UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
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D6VTN7
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MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLKTLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND
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ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly. Increases frequency of mitochondrial genome loss. Present with 161 molecules/cell in log phase SD medium. Belongs to the YFH7 family.
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C5DXG0
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MLGCFFFFFIQYKVQVEIFVFKVHYLREDTPFPKMVVDVDALANEAIGLLDQCKDDNYRVCILIVGPPGSGKSTVAQDLSRQINHRFDEYRLQGNQKSAHGGTRSRASDVALASDVPEITTPLSEELAFNGGILPKYVEDVNFQPVKRRLENGDLQILGRGGLPNAFTISNDVEPDEESSFAQIVPMDGFHLSRQCLSSFQNPQEAHKRRGSPPTFDSNNFAQLCKTLAQTCTIKPGSCDAKSCFEFMAKTYDPHFPCIKIPGFDHSLKDPTPDQFCLNGHTRIVILEGLYLLYDKENWQRVHEILQNTGSLLVWYIDIEDHVIEERVAKRHFNSGLADSVEQGRLKFQGNDLLNARLIRKNLVQSGKVVTLRND
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ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly. Belongs to the YFH7 family.
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Q79EW1
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MKLRFGVTAAEKKAWIVFLVLLGLTAAVLIISAGLGQRFIPPWDVAKTFFGAGSKLDELMIMSFRMPRILTALCAGVCLAAAGAILQGLVRNPLASPDIIGITGGAAVAVVLLMMFFSDRSSSLTISLSWLPAAAFIGASAVGLIVYLLAYKNGASTFRLVLIGIGFSMSAQAMTTLLMIKGPIYRASQANVYITGSVYGSNWQHVKIAIILSVILLFICFVALKNMNIQVLGEDIAAGAGSAVQRNRFFLLLLSTALTGCAVSVAGTIGFVGLMAPHIARRLVGSSYGALLPASALIGALLVLTADIVGRTLFAPVEVPAGVFTAAIGAPYFIYLLYKTRNS
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Part of the ABC transporter complex YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen. The complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (YfiZ and YfhA) and a solute-binding protein (YfiY). Induced by iron starvation, repressed by fur. Strains lacking this gene show a reduction in growth stimulation by the iron-hydroxamate siderophores schizokinen and arthrobactin compared to wild-type. Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
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P21710
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RMAGRNRTEFYKLLSRHELDANDFKE
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Probable member of a two-component regulatory system YfhA/YfhK. Phosphorylated by YfhK.
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O31570
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MKEAEVLKYEAFTSSPGKGNPAGVVLQGDDYTEDEMQIIAERAGYSETSFIRKSESADLELRYFTPGHEMNLCGHATVASLYALCEKGMLESGKTYSIQTKAGILPVKISEKDGRIHITLEQASPQFKPFTGDRKKLADALGITDEDFHEDLPIVFGSTGIWTAIVPLKSLEASKKMVPDNKQFPEVLVDLPKASVHPFTFETVHPDSDLHGRHFSSPYSGTIEDPVTGTASGVMGAYMKHYGNAEQHKFIIEQGQEIGKDGKVEIEMNEAGGHVKVNMTGTAVYSETRILKI
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Belongs to the PhzF family.
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Q79EW0
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MPQTEQIHQHSVLRDIIRSRRSIRKFKQEPVPSAVILDMLETAKYAPNHRVTEPWRFIYVSSETGKANLINTFAAFSKKSKPDMTEEKLQNFKNTLGRVPGFLLVVFQEDENERARDDDFAATSSLIQNLQLLAWEKGIGMVWKSGKILYDKEVHQAFGLQDNERFAAIIQTGYPDEAPEVKKRTPIRDRFTEM
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Belongs to the nitroreductase family.
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P78886
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MTHTPSFDLSDIKSTLSTNVLHADDAYALENDVAPPIHISTTYTYPGTPDTLQPFTKLAEEDFPYYARISGNNVDRAEASLSSVLGAPSVVYSSGLAAIYGLLSYLNPKHIAVHKPGFGGYSGTIQIIARINRLTGLETSFIDGKCDAIGEGDVIWLETPLNPLGIAFDIPFYKELAKKKGAILVVDSTFAPPPIQDALVLGADYVVHSATKYLAGHSDVLAGVTASKDRSKILDLKADRAYLGTILHPQQAFLLLRSLRTFPLRIAKHSENGFLVAQHLNKLATDEQFATSLGIDSSLILEVYHNSLQTKEFVAKNLTGGHASCFSVLLKSDTVAKHLCCELKYFHHATSLGSVESLIEWRRMTDSKIDPRLVRLSIGIEDAADLIADLNRVFASLS
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Belongs to the trans-sulfuration enzymes family.
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A0A1S0T081
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MLFAYSGCLAPQCIPDISSFKALPFRDTESRFTTDSSVISSRFSSSFTSSSSKIIIITSIFSSKMDNEHVGASLIVSLSMASLILTNVFSFSSTSYSSQPSDYIACSPSGIDDQPVAEPSGYTPVGSSSPHSGCITSGLDAIGYQSSLNEGQSTNASSRFVTKVYSHSALTHIILHLLSILQKFYLQVSTIS
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Present with 300 molecules/cell in log phase SD medium.
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P43624
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MMVDPLYKGGLTKPLCSSGLRPITDSCVVIPNFDNSVRSIIVVNILVFAGILYSQFRNTLSIFSLWCPNTRAVFLFICPCLLYFYQGIFSTDEQIGTFNIIWMLRRLTIELIIRNLNAEKER
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Silenced by SIR3. Partially overlaps YFR055W. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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Q9UTE4
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MSSASMFGSLKTNAVDESQLKARIGVLALQGAFIEHINIMNSIDGVISFPVKTAKDCENIDGLIIPGGESTTIGKLINIDEKLRDRLEHLVDQGLPIWGTCAGMILLSKKSRGGKFPDPYLLRAMDIEVTRNYFGPQTMSFTTDITVTESMQFEATEPLHSFSATFIRAPVASTILSDDINVLATIVHEGNKEIVAVEQGPFLGTSFHPELTADNRWHEWWVKERVLPLKEKKD
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H2O + L-glutamine = L-glutamate + NH4(+) Belongs to the glutaminase PdxT/SNO family.
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Q79ET3
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MRTYSNKLIAIMSVLLLACLIVSGCSSSQNNNGSGKSESKDSRVIHDEEGKTTVSGTPKRVVVLELSFLDAVHNLGITPVGIADDNKKDMIKKLVGSSIDYTSVGTRSEPNLEVISSLKPDLIIADAERHKNIYKQLKKIAPTIELKSREATYDETIDSFTTIAKALNKEDEGKEKLAEHKKVINDLKAELPKDENRNIVLGVARADSFQLHTSSSYDGEIFKMLGFTHAVKSDNAYQEVSLEQLSKIDPDILFISANEGKTIVDEWKTNPLWKNLKAVKNGQVYDADRDTWTRFRGIKSSETSAKDVLKKVYNK
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Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Binds citrate-dependent Fe(3+) and delivers it to the surface of YfmDE (Probable). The complex is composed of one ATP-binding protein (YfmF), two transmembrane proteins (YfmD and YfmE) and a solute-binding protein (YfmC). Transcriptionally regulated by fur. Belongs to the bacterial solute-binding protein 8 family.
