lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MKPKSEGLLSMEEEQVTNAVLNYALEIIHLLTGEDYNLVKKLAYSASNSSNIWMSRIHNIKQQLSLEHSVIIGKHDRNGENRLVSQMILELAQKIIQELTKQVPIKHDDIAVYFSMEEWEYVKSHKEQYNNMTTVDNQAHCSHVVCSYSIPSCINPKSDEYHNEENQEPDTVKNITGDPSRDHILEQHSIIVCQIKEEPFDNFCTQEQMVAENIHKEDFLPMNGDRDLGEDKDPEEKCSTKKHKKYKAKSCQCKVCGKWFCDKSRLARHLKIHTGERPFPCNVCGKTFACKSHVSVHQRIHTGEKPYTCMECGRKFTNNSHLVLHKVVHTREKPFTCPKCGKGFTRNSSLVKHLGIHADQKPHVCKECGKSYCQYANLVVHLRLHSGEKPYVCRHCGRGFICNASMVRHQRTHIEGKPYHCVQCSKSFTDNSSLNRHKKIHKEELYIQNHFTP
The following text describes a protein:
Function:
Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May have a role in synapse differentiation and growth.
Sequence:
MLGYEQGIRNCNACSLSVQQANPSFDSSGDQDNGGQGTDVWDFRDAVFPTVLMDGLNYLRTSGLLCDVILITGNDEHPAQRVVLAAVSPYFRAMFSGTGTSHEFLESKQNKITLHDIDSAILGQILNFIYTAEIQITENNVGDFLVAADFLQINSLQNLCCQYLRSQMNASNCVGIYLSAKSRNCRELAVNAKRYALEHFRHVVQEEEFLQLPFSELKGILGSHLLNTTGEGELLETITKWVEHKPSERSQFLQSLVSEIDVWQVPAEKLLSFVNSEILLRRLRDSGFTSEQLQLNDAVVLGGDFKMAVDKILSQRCDSPCSKAQSHQVAHSKKIRHSYEQEVIVALGGESSGFVLNSMECYTLGYDGWRCSIPTAVALSGIPNPTQVMPPMRTQRIFPACCSADYTIFVIGGICGGKLIDSCEFYSVQSNEWISLASLPIGIHGSGAALPNQVLCVIGGRSDQGIEKRAWVYEERFNLWEALPPMQLHRVHHGVTSLNCLLYAVGGLGGKHTDEQFLSSVECYDPALQRWIPIAPMHEARAYCGVVTVGSFLYAIGGFNGISWLRSMERYNPLTNQWTLLTPMSVARSSFGTTVWNGRIYVIGGCDGIHLLNTVEKFNPRTNRWHCAQAMQVRRLGLGAATVKIPLKME
The following text describes a protein:
Function:
Specific subunit of the TRAPP (transport protein particle) II complex, a highly conserved vesicle tethering complex that functions in late Golgi trafficking as a membrane tether.
Subcellular Localization:
Golgi apparatus, cis-Golgi network.
Sequence:
MDASEEPLPPVIYTMENKPIVTCAGDQNLFTSVYPTLSQQLPREPMEWRRSYGRAPKMIHLESNFVQFKEELLPKEGNKALLTFPFLHIYWTECCDTEVYKATVKDDLTKWQNVLKAHSSVDWLIVIVENDAKKKNKTNILPRTSIVDKIRNDFCNKQSDRCVVLSDPLKDSSRTQESWNAFLTKLRTLLLMSFTKNLGKFEDDMRTLREKRTEPGWSFCEYFMVQEELAFVFEMLQQFEDALVQYDELDALFSQYVVNFGAGDGANWLTFFCQPVKSWNGLILRKPIDMEKRESIQRREATLLDLRSYLFSRQCTLLLFLQRPWEVAQRALELLHNCVQELKLLEVSVPPGALDCWVFLSCLEVLQRIEGCCDRAQIDSNIAHTVGLWSYATEKLKSLGYLCGLVSEKGPNSEDLNRTVDLLAGLGAERPETANTAQSPYKKLKEALSSVEAFEKHYLDLSHATIEMYTSIGRIRSAKFVGKDLAEFYMRKKAPQKAEIYLQGALKNYLAEGWALPITHTRKQLAECQKHLGQIENYLQTSSLLASDHHLTEEERKHFCQEILDFASQPSDSPGHKIVLPMHSFAQLRDLHFDPSNAVVHVGGVLCVEITMYSQMPVPVHVEQIVVNVHFSIEKNSYRKTAEWLTKHKTSNGIINFPPETAPFPVSQNSLPALELYEMFERSPSDNSLNTTGIICRNVHMLLRRQESSSSLEMPSGVALEEGAHVLRCSHVTLEPGANQITFRTQAKEPGTYTLRQLCASVGSVWFVLPHIYPIVQYDVYSQEPQLHVEPLADSLLAGIPQRVKFTVTTGHYTIKNGDSLQLSNAEAMLILCQAESRAVVYSNTREQSSEAALRIQSSDKVTSISLPVAPAYHVIEFELEVLSLPSAPALGGESDMLGMAEPHRKHKDKQRTGRCMVTTDHKVSIDCPWSIYSTVIALTFSVPFRTTHSLLSSGTRKYVQVCVQNLSELDFQLSDSYLVDTGDSTDLQLVPLNTQSQQPIYSKQSVFFVWELKWTEEPPPSLHCRFSVGFSPASEEQLSISLKPYTYEFKVENFFTLYNVKAEIFPPSGMEYCRTGSLCSLEVLITRLSDLLEVDKDEALTESDEHFSTKLMYEVVDNSSNWAVCGKSCGVISMPVAARATHRVHMEVMPLFAGYLPLPDVRLFKYLPHHSAHSSQLDADSWIENDSLSVDKHGDDQPDSSSLKSRGSVHSACSSEHKGLPMPRLQALPAGQVFNSSSGTQVLVIPSQDDHVLEVSVT
The following text describes a protein:
Function:
Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.
Subcellular Localization:
Cytoplasm. Note=Localizes at the cell poles and at the septum.
Domain:
The structure of the N-terminal domain remains unchanged upon phosphorylation.
Sequence:
MGSQKRLVQRVERKLEQTVGDAFARIFGGSIVPQEVEALLRREAADGIQSLQGNRLLAPNEYIITLGVHDFEKLGADPELKSTGFARDLADYIQEQGWQTYGDVVVRFEQSSNLHTGQFRARGTVNPDVETHPPVIDCARPQSNHAFGAEPGVAPMSDNSSYRGGQGQGRPDEYYDDRYARPQEDPRGGPDPQGGSDPRGGYPPETGGYPPQPGYPRPRHPDQGDYPEQIGYPDQGGYPEQRGYPEQRGYPDQRGYQDQGRGYPDQGQGGYPPPYEQRPPVSPGPAAGYGAPGYDQGYRQSGGYGPSPGGGQPGYGGYGEYGRGPARHEEGSYVPSGPPGPPEQRPAYPDQGGYDQGYQQGATTYGRQDYGGGADYTRYTESPRVPGYAPQGGGYAEPAGRDYDYGQSGAPDYGQPAPGGYSGYGQGGYGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH
The following text describes a protein:
Function:
Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.
Sequence:
MTVSLNTMMGVDGLEDQEQLREIRNCLLKCISECSERGLVYAVRWAAEMLNGMNPIEMEHIPFSSTPTGEFDLDPDMANEKLLEVEEKNIYLLAKSYFDCKEFERAAYTLQNCKSSKSIFLRLYSKYLAGEKKSEEENETLLNTNLTLSSTNREFYYISEVLESLHYQGNKDPYLLYLSGVVYRKRKQDSKAIDFLKSCVLKAPFFWSAWLELSLSIDSLETLTTVVSQLPSTHIMTKIFYVYASHELHQVNSSAYEKLAEAEIIFPNSRYLKTQRALLTYDSRDFDEAESLFENILTNDPYRLDDMDTYSNVLFVLENKSKLGFLAQVASSIDKFRPETCSIIGNYYSLLSEHEKAVTYFKRALQLNRNYLSAWTLMGHEYVELKNTHAAIESYRLAVDVNRKDYRAWYGLGQTYEVLDMHFYALYYFQRATALRPYDQRMWQALGNCYEKIDRPQEAIKSYKRALLGSQTNSSILVRLGNLYEELQDLNSAASMYKQCIKTEETEISPETIKARIWLARWELGKKNYREAELYLSEVLNGDLELEEAKALLRELRSRMEHSYD
The following text describes a protein:
Function:
Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha-ketoglutarate (alpha-KG) and ammonia, has weak activity on L-glutamine, almost no activity on deaminated glutathione (dGSH) and none on glutathione (By similarity). May function as a metabolite repair enzyme (By similarity).
