lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. Unable to cleave either of the yeast Pcp1 substrates in yeast cells.
Miscellaneous:
MISCELLANEOUS: The functional differences between RBL12 and the yeast Pcp1 appear to be at least caused by differences in their transmembrane domains.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MKAIFNRRVVVDSSSRLTKLLANPTTHSHLNRQTFTSLYKPNQSRHFRTHYLPSSPSSPPVSRFDPSQLWRSEKIRGFFASALGNKAVKLGNLVESRVGFIGSQFPKKGFEFQRFSGFQRRGWKHWLQGLSDRDVVLGLVIANAGVFVMWRVFNQQFMMNNFMISLDNFKSGRLHTLITSAFSHIDIGHIVSNMIGLYFFGTSIARNFGPQFLLKLYLAGALGGSVFYLIHHAYMAATSPKGQGAFVRDPSRTPGLGASGAVNAIMLLDIFLHPRATLYLEFFIPVPAMLLGIFLIGKDILRITEGNSNISGSAHLGGAAVAAIAWARIRKGRFRF
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage.
Miscellaneous:
MISCELLANEOUS: The tRNA splicing endonuclease complex is present with 100 molecules/cell.
Subcellular Localization:
Nucleus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Note=The tRNA splicing endonuclease complex is predominantly associated with the outer membrane of mitochondria, suggesting that tRNA splicing mainly takes place on the mitochondrial surface.
Sequence:
MPPLVFDIDHIKLLRKWGICGVLSGTLPTAAQQNVFLSVPLRLMLEDVLWLHLNNLADVKLIRQEGDEIMEGITLERGAKLSKIVNDRLNKSFEYQRKFKKDEHIAKLKKIGRINDKTTAEELQRLDKSSNNDQLIESSLFIDIANTSMILRDIRSDSDSLSRDDISDLLFKQYRQAGKMQTYFLYKALRDQGYVLSPGGRFGGKFIAYPGDPLRFHSHLTIQDAIDYHNEPIDLISMISGARLGTTVKKLWVIGGVAEETKETHFFSIEWAGFG
The following text describes a protein:
Function:
Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents) (By similarity).
Sequence:
MLDLFADEAPWQEPLAPGAVVLRRFAFRAAQSLLDDIGFVASQSPFRQMVTPGGYTMSVAMTNCGALGWTTDRHGYCYAVRDPLTDKPWPALPLSFASVCRQAAIAAGYASFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGVPAVFQFGGLRRSDPIQRILLEHGDIVVWGGESRLFYHGIQPLKAGFHPMTGEFRYNLTFRQAAEKE
The following text describes a protein:
Function:
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Subcellular Localization:
Cytoplasm.
Sequence:
MTKTPAKKKRARSSKAKGTDANAALEARIGHSFADPNLLMQGITHVSALKSGRKRGDSYQRLEFLGDHVLGLVVSDMLYHAFPNADEGELSKRLAELVRKESCADVAKSLGLLDDIKLGSVGPSADARLRKSVLGDICEAVIGAIFLDGGHAAAAEFVKRNWTERMHKPRRPLRDPKTVLQEWAQGKGLPTPVYREVERTGPHHDPQFRVAVDLPGLAPAEGIGGSKRAAEKVAASVMIEREGVGGGNDG