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Q79ET2
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MYHSAKRRSSSRLMMFIIALIIFIFGLGLNLSVGASDISIIDSLKYLFVWDGSKEQLIISTLRLPRTLIGVFVGASLAVAGALMQAMTRNPLASPQIFGVNAGASLFVVASLVILPASPYSSVIFAFAGAAAGGAIVYMIASSGGMTPVKLALSGMAVHLFLSSMTQAIIILNESGEDVLYWMTGAIDGSNWQDVITIAPFSVIGIGLALVFSGSVSVLGLGDETAKGLGQNMNGIRILISLIILILSGASVAVAGPIGFVGLLVPHIVRKLIGEHYQYVLPFSALFGAILLVYADVLARWIAFPYESPVGIVTAIIGTPFFLYLARKGRNLK
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Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Involved in the translocation of the substrate across the membrane (Probable). The complex is composed of one ATP-binding protein (YfmF), two transmembrane proteins (YfmD and YfmE) and a solute-binding protein (YfmC). Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
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Q9UTE1
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MSNTGSARTEEFTKGTGYEATKPNNDTDDDAKQNYPSKEPHMKLGDYTEETSFVDDSIFKREELTPDRNSPANDVEKMEVPKPTPQWMKLKDEGKLGKHRKNRLRRPGRFPVRQESTIDIPGLTVSKRTENDSNNASYGIREKLIIILVGIPATGKSYIGSKLSRYYNWLKYNCRFFSVGDKRREEGASTYSMSADFFDIKNEETFKFRENVALETLEDLLHWMIHENGVIGILDATNSTHERRKHLYDRISKEADIGIMFLESLCTDDILFEENIKLKIKGPDYEGYDTESALKDLRERVDLYKKYYEPLDERDEQLPFLQYVKVINVGIKVVTHNIEGFLAGQAVYFMLNLNIQKRQIWLTRPGESLDTVAGRIGGDASLTPIGKQYAQDLANFMDRQRVLWQLRYTNDLASTNKRFSLSEASSFNVWSSVRKRAIETIEFFNPDSYNVKKIRLLNDLNLGSREGLTLREFSEKYPDEFDVIKRKDYAYRFSGQGGESYLDVIHRLQPLIVEIERSSGNILVVSHRIVSNILMTYFLNYHPEDIIDVGLPLHTLFCIESDRYGTTCMAYRYDAANRQFIKDPMFDLRKRT
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Synthesis of fructose 2,6-bisphosphate. ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+)
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Q79ET1
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MKKTTRKQKRPLLAILILAVILIVLSVISIGIGALYISPDAVVTNLLGLDHSFEFIIQQYRLPRIILAILAGAGLAAAGAILQGVIRNPLASPDVVGISKGSGLAAMAVILIFPESPVYVLPFSAFAGAAIIAVLLLMIARKKSIQPSSLALSGIALGAVCHAGMQYMMVKFPGDVNAALIWLTGSLWGRNWEEVKLLAPWLLILFPIVCILIPKLDLMSLGDELAQGLGENANRLRFILIFTAVALAGSCVAVVGSIGFIGLLAPHIARRLTGEKAKYLLPASALIGAIILLIADTLGRGIMPPVEIPAGILTAVIGAPYFLYLLKFEARKQ
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Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Involved in the translocation of the substrate across the membrane (Probable). The complex is composed of one ATP-binding protein (YfmF), two transmembrane proteins (YfmD and YfmE) and a solute-binding protein (YfmC). Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
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Q79ET0
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MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECCIMRSPIDQKPMCLPTGLCPKLRAK
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Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Responsible for energy coupling to the transport system (Probable). The complex is composed of one ATP-binding protein (YfmF), two transmembrane proteins (YfmD and YfmE) and a solute-binding protein (YfmC). Belongs to the ABC transporter superfamily.
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Q79ES8
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MSKGYYSILFSQTTTNLGFSLYTMVVISFLFKMTNSTTIASMVTLISIIFRIFGSAILPLITIRLKLPLTIIISQLIQMLLLICLFYALLRTYSNQTLILVFIIISCISFFNGWFSPLKSAIIGEIISPDRRVKANGLLSTVDQTFQFVGWSLGGLIIAFLGEGYTIILTIFLLFTSLLSLLFCLPHGHANSVIREKNSPNKSIVSGWRYLFSQKKLRTIIIMDLIESWAGMIWIGSVSLAFVNEVLHKGESWWGFINGAYYLGSMIGGFIIYKLSERFQNKLINFMLIGAVSYGSLTLIYGFISNSYLALILVLFMGPAYILRDLTQETLIQNITTEQTRINIMSARSSLVQFIFMFSILAIGAISDFLGVRLVYVSAGILLLVSAIYGFSQLQFKKKVNKHISF
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Belongs to the major facilitator superfamily.
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Q79ES7
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MTASQQQIQLARRPQGIPVHEDFRFETIPVPEPKQGEVLVKTLYVSVDPYMRGRMQDTKSYVEPFALDKALSGGVIAEVVSDGNHLKKGDIVIGNLSWQEFSAVSESALRKIDTSLAPASAYLGILGMTGLTAYFGLLDIGRPKEGETVVVSGAAGAVGSTVGQIAKIKGARVVGIAGSDEKIDYLKQELQFDEAINYKTADDIQKALQNACPDGVDVYFDNVGGPISDAVMNLLNEFARIPVCGAISSYNAESEADDMGPRVQSKLIKTKSLMQGFIVSDYSDRFSEGAKQLAEWLKAGKLHYEETITEGFENIPDAFLGLFKGENKGKQLIKVSDPS
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Putative quinone oxidoreductase that may contribute to the degradation of aromatic compounds. induced by stress due to exposure to 2-methylhydroquinone (2-MHQ). Belongs to the NADP-dependent oxidoreductase L4BD family.
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Q79ES6
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MASIDRFQVMQEPELKILEHWFENEDTRRRMDGMLLLDEWYARVNKDKHDTVIMAYDGQLPAGMVVIEFGEERTYIGLIVNPLYRLKGYGKQILQKLMTEPDFTSVREWVACIEEDNRISLACFQAAGFTLEDTEPDEDGFLTLILRN
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Belongs to the acetyltransferase family.
