lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be an export pump for cysteine and other metabolites of the cysteine pathway (such as N-acetyl-L-serine (NAS) and O-acetyl-L-serine (OAS)), and for other amino acids and their metabolites.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSRKDGVLALLVVVVWGLNFVVIKVGLHNMPPLMLAGLRFMLVAFPAIFFVARPKVPLNLLLGYGLTISFAQFAFLFCAINFGMPAGLASLVLQAQAFFTIMLGAFTFGERLHGKQLAGIALAIFGVLVLIEDSLNGQHVAMLGFMLTLAAAFSWACGNIFNKKIMSHSTRPAVMSLVIWSALIPIIPFFVASLILDGSATMIHSLVTIDMTTILSLMYLAFVATIVGYGIWGTLLGRYETWRVAPLSLLVPVVGLASAALLLDERLTGLQFLGAVLIMTGLYINVFGLRWRKAVKVGS
The following text describes a protein:
Function:
Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Sequence:
MDYSSGRQEEKKPHTTNTCFGQYSYSAEEYQAVQNALRQKLGPEYISTRQAGGGQKVCYIEGHKVISLANEMFGYNGWSHSISQQNVDFVDLINGKFYVGVSAFIKVQLKDGSFHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALKCFGNALGNCILNKEYLIAINKIPKQPPPPLDADKTKRSDLEPSVEKARFDSLAQTNSRQFTKLEKSANIPIEQMGNLPVREGHESATGPRTSLTNTTALPGNTTTHQDTENRPSNTSRSASDTTELSSSDPLLDSKQQRKLRQQQLQQKFRQEMEAKKLLQEKKDQQPTLHIKQEQGVGPVNHSTPNGHLVTKQEQYMADDPEMWDFTLDGIDMLDDPSTRSTDPPRPSTPNQHTMTTRSKTPQRPQCLRPPAQPQGHFRSSTAGGPSSPYRHGQMMKKRRLDT
The following text describes a protein:
Function:
Catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). Uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Sequence:
MTKIELRALGNTGLKVSAVGFGASPLGSVFGPVAEDDAVATVREAFRLGINFFDTSPYYGGTLSEKMLGKGLKALQVPRSDYIVATKCGRYKEGFDFSAERVRKSIDESLERLQLDYVDILHCHDIEFGSLDQIVSETIPALQKLKQEGKTRFIGITGLPLDIFTYVLDRVPPGTVDVILSYCHYGVNDSTLLDLLPYLKSKGVGVISASPLAMGLLTEQGPPEWHPASPELKSASKAAVAHCKSKGKKITKLALQYSLANKEISSVLVGMSSVSQVEENVAAVTELESLGMDQETLSEVEAILEPVKNLTWPSGIHQN
The following text describes a protein:
Function:
Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Also together with the LSM1-LSM7 complex, the LSM1-LSM7 complex binds to osmotic stress-activated mRNAs to attenuate the osmotic stress response, probably by limiting ribosome access to the mRNA and consequently translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the pre-initiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Structural component of the kinetochore and associates with centromeres in a NDC10-dependent manner. Involved in maintaining the structural integrity of centromeric chromatin to facilitate faithful chromosome segregation and proper kinetochore function.
Miscellaneous:
MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, P-body. Chromosome, centromere, kinetochore. Cytoplasm, Stress granule. Note=Shuttles between cytoplasm and nucleus. Exported in complex with LSM1.
Domain:
The region at residues 254 to 422 is required for stimulation of decapping. The region at residues 422 to 763 is required for PAT1 and LSM1 to accumulate in P-bodies and responsible for translation repression and P-body assembly.
