ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
11.1k
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A4F7F6
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MRPGEIITGDGPVPLNPGRPRVRITVVNRADRAVQVGSHYHFAAVNEGLEFDRAAAWGHRLDVPAGTAVRFEPGVEREVRLVPVGGSRRVPGLRPEYAGELDGRGHEPTAPNYGEKGQGHFE
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Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13238
Sequence Length: 122
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
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P41021
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MSNNNYIVPGEYRVAEGEIEINAGREKTTIRVSNTGDRPIQVGSHIHFVEVNKELLFDRAEGIGRRLNIPSGTAARFEPGEEMEVELTELGGNREVFGISDLTNGSVDNKELILQRAKELGYKGVE
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Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13959
Sequence Length: 126
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
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P0A677
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MRLTPHEQERLLLSYAAELARRRRARGLRLNHPEAIAVIADHILEGARDGRTVAELMASGREVLGRDDVMEGVPEMLAEVQVEATFPDGTKLVTVHQPIA
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Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11090
Sequence Length: 100
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
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P08298
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MKLSPREIEKLDLHNAGYLAQKRLARGLRLNYVETVALIATQILEFVRDGEKTVAQLMCIGRELLGRKQVLPAVPHLVESVQVEATFRDGTKLVTIHDLFACENGNLELALFGSFLPVPSLDKFTENEEDHRTPGEIICRSENLILNPRRNAIILRVVNKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGNATRFEPGECKSVVLVSIGGNKVIRGGNNIADGPVNDSNCRAAMKAVVTRGFGHVEEENAREGVTGEDYSLTTVISREEYAHKYGPTTGDKIRLGDTDLFAEIEKDFAVYGDECVFGGGKVIRDGMGQSSGHPPEGSLDTVITNAVIIDYTGIIKADIGIKDGLIISTGKAGNPDIMNDVFPNMIIGANTEVIAGEGLIVTAGAIDCHVHFICPQLVYDAVTSGITTLVGGGTGPADGTRATTCTPAPNQMKLMLQSTDDMPLNFGFTGKGNSAKPDELHEIIRAGAMGLKLHEDWGTTPAAIDSCLTVADQYDIQVNIHTDTLNESGFVEHTIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGEKNVLPSSTNPTRPYTHNTIDEHLDMLMVCHHLNKNIPEDVAFAESRIRAETIAAEDILHDKGAISIISSDSQAMGRIGEVISRTWQTADKMKSQRGPLQPGEDNDNFRIKRYVAKYTINPAIANGLSQYVGSVEAGKLADLVLWKPSFFGAKPEMVIKGGEVAYANMGDPNASIPTPEPVIMRPMFGAFGKAGSSHSIAFVSKAALDEGVKASYGLNKRVEAVKNVRKLTKRDMKLNDTLPQITVDPETYTVTADGEVLTCTAAKTVPLSRNYFLF
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Cofactor: Binds 2 nickel ions per subunit.
Function: Catalyzes the conversion of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source (Probable). May be involved in plant defense to pathogenic fungi .
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 90710
Sequence Length: 837
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
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D8JBB7
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MNYGKEQVAVYRTYANPLEGVRTIPESSFDGRDNILFGLEVRVQFEGEEFLPSFSEADNTTVVATDSMKNFVLHQAGEYEGATAEGFLHFVGTEFLETYPHVEAVTMSATEYPFDERPVPGDDGFDPSDLVFRVSDDESAFGEIYLEREGDELRFEEQTSGVTEIELVKVKENSFTGYVQDEYTTLPEREDRALYISLDVFWTYSDPEDALGDEPQRYVPAEQVRDIAQVVFHEVNSNSIQDLIYQIGLRVLERYPQLESVNFEANNRTWIEVRDDLDGDAKVLREPPRPTGYQQFSMDRSDLEEQ
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Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Mass (Da): 35081
Sequence Length: 306
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
EC: 1.7.3.3
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P25688
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MAHYHDNYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKLRGIRNIETFAMNICEHFLSSFNHVTRAHVYVEEVPWKRFEKNGIKHVHAFIHTPTGTHFCEVEQMRNGPPVIHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYQRRDVDFEAIWGAVRDIVLQKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLPSRL
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Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
PTM: Acetylation of Lys-118, Lys-164 and Lys-290 is observed in liver mitochondria from fasted mice but not from fed mice. May be deacetylated by Sirt5; however it is unclear whether Sirt5 mediates deacetylation or desuccinylation of Uox; additional evidence is required to validate these results .
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Mass (Da): 35039
Sequence Length: 303
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Subcellular Location: Peroxisome
EC: 1.7.3.3
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P16164
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MAHYRNDYKKNDEVEFVRTGYGKDMIKVLHIQRDGKYHSIKEVATSVQLTLSSKKDYLHGDNSDVIPTDTIKNTVNVLAKFKGIKSIETFAVTICEHFLSSFKHVIRAQVYVEEVPWKRFEKNGVKHVHAFIYTPTGTHFCEVEQIRNGPPVIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYHQGRDVDFEATWDTVRSIVLQKFAGPYDKGEYSPSVQKTLYDIQVLTLGQVPEIEDMEISLPNIHYLNIDMSKMGLINKEEVLLPLDNPYGRITGTVKRKLTSRL
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Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Mass (Da): 35008
Sequence Length: 304
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Subcellular Location: Peroxisome
EC: 1.7.3.3
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P11645
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MATTKKNEDVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLSSKQDYVYGDNSDIIPTDTIKNTVHVLAKFKGIKSIEVFAMNICEHFLSSFNHVVRVHVYVEEVPWKRLEKNGVQHVHAFIHTPTGTHFCEVEQRRSGLPVIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYQHSQDVDFEATWDIVRDTVLEKFAGPYDKGEYSPSVQKTLYDIQVLTLSRVPQIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLSSRL
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Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Mass (Da): 34501
Sequence Length: 300
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Subcellular Location: Peroxisome
EC: 1.7.3.3
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O74409
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MSETTYVKQCAYGKTLVRFMKKDICPKTKTHTVYEMDVQSLLTGELEESYTKADNSIVVPTDTQKNTIYVFAKNNDVSVPEVFAAKLAKHFVDKYKHIHGAALDITITPWTRMEVQGKPHSHSFIRNPGETRKTHVVFSEGKGFDVVSSLKDVLVLKSTGSGFTNFHKCEFTTLPEVTDRIFSTSIDCNYTFKHFDTFEELAGFDFNSIYEKVKEITLETFALDDSESVQATMYKMADTIINTYPAINEVYYALPNKHYFEINLAPFNIDNLGSNCSLYQPQAYPSGYITCTVARK
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Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Mass (Da): 33610
Sequence Length: 296
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Subcellular Location: Peroxisome
EC: 1.7.3.3
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A2RJJ9
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MGENTVPQKSSDNVGSIVALMVALLVAIFAFQLNASMLSPALVTMQAQLHTTASSIALTQTIFFTAAALFALFLPRLADLIGRKKVLIGMLTLTMIGCLISGFATNVGILMIGRILQGAAGPVVPLCLIILHVKVRDEKRYAKLMAILTSINGGIAGVDALAGGWLVSHGGFRSVFFVMGITAALAILLVSFGTQESTAKDTPKMDWTGVILLVVAMGALLSAVNALQGSFGNLGLPNWLLASILALLGLICFVGFWQVEKRVNHPMVPIHYLKQRRTWGLLITTLLTMTGVFAIMNGIIPALGQDGKFGLGLGADMVSLVTLTPYALAGLFFGPVSGFLAARFGFAKVLRVGLLTTIIGIVLAVAGVLQPSIWLLLLVSTFIGITYAGITNIMLNGLGIVLSPEDNPGYLPGLNAGMFNLGAGLSFIILYAVPTVLHTSVGGSSSGYISGIVTGLILVIIAFFTSFLIPDSKDCKINLE
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Function: Responsible for the uptake of uridine and deoxyuridine. Not involved in purine nucleoside uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50377
Sequence Length: 480
Subcellular Location: Cell membrane
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O74427
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MPEAFERYSSNPTYEPPWRKVRFIGIAGPSGSGKTSVAQLIVKALNLPHVVILSLDSFYKSLNAEQKKRAFNNDYDFDSPEAIDWDLLFVKLLELKQGRKVDIPIYSFNEHNRLPETNTLFGASIIILEGIFALYDEKIRSLLDVSVFLDTDSDVCLSRRLNRDINYRGRDIVGVLEQYNKFVKPSYENFVRRQLSYTDLIVPRGRDNKLAIDMVINFIRRTLSIQSETHVKNIDSLQQIVPTIPHLPLNLVQLKITPEISAIRTILINKNTHPDDLQFFLSRIGTMLMNLAGDSLAYEKKTITLHNGNQWEGLQMAKELCGVSVLRSGGTLETALCRQFPTVCLGKILVQINKVTQEPTLHYHKLPRGIATMNVVLMASHLTTHADVLMATQILVDFGVPEENIIIVVYVCYSESIKALAYIFPKVTIVTAFLESVAEPVVGRLDIEKVYYGC
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Function: Catalyzes the conversion of uridine into UMP and cytidine into CMP in the pyrimidine salvage pathway.
Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 51390
Sequence Length: 454
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
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P27515
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MSHRIAPSKERSSSFISILDDETRDTLKANAVMDGEVDVKKTKGKSSRYIPPWTTPYIIGIGGASGSGKTSVAAKIVSSINVPWTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVKPTMKNADAIIPSMSDNATAVNLIINHIKSKLELKSNEHLRELIKLGSSPSQDVLNRNIIHELPPTNQVLSLHTMLLNKNLNCADFVFYFDRLATILLSWALDDIPVAHTNIITPGEHTMENVIACQFDQVTAVNIIRSGDCFMKSLRKTIPNITIGKLLIQSDSQTGEPQLHCEFLPPNIEKFGKVFLMEGQIISGAAMIMAIQVLLDHGIDLEKISVVVYLATEVGIRRILNAFDNKVNIFAGMIISREKLQNHQYKWALTRFFDSKYFGCD
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Function: Catalyzes the conversion of uridine into UMP and cytidine into CMP in the pyrimidine salvage pathway.
Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 56296
Sequence Length: 501
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
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P09728
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MLRRGSLRNPLAICLLWWLGVVAAATEETREPTYFTCGCVIQNHVLKGAVKLYGQFPSPKTLRASAWLHDGENHERHRQPILVEGTATATEALYILLPTELSSPEGNRPRNYSATLTLASRDCYERFVCPVYDSGTPMGVLMNLTYLWYLGDYGAILKIYFGLFCGACVITRSLLLICGYYPPRE
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Function: Plays a role in the modulation of host immune response by reducing the presentation of HLA-G molecules at the cell surface. Selectively targets HLA-G molecules for degradation by a mechanism distinct from that used by US11.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 20771
Sequence Length: 185
Subcellular Location: Host endoplasmic reticulum membrane
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P09727
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MNLVMLILALWAPVAGSMPELSLTLFDEPPPLVETEPLPPLSDVSEYRVEYSEARCVLRSGGRLEALWTLRGNLSVPTPTPRVYYQTLEGYADRVPTPVEDVSESLVAKRYWLRDYRVPQRTKLVLFYFSPCHQCQTYYVECEPRCLVPWVPLWSSLEDIERLLFEDRRLMAYYALTIKSAQYTLMMVAVIQVFWGLYVKGWLHRHFPWMFSDQW
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Function: Participates in the inhibition of the host immune response. Redirects newly synthesized major histocompatibility complex (MHC) class I heavy chains via the SEC61 translocon to the cytosol where they undergo proteasome-dependent destruction. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25264
Sequence Length: 215
Subcellular Location: Host endoplasmic reticulum membrane
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Q9FMU5
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MSLSQNAPKSKGIKREELKKQYEDVEDEEEIGSDDDLTRGKRRKTEKEKQKLEESELVEMKKLENLIFGSLYSPVTFGKEEEEDGSALFHVDRSAVRQIPDYEDDGDDDEELSDEENGQVVAIRKGEAAWEDEEEKQINVDIASVNRLRKLRKEENEGLISGSEYIARLRAHHAKLNPGTDWARPDSQIVDGESSDDDDTQDGGVDDILRTNEDLVVKSRGNKLCAGRLEYSKLVDANAADPSNGPINSVHFHQNAQLLLTAGLDRRLRFFQIDGKRNTKIQSIFLEDCPIRKAAFLPNGSQVIVSGRRKFFYSFDLEKAKFDKIGPLVGREEKSLEYFEVSQDSNTIAFVGNEGYILLVSTKTKELIGTLKMNGSVRSLAFSEDGKHLLSSGGDGQVYVWDLRTMKCLYKGVDEGSTCGTSLCSSLNGALFASGTDRGIVNIYKKSEFVGGKRKPIKTVDNLTSKIDFMKFNHDAQILAIVSTMNKNSVKLVHVPSLTVFSNWPPPNSTMHYPRCLDFSPGSGFMAMGNAAGKVLLYKLHHYQNA
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Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Sequence Mass (Da): 60988
Sequence Length: 546
Domain: The DWD box is required for interaction with DDB1A.
Subcellular Location: Nucleus
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B6EGH8
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MTSAYELVSDYQPAGDQPQAIKTLNEGLENGLAHQTLLGVTGSGKTFTLANVIAKSGRPTVIMAHNKTLAAQLYGEMKAFFPNNAVEYFVSYFDYYQPEAYVPTTDTFIEKDSSVNEHIEQMRLSATKALLERKDAIIIASVSAIYGLGDPQAYLSMMLHLSRGDIINQRDILRRLAELQYKRNDMAFERGTFRVRGEVLDVFPAESEHEAIRIELFDDEVERISKFDPLTGSIITKDMPRCTIYPKTHYVTPREKVLDAIEQIKVDLAERKKELLANNKLVEEQRISQRTQFDIEMMNELGFCSGIENYSRYLSGRPQGEAPPTLFDYLPKDGLLIIDESHITVSQIGAMYKGDRSRKENLVEYGFRLPSALDNRPMRFDEFEARAPQTIYVSATPGKYEIEKSGSDIAEQLVRPTGLLDPIIEVRPVGTQVDDLLSEIRIRTKVGERVLVTTLTKRMSEDLTEYLAEHGVKVRYLHSDIDTVERVEIIRDLRLGKFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQAIGRAARNLEGKAILYADRITGSMEKAIGETERRREKQILHNEALGIVPTALKKNVADILELGDMTKNKRKIVAPKMKLSEVAEEGASYQSMTPQQLEKEVQRLEAKMYQHARDLEFEQAAKVRDEVEKLRNQFITNS
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 76637
Sequence Length: 676
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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B9KH59
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MQRFKISSEFNPSGDQPGAIDSLVRGISCGAKEQTLLGVTGSGKTFTMASVIEQTQRPAIIIAHNKTLAAQLHEEMRSFFPENAVEYFVSYYDYYQPEAYIPQSDVYIEKDALINDKIDLLRHSATRSLLERRDVVVVASVSCIYGLGSPELYSEMTVPIALGMKLDMCQLQERLVELQYKHGNRYERGSFSVQGDVLSVFPSHYEDRIWKISFFGDEVDSIQEVDPKSGMVTLKLEKIKIFPNSHYVTPRPTLLQAISEIEKELDECALQFKQCNKIVEADRIVERTRFDIEMMRETGTCKGIENYSRYLCGKEAGDPPNTLLDYLPQDAIMFIDESHMTVPQIRAMYNGDRMRKANLINHGFRMPSALDNRPLTFAEWEDRKPTVVYVSATPGQYELQQTGGVATEQLIRPTGLLDPVCIVKGADGQIHDVMCESQATIARGYRVLITTLTKKMAENLTEYMREMGIKVAYLHSDVKTLERIEIISDLRLGVIDVLVGVNLMREGLDIPECALVGILDADKEGFLRSTTSLIQTIGRAARNVEGRVILYANVITKSMRTAMEETDRRRDIQRKYNQEHSIVPRTIQKPVQTSLSERVGSSRKKVSRDTNTDPANRDIVELQKEMLLCAENLDFERAVEIRNEIKRLTAP
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 73796
Sequence Length: 651
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q2GID5
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MRHFKITSEFDAAGDQPEAIRKLSEGIERGVREQVLLGVTGSGKTFTMASVIEKRQCPALIVAHNKTLAAQLYEEMRMFFPNNAVEYFVSYYDYYQPEAYIPHSDVYIEKDALINEKIDMLRHSATRSILERRDVIVVASVSCIYGLGSPELYSEMTIPLSIGMQIDLCQLKEKLVELQYKSGSQCERGTFSVKGDIVTIFPSHHEDHVWRISMFGDVIESIQEVDNNLGIAVANLEKVKVFPNSHYVTPRPTLMQALSRIEEELQECVINYRKNNKIIEAERILERTKFDIEMMKETGTCKGIENYSRYLCGKAAGEPPNTLLDYLPVDSLMFIDESHITIPQIRSMYNGDRVRKANLITHGFRLPSALDNRPLTFEEWESRKTTLVYVSATPGKYETERTSGVVVEQLIRPTGLVDPICIVKKASGQIADVVNESQATISEGYRVLVTALTKKMAENLSEHMREIGIKVAYLHSDVKTLERMDIIAQLRTGEIDVLIGVNLLREGLDIPECALVCILDADKEGFLRSETSLVQTIGRAARNMNGRVILYADRVTKSMKAAIDETNRRRAVQESYNKAHGITPKSISKSVATSLKDRITVKGTKGSKSKSAAVTEEDIIKLQKEMLLHAENLEFEKALEIRNQINKLSQHKT
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 73679
Sequence Length: 653
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q81X47
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MERQFEIVSAYSPQGDQPVAIEKLVEGINSGKKKQVLLGATGTGKTFTISNVIKEVQKPTLVMAHNKTLAGQLYSELKDFFPNNAVEYFVSYYDYYQPEAYVPQTDTFIEKDAQINDEIDKLRHSATSALFERDDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEKDRNQLLRELVDVQYGRNDIDFKRGTFRVRGDVVEIFPASLDEHCIRIEFFGDEIDRIREVNALTGEVLAERDHVAIFPASHFVTREEKMKVAIENIEKELEERLKELNDNGKLLEAQRIEQRTRYDLEMMREMGFCSGIENYSRHLTLRPAGATPYTLLDYFPKDFLIVMDESHVSVPQVRAMYNGDQARKQVLVDHGFRLPSALDNRPLTFDEFEEKTNQVIYVSATPGPYELEQSPEVIEQIIRPTGLLDPPIDIRPIEGQIDDLLGEIQDRIAKNERVLITTLTKKMSEDLTDYLKDVGIKVNYLHSEVKTLERIEIIRDLRLGKFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNENGRVIMYADRITRSMGIAIEETKRRRSIQEAYNEEHGITPKTIQKGVRDVIRATTAAEEPETYEATPAKKMTKKEREKTIAKMEAEMKEAAKALDFERAAELRDLLLELKAEG
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 75163
Sequence Length: 658
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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P56981
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MVEGRFQLVAPYEPQGDQPQAIAKLVDGLRRGVKHQTLLGATGTGKTFTISNVIAQVNKPTLVIAHNKTLAGQLYSELKEFFPHNAVEYFVSYYDYYQPEAYVPQTDTYIEKDAKINDEIDKLRHSATSALFERRDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEIERNALLRRLVDIQYDRNDIDFRGTFRVRGDVVEIFPASRDEHCIRVEFFGDEIERIREVDALTGKVLGEREHVAIFPASHFVTREEKMRLAIQNIEQELEERLAELRAQGKLLEAQRLEQRTRYDLEMMREMGFCSGIENYSRHLALRPPGSTPYTLLDYFPDDFLIIVDESHVTLPQLRGMYNGDRARKQVLVDHGFRLPSALDNRPLTFEEFEQKINQIIYVSATPGPYELEHSPGVVEQIIRPTGLLDPTIDVRPTKGQIDDLIGEIRERVERNERTLVTTLTKKMAEDLTDYLKEAGIKVAYLHSEIKTLERIEIIRDLRLGKYDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNANGHVIMYADTITKSMEIAIQETKRRRAIQEEYNRKHGIVPRTVKKEIRDVIRATYAAEETEMYEAKPAAAMTKQEREELIRTLEAEMKEAAKALDFERAAQLRDIIFELKAEG
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Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage (By similarity).