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Q79ES5
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MTQTWPFLHNAQSFIQENWNASGFQKPTPVQEQAAQLIMDGKDVIAESPTGTGKTLAYALPVLERIKPEQKHPQAVILAPSRELVMQIFQVIQDWKAGSELRAASLIGGANVKKQVEKLKKHPHIIVGTPGRVFELIKAKKLKMHEVKTIVLDETDQLVLPEHRETMKQIIKTTLRDRQLLCFSATLKKETEDVLRELAQEPEVLKVQRSKAEAGKVKHQYLICDQRDKVKLLQKLSRLEGMQALVFVRDIGNLSVYAEKLAYHHVELGVLHSEAKKMERAKIIATFEDGEFPLLLATDIAARGLDIENLPYVIHADIPDEDGYVHRSGRTGRAGKEGNVLSLVTKLEESKLKKMAKKLGVELSEAVYAGGKLKTK
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A probable DEAD-box RNA helicase that plays a role in ribosomal 50S subunit assembly. May be a non-specific RNA helicase. ATP + H2O = ADP + H(+) + phosphate In rich medium highest expression in exponential growth, expression decreases in stationary phase (at protein level). No visible effect at 37 degrees Celsius, decreased growth at 16 degrees Celsius. A quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) is not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes are decreased, while growth stops at 16 degrees. Belongs to the DEAD box helicase family.
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Q79ES4
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MSILSVKDLSHGFGDRAIFNNVSFRLLKGEHVGLIGANGEGKSTFMNIITGKLEPDEGKVEWSKNVRVGYLDQHTVLEKGKSIRDVLKDAFHYLFAMEEEMNEIYNKMGEADPDELEKLLEEVGVIQDALTNNDFYVIDSKVEEIARGLGLSDIGLERDVTDLSGGQRTKVLLAKLLLEKPEILLLDEPTNYLDEQHIEWLKRYLQEYENAFILISHDIPFLNSVINLIYHVENQELTRYVGDYHQFMEVYEVKKQQLEAAYKKQQQEVAELKDFVARNKARVSTRNMAMSRQKKLDKMDMIELAAEKPKPEFHFKPARTSGKLIFETKDLVIGYDSPLSRPLNLRMERGQKIALYGANGIGKTTLLKSLLGEIQPLEGSVERGEHIYTGYFEQEVKETNNNTCIEEVWSEFPSYTQYEIRAALAKCGLTTKHIESRVSVLSGGEKAKVRLCKLINSETNLLVLDEPTNHLDADAKEELKRALKEYKGSILLISHEPDFYMDIATETWNCESWTTKVL
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Belongs to the ABC transporter superfamily.
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O06473
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MDKTTQVNQKTGLLSQPKAVWAVAFACVISFMGIGLVDPILPAIAAQLHASPSEVSLLFTSYLLVTGFMMFFSGAISSRIGAKWTLILGLIFIIVFAGLGGSSSSIAQLVGYRGGWGLGNALFISTALAVIVGVSVGGSAQAIILYEAALGLGISVGPLAGGELGSISWRAPFFGVSVLMFIALIAISFMLPKLPKPAKRVGVFDAMKALKYKGLLTMAVSAFLYNFGFFILLAYSPFVLDLDEHGLGYVFFGWGLLLAITSVFTAPLVHKALGTVRSLVVLFIAFAAILVIMGIWTDHQTLIITCIVVAGAVLGMVNTIMTTAVMGSAPVERSIASSAYSSVRFIGGALAPWIAGMLSEHFTASTPYTVGGIVVFVGMLVLLMGRKHLAGIKAGH
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Acts to efflux copper or a copper complex. It is possible that YfmO could contribute to copper resistance. Repressed by YfmP. Cotranscribed with yfmP. Belongs to the major facilitator superfamily.
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O06474
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MEWMKIDQVAKRSGLTKRTIRFYEEIGLIPAPKRTDGGVRLYSEDDMEELEKVISTKEVLGFSLQELQHFMETSRQLELNKEGYLLSLDPKERKEKLEEIQETLNHQLDLIDEKIRTFQSFKERLQGMKGKAERAIQSIE
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Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. YfmP is autoregulated. There is no induction with copper or other metals. Binds a DNA inverted repeat of the yfmPO operon.
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P0C5N2
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MELVSLCNTITIISHSVLYVSLSYYIINPCTSASSNFDDSFS
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Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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Q8TGP1
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MFMTSSCKPGNKVSMIWNSLTGKECKKISSMVVILPALTNLPSLVTGTHPFSSVFLGPLLFGRPLLRPPKPPLFCC
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Completely overlaps RPS2. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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D6VUH7
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MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY
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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). Homotrimer. The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). Ty1-GR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4. The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Produced by conventional translation.
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D6VUH6
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MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPGINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endonucleolytic cleavage to 5'-phosphomonoester. The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity). The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR038C-A ORF.
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D6VUU4
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MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSYASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNSNKRIIAKLKMQYDTKIINLGESDDEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPNGRKLGAPGQPGLYINQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endonucleolytic cleavage to 5'-phosphomonoester. The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity). The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift between the codons for Leu-435 and Gly-436. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR161C-C ORF.
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P53205
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MLGPSCFPMISCMNTEEISLLSNNLFTMIFPLRKCGFSSDVECQFNIFFQTLSSVTSKSIIYTLIKVNRSSRSWIAKSEFITTLILQQFKFTTFLFKVHRKKVPGCTI
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Partially overlaps NMA2. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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O94694
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MKLHTFLLLSVLCFAGCIQQSLQAEVYGKVLTNTILPKINLLSYDTRARLISSNKTFETVVERDGSFTFPNVPDEIYFLRLESIDYEFSEFHIIINESIVYPYYTSPAEKRPASSTAKNTSYPIKVRAVLKRDYLKEPRKFSLIRLLKSPMMLLSLASVVLVFILPKLNIEAKALEQARLAEAAEKKTA
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Belongs to the UPF0620 family.
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D6VUF2
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MSRLRRFNRKILSLSSDYTHDGESDQEDVSILPLDTEEQEELIQKFETNAHITNKLYINLLSILYLLYGGLLMILVRKSRGYIKLALLAGANSLICSCITLRYDIVNDYLLFKKFKLRVSNFSINIINIILLVLMAWISFNHVVEDKKTVLCLQVPMFLFWVAVLVKRWARNIEDEIADLRCLKYKYKNA
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Present with 238 molecules/cell in log phase SD medium.
