASHYNDDNRVSEEHNFLKPQFLDALLKILEGWLYTYAKVGQFPFKRLTQASSPHTQISLDKNPLNRRLLEHVCCDLTSKLLIVVSLSNTITPEFSQQFCELRGHYGPKLSAIVDEFLN
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Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the rad21 subunit of the cohesin complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
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O13820
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ERG5_SCHPO
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C-22 sterol desaturase ERG5 (EC 1.14.19.41) (Cytochrome P450 61) (Ergosterol biosynthetic protein 5)
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MEMNQTETLIPAARNVIRVLGYEIEYSKWTICFALLAVCIAYDQISYQMQKGHIPGPRFKIPFMGSFLDSMKPTFEKYNAKWQTGPLSCVSVFHKFVVIASERDLARKILNSPSYVQPCVVDAGKKILKHTNWVFLDGRDHIEYRKGLNGLFTTRALASYLPAQEAVYNKYFKEFLAHSKDDYAQYMIPFRDINVATSCRTFCGYYISDDAIKHIADEYWKITAAMELVNFPIVLPFTKVWYGIQSRKVVMRYFMKAAAESRKNMEAGNAPACMMEEWIHEMIETRKYKSENKEGAEKPSVLIREFSDEEISLTFLSFLFASQDATSSAMTWLFQLLADHPDVLQKVREEQLRIRKGDIDVPLSLDLMEKMTYTRAVVKECLRLRPPVLMVPYRVKKAFPITPDYTVPKDAMVIPTLYGALHDSKVYPEPETFNPDRWAPNGLAEQSPKNWMVFGNGPHVCLGQRYAVNHLIACIGKASIMLDWKHKRTPDSDTQMIFATTFPQDMCYLKFSPFDASTVDWKNSKEAFSNEAVSAATVETESA
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C-22 sterol desaturase part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway. Erg5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable).
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O13821
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VPS27_SCHPO
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Vacuolar protein sorting-associated protein 27 (Suppressor of ste12 deletion protein 4)
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MSRWWNSNSQFASDIEKATSETLPAGSEEISLYLEISDQIRSKSVDPKFAMRILKSRIDHSNPNVQIMALKLTDTCVKNGGSGFLLEIASREFMDNLVSILRSPAGIDEDVKMVILRYIQSWALAVPDTNSPLSYIIHVYQNLKDGDYEFPEPSQNITSKFLDTETPPDWTDSEVCLRCRTPFTFTNRKHHCRNCGGVFCNQCSSKTLSLPHLGINQPVRVCDSCYSLRTKPKGSKSRARNERKFHAKTRKTPSKPVTNNEDEDIKRAIELSLKEMPQSREPPSYERPSEANVVISQDQHLTEDEDEELKRAIAISLEEAQKSSQKDDNVTAPNNMNISYPSVPAHTVSTDIRSSPFSGRPSDNPSTLISTADADNITLYATLVQKLKKLPPGSIFTEYQLQELHENMGVMRTRMMRSLGETMSKYNGLIQALQKLQTCMRLNDALIEQRLSSTYAHHYIDSSMDSNRSIEPEPDVISTVRNSSTIPQASSSSVPKIVVDSSPVTENPPSHSDVMGQKDTISSYYSTDTDVSANVMGNRHDEVVFSDTASGEKNTKLNIDESTNYYNTDSIDKVGEPFDEISSGYDDLMNGNDKQGNDIPEVQEASLIEL
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Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
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O13826
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RFP1_SCHPO
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E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1 (EC 2.3.2.27) (Meiotically up-regulated gene 140 protein) (RING finger protein 1) (RING-type E3 ubiquitin transferase rfp1)
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MQFNGSNGIDESSVIDLTRSPSPPVETSISSTNIIDLDAIPDDSFPSSPVLSPRRRRMNRRRNERSRNFPSNHLSYLEDMIYLGPQVSTRRSSSRRDLMGMIARTFPEFSSVNSLSPSLFQLIVNRMRFDAIHPEWTNGSDDEYFSNHFEESYDDFTSSLENIKQSYKPPGPPKSGFTRSFNNDTLMVCPRCQEPLGTSKSKEKSALWATKCGHVYCGSCAKVLKTSKRSQSKCLVNDCGRYLNTKNAMWELFY
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Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Involved in maintaining genome stability where it acts in the cellular response to DNA damage. Has a role in meiosis.