Sequence:
MPGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTSGFAMEAAASSLAQDDVVNWMTAKAQQCNALIAGSVALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLALYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREYREKFPAWQDADEFRLW
The following text describes a protein:
Function:
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11. RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity).
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to DNA double-strand breaks (DSBs).
Domain:
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer.
Sequence:
MTSIEKLLVQGIRSFDPREASVIDFYSPLTLIVGQNGAGKTTIIECLKYTCTGEMPPNCSSGQAFIHDTKIAGESEVKAQIKLRFKNPIGKPIVASRSLSLIQKSNKKQEYKQIDASLQSYTSDGQKVSKSFRCSDMDKEIPDLMGVAKPILKHVIFCHQEDSNWPLSESAKLKLKFDEIFSAVKYTKALKSLKDKRKELTTLIKELKLRLETISANIEHCNRIRKELIKAEEIYSNGNKSLEDIKIAIIEKQKTLSTIKIAESKLQELKNEVTVLNARKLEMERVKNQLFNSLTEVYQNETDEELVFMQSEFNRECETMATAEKELLENSEVLLSQKEVINNLIKENSSQKGRLQSLISQQDSILSDRDKQMKELVTRYKMSDFIQIQLPYQKEIVIKFINEITQKFDTLTSGISNYSKTNKQKLNAIQMKINQKRVDSNQFTSSSNEKMSTITLNSKKIQSLDQEIQQHTNSIGEIDTLEKQIQFSQSELSILKSDANLQEIQQSLDNLTTEKLEIEKEIQSLQSSLKLLNLQASSRTRLNIKRKEIQQNQQNINSQLNSQIINSINLILPNEFNNDNNNDDDDDQFRFNIIQRIEPIVPLINKKRLIFTNQLNELKQQFQILQNKKNQIDAQLTSSIEPQLKKKQIELESYEKLINDSKLKQSNLFENVNSNNNNNNNNNNGITVLLFENKINEMKLSLEKLEKSFIVLESEDILYKEYIEKANQDKECSLCKNEMNGNELTSFVHTLETHCNDIPNQLKQLKIEISNSKIQLEKFNKLLPIIVKREELIEKSIPELKESQKNLLEQQLKSNEMVLEKQNQIESLESQSVLYQQVTLVFQYIDQTKQSIQSIESEIQKEEKEIMKQSSDLRTIEEVDKDLEIQQEQLKTIEKEISNFTNKQKNDQIGIFEKERQLISIKNQLTTIKSASGIIDHLRDTKKELQSNNQQLQLEIENLQQSIDQSNNDAKQLENEFQQLEIEFEKKIDAYSKEKNTFSVRLDSINSLQSKILDPSELCKQLNEIQEKNQELESNLSTLSQDYLIGQQHISTIQQNLSSKDITKRAISDNISFRQHKNNVEQIIRQISRKNELIKEMMQSQLEIDSNKLEQEINSLKSKFDQITGQTAVLQSQINSNRQELSKPTYKNIDDVNKDLLIKLQTTETVGKDLDKYYKALDKSLMKYHTLKMDEINRSIKEIWQTTYKGSDIDTIEIRSEESGTANKTINYRVVMIKGDVELDMRGRCSAGQKVLACLVIRLALAENFCSNCGILALDEPTSHLDRANIESFANSLLNIIESRKSQKGFQLIIITHDEEFVQYLSRGNYCDYYWRVTKNANQHSHLERKEIAEL
The following text describes a protein:
Function:
VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MNDRLEEATLYLAATRPALFLGVPLTLAGLLVMFAGFVIVIVQNPLYEVVLVPLWFGARLVVERDYNAASVVLLFLQTAGRSVDGLIWGGASVSPNPIKVPARGRGMA
The following text describes a protein:
Function:
Participates in the repair of UV-damaged DNA by excising pyrimidine dimers that are the major UV-lesions. DNA glycosylase activity hydrolyzes the glycosylic bond of the 5' pyrimidine of the dimer. This leaves apurinic/apyrimidic (AP) sites in the DNA. These AP sites are removed by the AP lyase activity which cleaves the intrapyrimidine phosphodiester bond. Catalysis proceeds via a protonated imine covalent intermediate between the alpha-amino group of the N-terminal threonine residue and the C1' of the deoxyribose sugar of the 5' pyrimidine at the dimer site.