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O94695
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MVLRERLSHILFHEKVGFLLLCLLWYISSAVTNTTSKSIFNELRCPVTLTFLQFGFVAFFSAVCLLFRKQFLGGTGIQKPSKYVLYTTLPLSIFQIGGHVFGSLATTKIPVSTVHTVKALSPLFTVLAYRFMFRHVYSAMTYFSLVPLTFGVTLACSFELSADIVGLLYALISTCIFVSQNIFGSKIFMEAKSHSTHTKKHYNKLNLLLYSSGVAFIVMIPVWLYQEGFAYLPEVGSPVFLNLIYNGLSHFFQNILAFTLLSIISPVAYSIASLIKRIFVIVVSIIWFQQATNFTQGSGIFLTAIGLWLYDRSKKGNLYESCKVKEFEKDALELEEQTMEDEKSYPSSGTQSPFYGKNFLPQITPRLDSVVPLISDSPMTPNSVYSNEGVTSSVSGNATPASVRQSTQNDFSNSNIHDRRSSYTFQLNNFKAPQPSRLWATETVPTLKI
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Belongs to the TPT transporter family.
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D6VUF3
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MSHQMAPWIPMFIQSCKNNTEPFVSFQFATVDELTNKPRCRTVVFRDFLFHDKRTNVLTFNTDMRSSKITESFITPNSNNSSDSKRCETPFFEACFYFPETWEQYRFSGQCFTISKQFKKIPAEIVTKYDIFSPRFSETNDDSTDEEIDTPINDDDDDDKNNDADNNDINEDNKLIESIENDEHHEDEDDYYPQPQEWEAELLRQWSSLSRHTKSLYRKPAPGQKLTSETSKQLDKLHRGVDGAKEDAGLENFGIVCLCVDSVDFLNLKEGRGGERWIFQKTDGKDEDLWEEQEVCP
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Present with 2840 molecules/cell in log phase SD medium. To S.pombe SpBC725.03.
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Q1L853
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MSKIEKKQASASNLLLGAGLNLFETSSLGQPLEVTKVQMAANRTQTMAQAIKAIMSRGGILGFYQGLIPWAWIEASTKGAVLLFTSAELEYWGRRLGLGATSAGAIAGMGGGVAQAYATMGFCTCMKTAEVTRAKQAATGQEVKGTFRVFADLYKEKGIRGINRGVNAVALRQMTNWGSRLALSRFLEKPIRYFTGRTEAEPLTTGQRFVASVSAGALSCWNQPLEVARVEMQSLTKGIQHSSPGIMQTIMSIYKNNGIKGLYRGAVPRMGLGAYQTFVMVFLADCVRGYLAK
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Belongs to the mitochondrial carrier (TC 2.A.29) family.
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D6VUF6
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MLVRNRYLGELLKNSRSFSVLNSSVRSGHNKWSTIKHGKAKNDAERNKINNKFANQIAMSVKLGNGITDPSMNIRLATSIELANKNNVSKKVIENAIRKASGSSASGKDSNASELCVYEGMGPGGVAIVVEALTDNKNRTIGLIRSAFNKANGSMTPTLFFFDKKGYVTMVPPKMLDTEDKVLESVLEIQGIEDIAPVQEDAEDLECDTETETTGQTYEAVMEPADTNKVAALLKERGFHIRDLGIGYNAKPDMEVFVQGDETLEKLQKLTTALEDIDEVTSLYTNASNA
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Present with 1780 molecules/cell in log phase SD medium. Belongs to the TACO1 family.
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Q2M9P0
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MNAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family. Extended N-terminus.
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B7N7K6
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MSAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family.
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B6I789
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MSAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family.
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B1LDG2
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MSAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family.
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B7LPS0
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MSAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family.
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B5F5M7
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLIKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEITALTE
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Belongs to the UPF0235 family.
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A9MQS2
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MSAVTRCEDGLVLRLYIQPKASRDCIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVAIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B5FUW5
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B5QY78
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B5RE62
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B4THI7
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLIKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEITALTE
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Belongs to the UPF0235 family.
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B4T5K9
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLIKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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Q5PML0
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLIKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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A9N4P8
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B5BFQ9
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLIKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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B4TV71
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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Q8Z3U7
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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Q8ZM46
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MSAVTRCEDGLVLRLYIQPKASRDSIVGLHGDEVKIAITAPPVDGQANSHLTKFLGKQFRVAKSQIVIEKGELGRHKQVKIIHPQQIPPEIAALTE
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Belongs to the UPF0235 family.
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Q83JS1
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MSAVTVNDDGLVLRLYIQPKASRDSIVGLHGDEVKVAITAPPVDGQANSHLVKFLGKQFRVAKSQVVIEKGELGRHKQIKIINPQQIPPEIAALIN
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Belongs to the UPF0235 family.
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Q22836
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MSMKLRDILPAPVAADEAASQIRRDPWFGGRDNEPSAALVSKEPPPYGKRTSFRPRGPEDFGDGGAFPEIHVAQFPLGLGLGDMRGKPENTLALQYGTDGKLQHDAIARIGHVKDKVVYSKLNDMKAKTWNEDDDDIQKPDDDAVIDATEKTRMALEKIVNSKVASALPVRHADKLAPAQYIRYTPSQQNGAAGSQQRIIRMVEEQKDPMEPPKFKINQKIPRAPPSPPAPVMHSPPRKMTAKDQNDWKIPPCISNWKNPKGFTVGLDKRLAADGRGLQQTHINENFAKLADALYIADRKAREEVETRAQLERRVAQNKKSEQEAKMAEAAAKARQERSAMRRKDDEDDEQVKVREEIRRDRLDDIRKERNIARSRPDKADKLRKERERDISEKIVLGLPDTNQKRTGEPQFDQRLFDKTQGLDSGAMDDDTYNPYDAAWRGGDSVQQHVYRPSKNLDNDVYGGDLDKIIEQKNRFVADKGFSGAEGSSRGSGPVQFEKDQDVFGLSSLFEHTKEKKRGGDGGDSRGESKRSRRD
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Belongs to the SNW family.
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O94386
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MEIHGKNFLETLKELEKHVDSAHYVSIDCEFSGLLRDFNLNNKNTLQDRYELLRKSSIRYTILQIGITFIYLQNNGKSSCIPVNINVSPLVKDELHLKRDFCSEASSIKFLIQQGFDFNKQLTEGVPYLSRIEERNLIDKVNERSTDDLTSSILDACDEEILVDARNQIKNWLSSELSHSTSKYLNITTSNRFIRKAIQSLVKIEFPTLKSYPKRTFLQVRKAIENSTTQCSATSKSELKEDIASDQLILNNLNLIKQNVGLRHLWDYILKKKKSVVCHNGMADLVYLFSLFEGKVPETILEFSELCLSSFKSIYDTKLLYLKSDDLQHVSDGIPTDLLSLVSKISLPPVPSNSSSQRSNVSLNSLIECPYKSMMSRKRPHEAGKDSYDTALLFVYYVMRTKHSDIQRWQNVLPIHGSFLDLNKYCS
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Belongs to the CAF1 family.