Sequence:
MSFFGLENSGNARDGPLDFEESYKGYGEHELEENDYLNDETFGDNVQVGTDFDFGNPHSSGSSGNAIGGNGVGATARSYVAATAEGISGPRTDGTAAAGPLDLKPMESLWSTAPPPAMAPSPQSTMAPAPAPQQMAPLQPILSMQDLERQQRQMQQQFMNFHAMGHPQGLPQGPPQQQFPMQPASGQPGPSQFAPPPPPPGVNVNMNQMPMGPVQVPVQASPSPIGMSNTPSPGPVVGATKMPLQSGRRSKRDLSPEEQRRLQIRHAKVEKILKYSGLMTPRDKDFITRYQLSQIVTEDPYNEDFYFQVYKIIQRGGITSESNKGLIARAYLEHSGHRLGGRYKRTDIALQRMQSQVEKAVTVAKERPSKLKDQQAAAGNSSQDNKQANTVLGKISSTLNSKNPRRQLQIPRQQPSDPDALKDVTDSLTNVDLASSGSSSTGSSAAAVASKQRRRSSYAFNNGNGATNLNKSGGKKFILELIETVYEEILDLEANLRNGQQTDSTAMWEALHIDDSSYDVNPFISMLSFDKGIKIMPRIFNFLDKQQKLKILQKIFNELSHLQIIILSSYKTTPKPTLTQLKKVDLFQMIILKIIVSFLSNNSNFIEIMGLLLQLIRNNNVSFLTTSKIGLNLITILISRAALIKQDSSRSNILSSPEISTWNEIYDKLFTSLESKIQLIFPPREYNDHIMRLQNDKFMDEAYIWQFLASLALSGKLNHQRIIIDEVRDEIFATINEAETLQKKEKELSVLPQRSQELDTELKSIIYNKEKLYQDLNLFLNVMGLVYRDGEISELK
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MGAAVGKPAFGVAVAPKSQAEERLALAEHALLQWTRSPGADAGIWDADASYTNRGLLAAVDEVLLLAAEDPFPFPAAAAASARLRLDSAVGAAASRMVEEFLRVRVWNASRLRGAVHRLSLASTGLSLLVFPSAGERASSAGTGGEGEVDASDGSRSRASSGVPYDVADLLDAEVWDGLDLICPAGVSVLHEIALRIVRAGCTEELVRAFANAPCNVLDSFLSILRVECSQQTAEAVIKRWTTVTKIIGKAIVAMRRQLYAQNPGAFDGFRDEYLLAIAENRILILLDFANGFTSITSHEKLVYMLGMYEALADAAPSLLLLFSGARKQLIAERTQGILMKLAGAIRVMVSGVMAKIQGECMSPRTPSAAAGGVHPLARDAMTCVELLARHRTTLDLILADAGGGDERGSLAGVVSDLIAGLEHNLQGRLAVACADAGGSRHLFLANNISFVLSRVADADGVAAMLGAAFAARRRSRLEQHLASYAASSWGPVVALLDTPVCGRGKPAKILAEFNAAFTRTRDSEVCREVPDPVLRAVLRHALSDMVVPAYCAFLQKQPKLWKSVRYTADDLAESLSELFEGEVTDARKI
The following text describes a protein:
Function:
Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity.
Sequence:
MNEAILSRNHVKVKGSGKASIMFAPGFGCDQSVWNAVAPAFEEDHRVILFDYVGSGHSDLRAYDLNRYQTLDGYAQDVLDVCEALDLKETVFVGHSVGALIGMLASIRRPELFSHLVMVGPSPCYLNDPPEYYGGFEEEQLLGLLEMMEKNYIGWATVFAATVLNQPDRPEIKEELESRFCSTDPVIARQFAKAAFFSDHREDLSKVTVPSLILQCADDIIAPATVGKYMHQHLPYSSLKQMEARGHCPHMSHPDETIQLIGDYLKAHV
The following text describes a protein:
Function:
Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Endoplasmic reticulum.