Sequence Mass (Da): 75455
Sequence Length: 658
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q884C9
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MSEFQLVTRFEPAGDQPEAIRQLVEGIDAGLAHQTLLGVTGSGKTFSIANVISQIKRPTLVLAPNKTLAAQLYGEFKAFFPNNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDHIEQMRLSATKALLERKDAIIVTTVSCIYGLGSPETYLRMVLHVDRGDKLDQRALLRRLADLQYTRNDMDFARATFRVRGDVIDIYPAESDLEAIRIELFDDEVESLSAFDPLTGEVIRKLPRFTFYPKSHYVTPRETLVEAMEGIKVELQERLEYLRSQNKLVEAQRLEQRTRFDLEMMLELGYCNGIENYSRYLSGRPSGAPPPTLFDYLPADALLVIDESHVSVPQVGAMYKGDRSRKETLVEYGFRLPSALDNRPMRFDEWEAISPQTIFVSATPGNYEAEHAGRIVEQVVRPTGLVDPQIEIRPALTQVDDLLSEIHKRAALEERVLVTTLTKRMSEDLTDYLSDHGVRVRYLHSDIDTVERVEIIRDLRLGTFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSDRSLIQTIGRAARNLNGRAILYADRITGSMERAIGETERRREKQIAFNLEHGITPKGVFKDVADIMEGATVPGSRSKKRKGMAKAAEESARYENELRSPSEINKRIRQLEEKMYQLARDLEFEAAAQMRDEIGKLRERLLAV
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 76215
Sequence Length: 671
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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A1STV6
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MDKRFQLVSQFSPAGDQPQAIEQLINGLKSGLAFQTLLGVTGSGKTFTLANAIAKLNRPTLILAPNKTLAAQLYGEMKEFFPNNAVEYFVSYYDYYQPEAYVPSSDSFIEKDAAINAHIEQMRLSATKALLERKDVVLVASVSAIYGLGDPTAYLQMMLHLTVGEIISSREILQRLVDLQYNRNETELSRGTFRVRGEVIDIFPADSEKEALRIELFDDEVEQISVFDPLTGQGIDKLARVTVYPKTHYVTPREQILKAVDAIKVELNERKKEFLEQNKLLEEQRISQRTLYDIEMMNELGYCSGIENYSRYLSGRSEGQAPPTLFDYLPKDALLIIDESHVTVPQIGAMYKGDRSRKENLVNYGFRLPSALDNRPLKFAEFEKIAPQTIYVSATPSDYEINKSQGEIIRQVIRPTGLLDPVIEVRPVTTQVDDLLSEINIRLPLKERVLVTTLTKRMAEDLTDYLHEHGIKARYLHSDVNTVERVEIIRDLRLGIFDVLIGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTMGRAARNLNGKAILYAARITGSMQKAIKVTEDRRELQNKFNIENGIIPQGLSKQVNDVMQLGQKNLKKGNLKQGKVAEYKANYQIHSEQDILKQIALSEKQMFACAKNLEFEKAALFRDEVTKLHEQLVSIG
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 75838
Sequence Length: 670
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q98I01
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MVSDFEPAGDQPTAIKDLVEGVDNNDRTQVLLGVTGSGKTFTMAKVIEETQRPALILAPNKTLAAQLYSEFKKFFPDNAVEYFVSYYDYYQPEAYVPRTDTFIEKESSINEQIDRMRHSATRSLLERDDVIIVASVSCIYGIGSVETYTAMTFQMQIGDRLDQRALLADLVAQQYKRQDINFVRGSFRVRGDTIEIFPAHLEDRAWRISMFGDEIEQITEFDPLTGQKTGELKSVKIYANSHYVTPRPTLNQAIKSIKEELKQRLVELERAGRLLEAQRLEQRTRFDLEMLEATGSCAGIENYSRYLTGRQPGDPPPTLFEYIPDNALVFIDESHVTVPQIGGMYRGDFRRKATLAEYGFRLPSCMDNRPLRFEEWDAMRPLSVAVSATPGGWEMEQSGGVFAEQVIRPTGLIDPPVEVRPAKSQVDDVVGEIRETTKAGYRTLVTVLTKRMAEDLTEYLHEQGVRVRYMHSDIDTLERIEILRDLRLGAFDVLVGINLLREGLDIPECGFVAILDADKEGFLRSETSLIQTIGRAARNVDGKVILYADQVTGSMERAMAETNRRREKQMEWNAANGITPESVKSRISDILDSVYEKDHVRADISQFTDSAGAMMGNNLKAHLDAMEKQMRDAAANLDFEKAARIRDEIKRLREMELSISEDPLAKYADMESPVSGREKGKHNKGVAKHRTAEEQERFRKLDEARAAEEAARAARPNLFRKPALDEMGADGAVPAKKPLFAKPSIDDMGPGTDMPTPAGAVSRSLFKKQSASEAHGSDFGIPGEPVRPLFKKNSLDEMTVRRTEKPVEGKVPAKPQPISHPVGAGRTDVKDRDDSAKPIVRQRAGIGSYEDPGDARREKRRPGKTGRPGK
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 97533
Sequence Length: 870
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q7UFR2
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MSITKLAPAAFDLHQPFPPSGDQPAAIAKLIEGIQSGKTAQTLLGATGTGKTYTMANVIASVQRPALILSHNKTLAAQLYGEFKEFFPNNAVHYFVSYYDYYQPEAYIPQRDVYIEKDSSINEEIDRLRLATTSSLVSRRDVVIVASVSSIYGLGSPDDYRQLVVDLHQGEQTRRDHLLLKFVDLQYQRNDIQFERGKFRVRGDSIELWPSYEEFAYRIEMWGDEIEKISLIKPTSGETIKTVEHLYIYPCKHFVMPEDRIQRAIRLLREELTQQLEIFQSQGKLLEAQRLSARTKFDLEMLAEVGHCPGIENYSRPLSGKEPGATPDTLYDFFPKDFITFVDESHVTVPQVRAMYAGDRSRKITLVEHGFRLPCALDNRPLKFDEWEERTGQICFVSATPSDYELERTGGEVVEQIIRPTGLLDPEVEIVSARGQVTHLLEQVRIRAERDERVLVTALTKRLAEDLATYFQEQGVKCRWLHSELNAFERVDLLQELRAGQFDCLVGVNLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNANSRVILYADKVTDSMQMAIDETERRRVIQMEYNAKHGIVPKTVRKSIRKGIDTEAANHKESTRKAQDSGEAIYITIEYVDKLEQEMLAAAEDLEFERAARLRDRVLQLKEHIGKPLSEVEIVDEKSAGKSGGRGRGRRGAKKKGASKGTKIPRPKRG
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 80351
Sequence Length: 708
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q1RHI9
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MSNFSIISDYKPAGDQPKAIDEIIKGLNNKKRSQMLLGITGSGKTFTMANIIERTNRPTLIMAHNKTLAAQIYSEMKSIFPKNAVEYFVSYYDYYQPEAYIPKTDVFIEKDSSINEQIDLMRHSATRSLLERRDVIVVSSVSCIYGLGSPDLYYQMTVNLEPGKSYPRDKLLNDLVNLQYERNDIGFERGCFRVKGDNVDVFPSHYSDKAWRLSFFGNELEYIHEFDPLTGEKLVKLDKAIIYGNSHFVMPKETVNKAISEIEEELQKRIAFLKSQDKLLETQRINQRTQYDLEMLTETGSCKGVENYSRFFTGRKAGEPPPTLFEYLPKDALLFVDESHVSVPQIRAMYNGDRARKEVLVEHGFRLPSALDNRPLKFEEWDNFRPQTVFVSATPSLFELNETGGEVVELIIRPTGLLDPECIIKPATNQVEDLVGEIQSTIAKGFCVLVTTLTKKMAEDLTNYLQELKYKTSYLHSNIHTLERIEILRDLRQGTIDILVGINLLREGLDIPECGLVAILDADKEGFLRSEVSLIQTIGRAARNSEGRVILYADKMTKSIDKAISETMRRRTIQQEHNEKYGIIPKTINRTIHALAELEKVDSKLDKKQTHNLFENPAKLKAHIDKLRKEMLKAASNLEFEQAAKLRDQLKTLEEAALELS
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Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 75518
Sequence Length: 661
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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P0A5A4
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MSVHATDAKPPGPSPADQLLDGLNPQQRQAVVHEGSPLLIVAGAGSGKTAVLTRRIAYLMAARGVGVGQILAITFTNKAAAEMRERVVGLVGEKARYMWVSTFHSTCVRILRNQAALIEGLNSNFSIYDADDSRRLLQMVGRDLGLDIKRYSPRLLANAISNLKNELIDPHQALAGLTEDSDDLARAVASVYDEYQRRLRAANALDFDDLIGETVAVLQAFPQIAQYYRRRFRHVLVDEYQDTNHAQYVLVRELVGRDSNDGIPPGELCVVGDADQSIYAFRGATIRNIEDFERDYPDTRTILLEQNYRSTQNILSAANSVIARNAGRREKRLWTDAGAGELIVGYVADNEHDEARFVAEEIDALAEGSEITYNDVAVFYRTNNSSRSLEEVLIRAGIPYKVVGGVRFYERKEIRDIVAYLRVLDNPGDAVSLRRILNTPRRGIGDRAEACVAVYAENTGVGFGDALVAAAQGKVPMLNTRAEKAIAGFVEMFDELRGRLDDDLGELVEAVLERTGYRRELEASTDPQELARLDNLNELVSVAHEFSTDRENAAALGPDDEDVPDTGVLADFLERVSLVADADEIPEHGAGVVTLMTLHTAKGLEFPVVFVTGWEDGMFPHMRALDNPTELSEERRLAYVGITRARQRLYVSRAIVRSSWGQPMLNPESRFLREIPQELIDWRRTAPKPSFSAPVSGAGRFGSARPSPTRSGASRRPLLVLQVGDRVTHDKYGLGRVEEVSGVGESAMSLIDFGSSGRVKLMHNHAPVTKL
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Function: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 85050
Sequence Length: 771
EC: 5.6.2.4
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Q9CD72
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MSVHTTDAKPDSEVDRLLDGLNPQQRQAVVHEGSPLLIVAGAGSGKTTVLARRIAYLIAARSVGVSQILAITFTNKAAAEMRERVARLVGDHTGPSMWVSTFHSTCVRILRNQASLIGGLNSNFSIYDVDDSRSLLQMIGQDMGLDIKRYSPRLMANAISNLKNELIDAESAVANLSSDTDDLARTVATVYGEYQRRLRTANALDFDDLIGETVGILQAFPQIAEHYRRRFRHVLVDEYQDTNHAQYVLVRELVGHGARNSPDDMPPGELCVVGDADQSIYAFRGSTISNIEDFERDYPDTTTILLEQNYRSTQNILSAANSVIARNFGRRDKRLWTDAGKGELIVGYVSDNEHDEAKFIADEIDALVGGGEITYDDVAVLYRANNLSRSLEEVFIPTGIPYKVVGGFCFYESKEIRDLIAYLRVLDNPGDAVSMRRILNTPRRGIGDRAEACVSVYAENTGTSFADALQAVAEGKVPMLNTRSVKAIAGFVALLDDLRCRVDDDLGELVESVLERSGYLRELESSTDPQELARLDNLNELVSFAHEFSTEQANAAALAKSLHTPEDEDVPDTGALAAFLEKVSLMSDTDQIPENNSGVVTLMTLHAAKGLEFPVVFVTGWEDGMLPHMRTLGDPTELSEERRLAYVGITRARQRLYLSRAITRSSWGQPILNPESRFLREIPPELIDWRRSILTDSYSTPASGASRFGRVRPSSIRSGASKRALLVLAPGDRVTHDKYGLGRVEEVSGVGESAISLIDFGSSGRIKLMHNHAPVTKL