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O94387
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MENDEAFDRLIRKIQENQKHPSFEGSNKVLHLALSYLNTNRQNPHWVCDPKLQVAVRECLFLFSFQNDNEYLVWFKKHLNERLQLCPKCIVKYHQSLDDFKSLCLNIFHFDPNTLEIVMEKIYSWDIFRLQEVLKTVPKIDTSSASKPILCAFYEILYSPRILHNKEIFPLFRNRFLESGFLRLSKNLVPGVISLLFSRDDELRRWACSILSDVKTISDNEFKILEGPLLQEIRSLDQKKENENEMQIFLKGLSLLLKHVDHLYFRGLTGKNFNVADFILSGLQSDHTNLCPSFLVCLHSLLYCYGRNFWTPEISPSEVIDKIFNGNAYKRWTEENTSNFSNDQKAENPFEWATSLLKTISIIDEVELINKILINYTMQYKKELEVGFKNVQLLQSLADIFSVLFSEYFMIFPHSDQSLQNKVFELHSTLAIKFDELFRLLNLENEESVEWRLIKKVFEYRLNLDLYILKQFYCHYLDRNRKPPLNIKSVSESFKNFWVYLQNVFREEKFFMVRIVFRACSTVCLIDKLPPKKVDIPFKSDFENALNGFVATFSEMLIQTQCWHLSAQTQLVSNPLTFRGIFSLVFSPILEISTGSISIIKSISLSDSVVDTIGELLRSQFSNTLNSSCYVLLQWLKVRNFGGAKHIVYFNKLIINTIFDSVDGLTSKDATFAKQVEKKESLKNFWESLWKFFTHFFIVLPTWPVHDKDNLVDLMRDTLDFCDMLINIFEEVNGFIFGLSDNDIKIVSANDKGSALAMCIADSLVTVSYWLKLTDSSLLTSVVKVICKMLKICKKLECPISQNVIDIIHRASITSDEQTILTFTEREDLFISLTPYLSEDVLNHSPFNDTNTLETKLQSDDRGLLSKDQTIGIAKKLPESNISTSNHFLLPPKAISASKAINRNAQKSQNLNFLKSKQETTQRIRESAKVPRTSAGNHLSEKLNSDNHIPKALQKLDSADPIRKPSLLHTSKSYSNPDDKNTSTSDEDTSESEEESSNGLFSLAREANSHASKSLPQRRQIQFLDFDSLKTKNVVHPTQLRRNTQQSAQLARLRLNPDVQEFYKVILGWNPLADSFSASNVEMQCVQAKFTYNDSNAYEKVFKPMLFHECWAQVKSAVEEKQYPPIDLILNTRSTVDNFVDIYFTSCSPTEVSFLSDTDICLLSKSQSSGDTNNPKSFQLCKIQSISRKKESLELCLRMNIESIDLQEYAPNIRFTAQKLFNATTSLREFAALKSLRHLPLSQRILDANVTRLPSNFTDDKKQKIMKSYGVNEPQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQGLQFNVPGQTRKTSKNKILICAPSNAAIDEILLRIKAGVYDHEGIKFFPKVIRVGFGDSISVHAKEFTLEEQMIKQMELTNLKKDQEANNSSDTRKKYDSIIKKRDSLREDLEKFRSTGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLLNAGLTFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMSAVTSRPWHEDPQLGIYRFFNVHGTEAFSNSKSLYNVEEASFILLLYERLIQCYLNIDFEGKIGVVTPYRSQVQQLRSQFQRKYGSIIFKHLDIHTVDGFQGQEKDIIIFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSKPLMQEDIFYSLIEDAKTRGVWRDLSANQFKNSKSISNVSTHLASNNLNLASRDTPIKSPSVGICEEKQEAHKVKKRHNIDSANLSRGTERDEDIPNKRAKNKVSTDQTAADNKVTKPRLDESSSSKQDVLNKIDESEIEQASSKKPGYVEKNKDKGHMKKSKKPKSKLALAAMAHGFAPPKVEHFKRK
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Belongs to the DNA2/NAM7 helicase family.
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P53103
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MFFSSYYDKGNLKKNSCLAIISASSSQPKPLLTKARSNIFLALKILNNEPNLPSFLLFYASKKSKITAQITKLHIKGDLPSHRYSLRYRLNGGNFMCSIINIQQWYV
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Partially overlaps MND1. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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D6VTW9
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MCDSPATTGKPTILFIADPCETSATLNSKAFKEKFRILRYQLDTKEAFLNFLERHEQDKICAIYAGFPAFKKIGGMTRSIIEHKSFPRKNLKCIVLCSRGYDGWDLDTLRKHEIRLYNYQDDENEKLIDDLKLHQVGNDVADCALWHILEGFRKFSYYQKLSRETGNTLTARAKAAEKSGFAFGHELGNMFAESPRGKKCLILGLGSIGKQVAYKLQYGLGMEIHYCKRSEDCTMSQNESWKFHLLDETIYAKLYQFHAIVVTLPGTPQTEHLINRKFLEHCNPGLILVNLGRGKILDLRAVSDALVTGRINHLGLDVFNKEPEIDEKIRSSDRLTSITPHLGSATKDVFEQSCELALTRILRVVSGEAASDEHFSRVV
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Present with 1430 molecules/cell in log phase SD medium. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
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P53098
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MKSQKIHNQKDREKVEIYFYLKILINISTIHVITDYYFYLCQRWLARGCCEVTSKRF
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Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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O43062
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MNFFKRLRLHTRLLLRSKFVLISLILLLNLGLLLGIQIYRDPAFPGSLISSAAYEFGLHKHGPYYNDNVDDLKRYTFMGLLTLPTSEHDVYFNATRVLVYKLKHHPETKSKYPVHVLVMKGVDEWKIERLRLDGAEIIMVDQIKTEDLIESGLSIGMGSYRYQYMFTKLSVFEQTQFDKVCILDSDLLVLKNMDDIFDTPYVYESPAEPDMFSFPIFKKPDDEEDYQFSDNFDAYGAPRSEFYPYLLGACDDRNPGHATPPEESETFNAGLMLVHPSSLHMHRIKKIARYPYMYDDARMMEQSLLNLAYNKYGWFPWTRLDFSYNGVWVTEEDLPYLRAAHGKFWEYDNTEFPQILTAEWHKAFGELLAFHDYVVE
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To S.pombe SpAC5H10.12c.
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O43033
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MGILKKTIFIGGIYGLGVYIGAVAWRLRKDVLNYESRQKSDLLIPNSNSISIYNQIADKYSRKITREEIFSGIYFLRYFLLRNAKGDVLEVGSGPGTNFPFYKWKKINTLTLVEPAEKMREIADARAKKKVPPNVLYRQFADLRQLPPNQSYDTIIQTFCICSQEKAVEQLNNYRSLLRSDGRILLIEHGKGKYKFLNRILNAYAESHYESWGCVWNRDIEQLLEDSELTIDSCKRFNFGTTYVIEAH
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Probable methyltransferase. Belongs to the methyltransferase superfamily. METL family.