Sequence:
MHTPKCRRPSMSATLSHKDLAGLAGCSALAFVLYLNTLNAGFVYDDRRAILANGDVTGARPLANLLRNDFWGTPLVDSGSHGSWRPLCVLSFRLNYLAGGMTPLGYHLVNVMLHCVATWLVFLVARTLLPSRMGVLAAGALFAVHPAHTEAVAGLVGRADLASCVCYLLAYLSYRRHMLNREWGSLILTIMLALAALLCKETAITALLLCGLCDVLSPVGRENSDKVCDGSISGLASFNFQRRFRSLSILGFTLLCGLYCRLSLLPRPSTAFSAADNPTAHESCFWTRTLTFLYLPVANFGILLWPQELSFDWGMEAVSRIRTLWDARNILTAGFYGSLVAILWKGSGLRSAASPMDFAEVANISLPLLRRLGGNSCHTWLGLTCDCHHQLSAPSYRSASAIYSTSSKSKSASWTAAPILGTAFLVLPFLPASNLLFYVGFVMAERVLYLPSVGYCLLFGLGFGHLWQRVNSSWRSRLMLLCGLALLLGVHGVRTFRRNLDWRDEEQLFRSAISINPPKALGNLGSVLSAQGRYEEAELTLRMTLGHRPTMADAHFNLGVVHQKQLNFSSAIPCFRRAIELRPQLAVAYLNLGTSLISLGDHRQEAISVLRTGARLEGSGVRDRGAHVEARYTCYLQLSVLYRSDGRLQDAAAALRESLKALPLLPQKQRAVLHLRLGEILAELQDWNEAEHQQRLAMQLQPEQGAAYVTYGQTLARNGSRLAEAESWFKRALQLAPLEPSSHHHYADFLEQQERHHEALGLRLRAAALAPQDYTLQSCVADALRLLNRLAEAELWYRKAVTLQPMAAHAHANLGAILQMRGLRKEAVACYHKALELQPGHAISRANLARMNVHKHENE
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Domain:
Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines.
Sequence:
MDPNCSCSTGSSCSCAGSCTCKACRCPSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA
The following text describes a protein:
Function:
Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events (By similarity). PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (By similarity). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex. The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, mts/PP2A catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and Spt5, thereby preventing transcriptional elongation.
Sequence:
MEDKATTKDLDQWIEQLNECNQLTETQVRTLCDKAKEILSKESNVQEVKCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDSLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNNTNGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAALMELDDSLKFSFLQFDPAPRRGEPHVTRRTPDYFL
The following text describes a protein:
Function:
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
Miscellaneous:
MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MLVDLNVPWPQNSYADKVTSQAVNNLIKTLSTLHMLGYTHIAINFTVNHSEKFPNDVKLLNPIDIKRRFGELMDRTGLKLYSRITLIIDDPSKGQSLSKISQAFDIVAALPISEKGLTLSTTNLDIDLLTFQYGSRLPTFLKHKSICSCVNRGVKLEIVYGYALRDVQARRQFVSNVRSVIRSSRSRGIVIGSGAMSPLECRNILGVTSLIKNLGLPSDRCSKAMGDLASLVLLNGRLRNKSHKQTIVTGGGSGNGDDVVNDVQGIDDVQTIKVVKRSMDAEQLGHASKRHKP
The following text describes a protein:
Function:
Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Good candidate for an inducing factor with possible roles both in mesoderm induction at the blastula stage and in the formation of the anteroposterior axis at the gastrula stage.
Subcellular Localization:
Secreted.
Sequence:
MTVPSALVPILLLGMAAVVVQGLPLSSSLRNDTLERRWETLFSRSMARIPGEKRDMSRESDYLLGIKRLRRLYCNVGIGFHIQVLPDGRINGMHNENRYSLLEISPVEVGVVSLYGVKSAMFVAMNAKGKLYGSRHFNDECKFKETLLPNNYNAYESRKYPGMYIALSKNGRTKKGNRVSPTMTLTHFLPRI
The following text describes a protein:
Function:
Golgi auto-antigen; probably involved in maintaining Golgi structure.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
Subcellular Localization:
Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.
Domain:
Extended rod-like protein with coiled-coil domains.
