UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
Q8TGM8
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MHLSTLPNVPWPNRSFTTKRPPLPNMSFSW
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Completely overlaps KNS1. 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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Q07811
|
MNSIRKLSCFGTGSSIYSGKCLSSTQQKGLPQRTLWTMNGLIWAYWMMVLQLIIIPKDSGCSRSTFLFFFSHLLLVPFFFFLTLLFHFPVFNNISLNFYIQ
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Partially overlaps KNS1. 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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Q6ZV60
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MSFSPYSTMITVCVCFNSRVQLTVPSFTAWLRSRYSKALFMVLRRAAQEKDKGVCQGWHCVKKWACKGRIPGQPLQPQPLGPYLRSLSQHPATQTPRPQARASSRYLELHRSQNRGGSEFKFWFCYCLIACCRDSISSSGKWE
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Product of a dubious CDS prediction. Probable non-coding RNA.
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Q5UPA9
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MCWVGENIEKTTKINYRYDDVNKVLDKINSCIVDKYNANKYVLCTHEILLKKKVSLHRYLIAVSDADDLTPEILDYLKFNYPDVKVLTELPESADKLNKIIENN
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Belongs to the mimivirus L28/L54 family.
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Q12174
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MIMQKRLLNRNSSVVKSRNCLARHQHESSISKLHVSLRLHRCLRPIVRFDFLHNAGSKVCSQNSCPSPQLHVGTMALFHTVFILWPHFCGILWTVHEKLYNYLLSIEVY
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Overlaps YLR122C. 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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Q12327
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MTPLFPESVSTYIYEYSTIWRSGALLIKMMQRVITSCVTGPCKNCYVFLVLGIASWRYIFSYQDGILQSENSKWCSKEKKKKCSAIYPHYNHRDSLGNGAVPRNLLSTYHPMLM
|
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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D6VYC1
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MTVKKIAILYTDEDNEWSKPWGNFVDMAIKLLEQTRKLECIAEDVEYEVFHVQKNVFPQLSDLQKDEYLGIYITGSKYDSFDNEIEWIMKLRSFLNEMLTSKTEYPPVAGICFGHQVIAAALGSSVGRNPKGFEGGVVSLKLNSVGQKLFGAQELNLSEVHSDCVFDVPEGYQNWASSEKCQNQGFYRQNRVLTFQGHPEFNSDVAQKGLLKSQDKLTLEEFNRYERQCQELDNNGIQAARNIWRLFLQKI
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May have a role in copper and iron homeostasis. Induced upon copper deprivation. Present with 1510 molecules/cell in log phase SD medium.
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Q5UPK7
|
MTSSIVLKFFLIATLLVIANSLPACHNGQFLKINKGPNCDDAKYENPDYVIVGGGAAGSVLLDKCISYGYKCTLIERGIDYEDEQVVSQPSGSGLVQSSNAVLLTTTYPNSNIFNKTLVITEPNIIGGSTSINGEISVFTDIENFFEEISIPGWSYLDVLPYYLNVTNSVNRPSHQGAVDVTNTLVTDPKYVAFKAAIQQVFPNIHEKLPDMNTASLNGGFPGYGPPETSVKTSFIPIGDTQVPVSGFRESAYRAYIHPIRNHPNVRIMLRSRVDKVAFDKCGETAKKVFVTYQNYQGSDSQCELKAKKGIILSAGALRTPQILMQSGVGPADHLNELGIPVVSDMPDVGQHLDDHPTVVRTFLGIIPDSSISANIDGHAYWNHLDDPNKVPNWSIQISGFYGPNFKNILNVYMDQMSRGWIKLRSTDPADTPIFNLGHFSDLEDVGPASLGFNKTNQVISNLQYIPIPGLTDVVCPSFIPNCQSNLTEYYMAAYYQFGYSGYHYTGTCAFEKVVDPNTGLVYGFDNLYVVDASVFPKAPRGNTQIGTYAISAKLADIIFGCQ
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Belongs to the GMC oxidoreductase family.
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D6VYF8
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MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YLR157C-A ORF.
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A0A143ZZX1
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MEEIENAHYQNLENFNDETSEDVNDTSDDINKNNDDNNKYDDNNVNVLDDKNKLENEEDNNNNDNMMIFSSILRYQRYKTKKGNIYFDFKNTNLSLNEKDMLVQSSNFYHLFDIKSLLCPHIYLNVSSHININISDYKNYLKRILNNDNVLDDKNENVKYSSCQEFIFEAVEQAEHIEVFTKVQIVKKLFLFLNQNVAEKMKNYIDNIPIINSNDYVLVQTNLKNDLLLGYVKGIKYNLFFEILNMKKCFHSFLNENIVIYEINEDKEGYFKTIDGKKYLKEQIVYEKKDLLKNLDFYSMYYCDYYFSSNSIIELEKKNNNNINCVNNNINSVNNNINSVDNNINNVDNNINSVNNNNNISDKITHKFEYNDYNDIHLFFSFNICIKSVKNNLFLHIIYNDNNLKNGDEYLNETFPHYEELNLYNKQFDINKMDKNLFKSNTFFINNLYYHLKCKLLCVFKFINMSDDDFMTDIHISQIKKRRYVNEQDSYMLYTFNIHTLSNEGMVYIFFCNLYISNMFKENNFEIRVHTYLHFQLNKQNSYKKLKLIKYSSKFLYSLCFKEKSDSKKKKKKNDHHERDSDNNNNDSNNNNYYNSNNNSNYCGSNNIIYGHDENFIFNSCDFNTLDQIKSGNYLIKDETINENFIFEVRNYKYTFILISSKCNIIIITLRKKKRKEEYNKKMSKYSSCSLNENVYMEGVEILNYCSSNNKNTNNIICNTIINKYNYEINNNIKNKNKSYILFEIVCFYENGEIQKYIYTCSLKNGNFEFFLNVKEDEKTKSINCKKCFFKPILFPFNEELLNKTKSSNDLVLYNIKLSHFKNLIYIYFQEKKIEGISLTINNECLIINYIKMVSKLLKKILQNLYNSDDIDIVYNFQHNTKNKCNYLSQNVNIPSDNTISNVIKKNEMDNNDIKYNLFTQREVKSSFFEFKYILFGFYDLFLMNQKNYTDLNEKKKEEYKKKNFINCFDSHSHYNFLNIIKEYINYDYIIDKCSYNISNDTQKKKKIKLNFYYFLLIIQYFKNTYTQEKKRSFFYMVYNELLQRDKYLKHFYYTYHEIDRKTNMHLNHNDNNIDTKEAKKNEETELILKNVNFYDNYELINIRKYDVILFCFLFHMYNFCLKQNGLSNDEFNSHITYFLINKKMKKYKKKYRYISKKKIDTNEKNDDNNNINVCDSKNYKGTKNFDDTTNNILNKQNESLDNLKKNMYLSKNNYDNQLSSYKNTKQNKTNINEKYNNNNIIMNYLTWKKCLYYIYKIKKYTRKIETHEGLYISSMLYINIYLCQIFFILLNILRINNTNIYTNIHFDIRKNNLDYFYLLILLNFYSLFYILISDQKYILHEEENDTYISKNIDNKEQMANDKNIISLLSFFNNIYEQNKEGMLKNDQNKNNHNTKTDILYMSSSGMNISINTPFLEKYLILIYNIIKDKINIVKEDNYIMEKLFFKINCMICNKVCVTNIYNNYYICENNHIFNKCMLTFGCIYKNHIILPTIYLLHDINDKLFPINNDHILSYNLQYELDYIYFCSFCYNFITTQNSFYKKFFLFNQCPFCNHELNIL
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Expressed during the asexual cell-cycle on the cell surface of the host erythrocytes. Possible candidate for an effective malaria vaccine as determined by epitope response in sera.
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Q5UPL0
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MHKIPCFVLIYEQFDIIKKCLTFLTKYAHRLHIVIIENYSVNTNQQIKPYVMDLLEKGIICKYYLFEENIANNAVHIVLEEAIAKYLDPTVFPYVFVTDGDLTIEDTNWIDEHVNIMDKHKNVFICGCSLDNSNLPTKTMPNAVHWIKPGIDQGDYIKGITGTTFTLHRTNELIEAIKFFNSKGWRYLDSNLHKFCFDAKRMIWARTKKAKCYHLTWDLYLDLTHPYTIMKLKNVNTMWKRSQSSKFQLYENSSDLRLDIYQELNDTKETIIVRKLKVISSGFDLGLDQSGIEYNGIFYPASRGFTVYTITDETVSVSNFDTHINSCTVNLARHIRESYRSGCHYIISVVHDDGFKKLSKNQLKEVGGLLSLDKIFYLYIRFSYYFVYDNIHKSLIDEDVSKVSFLSKEFSDLKFSKLISNNQITPSSTISNSNSQDLNIPDSTIIPLLSNNNGPITKQYHIVCLKWMLMFYREYIESFGSLLNIDYILLDNFNNYNYINSPEHVYIFCQLTDDSLLTKPFQKMILNTEQLTIAKYMDRTRKYINHGIQIIDYSIENIKLCNNPSTIYLPYQYSDSEIQILKKLYDSTPKKYDLVFCGSISQRRRYILDSLKSHGVSILELVTGHWGHPRDVEMASCKMLINIHYAHDYNIYESMRCDRWAFATMPVVSEDSIHYGLLDVKKHGLITFCEYDQLILKTLEALKNFKKTNENIINTVKKEREHQLIKVFTELK
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Belongs to the mimivirus L137 family.
