UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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B7MVU0
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MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
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Belongs to the UPF0181 family.
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B7M285
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MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
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Belongs to the UPF0181 family.
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C4ZZG7
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MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
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Belongs to the UPF0181 family.
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B1XH79
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MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALVAEELRANHSGERIVARFEDEDE
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Belongs to the UPF0181 family.
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C1P604
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MYIFITHFFTEYVILKYLLPI
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In stationary phase, induced at 45 degrees Celsius (at protein level).
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O34596
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MIYSKVENFINENKQNAIFTEGASHENIGRIEENLQCDLPNSYKWFLEKYGAGGLFGVLVLGYNFDHASVVNRTNEYKEHYGLTDGLVVIEDVDYFAYCLDTNKMKDGECPVVEWDRVIGYQDTVADSFIEFFYNKIQEAKDDWDEDEDWDD
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Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YobL (PubMed:34280190). Neutralizes the toxic activity of cognate toxin YobL upon expression in E.coli. Does not have immunity protein activity on other LXG toxins (PubMed:22200572). Interacts with cognate toxin YobL but not with non-cognate putative toxin YeeF. The interaction inhibits the toxic activity of YobL. Expressed on rich and minimal solid media likely in early stationary phase; not dependent on DegSU. Not expressed in liquid LB, but only under conditions that promote biofilm formation. Deletion of the yobL-yobK operon has no visible growth phenotype, however it is out-competed by wild-type cells.
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Q796E2
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MKVFEADSLLFEADKRTKEYKELRSQMVKLKKAFKEVANLDDSEFSGKGADNIKAFYHGHVGVTDQWIDLIDMKIAFLSSMSATLEDAKMSDAYIEESFLEHELANAYAKSKSIMSEQKKAMKDILNNINDILPLEIFSTEDFKDKLSSADDKREKTIDKLNKLDEDLKTEYAETEPNEQFIQQDFKKLQESTGKGKNATPIHYNAKAYRESDIHKKKGDIEKHSEAYLSVKKEEAKEREIKELKKKLNDGVSDPDEYLEIAKKVGYENLEPTQVQLAVQIEQAKQLEGAGEITWDIVKGVGVGLYDVGKDTVTGIWDFITDPGETLSALGNAAMHPVKTYDAISAAIEESYQKDMVNGDAYSRSRWVTYAIGSVAVAVVGTKGAGAINKADAAGKVINKASQAGKKIKDVKIPDLLPYNPKYKLALADNVPYNVVDSQNLKNELLTNAKKIPDGTRKPFTGQKKSPPWLNKEKYDAYEIEGKVKAKGKVKDVSRRVYTMKDIDINQKTEFGVTNLQLMKNGNAPYAKDGTQINLHHLIQEEPGPMLEIPNSLHTKYSDVIHQLKSDGESFRNDKVLKAQYESFRKRYWKWRAKQFENEN
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Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YobK does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation. Interacts with cognate immunity protein YobK but not with non-cognate putative immunity protein YezG. The interaction inhibits the toxic activity of YobL. Delivery to target cells requires the type VII secretion system (T7SS) and YukE. Expressed on rich and minimal solid media likely in early stationary phase; not dependent on DegSU. Not expressed in liquid LB, but only under conditions that promote biofilm formation. Deletion of the yobL-yobK operon has no visible growth phenotype, however it is out-competed by wild-type cells. In the N-terminal section; belongs to the LXG family. Was originally thought to be an RNase; when the C-terminus (residues 449-600) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YobK, but not by immunity proteins specific to other LXG toxins. Mutation of His-562 to Ala leads to loss of growth inhibition and RNase activity in E.coli.
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Q796E1
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MTNFVHKTVNGLKSLLDEKGAIKLFCSEGDIMEFLVTFSQDKATLNDIQSFEAKHQLTLPQDYQKFMTLHNGAKIFEILSDGENIGGGLQLFSLEEIEEELKYEDLFEDINGIPIGYLLEECHLMIDKDKVNQGDPNYLYIFESGLEYNPLNLNFEKFLDRYILANGEPFWDWRYYTAENYYRTR
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Truncated N-terminus.
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Q796E0
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MNSLMNDDMVKIIRNGLSASQHPKHILVIGAGLSGLVSASLLKNAGHRVTILEASGRAGGRVCTLRSPFSDDLYFNAGPMRIPNNHSLTLEYIKKFKLPTNVFINRTPMDIIYANGIKTRLQVFERAPGILRYPVAPNEQGKTSEELMLSLLQPILNFINQNPARNWRIVEEQYKNHSLSSFLNTYFSYGAIDMIGVLLDMEAYMGMSLVEVLRESIFFSSPAHFYEITGGMDLLPHAFLPQLKTNILYHQKMMKMSQGENRVTIHCQHQQTAEFTSFTADLAIVTIPFSTLRFVKVEPYHSFSYYKRRAIRELNYISATKIGIEFKSRFWEKAGQHGGKSITDLPIRFSYYPSRNIGANGHAVILASYTWADEALIWDSLSEGERIQYTLLNLSEIYGDIVWSEFVSGTSFSWSQYPYSAGGFTAFEPGQELELYPYIPVPEGRVHFAGEHASLTHAWMQGAIESGIRVAYEVNRLP
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an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+) Belongs to the flavin monoamine oxidase family. FIG1 subfamily. Truncated N-terminus.
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Q796D7
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MDDIRKIERLAAASWPAYFQKSIGKWLLRANFGVTKRANSVWTSADMPEGDFQLEAELFYQSLGLPVCFHISNASPKGLDDALADSRYEKVDECFQMTALCRSIMSRTNDNSRFTYKWEQEPSSVWIDEFIQLEGFSPERHKGYKHIFERMPPCKTFFKMYDKESLTALGTVSVIDGYGGLSNIVVAEEHRGKGAGTQVIRVLTEWAKNNGAERMFLQVMKENLAAVSLYGKIGFSPISEHHYRIKR
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Belongs to the acetyltransferase family.
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Q796D5
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MRITQYQTVWQLTFFPALFPVNCYLVEEENEVTLIDAALPGSYKGIIQAVNQLGKPLQHILLTHAHGDHVGSLDTLAQTFPHAKVMISERDSFLLQGDTSLRQDEPQTPIKGGIPKHIQTKPHQLLTGGETIGSLLAIPTPGHTPGSMSFLDTRNGTLIAGDAFQLRGGIAVSGQIKWAFPFPAFATWNKEEAIKSAQLLADKAPSCLAVGHGKFLRSPSERMRQAIQKAKKG
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Binds 2 Zn(2+) ions per subunit. Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
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Q9Y811
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MLCAARKCLNKTFISVRLNAFSCLAELNFRHTWYCSKKETPYQLERLQEEDIEETFICGKGPGGQKINKTSIVAQVKHIPTGIIVRSQDTRSREQNRCIARKRLTEKVDEFKHGNDSLLARKVQRIVKKKKQREKKSKRKYGNKIDDQDSSLNNNEAKQDVI
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Belongs to the prokaryotic/mitochondrial release factor family.