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MAQDLSEKELLKMEVEQLKKEVKTPRALISKTGKEIKDYVEAEAGNDPLLKGIPEDKNPFKEKGGCLIS
The following text describes a protein:
Function:
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MPKEHKKRGRREEQKKRKRDHDHVDAAPKRLKKEDDVELESIENGEAFHHEPVDVTRPGELTYYGMLDDEEQEYFKRADEMLELNQFEDPEARNLFLASVYKEADGKELKIANSQSCSRLLERLILLSSPDQLKNLFQKFNGHFLNLVQHRFASHCCEALFIHAAPVVTLELAEPQTLQTPPSSDPNAIIVSMESLFLYTLAELEEHLGYLMTDRFASHVLRVLLVVLSGAPLAKENKNKSVLQSKRKEKVGIAGTERGQDWVLEKRPVPKSFLEALEKTINASASTLDTANLRLLATHPLGNPTLQLLLKLELAHFGKSRAKDENSIIHKMLPDDPIAEGTESAAFINGLVYDPIGSRLLETIIESAPGKLFKQIYSEFFKERMGSLSRNEIAGYVAGKILERLGKDDLDEAMRQIVEQIPNLVERNRTAIIKTLLERCIARNVDISLIKDQLEAVYSGPNGFEVTRILRVSESPAENLKQNGKQDHSPEKVHGSLLAQTMMAVDGPLGDLIFDSLAKLTPELSVQLARDPTASRTLQAALTAEHASVIFRRKMIQQFYGHVGELALDPAASRVIDAVWHGTHGLAFIRERIAEELAENENSLRESFVGRAVWRNWRMDLYKRKRGDWVKQSKYTAGNDGFQSFPESNGESSTTPPHRQSHAQNQRGGKHMSAIELARQKHAAKAVEAKKREAQTDKKMKREKKDKHVGVAESSKGKEKASVVAQ
The following text describes a protein:
Function:
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MWRATRPALALTAALRSVTLSGARMPTRALSAGRCLARADGGADQPQAQQVGDEVVIRPYRPPRKPENDDQLRARLVYQARKRGIKENDLIFSTFCHKYLDQLSRPQMEQLDIILNEHDNEWDMFNWLSGTRPAPEYLKELELFGALVDHTQNRSKEVRVTMPPLKPPSDKA
The following text describes a protein:
Function:
Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS4 is essential for histone acetyltransferase (HAT) activity of the complex.
Miscellaneous:
MISCELLANEOUS: Present with 800 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MGIFQSIEEANNTSERLLRSEIKNSHGEFEKFDFDTEEYEINPKRKLRLVSRINPNAGHLRKSKSCFTVDEHVDETRCQKPVMKSPFMSNVDDEIKKKRETITKMTLEIEHHELSQNIRKPTDDLLPDSTYQPYHKKMLKQENRMIQSDIVNGENEADRLSLISDRLGMLNWEVTLQKVTKINDPTDENEMETKRYQTKELIDSMLHKFESMKKKSRNLARRPASSDSLLKLVSGKDWPKIYTRIDRTFIPDYASSSDEEEEKITVEEIRERRLKKREQQCGGSIIVLLSDHQSQKGMTRFAIVAEPLRKPYLIKTSTKERNSWKNKVPTNPKKFKKAPRISTQIAVKRRREVIPLTMEVEPEVIRDIRQDTQKSMKLNVKAEEISVTETVKSKEMNALRNNAASISPTLSEKAPLGSISSCTASQISQRSSENVGAIINNINPNLAIVPSCNEKTFVKTHNGMKTNSGINILPVRKKKKV
The following text describes a protein:
Function:
Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs (acp3U(20)).
Subcellular Localization:
Nucleus.