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Q5UPK9
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MSNKQKIPCFVLIYEQVDIIKKCLSFLIKYSDRLNIIIVENYSSNTQTIIKPYVIDLINNKLIWKYYLFEKNIYNVAIHISINHAIKTYLDPNEYPYVYVTDGDLTIEDSNWIDEQLSILDKCPNAFVCGCLLDYSNLPIETIPDSVGWIQKYTDRGDYNVGITGTVFNSYRTPVLIEAMKYLNDNGLKYLDYHLHHYHHEIKNMIWTCTKKAKSYHLTWDLYADPENPYTIYKLRNYKTMWFNNTEASYQLFEHDDINNQSDNQSNSELDNRPNIEPNGQSNSEPSNQPNNEPNYQSNSEPSNQPNSEPNDQSNSELDNQSINEPNTEPNTESNGQSNSELNNQSDNHPNNEPNSEPNNEPNNQFNKPDNEPDDKIILKVVSTGFGKGTEKSGLYFQDQFYPGTRGFNIYTITQNKSITFQNYDSSGKQCIGELVRYIKTFYDTDHEYLIVLVDDDATRSININFMNEVVELYDLNKMYMLRVRSSYYFVYNLKQKKLIDENASDFITVKNSYNRKDLDLLSETQTTTINPTTINPKTNNINNPTNYVNVDESIEINNLNDINGLELDGLKTVKIMSEDNSDLEFSENEIEEPIEPIKYHIVCRESIYHYFKDYVESFIDKLNSDQSNNPKEKSTANSIISNQIHIYNYIDSPNHVYIFCQCIDDHLFKKSFNKMVIFTEQLTKKQELNQISRYVNHKIPVIHYSIENMKINNNPTDIYIPYQYNKKEIKVLRNLYLNTPKEYDVAFCGSMSPRRRKIIDDIKSNGLKVLELVRGYWGNIRDCSIAKCKVLVNVHYSHDYNVYEPMRCDRWAFATMPIVSEDSIYDELLDVKKYGLVTFCPYDELVTKIIQTLKGANKHNLSAIKIIKHSRKKKFYQTLQHL
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Belongs to the mimivirus L137 family.
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D6VYM8
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MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAAKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YLR227W-A ORF.
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Q5UQ80
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MNPTNLNFGKILKQVEMVDVNEDSLDLKFPKRTIVDISTDTFIKIIFEKDDNYYLFLNYVNALDLYLNYYTNINLVSSNKQLLNQDEHIDVYFKGGNVMNYHFRTMVSDPRLKELFSAYFKKSDFDFSVSIHTDTDNRFNQLKTYVYPKIIDYLITTSNLFNEYLQEIINGDINKSTIKIDPKFLHNFKQDNADLKYYTIRDTIKDIIGLPRFNFVKEIIDNTRNTNTKNFMHIRQIDNIGRYIRVKFHDNSIIQFIPSDKSFYELKYTPYIINNFNQVIDYYNEYVLNGLIPVYHNFYENSKYHACLLYPYYKYLVEPIGQHEMEYSDLIDKIIKYNFSLLEKSEFYTKEKINSMLQQISTSLNELKDTYYEKNSDNPPDKTEVTNSNAFIRYTVNKNRSDNPHIELAPTNNFLVYNDFEKSDPLSIINFDDNQTIKTTNNVHYVSGNMLIKNILGNRQILDFDLFRIKFNLVAVNYIFENEKLLREFKIPSEFIDVSVTIIDSNVYNEDHQTFIMPIKLDNTIIPDIPVKSHSYTYFIGDLIRILFTDFNFFPWMKGKYEKRIKRLLLLLYLYDQQHQTNYLDTLYNMATNIKYNLTNPNKTQKNMDKYALSKVHLNSYKDYSNLFDLVYIDNKYGPIKEPMKMLLIVSEILDKNNALDIINHFRKYLKLAPLTNISNLKTEFGKFLDEIISTYNDINPQNIQAKSSINTLVSRNNYSMIKNNRRNY
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Belongs to the mimivirus L515/L516 family.
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Q5UQ79
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MIRLQTPIIKETIHPKKTPTALNWLYPEKIIHNISSKALIDNIYSENYQHILVGLISLIEPWVYLHTNLKLIDNGHLPLIDDETIILISSGEYMIDYYYRIEVNKYGKQTDLFDKLLQSVNNSNKDFFDKYKNYFKISGIDFDLNINTSNTNRFEIIEKYVIESLVEILDKITDGLDAIYNYDNQRDVLLPIFNNNYNNDNVESIDIDYDLDLLKKVKTIMANPTFKFDKDLMFHPTKSLIMEARETNYRVFNDLGNQIDAIMKNSNNIMIFPYAYFLIKNVHGKNDYPNSSYKKFDNIIINQLNQYFIELSNGEIYSNYHKNAFFVDSINGFRSINHDLYLKRFNDFVPEENNNNAFYDTIKFPNITQVNNMEIIPSDSFYIYNQGKEVIDSIVEKKHNIVVNQSKAKATRSNTYIIDKDTIELNLSVVFKGLLFNNKPVVYPISSNIVTFEIERINSTNYVDNVNVPYQVLQIKNPKVTIKTYDRKTLINKLMKKLFDEDHFLPWYIPNYNQNIVKLLFLINLDKHEYIDFLKKLLQTQNKKELVDYSLYYCFDYQSYSFYNLIWIDPMTVDRYYEIQYLIKFIIIMDNILLLPDVSLRKILIDFNSSYGWYDPNVDLSSVKVSYQNFKNNLLNTLNELDDIYHNKSK
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Belongs to the mimivirus L515/L516 family.
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Q5UQ89
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MNNSNNCNNLNNQNLSINIQCQNIEDLRKLQELLNNFNLNTSSQNNLSQNNDEPEDILEPIVITNDDNEITENDLENSDEQIPNFTDNKDKEDVKEDELDLESDGELNRESVESNHKPIHESNHESNLIDTNIQSFESQSSSTESLLDSQSDSQSDPQSDYQSNYRSDLQTDSNKNYKTNPQLNYRTEPQIHPRKKTFDQNKITLNVGGKKFNVKKKLLQFLNINYSRLYKMQLDNSVIYFLDKDPHYFSKIIDLLKLCNFDESVIMENLDEYSEQFISELCYYGITDKKYCPNSKLKLKKQVSFPSRHSEIIKIIVGNQIFATLSTTLSRSTFFNNKLKLSRSKQFSVSDIDPVVFRYVLNFLRSGELYVYNSDIINYLDTYKIDYEITEISKTVTEDIVANYLPNNIDSFNNQVNKCIEYLHPDNNKIQSMEPYHFIDNKCYYPNNMFSSSSAENINIITTNSELVFGSDIVFNLSENVFGESIEDLVLCIDMPVLKPTENIQYVNNIEYNIIDYIYLTINNKQDESSGQIKKVFQRTGDTIHMYPLIYKSNHTDYHDISKNKNSHMKLLYNDTLIDIVRITLPLYFFRNRRNHLPIKKMISNGLSSDLIVKMAPINKILSGGYKDIPLLNVFLMANHINTSSKAFVVQPEQKSPTGYKIMEIPNNIELKEIPMLYVYDDIKEIILQVHERHQLYDVYLLPLENFEMIKDFFFTINNNDKYNNLNNNFNDSLIELEILRLDKTGNIQTYGKYDSIMLGLYIPLKYLNHSVPKGIYYYSFSVNPLESNIMGGLNGKDYYVRIKTKKIDGYIKFYVNQYYKFIV
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Belongs to the mimivirus BTB/WD family.
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Q5UQ90
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MVLSDILFSIYEHREKSPVFSWFAYLLRILDWIIQFLSFGLIPSIGGDLYDLVDNGLFKFVLDRNIQKKQNQLYDKFRLGTVKMCLVFDGELTKKLLLDNSIRRGGLYNLLTKFFGKGIFTSNIHSRWMKQRKAIFKLFSPQNLIQITPELTTSMFEELDRLITIKKDLDLVTVLSLIGLVGFCKVIFGVDVTDMSEELIEPLNDLLIYINGAVEPVLITADPSYRRFITNKKFVHNWMRKLIDKARKSENCFEIMRQQLDDIGSDDETELIEFILSVVLGGHETTARLMLGIIYSVCHNKEIIEKLNNETDEYPKGDYINLKKRPYLNNIIKEGTRLFPPVWLLSREAKNDTTIDNHFFKKGTQFLISPLIILRDYNVWGSNAEKFDPERFSNMDPKSKASKLYIPFIVGSEDCPGKKFAILESAIVVSKLFKEYEITVLKHKLNPMSAGTFRLSDKLPVSIKKLKN
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Belongs to the cytochrome P450 family.
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Q5UQ98
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MDSIILKNHQKKPIEFMKNNRGVILYHSTGAGKTLTAIYSVYQFDYPIIIIGPKSSKKAFTDNIEKAGMDISRFTFYTYTKIKMILESDITIFKNMSVIVDEAHSLRNENMYNLYISSALMLASKIILLTATPVVNYFNDLAVLVNIVRGEDSLPTERALFDQMFYDEETMTLINAPILFNKLLNTISYYKIIDTINYPTSESHIKQVEMDHLQIDEYKYYIKQILYSNENVPDNVDIFNINYGLLPSKKRNFFLNVTRQLSNVAKIADTSPKIEDIMKYIISGPYPIVIYSNFLKSGIYTLAVRLEKENISYKIISGFVSQDKLNMIVNNYNNGLFKVLLISSAGSESLDLKNTHQVHIMEPHWNESKIIQVIGRSIRYGSHISLPQNERKVDIYRWISIFPNQYRNISADEYLTTLSQRKMELWNKYNQIVIDASIENNYFAK
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ATP + H2O = ADP + H(+) + phosphate Belongs to the DEAD box helicase family. DEAH subfamily.
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Q5UQ96
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MASNLTFEDKIGILDPKGLRPNPLNNEPYSDDYKKLAMVWSTYPAYSAADRVLSALENYQLVFVTSSTGSGKSVLIPKLALHYTNYNGRVVMTLPKRIITLSAAIFSAKVSDVKLGESIGYAYKGSDKSMYNDQNKIIYVTDGIFVMEYVRDPLLSKFNVVIIDEAHERRIQIDLILLFLRTLLQSGNRPDLKVIIMSATIDTDKYQKYFNSVDSTVIDIAGQPNHPIETHFMDKPVTSYMKEGLELIEDLIHQQIKKDMLFFITTSNEALQLCRSIRPQYPRVYCVEVYSDMDKNLKQYAESRDKYLELGNYDQKLVMATNVAESSLTIDGLVYVIDSGYELSSRFDPECYGQILEKKFVSKAQALQRRGRVGRTEPGVCYHLLTKQQFDGLADYPTPDILRQDITMDLIKIIQVSPNKTYAEGINMMNQLMDPPLRSHINATRNLFDLYNVVDDNGILTQVGIVATQFSSLPLNRILFLIYAFELQCAREASIIVAMTEFLNGRVTNLFYKSDTICESNCEKQAANLLLEKLIQKRGDHFTYLKIYQEFSKSTDQKSWARKYGVRLDTINNIERTANQYFYRILNLLRKPRLPNNKNTLIDTSIDTPMDIQSRISSTDTKTNLLNALKKSHQHLTASKLKPTYSKENITGKISRDSVLNQIYKKNEISKKKIIYDELSNINGKWEFRTVTIIS
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ATP + H2O = ADP + H(+) + phosphate Belongs to the DEAD box helicase family. DEAH subfamily.