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O31947
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MASKKVHQINVKGFFDMDVMEVTEQTKEAEYTYDFKEILSEFNGKNVSITVKEENELPVKGVE
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Octamer.
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O31945
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MKGKKDGLNKQVHIYSIDTSAFYNDQENKLHNKILKSYRYRDHLRKLEHVDKKHKKYITQRIISLKEKLYNAFNDHNQIRTLRTDSLKDNNVISLFDSVLTRTLGIKENSLSEEIMVVQTYHFQILRDIIDKGFIHNNEKYVYFTSSAGQIRTKKSCFIKQSTLDKYQNALTCGLSVEHINAQGGSSINKWNSYMALSNSASSSWEIDIDKAIVVNDLETNVSSLVDYIDRDTYEITRKIMDIPIEHTDGCGMMLPSLSQKSFMVRLPWVKGLLVPFDFRKFAEKHSSFIVKDVYGKEWDIIKDDIQIIFTKSQFKMWKYYDSWDDYRYKFKKYGCLGAKLNEEDPSVEGKLTYQMLQTLTDITDEELKQISSKTVSEITQLGTDKETMMKVLGATEKNKHKTSLQEALLIYPELLNDDHTKEIIKNKKKSMIKDAKSGKLLVSDARYTYLCPDLYAFCERLFLGIESPKGLLSGSDVHCSLYDEGYIDILRSPHLFREHGVRWNKKNEEYEKWFITPGVYTSIHDPISKLLQFDNDGDKALIISDELIVNIAKRNMADIVPLYYEMSVAQKQEINSRNIYEALTLAYGINIGEYSNNITKIWNSDNINLDVIKWLCMENNFTIDFAKTLFMPTRPDHVDEKIKDYIKNKVPHFFINAKDKEEHSVESINESTVNKLDSIIPSDRINFAAVAGKFDYRFLLKNKEIKLNEAVINEYKRLDRNKKWLMNDEEAKPGQKLYVYKIIKQKLLEIHNDDGFITDVLVKHLYKKKSKYKSTLWECFGDIVLENIKHNLKTFKGCCICGKAFKPTSNKAKYCQSCGKKKERDKYKKYNKKRINHR
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A single subunit DNA-dependent RNA polymerase (RNAP) that catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates (rNTPs) as substrates. The enzyme is more highly processive than the multisubunit RNAP from E.coli but is considerably more error-prone. It has no detectable proof-reading function but can perform pyrophosphorolysis. Transcribes the late genes of the SPbeta prophage starting from yonK (approximately 35 genes are encoded in the prophage downstream from yonK). a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Uses Mg(2+) and Mn(2+) equivalently. No expression under phage non-inducing conditions; induced by mitomycin C (at protein level). No longer forms lytic phage. Encoded by the SPbeta prophage. Belongs to the YRH RNA polymerase family.
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O64076
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MKGKKDGLNKQVHIYSIDTSAFYNDQENKLHNKILKSYRYRDHLRKLEHVDKKHKKYITQRIISLKEKLYNAFNDHNQIRTLRTDSLKDNNVISLFDSVLTRTLGIKENSLSEEIMVVQTYHFQILRDIIDKGFIHNNEKYVYFTSSAGQIRTKKSCFIKQSTLDKYQNALTCGLSVEHINAQGGSSINKWNSYMALSNSASSSWEIDIDKAIVVNDLETNVSSLVDYIDRDTYEITRKIMDIPIEHTDGCGMMLPSLSQKSFMVRLPWVKGLLVPFDFRKFAEKHSSFIVKDVYGKEWDIIKDDIQIIFTKSQFKMWKYYDSWDDYRYKFKKYGCLGAKLNEEDPSVEGKLTYQMLQTLTDITDEELKQISSKTVSEITQLGTDKETMMKVLGATEKNKHKTSLQEALLIYPELLNDDHTKEIIKNKKKSMIKDAKSGKLLVSDARYTYLCPDLYAFCERLFLGIESPKGLLSGSDVHCSLYDEGYIDILRSPHLFREHGVRWNKKNEEYEKWFITPGVYTSIHDPISKLLQFDNDGDKALIISDELIVNIAKRNMADIVPLYYEMSVAQKQEINSRNIYEALTLAYGINIGEYSNNITKIWNSDNINLDVIKWLCMENNFTIDFAKTLFMPTRPDHVDEKIKDYIKNKVPHFFINAKDKEEHSVESINESTVNKLDSIIPSDRINFAAVAGKFDYRFLLKNKEIKLNEAVINEYKRLDRNKKWLMNDEEAKPGQKLYVYKIIKQKLLEIHNDDGFITDVLVKHLYKKKSKYKSTLWECFGDIVLENIKHNLKTFKGCCICGKAFKPTSNKAKYCQSCGKKKERDKYKKYNKKRINHR
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A single subunit DNA-dependent RNA polymerase (RNAP) that catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates (rNTPs) as substrates. The enzyme is more highly processive than the multisubunit RNAP from E.coli but is considerably more error-prone. It has no detectable proof-reading function but can perform pyrophosphorolysis. Probably transcribes the late genes of the SPbeta phage starting from yonK. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Belongs to the YRH RNA polymerase family.
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P34633
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MKVNEEGFAIDDKEYAMKTELKFASKHSSRLKIERNVMESYSKCDAQCKEHFSELIDFGQSPVWKWIVMTIVGPSLEELKMKYKPSDIPPSTILQCGLQTMKAIHDFHQIGFLHRDIKPANYCIGYGSKSETIYVLDFGLARKYRLPNGQVRPPRPKTKMIGTPRYCSRASHRCEELGRRDDYESWFFMFIDLVDTTLIDWKGLTRPDAYAKKQELFTKLKTYEKHPMFKVISIYLDNLVYDSEVKFGVLREAITDYARGCKLTLKEPLVWFNQSTCPSPSTAPGTGASRMATNIDLKSIASDRNEENSLDRSKTGTLSFNNSKNKKPSRY
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ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
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O94287
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MKDDQLIDWIHERYEEQKSANRLAGRFRFLGLETKYSIISIISGIFIGLTAALLNALASLLNSFREGYCTVNILFDKQTCCSTLTEDYECQEFFFWRNNHSVFVSCLIYVSVSVGFAFIATTLGYVVAPAARASGIPTIKAILSGYKYPDMNVFFSIKTLCSKSLAVCFSVASGLWVGKEGPFVHIATNIIYLVERIAPSLADSEIFTRQLLAAAMASGIAASFNAPVGGVIFALEQLASSSFPSLFTGSIWYEFLCSASSVVALQLIRSWHTDVGYLSYVSLDRRWSYKDTLPFIFISILCGCLGSVLIYLNMKFASKTKGFSKISNVFFVIFLSLITSLTAYAILGESELLFNPMELFPQVINSCSPSSSTVLCETTFWVTAIVLFTSALLGLLLTSATFGAAIPTGIIVPSLAIGACIGRAVGTLLKSRFPSLAGTSIYGVIGSIAFLSSTTRLVVALVVILFELTGALNIALPLMLATLISKWVSDSIIETSIYDAWIQFRNIPYFPSSNSLKFSIPLNFPVRSPEQLVRLPIRSCSIEELERAMHDSSQSFFVVLKNDTEFFEGFISRNKVSELLNRRPMSSNMQTTDNTGLDPLRSASAPVDSTFDLFDYIHPTTFTLNYDTPPVLMLKLFKDAGITNLALLNHGKLHGVLTKIDIIEYAKKCKTHTGNTYSELPTGVTYETDIFNRADD
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Voltage-gated chloride channel. Belongs to the chloride channel (TC 2.A.49) family.