Miscellaneous:
MISCELLANEOUS: Phage T4 deficient in the enzymes are extremely sensitive to UV.
Sequence:
MTRINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLKRGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
The following text describes a protein:
Function:
Possibly involved in the regulation of flight muscles contraction, possibly by modulating actin-myosin interaction.
Sequence:
MADEEDPWGFDDGGEEEKAASTQAGTPAPPSKAPSVASDHKADSVVAGTPANEEAAPEEVEEIKAPPPPPEDDGYRKPVQLYRHWVRPKFLQYKYMYNYRTNYYDDVIDYIDKKQTGVAREIPRPQTWAERVLRTRNISGSDIDSYAPAKRDKQLIQTLAASIRTYNYHTKAYINQRYASVL
The following text describes a protein:
Function:
Cell adhesion molecule that promotes cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Cell junction, adherens junction.
Sequence:
MALTMTAHFLRNNPIQLGLNLRVLLMLSFVSGLVYGSQVIVPPKVNAVLGKNVTLSCRVQVDTNLSLTQSSWERKLPNGWVTLAVYNPMFGISIPPDYERRLSFRSPSALDATIMLEDVGFADIGVYTCKVATFPLGNTQASTTVSVLVEPKVYVSAGSSALIDGGNETTVATCIAERARPPADVSWETNLYGMSEAHMQEDANGTTTTQVHYIWQPSRHAQGHTLTCVVKHPALQSDFRIPYIINVQFAPDILVLGYDGDWYVGRENVQLKCRAKANPPAQHFRWIRLDGEMPNGAERVNNTLVFTRPLQKNDSGVYRCEVANDIGLHSRDIRIRIQDPPSTTTMPPTTPVRLLTADISATAPGNKQRALITSPTLAPLHEGSLGTIVGGAVGGALFLLLLLILAGVYYQRQRRTFRGDYYTKQYHGPSDMQKAPQPHELQQVYSKGSPDTKLKSNQDNGTIYPDKDREEWGDFDRERSPNGRSRALREAGQLNHHNHQNHEHGFHSNHHTGHPQSYSPAHHIQRSSLQPQPRRYPAPQVMSNGSPYLPEDCYDNEYVSHTDGSMISRREWYV
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MDINNIMEEVQAIKVLPHMMFNASKLKVLSDYVNVAFENNEYYDNDVMLTLLRLFCLYPHCYDKDIIKKILICVLYNINNVDMNMYMSLINSSLYDDNIKSVIYIYELIKNCQYKKLWNCINNNIGNEYNNCDYSYLKNDKNFICNIRKYILNTISISFESIYLKNMSEYLNIQDNTQLEQFLNENKWTIKMINHKGKDEQICYNGNIETVQNKKNINTYFTEDNIGSYITKLNH
The following text describes a protein:
Function:
Component of the outer dynein arm complex required for assembly of the outer dynein arm-docking complex (ODA-DC) and the outer dynein arm onto the doublet microtubule.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MPSADATRGGGSAGSMGKGTLGAGDTLGHKSVLDKQRAAIEKLRAQNEQLKTELLLENKFSVRPGDPFAQALINRLQDEGDMLARKIVLEMRKTKMLDQQLSEMGSTLTTTRNNMGGIFSAKEQSTAVQKRIKLLENRLEKAYVKYNQSITHNKQLRESINNLRRERIMFESIQSNLERELAKLKRDMADMIQQANGAFEAREKAIGEMNALKAQADKEQQGFEEEWRQLTTIIEEDKKERERARAQELAMRERETQELLKMGTLSSAEKKKRITKGSWNVGYNKAMAQNVAAEKVEMYGQAFKRIQDATGIEDIDQLVNTFLAAEDQNYTLFNYVNEVNQEIEKLEDQINIMRGEINKYRETGRELDMTKSRELTEEEARLAASEAQSQLYEKRTDSALSMTTALKAGINDLFERIGCNTPAVRDLLGEEGVTEANLTAYLGIIEQRTNEILQIYAKRKAQQGTDGLAEALLAQPLTQPGNRIIIEPPSTTQEEEVEGLEPEPVEEDRPLTREHLESKVQRTLPRKLETAIKVRPAGADATGGKRGSPTRR
The following text describes a protein:
Function:
Inhibits translesion DNA synthesis by preventing monoubiquitination of PCNA, this is necessary to counteract damage due to ultraviolet light-induced replication stress. SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage; Plays a role in pre-mRNA splicing by facilitating excision of relatively short introns featuring weak 3'-splice sites (ss) and high GC content. May recruit CACTIN to the spliceosome; Plays a role in ribosome biogenesis by enabling SNORD3- and SNORD118-dependent cleavage of the 47S rRNA precursor. Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAETAALVWLRGPGFGCKAVWCGSAPCSIRDFIRRHCEDQVVPVECFFVKCNGSLVNTSDTVQHGAVYSLEPRLRGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPRHCFSSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEIGESRKRPNKSKTDGGASAGKRKCFWMGMEGLGTTEGSSSENSDNDSEEAPGTSGMSFHVSQNGCDGVDMAAEIPSSSQQARVLNTDCRSPEKLQSPLTDSGNSISEDLHAELGETPTQEYMERKRAVETENTREKKEAEGREPLEKEAAGGGQNTEQETKETTDGERAAKGAPGEDRENIAVARLAASQSGNTDISQETLDLLAISSVAEMELLGLEKLKCELMARGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPSKGKKK
The following text describes a protein:
Function:
Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.