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O13828
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DCP2_SCHPO
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mRNA decapping complex subunit 2 (EC 3.-.-.-)
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MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNLPLNPPIQSSNSRLSHDNNSFDPFAYLGLDPKNPSASFPRVVSQNNMLTNKPVLNNHFQQSMYSNLLKDQNSVQHLFAASDMPSPMELPSPSTVYHQVFYPPTSTSVSSYGLGKTPQPAYGSSSPYVNGHQTQQISSLPPFQSQTQFLARNSDNSGQSYNSEGDSNSKRLLSMLSQQDTTPSSSTLSKEANVQLANLFLTPNSLETKKFSDNSQGEEISDNLHGESCNNPNANSVHSAQLLQALLHPSATETKEETPKKTSDSLSLLTLLKSGLPTPANDLQNKSQNNERKASSQVKELEVKNYSKSTDLLKKTLRIPRNDEPLEAANQFDLLKVSPQQKSEVPPKRNELSQSKLKNRKKKENSETNKNHVDMSPGFVKILKRSPLADQKKEDTQESDFKGSDDHFLSYLQSVVSSNSNGLH
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Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.
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O13833
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CID1_SCHPO
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Terminal uridylyltransferase cid1 (TUTase cid1) (EC 2.7.7.19) (EC 2.7.7.52) (Caffeine-induced death protein 1) (Poly(A) polymerase cid1) (PAP) (Poly(U) polymerase cid1) (PUP)
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MNISSAQFIPGVHTVEEIEAEIHKNLHISKSCSYQKVPNSHKEFTKFCYEVYNEIKISDKEFKEKRAALDTLRLCLKRISPDAELVAFGSLESGLALKNSDMDLCVLMDSRVQSDTIALQFYEELIAEGFEGKFLQRARIPIIKLTSDTKNGFGASFQCDIGFNNRLAIHNTLLLSSYTKLDARLKPMVLLVKHWAKRKQINSPYFGTLSSYGYVLMVLYYLIHVIKPPVFPNLLLSPLKQEKIVDGFDVGFDDKLEDIPPSQNYSSLGSLLHGFFRFYAYKFEPREKVVTFRRPDGYLTKQEKGWTSATEHTGSADQIIKDRYILAIEDPFEISHNVGRTVSSSGLYRIRGEFMAASRLLNSRSYPIPYDSLFEEAPIPPRRQKKTDEQSNKKLLNETDGDNSE
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Cytoplasmic uridylyltransferase that mediates the terminal uridylation of mRNAs with short poly(A) tails such as such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA decay. Uridylates the 3' ends of actin mRNAs upon S-phase arrest. Has also a weak poly(A) polymerase (PAP) activity. Residue His-336 is responsible for the specificity for UTP. Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis.
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O13836
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DXO_SCHPO
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Decapping nuclease din1 (EC 3.6.1.-) (Dhp1-interacting protein 1) (NAD-capped RNA hydrolase Rai1) (DeNADding enzyme Rai1) (spRai1) (EC 3.6.1.-)
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MLREFSFYDVPPAHVPPVSEPLEIACYSLSRDRELLLDDSKLSYYYPPPLFSDLNTGFPNRFHPPKSDPDPISIVKDVLMTKGIQMNSSFLTWRGLITKIMCAPLDPRNHWETYLVMDPTSGIIMMEERTRSETSYANQDRMCYWGYKFEAISTLPEIWDACSRDQIEQRDNQDVVPDEQYCSIVKINIGKSKLILAGEVDCIWDKKPCSAKESDVHSDDGTIEEDASNAENPNLHYVELKTSKKYPLENYGMRKKLLKYWAQSFLLGIGRIIIGFRDDNGILIEMKELFTHQIPKMLRPYFKPNDWTPNRLLVVLEHALEWIKQTVKQHPPSTEFTLSYTGGSKLVLRQII
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Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective m7G cap and is part of a pre-mRNA capping quality control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
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O13837
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GABAT_SCHPO
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4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase)
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MSSTATVTESTHFFPNEPQGPSIKTETIPGPKGKAAAEEMSKYHDISAVKFPVDYEKSIGNYLVDLDGNVLLDVYSQIATIPIGYNNPTLLKAAKSDEVATILMNRPALGNYPPKEWARVAYEGAIKYAPKGQKYVYFQMSGSDANEIAYKLAMLHHFNNKPRPTGDYTAEENESCLNNAAPGSPEVAVLSFRHSFHGRLFGSLSTTRSKPVHKLGMPAFPWPQADFPALKYPLEEHVEENAKEEQRCIDQVEQILTNHHCPVVACIIEPIQSEGGDNHASPDFFHKLQATLKKHDVKFIVDEVQTGVGSTGTLWAHEQWNLPYPPDMVTFSKKFQAAGIFYHDLALRPHAYQHFNTWMGDPFRAVQSRYILQEIQDKDLLNNVKSVGDFLYAGLEELARKHPGKINNLRGKGKGTFIAWDCESPAARDKFCADMRINGVNIGGCGVAAIRLRPMLVFQKHHAQILLKKIDELI
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Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source. Deaminates GABA to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase. Cannot transaminate beta-alanine (BAL).