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P34634
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MSNSQKPPSLQPNEIIKRTKPDYNWKVIVELGKGGYGTVNKVIKVNEEGFAIDDKEYAMKTEQKFASKHSSRLKIERNVMASYSKCDAQCKEHFPELIDFGQSPVWKWIVMTIVGPSLEELKMKYKPSDIPPSTILQCGLQTMKAIHDFHQIGFLHRDIKPANYCIGYGSKSETIYVLDFGLARKYRLPEWYCSRASHRCEELGRRDDYESWFFMFIDLVDTTLIDWKGLTRPDAYAKKQELFTKLKTYEKEPMFKVISIYLDTLVYDSDVKFGFLRDAITDYARSCKLTLKEPLVWFKERNDNESGSTPTTSATACSPSSSTGTGTGTGVSKIASNIDQKSIASDRNEENSLDGSKTGTWKSTKTRNKKPSRK
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ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
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O94296
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MARDVDNKQNAKRISRDEDEDEFAGESMVGRTLDNPFLGEDEFEDIFGSESQYISSSGQNSTNPFLADTRIENSPLGSESKANQLNKQGTNVNHIEIPLRDFNDPTQPESFLPPPKNTFTSRIKKIKNLFKKEKKQVKPEDLGPRQIILNDYSANHFLHNAVSTCKYSAFTFLPKFLKEQFSKYANLFFLFTAVVQQIPGITPVNRYTTIGPMLIVLSVSGIKEIMEDIKRKKQDQELNESPCYVLQGTGFVEKQWKDVVVGDIVKIVSETFFPADLVLLSSSEPEGLCYIETANLDGETNLKIKQALPETAGLLKPVELGQLSGEVKSEQPNNNLYTFDATLKLLPSDRELPLSPDQLLLRGAQLRNTPWVYGIVVFTGHESKLMKNTTETPIKRTSVEKQVNSQILFLLCIFVFLCFASSLGALIHRSVYGSALSYVKYTSNRAGMFFKGLLTFWILYSNLVPISLFVTFELVRYIQAQLISSDLDMYNEETDTPAACRTSSLVEELGQVGYIFSDKTGTLTRNQMEFRQCTIAGVAYADVIPEDRQFTSEDLDSDMYIYDFDTLKENLKHSENASLIHQFLLVLSICHTVIPEYDESTNSIKYQASSPDEGALVKGAASIGYKFLARKPHLVTVSIFGKDESYELLHICEFNSTRKRMSIVFRCPDGKIRLYVKGADTVIMERLASDNPYLQTTIHHLEDYATVGLRTLCIAMREVPEDEYQRWSTVFETAASSLVDRAQKLMDAAEEIEKDLILLGATAIEDRLQDGVPDTISTLQTAGIKIWVLTGDRQETAINIGMSCKLIDEDMGLVIVNEETKEATAESVMAKLSSIYRNEATTGNVESMALVIDGVSLTYALDFSLERRFFELASLCRAVICCRVSPLQKALIVKMVKRNTGEVLLAIGDGANDVPMIQAAHVGVGISGMEGLQAVRSSDFSISQFCYLKKLLLVHGSWCYQRLSKLILYSFYKNIALYMTQFWYAFCNAFSGQVIFESWSISLYNVLFTVLPPVVIGIFDQFVSAGQLFQYPQLYQLGQRSEFFNLKRFWSWITNGFYHSLLLFLCSIAVFYYDGPNKDGLASGHWVWGTTLYAAILATVLGKAALISNHWTQYTVIATLGSFLLWIVFMPIYAVAAPAIGFSKEYYGIIPHLYGNLKFWASLLVLPTIALMRDFVWKYSSRMYYPEEYHYVQEIQKYNVTDYRPRIVGFHKAIRKIRQMQRMRKQRGYAFSQGEEDQSRILDAYDTTHTRGAYGEMR
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This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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D6W3B2
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MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YPL257W-A ORF.
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O13566
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MSISIPEELLLSDDDIPDMPDMLESEVVCALAELVGVLLIDIDIPDIELLPIDILAIDDIVDANVLLALDIASMLIDDMLDNIVLLALDIASMLIDAILDATVLDALDMASIFMLLPIFIPSILNVKYNTLFFIFYSILPTNVI
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Almost completely overlaps CTR1. 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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O13567
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MLARVAESVSCGLMGQVKTGLLLFDGSGFSDRLGVMRFYVWSSRIYVLVLVVQAQLILDAHNGVLFLLLFFLHNFFLLPQLFQFLLSGCLIFLNDVYFNLMV
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Almost completely overlaps YLH47. 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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D6W4D4
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MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YPR137C-A ORF.
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P03859
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MKGLVRYMLHMDDPNKFKYQKEDMIVYGGVDVDELLKKTTTDRYKLIKEMIEFIDEQGIVEFKSLMDYAMKFKFDDWFPLLCDNSAYVIQEYIKSNRYKSDR
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Belongs to the Gram-positive plasmids replication protein type 2 family.
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O13568
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MYILNDILNLHRNIILKFNVGRRLRKLVGWSAVRVVLVLIGATIILVVISVLVVSTLAASSSVSSVSPIISTPTTEASRVKSWSGRSLSKGVNVQHFFFLPSHIGISFSRSGDGVEKRRFFIIKLLIRFILLVNS
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Almost completely overlaps SCD6. 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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Q8TGK9
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MAEPHPKVLNLTSSITPVESLTLICNLITSPHAGAPTRPVPTLGNFLSNEPTFLGCV
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Completely overlaps ISU1. 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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O13519
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MASTVAGLSMSAESLRLPLLIGVSSGMLSVSDAEVLPSFLFKSGFSVLQSAALDTDDDLARGLSLLDLLPLVLLSPFFEEDVDEEEAGDVEGLDGFVFVFRLLLPLYNQSTGTSNSVLVIIT
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Completely overlaps GIP3. 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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D6W4F5
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MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YPR158W-A ORF.