Sequence:
MKTEMLGYSVFNGSKEELLNIIDKYEKVNIISGNPEVLYNGLNNEELFKNFTDKDSIIIPDGVGVVLASKIIKSPVKEKIAGIEVMDSILKKCNENGKAVYLLGTTEDVLKECERKLLIKYKNLNIVGKHNGFFDMDSCKDILEAIRESRPYALFIAMGCPRQEKFISKYMNELPCKIYMGVGGSFDVFAGKVKRAPRWMINCNLEWLYRVAKEPYRIKRLASIPKFLLKVALNKRSY
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 (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MLAKAFAGSKSHKILINAWFTTLPGQCQKPIVQFVLSPILVSTNLTPSILSLPVQEKSSSSFVMAYRLVVAPEQIIEATVTLTTAQLHYLQRVLRLQKGDGFMVLDGGGGVWRAQLNDLAHGTAQLLETVSEQNELPLPVTLAIALPKGSGFEEIIRPCTELGATAFQPLLTERTLLKPSQNKLERWQRIVTEAAEQSERQWLPPVAAPLTFGQFVEKVAGPETLALLCVTRLNSPMLGAYLKQSNLPAQIVLATGPEGGWTDNEISLAIAKGFQPVSLGKRILRAVTAPTVALAQINALLES
The following text describes a protein:
Function:
Regulates mitochondrial small subunit maturation by controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor of the 15S rRNA in a position that is subsequently occupied by mS47 in the mature yeast mtSSU. Uses structure and sequence-specific RNA recognition, binding to a single-stranded region of the precursor and specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47 is coupled to the irreversible removal of precursor rRNA that is accompanied by conformational changes of the mitoribosomal proteins uS5m and mS26. These conformational changes signal completion of 5'-end rRNA processing through protection of the mature 5'-end of the 15S rRNA and stabilization of mS47. The removal of the 5' precursor together with the dissociation of Ccm1 may be catalyzed by the 5'-3' exoribonuclease Pet127. Involved in the specific removal of group I introns in mitochondrial encoded transcripts.
Subcellular Localization:
Mitochondrion.