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P0C5P9
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MLLLKSIRRHQDRSIVHLLRGPNLRSLSLRVWVLHPNTRIDVRLLGPCFKTGGI
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Completely overlaps the 25S rRNA gene. 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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P0C5Q0
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MLLPKQKNPFSKLLNFFNDPSAGSPTETLLRLLVPLNDQVCPNSPL
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Completely overlaps the 35S rRNA gene. 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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P0C261
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MAGTLFIILRFVDTTLPSSRVYCVRSLEVSVAVELAAATVLAFESIGVVDDCGRSVLFSIILIAAFICSVFLIASEDIAGSRRSTGSCVTLWEGRNISFCLYRSNWLNTVPVGYMFFLRKNRSLDERYF
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Partially overlaps CMP2. 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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G2TRN7
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MGVRLVVHYRLPASSMDYVQETGRAGRDGKYAIAALFYEKYDSTWSSYVEDSMKNFLNDNTMCVRSFLASEMDGECVCYSLLGEESTVSTMYGVKPTLPETPKPAIATHSRYNASFSSSPPPQPGSSSGMSAMNTNTTSTTPVSGKT
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Truncated ATP-dependent 3' to 5' DNA helicase. Belongs to the helicase family. RecQ subfamily. Is probably not a functional DNA helicase since the N-ter is truncated and misses the ATP-binding domain.
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A0A8D9PCP6
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MYVRRFYSDWFSGFSMFKNFNSSSFGLDSIIFFKYNRCFISSLEKSLNCIESSSFGTTTLVSSFKSHNFLKLLLLEADLLLLLLSLLLTWKYIKEAMSLTILSSLLPFWDPFDTNLSIKLS
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Almost completely overlaps RCO1.
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B3LLX6
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MCGIFGYCNFLIEKTRGEIIDTLIEGLQALEYKEYDSSGISIQGDELKSLNIYKQTGKISSLKEEIDLYNLNKNLPFISHCGIAHTRRATHGGLRRANCHPHNSDPSNEFVVVHNGVITNFANLKALLVAKGYVFKSDTDTECIPKLYKHIYDTSIELGYNLDFHVLTNLVLKELEGSYGLLCTSSHFPDEVVAARKGSPLVIGVKGKTDMDVNFVEVEYLDQEEDYLKLNTQTKSSGNVLAAAPVKYNTCLRKSPPLRSQYLRNSTTSTFNHGSSTETPAENGLPRPMEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHCSKIGSEDFSFRTVQKLELELSKIKKGPYDNFMQKEIYEQCETTKNVMRGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKSSFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMSEDLVSKIERRKEIIQALTIIPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTDELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMSAPDI
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Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins). D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
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C7GL41
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MCGIFGYCNFLIEKTRGEIIDTLIEGLQALEYKEYDSSGISIQGDELKSLNIYKQTGKISSLKEEIDLYNLNKNLPFISHCGIAHTRRATHGGLRRANCHPHNSDPSNEFVVVHNGVITNFANLKALLVAKGYVFKSDTDTECIPKLYKHIYDTSIELGYNLDFHVLTNLVLKELEGSYGLLCTSSHFPDEVVAARKGSPLVIGVKGKTDMDVNFVEVEYLDQEEDYLKLNTQTKSSGNVLAAAPVKYNTCLRKSPPLRSQYLRNSTTSTFNHGSSTETPAENGLPRPMEFYLSSDCASLARYVSKVVYLEDNDTAHIYDGELHIHCSKIGSEDFSFRTVQKLELELSKIKKGPYDNFMQKEIYEQCETTKNVMRGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKSSFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTDELGHRVLAVTSDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMSAPDI
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Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins). D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
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A6ZME2
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MCGIFGYCNFLIEKTRGEIIDTLIEGLQALEYKEYDSSGISIQGDELKSLNIYKQTGKISSLKEEIDLYNLNKNLPFISHCGIAHTRRATHGGLRRANCHPHNSDPSNEFVVVHNGVITNFANLKALLVAKGYVFKSDTDTECIPKLYKHIYDTSIELGYNLDFHVLTNLVLKELEGSYGLLCTSSHFPDEVVAARKGSPLVIGVKGKTDMDVNFVEVEYLDQEEDYLKLNTQTKSSGNVLAAAPVKYNTCLRKSPPLRSQYLRNSTTSTFNHGSSTETPAENGLPRPMEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHCSKIGSEDFSFRTELSKIKKGPYDNFMQKEIYEQCETTKNVMRGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMSAPDI
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Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins). D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
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C8ZET7
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MCGIFGYCNFLIEKTRGEIIDTLIEGLQALEYKEYDSSGISIQGDELKSLNIYKQTGKISSLKEEIDLYNLNKNLPFISHCGITHTRRATHGGLRRANCHPHNSDPSNEFVVVHNGVITNFANLKALLVAKGYVFKSDTDTECIPKLYKHIYDTSIELGYNLDFHVLTNLVLKELEGSYGLLCTSSHFPDEVVAARKGSPLVIGVKGKTDMDVNFVEVEYLDQEEDYLKLNTQTKSSGNVLAAAPVKYNTCLRKSPPPSFTIPEKLYNFYIQSWLIHRNASRERLAATHGILFVIRLCITSAVCE
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Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins). D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. This is a truncated version of a putative glutamine--fructose-6-phosphate aminotransferase. Strain Lalvin EC1118 has a frameshift in position 258, which disrupts the gene coding for this protein and produces two ORFs. A contiguous sequence for this protein can be found in strain YJM789 (AC A6ZME2).
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Q6WV01
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MEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHCSKIGSEDFSFRTVQKLELELSKIKKGPYDNFMQKEIYEQCETTKNVMRGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMSAPDI
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Could be the product of a pseudogene. This is the C-terminal part of a putative glutamine--fructose-6-phosphate aminotransferase. Strain S288c has a frameshift in position 258, which disrupts the gene coding for this protein and produces two ORFs YMR084W and YMR085W. A contiguous sequence for this protein can be found in strain YJM789 (AC A6ZME2).
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C8ZET8
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MEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHCSKIGSEDFLFRTVQKLELELSKIKKGPYDNFMQKEIYEQCETTKNVMRGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKSSFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTDELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMSAPDI
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Could be the product of a pseudogene. This is the C-terminal part of a putative glutamine--fructose-6-phosphate aminotransferase. Strain Lalvin EC1118 has a frameshift in position 258, which disrupts the gene coding for this protein and produces two ORFs. A contiguous sequence for this protein can be found in strain YJM789 (AC A6ZME2).
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Q6Q571
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MLLFCYCLLLGTRIGTRIGTRIFIVHPIISPLIAVETAKKKKHIKWRFLDYSLLKNPLYVTVHGSHRSEVERARKRIKYITCTRREFLPRVPISFYQRFFSVFCRNYPSFLL
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Partially overlaps YMR086W. 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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P15609
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MLRLNDVVLKDVVSYHSFFSKQAPGVKGPTIEKFLKRFEYNAPLDLYQVVDLEDFNLFFLDFFFKIFPKNLSIFDRQAANIVTANIIWSYRSWRHFKGLPCRGQRTWSNASSCYRSNLILRDYKKKNVRKIFGKYGGPEQKICFLCEYINYLWKSQWFSEWMHSRKWIKYTLKKKKVVFYLDLYATSKGLLGNLRSDAKGVTKKKKKMLTGHVGFDQGFTKIYLKAKYAVSKKVRRKLSLR
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Belongs to the universal ribosomal protein uS13 family.