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Function: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 85635
Sequence Length: 778
EC: 5.6.2.4
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P53528
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MVMVVNPLTAGLDDEQREAVLAPRGPVCVLAGAGTGKTRTITHRIAHLVGAGHVATGQVLAVTFTQRAAAEMRSRLRALGAAVQAVSDFGVVRVLTFHAAAHRQLRYFWPRVIGDTGWQLLDSKFATVARAASSVRLHAGTDDVCDLAGEIEWAKASLIGPEEYVAAVAAIGRDTPLDAAQIASVYAAYEALKARGNGVPGVTLLDFDDLLLHTAAAIENDAAVAEEFRDRYRCFVVDEYQDVTPLQQRVLSAWLGDRDDLTVVGDANQTIYSFTGASPCFLLDFPRRFPDATVVRLERDYRSTPQVVSLANQVIAAAHGRVADSKFQLSGQREPGPAASFHEYSDEPAEAAAVAASIARLIEFGTSPSEIAVLYRVNAQSEAYEEALTEVGIAYQVRGGEGFFNRQEIKQALLALQRSAERSSQTEPNSPLSDVVRGVLEPLGLTAEKPVGSRARDRWEALTALAELADDEVAQHPRLDLPGLLAELRLRADARHPPVVQGVTLASLHAVKGLEWDAVFLVGLADGTLPISRALAHGAESEPVEEERRLLYVGITRARVYLALSWALSRTPGGRQSRKPSRFLNDIAPQMGQNPASSRSRRNRTATLRCRICKNDLTTPAAVMLQRCQICAADVDEELLLQLKAWRLSTAKEQNVPAYVVLTDNTLIAIAELLPADEAALIAVPGMSVRKIEQYGSDVLQLVRCRAVAVRTQT
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Function: DNA-dependent ATPase, stimulated equally by ss- and dsDNA. Has both ATPase and helicase activities (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 77343
Sequence Length: 714
EC: 5.6.2.4
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P03018
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MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
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Function: A helicase with DNA-dependent ATPase activity . Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA . Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 81990
Sequence Length: 720
EC: 5.6.2.4
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P45612
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MSVDNLLDLLNDQQLAAVLNIDKPVRIIAGAGSGKTRVITTKIAYLIEKQNIDPSRILAVTFTNKAAKEMKERVLQITNNSFKSPFISTFHSWCSKVLRIDGKHIGLEDKFLIIDSDDQKRIIKSALKESNIELSENDKKTFDKKILYKIKEWKEELVDPSEAILNATSTLEKNFAVIYRLYQNTLLKNNSLDFDDLQIYVYRLFKQNNEILNKWRNAYDYVLVDEFQDTNELQFSLIKFLTINTNHLTVVGDPDQTIYSWRGAKLDIILNFNKTYSNAISIVLNQNYRSTKQILDISNSFIKNNKFREHKEIFTNNKSGKKVVLKECNSKTSEASYVSSKIKELVKQGYHYKDIFILYRMNAWSQEFEKELANKKIPFQLIGGIKFRERKVIKDAMAFLKMISIKDNLSSQRVLGLIPKIGNITIEKIINTANLNHLNIFDLITNEDKTLLHSITKNLDELIEVFKTAHQLYLDNTNIEEILKYLLIQSGYENKLKIRKEQDDLENINALYDQLKRFDEDFDPKYYSEENKLIAFLQEEALTSDIDEAEQIDKVSLLTVHAAKGLENKVVFITGLNQGIFPSRISETSINELEEERRALYVALTRAKDELFLTYVKGDYSHIMQSELKPSKFIHELDKDLYEFETQFLNTLLYDSNDYKQSSFYVSPKQHNLYNVGDHVEHKLFGKGVVVKIINDQLQISFTNSSYGIMMIATNNSALSKV
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Function: Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 83641
Sequence Length: 722
EC: 5.6.2.4
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P47486
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MNEQQKQAISCGKGVNVVYSGAGTGKTTIITNRFAYLVNKEKVDPSRILAITFTKKAAKEMQFRILKLIDSSLAEKTNIYTFHSFCNKFLIQTLKKRFIIDDDISYFLKEFLADSKLDINLAKQIIDNFKNTFADFEINKLDQDERLISLCEHSLLNKDEEYSTLKTQLINAFISYEKNKILNNKLDFHDLLIKTCNLLSNDNDLLNQWSEQFQHILVDEFQDTNQIQYELIKMLVTKNKNLFLVGDNNQMIYRWRGAVNGIITALKHDFNVPKSNEFFINQNYRCDQNILAVANQILLKIMAYEKQVKTEKNLLFSTLNSDKKPVYFQAESVENQANWIFNKIKALNQTEKINFKDMAILFRKNRDITTMVELIEADGTIPLPKQKSYFNQLVKLQRVLIAISTRTNLDIKRALQALKIWSNDLKELWKQSDKTNLFDFLKWSELNQKNHSSKLKATGYFNLLIKLAEDQQINLLFTELFKKLKVDQTIENLLWKKLTEFQKDKTEFSLSEFITSLALEFDSIIENSSDTINLLTVHAAKGLEFEAVFIYGMNQGDFPLFLSQNQNDEQHLIDELKLFYVAITRAKRFLFITAVLQINNNSIKPSSFLNYINKSEYLDIATINYVLEQDDDFFDSTKKTDYTKKLRKESLDIIVGDLVTSRYFGKGVVVEVRDKEVLVAFKDTRYGMKWILKNHKSLTKALY
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Function: Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 81959
Sequence Length: 703
EC: 5.6.2.4
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F4IHS9
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MGEMKSMQMGVIGALFLSVASSVSIVICNKALMTNLGFPFATTLTSWHLMVTYCTLHVAYKLNFFENKPIDMRTVVLFGLLNGISIGLLNLSLGFNSIGFYQMTKLAIIPFTVLLETLFLNKKFSQKIKFSLFLLLVGVGIASITDLQLNFVGSVLSLLAIATTCVGQILTNTIQKRLNVTSTQLLYQSAPFQAAILFVSGPFVDKYLTSLNVFSFHYSPIVVGFITLSCLIAVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYTLLHDPFTPRNIAGILIAVLGMLLYSYFCSVASKSKQASSDSTFLGKDRDTTPLLGQENENHHEAKKLDKHSPV
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Function: Nucleotide-sugar transporter that transports UDP-xylose and UMP in a strict counter-exchange mode.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37444
Sequence Length: 342
Subcellular Location: Golgi apparatus membrane
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Q8RXL8
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MSEGQKFQLGTIGALSLSVVSSVSIVICNKALISTLGFTFATTLTSWHLLVTFCSLHVALWMKMFEHKPFDPRAVMGFGILNGISIGLLNLSLGFNSVGFYQMTKLAIIPCTVLLETLFFRKKFSRKIQFSLTILLLGVGIATVTDLQLNMLGSVLSLLAVVTTCVAQIMTNTIQKKFKVSSTQLLYQSCPYQAITLFVTGPFLDGLLTNQNVFAFKYTSQVVFFIVLSCLISVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYVLLRDPFDWRNILGILVAVIGMVVYSYYCSIETQQKASETSTQLPQMKESEKDPLIAAENGSGVLSDGGGGVQQKTVAPVWNSNKDFQA
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Function: Nucleotide-sugar transporter that transports UDP-xylose and UMP in a strict counter-exchange mode.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39038
Sequence Length: 357
Subcellular Location: Golgi apparatus membrane
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Q9UBK9
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MATPPKRRAVEATGEKVLRYETFISDVLQRDLRKVLDHRDKVYEQLAKYLQLRNVIERLQEAKHSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLAEALKFIDRKSSLLTELSNSLTKDSMNIKAHIHMLLEGLRELQGLQNFPEKPHH
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Function: Involved in gene transcription regulation . Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription . Together with URI1, associates with chromatin to the NKX3-1 promoter region . Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm . May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity . Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling . Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC . Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM .
PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO7; leading to proteasomal degradation.
Sequence Mass (Da): 18246
Sequence Length: 157
Subcellular Location: Cytoplasm
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Q8UAW0
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MRHTWRWFGPVDKVTVQDAAQAGAEGIVSALHHITTGDVWPVDEITKRHEAIKAGGLYWDVVESVPVSEDIKTQTGDWKNHIANWQETLRRLSASGIRTVCYNFMPVLDWTRTDLRWETRHGARAMRFDLTDFAAFDIHILKRPDAKADYPDWLLEEAAKRFAEMPDTKIAALGRNIGAGLPGSADGYTLAQLLEKLRSYHGINRGRLQQNLIDFLSEVTPVAEEVGINICAHGDDPPWPLLGLPRILSTEADYAHMLSQVDSRANGVTLCTGSLGARADNDLPFIAGRFADRIHFVHLRNVTRDTDTVPCSFFEDEHLEGGTDMVAVIAALITEEARRRAEGRDDHTIPMRPDHGQEILDDLTRGAQPGYPAIGRLKGLAELRGIERTLSHGRFGLATGKG
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Function: Catalyzes the dehydration of D-mannonate.