Sequence:
MDGASAEQDGLQEDRSHSGPSSLPEAPLKPPGPLVPPDQQDKVQCAEVNRASTEGESPDGPGQGGLCQNGPTPPFPDPPSSLDPTTSPVGPDASPGVAGFHDNLRKSQGTSAEGSVRKEALQSLRLSLPMQETQLCSTDSPLPLEKEEQVRLQARKWLEEQLKQYRVKRQQERSSQPATKTRLFSTLDPELMLNPENLPRASTLAMTKEYSFLRTSVPRGPKVGSLGLPAHPREKKTSKSSKIRSLADYRTEDSNAGNSGGNVPAPDSTKGSLKQNRSSAASVVSEISLSPDTDDRLENTSLAGDSVSEVDGNDSDSSSYSSASTRGTYGILSKTVGTQDTPYMVNGQEIPADTLGQFPSIKDVLQAAAAEHQDQGQEVNGEVRSRRDSICSSVSLESSAAETQEEMLQVLKEKMRLEGQLEALSLEASQALKEKAELQAQLAALSTKLQAQVECSHSSQQRQDSLSSEVDTLKQSCWDLERAMTDLQNMLEAKNASLASSNNDLQVAEEQYQRLMAKVEDMQRSMLSKDNTVHDLRQQMTALQSQLQQVQLERTTLTSKLKASQAEISSLQSVRQWYQQQLALAQEARVRLQGEMAHIQVGQMTQAGLLEHLKLENVSLSQQLTETQHRSMKEKGRIAAQLQGIEADMLDQEAAFMQIQEAKTMVEEDLQRRLEEFEGERERLQRMADSAASLEQQLEQVKLTLLQRDQQLEALQQEHLDLMKQLTLTQEALQSREQSLDALQTHYDELQARLGELQGEAASREDTICLLQNEKIILEAALQAAKSGKEELDRGARRLEEGTEETSETLEKLREELAIKSGQVEHLQQETAALKKQMQKIKEQFLQQKVMVEAYRRDATSKDQLISELKATRKRLDSELKELRQELMQVHGEKRTAEAELSRLHREVAQVRQHMADLEGHLQSAQKERDEMETHLQSLQFDKEQMVAVTEANEALKKQIEELQQEARKAITEQKQKMRRLGSDLTSAQKEMKTKHKAYENAVGILSRRLQEALAAKEAADAELGQLRAQGGSSDSSLALHERIQALEAELQAVSHSKTLLEKELQEVIALTSQELEESREKVLELEDELQESRGFRKKIKRLEESNKKLALELEHEKGKLTGLGQSNAALREHNSILETALAKREADLVQLNLQVQAVLQRKEEEDRQMKHLVQALQASLEKEKEKVNSLKEQVAAAKVEAGHNRRHFKAASLELSEVKKELQAKEHLVQKLQAEADDLQIREGKHSQEIAQFQAELAEARAQLQLLQKQLDEQLSKQPVGNQEMENLKWEVDQKEREIQSLKQQLDLTEQQGRKELEGLQQLLQNVKSELEMAQEDLSMTQKDKFMLQAKVSELKNNMKTLLQQNQQLKLDLRRGAAKTRKEPKGEASSSNPATPIKIPDCPVPASLLEELLRPPPAVSKEPLKNLNSCLQQLKQEMDSLQRQMEEHALTVHESLSSWTPLEPATASPVPPGGHAGPRGDPQRHSQSRASKEGPGE
The following text describes a protein:
Function:
Plays a critical role in the metabolism of the essential lipid carrier used for cell wall synthesis.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLFTLKKVIGNMLLPLPLMLLIIGAGLALLWFSRFQKTGKIFISIGWLALLLLSLQPVADRLLRPIESTYPTWNNSQKVDYIVVLGGGYTWNPQWAPSSNLINNSLPRLNEGIRLWRENPGSKLIFTGGVAKTNTVSTAEVGARVAQSLGVPREQIITLDLPKDTEEEAAAVKQAIGDAPFLLVTSASHLPRAMIFFQQEGLNPLPAPANQLAIDSPLNPWERAIPSPVWLMHSDRVGYETLGRIWQWLKGSSGEPRQE
The following text describes a protein:
Function:
Component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway. In the Pelota-HBS1L complex, pelo recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel.