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Q08916
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MFNRVLIQSTNLDVGWVQEDSNRSTEGLGWQIVSEGGSNDTRVTVSSGNLTPHNSNLRTPDFLGGSVDVGNTLTQVKLSILWSSDTFDLDQRDIWVVDSLGSLVG
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Completely contained within RPL33A. 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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D6W4E4
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MTVKEYTKSKLPCSILNIKPTVTKSGEDAPLLVWIPGNPGLLYYYQEMLHHLHLKHPDWEILGISHAGMTLNAHSNTPIFSLQDQVDHQVEVINNFSCKNRKIIIMGHSVGAYIVQKVCLSNKLVGSVQKVGLVTPTVMDIHTSEMGIKMTAALRYIPPLAHVVSLFSYIFFYWILSEGFSRFIIDKFMGCGSTGYQAVLSTRIFLTHRQFVRQSLGLAAQEMEEITTNWEFQDRFINYCEENGISIWFLFSSNDHWVSGKTRSHLSDYYKDKVKQERLKIDVTDKIPHSFVVKHAEYAINAFF
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Shows both triacylglycerol (TAG) lipase and ester hydrolase activities. May play a role in TAG homeostasis. a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+) kcat is 0.87 sec(-1) with p-nitrophenyl acetat as substrate and 0.44 sec(-1) with p-nitrophenyl butyrate as substrate. Optimum pH is 7.5. Optimum temperature is 30X degrees Celsius. Accumulates lipid droplets. Present with 2190 molecules/cell in log phase SD medium. Belongs to the AB hydrolase superfamily. LDAH family.
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D6W4E5
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MSGYFSGFSLNKITDSIATAAHKTQDTLNNALANANVNLNDPQTRLSIKSRTRFVQESLGTVSDISKLPPQYQFLEKKSDSLEKVCKRILLVSKTFEVEGYDYPPNLTESISDWWSLNKDGWFGSKKSESSTKKKGSNHDDAFLPRSFAQAISKAAVDCECEFQNLEHNEKAELKKKKESIKTAQTTEAQGADHNEEDEEDEEDEEDDEDLSNLIKVFDSWSTCYKNIDEGKAEMDSMMVKEFNKKLETLINQDFKKVHDLRKKVEESRLKFDTMRYEVKAKEAELEAKKAEATGEAHSKDVSAKDISANTTTSFDETPSTEDEKPKSEGAEEESKKEANEPTVDDVADRKEDLKSNKVNDEPPIEESEDNKLLEKLEDEFVSNTTAAVETMEEITDSSEILGLIKLFQNFQLVYFRQCVQEVEANLKVLNGLEI
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Cytoplasmic punctate structures.
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D6W4F8
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MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY
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Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). Homotrimer. The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). Ty1-PR3 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4. The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Produced by conventional translation.
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D6W4F7
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MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
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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 YPR158C-C ORF.
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D6W3L9
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MVNPVGSSKLEQNNIKSIIGSSYNRLYSQFTSDELTEVGNYKILKQIGEGSFGKVYLALHRPTHRKVCLKTSDKNDPNIVREVFYHRQFDFPYITKLYEVIVTESKVWMALEYCPGKELYDHLLSLRRISLLECGELFAQISGAVYYAHSMHCVHRDLKLENILLDKNGNAKLTDFGFTRECMTKTTLETVCGTTVYMAPELIERRTYDGFKIDIWSLGVILYTLITGYLPFDDDDEAKTKWKIVNEEPKYDAKVIPDDARDLISRLLAKNPGERPSLSQVLRHPFLQPYGSVVLDQTQKILCRQRSGGTQFKSKLERRLLKRLKQSGVDTQAIKQSILKKKCDSLSGLWLLLLAQGKKQENCKYPKRSRSVLSVKKVIESATHNDTNGISEDVLKPSLELSRAASLSKMLNKGSDFVTSMTPVSRKKSKDSAKVLNPTLSKISSQRAYSHSIAGSPRKSNNFLQKVSSFFKSKKSSNSNSNNSIHTNVSESLIASNRGAPSSGSFLKKNSGSIQKSRTDTVANPSRTESIGSLNENVAGAIVPRSANNTTLENKKTSGNEIGLKVAPELLLNEHIRIEEPRLKRFKSSISSEISQTSTGNYDSESAENSRSISFDGKVSPPPIRNRPLSEISQISNDTYISEYSTDGNNSSFKISDTIKPSYIRKGSETTSQYSASSEKMTNGYGRKFVRRDLSIVSTASSTSERSSRTDSFYDITTATPVVTTDNRRNKNNNLKESVLPRFGTQRPWTGKRTYTTSRHGKNARRSSKRGLFKITSSNTDSIIQEVSSSEEEDHNVIYSKGKGLPTPVLQTKGLIENGLNERDEEGDDEYAIHTDGEFSIKPQFSDDVIDKQNHLPSVKAVATKRSLSEGSNWSSSYLDSDNNRRRVSSLLVEDGGNPTA
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Putative serine/threonine-protein kinase. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] By methyl methanesulfonate (MMS). Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
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Q5RDN9
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MVKMTRSKTFQAYLPSCHRTYSCIHCRAHLANHDELISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIYCENCKTTLGWKYEHAFESSQKYKEGKYIIELAHMIKDNGWD
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May interact with FAM168B. Belongs to the yippee family.
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A6QPH8
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MVRISKPKTFQAYLDDCHRRYSCAHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIHCENCKTTLGWKYEQAFESSQKYKEGKYIIELNHMIKDNGWD
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Involved in proliferation and apoptosis in myeloid precursor cells. Probably ubiquitinated leading to its degradation by the proteasome. Belongs to the yippee family.
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Q65Z57
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MVRISKPKTFQAYLDDCHRRYSCAHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIHCENCKTTLGWKYEQAFESSQKYKEGKYIIELNHMIKDNGWD
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Belongs to the yippee family.
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Q6NWI4
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MVKQTKAKTFQAYLDSCHRRYSCVHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERLLLTGLHAVADIYCENCHTTLGWKYEQAFELSQKYKEGKFIIELSHMIKDNGWD
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May be involved in proliferation and apoptosis in myeloid precursor cells. Belongs to the yippee family.
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Q9CQB6
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MVRISKPKTFQAYLDDCHRRYSCAHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIHCENCKTTLGWKYEQAFESSQKYKEGKYIIELNHMIKDNGWD
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Involved in proliferation and apoptosis in myeloid precursor cells. Widely expressed. Probably ubiquitinated leading to its degradation by the proteasome. Belongs to the yippee family.
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Q9D0U3
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MVRISKPKTFQAYLDDCHRRYSCAHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIHCENCKTTLGWKYEQAFESSQKYKEGKYIIELNHMIKDNGWD
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Involved in proliferation and apoptosis in myeloid precursor cells. Widely expressed. Strongly expressed in heart, brain, testis, lung, spleen, liver, kidney and myeloid cells. Up-regulated after the removal of interleukin 3 and exposure to granulocyte colony stimulating factor. Probably ubiquitinated leading to its degradation by the proteasome. Belongs to the yippee family.