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 44690
Sequence Length: 402
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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Q8UA46
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MKETWRWFGESDPITLEHVRQTGASGVVTALHQIPDGTAWPAEEIAKRKAMIEAAGLEWSVCESIPMEQSIKRGDADAPKAIARWKDTLSRLGRAGVPVVCYNFMPVVDWTRTNLRWQARNTGLALRFEMADFVAYDVFILKRIRAAENYDPALVARAEERFAQMSEDEQSLLERNIIAGLPGGALVQTRQSIAALIASFDGIDSATMQGNLLAFLKEVVPVAEEVGVHLGIHPDDPPFSLFGLPRVVSTPADIRAILSAVESPNNGITLCTGSYGARSDNDLVAMAKEFASRVNFAHLRNVTVEADGSFFEDDHLDGGADMIGVIEALLREERSTAKAGRRTNIPMRPDHGHLLGDDITKKTNPGYSYIGRMKGLGELRGVIRTIERQLRREEAAA
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Function: Catalyzes the dehydration of D-mannonate.
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 43649
Sequence Length: 397
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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Q65IW0
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MQMTFRWYGDSDPVTLEYIRQIPGVTGIVSAIYDIPVGEAWPYEKIVELKEKIENHGLSLSVIESVPVHEDIKLGLPTRDQYIENYKTTIRNLAKAGVKIVCYNFMPVFDWTRSSLDYALEDGSTALIYEEEKVRQMNPLHGELKLPGWDTSYEDGQLKNLFQQYQHMTEEDLWENLSYFIKAVIPAAENEQVKMAIHPDDPPWPIFGLPRIITNKENLERLIHLYDSSFNGLCLCSGSLGVKSTNDIPELIRYFGKKGKVNFVHLRNIKIIGEKSFQESSHRSEDGSLDMYEIVRALRDIDFAGPARPDHGRMIWGETGKPGYGLYDRALGAVYLNGMWETLTKEKKRIALECNK
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Function: Catalyzes the dehydration of D-mannonate.
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 40830
Sequence Length: 356
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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O34346
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MNMTFRWYGRGNDTVTLEYVKQIPGVKGIVWALHQKPVGDVWEKEEIRAETEYIQSYGFHAEVVESVNVHEAIKLGNEERGRYIENYKQTIRNLAGFGVKVICYNFMPVFDWTRTDMFRPLEDGSTALFFEKAKVESLDPQELIRTVEEASDMTLPGWEPEKLARIKELFAAYRTVDEEKLWDNLSFFLQEILPVAEAYGVQMAIHPDDPPWPIFGLPRIITGEASYKKLRAISDSPSNCITLCTGSMGANPANDMVEIAKTYAGIAPFSHIRNVKIYENGDFIETSHLTKDGSINIQGVMEELHKQDYEGYVRPDHGRHLWGEQCRPGYGLYDRALGIMYLNGLWDAYEAMAKKEVGI
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Function: Catalyzes the dehydration of D-mannonate.
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 41024
Sequence Length: 359
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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Q68F29
|
MSFFGFGPAAELDIALTDGESRRRAEHKTEDGKKEKYFLFYDGETVSGRVTVNLRNPGKRLEHQGLKIEFIGQIELYYDRGNHHEFVSLVKDLARPGEISQSQSFDFEFTHVEKPYESYTGQNVKLRYFLRATLSRRLNDVVKEMDIVVHTLSTYPELNSSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIKHMEIDIIKRETTGTGPNVYHENDTIAKYEIMDGAPVRGESIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEIVLWRKGDIVRKSMSHQAAIASQRFEGTSHPETRPQHSGAAAVEQEHE
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Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. Retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39188
Sequence Length: 337
Subcellular Location: Cytoplasm
|
O70410
|
MASRQISLALGFLAFLWAVLGAQNKTEEVQCRLMAKFNLSGYVDAKNHSLVIAGLFPIHSRIIPVDEAILEPVSPMCEGFNFRGFRWMKTMIHTIKEINERKDILPNHTLGYQIFDSCYTISKAMESSLVFLTGQEEFKPNFRNSTGSTLAALVGSGGSSLSVAASRILGLYYMPQVGYTSSCSILSDKFQFPSYLRVLPSDNLQSEAIVNLIKHFGWVWVGAIAADDDYGKYGVKTFKEKMESANLCVAFSETIPKVYSNEKMQKAVKAVKTSTAKVIVLYTSDIDLSLFVLEMIHHNITDRTWIATEAWITSALIAKPEYFPYFGGTIGFATPRSVIPGLKEFLYDVHPNKDPNDVLTIEFWQTAFNCTWPNSSVPYNVDHRVNMTGKEDRLYDMSDQLCTGEEKLEDLKNTYLDTSQLRITKQCKQAVYAIAHGLDHLSRCQEGQGPFGSNQQCAYIPTFDFWQLMYYMKEIKFKSHEDKWVILDDNGDLKNGHYDVLNWHLDDEGEISFVTVGRFNFRSTNFELVIPTNSTIFWNTESSRRPDSFCTQVCPPGTRKGIRQGQPICCFDCIPCADGYVSEKSGQRECDPCGEDDWSNAGKSKCVPKLVEFLAYGEALGFTLVILSIFGALVVLAVTVVYVIHRHTPLVKANDRELSFLIQMSLVITVLSSLLFIGKPCNWSCMARQITLALGFCLCLSSILGKTISLFFAYRISVSKTRLISMHPIFRKLIVLVCVVGEIGVCAAYLVLEPPRMFKNIEIQNVKIIFECNEGSVEFLCSIFGFDVLRALLCFLTTFVARQLPDNYYEGKCITFGMLVFFIVWISFVPAYLSTKGKFKVAVEIFAILASSYGLLGCLFLPKCFIILLRPKRNTDETVGGRVPTVDRSIQLTSASVSSELNSTTVSTVLDE
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Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102349
Sequence Length: 912
Subcellular Location: Cell membrane
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Q6TAC4
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MKLLTAFSPLVVLILFQEQISCYYLTKYASSGYYQDADFVIGGLFSLRVTDGDTFISRSGVEDTSHIAEYVFADLIKYYQHILAMVFAIEKINKDPNILFNKSLGFFLFNVNFIEMKAAEGSMALLSGESPPIPNYSCRPEKTDKLVAVIGGISTSISIQISRVLSLYNVPQISYAPFDQILGTRVQLQSPYQFSMHTAALYQGIVQLLLYFTWIWVGLVVPDDMRGELYLRDITKEMISHGICFAFAEKVTEYSSMDTVNWKHFMERLTLTPVIITVGDTHSLLRIVYFVIFYNLSGNVWITTSDWYITTLPFEQNLIYTHFGGGLSFSFHMDEILGFKDFLRSVQPRKYPHDIFIRHVWSSLFGCPHYYQHRLWDLSQCEPNGSLSTRPLHAWDMNTSPYSYKVYAAVYAIAQALHEELSLRVEGDSSNKCLLQAPLPWKLHPFLQKGQLGRSTNEENTVNKEVSAIKLDIFNYQSLQSGTEAHVKVGEFVFDSHSVQHLSLNDKIITWGKHRSQTPLSVCSQSCPFGFSKTAVEGKPFCCFDCVPCPDGEIANKTDMDQCIKCPEDQYPNKQRNQCLPKIMVFLAHEDPLGTVLVSLAISLSAFSAMILGLFICYRETPIVRANNRNLSYLLLISLKLCFSCSLMFIGQPRTVTCVLRQIIFGIVFSIVISAILAKTFIVVMAFKAIKPGSILKMGMVTRLSNAIVCCGSIIQVCICAVWLGTYPPFPDVDMHSEFGQIILWCNEGSTLAFYCVLGYLGFLASLSLLIAFLARRLPDSFNEAKTITFSMLVFCSVWISFVPAYLSSKGKTMVAVEILSILASSAGLLGCIFLPKCYVILLKSGGHSRKKFFK
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Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96200
Sequence Length: 855
Subcellular Location: Cell membrane
|
O94262
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MSEPKPMQMSVETETVLNVSQVQIPSSCDRKASLETLKTKKNAQKKKKISLPNVMTSKAAMFAARVASAVDQDPNDEESENFVYENLIPTNDDELHSPSASIHSFQTYNLPLEMLPTINHVPYYGSAGTNALNGGPLSNSRKLIPKRSAKFSSMVGSSDTRCNSPTTARGLATSPLQINPTTSKSPLLNKKLSSTSQEPFRTSRRSGQESGDVTTKMLRNLLHKRLWISFFFACFVVLSLVYFHYAVQPLL
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Function: Component of the PI(3,5)P2 regulatory complex that regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Directly involved in vacuolar membrane scission. Required for normal vacuole acidification, inheritance and morphology (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27747
Sequence Length: 251
Subcellular Location: Endoplasmic reticulum membrane
|
P0CM61