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Q7LHY8
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MSTMNFLLSTILPGMYNDADAGTSSFCPSFPAWETVLISSIHSVNLPLAMVNACKDCVKCCNSWSNCCFTAFSCSGFSLVKSTKFRTCSNLKVSKVSVRWQQRRSYSFTYFFERTWLDFYSALSCLGHSKIFI
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Partially overlaps GIM5. 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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Q6B2I9
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MNSENSKITFKPNILIKGVYIFVLYGMCICIVKNYFKTQLFQLLAPAIHEKSKNNIFMIASDSFPNLYKQNTNYRPAHPLSVASKLPTLLAWLPNRSPLHFQLIWLPIF
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Partially overlaps ARG81. 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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A0A023PYJ0
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MKKKDRDSVFHRNIEIFITILINVVILKSFLLISSWVILVLLLVINDLPMYCYHHSLTYFLGCSKQTYFHRLGYPMQKLRHLLYFYYCYFLPRWKPRRRLTYHRYHPK
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Partially overlaps SPT5 and YML009W-B. 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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Q54K38
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MASPSSRLLKFITNGSKLHSAKNNNMIKNKNIISPTITKLFSTSKISNEIGNIRNFNNKISTNLINSNINTKPFFEIPKLFEKKYYSYIPPTWEEKDKEKQFNSITSTREEGGDNEESNRMGNGSIKDAIVWVNHLYPIKVSRLDFRSLFFHIPITKKLNSLFPNDVKIISIEKRIKEGGAYIHFQYDSSNPEYKSIEMVMSKLKSIFAQEKKHFHFASRPAKCKLVYGRPFVEDIDYRFPSTTLKITFKGSEMSPDDLFRLMRPYGHIKDIHYSSPIPSKDGPRQATITFKRMEGAIATRNCLHNKYFPEFNTSLYMDYEQLMRINKLKEQFSKHPKIMIPLLGILATLLTLLLFNPLREYFINKKLSSPCYFGEQEEDDWQERSEQKVLQTHFNFPPNSIVMISAPKGSGKSSLIDKVLENRINTLLIDCNQEVNNNDEEFIESFSKDIGFSPSYSLYSSFGSVIDAIIPTGKGAFHSTTNYQMQTILKLLDEVLAKKAKQFPVDPHQPYEYPLIVIDGFFGMIQAMESKEKANIIMDSVIQWAITSTQRGHAHVVFLSSDSFAGDIIKKYLDNRGGGQISTIQLGDVQPSMAINYIKKRIGPNTPITQHDMELVVDNLGGRYYDLNVLSQRMIAGDSVERALSNMISKAVSEIRAEGFGLSKRNDDSKIGGTKLKWSRPQLWETIKKIAENDFVSYDDLLFNVFLGDESSLNNLISSNLLRFQNVDNERKVTAYSPLYCSAFKQMVNDLEFNVGMDVLVQKARIEEELSKLSKVEDELLKIKNLTSKSWFEPLSIKKRRILLEDKLKDHVAKIEHRENILKKHSLFQKFLREEQMIQMELIKKQREQSKFERQQQQLLQQQQLQQQQQQQQQGSI
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Plays a role in maintaining the mitochondrial genome. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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Q6CTB6
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MFLSRSIPQAFSLRYTTRYGKLILRPGRRFVSSEIQQKDEQAGESNTATDTGIIHKTEQETLIYFDNVYPRAMSLWSPTQWYNLLMSNQTRNAVRAKIFKFANPPDNPIHNLELRSTIPIKRDGGVFATFLVPPNYTTAEVNAMIQKNTQQESSKSWFSFFTEVTAFPVKGSPWIEDLRRLPSNQIRVKFEGGFLTEEEVYALFRRYGTIINIYPNPKEMTYLISYRSFRGAICAKNCVSGMEVHNSIIHVQYEQLTQGHVISDFFVNHTRIAVPLLLALLSILAVIVFDPIREFTIEQKITHKYSLSWDNYFLKKILSVTSSTMSSVKEYWGITDRHVQKRQLWEERQEKVADLKLWLQENNNTFVVLRGPRGSGKHELVMQHTLHDRPNVLYLDCDKLIKSRTDAKFLRNAASQLGYFPIFPWVNSVTNLLDLAVQGLTGQKSGLSESKELQFRNMLSTAMMSIRHIALKGYKPVIGSGDSIINVKEEDYLQQHPEKKPVIVIDRFNNRAEMNGFVYKELSDWAAMLVQMNLAHVIFLTETVSPNQLLAESLPNQVFKMMTLSDASKKSARRYVLAQLQETTEDDDDIDTSKPLDLNEKFVHEIDDSLDPIGGRMLDLQAFVRRVKSGEQPKEALEKMVEQASEQITQIFLSGSADPLRGAQAWELIELLSANGSIRFRDIIYRPLFKAAPEAALLDLEKNGFVTMTRDRGVLTDIYPAKPLFCAAFQYLLNNKEMYNVLRTSYLLRMVTFETGRIKKWEEELRALGKVSDQKMFRSRLAYLAGKIDASSAAIDDCESEVKELSKK
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A5DSF0
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MMRLKILRASRINPALLRLRPPHLYSINKSQAFRFYATDIEDLKRQSDRTESDNSASTTGVIDKEANEVLLYYSFSNSRNFVKQYISRFLPSKFLGEQVEEKVKDVSYPLPQNSSITEVLHLPRDSGAFVKFKYSPSLTAKEFIQDIRSNIAESNTKRYSNIFMKAIGFVWDRSTQVYTVKGVPWIEDLKRFPSQKIGITYEGNPLTEEELYVLFRRYGLIDDIKVESTQSFVLFDTVRAAICAKHCITGMQLNGGKTTIHIQYVPVKKTNFIIEMISSHTKIALPIILALLATFAVLIFDPIREWFIQLKITRASHSFDEFKENKWFKIVYIPYKQLLNAVSSGYDYIDTQLHEVTGINNVDECLDDNQVLQEKNWESNMFWRERFEKAKQLKLWIMENIDTFIIVKGPQGSGKEEFVVDHTLMADAKLRKKVLLLECDELSKARSENSLIASTASQLGYFPVFTWTNSISQFIDLGLQGLTGQKSGLSESKETQIKNMFSLATQAIRSLTDGDYNKYKTNIEKKNRRLKDDEKIEVLRLEEFLAQHPESKPIIVINKFARKADVLSNDFIFPLIADWASGLIQNNIAHVVFTTADVGSLQHLNDALPNQVFKNISLSDASIASSKQYICDALKMKDTATLDDCIAPLGGRMLDLQAFIRRIKSGEDPLQAIDEMVNQAAELITTFFLHEHKFSNDDSNWNPSQVWLIMKLLSKKDVIDYDSLIKLPLFKQSKETLDTLSTLEKYDLVSLKREKGVLSKILTGRPLFTAAFENIISDVRIWKLYETQYLLNLVSLEVQKLTKFENELTTIYKINKLDGRIDYLSKKIDESNQKIVDYEKEIKDIAAYKGEPKQRHSFLGIF
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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G4MNU2
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MIGGTRLLPFRLLAFGPAATRQPTTALRRSRVTLTGAPRGIYLGLGSGSGLNINNRRWESTTATTATASSSRPKSDDVAAEVDYGHIVPRANEAALYFDNIFPLGLSAILWRRWGTDEDFSEQLLKRFEKSSFGFGITDPISMVKRSIPKSLPIKVTEIIPRLKDGGAFVKFSHGPETTPAEIEESLAKSLQDRPVKPWFNPFTSVRVNAVKGVPWLEDLYRLPKARLKVEFCPPKELSKDSTSTELSQEALYGLFRRYGKLSEITPQPSDSKVTPRFAHVDFVRVRDAVMARNCLHGLTISQDNSATRLRLSYEQKVKPHKIWEWTTSHPRIVIPILAALLAAFTVVVFDPIREFFVRAHVQGSFRVSNSRLYRWFKRRTADVTNSVFQRHHDKGEQAGLQALWSQRKDIIDSVQKWLLETADTFIVVQGPRGSGTKELIIDQALKGRPNVLVIDCKPIVEARGESGTIRKLAVAVGYRPVFSWANSLSSMIDLAVQGTTGVKSGFSETLESQIVKILHTTASALKKVSLEQYQKDGSGAEISEDAYLEAHPEKRAVIVIDNFLHKHDDGGLVYDKIAEWAAAMVQSNIAHVVFLTNDSSYSKSLSKSLPDRIFRQVSLGDLSASVAKKYVLGHLEGLDRDESLKDDSSEVSRDDKGAENPSEDDIEAESKRRRDLAELDGCIDTLGGRLTDLEFLARRLKSGQSPRNAISEIVDQSSSEIIKMFLLAKKSTESTQTQWSAEQAWFLIKEIASKTSLRYNEVLLSPTFASSTTPSAADGEAAIEALAAAELVTVTSHRGRPQTIRAGRPVYQAAFTQLTQDAVLKARMNLLLLTELSKVEAKNIDKVETELALLGALPKQPREVTDRVTYLLGKLHSSQVKISELDREMAMLKGVLVREV
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A1D3P4
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MIDVISRYQASPLIESTLGYQSITIIFGNAHLQSSKKNVILAAMMRTRIPGLVPRICQTPLPWKPPTQLTRVRYARWSTSHAVSWFETGHIDLKENEGLLFINNIFPSKLQWLLRGPLGGMRSYEEAVKRIDRPQLAASDTFQIIQRVVPKNLNIQVKEVVPRFREGGAFVKYTRPSNVNDADIEASIKENLKEHPIRPWFNPFQEVQVCRVIGRPWIEDLYRLPSPRLKVAFHPVSPEASAADLNTETLYTLFRPYGKIRDIEKQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGFTVPEQEGGGKSGTRLKIKYERKIKLSMIKDWLLSHPRIVIPVLAALLAAITVTIFDPMRTFFIKLKIKSTLQTEENGVMQWIRKQVNKANIIYFGRKGADPRGLTAIWEDRQEDITRLQSWLMENVETFIVVHGPRGSGKRELVLDRALVDYKYKIVIDCKQIQDARGDSAKIARAASQVGYRPVFSWMNSISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTATALKKVTLEHRKKNHKDSHLTDEEYLEAHPELRPVVVIDNYLHNASESSVVYDKITEWAAGLTAGNIAHVIFLTTDVSYAKPLSKALPNSVFRTITLGDCSLEVGRKFVVNHLAYESKDGKTQPRRAEELEDLDACIETLGGRVTDLEFMAHRIEAGETPRGAVNRIIEQSASEILKMFLLTPETIEQSWTHEQAWYLIKRLAESKDGALSYNEIVLSELFKENGEITLRALEHAELISIAAVNGCPQTIRPGKPVLRAAFKKVTENKALSSRMDLAIITQKINKENKSIGKYEEELSLLGSLPRQPRELTDRIQWVLNKVYSSQNKIAKYEKESAYLQKILRSEH
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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Q873L8