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P53092
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MEMYEISDTLWCGLVSLRCNAITSKMNQLDTNRLENSDRACDTNREYNMINARGAHRSQLAEMSLSAAPIPSSEGLKNEGKCGYTTCFSLELISTTSRFSVCSTVSSSVPLLPEFCIVPPMLSATPPEAAKGASGSMKSGSIVVSSLPYDILPALL
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Product of a dubious gene prediction. Almost completely overlaps YIP4. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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O43021
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MSETSEQMEETVQSGNEPISKSTWMGFIKNLATFTGDLSTLSAPSFILSGTSLLEYMSYWFEFPELFVTIVDFPTPKERMLAVLKWYITGLSREYASRNKNYGTEKKPLNPILGELFYGSWDSSKGKVELTAEQVSHHGPESAAHVVCKEAGITVDTHNKYRSGFSGRTVYVNQLGQLRVHLEKYNETYYITLPNISLEGLWFMAPYIELYGSTYIVSNTNYITKIDYSGRGYFRGTKNSFKATIFEKNEDPDYIVEGVWTGESKLTIPSLKSTIFFLSIPSLEATPITVKPESEMGDWESRNVWKEVSAALASGNYDIVSSKKSTIEQSQRDMRKKEEAEGAVWARRYFKWEEHDSDARNALAQAVLEVIEPGFWIYIGDTHPSLPAGEQPVKRME
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Belongs to the OSBP family.
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O43022
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MVIEKRESFIEVVINSLLNDNPAQAKFDKYSILVSLGFSSLLSVILLCIFTLLRTKFNTYDRCIPPMKKSLWGWIEPLWSIKVEDCLYNMGADAVISLLFSRFCRDVFLILAAICCTILIPINIVATNKTLANSDSQNAYAKLSIQNVTGNWTWAHVVICYVFNVLVLFLLARYYQIVMRIRQRYYRSPTYQQSMSSRSLLIMDIPTTMRSNNGLSILASRLKSSEAPMHVHICHAIKNLPKILKKHDNAVRSLEAVLAKFFKNPKKLPDDRPVRRVKQGLLTSEKVDAIDYYSAKIENYGLRVDAARESLYENEFEHYGFITYKSSYIAHDTARHNSRVAGASVSMAPEPSDFLWDNLSLAWSTRLFNRMIGNILFIILIIAWIIETALVAIFISNLYHLGSVWPWLQQQLTSRSGFWSIVQGILSPAVAGFTFMILEIIMRRISYWQGSFTKSSRERGVLNKLHIIFTLDNFIIYTLMAVFWRLGVIIAYKTKEEGNFAEGMSAFATFDTVGLSVSSFVQFSTFWIMFIAHSTCSFFVEIAQPITLTIRLIKTKFFSPTPRDLLEWTAPTKYVYSQVLNKLIYFFTIAICYACINPLVLLFASVLFCVNYLTQKYILMYVSNSSTESGGGYWRPVVNRILLGLELANIILFLCLWVQGGRVRAYCIIPNFSFAIAFKIWCMFALDPKSHYMIEDPYMKVVEPLENEISESEMCFGHPSTYAPLLVPMVRSDARALLPLFYSGRTETHNKFDFATDSDDASEKHLRGEEEPLENVDFVDIDNVDTAKEVHDQQQVQQLKKNLSRSYTRSRGVSLRARLNEEELPLTESITQDSQISIPETLESQSTEITPINVSEHYDKYYHIF
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Acts as an osmosensitive calcium-permeable cation channel. Localizes to the cell tip and the barrier septum. Belongs to the CSC1 (TC 1.A.17) family.
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O43023
|
MTDEKHVYVPPPKDPPSYEEVALHSALNNSAPPNDGEQNETSMEEMEIIEPPSEDSSRFPLLRTKLAAIHEGWESACHSFEIRFASTFHRIPFQFLYLAVIATVIILASYYGYFDGVPAWRSVHHYGEDVLLNYIKGCDISDTRQQVMTLSSIPHLAGTVGDSSLLQMIMNRLYYEKGTIVDFREFYAYLNFPQLVSLSIDGDDSFHPSLIESYQVGGYDGVSIPTPATFGGSPSGFVNAPLVYANRGRIEDFEWLVNSGIYVESSIVLVRANQSDFALATANAEKYNASAILIFEDTYLTSLDNLNQVYPAGPYPSANSLYRGSVANHYYYVGDPLTPGWSAHEETNRISPKDANVLPSIVSIPITFNDGIELLKRLQGHGHLVKDSNWCQDLAPVLSEVWTGSKISSPGLEVNVLQDIEDKQKIINIMAQIDGYESDQILVVGAPRDSWCTGASDSSVGTSLLIDVISTFANMAQDLSWKPRRTIVFASWDARQFNAIGSTEFLEYWKESLEAKAVAYINVDVAVSGDTFTARTVPGLKKVIQRAFDVANEEDEMKAANIITDDFDYTSDLTSFLTFAGIPVVNLAFERNEENPTPMPFLGSCEDTVSWIDTFGSEYWENAARLGKIWSYLILFLANDPVVPYDLEDEINGVGEMLKRIPEIPGANALDLRKINEEFSELLESLIRFEDEIREWKSLMMHNSYTVSVKKHPELEGYNAKLARFERSFLDEAGLPGHEWYKHLIYGPNLRNSHSQLFPSIFDALLYGDVEAAQKEVKRIALALDRAHNEIRFA
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Belongs to the peptidase M28 family. M28B subfamily. Although related to the peptidase M28 family, it lacks the conserved zinc-binding and active sites and therefore has probably lost hydrolase activity.
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O13653
|
MTLLDSSIFRFRLSSLHVSSRSLGVYFAGIMFASAVWVFVDAALYSAFDYARNLHITFIDWIPFLCSILGIVIVNSIDKSRLSGDSFAYTDESLARKARFILFIGFALLAGGLGGSFTVFILKYVVAGYEGKSLLMGSANIISNILFMISATALWITGNMNDDYHYNLQL
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Belongs to the UPF0220 family.