Sequence:
MKCLSALRHVQCVRFMQVAAQVSKRISPVQNAQAAYQSLPPGTQSAMQNAREKADLGEEDLTLISQCNIRNSTVLRGAVLQYFKTFEQYGAVKKVAARLLMEPNGDFRGDLTLAETKLYLESLVELRQFADAVQAVEKMIRQSALRSPWQAHKLVCVLFTRLWAHIPPQEVLAYLASMLRALHGTCSFGPPWVNTDIVKLFFHFFRAFPEIESYQHQALSLIESQLDACAAAEFSSTLLQIHLVHRRFQLCEQVWKYKVQKKFPTTSADLTAIMEAYSHKGDWQGVVDLYESHSSVRNLSNHFELKLYAHARLHDWRNLKDSFNCLFGLGKLPSLEHYSVVMLALAHNGNTDLVEQLYLQLLRRGLTPTNAILRSMVLAGYKAGDLSRAVNNFELFKHNGIKPTSGDYLLLLRVYRRLGDLELSFKALRRLTQESYTLYDKHFACIIDTCAKTCSHGVASELFKLMEEHYGVTATGHSVSSLMRVYLSSMLPQKAVNLFKIYSNKPLDSKFLLYPVLLEAYLQLRNYKRFEETLKEFTSIEQSSYLNVCEVTIRYLAEHKHDTKAAEAVLDQFIKKNPSSIRANLFEPILKEYDRTQDTDASLALFKNMAELKVAMSTKTLLYLLKSTFKRSLKTHQDLNDYVEWSINILKRVRDKNIIMENSFLYPAVVAYPVKMLAKHHHPNTAVRLLTEYYEIFGKKIPRSDESIVVTKALMVVAGEAQNWQEFEEHYSNLMEKISKMKGPENKVQDNKRISNVLFGVLGYKMESMQATGKIQEIPSVLQEYEQMGLILTNSMWNKIIKTLVSDDKTIKLGIGFANENFIQGYSLRNANKLIQTSDEQFLSPFQKHIKERQKVNPKAFKPKKYLNYSTYCEIAKSLDEYLNRRCDQLDEEVAQLTNTYPRFMKRYLRRSRNVRNWRDFERRHNNFFEHLHMQNELLLQAL
The following text describes a protein:
Function:
Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Dispensable for growth and sporulation on solid acetate and oleate media, but is essential for these processes to occur on petroselineate.
Subcellular Localization:
Peroxisome.
Sequence:
MNTANTLDGKFVTEGSWRPDLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGMWHLGTYFGHELYPEALIKSMTSKL
The following text describes a protein:
Function:
N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Involved in biosynthesis of N-linked keratan sulfate proteoglycans in cornea, with an impact on proteoglycan fibril organization and corneal transparency. May play a role in the maintenance of tissue architecture by suppressing cellular motility and invasion.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MIYPCLNYSPLFYFFFRKCLPKESGGKIYNILQSIILVIILVVTIVLVQAAMQRNQDSVPKKHYQDTQKPSKSLASWQQSSFWMQYKNGSLIDKSIVQGWDVTNANCSANSNMVKYPWFSKVGERIQRFLLYRHCRYFPMIFNHPEKCGEDIYLLMVVKSVITQYKRREAIRRTWGQEKEIRGKKIRLLFLLGTDSKGEQQAHHQKLLEYEDRVFGDILQWDFEDSFYNLTLKEVGFLKWFSIYCQSVPYIFKGDDDVFVNTVNVVEFLESNKNTTDLITGDVLTTSAPNRDRNSKYFIPEVMFSETFYPPYVGGGGFLMGGPLAMRMYGASNELELFPIDDAFIGMCLRVLQVSPMHYSGIKTLGIKVKSGGNGMNKDPCLYRNLLLVHKLAPDELIQMWEQVNSNLICTQAKYIE
The following text describes a protein:
Function:
Not known. Seems to be able to provoque the non-Mendelian trait [PIN(+)] which is required for the de novo appearance of the [PSI(+)] prion.
Miscellaneous:
MISCELLANEOUS: Present with 996 molecules/cell in log phase SD medium.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MNVCKLKEIVPLFPRSSFTDGVVSTGKSFRSWDTCMDNKACKIIAIVGIVLACILVIWLIGGLLTCFRQGVTGIGQFICWCCRCSNDRNGNNTMPVNEGFSRVNMGVAPPSTVIYQPIQQPESAYYRNDAKNDTFYDEVKTPSNEVYELEEDFDLEKQKEKTRKKQQKERNKEGRSPSRVAPLVYEEENFEGSSPQPQYDARNSFIQNAANTGSNNAHVASQSPIFDISDYGENYYYDNNNINNNLQGNSYNTPSSNHRSPYPTENYQSYQGYKPNQSDRYY
The following text describes a protein:
Function:
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro.
Sequence:
MILHAQAKHGKPGLPWLVFLHGFSGDCHEWQEVGEAFADYSRLYVDLPGHGGSAAISVDGFDDVTDLLRKTLVSYNILDFWLVGYSLGGRVAMMAACQGLAGLCGVIVEGGHPGLQNAEQRAERQRSDRQWVQRFLTEPLTAVFADWYQQPVFASLNDDQRRELVALRSNNNGATLAAMLEATSLAVQPDLRANLSARTFAFYYLCGERDSKFRALAAELAADCHVIPRAGHNAHRENPAGVIASLAQILRF
The following text describes a protein:
Function:
Plays a role in DNA double-stranded break repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecR. Is recruited to repair centers, foci that are the site of double-strand break(s) after RecN and before RecF; may actively recruit RecF. A positive modulator of RecA.