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Q65Z54
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MVKLTKAKTFQAYLDSCHRRYSCVHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERLLLTGLHAVADIYCENCHTTLGWKYEQAFELSQKYKEGKYIIELSHMIKDNGWD
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May be involved in proliferation and apoptosis in myeloid precursor cells. Belongs to the yippee family.
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Q65Z56
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MPSCDPGPGPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD
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Belongs to the yippee family.
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Q65Z98
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MPSCDPGPGPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD
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Widely expressed. Detected adult brain, lung, colon, small intestine and ovary, and in fetal brain, lung, liver and spleen. Belongs to the yippee family.
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Q65Z93
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MPSCDPGPAPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD
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Detected in brain, spleen and testis. Belongs to the yippee family.
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Q5XID5
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MPSCDPGPAPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD
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Belongs to the yippee family.
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Q3ZBE7
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MGRIFLDHIGGTRLFSCANCDTILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
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Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (By similarity). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. Belongs to the yippee family.
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Q65Z55
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MGRIFLDHIGGTRLFSCANCDTILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
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Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (PubMed:20580816). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. Belongs to the yippee family.
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Q9Y3C9
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MGRIFLDHIGGTRLFSCANCDTILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
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Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (By similarity). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. Belongs to the yippee family.
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Q4R4Q6
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MGRIFLDHIGGTRLFSCANCDAILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
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Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (By similarity). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. Belongs to the yippee family.
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Q5RDU7
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MGRIFLDHIGGTRLFSCANCDTILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
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Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (By similarity). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. Belongs to the yippee family.
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P45495
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MLYGDRSIENTDGTIRSLSNRHVQMIAIGGTIGTGLFLGAGTTISATGPSVIFIYAIMGLFFFFLLRALGEMFYFDSNSHTFVSFITRYLGEAAGRFAGWTYWIGILFACMAELTAVSTYVQYWLPGLPAWLIEVSVLGLLTLLNLTAAKLFGETEFWFAMIKIIAIISLVVTGI
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Belongs to the amino acid-polyamine-organocation (APC) superfamily.
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A8JUP6
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MVKTFQAYLPSTNRTYSCVHCRAHLASHDELISKSFQGSQGPAYLFNSVVNVACGQTEERVLLTGLHAVADIYCECCKTPLGWKYEHAYESSQKYKEGKFIIELAHMIKENGWD
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Involved in regulating synaptic transmission in presynaptic neurons (PubMed:32461240). In class IV dendritic arborization neurons (nociceptors), involved in regulating activation of their second-order neurons (SONs) and maintaining synaptic contact between nociceptors and their SONs (PubMed:32461240). In larvae, predominantly expressed in subsets of neurons, including a subset of sensory neurons comprising the class IV dendritic arborization (da) neurons (nociceptors), class III da neurons and chordotonal neurons (both mechanosensors). Larvae display reduced nociceptive rolling behavior due to impaired activation of second-order neurons (SONs) in the nociceptive pathway and reduced the synaptic contact between nociceptors and their SONs. Belongs to the yippee family.
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Q86S45
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MGRQFAGICGARGSLYGCVVCNTYLTCSKELTSKAFTGSTGPATLFKRAWNVVYGRCEHRKMTTGWHTVRDVFCVTCNQKLGWMYEMAVSESQTYKETQVIIENANFEKIAGAIKDPLGEDRQEAPPAPNLEMSRYPLEAEKKSRPQYRTVSVSSSSSAEC
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Belongs to the yippee family.
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Q936F2
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MIKRVNKLVLGISLLFLVISIAAGCGIGKEAEIKKSFEKTLSMYPIKNLEDLYDKEGYRDDEFDKNDKGTWTISSEMAIQKKGEALNIKGMVLKLNRNTRSAKGFYYVNAIKKDEDGRPQDNQIEYPVKMVDNKIIPTKEIKDDNIKKEIENFKFLVQYGNFKDLSKYKDGDISYNPEVPSYSAKYQLTNDDYNVKQLRKRYNIPTNKAPKLLLKGTGNLKGSSVGYKDIEFTFVEKKGENIYFSDSLHLKPSEDK
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Belongs to the staphylococcal tandem lipoprotein family.
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Q936F4
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MIKRVNKLVLGISLLFLVISITAGCDMGKEEEIKKSFEKTLSMYPIKNLEDLYDKEGYRDDQFDKNDKGTWIIGSEMATQNKGEALKVKGMVLYMNRNTRSAKGFYYVNAVKKDEDGRPQDNKIEYPVKMVDNKIIPTKDIKDGNIKKEIENFKFFAQYGTFKDLSKYKDGDISYNPEVPSYSAKYQLTNDDYNVKQLRKRYDIPTNKAPKLLLKGSGDLKGSSVGYKDIEFTFVEKKGENTFFTDSLHLEPSEDK
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Belongs to the staphylococcal tandem lipoprotein family. Truncated C-terminus.
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P54156
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MNSAPKLNTFQHLIGEHQTFLEAKRIAKQFSLSELPVLITGKIGTGKNHFAHAIHLESSRSNEPFISVNCSTHSEETLIHELFGPNGNTGVFQKAVRGTLFLDDVWRMPASVQAQLLKALDSDTEKPRMICASADRSVEHTFRQDLFYRLNILTLTLPELSERKSDIPLLTQHFLSNSGQQLLIDPSVFPVLEKHAFEGNVRELKNAADYMAAVSSGGTIQPYDLPPYIRGTIDGKTSKKKAKLLTLMEKAEFLFILETIKVLNEKGEPASRRIISEHSKNTQTSLTPQQVRSRLDYLEKKDYVTKSRGRAGTKITFEGLSFIETLKNQMI
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May play a role in cold adaptation. 8-fold induction by growth at 15 degrees Celsius. Cells grow much more slowly at 15 degrees Celsius.
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P32968
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WFNDLKQQCRAEMISIIDVTCQAIKHANTTRVGLLATTATVKARIYQDNLITDNIDCYTPDDADQHQVMESIYAYKSGDIAGAYSLLSPVKDRLLQAGVEKIILGCTELPLILEQEVRTSPQHYVDATEELIKKTVEWYFTHNTRNNIAA
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Belongs to the aspartate/glutamate racemases family.
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P54181
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MKAYDFTQGNVLKQLVLFSMPIMLGNALQVSFQFIDSLWIGNLLGAKALGAAAVSSTIVLTVLSFILGLNNATLTILSQQKGKDDIKGMASYINAFVVLLTGLSIGFGAAGFFLSELLLRLLKTPESMIPLAETYLQIQFIGILFLFGYNFISTVLRALGDSKTPLRFIAFAVVLNTVLAPLFISVFRMGIAGAAYSTILSQGIAFLYGLFYVIKHKLVPFSIPRMPKWEESALILKLGIPAGLQMMVITGGMMAIMSVVNSYGDHVVSGFGAVQRLDSIITLPAMAAGTAVNSMAGQNIGIGNEKRVGTIARLGVIAVISCMLVIAVMIWVFGKYLIRLFISEPDAVAFGEQYLKWIAFFYPFIGVNFVLNGIVRAAGAMLQVLVLNLISFWVLRYPFTALFSAWLGQKGIGLGIGMSFLFSSCAAFLYYRYGRWKAMKLFTEK
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Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
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O32013
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MIDYPININNVSGNSVINVGGAFMIRPLTLSKSVFGSGGLNTGIVFENNFVSKAKMINHQFTDQNVTKTF
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Belongs to the GerPA/GerPF family.