Subcellular Localization:
Cytoplasm.
Sequence:
MKLLGQKLVPNQPGTITIIPEQPDDLWFLYNLIANGDIISAPTTRKIQTCSDKKNTSRVKLELEIRITSFDYDKSCSIIRVRGKTITSNDHVKSGVFHTLELGKNKEFNLMKKLWDEETIGILKDGSDPNGGSKVDLAVILMKEGLAQIFLIRQSATSHCATIQGDKITNNSGSKSFFENIFVSFRKHIDMDVIPYVVIASCESIKDEFRVYLLLEAHRSKIKSIENNKSRILLVNKNNVKEILHDKVVMSMMKNTKSEIDIKVLDEFMNMVSTNSKRACYGTKDVEYAHELMAIETLLITKEILRNEDNKMRQKYLRMEKSVKKAGGKVVQFNQDVGQRLAQLTGIAAILRFPLPDVDELVL
The following text describes a protein:
Function:
Plays a role in pre-mRNA splicing by facilitating excision of introns featuring long spacing between the branchpoint and 3'-splice site. Assists the splicing of several components involved in chromatin organization, such as several shelterin complex subunits.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNSIHIKKKSNRSFRRRKVFGNEKEFDLEELDDNDIRLRQALEATKRRKIRNSIIGINAEKLLNQETKKEKQLNTANEPHEANDQTSAQSSKLIEAQLPTVEDRFAKQTNEVDINTHLLNFVEKKLKQERLAQNYSENGETNALNTKNESTVQNIKNSLHPNEHSFIRDAAALGAIREVDLGIISTDVDNLKNGRKRQKKRARMKEKLDSKALRTSEDAARDEFIEKMLKPISQDEESKGIYRRFRVYKDGTQD
The following text describes a protein:
Function:
Prevents the establishment of cellular antiviral state by blocking the cellular IRF7-mediated innate immunity. May also inhibit viral replication by modulating BRLF1 activity.
Sequence:
MAEAYPGGAHAALASRRSSFRNSLRRLRPTEKPDTSFMRGVWKYEIFPSYVRVTNKQVLQLDAQCQELPPCPSVGQILSFKLPSFSFNTTTYGSRYFTVAFLFFGAEDNEVFLKPFFVMHSDQDIVLSVLNPRSLFIEKGKFTWYIVPIRLVKNPYLYLQILPGQSDIQLTRSCTQSGDKLNTSEPQIFLSGSPVTSQDECLPYLLAQHTPPFLKSYARIHTFPGKVCPVNAIRRGKGYVRVSVDTPDLKREGPLNVKVGMTLLDDVIIAFRYNPYPKSHWRWDGESTDIRYFGSPVIIPPNFITELEYNNTYEAPLSSKITAVVVSHSSNPVFYVYPQEWKPGQTLKLTVRNISNNPITIVTGQSMAQAFFIYAGDPSISTIMRRYIQRQGCALTLPGNIVVESSSLPTFERINKTFNGNIVASEGTL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically mediates the formation of polyubiquitin chains and plays a central role in DNA repair. Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by UV and ionizing radiation for example. Functions in double-strand break repair, and is required for homologous recombination between sister chromatids in meiotic and mitotic cells. In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. Required for normal cell cycle progression. Along with brap-2 modulates the expression of cell cycle arrest protein cki-1 in response to increased levels of reactive oxygen species. Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase. Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites. To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm. Note=Mainly localizes to the nucleus and a small proportion is chromatin bound. Co-localizes with brd-1 in germline nuclei at meiotic prophase I. At the transition between mid- and late- pachytene, localization together with brd-1 is less diffuse and becomes a linear pattern along the chromosomes. In late pachytene nuclei, co-localizes with brd-1 and syp-1 at crossover sites and the short arm of the bivalent. Co-localizes with the pro-crossover factors cosa-1, zhp-3 and msh-5 at crossover sites in mid-late pachytene nuclei. Co-localizes with plk-2 in pachytene nuclei. Localizes to DNA damage sites on chromatin following DNA damage.