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MISAHILSRQATRPGHRGPRFTTHSTALLVQRSLGQGLPLAHRRTTRAWESTSSSTASTGSHKESGHIETAPHESLLFFNNLFPLKLSSILIWRPWTSEDLLQRFEQSSYSFIDPIRLVKRAINTHDQVPIEVTQIIPRLKDGGAFVKFTHPSDMSAAVVESKLSELLQNNPIKPWFNPFGRVKAGLVEGVPWLEDLYRLPRSRIRVEFVAAKDDASPAELSQETLYSIFRKFGKITEITSQPTDSKVLPRFAYIDFVLVRDAIMARNCMHGFVLREQGSKNATKLRLSYEQRVKAHHIWAWFTSHPRIVIPLVAALIAAFTVAVFDPIREFFVKAHVQKYFEFTNSRLYKWFKSQTSDILAFRRRKTEDAGLNALFTHRKDLIDSIQTGLLESVDTFTVVHGPRGSGKKELILDQVLKERSNVLHIDCKPVVEARGEAGTIGRLAFEVGYRPVFSWSNNISSLVDLAVQSTTGVKANFSENLESQVVKILQTTASALKQVGLSERKKEDKDADLSEDAYLEAHPERRPVIVIDHFLHKSEEKGVIYDRIADWAAALVQSNIAHVIFLTDDASYSKPLQRSLPDRVFRSVTLGDLSPDVAKKFVISQLQTDTKFAHDGQQKDSESGDQDNDNKNQKKDSNTPAPLDPTLLKELDTCITALGGRLTDLQVLARRLKIGQSPRKAVQEIIDSTASDILRMFLLSKSSTSDRKYTTEQAWYLISHLAASPSSSIPYNSVLLSNTFASSPETALEALANAELITVKSQNGMPSEIKAGKPVYQAAFQKLASDEKVKARMDLLVLTELAKMETQKIEKVEQELVMLQGLMARRPGDVSERVEYLLEKMKGGQARLKGLEKEMGVVKGQMVKG
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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Q0V3D6
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MRVEDHCSVFAWSSLQASRPWPAAGRYASLQAGEDKTGHISAGPNEGILFFNNVFPIQIRKIMGLPMPRILDRLISPAMSGTDPNTVIQRAKAKRNLPIESTEILPRVREGGAFVKFTHDGSTPTSEIEKTLQEYLRDEPVKPWWSPWKRMRAKVVKGRPWVEDMMRLPAPRLRVEFVPGEPGASVTEAVDLSQEQLFQFFRPYGKLSDIVMQESDSKVLPKFAYLDYSSIGKAIMAKNCMHGYLVSEAEGGGKKGTFLRLKYEQKIKPRYIRDWIINHPRIIIPIIAALIAGTVAIVFDPIRTFFVKAHITRTLHLEDNKWYKWIKGYASDIIRGHKRDEDDSYDAIWDDRKGNIEQIQTWLMETADTFIIVQGPRGSGKKELVVDQALQDNKLKLVIDCKPIQEARGDSPTISAAAAAVGYKPVFSWMNSISGMIDMAAQGATGMKTGFSETQETQLNKIWNTTTTALKQIALERRHKDDRDANLADDDWLEAHPEHRPVVVIDNFLHKSHEGGIVYDKMAEWAARLTTTNIAHVIFLTNDVAFSKSLSKALPDRVFRQISLSDCSPDVAKKFVVTHLDADVEDDPAPKDGSEKKLPSQHRTDLAELDSCIDLLGGRLTDLEFLARRIKTGETPNKAVNEIIDQSASEILKMYIFGAEDDGGRRKWSPEQAWMLIKELAQKESLRYNEVLLDDILKTGGESALRDLEQAELISIISGPNGRPSTIRPGKPVYHSAFKRLAQDKVLKSHLDYAILTNLTKIENATIDKCENELLLLSKLRNQPAQTAGRVQYLLAKLSASQVKVEKYETEIKGLKKVMAEED
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A5DAI1
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MIRTFATIANRGPGIRLATLAASRNLGYSSGGRISSVRIEKLRFSPFRSSTSLRYTSDIQHVMQEADSLDVNNSVSNTGVLDYDRKNAVVLYFDHIYPFSVSRYSWKQYFTLLFPVNRCSEDDIRERVMNLSSTEKEPLPKDVRILELVPMRRDGGVFVKFQLPATMSARELVGLICQNTKENEQAYGERFLVGPLNKIWNHFPRCFQVKGTPWIEDLRRFPSVKLSVKFEGERLTEEELYVLFRRYGLIIDIAPGSGTEPAVIHFRKIRSAICAKNCVTGITLNSGNTVVHIQYLPLKRVNYITDFIGNHQRIAIPIILALLATAAVFIFDPIREWFIMQNVSHRHALDSYKDNKFLKLVSLPYEQVRRWIDSGYDYFDSKFGCDEEDEFGGEKGEAPNDLWSERYEKVKQLKLWIYENINTFIIVRGPKGSGKEELVLEHTLRDDPILGNKLLYIDCEALVKSRSDNALIEATAQQLGYFPVFTWTNSISQFVDLGVQGLTGQKSGLSESKETQLKNMFGLTSSAIRKLALQDYAKYKKSVLRQRRRQQGDSTSEDILSEDEYLSQHPERKPVIVIDKFAGRADGDQDFIFKMISEWSAQLVQSNLAHVIILTHDVGSMSHLTSALPNQVMKSISLSDASQRSARHYVLNQLNKESQAQVNELDSCLEPLGGRMLDLQAFVRRMRSGEAPGDALEEMVSQASEQITTFFLSASSTQNSWSTAQVWLLIKLLAKQESISYETLCHDPLFKSPDSLSILSTLEKHDLISLISDKGVLNTVSTGRPLYKAAFRSLVEDPKIFRIYEEDLYNKLIALENAKIAKLEDEFAKLASVDARLVRNRLDYVSNKIVASTDKITDYEEKISGLSSKKSSWF
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A3M0D8
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MISSSRVAAMALRQSSRAIVPLAVLSSNGLRSRYFTPGLAHKTQIRTVTSDIAEIKQEIDKDESDNSAETTGVIDVKNQHEVVLYYDHIYFLGASSPAYFNVFLQFLRIRKQTPAQIRDKILKVSAPIPAEAEITQLIPFMRDCGAFAKFQVPPGVEVAEFVQQIRQNVVHNEKAYNSGIFRRVLSLFWSHYPAVYSVKGTPWIEDLRRYPNTKLKVKFEGEPLTEEELYVLFRRYGPLVDIIPGPESAEATLIYRGLRSAIAAKNCITGVSLNKGRTVLHLQYIPIKRVNYITEFVTNHQRIAIPIILALLATLAVLIFDPIRQYFIEVKITKRYSFDTYKDYAVVKTITKPLRVVHNWLSSSYDYIDKKIDSISSPGTASDEKSDDSDVSQALQTASTIWNERSEKSKQIKMWIYENVNTFIIVKGPKGSGKEEFILDHTLLNDEKLRHKILYINCSELAKARSDNDLLKSTANQLGYFPLFTWTNTVSQFVDLGVQGLTGQKSGLSESKETQLKNMFTLTSQAIRSIATRDYQKYHASVTRKNNRLPEGENIEILKEEEYLQQHPECKPIVVIDKFNRKADAASNDFVYPMIAEWSSVLVQNNLAHVIYVTSDVGSIQHLNNALPNQVFKSISLSDASSFSAKSFLMHQLKLEDDHTISGAFEPLGGRMLDLQAFVRRINSGETPPEALEEMVNQASEQVTTFFLCAHKIDDDTNWNAAQVWMLMKLLSKSDSINYSDLNKSPLFKPEEDTVATLTTLEKHDLISLQRDKGILDKISIGRPLFKAAFKQLISDPKISKLYEVDYISTLIKIENEKIKKFEGELISIQKLGDKLGSRVLYLSKKIDASNAKVVEYEGKIAEINSKPASKNFLKLF
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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O94689
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MNLFLSRFTGLRNTSFLGHARPFMFPRRYAHSLVAHNIGHIKLDPNEGLFFVDNLVNTPTYFYIQRYTALLFQNNLKKQLSAAFPSSDTMQLEDIIFRWQDGGAFLKVRYKEFPQDTEAVSEHVRESFRKRPVRTILHPFSTPIPHMVHGIPWLQDLYIFPSRTVDVNFEGPPLSQERLYSIFRTYGKLRSVTINSPTSATLSFSSLRSATSALNCMHGFVYGKTEFHMRYRHMNRFVAFKDWLFSHPRFTIPLVAAAITVLTASLFDPIRKFFVETNIVHGQKLRNINVVGWVKKKTRDIVLSPFHENGTNIKAPIWTTREKDCEQLKEWLDEALHSFIVVQGPRGSGKRDLVDRVVKERKNVLFFDCDRLFSTTNTEMFVSTLASQTGYFPLFSFLNNISSLIDMAAQGLIGQKTGIVSSSEGQVRQILNTTQTVLRSLALREHKEADTSVLDESEFLEVHADRLPVVILDNFQLRKLSNPMQRVVAEWAGNLVKEGIAHVLMLTPDVGGTKSLEQYVNGWENRTLLLGDADPVLAQRYVIESLPEEMQTEELRKELRVQLPKIGGRLRDLDYVARRLRVNSSSVSEAIGGIVSQNASDILQTFLRPASLTSEEKPTFTPEESWTLITYLSQHEYIPYHMLMLDPLFKGHDDAVRALEESELITITTVNARPDKVYAGKPVYVTAFRQLVNDPVLSANMQLVRCNALIGMANNAIKNDEQELQMLKDLGNLESGVKDRAHYLTTRIQKNQGVITDNEKSIERLTEALKKID
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A7TML0
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MYRSGLLTSGGGSAALTALRAIGSRSSLSNGKFIWNVGKRFITSEIQEKDQQAGESNTATDTGIIHKTEQETLVYFDNVYPRDTSLWNPAQWYNLLLVNQSREAVRDKITEFASPPSNPIHGLELRSTIPVKRDGGVFATFLVPSKYTKAEVNAIIQKNTAEESSKSIFSFFTRASAFPVKGFPWIEDLRRLPTNTIKVLFQGPPLTEEEIYSLFRRYGTIIDIVPASDSVKNASVRYKSLKGAICAKNCVSGIEIHNTVLHIQYQQEARNFVISNFFVNHTRIAIPVMLAVLSIIAVLIFDPIREFSIEQKITHIYSLSWDNYWIRQIRNFTNSTVTSFRNYWGVNENAFAEKHLWEERIEKVNDLKMWLQENNNTFVVVRGPRGSGKNELIMQHTVGDRTNVLYLDCDKLIKSRTDAKFLRNAASQLGYFPIFPWINSVTSVIDLMVQGLTGQKSGLSETKEAQFRTMLTTALTSIRRIALKGYKSVIVDGGEDVNVKEEDYLQQHPEAKPIIVIDRYEGKSEINGFIYKELADWASMLVQMNVAHVIFLTETVSSNQQLSESLPNQVFKTLVLSDASKENSRKYVLSQLQSFVDSKQKSKEDIKITENIEAEKSKITDQIDDALEPLGGRMLDLQAFVRRVKSGEQPTEALDKMIEQASEQITQIFLSDKVDGIKSAQAWELIELLSAKSVVSYDDIVFKPLFKAAPELGIVELENSGLITVSRNRGVLDKIRPAKPLYKAAFYYLVNSQELSTILRTRYLLKVITFETGRIKKWEDELRPLGKSGDPKLFRGRFEYLSGKIETSNKVIVASEAEIKALSERKQNQK
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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A6ZN18
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MLLVRTTSLNVSRMPVPCLARGIGILKGKYRLANLMNAQPSVRHVSSEIQQKDQQAGESNTATDTGVIHKSDEETLIYFDNVYARATSVWNPTLWYNLLLRNQSRDAVREKIRNLASPPNNPIYGLELKSTIPVKRDGGVFATFVVPPKYTKAQVNSLIQQNTARESSKNLLSYFTRVSAFPVKGSPWIEDLRRLPSTTIVIKFQGPALTEEEIYSLFRRYGTIIDIFPPTAANNNVAKVRYRSFRGAISAKNCVSGIEIHNTVLHIQYENIIRGHLVSNFFTNHTRIAIPVLFALLSIFAVLVFDPIREFSIEQKITHKYSLSWDNKFWKQLKTLTSSTMTSIKYYWGGPDDNHQRKHLWEERIEKVNDLKMWLEENNNTFVVIRGPRGSGKHDLVMQHTLQNRANVLYLDCDKLIKSRTDPKFLKNAASQLGYFPIFPWIDSVTGVLDLTVQGLTGQKTGLSETKESQFRNMLTTSLMSIRRIALKNYKAFVSTGDGTVNVKEEDYLQQHPEAKPVIVIDRFEGKSEINGFVYKELSDWAAMLVQMNIAHVIFLTETVASNQRLSESLPNQVFKNLILSDASKENSRNYVLSQLEDYLYYNKKSKGENVKEPESEKEIAENNDSDSEADTSVKEAEVILNEKELQEIDASLEPLGGRMLDLQAFVRRVKSGEEPSEALDKMIEQASEQITQMFLSDKIDSNKSAQAWELIELLSANPVIPFREIVNKPLFKAAPETGIMELENNGLITVSRDRGVLQEIRPAKPLYRAAFTYLINDPELAKVLKTRYLLKVVGFETGRIKKWEEELKPLGKVPDQKLFKTRLDYLSGKINASNAVITKCEEEIKNLSK
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). Belongs to the YME2 family.