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MGSALSSCCSPRRKNAYEPLLLETEREAVADLLQYLENRSTTNFFAGSPLAALTTLSFSENVDLQRSAALAFAEITEKEVREVGRDTLDPVLYLLSSHDPEVQRAASAALGNLAVNAENKLLVVSLGGLEPLIRQMLSPNVEVQCNAVGCITNLATHDENKTQIAKSGALVPLTRLAKSKDMRVQRNATGALLNMTHSDENRQQLVAAGAIPVLVSLLNSPDTDVQYYCTTALSNIAVDAANRKKLAQSEPKLVQSLVQLMDSQSLKVQCQAALALRNLASDSKYQLEIVKFGGLKPLLRLLHSSYLPLILSAAACVRNVSIHPANESPIIESGFLQPLIELLSFDENEEVQCHAISTLRNLAASSEKNKGAIVEAGAVEKIKSLVLTVPLAVQSEMTACVAVLALSDDLKPQLLEMGICEVLIPLTNSPSVEVQGNSAAALGNLSSKAAEDYAPFNAVWNKPDGGLHAYLVRFLSSADITFQHIAVWTIVQLLEAEDEQLTNNIRSSPILISSIRQLAKSPPPSRAGGAPRHDPNDPSAGSSEDEFEDGLTDQEGEGEIVSLARRILDLTEVGEEGDEFGERAGRNVPVGSHGQAPGQGQTSQVGSMGSEHAALRASVHRALSGGGRDR
|
Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Location Topology: Lipid-anchor
Sequence Mass (Da): 67316
Sequence Length: 630
Subcellular Location: Vacuole membrane
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Q4I1B1
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MGICSSTCCGGRARDGLYEPVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVFSENIDLQRSASLTFAEITERDVREVDRDTLEPILFLLQSPDIEVQRAASAALGNLAVDTENKVLIVQLGGLTPLIRQMMSPNVEVQCNAVGCITNLATHEENKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSPDVDVQYYCTTALSNIAVDASNRRKLAQSEPKLVQSLVNLMDSTSPKVQCQAALALRNLASDEKYQLDIVRANGLHPLLRLLQSSYLPLILSAVACIRNISIHPMNESPIIETNFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKALVLDAGAVQKCKQLVLDVPITVQSEMTAAIAVLALSDDLKSHLLNLGVCGVLIPLTHSPSIEVQGNSAAALGNLSSKVGDYSIFVQNWTEPQGGIHGYLCRFLQSGDATFQHIAVWTLLQLFESEDKTLIGLIGKAEDIIEHIRSIANRQIEPDNEFEDEDEGEVVNLAQRCLELLGQSMSKAHIEG
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Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Location Topology: Lipid-anchor
Sequence Mass (Da): 60829
Sequence Length: 559
Subcellular Location: Vacuole membrane
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Q7RXW1
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MGASCSSCCGGKSRDGLYDNVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVYSENIDLQRSASLTFAEITERDVRAVDRDTLEPILFLLQNSDIEVQRAASAALGNLAVNTDNKVLIVQLGGLAPLIRQMMSPNVEVQCNAVGCITNLATHEDNKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSTDVDVQYYCTTALSNIAVDANNRRKLAQTEPRLVQSLVNLMDSSSPKVQCQAALALRNLASDEKYQLEIVRASGLGPLLRLLQSSYLPLILSAVACIRNISIHPMNESPIIEAGFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKALVLEAGAVQKCKQLVLEVPVTVQSEMTAAIAVLALSDELKTNLLELGVFEVLIPLTKSPSIEVQGNSAAALGNLSSKVGDYSVFIHNWNEPSDGIHGYLSRFLASGDATFQHIAIWTLLQLLESEDKKLIGLIGKSNDIVDMIRQIANRQIESDNELEDDDEGEVVSLAQRCLELLGQGNAKAHIEG
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Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Location Topology: Lipid-anchor
Sequence Mass (Da): 60533
Sequence Length: 559
Subcellular Location: Vacuole membrane
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O43028
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MGNCLSCCEKSKDEQYEPLLADREREAVADLLSFLEDRNEVNFYSEEPLRALTILAYSDNLDLQRSAALAFAEITEKDVREVDRETIEPVLFLLQSPDAEIQRAASVALGNLAVNAENKALVVKLNGLDLLIRQMMSPHVEVQCNAVGCITNLATLDENKSKIAHSGALGPLTRLAKSKDIRVQRNATGALLNMTHSYENRQQLVSAGTIPVLVSLLPSSDTDVQYYCTTSISNIAVDAVHRKRLAQSEPKLVRSLIQLMDTSSPKVQCQAALALRNLASDERYQIEIVQSNALPSLLRLLRSSYLPLILASVACIRNISIHPLNESPIIDAGFLRPLVDLLSCTENEEIQCHAVSTLRNLAASSERNKRAIIEANAIQKLRCLILDAPVSVQSEMTACLAVLALSDEFKSYLLNFGICNVLIPLTDSMSIEVQGNSAAALGNLSSNVDDYSRFIECWDSPAGGIHGYLVRFLSSEDSTFAHIAAWTIVQLLEAGVPRLTAFIQSSDDIIELLNDIVARDANNGEYEDGEGDVILLSGRALHLIEQDTDS
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Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Location Topology: Lipid-anchor
Sequence Mass (Da): 60233
Sequence Length: 550
Subcellular Location: Golgi apparatus membrane
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P39968
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MGSCCSCLKDSSDEASVSPIADNEREAVTLLLGYLEDKDQLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEITEKYVRQVSREVLEPILILLQSQDPQIQVAACAALGNLAVNNENKLLIVEMGGLEPLINQMMGDNVEVQCNAVGCITNLATRDDNKHKIATSGALIPLTKLAKSKHIRVQRNATGALLNMTHSEENRKELVNAGAVPVLVSLLSSTDPDVQYYCTTALSNIAVDEANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLASDTSYQLEIVRAGGLPHLVKLIQSDSIPLVLASVACIRNISIHPLNEGLIVDAGFLKPLVRLLDYKDSEEIQCHAVSTLRNLAASSEKNRKEFFESGAVEKCKELALDSPVSVQSEISACFAILALADVSKLDLLEANILDALIPMTFSQNQEVSGNAAAALANLCSRVNNYTKIIEAWDRPNEGIRGFLIRFLKSDYATFEHIALWTILQLLESHNDKVEDLVKNDDDIINGVRKMADVTFERLQRSGIDVKNPGSNNNPSSNDNNSNNNDTGSEHQPVEDASLELYNITQQILQFLH
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Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole (cvt) . Involved in the formation of nucleus-vacuole junctions (NVJs) during piecemeal microautophagy of the nucleus (PMN) . NVJs are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane . Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process .
PTM: Palmitoylated on one or more of its N-terminal cysteine residues by PFA3, which is required for vacuole fusion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 63208
Sequence Length: 578
Domain: Comprises a flexibly connected N-terminal H1 helix followed by armadillo repeats (ARMs) that form a right-handed superhelical structure.
Subcellular Location: Vacuole membrane
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O07783
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MNVRRALADTSVFIGIEATRFDPDRFAGYEWGVSVVTLGELRLGVLQASGPEAAARRLSTYQLAQRFEPLGIDEAVSEAWALLVSKLRAAKLRVPINDSWIAATAVAHGIAILTQDNDYAAMPDVEVITI
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Function: Toxic component of a type II toxin-antitoxin (TA) system. Probably exerts its toxic effect by binding to mRNA, inhibiting translation. Binds to, recognizes and cleaves ssRNA at ACGC and AC(A/U)GC sequences, usually between the G and C; cleavage is not very efficient, nor is cleavage required to inhibit protein synthesis. Upon expression in situ, in M.smegmatis or E.coli inhibits cell growth and colony formation; in at least E.coli also causes increased levels of cellular RNA. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB4.
Sequence Mass (Da): 14112
Sequence Length: 130
Subcellular Location: Secreted
EC: 3.1.-.-
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P96917
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MSTTPAAGVLDTSVFIATESGRQLDEALIPDRVATTVVTLAELRVGVLAAATTDIRAQRLATLESVADMETLPVDDDAARMWARLRIHLAESGRRVRINDLWIAAVAASRALPVITQDDDFAALDGAASVEIIRV
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Function: Probable toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is VapB5. Has limited RNase activity on substrates; activity is seen with a VapC5-VapB5 complex.