Sequence:
MADVALRITETVARLQKELKCGICCSTYKDPILSTCFHIFCRSCINACFERKRKVQCPICRSVLDKRSCRDTYQITMAVQNYLKLSEAFKKDIENMNTFKSLPPEKMFMESQMPLDITIIPENDGKRCAPDFAIPFLPVRRKRPSRPQPPSAFAEEPAEPVEPPEPATKQPVELQSRVFPLEKLKKDVETSTETYKISREELKNVDIEEYINTLRENSTEIDEIDALFQLMPTMRQFLRNNINQLMEKFHVAPPKKSEKPANRRVSFASSQDLENIKIMTASESLETPPEPIQKLAQKPEVFKSTQNLIDLNLNTAVKKPVVVASDDDEVVEDSEGELQIDEDDLANVTCATSSTTLDADRTPKAIQDDEDRIDDELSQVPKTIVCSRIHNDADEVVGLELLSDFYHKFLSNACRFAEDVNEHTTHLVMMNSEGRSISQKSTAYLYAIARKCVIVGRQWLVDCITTGLLLSEADYTITSCSSTIPVKIPPSIGSEMGWLRSRNDEHGKLFAGRRFMILRKFTMNPYFDYKQLIELVQQCGGEILSCYENLSPEKLYIIFSKHSKAIEESKNIENLYKCDVVTMEWVLDSISEYLILPTQPYKAVDSIGCLQD
The following text describes a protein:
Function:
Involved in sporulation. Required for the full activation of the early meiotic inducer IME1.
Sequence:
MIITIKFESKEKLVSMKQYITVVGVSVNQEGTFSWRPGTFYMKIHEESAAGPFAKGAEISDLSNSSAIGCGISINQEGGDGSIRVKESSLRKKQERMSTKYPTTMSCREAFDQLTSCYSIGGQFRSYYRYGDFTSCDKQVSKFKFCIIHGNDPVKVQEWYKDQVSNNKALENTSGVIWQERETTANK
The following text describes a protein:
Function:
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAPKRKQPYTEEGIDFKFTQFQIVPPINQKNFYTEYLKRDDQMYIWRDSAGEKDAKETESESANGDTKQDDSKKSQVEEEEDGIEESELGEEKDNKTIVLHIGSQNLRIGLASNKTPTTVPMVIARKMRAPFAQERCLLKDICHVNEDGNVAFDSEFDSNLKLLDSELKSWLKAQKKRSVPNGTQLVKNYNKISKPETVPPDDDPEKPDWIHFEQDDHVDVICGKEAFLLPLNEYPEYKLFYPIKSGVFNESDYASSQQLLADIYEIFKYSITSLLQIPVSQLSQYSVIFIVPDLYDRVYVEKILDILFFDLHFGKAAIVQESLCTSFGAGMSAACVVDMGAQKTSISCVEEGVVVPNSRIKINYGGDDITLLFMKLLMRSHFPYQDIDLKTPYDWSLANALKIKYCGLSEATYNVQLNSFFSRTPDKGTRKFTFKSLDETMLAPLGFFRPDIFENENKLHDRYTLFPVPVDVYDNQPNNPESLAQTTLLQISTPISNIKANGKDDEEKKEESDLVTPSVKFKPPRVVYCGSLAAPEIKNEKLIYPLDDAINQSIFSACDGNLSDEKAKNLYSSILIVGGAGQFPGFAHLLEERIHSKRANIPTISVIPPPRSMDAQFVAWKGACIYNRIRIVSELWIKNSDWKMLGSRVLQYKTLGYFWTG
The following text describes a protein:
Function:
Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor.