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O13838
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NUP40_SCHPO
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Nucleoporin nup40 (Nuclear pore protein nup40)
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MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQPRNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF
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Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm).
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O13839
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FIN1_SCHPO
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G2-specific protein kinase fin1 (EC 2.7.11.1)
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MEKYKILECIGHGSFGRIYKVQRLKDGALLAQKEIHFGNITRQEKQYIADEVNILRNLKHPNIVQYCGEELNRSAQVINLYMEYCGHGDLANLIQRYKEEKKRFTEQEVLKFFTQLLLALYRCHYGENAPACDSQWPREIFHPKQSVLHRDIKPANIFLDENNSVKLGDFGLSKLLDNTRVFTQSYVGTPYYMSPEIIRSSPYSAKSDVWALGCVIFEICMLTHPFEGRSYLELQRNICQGNLSCWDHHYSDDVFLLIRHCLEVNSDLRPTTYQLLRSPILSDIRSKLESERVVLEQSDLLHKKHQMLIQLENDLQFREQRLSARESELENVIASRLAQREEILRRELEKQLRDMDARYQRHMQTVVNSMQKMRVTSPVDHNEQPESSTAEMFVDCTIEASQSPLLHIPKLGISKPLQTLSCPGFTLTTQQPILKRPTLRKELSSRALHTTATLMKYRANASSLRTTPIDKDGQITSLQQKNGTSNQVADCMNKLLHTSLDGKKLSPSELCNKFSDGEGLPNRKVSKLSVESDETAVSASSGESVPTDSTLTDTKSKSVFVHPPSPQSLYVEKLEKLNIRSDEVSKPSKASKTLHGYALPSLASPYDVHAEEKIARENEMDGNFKTMKINQHPDEYVLRTPKKIQLLEGQKRSPVKQLGRLGYNKLRRSAMDNAGLELRKAASTSNYTSLQSRTLPGSWRDDEEEIPRPFLRKMLDARMMRA
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Promotes chromosome condensation and nuclear envelope dynamics during mitosis. Activity appears at metaphase-anaphase transition.
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O13842
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CDA1_SCHPO
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Putative polysaccharide deacetylase (EC 3.-.-.-) (Chitin deacetylase 1)
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MYETRDLTGNAGKPVDTNPWPNNSKIAVSFVVNYEEGGERSLLYEDEGFETFLTEAGLMPFPNRPVRERSIESCFEYGSRCGFWRILNLFKKHKVPFTCWAIGQAVEKNPVVVGAMEEAGCEVGSHSHRWINYEGVPPETEYEHIKKSVQAIQKASPSNSAPRSWYTGRASLNTRKLVCQVYKDLGLPQPFDSDEYNDDYPYWVADPLASKPGAEDDKGLLIVPYTLEVNDMKYAVAPGFCNSDDFYTYARDAFDVLYEEGLEGAPKMMTIGLHCRLTGRPGRFRGLQKLMEHITSKEGVWVATREQIAQAWSAKHPYKA
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May deacetylate chitin (Probable). Required for spore formation.
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O13849
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CBPY_SCHPO
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Carboxypeptidase Y (CPY) (EC 3.4.16.5)
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MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA
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Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
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O13853
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ITS3_SCHPO
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Phosphatidylinositol 4-phosphate 5-kinase its3 (EC 2.7.1.68) (1-phosphatidylinositol 4-phosphate kinase) (Diphosphoinositide kinase) (PIP5K) (PtdIns(4)P-5-kinase)
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MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS
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Involved, together with the calcineurin ppb1, in cytokinesis.