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Q6ZRG5
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MMRWNFSPEDLSSIFRNNSTLPKITVKNVDIEFTIPTAVTIEVEPSPVQQDNPPISSEQADFSLAQPDSPSLPLESPEESESSAQQEATAQTPNPPKEVEPSPVQQEFPAEPTEPAKEVEPSATQQEASGHPLKSTKEVNPPPKQEIPAQPSEPPEKVELSPVLQQAPTQLLEPLKKVECSPVQQAVPAQSSEPSIVVEPSPVQQIAHLCLQSSLRKWNPL
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Product of a dubious CDS prediction.
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Q17405
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MEDVDLGKDRTQLIDFVYANGNGSASNLNNRNNIPLSEKAAKEPLQTQPQEAPPAPKPKVQKQKPPVKPKKRIACSPGSAICLFLLAVAAIIFAAFLGHYLTKQNYEMMQFKSANESMTTCKNFTRSHKKHQDIVNEEDADENASIKQPTKEELALPKNVQPVWYDVSLSPKVGGNGTMGLAHVKLNIEEPTNKIVLNAKDIEFTRNLEKIQLSKEVTKRAKKSVDSGTNSTSEMPEGSGEEAMATTATTTTTESTTPVSSFVDTGIKVTNIEFDENLEKVTLTLDQELKKGSTVVLKIPFTSKVSNNNGLKEYKYKNSEGKEQSMFTTQPSYSYLRHVFPSFDQEAFKAPAAITLMHSKGSIVVANTGVKTKDDGDAQTSTLNKVLDPDFVIGDLVASEVNTTSGITIRIWTRPEVKHSTEQSLDYANQAIDAMEHILQSRLESKSLDIVAVPGFQTGNRVSPSFIVLPEEDILYNEQSNDINQKTRIARMISNRIAAQWFGGITNPEEFGTFWLNEALPRFLEVEALEKILDINSDDLWTYEMEKILERDATATSQPLRVKNVFSSADIAEIDHEFIGKKGAAVLRMIQKSVGVNVFNKAIRSFVSSYRSAYPYDDGLWKSFEKALGGKLKGWNNEPLDVAKFVNTWVDQIGFPLVSVEKLDDETVELSQERFKNDHKTKEQFKFRNAKYWFNWEVPLFLKSSGPVGNVSWLHEAFRLPLNTSDSIYLNTDSNGVYRVNYEEKRWNDIAKQLEKSHGKLSERTRARLISDVFALANSGALPFETALNVTSYLPMETATVPWLIATRIFKKLTERLEGAPIQDKLNSFIYQKIHKKFEEISSSPGEASSNYLKNRLYANLLDLMAIVKPEKSNEKLNELFVEGFLAPCQFSGNFSSDCSEVPGDLREKVYCNGVEFGNDTVFETVRELAEKEVDGAEKDLLQNSLACFRDPRALRRLILDNLNSTSTVTLLLRKMNSRPVGKEIATNWIIDNWSTVLKKKFKNDPETLNAIADAGIILDNEREKSMIETFMEHHHKSTHGIESLDKKIEEATTDIYWRKQKINELNDYLDGKMKGPAKDDEMESSEEQE
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Belongs to the peptidase M1 family. Although strongly related to the peptidase M1 family, it lacks the conserved active metal binding Glu and His in positions 496 and 499, which are replaced by a Arg and Ala residues respectively, suggesting that it has no activity.
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A6NG26
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MRCVTRTRNWWRRAARMPRAGSSAWWVAVCKQVCTRVGTYAVCWCSWNTGRFTGCPSWKDFWKPVGPALHVFNVKCEAQRGLKLTQPFTVACKIDPVLCKSGLGFPPQLFTGCVYLSTYTYPWQAQAECVRCPRDSNRCKRITPSACL
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Could be the product of a pseudogene.
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A8MZ25
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MGQKKTMGTERSRGGKRGPQPGAERPEEPGATFSKKPPEGARAPRCLSRPTAPKSGACLARRRPPGSPCSIRDAPFHTGDDRFLARENFPNVLQPLPRMFAVQQAADFESQCPRRWDSRKRPSEGLPSAGWGRWRGRPIHLGLWVSGSVRRKVSGSHVSRSLHL
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Product of a dubious CDS prediction.
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A8MUN3
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MSFEYRHYKREAKICTCRGGWAHVLLCIGVSQGACAEHLPHRPAVEKDVPGAGEVLFMCSWRIFPVASASPSSSISGLAGHSVFLVPGLAAHPGSHSDQPPGVPSRRKSRLERWSPSVSRSTSPPTEAPFCL
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Product of a dubious gene prediction.
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Q6ZS49
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MEISCTSQGFFFLKEHSSGVSSVKAAQMPGRTLYRSLCSCVFPLHSPTRPPSPASAPKGFLLLSPTSSNASKLMPYYLFHRSRGVDNSKISVLILLGCELEQTKKKKLGPATALGNSGRVE
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Product of a dubious CDS prediction.