Sequence:
MKSYQAVYQILSKETDYISGEKIAEKLSLSRTSIWKAIKRLEQEGIEINSIKNRGYKLMNGDLILPEILEENLPIKVSFKPETKSTQLDAKEAIDLGHEANTLYLASYQTAGRGRFQRSFYSPQGGIYMTLHLKPNLPYDKLPSYTLLVAGAVYKAIKNLTLIDVDIKWVNDIYLNNHKIGGILTEAMTSVETGLVTDIIIGVGINFTIKDFPQELKEKAASLFKATAPITRNELIIEIWRAFFETPAEELLYLYKKQSFILGKEVTFTLEQKDYKGLAKDISENGKLLVQCDNGKEIWLNSGEISLNSWK
The following text describes a protein:
Function:
3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation.
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body.
Domain:
Specifically recognizes and binds polyuridylated RNAs via 3 RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form an open funnel on one face of the catalytic domain, allowing RNA to navigate a path to the active site.
Sequence:
MDPGGHVRGPPAHGVRESPGKPASTTKNAYTRLVQQHHSVRFRSYLNYVAQKLQLEAEAGADTDSARKRGPTQEASFRNGLTVHGYSPGRAALAGIPECPGVQRRLEDGFETFRRPRASTPAEQSRRDLGAGREGNARSGEDCRPRPRHVFPRDSPKAIEVLGNRGPGRNPRPFGAPPRFPGPEERDEAETGRNRARRNRAGANPGRADDFRAAEQLGTDSPPSRSGRRGLSHWDRTPGGDKIPFQTRKNLEASSVPQNFERKKPLLDEIMSHADGRGNPRQFGTPRGVAHMVSPHGVGFKPGDKRSPSKPMRGKKRNVFEAYLSRDRVSEGLKRGELIQGLLRINPKKFHEAFIPSPDGTRDIFIDGVVARNRALNGDMVVVKLLPKEQWKVIKADGSDKETEVVNDSDEFLGTSLPQPPVRSDADSPDVIIEAQFDDSEAEDGQGSSQNVLSDGIKKLSVGTPEKGVNSPDTGSAKQADSIKEQDLEKLLQRSAKVVYILEKKHTRAATGFIKPLADKSSDHFRKWALFSPSDHRVPRVYVPLADCPADFATRSKDYANTLFVCRIVDWKEDSNFATGHLAKSLGQAGEIEPETEGILMEYGVDFSDFSPEVLSCLPQGIPWTIPPTEFSKRRDLRRDCIFTIDPSTARDLDDALSCKPLPDGNFEVGVHIADVSYFVPEGSALDEAASERATSVYLVQKVVPMLPRLLCEELCSLNPMMDRLSFSVIWTLTPEGKILSEWFGRTIIRSCVKLSYEHAQSMIEEPGKRFSPEELPPVCPEHSIEQVHRAVLNLHGIAKQLRKQRFADGALRLDQLKLSFTLDQETGMPQGCYIYQYQDSNKLVEEFMLLANMAVAHQIHRSFPKQALLRRHPPPQSKLLNDLVEFCHQMGLDIDFSSAGALNESLNDMFGADKYAAARKEVLTNMCSRPMQMAVYFCSGVLRDREQFRHYALNVPLYTHFTSPIRRFADILVHRLLAASLSHSKLPNLEPDALQKQADHCNDRRMASKRVQELSTNLFFAVLVKESGPLESEAMVMGILNKAFDVLVLRFGVQKRIYCNTLPLLDYHFQKVGKKPKLTLVWEPENQEQDAVHQEIRIFSLVEVVLKAEDTALKFNAALKRPGSEKAAAQKDQRESEPEPEDQE
The following text describes a protein:
Function:
Not known. Could form, along with HyaD, a complex involved in the processing of the hydrogenase 1 structural operon.