Sequence:
MDETSSEQMTPVERDTNERLEVAEIYRNKHKGRKFKNPRTAHRSIFSTCMARCENQQPFSGLKTSNTTFLDEIDRRGNCENCGRSRKFFCYTCHIPLPAIKELVPYIPSLPCRIDVIKHPNEHDGKSTSIHAAVVAPEMVKIYTFPNFPDYSIEDGVVLVYPCDGAVPMTTMTTSRAAEIQKMVFIDSTWAQAKQIYKDPRLKALPCVVLRTRKSLFWRYQLGKPDSYLATIEAIYDAVVSLDERRRESDSDGASSYDGSYDNLLFFFRYFYEKMEELYFHKSPAV
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MRMAKQIVKVGITTEEIDYHVHKAIIEHGAYPSPLNYRGFPKSVCTSVNEVAVHGIPNSRCLQNGDLLSVDISLFYGGVHGDLCETFLVGNVDESGRRLVDICRQSLDEAISICGPGVRMSTIGNTISLFAKKSGYSVSECCNGHGIGSVFHALPDVSHVANNRPGKMQPGMTFTIEPVLCEGSSKLYTWEDEWTIVTSDGMRTAQFEETVLITEDGVEVLTFDYEQQEA
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MVQLFHLTFTQGFFIGQLSVIVIVYIFLRFFLFCTKEELKNVQEESYPLSPSNEKSTTEFNDATHKVTPSLSEIYDVKTHEEESLDWFNVLVAQALSQIRQDAVSDDAALKKLQTLFNGKRKPSFLGPIHIKSISLGQRYPVFSNCRIQAQPDDTNGLRATMDLSLEDDIHFVVNTSAVLNVPRPAFAMLPVSLSVRIVHIRGKLSIYFSQSSKSAKRAYLNFTFDPDFDMGIEIQSLVGSRSKLQDIPKIAHIIETRIRKWFITRCVSPQFQQISIPNIWPSSAREGHRQKSTE
The following text describes a protein:
Function:
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MNLILIKSSELSSSQSVDLSRSDERSKHILKHLKKQSGGVVSVGVVDGCKCKAVVELYPGTQEGDANGSDSTNKGDNSIRLVLQMETFVQPQNEPEITLILAVPFPARLKALWPVISSFTHVKRIVIVKGQLSNAEFFETSALLPKIYEPLIEKGMSQGGRTRSVKVDVCLQDSTISRTLLSKLGLLGGGGAGAAVDGIARIFLDCGDETVVPPPARDIVLKHCQNTTSVDHTPKAIVAVGPERGWTDEEANIFVDQCGFETATLGSSILRVDTAVIAGLGVVSAALDECLKDNTTVRASCKRERQEDE
The following text describes a protein:
Function:
May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence:
MDTNDDPDEDHLASYDIQLSIQESIEASKTVFYPERFVPLSDQNRKIVEAIKQGHILQLQEYVKCKYALDEADEKGWFPLHEAVVQPIQQILEVVLDASYKTLWEFKTSDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSALLKHNTSLDQPCVKRWSAMHEAAKQGRKDIIALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVFALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIQKSGMTPIHSAADGQNVQCLELLIENGFDVNTLLADHISESYDDERKTALYFAVSNNDIHCTEVLLAAGADPNLDPLNCLLVAVRANSHEIVRLLLSHGANVNCYFMHVNDTRFPSAIQYALNDEVMLRLLLNNGYQVEMCFECMHGDIFGNSFVWSEIEEEVLPGWTSCVIKDNPFCEFITVPWMKHLVGGVIRVLIDYMDYIPLCAKLKAALEGQREWPEIRQILENPCSLKHLCRLKIRRLMGLERLCQPASMEKLPLPPTIQRYILFKEYDLYGQELKLP
The following text describes a protein:
Function:
Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines.
Subcellular Localization:
Cytoplasmic vesicle, autophagosome. Cytoplasm, cytosol. Mitochondrion.
Domain:
The N-terminal region is essential for activation of the IFNB promoter activity.
Sequence:
MAQSAEVQPSFEDIFNILSQVPAEKLLSLKHKLKHLIFAPSSKLLQAMVLLTLGQEADARICLNALGDNLAALYIHQTKLGTAAVQKDGGNSQHPQLDAGAMAFLAQIYLLLANEKLCSHEAVVKAEQAANNASRDAQRDTLNSIPVGDQERYGLAISTVDSDSKFRTLRSDVSTGFLRMTSPNNTVKSSPMKIRKTSDLSGTQTLQSSGISDSFTSLLISQSPTAIFCTPTPSCQSSRLCEVSTSDAGQPDGERQSHSLQETGRASSPSSHSRQDTNPQVPHLGKTLQVSSSRLSLPIVETQLPILGAVGQPVESNDISSTVIAEPQVPKESRDQKQKLSTSLPYSRMTINTGPACIPIEDSYIPAGTSNSAPASTSVCSFPPQTYFSSAILRPLQSIPYNVPFPPPLHSSPSPTGPPPLKTVEASLAPEPNGEKKKFFTFVVLHAWEDEHIACRIKDLLENMGVPNGATFCEDFLVAGHNQLTCFQDAMENSAFLILLLTKNFLCHQCMFQTNSALMESIQRPSKHNSVIPFVPKENPLERSQIPSMLSVLVALDENSPVFARTVQNTFTPEKINERKAMWCQIQQVQEQKRKLELYQDHCQTLQNLGALTLGSLPQMSPSAMQLNQSSLEQLLEQLLPLQSSQQCHPPVSVSAATRPLPRAGHPTSAQVGPSPSQPLNLPSGQHYTTTDPGGARSIIIQHARMVQIGNHNTMHVETAAPGPQDSEEESRENA
The following text describes a protein:
Function:
N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine. Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides. Non-essential component of the NatA N-terminal acetyltransferase.