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D6W0C9
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MLLVRTTSLNVSRMPVPCLARGIGILKGKYRLANLMNAQPSVRHVSSEIQQKDQQAGESNTATDTGVIHKSDEETLIYFDNVYARTTSVWNPTLWYNLLLRNQSRDAVREKIRNLASPPNNPIYGLELKSTIPVKRDGGVFATFVVPPKYTKAQVNSLIQQNTARESSKNLLSYFTRASAFPVKGSPWIEDLRRLPSTTIVIKFQGPALTEEEIYSLFRRYGTIIDIFPPTAANNNVAKVRYRSFRGAISAKNCVSGIEIHNTVLHIQYENIRRGHLVSNFFTNHTRIAIPVLFALLSIFAVLVFDPIREFSIEQKITHKYSLSWDNKFWKQLKTLTSSTMTSIKYYWGGPDDNHQRKHLWEERIEKVNDLKMWLEENNNTFVVIRGPRGSGKHDLVMQHTLQNRANVLYLDCDKLIKSRTDPMFLKNAASQLGYFPIFPWIDSVTGVLDLTVQGLTGQKTGLSETKESRFRNMLTTSLMSIRRIALKNYKAFVSTGDGTVNVKEEDYLQQHPEAKPVIVIDRFEGKSEINGFVYKELSDWAAMLVQMNIAHVIFLTETVASNQRLSESLPNQVFKNLILSDASKENSRNYVLSQLEDYLYYNKKSKGENVKEPESEKETAENNDSDSEADTSVKKAEVILNEKELQEIDASLEPLGGRMLDLQAFVRRVKSGEEPSEAVDKMIEQASEQITQMFLSDKIDSNKSAQAWELIELLSANPVIPFHEIVNKPLFKAAPETGIMELENNGLITVSRDRGVLQEIRPAKPLYRAAFTYLINDPELAKVLKTRYLLKVVGFETGRIKKWEEELKPLGKVPDQKLFKTRLDYLSGKINASNAVITKCEEEIKNLSK
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Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA. Present with 5260 molecules/cell in log phase SD medium. Belongs to the YME2 family.
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Q9CG85
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MTIINLKNINLTRNKKEILKDITWKVNPGENWVILGLNGSGKSSLLKLILAEEWKTSGEITVLNTQFGNGEIPKLRKRISVVGSFIAERFQPNIKAENLVYTGKFNSSMLYKPYTDQELDEARQLLRQMGAKSLIGRNYASLSQGEKQVLLIARSLILKPELLILDEATNGLDLFAKEKLLKQLQQINQLKTAPTLIYISHHPDEITDIFTHLLLLREGKVIQSGKKENLLNEKILTDFYQEKVEVHRFEQKYFVIPAN
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Belongs to the ABC transporter superfamily.
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Q9W1Y0
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MFSTTTHSVPYLYLGNFSRKPHYYSVNRTKLHGSAGAARLSKSTSTSSRSHDLVLDLRNLLSRSSASIQGMVERAARLNGILDRRLVDDVLAKVTSMLPSMRDVRVTLEESATQIGRVQLQNYQFEVSLTGAAGSVPTGANVKVIPTITPGLLRPLFSQQQLNQIRGFKTDRSIEAEQKRNPTMTSRLKNALANSPQRLDGDTPLQAEKLRRLLAKSEEHGFNKAESLKIAFAEGYLAAANSEDSPKSGKTMKYLKTLQTIVVIVVFLGIFLSFFTTSNGSVFRSIQLGNQVEVDPEEINVTFEDVKGCDEAKQELKEVVEFLKSPEKFSNLGGKLPKGVLLVGPPGTGKTLLARAVAGEAKVPFFHAAGPEFDEVLVGQGARRVRDLFKAAKARAPCVIFIDEIDSVGAKRTNSVLHPYANQTINQLLSEMDGFHQNAGVIVLGATNRRDDLDQALLRPGRFDVEVMVSTPDFTGRKEILSLYLTKILHDEIDLDMLARGTSGFTGADLENMINQAALRAAIDGAETVSMKHLETARDKVLMGPERKARLPDEEANTITAYHEGGHAIVAFYTKESHPLHKVTIMPRGPSLGHTAYIPEKERYHVTKAQLLAMMDTMMGGRAAEELVFGTDKITSGASSDLKQATSIATHMVRDWGMSDKVGLRTIEASKGLGTGDTLGPNTIEAVDAEIKRILSDSYERAKAILRKHTREHKALAEALLKYETLDADDIKAILNESQT
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ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:26160069). Plays an important role in regulating mitochondrial morphology and function by cleaving Opa1, giving rise to a form of Opa1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:31125351). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (PubMed:26160069, PubMed:31125351). Required to control the accumulation of nonassembled respiratory chain subunits such as ND-30 (PubMed:26160069). Binds 1 zinc ion per subunit. Viable but lifespan is reduced and males are sterile. Mitochondrial proteostasis is disrupted leading to crista disorganization, mitochondrial unfolded protein stress and impaired complex I activity which increases levels of reactive oxygen species (ROS). These defects all likely contribute to the increase in Dronc-mediated apoptosis in neuromuscular tissue. The severity of the mitochondrial abnormalities and their resulting phenotypes increase with age, resulting in the progressive degeneration of photoreceptor neurons and locomotor activity and increased sensitivity to genetic and environmental stresses. In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.
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Q9UMR9
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MFSLSSTVQPQVTVPLSHLINAFHTPKNTSVSLSGVSVSQNQHRDVVPEHEAPSSECMFSDFLTKLNIVSIGKGKIFEGYRSMFMEPAKRMKKSLDTTDNWHIRPEPFSLSIPPSLNLRDLGLSELKIGQIDQLVENLLPGFCKGKNISSHWHTSHVSAQSFFENKYGNLDIFSTLRSSCLYRHHSRALQSICSDLQYWPVFIQSRGFKTLKSRTRRLQSTSERLAETQNIAPSFVKGFLLRDRGSDVESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
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ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:26923599, PubMed:27786171). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:18076378, PubMed:26923599, PubMed:27495975). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (PubMed:22262461). Required for normal, constitutive degradation of PRELID1 (PubMed:27495975). Catalyzes the degradation of OMA1 in response to membrane depolarization (PubMed:26923599). Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (PubMed:22262461). Binds 1 zinc ion per subunit. Homohexamer; may also form heterohexamers (PubMed:27786171). Exists in several complexes of 600-1100 kDa (PubMed:22262461, PubMed:27495975). Interacts with AFG1L (PubMed:26759378). High expression in cardiac and skeletal muscle mitochondria. Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. The disease may be caused by variants affecting the gene represented in this entry. Mutagenesis of Glu-543 to Gln does not complement excessive accumulation of subunits (NDUFB6, COX4,ND1) due to YME1 deletion mutant. Probably has no ATPase activity. In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.
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Q7TNN5
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MFSLSSTVQPQVTIPLSHLINAFHSPKNISVSVNTPVSQKQHRDTVPEHEAPSSEPVLNLRDLGLSELKIGQIDKMVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLRSICSDLQYFPVFIQSRGFKTLKSRTRRLQSTSERLVEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDKSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRESYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
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ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (By similarity). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure (PubMed:17709429, PubMed:24616225, PubMed:26785494, PubMed:27495975). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (By similarity). Required for normal, constitutive degradation of PRELID1 (PubMed:26785494). Catalyzes the degradation of OMA1 in response to membrane depolarization. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (By similarity). Binds 1 zinc ion per subunit. Homohexamer; may also form heterohexamers. Exists in several complexes of 600-1100 kDa. Interacts with AFG1L. Detected in heart and skeletal muscle (at protein level). Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. Complete embryonic lethality; embryos present a clear developmental delay at 8.5 dpc, and the hearts of mutant embryos fail to beat properly at 9.5 and 10.5 dpc. Cardiomyocyte-specific gene disruption gives rise to animals that develop dilated cardiomyopathy and myocardial fibrosis at about 20 weeks after birth; mutants have a median life span of about 46 weeks, much shorter than wild-type. Mitochondria from mutant cardiomyocytes are smaller than normal, but have normal cristae architecture and display no significant difference in the assembly of respiratory complexes. Keeping mice with a cardiomyocyte-specific gene disruption on a high-fat diet leads to weight gain and reduced glucose tolerance, and prevents the development of cardiomyopathy. Mice with Yme1l gene disruption in cardiomyocytes and skeletal muscle have a median life span of 125 weeks, similar to wild-type. Their heart function is normal, in spite of the presence of fragmented mitochondria due to the loss of Opa1 cleavage at position S2. Skeletal muscle mitochondrial dysfunction is known to be associated with impaired insulin signaling and glucose intolerance, and as expected, these mice display impaired glucose homeostasis with decreased fasting insulin levels in the blood serum and glucose intolerance. Mice with a double, cardiomyocyte-specific gene disruption of Yme1l and Oma1 have normal cardiac function and do not display myocardial fibrosis. Likewise, cardiomyocyte mitochondria have normal morphology. Mice with a skeletal muscle Yme1l gene disruption plus a double, cardiomyocyte-specific gene disruption of Yme1l and Oma1 display normal glucose tolerance. In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.