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Q09449
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MLPTSSNNEENRKPENSFPPTHFDTWERLSDYQKPSSSTTDDAYGKPVAKISPTASIDERETGIIGSTLRQDSTDSDSTGSSNMNPYDRLDKEVISKKNAHTNSYRNDVDELEGSLRTLGLQKVNAPTISSFSAWKSQSSALPAPSSSETSKIVKAEIKAPQQPMSLNPNYFDVMREMEKSMNIFTKLFRGSQIRNKNDLPSGRHLVNYRQNHAFDFAAMSHIWKENKMENLPKLPHRANLVMTLPSSRVRNSKICAFYRVLEKKEDKYILVACHVNIHGFHRGDLRFVEVNNRTVLKGFERSSVIGHLFLGDILTVTELTRCNETVSNVASSVEDASPDAPCQWMASKVVLFPRHEPVNVQFKFTCNGMASVVSTNEPMSVILNNLTEAKTNVEYTGIAFKSASYTVHTEDYTKKWYERIQEEISNIMIYPKALSTIYQYEEYTPNFVVEKQEQEEHPYQQDLEDLDLYRQHEMQTNVFTKFFDIGKSEKRKFGPGKSISNCRHSDAIDFAAMSYIWKNIRQQHLPKLPKLPNMVLPLPTSMPLDSEICAFYRVLVENKSKYILIACHMNVHGYHRGDLRFLEINESTKLYGFEGRSVIGQLFLGDIVAVTELARCNGHGSDAFKIPFDVSMSSQNTCTWMASKITLPSRPPPASVLFSFMKNRMAVVKGCDEPMNVEVKSIQNVEPDLIYKGTAFKPEKPELNFTEGFIKKKRHQIGSITLRIASYPNSFGTIYNFQESDIDNEHYKIGINAFSEEKFTEISLDEREKIVETCSLMGFSAANTIFNGRFDCRAFKMEEIKKNGMTVMFCIENPTSQPTLGLWCAGNRIVIGGPNGDVNGAIETVIDDPDIGYLRIAARLSRDIPKKFSFKGDGEFFVSQREVFENEILDDGYFKTLDPGCNGRRIIETLYGGKPLERVVVDKRDSSIERMMSQLFGVGSGISEHKTSGKKSEDTPTQFYFPSTPEPLALNKYQCEYVQMLLDGNPLIIGSSPFGCGKSMTIITAALELYKLKKNRKQLLITQSNYASVNLIDIAQRVCLSGDDDLKDLKFVRFVSEKNWNELPSNCRTDSDMPYLMNKLFKDWAMGRIDLTNLTCLKTHHYVQMVSHIIKNDLVNPMLFGDHIAQIYDKLSADFSRAPHAQTLVEAFFMIYKPDLVMVTADSAKGLLNILRDVCAVQIDEASQLAECTLLGLLKSFNNASFGLIGDIHQLPPYCEEGLEGKLKDFGIGNTMERAIKEKMFPVCTLRNVYRCHPKTTELLSELFYDGALVSGVSELARSDFMTKRDDFWPNPKFPMMFVNNTGASTKMGTSTSNSSEKSIVGEIVQNLINDPRNPVNPSDIGVISFYSAQTSILTEHLRGSGVKCGTVDAFQGSEKEIIIMCSTNERISDFMQLSNRLNVAMSRAKQVTIIIGHLDGLRRANYWSTIVNKIEQNGNLVNANDWYQNQRRNKVSLSSYPLISTSRQSKQQRANEYNSQHKHVKRQSNNDYGSQRSVTNSLNPEFVGKWDDETYGDWPTIQKST
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Belongs to the DNA2/NAM7 helicase family.
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O94520
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MHINEETDWIDLVKPALAKKPKKIVDNSDKFPTPRGFQQKSLVSKNIHSGNSASSTSIFAKREEELQKDLLLKKAWELAYSPLKQIPMNAILAYMSGNSLQIFSIMTTLMLLVNPLKAITSTGSAFTPFKGTHPGTLWPAMGAYILFQLLLMGIGVYKLQRMGLLPTTTSDWLAWEVSKVFMDRSYGPSKTVL
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Belongs to the EMC4 family.
|
Q9UUN0
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MNLICSILPKKEPSYLKLWRKQVIYQVLTDRFALDEDNFYAKASGNLYLGGTWKGITRNLDYIKSLGCTAIWISPIVKNISETTDCGQAYHGYWAQDMTQLNENFGTEEDLKELVNAIHEKNMLCMVDIVVNHMGHAGSKPVNFLLYQPFNSGKYYHNWQFVQNYDDPHETITGWLGDSHVNLPDIRTEKNEVRKFFQNWVSDLIKRYQFDGIRLDTAKHVEKSFFPTFIEAANVFTTGEVFHGDPKVVGDYQKYLPSTLNFPLFFQLRETFLDPKHSMFSFYDKAVLDVRHYFKDVTVLCNFLENHDFPRFFHETKDIALALNALTALIFMDGIPIIYYGQEQMFDGGSDPDNREGLWKSKYNTSNPMFRHLSSMIRTRQNLVETYPEFTYVLSFQLYIDDSVYVFTRPGVIIAISNEGSTSSFKVEIDLKEHWKEVPSSFTDILTQKTIPCKDHKLKIKSKSGLPKILISSDPSFL
|
Binds 2 calcium ions per subunit. Belongs to the glycosyl hydrolase 13 family.
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P54478
|
MTPTKQHKKETFTHFIFRVFMILVGAASAAVSIELFLIPNDFIDGGIIGVSLILDHLFMSNPFLNFAFFVVILNIPFMIFGYKYIGKTFLVSTFIGIVGLAVIESSLHHVEAITTQPILATVFGGLLLGFGVGLVIRNGGSMDGTEILGILLTKKLPFSVGEFVMFINVFIFIWAVFVFGPEQAMYSFMTYYIAMKTIDAVIQGLDETKAVIIVSEQYDEISDAILHRLGRGTTKLKGKGGYTDEEKDVIYAVVTRLEVTKLKSIVFEVDQNAFITIMNTHETRGGKFKNAIH
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Belongs to the UPF0750 family.
|
P54480
|
MLRLGIDIDGTITAQDTFVPYLNRSFNLSISLNDMTDYDLTKLLNITQEEFWDWMNQNEAIIYKEALLAQHAKQSLDLLKEEHKLIYITARRTHLTDITYEWFDRQNIHYDHIELVGGHHKVEAVKNHNIDLFFEDHHGNAMMIAKEAGIPVILFNSPYNQLPIDSNIIRVNNWLEAVQWMNNNKHHLIRVNN
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Belongs to the 5'(3')-deoxyribonucleotidase family.
|
O94419
|
MSKSVNASLSSAINSVTLVKQENLKENLQNGSAVSVGSSESSNHSMKEISLDYSSPSLQQTEEQDRELNFIDSSMLRPTPPQESDNRLAVEKPNIQPLQGHSPVPSFMSTASTNISSSKINNNQTEFEQLRDSYKSHGDLNSAINDSRIQSIIFELNQQCEKESIPVSNIDWLQWASVPLFAYDLPPDPSNPNATSSSPPPLTPILELIKQNNFCIPSPCRKLVWQSLVSAERNELLTLYATLSTTNNSLDSSIRKIIRMQSFRGPLEPFKYSSTTRHKVSTESIFHVLHAFTLFDTTVEYNIEPLLWLTCAFLSYMAQGNAFRSLVCFIQRGGIREFFISQSSSLDESLFALVWGCLGDLAPSVAISLQRIKVSSLCILYPSLACCFADSLQLPEALRLMDLIAIYGLEMFVRLLVAIFLKDRDKIVNMVSHEQWVKYLRSDVLASYRQPLVQKYTFYTRTPVDLNAWVEDSLALNIDTTQFPSYLSYHETSVSHNTYRQNNLEELKNQNDYLTSQITNLEEGMVMLNKENTKLSEALSNHRVTRSEMEEATEILKNNSADLKAQLEKQPQELENRLLQEISILKQRNQKFLKNNATSIQQIQYLDEELGKTLKQLNDLKEKHAQLQTKWKSVSEMFRN
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Belongs to the GYP5 family.
|
P54484
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MKQGKFSVFLILLLMLTLVVAPKEKAEAASSGWQPVSGISGCKIRVITDAYTYTKSATSIDAYAETNGKCGKLNYKSFGVSIVEGGDIGPQYSGYFSSRTPTKKFYFSKLPKPTGTPWAVGLSVYKGKAKGAAFVYINPQKR
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Found in a complex with F(1)F(0) ATP synthase and SpoIIIJ and YqjG.