Miscellaneous:
MISCELLANEOUS: Present with 2370 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MGRDICTLDNVYANNLGMLTKLAHVTVPNLYQDAFFSALFAEDSLVAKNKKPSSKKDVHFTQMAYYSEIPVGGLVAKLVPKKQNELSLKGIQIEFLGVLPNYRHKSIGSKLLKFAEDKCSECHQHNVFVYLPAVDDLTKQWFIAHGFEQVGETVNNFIKGVNGDEQDAILLKKHIS
The following text describes a protein:
Function:
Essential for murein biosynthesis. Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL-2,6-diaminopimelate (Probable).
Subcellular Localization:
Cytoplasm.
Sequence:
MEHLLNPKAREIEISGIRKFSNLVAQHEDVISLTIGQPDFFTPHHVKAAAKKAIDENVTSYTPNAGYLELRQAVQLYMKKKADFNYDAESEIIITTGASQAIDAAFRTILSPGDEVIMPGPIYPGYEPIINLCGAKPVIVDTTSHGFKLTARLIEDALTPNTKCVVLPYPSNPTGVTLSEEELKSIAALLKGRNVFVLSDEIYSELTYDRPHYSIATYLRDQTIVINGLSKSHSMTGWRIGFLFAPKDIAKHILKVHQYNVSCASSISQKAALEAVTNGFDDALIMREQYKKRLDYVYDRLVSMGLDVVKPSGAFYIFPSIKSFGMTSFDFSMALLEDAGVALVPGSSFSTYGEGYVRLSFACSMDTLREGLDRLELFVLKKREAMQTINNGV
The following text describes a protein:
Function:
Component of the DZIP1-Fam92-Cby complex which promotes ciliogenesis in sensory neurons and spermatocytes by acting downstream of Cep290 to initiate early ciliary membrane formation and thus transition zone (TZ) assembly. During spermatogenesis, also regulates distal elongation of the basal-body and their docking (anchoring) to the plasma membrane and as a consequence, regulates the initiation and proper elongation of axonemal microtubules. Within the complex, required to recruit or stabilize Cby at the distal basal body of cilia to promote DZIP1-mediated early ciliary membrane formation and initiate TZ assembly. May also act with Dzip1 to restrict Cep290 localization to the proximal part of the TZ. May also be involved in recruitment or stabilization of Mks1 at the TZ.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes at the transition zone (TZ) in type I sensory neurons and spermatocytes. Localizes at the centriolar distal ends of early spermatocytes and in elongating spermatids, when the TZ migrates away from the basal body, localizes at the ring centriole.