Sequence:
MSNDTPFDALWQRMLARGWTPVSESRLDDWLTQAPDGVVLLSSDPKRTPEVSDNPVMIGELLREFPDYTWQVAIADLEQSEAIGDRFGVFRFPATLVFTGGNYRGVLNGIHPWAELINLMRGLVEPQQERAS
The following text describes a protein:
Function:
Orphan nuclear receptor which acts in concert with the insulin/IGF-1-like signaling (IIS) pathway during osmotic stress, perhaps in response to a ligand modified by the sulfotransferase ssu-1.
Subcellular Localization:
Nucleus.
Sequence:
MNGTLADQLQSHLANYGQPMVNSQRNEDPSMYMNGSAASVSHTNGSSSMGNDQKFPSYKRMAQRRKVPEGELCAVCSDLATGYHYGVASCNGCKTFFRRTIVSEQTFICQYNGNCDVNKNIRCACRHCRFNKCLLVGMDAKALQIPAIQNDRDRIGPTKKIKMSSGSDDEQATTPHRLQDQEIIDQLTQVEGLCQELRRCIIPEVTGVTHALTSPCLLFETTDLKVDVSLTNTIFKELFPASMNDIRMWNIREMRICIEWAKTFDVYQRLNLFDQFALVRNFAFAFNLLNRVFYSPDHGPDKIVFQNGAFIMRQPQQQVQLSGCRPIYTRQMDEIMIPFRKLQLSVAEFATFKAALFFNPDALDLSPQAKQEVFEERNKYLGGLFTCITQKIGIPTGVQKYGSLLMMTASIQNILAQNEENMQVMELFKNWEVDPFVKELCMKRA
The following text describes a protein:
Function:
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes to the plus ends of microtubules at the hyphal tip, and this requires clipA and nudE. Localizes to the mitotic spindle poles, specifically to the spindle pole bodies (SPBs).
Domain:
Dimerization mediated by the LisH domain may be required to activate dynein.
Sequence:
MSQILTAPQAEALHKAMLAYLSVINAPQTAETLREELHFDESYNEATCKKFEGVLEKKWTGIARLQRRINDLEAEVRSLQAELEASPSAARAKNQDPTNWLPKPSSTHTLTSHRDAVTCVAFHPVFTSLASGSEDCTIKIWDWELGEIERTLKGHIRGVSGLDYGGQKGNTLLASCSSDLTIKLWDPSKDYANIRTLSGHDHSVSSVRFLTSNDNHLISASRDGTLRIWDVSTGFCVKVIKSATESWIRDVSPSFDGKWLVSGGRDQAITVWEVSSAEPKAALLGHENFIECCVFAPPASYEHLATLAGLKKPPPATSSCEFVATGARDKTIKLWEARGRLIKTLHGHDNWVRGLVFHPGGKYLFSVSDDKTIRCWDLSQEGRLVKTISGAHEHFVSCIRWAPSPNTDNPDPAGEKAGKKDAVKPSYRCVIATGCADNSVRVFS
The following text describes a protein:
Function:
Involved in growth arrest during conjugation. May interact with the G protein alpha subunit.
Miscellaneous:
MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
Sequence:
MEDGKQAINEGSNDASPDLDVNGTILMNNEDFSQWSVDDVITWCISTLEVEETDPLCQRLRENDIVGDLLPELCLQDCQDLCDGDLNKAIKFKILINKMRDSKLEWKDDKTQEDMITVLKNLYTTTSAKLQEFQSQYTRLRMDVLDVMKTSSSSSPINTHGVSTTVPSSNNTIIPSSDGVSLSQTDYFDTVHNRQSPSRRESPVTVFRQPSLSHSKSLHKDSKNKVPQISTNQSHPSAVSTANTPGPSPNEALKQLRASKEDSCERILKNAMKRHNLADQDWRQYVLVICYGDQERLLELNEKPVIIFKNLKQQGLHPAIMLRRRGDFEEVAMMNGSDNVTPGGRL