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O13877
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RPAB5_SCHPO
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DNA-directed RNA polymerases I, II, and III subunit RPABC5 (RNA polymerases I, II, and III subunit ABC5) (ABC10-beta) (DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide) (RPC8)
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MIIPIRCFSCGKVIGDKWDTYLTLLQEDNTEGEALDKLGLQRYCCRRMILTHVDLIEKLLCYNPLSKQKNL
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DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft (By similarity).
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O13881
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CLR2_SCHPO
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Cryptic loci regulator 2
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MPAITCVWSDGRSDTWPNVNGHSRTRSVPSLKPLPHQDSKNLLYRQICGRLLAQHVFGGAGSTQPILNQLCKRLSTGNPNNTNASTVVTAPEKNVVSARHVRPNPKSSKDTLEKQPKYSSQIYLTDSFENYYLASLPTNYQLYQRDSNRENGNGKREFWLYGHPSGRPFRSVNDFLHHLYWLISDLTRNESTCCCVLCSGNMTRVRKNLQKENERMFHECKDDTYTWPSSYRLGEVVWIDINNELIPAIIVARNLINYESNQMDAVKLISDTFVEPYQYHCKQLGNSRYYFDMAAADIEPWSRHPLDLQKQEHLVAHSICQTWNLFGIFQPLEGIDMEEPKFHDENYSIPLTVLPTFGGESNSLDDHFYGIFRGAEKLWINDLCVISTSSLPSVLQKTSFMYISDIYVNEDDIVCFQGSLWTQIDKNALDYNDSADNIDEHKDDLKELPRRLQMVSKLSNTYFRCLHDKSVEYVCPFADVLGRWYEPWFVKGDLNYTSEVKERTSSRLSAVGSENWVDDDFYEYLLSEIDMVSAVVM
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Required for deacetylation in the mating-type region and the centromere. Acts upstream of the histone deacetylases to promote transcriptional silencing. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).
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O13889
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E2AK1_SCHPO
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Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor 1)
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MLGTSTKCSKRDCNYAKENISRIMPTIGLGYKQNFEKKTADTQSSCKLLLVALLESFCKHSDQTPEQSKQMFLYVAHSLQNSGIIDFEFSEELEPIRNAYADSLHNLLSKAFRSTLPMSSTKDSKKSRYSSPDGVLAKTASFLSVLSDGGYEDDVMNVKPSVNVLSNRLNHLPVEALESCFPQTTLESSTFADFCEHKDGTGNLSFSNFDSFPTVQRSRYASDFEELELLGKGGYGSVYKARNKFDGVEYALKKIPLRLRSFSTSSNIFRESRTLARLNHPNVIRFFSSWVELLPSSEKQIEEEPLASADETLSQSADIDNFMFDMDTGLLQHTYPSSVQILFQEDSVADDLTPCYSTKNSTCNLTDLFKKEADQDYAESHDCSSTTSQVDTLGKLAPTKSASEMLLMDSFLSEREEDECSNIPSFDQQPLCLYIQMALCEETLEKHINRRNKHIHGVMSKGLRNCYILLFARILEGVLYLHDAMHLVHRDLKPRNIFLSSGVHSEPCSVCLPNFSDEDNVEVSNAYEPVNQRTLCVVPKIGDFGLVLSQSDNLEEGTNSSAESSFVGTSTYAAPELFSKHMRSVMNNNSSTDIYALGILFFELLYPFNTRMERASAIANLKKGIFPHDFLDSMPEEASLIRSMLSSSNKRPTAAQLLTSNLFHDLVVNELHVYQALLEDAEKRNNNLKAELNILRVLNPNYDC
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Mediates down-regulation of protein synthesis in response to stress conditions by the phosphorylation of the alpha subunit of eIF-2 (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of initiation. Activity is inhibited in the presence of heme.
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O13898
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PMT1_SCHPO
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Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC 2.4.1.109)
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MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMDVYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIFDNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLWNLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVTIRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHKPIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQREVTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFYEQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHYLPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDNLSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASEAAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQEENVAESAQARVE
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Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1.