Sequence:
MFRRGKLSFLNTKDDRVKIINERINITERHLMEMCSSFALVTRKMAKYRDSFDELAKSVKSYADDEEINESLCQGLKSFTNAVTIMGDYMDINVHRLEHKIVNELAQFEQLCKSTRDNLRLAVIARDKEVLRQRQMLELKSKFSANNSAADSELFKAKMEVQRTNKEIDDIIGNFEQRKLRDLKQIISDFILIAMKQHTKALEILSASYYDIGTIDERDDFIEFQKLMKTKEELASRKTALKKGLRSQSMDSLEHEHLVSPLKRRPKLSRSNRNLTGAGINHGSKTEPEDETDEQDEEEDDEDEETEQSGEEDEESGTATDDEREPTQPGNQVPPRENVFGAKIRSASKDIATPSTSASATSAPSKPSRQTVKHPFKAVASTHVRLQKQFHVPQH
The following text describes a protein:
Function:
ATPase histone chaperone which facilitates loading of histone H3-H4 onto DNA in an ATP-dependent manner. Plays a genome-wide role in nucleosome organization and establishment of chromatin. Also plays a role in heterochromatin assembly by stabilizing recruitment of the histone methyltransferase clr4 to methylated histone H3, to promote the transition from H3K9me2 to H3K9me3.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MKEEASEHGGSADETQELSPVSDSSDEMPNNAKRRRRSQSMIANKRIHQAFQEDEGDEDWEEEEHKPKAKRRYNTRSNESFSEGDDEPFEVSESSALEDELSDSEDSFIRSVRSKPKYKPGTRRSTRLRNRRSQDEEESEEEHRPILRERTSRINYSVPLAFPPVDEMDGDPSSQVNQSRSRKTHSELAITKLLRQQVSSFMPYIDSSGSESESDNTRIKKSSAKTIKALTDPANSGGPPDFGRIREKSDLADSDPLGVDSSLSFESVGGLDNYINQLKEMVMLPLLYPEIFQRFNMQPPRGVLFHGPPGTGKTLMARALAAACSSENKKVSFYMRKGADCLSKWVGEAERQLRLLFEEAKSTQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMESRGQVIIIGATNRPDAVDPALRRPGRFDREFYFPLPDRDARKKIIEIHTRNWDPPVPEWLCSMLAEKSKGYGGADLRALCTEAALNSIKRTYPQLYRSTKRLQIDPKTIKVKVKDFVMSMKRMIPSSERSSISPSKPLSPELKPLLNEAFQDIEKTLQKLMPVASKLNPLEEVMYDDPKENDFEYQQRLETFETLRIYKPRFLICGRKGLGQTALGPAILQQYEGVHVQSFDMSTLLQDSTQSIETSIIHLFLEVRRHTPSIIYIPDIDNWLNVLPLTAITTFSSMLERLDFSDQILFLALSSSPLSELHPQLREWFSSKQSVYSLQYPTRDSIIAFFQPILELIKASPTELPGGIPRKRRVLPELPLAPDPPPFTSQKITLKQTKQADMRLLNKLKIKLNALLGSLRARYRKFKKPLIDFNDIYCVDPETGHSYRSREECHYEFVDDVVKQIGSDQKFSMMSLEEIEKRTWDNCYCTPKQFVHDIKLILRDALQLEDSETIKRAQEMYANVLLGVEDMEDDQFSQRCERMALREAERRKLRHGKLQKHLDETKADMQFTSEKPSVDESITEVDDAIKDGPPVLAETLTNSLMEDVGPENVDMDIEDNEIFTNQSTMSVPSMLVENEESPKPDEYIDQKDKVQSPLLNGKSPVGVPSEAALRVSTDVSTNISSNGRADIPVDTLITSPADVPNNAPTDAHNITSADGHIENIEQEVVFPDLVFDEDRLTPLKQLLIDSTTGFTVDQLLHLHSFLYQIIWNTKSEWNRNSVVDECERAVKEFMINALQ
The following text describes a protein:
Function:
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. Required for spore germination.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNEAIEPLNPIAFQLGPLAVHWYGIIIGLGALLGLWIAMRESEKRGLQKDTFIDLVLFAIPIAIICARIYYVAFEWDYYAAHPGEIIKIWKGGIAIHGGLIGAILTGYVFSRVKNLSFWKLADIAAPSILLGQAIGRWGNFMNQEAHGEAVSRAFLENLHLPEFIINQMYINGQYYHPTFLYESLWSFVGVIVLLLLRRANLRRGEMFLIYIIWYSIGRYFIEGMRTDSLMLTDSLRIAQVISIVLIVLAVAAIIFRRVKGYSKERYAE
The following text describes a protein:
Function:
Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass type II membrane protein.