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P46877
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MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
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Belongs to the YqgB family. Extended N-terminus.
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Q2M9Q4
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MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
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Constitutively expressed; increases in exponential phase (PubMed:19121005), repressed by H(2)O(2) (PubMed:19121005) (at protein level). Belongs to the YqgB family. Extended N-terminus. Extended N-terminus.
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Q1R788
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MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
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Belongs to the YqgB family. Extended N-terminus.
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Q31WK2
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MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
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Belongs to the YqgB family. Extended N-terminus.
|
Q32C08
|
MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
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Belongs to the YqgB family. Extended N-terminus.
|
Q0T0V2
|
MKKKPVAQSERQHTLLENPCAYGLLSQFQAATVVNCFTLNKII
|
Belongs to the YqgB family. Extended N-terminus.
|
Q7C029
|
MKKKPVAQSERQHTLLENPCAYGLLSQFQAATVVNCFTLNKII
|
Belongs to the YqgB family. Extended N-terminus. Extended N-terminus.
|
Q3YXT2
|
MKKKPVAQLERQHSLLENPCAYGLLSQFQAAIVVNCFTLNKII
|
Belongs to the YqgB family. Extended N-terminus.
|
B2V3W4
|
MRILGLDLGKKTIGVAISDPLGFTAQGITTIRRANKEKDMEELRKICDEYKVETIVIGLPKNMNGTIGPSGEIAMEMGKLVEEALNIKVEFWDERLTTVAAHKAMLEADLSRSKRKKIVDKVASTYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
B2THN2
|
MRILGLDLGKKTIGVAVSDPLGFTAQGITTIRRANKEKDMEELRKICDEYKVETIVIGLPKNMNGTIGPSGEIAMEMGKLVEEALNIKVEFWDERLTTVAAHKAMLEADLSRSKRKKIVDKVASTYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
A7G659
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
C1FTB8
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
B1IJG5
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
A7GGE9
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
B1KXB5
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q18BF1
|
MLDGRIMGLDVGDKTIGVAVSDLMGLTAQGVKTIKRVGKKKDIEELKAIIKEKQVNKIVSGLPKNMNGTLGPQGEKVIKFCELVKAETGIDVEFWDERLSTVAAERSLLEADVSRQKRKKVIDMLAAVIILQGYLDFKINS
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
B9E198
|
MRILGLDIGNKTIGVALSDPLGITAQGITTIKRKGEDRDIEELKAICDKYKVEVIVCGLPKNMNGTLGPQSEKVLKFCNIIEEVINLPIKMWDERLTTVAANKAMLEADLSRAKRKKIVDKMAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
A5N7T7
|
MRILGLDIGNKTIGVALSDPLGITAQGITTIKRKGEDRDIEELKAICDKYKVEVIVCGLPKNMNGTLGPQSEKVLKFCNIIEEVINLPIKMWDERLTTVAANKAMLEADLSRAKRKKIVDKMAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
A0Q149
|
MRVLGLDVGDRTIGVAVSDPLGFTAQGITTVHRKSVKEDIDELKKICKEYAVELIISGLPKNMNGTVGEQGEKVIEFCELLKSELKMPIKMWDERLTTVAAHRAMLEANLSRAKRKKIVDKMAATYILQGYLDSI
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q0TPH6
|
MRILGLDIGSKTIGVAVSDPLGWTAQGVTTIKRDCYTKDVEAVMKICKEYGVETIVAGMPKNMNGTIGPSGEMVKNLCEQIEKSFDGKIEFWDERLTTVAAHRAMLEADLSRAKRKKIVDKIAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q8XJH8
|
MRILGLDIGSKTIGVAVSDPLGWTAQGVTTIKRDCYTKDVEAVMKICKEYGVETIVAGMPKNMNGTIGPSGEMVKNLCEQIEKSFDGKIEFWDERLTTVAAHRAMLEADLSRAKRKKIVDKIAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q0SS44
|
MRILGLDIGSKTIGVAVSDPLGWTAQGVTTIKRDCYTKDVEAVMKICKEYGVETIVAGMPKNMNGTIGPSGEMVKNLCEQIEKSFDGKIEFWDERLTTVAAHRAMLEADLSRAKRKKIVDKIAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q896F1
|
MRILGLDVGDRTIGVAISDPLGWTAQGVKTIKRSNLKNDIKEIEDICNEYKVDKIVSGLPKNMNGTLGPQSEKVTEFCDILKKELEKEIIMWDERLTTVAAHKAMIEGDLSRAKRKKIVDKIAAIYILQGYLDSVYNK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q486M1
|
MSTKTKSPIGQRTVIGFDFGKKYIGVAVGQEMTGSATPLGSVKATDGIPHWDNLAKYLKEWQPDFIVVGLPLNMDGSEQQLTLDAKKFGNRIHGRFGIQVEFQDERLTTADAKEQLFARGGFKNLKKDNIDAESARLIIESYFEQQYT
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
C3PGN1
|
MAVEPDKPGVDDPGPGRRLGLDVGTVRIGVAVSDRDARLAMPVETVRRETGFKDRDKDDIDRLLDLIHEYDAVEVAVGLPRDLKGNGSSSVKHAKEIAFRIRRRLAKDDRMKEPPPVRMVDERLTTVVATSALRASGVSEKRGRSVIDQAAAVEILQSWLDARHFALNGHSPSNVGDEVREP
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
Q6NGZ8
|
MVVQPDIPGDNDPGMGRRLGVDVGTVRIGLAMSDSGARMAMPFETLARETGLKDSDKQDIDRIAEVICDNHIVEVVVGLPRDLKGNGSKSVKHAKDVAFRIRRRMHKNGWEHVAVKMADERLTTVVATQALRASGVSEKKGRRVVDQAAAVEILQSWLDARINVLENRTIP
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family. Extended N-terminus.
|
Q8FT24
|
MKVTPDTPGRDDPGPGRRIGLDVGTVRIGVAASDRDARLAMPVETVPRETGMKGPDRGDIDRLIDIITEYDAVEVVVGLPRDLQGNGSASVKQAREIAFRIRRRLTATGREIPVRLGDERLTTVVATQALRASGINERDGRKVIDQAAAVEILQTWLDGRATALNTLPETPHTDEKGNFPR
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family. Extended N-terminus.
|
Q8NQ23
|
MKVSADTPGHDDPGPGRRLGLDVGTVRIGVAASDRDAKLAMPVETVPRETGFKGPDLADIDRLVAIVEEYNAVEVIVGLPTDLQGNGSASVKHAKEIAFRVRRRLTNAGKNIPVRLGDERLTTVVATQALRASGVSEKAGRKVIDQAAAVEILQTWLDARTRALEPQSTDTQDFDEKGNFPG
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Belongs to the YqgF nuclease family.
|
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