Sequence Mass (Da): 14408
Sequence Length: 135
Subcellular Location: Secreted
EC: 3.1.-.-
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O57728
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MVAKGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPGLLTSIYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIVEIAEEGDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLVLTKEFGLIKIKELYEKLDGKGRKIVEGNEEWTELEKPITVYGYKDGKIVEIKATHVYKGVSSGMVEIRTRTGRKIKVTPIHRLFTGRVTKDGLILKEVMAMHVKPGDRIAVVKKIDGGEYIKLDSSNVGEIKVPEILNEELAEFLGYLMANGTLKSGIIEIYCDDESLLERVNSLSLKLFGVGGRIVQKVDGKALVIQSKPLVDVLRRLGVPEDKKVENWKVPRELLLSPSNVVRAFVNAYIKGKEEVEITLASEEGAYELSYLFAKLGIYVTISKSGEYYKVRVSRRGNLDTIPVEVNGMPKVLPYEDFRKFAKSIGLEEVAENHLQHIIFDEVIDVRYIPEPQEVYDVTTETHNFVGGNMPTLLHNTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIDPEWKAMRDKAMALLQKESELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRGVPLEEIAKLPVREEIGRMKFERDVSKIRSLIDKTNEQFEELFKKYGA
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Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 107855
Sequence Length: 964
EC: 7.1.2.2
|
P31406
|
MAGGIELAKKAIRSLKNYDEHENRYGSIFSVSGPVVVAANMLGCSMYELVRVGHEELVGEVIRIHQDKCTIQVYEETSGLTVGDPVQRTGKPLSVELGPGLAETIYDGIQRPLKQIFDKSQSIYIPRGINTESLNREHKWDFTPNKDLRIGDHVSGGDVFGSVFENSLFNDHKIMLPPRARGTVTYIAEAGSYHVDEKLLEVEFNGKKHSFSMLHTWPVRAARPVADNLTANQPLLTGQRVLDALYPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDLIVYVGCGERGNEMAEVLMDFPELTIDINGKPEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYYRDQGKNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGAKLASFYERAGRARCLGSPDREGTVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINTSLSYSKYINALQPWYEERVPGFNTLRDQIKQIIQQEDSMLEIIQLVGKSALSETDKVTLDIAGIIKNDFLQQNGYSDYDRCCPLYKTYHMMRNMIAYYTKAKSAVETGSVPWSKIKESTSDIFYELTSMKFENPNEGEKEIVEHYETLHKKIEDKFHTLTE
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Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68806
Sequence Length: 619
Subcellular Location: Endomembrane system
EC: 7.1.2.2
|
A3DNQ6
|
MSLGITGKIYRVSGPLVIAENMRGSKVYEVVEVGSDRLIGEIIGVEGDKAIIQVYEDTSGLRVGDPVYGTGYPLAAELGPGLVGSIYDGIQRPLPLLQELVGFFVKRGVKAKPLPRNKKWHFKPLVKQGEKVGPDDVIGYVEETPVIKHYIMIPPDTHGVVEEIVGEGEYTIVDPIARINGKEIVMLQKWPVRKPRPYREKLEHREPVLTGQRVIDFFFPLAKGGKAAIPGGFGTGKTVTLQQLTKWSAVDIAIYVGCGERGNEMADALHSFRRLVDPRTGKALVERSVFIANTSNMPVAARETSIFLGATIGEYFRDMGYHVLMVADSTSRWAEAMREISGRLEELPGEEGYPAYLGSRLASFYERSGYVKTLGRPDRTGSLTIMGAVSPPGADFSEPVTQATLRIVRALYALDVNLAYRRHYPAINWLISYSLYVDNVTDWWHKNIDPSWRELREKALAILQKEAELEELVRLVGAEALPEEDKLLLEVARMIREDFLQQNAFHEIDTYCPPRKAVLMMKAIMLFYELGLEAIKRGISMEKIRELKSRVKIARMKEIPNIDFEDAFKSLFEDIRRDFESLMKEAETIAEL
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Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 66549
Sequence Length: 592
EC: 7.1.2.2
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P11593
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MADPRVPSSYNVTPRIRYNTVGGVNGPLVILDNVKFPRYNEIVTLTLPDGTQRSGQVLEARGNRAVVQVFEGTSGIDVKKTKVEFTGESLKLGVSEDMLGRIFDGSGRAIDKGPKVLAEEYLDINGSPINPYAREYPQEMISTGISAIDTMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVQRQGITNKGVHDGHEENFSIVFGAMGVNLETARFFTRDFEENGSLGRTTLFLNLANDPTIERIITPRLALTTAEYYAYQLEKHVLVILTDLSSYCDALREVSAAREEVPGRRGFPGYMYTDLSTIYERAGRVAGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRGLHNRGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGRDAAAMKAVVGEEALSNEDKLSLEFLDKFERSFIAQGPYESRTIFESLDLAWSLLRIYRKDMLNRIPKKIIDEFYSRSAADRKGKGKDKPTTKDTRDTAAPEEENLIDA
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Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56808
Sequence Length: 513
Subcellular Location: Vacuole membrane
|
Q9C9Z8
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MNDADVSKQIQQMVRFIRQEAEEKANEISISAEEEFNIERLQLLESAKRKLRQDYDRKLKQVDIRKRIDYSTQLNASRIKYLQAQDDVVTAMKDSAAKDLLRVSNDKNNYKKLLKSLIIESLLRLKEPSVLLRCREMDKKVVESVIEDAKRQYAEKAKVGSPKITIDEKVFLPPPPNPKLPDSHDPHCSGGVVLASQDGKIVCENTLDARLDVAFRQKLPQIRTRLVGAPETSRA
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Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26853
Sequence Length: 235
Subcellular Location: Vacuole membrane
|
P0CAN7
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MNDADASIQIQQMVRFIRQEAEEKANEISISSEEEFNIEKLQLVEAEKKKIRQEYEKKEKQVDVRKKIDYSMQLNASRIKVLQAQDDIVNAMKEEAAKQLLKVSQHGFFNHHHHQYKHLLKDLIVQCLLRLKEPAVLLRCREEDLDIVESMLDDASEEYCKKAKVHAPEIIVDKDIFLPPAPSDDDPHALSCAGGVVLASRDGKIVCENTLDARLEVAFRNKLPEIRKSLFGKVGAA
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Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27085
Sequence Length: 237
Subcellular Location: Vacuole membrane
|
O43046
|
MSSQSYRERTLVSVIGDDDTVTGMLLAGTGQVNENGDKNFFIITQKTTDEQIAEAFDDYTTKRKDIAIVLINQFAAERIRDRIENHVQAFPAVLEIPSKDDPYDPEKDSILRRVRKIIGE
|
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13618
Sequence Length: 120
Subcellular Location: Vacuole membrane
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A7TMI5
|
MSVDKRTLIAVIGDEDTTTGLLLAGIGQITKETNEKNFFIYEDGKTTKEQILNNFINYTQERQDIAILLINQHIAEKIRSDIDNYTNAFPAILEIPSKDHPYDPEKDSVLKRVRRLFGE
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Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13640
Sequence Length: 119
Subcellular Location: Vacuole membrane
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P39111
|
MAEKRTLIAVIADEDTTTGLLLAGIGQITPETQEKNFFVYQEGKTTKEEITDKFNHFTEERDDIAILLINQHIAENIRARVDSFTNAFPAILEIPSKDHPYDPEKDSVLKRVRKLFGE
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Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13461
Sequence Length: 118
Subcellular Location: Vacuole membrane
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O82628
|
MESNRGQGSIQQLLAAEVEAQHIVNAARTAKMARLKQAKEEAEKEIAEYKAQTEQDFQRKLEETSGDSGANVKRLEQETDTKIEQLKNEASRISKDVVEMLLKHVTTVKN
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Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12397
Sequence Length: 110
Subcellular Location: Cell membrane
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P19320
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MPGKMVVILGASNILWIMFAASQAFKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHIDDMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPELLVLYFASSLIIPAIGMIIYFARKANMKGSYSLVEAQKSKV
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Function: Cell adhesion glycoprotein predominantly expressed on the surface of endothelial cells that plays an important role in immune surveillance and inflammation . Acts as a major regulator of leukocyte adhesion to the endothelium through interaction with different types of integrins . During inflammatory responses, binds ligands on the surface of activated endothelial cells to initiate the activation of calcium channels and the plasma membrane-associated small GTPase RAC1 leading to leukocyte transendothelial migration . Serves also as a quality-control checkpoint for entry into bone marrow by providing a 'don't-eat-me' stamping in the context of major histocompatibility complex (MHC) class-I presentation .
PTM: Cleaved by the metalloproteinase ADAM17 to generate the soluble form.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 81276
Sequence Length: 739
Domain: Either the first or the fourth Ig-like C2-type domain is required for VLA4-dependent cell adhesion.
Subcellular Location: Cell membrane
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Q9M2D2
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MYQSMNLSVSSNFTHRSLLESRFPIFSTGFRKSVNLKPPRVSSGPESNDSGHETLTDKLIHLLRAVPDWADEIKERGMQQKRSLYTHEKWVEHRSSLRHVRHLLSSFSSRVILSLIPPVFFFTSVAVVIASYNSAVALDWLPGIFPILRSSSLPYQLTAPALALLLVFRTEASYSRYEEGRKAWVGIIAGTNDLARQVICSVDSSGDELIIKDLLLRYIAAFPVALKCHVIYGSDIARDLRNLIEADDLSLILQAKHRPRCVIEFISQSIQLLKLDDAKRDLLESKMLHLHEGIGVCEQLMGIPIPLSYTRLTSRFLVFWHLTLPIILWDECHWIVVPATFISAASLFCIEEVGVLIEEPFPMLALDELCDLVHSNIQEAVKSEKVIRNRIIAKIKLHEFKHSSNGRHRS
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Function: Voltage-dependent chloride (Cl) channel critical for proton motive force (PMF) partitioning across the thylakoid membrane by anion influx into the lumen during illumination, thus being required for photoprotection under fluctuating light conditions . Influences thylakoid ultrastructure, including lumen size and organization . During photosynthetic response on transition from dark to low light, involved in a sequential mechanism of adaptation; VCCN1 and CLCe first trigger the activation of photoprotection, which is later down-regulated by KEA3 to a low steady state, while adjusting electron transport . On transition from low to high light, accelerates the activation of photoprotection by building up a pH gradient across the thylakoid membrane .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46539
Sequence Length: 410
Subcellular Location: Plastid
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P04014
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MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRALYWFRTGISNASTVIGEAPEWITRQTVIEHSLADSQFKLTEMVQWAYDNDICEESEIAFEYAQRGDFDSNARAFLNSNMQAKYVKDCAIMCRHYKHAEMKKMSIKQWIKYRGTKVDSVGNWKPIVQFLRHQNIEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAVYELSDANWKCFFERLSSSLDIEDSEDEEDGSNSQAFRCVPGSVVRTL
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Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
PTM: Phosphorylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 73530
Sequence Length: 649
Subcellular Location: Host nucleus
EC: 3.6.4.12
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P50760
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MDDDKGTDTTDAKEGCSGWFMLEAACSDDSDLDNSLEKLFEDGTESDVSDLINDDDTAAQGNSRELLCQQQSEECEQQIQYLKRKYFSPKAVQQLSPRLQSMNISPGHKSKRRLFVEHDSGLECSLNEAEDLTEEVEVPASAPAPAAQGGVGSGHYTSLLRCNNVKAVLLGKFKDAFGVSYNELTRQFRSNKTCCKHWVLAIYAAKDELIDASKQLLQQHCTYLWLQTFSPMSLYLCCFNVGKSRETVMRLLSSMLQVNENHILSEPPKIRSMIAALFWYKGSMNPNVYAFGEYPEWIMTQTMIHHQTADSVQFDLSEMIQWAYDQDYVDECTIAYQYARLADSNSNARAFLAHNSQAKYVRECAQMVRYYKRGEMRDMSISAWIHHCISKIEGDGHWQDIVKFLRYQGLNFIVFLDKFRTFLKNFPKKNCLLICGPPDTGKSMFSMSLMKALRGQVVSFANSKSHFWLQPLADAKLALLDDATEVCWQYIDAFLRNGLDGNMVSLDMKHRAPCQMKFPPLIITSNISLKKEKKFPYLHSRIYEFEFPNKFPFDANDTPLFKLTDQSWASFFKRLWTQLELSDQEEEGENGETQRTFQCTTREVNGLI
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Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
PTM: Phosphorylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 69698
Sequence Length: 608
Subcellular Location: Host nucleus
EC: 3.6.4.12
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P22156
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MMEALAERLSALQDRILELYEADSKDLKDQIEHWKCVRQECAVLYKAREVGFSHLNHQVVPSLTVSRAKAHKAIEVQLALESLQNSEYNNEEWTLQDASLEMWHTEPKGCFKKTGVPVTVLFDCDKDNTMEYVLWGHIYVWGDNGWVKTFGEADNWGLHYTVAGEKVYYVQFYEDAKKYGHGNGNGDGYEWEVHVGGTVMHYSDSVSSATHCDKLPTVEIVSGLQHINPSPPPANPSAKENVWSSPAKRVRRSDSGGDPVRALDGKSRSVLCGSAHNNATGSSGDSDYTPIVHLKGESNCLKCLRFRLGKHKHLYINISSTWRWANHASEKAIVTVTFANELQRQQFLNTVKIPSTVTLSQGVMTV
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Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 41025
Sequence Length: 366
Subcellular Location: Host nucleus
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P11329
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MKMSAASDHLLAAQETQMQCIEKDSRLLQDHACYWGAVRREKLLLYAARTKGLKTIGCVPVPPCSVTAEQAKQAICMQLIVEELLHSPWAKEPWSLTDLSWERYQAAPKGCLKKGARVVEVEYDGNSSNKTWYTAWSTVYVRGTEEEGWETAVCAADGQGIYYCAGMSSKVYFETFETDARRWSRTGHWTVRDNDVIYHSTFGAPPHSRNDRDCIEGFWSDAGERRGSRGSDTTDRALPYPAARQSPICRPVRTGENRSRAVHRQAPYSAPSSPGSSVGPDSPSESSRQVPLVLLPGPSDPAPPSPDSTDVIAEGDKEPERFSILSKPGGQPCLILSGNGNQAKCYRFRCKRYFREHYQHITTTWWTVGERGSERHGDACVLVTFKDSSQRGVFLKRVPLPPGMRAQALTMIADF
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Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 46245
Sequence Length: 415
Subcellular Location: Host nucleus
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P06926
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MANDKEIAQTESGSHPKDLKETLQEKKPSQPSLSLLCSAPPPAVPSEQASVGYGTVLARTPTIFLQARGALFSALPPPRAGHGTGGLGIKAGRRGAVARLHRGRTSDSPKAHHQ
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Function: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions.