Sequence:
MNNNNVTEATSRAQIRPYYDPDSFNAGYSAVFKPDEGVVDPHGYTIASKLNVINSSPTTKRMANALFKSSPMKKLSNSVNDGLSLEGSNGEITGLNNFEWAELVNIQKWRKIFEQLLDMFFRKYFQLLIQQPFDVARLLIQVGEFKIFKTTVDTNKPQAPIILRDEEGDGAAREGEEDAYDEEEIDFFPIERKIAEANSTAPIMAEETDHSHHEPTDISLTIAPQSLHTIDVINALFDQEGIRGLWKANNTTFIYNFLSLSIDTWFTGLLSSFLGVPDPYFMEVINSPDISKSFILALGAGVFTSIILLPVDLIRTRLIVTSFKKKKNVKTDGKNMVTNTRSLRQLIRCWSWRKNGVSIPLDMWSLTILQSINNSFFNKLFDLVIYNQFHIEKYSQTVMYNTMKFFSKSLELFIKLPLENLLRRCQLNYLLNDQRLSFKVDSTELIVKPKKYNGIWDVIRNNSNTNRGQLWNGWKVGVISLICGYGLQMMNKVDINMEQEKF
The following text describes a protein:
Function:
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Subcellular Localization:
Nucleus.
Sequence:
MGFALIRPPGHHAISKGPMDFCVFGNMAIAARYAQRIHELKRVFIIDFDVHHGNGTNDAFYDDPDIFFLSAHQDGSYPGTGKIDEVGHGSGEGRRHQLLNEICSESGNNGDGDLCHDKGFEGHDSCFKCSEECDSFEVNQKSLSRRKGESSGVGHPAVPYPSVEIGTRKQGRIASLLPTYEDGLCPLLQRAILNKTGTYVQISSKAESIIWRALRLFFLNGEQDLPAFLLVDLGIVKYPTYNRINSDHIFPGLNDLLAYEEAIEVAQIMDEVLDDNNSGLVLRCISISNSRLFISCSKSTQASVSKSAATFLSCLLASGVYLKAVLLGISFLKREHG
The following text describes a protein:
Function:
Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingoid base, lactosylceramide, and monogalactosyldiglyceride (By similarity). C.elegans contain specific sphingoid bases, which are unique or different in structure compared to the sphingoid bases found in other animals. Two examples of these distinctive compounds are: 15-methylhexadecasphinganine and 15-methylhexadecasphing-4-enine.
Sequence:
MFSIFIKIILILPSIATKTNNIDIKSWRSAQTFDGFGAVSGGGATSKLLFTYFSEKSDRKQVLESLFNKDNGLQLLKVEMGGDDQSTEGTESSHESEKGKISKNNYEFQLISEVREINPTIPICVLPWAFPGWIGNTPYDNVTETAEYVVNWLKIGRDTWNFDTFCVGVWNERNFSESYVKELRKILNLNGFNETLIVAGEGFRMDDSYSRLLDKRFINEYDIIGVHYPGGRIPENVQKSGKVIWASEDYSTDNRDTGEGCMARTMNWNFINGNITGMISWHLMSAFYPQLPWYRCGLARIDENKFQTEKAFHVLKYITSHVKRGWKILRESSGRFDGGGTYVTYTNGKDSTIFVETMSYKKSLCEYSSPRPYHVKPSQLIRFKFSEIPSFQGLNMSLNFGPSKFFSKSVNSTITILLPVNSFGILTTLPVSTPKRVTIKTPLVPLNYHDDFENYEFDEEPKFWMPQKGSWVVRNGRAVQKVTRPSISWCTSHIRTPYAVMAYRKKNSILNAEVNIPKHSTAKSIILGIRSNCSGCDIEVINCRGIFVEIEFSNKKVTIFSDFVDRSIIAEFKARRKVEFGKFYKFSIHLLDSHLFIKFGNHHVMTSVEIPEEQLNKTNNDTLFVIGTGNFGISEWDNISTDYFH
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MTTDQQLDSALDLMRRLPPQKIEKNLSDLIDLVPGLCEELLSSVDQPLKIATDKKCGKYYLLCDYNRDGDSYSRPITQEKSTGRSAHYKLTSTAMLWLQTKKPGSGTMNLGGSLTRQMEQDSAVSEAVPHIANIGKMVEDMENKIRTTLNEIYFGKTKDIVNGLRSQPTHIFRITPVHFYYYSGPPGATATTRRWRTGRSRRSVCASWRWMPTRPLTSTGRCTSKAECPRSTCGTWTTALRALCSSRRAGTAPGRSWAAGTPSTSWKCRCAGRPVSPTRARQPERVRGRRVCRKVLAEFTVPAFIYLFPQLPRSARGVTAEFQVKRVKTKLKNKVLSNLCHTRYNRLGVTAGEKGDAR
The following text describes a protein:
Function:
Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.