Miscellaneous:
MISCELLANEOUS: The mutation previously known as recL16 is a mutation in this gene.
Subcellular Localization:
Cytoplasm, nucleoid. Note=Cytoplasmically located in untreated cells. Recruited to foci following treatment with DNA damaging agents; these foci are presumably the breaks themselves. They are almost always located within nucleoids. Another study found it localizes in tight foci on the nucleoid with active replication forks; targeted via the 6 C-terminal residues of SSB (ssbA).
Sequence:
MLTKCEGIVLRTNDYGETNKIVTLLTREHGKIGVMARGAKKPNSRLSAVSQPFLYGSFLMQKTSGLGTLQQGEMILSMRGIREDLFLTAYAAYVAELVDRGTEEKKPNPYLFEFILESLKQLNEGTDPDVITFIVQMKMLGVMGLYPELNHCVHCKSQDGTFHFSVRDNGFICHRCFEKDPYRIPIKPQTARLLRLFYYFDLSRLGNVSLKEETKAELKQVIDLYYEEYSGLYLKSKRFLDQMESMKHLMGENKS
The following text describes a protein:
Function:
Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Efficiently blocks type I IFN signaling following infection by behaving as a substrate receptor for CUL4-DDB1 E3 ligase complex and targeting host STAT1 for proteasomal degradation. Blocks the type I interferon signaling pathway by disrupting the RIG-I signaling pathway (By similarity).
Subcellular Localization:
Host cytoplasm.
Sequence:
MDPTDLSFSPDEINKLIETGLNTVEYFTSQQVTGTSSLGKNTIPPGVTGLLTNAAEAKIQESTNHQKGSVGGGAKPKKPRPKIAIVPADDKTVPGKPIPNPLLGLDSTPSTQTVLDLSGKTLPSGSYKGVKLAKFGKENLMTRFIEEPRENPIATSSPIDFKRGRDTGGFHRREYSIGWVGDEVKVTEWCNPSCSPITAAARRFECTCHQCPVTCSECERDT
The following text describes a protein:
Function:
Cilium-specific protein required for cilia structures. Axonemal dynein-associated protein that participates in a structural link between inner and outer row dyneins.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MCACMTKEALLEVCKQNGLYRTASLNDKLYCNFKGFSQIACLEDYVNLKALFLEGNVLETLEGLPPLADLKCLYVQQNCIWKISGLEAVPGLDTLNISNNQLTKLEGLACCPALRTLIATHNHLVTLDSVAHLAECKALQTLDLQNNELEDPGIVDILKQIPDLRCLYLKGNPVVSNIKNYRKVLVTSIPSLTYLDDRPVFDNERKIAQAWLEGGLEGERAMRNQLKEEEEERSRKNHEFMMQMRAAGWRERRKRMGLPDGDTDPALDDMSDGEYEFDEEPEELVEARQRLAAYTARPGEEEPAELASARQGLARDGKPIQEGAWGSGAAAESDSAIYLQSVKAAQAELDVVRQQQPRQLPTAQVLIEELDEPCGGKAPAADEGSTPPALSPMTSPSGSEGQGGEGVAAAKKGAASGAAEGISAAVDINDLD
The following text describes a protein:
Function:
Putative transporter for the divalent zinc and iron cations.
Subcellular Localization:
Cytoplasmic vesicle membrane; Multi-pass membrane protein.
Sequence:
MWLSTFLALLIFVECVIVVYIPAYIESKLSKIKKNRFFNMENFENIASGAILALAFLHMLPEVIILSNKKNMNLYYIFILVLVSVTFLNITDILYDHHFESTFDVNCTLACENSNNQIKNINDKEITTNYIDIKSNEVIDLELKAMDTNINNNNNNNNNNKTDPCKTNIFFEIFKSNSFFIVLSLFIHSFIEGLLMGSLKDKNAIIIVGLSMLAHKWAECLIVYKNVVNKIENPLLASIYAWSFILSLPLGVFIAIFSFPSNEFVEIIFSSIACGFFLYLSFNMTKEIKITKSNKHFISFSYFLGVGGMSTLMILFNSFESNNII