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P53087
|
MIVRLHAIYQDITRDYLPPASLNHLMLLSKQTQHKLSFKSAPIPDLQPFFKNFTSKTPGSAKESPCSSTAKISSSISISSQCIFNVVILSFVFTSQNLNLPSHPALHNVSPESLNDRLMTQLECANSPRLACELWVGTDKEPILSPNSVSYRVMQPNEFES
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Almost completely overlaps SKI8. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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P53085
|
MSILSSTQSTILRIPSGLITFLLSKLFLLLRVEPSSASMSISESELLLMGNINDESPKPGKLASAPLASLTNLVFSIDVKGLTLIATTMEDCLVSGTFMLVSIVYSWKENSSS
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Almost completely overlaps KIP3. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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Q796Y3
|
MLCFVFGLNNVTVLCYNVPIKGAGLMEEQLISKKELLERTSISYGQLYRWKRKNLIPEEWFIRKSTFTGQETFFPREEILKRISMIQKMKENLSLDEMREMLSPKMKDVSMTADELLHKGLVSRPALEAYSEDGGSPVFSSSDLLSLFVLEGLLQSGNVSLAEAKMAAEVLKKHDTEEIEKQTELIVLRKLGVTTCFIAAAADSILFESSVKVVERVDLLKASEELKTTFMQEGHQWM
|
Truncated N-terminus.
|
P28636
|
MKQQAGIGILLALTTAICWGALPIAMKQVLEVMEPPTIVFYRFLMASIGLGAILAVKKRLPPLRVFRKPRWLILLAVATAGLFGNFILFSSSLQYLSPTASQVIGQLSPVGMMVASVFILKEKMRSTQVVGALMLLSGLVMFFNTSLVEIFTKLTDYTWGVIFGVGAATVWVSYGVAQKVLLRRLASPQILFLLYTLCTIALFPLAKPGVIAQLSHWQLACLIFCGLNTLVGYGALAEAMARWQAAQVSAIITLTPLFTLFFSDLLSLAWPDFFARPMLNLLGYLGAFVVVAGAMYSAIGHRIWGGLRKHTTVVSQPRAGE
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Belongs to the EamA transporter family.
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Q2M928
|
MKQQAGIGILLALTTAICWGALPIAMKQVLEVMEPPTIVFYRFLMASIGLGAILAVKKRLPPLRVFRKPRWLILLAVATAGLFGNFILFSSSLQYLSPTASQVIGQLSPVGMMVASVFILKEKMRSTQVVGALMLLSGLVMFFNTSLVEIFTKLTDYTWGVIFGVGAATVWVSYGVAQKVLLRRLASPQILFLLYTLCTIALFPLAKPGVIAQLSHWQLACLIFCGLNTLVGYGALAEAMARWQAAQVSAIITLTPLFTLFFSDLLSLAWPDFFARPMLNLLGYLGAFVVVAGAMYSAIGHRIWGGLRKHTTVVSQPRAGE
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No visible effect on bacterial persistence. Belongs to the EamA transporter family.
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P45742
|
MSQNDSGHFLISEENWSLHRKGFDDQQRHQKKVQEAIKNNLPDLVTEESIIMSNGKDVVKIPIRSLDEYKIRYNYDKNKHVGQGDGESQVGDVVARDGSDKKQGPGKGQGAGDQAGEDYYEAEVSLMDLEEALFKELELPNLQQKERDNIIHTDIEFNDIRKTGLTGNIDKKRTMMSAFKRNAMSGKPSFYPIYPEDLKYKTWNDITKPESKAVVLAMMDTSGSMGVWEKYMARSFFFWMTRFLRTKYETVEIEFIAHHTEARVVSEEDFFSKGESGGTICSSVYRKSLELIDEKYNPARYNIYPFHFSDGDNLTSDNARCVKLVNDIMKKANLFCYGEVNQYNRHSTLMSAYKNVKDEKFKYYILKQKSDVFQALKNFFRNEESGVSHQFS
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By phosphate starvation, via the PhoP/PhoR two-component regulatory system. Belongs to the UPF0229 family.
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P96769
|
WPPLHPLYRTDLSLEAAIEEEANRLDPLVQQANLLIDTAALSTHELAERLREFLSGHSDKELKIVVESFGFKYGIPLDADYVFDVRFLPNPHWNQGLRPLTGLDDEVANS
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Displays ATPase and GTPase activities. Belongs to the RapZ-like family.
|
O31593
|
MIEDETKGENKMNRGRLILTNIIGLIVVLAIIAGGAYYYYQSTNYVKTDEAKVAGDMAAITAPAAGKVSDWDLDEGKTVKKGDTVAKIKGEQTVDVKSIMDGTIVKNEVKNGQTVQAGTTIAQTIDMDNLYITANIKETDIADIEVGNSVDVVVDGDPDTTFDGTVEEIGYATNSTFDMLPSTNSSGNYTKVTQKVPVKISIKNPSDKVLPGMNASVKISE
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Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
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Q2M957
|
MSKKIAVLITDEFEDSEFTSPADEFRKAGHEVITIEKQAGKTVKGKKGEASVTIDKSIDEVTPAEFDALLLPGGHSPDYLRGDNRFVTFTRDFVNSGKPVFAICHGPQLLISADVIRGRKLTAVKPIIIDVKNAGAEFYDQEVVVDKDQLVTSRTPDDLPAFNREALRLLGA
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:26774339, PubMed:28596309). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:26774339). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed:28596309). In vitro, prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures at 55 degrees Celsius, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures (PubMed:27530919). Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity (PubMed:26774339, PubMed:26678554). Is a general stress protein; is required for the protection of bacterial cells against many environmental stresses, including oxidative, thermal, osmotic, UV, and pH stresses (PubMed:17933887). And plays an important role in protection against electrophile/carbonyl stress (PubMed:26774339). H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein] H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein] H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein] H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+) H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+) H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+) H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+) an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+) an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+) Glyoxalase activity is inhibited by zinc ions at pH 7.0. kcat is 118.44 min(-1) and 20.80 min (-1) for glyoxalase activity with glyoxal (GO) and methylglyoxal (MGO) as substrate, respectively (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554). The apparent kcat of MGO and GO degradation is 0.29 sec(-1), and 0.42 sec(-1), respectively (at 22 degrees Celsius) (PubMed:26774339). Exists in monomeric, trimeric, and hexameric forms. Cells lacking this gene are highly sensitive to oxidative, thermal, UV, and pH stresses, but only slightly sensitive to salt stress and insensitive to cold stress (PubMed:17933887). They display increased protein glycation levels, and decreased viability in methylglyoxal- or glucose-containing media (PubMed:26774339). They also show highly increased DNA and RNA glycation levels, and exhibit strong mutator phenotypes (PubMed:28596309). Moreover, the double and triple mutants lacking yhbO and yajL, and yhbO, yajL and hchA, respectively, display impressive amounts of glycated proteins, suggesting that the YhbO, YajL and Hsp31 deglycases display relatively redundant functions (PubMed:26774339). The triple mutant displays higher glycation levels of free nucleotides (GTP and dGTP) than the parental strain, and shows higher glycation levels of DNA and RNA than those of single mutants (PubMed:28596309). Belongs to the peptidase C56 family. The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648), which has then been rebutted by clear biochemical experiments showing that DJ-1 family deglycases are bona fide deglycases (PubMed:28013050). Deglycase activity is even strengthened by a novel article that reports nucleotide deglycation activity (PubMed:28596309). Extended N-terminus.