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Q925S8
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MFSLSSTVQPQVTVPLSHLINAFHSPKNISVSVNTSASPKQHRDTVAEHEAPSSEPVLNLRDLGLSELKIGQIDKLVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLQSICSDLQNFPVFIQSRGFKTLKSRTRRLQSTSERLAEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIEFPMHPYSRQTIIQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDKSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNEIRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRESYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
|
ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (By similarity). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure (By similarity). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (By similarity). Required for normal, constitutive degradation of PRELID1 (By similarity). Catalyzes the degradation of OMA1 in response to membrane depolarization. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (By similarity). Binds 1 zinc ion per subunit. Homohexamer; may also form heterohexamers. Exists in several complexes of 600-1100 kDa. Interacts with AFG1L. Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.
|
P53826
|
MVIYYGKKNCTLLLLLFILCNIYSGSNILLISCSFFFLVSGTSIQLNIINANRQAANMYPSLKSILDTIIGVKSDIKKLNIQLINVQIAIDMALVLRGNNSDTSTNVTGPNVIANQKIKQQVTIIKTIFEKSVSLPNVPTVAYVII
|
Partially overlaps HXT14. 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.
|
D6W0M6
|
MLWKVSKMFLGGLVALTTISVATLYHYQNRLVYPSWAQGARNHVDTPDSRGIPYEKLTLITQDHIKLEAWDIKNENSTSTVLILCPNAGNIGYFILIIDIFYRQFGMSVFIYSYRGYGNSEGSPSEKGLKLDADCVISHLSTDSFHSKRKLVLYGRSLGGANALYIASKFRDLCDGVILENTFLSIRKVIPYIFPLLKRFTLLCHEIWNSEGLMGSCSSETPFLFLSGLKDEIVPPFHMRKLYETCPSSNKKIFEFPLGSHNDTIIQDGYWDIIRDFLIEKGFI
|
Present with 259 molecules/cell in log phase SD medium. To S.pombe bem46 and M.tuberculosis Rv2307c.
|
P53825
|
MNPRRPYPVIFLCRPSSVASSKLASTFMISFLVKKTLSSNTVNSPRGTVRSISRIRNMVSLLLLPTIYIRSLVSYNVYLPITNLEVFLCLDPDVVSIPPPRVCSIASLFILVLFLFCFALRYYVSKLINFK
|
Partially overlaps FIG4. 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.
|
P0C5Q8
|
MSLFCLPLEMRNHWHFFSLFTNLPRKSKWHRASEFFFPLLMSEIEDFR
|
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.
|
O94511
|
MSITLSSRGRKIRKLPKSLEFPLDGSIDKLRDEVSSVTRLPVERLRFSTADGTTLLPNTTLRKYGVGPGATIWVKDLGPQIGWRTVFMIEYLGPLVIHLFFILNYKWIYRKDYNLCLNQKIAFVLVMLHFMKREYESIFVHRFSLATMPLRNIFKNCAHYHLLSGLFLAYFIYGPWHANDYIKPNHLLFLIVGWAFAVLSNFRTHIILRDLRPAGSKKRVIPTGYGFNLVSFPNYFFESLGWLFFALLTKSWASWIFLFVGSAQMFVWAKKKHARYLKEFPNYPRSRKIMIPFFL
|
a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA + NADP(+) Belongs to the steroid 5-alpha reductase family.
|
E9PAG2
|
MHGTCLSGLYPVPFTHNSHDYPHFNIYISFGGPKYCITALNTYVTPLLHRILTTQFIYTYANITKKSPLKSPKHKNILFFNHNT
|
Contained within a telomeric X element core sequence. Belongs to the UPF0320 family. 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.
|
P53820
|
MSLRPCLTPSSMQYSDIYIPTPTPTHHTHTPTPHPHPHTHTHTHHNPNPTLF
|
Completely overlaps TEL14L-XC, a telomeric X element core sequence on the left arm of chromosome XIV. 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.
|
P58016
|
MRSMAKKGLEEVLETLDRIIHDETVPRNVRRVASEIKEKLTTTDEVSLEAASAISVLEDISADPNLPMHVRTMIWNLTSQLERISVE
|
Belongs to the UPF0147 family.
|
P53717
|
MVFTSSESSSLLSSLKMTCSMVSMNSLEQISLIKGVPPFFTHILVSFQEDNWVFGLSAVLRILFFIQRIESLGFTLLDLNTSEISNAMGRSRSPLGMLSLVACSINASNSLGVLTDILFLVLYSLLIHLSKKKS
|
Almost completely overlaps VPS27. 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.
|
D6W1I9
|
MSSTDIKPCAVNIPVSAHITFHYKSIADRSSSRSSSSSSCSSATSKACSPRGSSVGLPPALSTDNEIVETVLNVSAPVVADPTRPSLFKSNYTAASCLTSDPTSPSLLPSSRRNSVLPASDFHQCAHHKNFQRRASEPQLPSFDNRSSSEMKRSVSYAQHSMMFPISDQQEPQTSASPNDHSDPSCPCNRHHHRRNSVAVKFDKPLYERLET
|
Present with 2360 molecules/cell in log phase SD medium.
|
D6W1J6
|
MSSSIFGPLTGFLERVNSLNAPYQALSYDEQKAMTIWQRVKFYNWTFELCALGVLFLVYAFYKFGNSVNLKRGNQIFQSLHSFLANDLKFSRVGFNINDSKIFTVEHQNTWFSSFATGRSAIKSINLNLHLVARSNPFSMCLEYLLGFFFASLKSKQLEEFMEIVIRPNGILVTSESAHPNKNAHEILTKFRFVTSIVNKEFMNQARTENYFLSIAHTSENDKLPNNFVYMSDVNQLSGFMFHYSKPYEVLSQAGNLLKYISFTDLPVNPPRDDKEWESSIEPKAIIRCAVPQNENELKLLNQIISLVVEIYDGFTQDLVQQSPNLFITNDILKRTTNLRQQELNKIKKFMKETELELAKEKKLELEKAKRRQLKASGQQEKVDQKMKEKRERRLKNKQRTRFQ
|
Present with 34906 molecules/cell in log phase SD medium. Belongs to the UPF0674 family.
|
Q9P791
|
MSQDQKPKVLEVSNLENQDAKWTSLKKIRWQDEKGKIRFWEMAERTTRSEANVDAVAILAIVPIDGSPHVLCQKQFRPPIGKFCIEIPAGLVDSKESCEDAAIRELREETGYVGTVMDSTTVMYNDPGLTNANLKIILADIDMSKPENQNPQQQLDDGEYIENFPIKLSSLQEELFSLEKKGFAIDVRLSTFALGLHAGLKYLSS
|
Belongs to the Nudix hydrolase family.
|
B4TVG8
|
MKKPLLLTLLCMILAGCDNPKSLESFTPEMASFSNEFDFDPLRGPVKDFSQTLMSENGEVAKQVTGTLSQEGCFDTLELHDLENNTGLALVLDANYYRDAQTLEKKVQLQGKCQLAALPSAGVTWETDDNGFVVSATGKEMKVEYRYDSEGYPLGKTTINSQNTLSVTAKPSADPRKKLDYTAVSRVDDRQVGNVTQSCEYDAYANPVDCRLVIVDESVKPAVSHHYTIKNRIDYY
|
Belongs to the UPF0257 family.
|
Q8Z6Z0
|
MKKPLLLTLLCMILAGCDNPKSPESFTPEMASFSNEFDFDPLRGPVKDFSQTLMSENGEVAKQVTGTLSQEGCFDTLELHDLENNTGLALVLDANYYRDAQTLEKKVQLQGKCQLAALPSAGVTWETDDNGFVVSATGKEMKVEYRYDSEGYPLGKTTINSQNTLSVTAKLSTDSRKKLDYTAVSRVDDRQVGNVTQSCEYDAYANPVDCRLVIVDESVKPAVSHHYTIKNRIDYY
|
Belongs to the UPF0257 family.
|
Q8ZPJ4
|
MKKPLLLTLLCMILAGCDNPKSLESFTPEMASFSNEFDFDPLRGPVKDFSQTLMSENGEVAKQVTGTLSQEGCFDTLELHDLENNTGLALVLDANYYRDAQTLEKKVQLQGKCQLAALPSAGVTWETDDNGFVVSATGKEMKVEYRYDSEGYPLGKTTINSQNTLSVTAKPSADPRKKLDYTAVSRVDDRQVGNVTQSCEYDAYANPVDCRLVIVDESVKPAVSHHYTIKNRIDYY
|
Belongs to the UPF0257 family.
|
P76171
|
MKYKLLPCLLAIFLTGCDRTEVTLSFTPEMASFSNEFDFDPLRGPVKDFTQTLMDEQGEVTKRVSGTLSEEGCFDSLELLDLENNTVVALVLDANYYRDAETLEKRVRLQGKCQLAELPSAGVSWETDDNGFVIKASSKQMQMEYRYDDQGYPLGKTTKSNDKTLSVSATPSTDPIKKLDYTAVTLLNNQRVGNVKQSCEYDSHANPVDCQLIIVDEGVKPAVERVYTIKNTIDYY
|
Belongs to the UPF0257 family. Extended N-terminus. Extended N-terminus.
|
P77291
|
MSKNERMVGISRRTLVKSTAIGSLALAAGGFSLPFTLRNAAAAVQQAREKVVWGACSVNCGSRCALRLHVKDNEVTWVETDNTGSDEYGNHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERISWDEALDTIASSLKKTVEQYGNEAVYIQYSSGIVGGNMTRSSPSASAVKRLMNCYGGSLNQYGSYSTAQISCAMPYTYGSNDGNSTTDIENSKLVVMFGNNPAETRMSGGGITYLLEKAREKSNAKMIVIDPRYTDTAAGREDEWLPIRPGTDAALVAGIAWVLINENLVDQPFLDKYCVGYDEKTLPADAPKNGHYKAYILGEGDDKTAKTPQWASQITGIPEDRIIKLAREIGTAKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGISGGNSGARESTYTITIERLPVLDNPVKTSISCFSWTDAIDHGPQMTAIRDGVRGKDKLDVPIKFIWNYAGNTLVNQHSDINKTHEILQDESKCEMIVVIENFMTSSAKYADILLPDLMTVEQEDIIPNDYAGNMGYLIFLQPVTSEKFERKPIYWILSEVAKRLGPDVYQKFTEGRTQEQWLQHLYAKMLAKDPALPSYDELKKMGIYKRKDPNGHFVAYKAFRDDPEANPLKTPSGKIEIYSSRLAEIARTWELEKDEVISPLPVYASTFEGWNSPERRTFPLQLFGFHYKSRTHSTYGNIDLLKAACRQEVWINPIDAQKRGIANGDMVRVFNHRGEVRLPAKVTPRILPGVSAMGQGAWHEANMSGDKIDHGGCVNTLTTLRPSPLAKGNPQHTNLVEIEKI
|
Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. Binds 1 [4Fe-4S] cluster. Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit. Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
|
P77783
|
MKIHTTEALMKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAEAPVEEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLAKIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV
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Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. Binds 1 [4Fe-4S] cluster. Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit. The complex consists of three subunits: YnfF, the reductase; YnfG, an electron transfer protein, and YnfH, a membrane anchor protein. Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Can also be exported by the Sec system. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
|
P77313
|
MTTQYGFFIDSSRCTGCKTCELACKDFKDLGPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCDDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNAEKGHMTKCDGCYSRVAEGKQPICVESCPLRALEFGPIEELRQKHGTLAAVAPLPRAHFTKPNIVIKPNANSRPTGDTTGYLANPEEV
|
Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. Binds 4 [4Fe-4S] clusters. The complex consists of three subunits: YnfF, the reductase; YnfG, an electron transfer protein, and YnfH, a membrane anchor protein.