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O13899
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CRLS1_SCHPO
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Cardiolipin synthase (CMP-forming) / mitochondrial hydrolase fusion protein [Cleaved into: Mitochondrial hydrolase (EC 3.-.-.-); Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41)]
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MLHTINYRSWHLAARQLGRSTFRKFTTESSTKSPIADVCFAFDSIDGVLIRGGRGLKEGTKTLKFLQKNNIPFILLTNGGGMHESVRAQRLSKTLSVSLTEDDFCQSHTPFRALADKYKHVLVLGGKDNSVRETAEKYGFKSVINELDVIAKLGTPFWPFTSFNEEDIKDAKDFDVTRPIEAVFTYVDPVRLGLDLQLVMELGQSKNGVLGTVSKTANEGPDIYFSNADLIWPNEYPLPRLGQGAFAICCESVFKELTGKDLRNTKYGKPHKLTYDYAKNILMKKHKTLGITNPPKEIFMVGDNPESDIRGANNYGWTSILVRTGIFQGDNSPKYSAKHVSDNVWEGVRWALSKHVPAAKLNKSMGEVRGFHTSSRVLNTVTKSNNSKPIQRPLRENIFTLPNLLTFSRLLSAPLIAYLYIYDYTKAAACFFLYAGFTDLVDGYIARKFDLGSIAGTVLDPLADKTLMTCLTICLAVRETMPLTLASLIIGRDVLLVSAVSYLRYKSLPAPKTFRRFFDFAIPTTELKPTRISKWNTALQLLLLGLLITEPILPFDASFAKSPLFYIVGCTTIASGASYCISRNTFRNIGKSKLQ
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[Cardiolipin synthase (CMP-forming)]: 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.
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O13902
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DAK1_SCHPO
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Dihydroxyacetone kinase 1 (DHA kinase 1) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase 1) (Triokinase 1) (Triose kinase 1)
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MDKHFINDPEVLVLDGLKSLADMNKTLTVHEEGKFIYFHDYNKKNVSVISGGGAGHEPTHSSFVGKGMLTAAVSGSIFASPSSKQIYTGIKQVESEAGTLVICKNYTGDILHFGMALEKQRTAGKKAELIAVADDVSVGRKKSGKVGRRGLSGTVLVHKIAGAAAARGLPLEAVTTIAKAAIDNLVSIGASLAHVHVPGHEPIAKEDEMKHDEMELGMGIHNEPGCKRISPIPSIDDLIAQMLKQMLDQSDKDRAYVKIEGDDEVVLLMNNLGGLSMLEFSAISHKVKEALAKEYKINPVRIFAGPFTTSLNGLGFGITLLRTTDRVKVEGEEYSLVDLIDQPVEAIGWPLCQPSDLKSKNKIGNVSIEEGQKDVKSPVTVDKEKVRQAIVNSMENLIKAEPKITKFDTMAGDGDCGTTLKRGAEGVLKFVKSDKFSDDPIRIVRDIADVIEDNMDGTSGALYAIFFHGFAKGMKDTLEKSKDISSKTWAAGLKVALDTLFKYTPARPGDSTMCDALVPFVETFVKTNDLNAAVEEARKGADATADMQAKLGRAVYVGDDVKVPDAGALGVVAIVEGFTK
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Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde. {ECO:0000250, ECO:0000269|PubMed:10091325}.
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O13911
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PNK1_SCHPO
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Bifunctional polynucleotide phosphatase/kinase (DNA 5'-kinase/3'-phosphatase) (Polynucleotide kinase-3'-phosphatase) [Includes: Polynucleotide 3'-phosphatase (EC 3.1.3.32) (2'(3')-polynucleotidase); Polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78)]
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MSSKKRKSPPQESLTSYFEKSSKSSKKYGSQNKDSDSSSTCLQQKIEIQWSITDSLYIAKYGKLKKTKKFIAFDLDGTLIKTKSGRVFSKDAADWTWWHPSVVPKLKALYQDNYSLVIFSNQNGIPRKPSAGHTFQMKIRAIFESLDLPIVLYAAILKDKFRKPLTGMWNSFLKDVNRSIDLSFIKYVGDAAGRPGDHNSTDLKFAENIGIKFETPEQFFLGHSFVPPNFESFHPKNYLVRNSSSHPYHFKKSEHQEIVVLVGFPSSGKSTLAESQIVTQGYERVNQDILKTKSKCIKAAIEALKKEKSVVIDNTNPTIESRKMWIDIAQEFEIPIRCIHLQSSEELARHNNVFRYIHHNQKQLPEIAFNSFKSRFQMPTVEEGFTNVEEVPFKCLKDYEDTWNYWYE
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Catalyzes the phosphorylation of DNA at 5'-hydroxyl termini and can dephosphorylate its 3'-phosphate termini. Has a role in the repair of breaks in single-stranded DNA.
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