Subcellular Localization:
Golgi apparatus membrane; Lipid-anchor.
Sequence:
MGAKESRIGFLSYEEALRRVTDVELKRLKDAFKRTCGLSCYMGQQCFIREVLGDGVPPKVAEVIYCSFGGTSKGLHFNNLIVGLVLLTRGRDEEKAKYIFSLFSNESGSYVIREEMERMLHLVDGKVPDSLRRCFSEGEKVNYEKFRNWLLLNKDAFTFSRWLLSGGVYVTLTDDSDTPTFYQTLAGVTHLEESDIIDLEKRYWLLKAQSRTGRFDLETFSPLVSPPIHPSLSEGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSHTELRDMVVALLEVWKDNRTDDIPELHMKLSDIVDSILNAHDTTKMGHLTLEDYQIWSVKNVLANEFLNLLFQVCHIVLGLRPATPEEEGQIIRGWLERESRYGLQPGHNWFIISMQWWQQWKEYVKYDANPVVIEPSSVLMGGKNPLATTAQSLEPSEDKTGGAGLDYLNTTEEKFSDDISSASEASESASSTFLYSSTPAADMCFARQHNTSDNNNQCLLGANGNILLPFNPQKPGAIDNQPLVTQEPVKATSLTLEGGRLKRIPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIKNSKTNIPELELFPRHLLFLRQQPATRTQQSNIWVNMGNVPSPNAPLKRVLAYTGCFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSENYLTLLDDEDHMLEYLKIQDEQHLVIEVRNKDMSWPEEMSFIANSSKIDRHKVPTEKGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDGRPDWEVAAEAWENHLRRNRSIVVDLFHGQLRSQVRCKTCRHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGTTPVRYGLRLNMDEKYTGLKKQLSDLCELKPEQILLAEVHGSNIKNFPQDNQKVRLSVNGFLCAFEIPTPGSPTSASSPVQTDLPTSPSTTGILNAPTNGDLPRPTLLPNGMPNTVVPCGTEKTFSNGMVNGHATILPGSPFIGYIIAVHRKMMRTELYFLSSQKNRPSLFGMPLIVPCTVHTRKKDLYDAVWIQVSRLASPLPPQEASNHAQDCDDSMGYQYPFTLRVVQKDGNSCAWCPWYRFCRGCKIDCGEDSAYIGNAYIAVDWDPTALHLRYQTSQERIVEEHESVEQSRRAQAEPINLDNCLRAFTNEEELGEDEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRENFNPGAFLVPRDPALCQRKTLPPQGDDSCDPRPPPGELKKVESQNGFTPGEGDALCKSPSSLSTNIVNNTKGSPSSARKSGSSCPSSKNSSPNGSPRTLGRSKGRLRLPQIGSRSKLSGSKENLDPSKENGADQSSESADGTSRGHVLGESQPELFTPQDNEGPVANGFFWGQEASANSCSNGQMENYSEEDITDDQREDVCIKPIYNLYAISCHSGILGGGHYVTYAKNPNNKWYCYNDSSCKELHPDEIDTDSAYILFYEQQGIDYAQFLPKIDGKKMADTSSMDEDFESDYKKYCVLQ