|
P77142
|
MGNGWHEWPLVIFTVLGQCVVGALIVSGIGWFAAKNDADRQRIVRGMFFLWLLMGVGFIASVMHLGSPLRAFNSLNRIGASGLSNEIAAGSIFFAVGGLWWLVAVIGKMPQALGKLWLLFSMALGVIFVWMMTCVYQIDTVPTWHNGYTTLAFFLTVLLSGPILAAAILRAARVTFNTTPFAIISVLALIACAGVIVLQGLSLASIHSSVQQASALVPDYASLQVWRVVLLCAGLGCWLCPLIRRREPHVAGLILGLILILGGEMIGRVLFYGLHMTVGMAIAG
|
Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. The C subunit anchors the other two subunits to the membrane and stabilize the catalytic subunits (By similarity). The complex consists of three subunits: YnfF, the reductase; YnfG, an electron transfer protein, and YnfH, a membrane anchor protein. Cells grow to slightly higher density than wild-type in sublethal levels of streptomycin (PubMed:25316676). Belongs to the DmsC family.
|
P77559
|
MNIELRHLRYFVAVAEELHFGRAAARLNISQPPLSQQIQALEQQIGARLLARTNRSVLLTAAGKQFLADSRQILSMVDDAAARAERLHQGEAGELRIGFTSSAPFIRAVSDTLSLFRRDYPDVHLQTREMNTREQIAPLIEGTLDMGLLRNTALPESLEHAVIVHEPLMAMIPHDHPLANNPNVTLAELAKEPFVFFDPHVGTGLYDDILGLMRRYHLTPVITQEVGEAMTIIGLVSAGLGVSILPASFKRVQLNEMRWVPIAEEDAVSEMWLVWPKHHEQSPAARNFRIHLLNALR
|
Belongs to the LysR transcriptional regulatory family.
|
P77705
|
MSRTTTVDGAPASDTDKQSISQPNQFIKRGTPQFMRVTLALFSAGLATFALLYCVQPILPVLSQEFGLTPANSSISLSISTAMLAIGLLFTGPLSDAIGRKPVMVTALLLASICTLLSTMMTSWHGILIMRALIGLSLSGVAAVGMTYLSEEIHPSFVAFSMGLYISGNSIGGMSGRLISGVFTDFFNWRIALAAIGCFALASALMFWKILPESRHFRPTSLRPKTLFINFRLHWRDRGLPLLFAEGFLLMGSFVTLFNYIGYRLMLSPWHVSQAVVGLLSLAYLTGTWSSPKAGTMTTRYGRGPVMLFSTGVMLFGLLMTLFSSLWLIFAGMLLFSAGFFAAHSVASSWIGPRAKRAKGQASSLYLFSYYLGSSIAGTLGGVFWHNYGWNGVGAFIALMLVIALLVGTRLHRRLHA
|
Belongs to the major facilitator superfamily.
|
Q2MB89
|
MREYPNGEKTHLTVMAAGFPSLTGDHKVIYVAADRHVTSEEILEAAIRLLS
|
Transiently induced by cold shock.
|
A0A385XN87
|
MTIEKHERSTKDLVKAAVSGWLGTALEFMDFKSHAC
|
Expressed at low levels in stationary phase (at protein level).
|
A0A385XJI0
|
MTNHIHFRCPCCHGSQYRTSSFDVSDMNPFGAKCIFCKSMMITFDNISQYLNASRLSLDLKK
|
By cold shock, 10 degrees Celsius (at protein level). Probably uses the non-canonical initiation codon AUU, which may limit its expression (PubMed:28861998). Part of the Qin prophage (Probable). Belongs to the YmcF/YnqF peptide family.
|
A0A385XJU6
|
MKAPSGAFLLGVYSMDTHILR
|
By cold shock (at protein level).
|
A0A385XJJ6
|
MNNPVCLDDWLIGFKSLCCTLAVIALLII
|
Expressed in both exponential and stationary phase; expression is considerably higher during stationary phase (at protein level). Encoded in the Qin prophage.
|
Q8TGL6
|
MNNIIDSSKYRLNRCIPSVFGDTNTPHITSSMIIDVLYVGKIYERCRLGCRTRTQGMFRVVLNAQLNIQ
|
Completely overlaps LEU9. 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.
|
D6W1W4
|
MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY
|
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-OL 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.
|
D6W1W3
|
MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
|
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 YOL103W-A ORF.
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Q08521
|
MFNLSTYYNHTRNTQKQLLEYFERRPIWMYNPFFALFLRYVIDSFKVLSRQSKYFPVRFDSIGIHRFWQDNITSLDVPANNNVSGLNVIFLRNFKDNRFLQ
|
Almost completely overlaps GCY1. 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.
|
Q99209
|
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPETY
|
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-PR2 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.
|
D6W2J9
|
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNSNKRIIAKLKMQYDTKIINLGESDDEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPNGRKLGAPGQPGLYINQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
|
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 YOR142W-A ORF.
|
P42547
|
MARSKKGKNLIYVLLGLVGLLAFFVLFVPTLTISASTPVWLENTITYATSFRDAFNVSGMVYMVILLGVLIAYLLLKYSKTRQNKDALKVVLAVVIAFAVYLLFTPALAAAFSDQVWLVDFSKLATDITSFIDTNNGFLTIIAGLGALTFFIVKKSK
|
May be a DNA-binding protein involved in virion nucleoprotein condensation.
|
P34668
|
MKRKNQKEDSDTENDDEIEPANGDGIEQEMNRVTNGNEDDESVGNDVAEPMETEDVEDSGEVEIEETAQNGEREIFKVLGKQEMKNLEALKVTSSWVQNATTFSATIDSSTSQKLSQIELPEHLTVPSAISTWFPVQYAVLPSLFFEIRSPPPLRPRDVAIAAPTGSGKTICYVLPVLAAVGSKPSKILQAVILVPVQTLVAQIVDEFKRWNDESGVAKVVSLSGANDFEKEARQLASDPPNVIVATPARLVQHLTSKIPPPIDLSKLRFLIVDEADRMGKLMREEWLDLVEFLCGGMERVACLKDIIRQRRAPQKIVLSATLSKDVEELHLWNLFKPRLFSATAVSVKDITSGIPQVDHVSGRLALPSSISHRLVVTDPKFHPLAVYQQITRNKFNRTLIFVNEVSSSNRLAHVLKELCKDQFEVDYFTAQLFGKRRYKMLEKFNKNENRVLICSDVLARGTDLNKVDCVINYNLPADDKLFVHRAGRTGRAGQDGYVISVGDKESKRLFVKMLKVTNLWGDTVEEQMEEYIFEKDMDRYSKALESLKATVSSQAKTGGSRQIAKRSGFEAKRKSRPNARGEKPWLKKKTTE
|
Probable ATP-binding RNA helicase. ATP + H2O = ADP + H(+) + phosphate Belongs to the DEAD box helicase family.
|
D6W1T7
|
MNTNKIAQDEVQDKVLQRAELAHSVWNLRFNLSKVAKRIRMETKVFPEIKINDAQSQLERSRCRIFSPDLEEEHVPLIQGFKCLDSPPPVPPSSSQGEDEENTVDSQY
|
By the zinc-responsive transcription factor ZAP1.
|
Q08272
|
MAFGWHSMHGSIIWFLQIAQLSTAISHDQNATAVHFLISNLFFLVSTGALWFELCAIFCDSSSSTSILSTSLLMLNYFSLKFSATGERHLVATNIAHIEAHTSIVGFMISLFTPLKETIITKYEMLVRT
|
Partially overlaps HRT1. 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.
|
O31830
|
MKKIASYYLMTLGLSSLTFGLLLGFYSFVMYGDMIIALFTAAIALLYGFVVYGLFAVPLQMKLQKKARTFNVMYLLIYSVVAFIAAFLFFVINEPASIAWTLQSYFYYMLSIAAAVIYWLWDSLILYKRTASGV
|
Belongs to the UPF0715 family.
|
P76247
|
MGKATYTVTVTNNSNGVSVDYETETPMTLLVPEVAAEVIKDLVNTVRSYDTENEHDVCGW
|
Homodimer.
|
Q2MB24
|
MGKATYTVTVTNNSNGVSVDYETETPMTLLVPEVAAEVIKDLVNTVRSYDTENEHDVCGW
|
Homodimer.
|
Q796F8
|
MKVKTKLLGIISILVVSIIGIGGSSVFMISSTVKKNEELKDKMEFQKEIKHIQYELTGLSNDERGFLITRDKEYDEGMKGKADDVLKSLDRVNDLIDEEKYQSNIEDIKTSFTQYRALNQQVVTAYSSNPKKAETIHFGEERTIRKEGVAPAVNKLSDRLDQEVEDLKDEIQGNGKMSQSLIIIVTGISVILGIVLSIMLLKSIMVPLRSINKQLEEIAHGEADLTKKVIVKNKDEFGQLAQSFNSFTHSLTQIVKQISSSSEQVAASSEELSASAEESKSTSEHISRAMQMAADSNVKQSSMTEKSAESITELLDSISSVASNTGNIADLSSSMRDKAEIGSKSVNKMLDQMKFIDKSVDSAGNGLQTLVASTAEISDISSLITTISEQTNLLALNAAIEAARAGEQGKGFAVVAEEVRKLADETNKSANHIQSVVATIQNESIETVNNIKVVQENVSSGIVLSQETTGNFNEILNLVEQVTSQIQEVAAATQQLTSGVEVIQHTVHTLAAGTKETSANTEAVANSSQEQLHSMGEISYAAESLSQLAEELQTVINRFKY
|
Transcriptionally regulated by sigma-D factor. Belongs to the methyl-accepting chemotaxis (MCP) protein family.
|
A7ZMT4
|
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
B7USI6
|
MFAGLPSLTHEQQQKAVERIQELMSQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
B7MBL7
|
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
B7L6T9
|
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
B5YQV2
|
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
B7NSW4
|
MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
|
Belongs to the UPF0181 family.
|
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