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A7ZS49
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METLITISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRGSGTEQA
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Belongs to the UPF0306 family.
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B7UJ49
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAIAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKLVWQR
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Belongs to the UPF0306 family.
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B7MB75
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAIAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRNSGTEQA
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Belongs to the UPF0306 family.
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B7LH88
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METLIAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRDSGTEQA
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Belongs to the UPF0306 family.
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Q8XA94
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDVQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRPDEIKFTDNTLGFGKKMIWLRGSGTEQA
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Belongs to the UPF0306 family.
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B5YS44
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDVQKVAFYILTEEKTRHAQMRGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRPDEIKFTDNTLGFGKKMIWLRGSGTEQA
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Belongs to the UPF0306 family.
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B7NKM3
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METLTAISRWLEKQHVVTWCVQQEGELWCANAFYLFDTQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARQAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRNSGTEQA
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Belongs to the UPF0306 family.
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B7N0T9
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARQAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRNSGTEQA
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Belongs to the UPF0306 family.
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B7M062
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METLTAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRDSGTEQA
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Belongs to the UPF0306 family.
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Q796W7
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MRQTRGEASPSAVSLAFKFASLAVLCVLLLLMVILGYSNSSTKAKEVTVTTNGQLRDEKESLKLKNDSPDLLIKHLQTKQNMGDKTVYLTFDDGPSAVTTRLLDVLKSADVKATFFMLSPRMNEFKQAVKRAEKEGHALGLHGVTHNNRLFYQTPTSPLKEMQEARDTLQDITGYKTDLVRTPYGSKPSLTASQIRNLEKDGFVYWDWTIDSMDWKYRNSQYVTAVLQQLENMEHSSSSRPNVILMHDLPATVNALPVLINKLKEKGYSFGVLEDTMVPVHE
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Belongs to the polysaccharide deacetylase family.
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P95509
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MEYQFTHSIHGVVAKCSMDHEAFARWLNAEITENPSQLAPIFAEIEKCRAAFPNHYECVFEGREYSLYFDYDEVMAKANNLDAAFDDEEMEEGFQFYNEESIAFCGLDDFEKFLKAYQHFVQTYH
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Belongs to the UPF0231 family.
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P45533
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MSRSLLTNETSELDLLDQRPFDQTDFDILKSYEAVVDGLAMLIGSHCEIVLHSLQDLKCSAIRIANGEHTGRKIGSPITDLALRMLHDMTGADSSVSKCYFTRAKSGVLMKSLTIAIRNREQRVIGLLCINMNLDVPFSQIMSTFVPPETPDVGSSVNFASSVEDLVTQTLEFTIEEVNADRNVSNNAKNRQIVLNLYEKGIFDIKDAINQVADRLNISKHTVYLYIRQFKSGDFQGQDK
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To H.influenzae HI_0575.
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Q2M711
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MSRSLLTNETSELDLLDQRPFDQTDFDILKSYEAVVDGLAMLIGSHCEIVLHSLQDLKCSAIRIANGEHTGRKIGSPITDLALRMLHDMTGADSSVSKCYFTRAKSGVLMKSLTIAIRNREQRVIGLLCINMNLDVPFSQIMSTFVPPETPDVGSSVNFASSVEDLVTQTLEFTIEEVNADRNVSNNAKNRQIVLNLYEKGIFDIKDAINQVADRLNISKHTVYLYIRQFKSGDFQGQDK
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To H.influenzae HI_0575. Extended N-terminus.
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P45535
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MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN
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Genetic data indicate it may be involved in ribosome assembly or function. Belongs to the ABC transporter superfamily. ABCF family. YheS subfamily.
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A0A0H2VBH0
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MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQNRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN
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Genetic data indicate it may be involved in ribosome assembly or function (Probable). Ectopic expression exacerbates the cold-sensitive growth phenotype of a bipA deletion (PubMed:30597160). No visible growth or ribosome-associated phenotype. Belongs to the ABC transporter superfamily. ABCF family. YheS subfamily.
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Q2M718
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MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN
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Genetic data indicate it may be involved in ribosome assembly or function. Belongs to the ABC transporter superfamily. ABCF family. YheS subfamily.
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P44808
|
MIIFSNLSLKRGQTELLENASATINPKQKVGLVGKNGCGKSSLFALLKKELMPEGGEVNYPANWRVSWVNQETPALDISAIDYVIQGDREYCRLQQKLERANERNDGNAIARIHGQLETLDAWTIQSRAASLLHGLGFSQEETIQPVKAFSGGWRMRLNLAQALLCPSDLLLLDEPTNHLDLDAVIWLERWLVQYQGTLVLISHDRDFLDPIVTKILHIENQKLNEYTGDYSSFEVQRATKLAQQTAMYRQQQQKISHLQKYIDRFKAKATKAKQAQSRMKALERMELIAPAYVDNPFTFEFRPPQSLPNPLVMIEQASAGYGIGESAVEILSKIKLNLVPGSRIGLLGKNGAGKSTLIKLLAGELTALSGTVQLAKGVQLGYFAQHQLDTLRADESALWHMQKLAPEQTEQQVRDYLGSFAFHGDKVNQAVKSFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALVDYEGSLVVVSHDRHLLRNTVEEFYLVHDKKVEEFKGDLEDYQKWLSEQNSTSENKVSEKVGDNENSVQNRKEQKRREAELRQQTAPLRKKITQLEEKMNKFSSELANIENQLADTELYNAENKEKLTALLAQQVDVKKALDDVETEWMTAQEELEEMLQA
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Genetic data indicate it may be involved in ribosome assembly or function. Belongs to the ABC transporter superfamily. ABCF family. YheS subfamily.
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Q2M719
|
MAQITTTDANEFSSSAEFIPMRGFSNCHLQTMLPRLFRRQVKFTPYWQRLELPDGDFVDLAWSENPAQAQHKPRLVVFHGLEGSLNSPYAHGLVEAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLPVDAAVIVSAPFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGTLPINLAQLKSVRRIREFDDLITARIHGYADAIDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGFIGGTLLHPQMWLESRIPDWLTTYLEAKSC
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Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
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A7ZSN0
|
MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
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Belongs to the UPF0270 family.
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B7UK65
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MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
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Belongs to the UPF0270 family.
|
B7MCX0
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MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVSDVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
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Belongs to the UPF0270 family.
|
B7L4N1
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MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
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Belongs to the UPF0270 family.
|
B5YTR1
|
MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
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Belongs to the UPF0270 family.
|
B7NMC2
|
MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
|
Belongs to the UPF0270 family.
|
B7N0Z1
|
MLIPWQDLSPETLENLIESFVLREGTDYGEHERTLEQKVADVKRQLQCGEAVLVWSELHETVNIMPRSQFRE
|
Belongs to the UPF0270 family.
|
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