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability.
Sequence Mass (Da): 11908
Sequence Length: 114
Subcellular Location: Host cytoplasm
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P11301
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MANDKEIAQTEFPHQKDLKETLQEKKPSQPSLSLLCSAPPPAYPSEQASVGYGTVLARTPTIFLQARGALFSALPPPRCRARYRWTWHQGRKKKKINRPTQQRRNL
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Function: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions.
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability.
Sequence Mass (Da): 12111
Sequence Length: 106
Subcellular Location: Host cytoplasm
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Q07852
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MADKALHTPPPSTLRNNSYPGPPPATPKLPSRRALLEGGNRGNPTRPPPRPLKPREYDYDEDDEKENQGPGQEKPPAKEEEEEEEEEERPNWDLHHLLQKWGADIDKLKDKVCRDLDSYKQKLGIRL
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Function: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions.
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability.
Sequence Mass (Da): 14595
Sequence Length: 127
Subcellular Location: Host cytoplasm
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P06924
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MTDPNSKAPRLQGRQEDKQTQTPPPRPPPPPQPPLTPRPDSSPHQNSHNKPKPEEEGTDGGPPASQGDRKRSKGDQGPDTGPGLGPGRGPSPKPTPLGPPPGPGPRRSPRLGPLQADRDPEEGPQPPAEGEVEGHPGGDQGHPPPPPPAPHNGHSGHEPKVQQPEGPEGREGHEEGAVGGEGGDEEGHPPPPPPPTNGHEGGLLSSVASLLVKWEGHFDQLVQSIQDDLEDYWKKLATPQ
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Function: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions.
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability.
Sequence Mass (Da): 25150
Sequence Length: 240
Subcellular Location: Host cytoplasm
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P25485
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MHGNRPSLKDITLILDEIPEIVDLHCDEQFDSSEEENNHQLTEPDVQAYGVVTTCCKCGRTVRLVVECGQADLRELEQLFLKTLTLVCPHCA
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Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10369
Sequence Length: 92
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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P17387
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MRGETPTLQDYVLDLQPEATDLHCYEQLPDSSDEEDVIDSPAGQAEPDTSNYNIVTFCCQCKSTLRLCVQSTQVDIRILQELLMGSFGIVCPNCSTRL
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Function: E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription.
PTM: Highly phosphorylated.
Sequence Mass (Da): 10918
Sequence Length: 98
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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Q80901
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MIGKEATIPEIVLELQELVQPTADLHCYEELSEEETEEERPHIPYKIVAPCCFCGSKLRLIVVATPIGIRSQEELLLGEVQLVCPNCRGKLRHD
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Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10612
Sequence Length: 94
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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A0A1U9YI05
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MARPWLSASVLITAVILLVDYLNYYRLRKRLGGIPVVGDASYFWRRIRWTESDTNFQKVIQHGYDTFSKKAKPFAFWGQHEDFILVLPPGSCEEVKHLGPEKLNFLQAVEDSYHFKLHTNILGRSHVDAVRQSVNKNMNQLHEIVVKKAEETIPKLFDDIAASNEPFAAFLTIWHLVHIVSASYLVGTEFCANEEYLQAIEYYCINVPNFIYGYFWVPVPLRRLYWYLSPQGYKVRACKAKLKTFIVPKIRETISAWQNGQKSSSYTLLGAMLDLKAQKGQIKRDPTAMTKAELERQIDIFSDEMIFTGFDSAGPVACMVTQLLFEALRDKDLTKALRQELKSALEANNGQWNVQAMNLTPKLDSFTRESLRVNGPTLLSVTRTVMEPMQLKSGLSLQSGSIISSPSWLIHNDEDNYENAHQFDPYRFYNPSTNAVTTKVTTASTNFLGYGYGTQMCPGRHLGIKMSQILFSKLLMRYDGEFADAKAGKPANIVTSGQVLPPYYAKVILKRRGI
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Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58465
Sequence Length: 514
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1V6NVX3
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MHPSARLYNNIALWFYDYLVHSIFMVYGWHCPTKSVGLPFFSSHVGPKHMDVGVGTGYFPVAVRKSSRKRNGQLKPQWPQKLMLVDLNPNCTAMAATRVGAPDCTETLTADVLQPIPAAGKHETFDSLSLMNVLHCLPGTSESKAQAFGHLKPFLKEDGVLFGSTILGRGVEHNRFGRLVMWLSNSLGIFHNYGDHPDDFVRALQKDFNQVEHVVVGRVLLFTAKEPN
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Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).
Sequence Mass (Da): 25431
Sequence Length: 228
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.1.1.-
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A0A1V6NWP3
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MTFRVIIVGGGVAGLTLASAFEKAGIDYILLECRPAFDVAVGASIALSPNGARILDQLGAWEKWLKIAQPLVRWGDRNSKGELIMPRSASTPLAKALTGYDMTFGLRRSLLQTLYDNIEDKSMLLPKKSVINVTCSQEGVAVQCADGCSYEGDILVGADGTYSKVREYMWRLADRDEPGLMDPDKKAMTAEYQCLFGISKASGSIAIGDADFIYDHDRSSFIFSDNCGRICYFILQKMDRVYEMVEIPRFSQANAQAYAQRHADIQIRPDLTFGNLYEHSESSILVALEEAKFKQWSWGRIVCVGDSIHKMTPNLGAGASASIESAAALLNSIKAMFDHSPEEGPTETQIRECFAQYQKSREVRATAIVDASSMTTRLQALRGWFEFLFVRLGMPIMGSFAADMASEIWVGATMLENLAPPKASLRGTLPFNPTQGQGQRESKLKRALLGLPFLALLLVAKTATDAKYASALRGYIWESGGMTSAMGSVPLLQRFYSMKGVGDLWSLRYINYLPDFYETNYESLSQAVSSSIDVGIVMSIWSFESIRRANALTMAQIPTLFTFYGQMAGLGRVSPLYYILYYINSPIEVFKGADMRLMHLNYAIAVLPAIIVSYYIPLSAAFFWPTVSGRKSWLFVWQMHPIWTAITLYLFSRIFPSTVKEDRVHGLRRDLPVIKFSMTVLVIGAAGFWMWSRWTSPSSVARVFFPTAVPSTQAPFAACVCAILKWDMLSTFGSTFLWLGYLIWDLKYAGMMQATWVRVAIYGVAAFVALGPGAAIGLGWLWRENILAHKRHKDAVTEENLAQTR
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Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89545
Sequence Length: 805
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1V6NZ11
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MLCWELANRRKRIGPNRFGFPIAILTRQQLIEVLYTALSDKSKVKTGKKVVRIESEERRITTWTEDGSEYEGELVVGADGVHSVTRSEMWRAADNQQPGFIQEEEKYSLSAEYSCIWGLSTPVPGIRQGEQIIRSYDRLTFLIFPSQNGCLGWFAIQKLNRKHVYPDIRPFSQKDTLARCEALRDLPIWNDVKFGDLLTLTEVCAMTPLEENLFQTWNYGRILCIGDSISKLTPNIAQGANTAIEGAAAVANGLHQLLHHNGLNQPSYDEIQEVLGRYSQSQRKRMKKLHWISHMVTRLQSREGLINKFVGRYIYSHTGNSTFYLTGKMIAQGPVLNYLSTPKEIEIGLRASFDQYGKDGGDMPWKTTIMFIALLTIVVLIYSFI
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Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43847
Sequence Length: 385
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1U9YHZ9
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MLSEMLGEIAALPMVSLLGAALIVVSVLGRRLLVSNIAWAITGQTPAKSLAKRSRLPGLPFKFPNGQGTEKFFGGRSAARRWRIQYGPIYAIWAGLKREVVLSTPEHVQAFYKDSHLHVKATDNNSGWLFAELLGSCVGVVSQGRWKRVRRPFEHPFSRPESLTRPKAFIHEARDYFAVLNPNIQELTINTSNDLKHCPFFMVASIFFGIHTTAQRDELKQLGPPREELFRHAFMGGMNRYAITKYLPGSALALLRQFQGKWEGFVKAAYNRSIQTGDGTIVPLFEAVNRGEMSMQELLQTLDESLFANLDVTAHAVSWNVIRIAHHQDIQQKVRIEIQANNNSEKSYENYVCRDDTLLAACVLETSRLHPVLPFSNPEAAEEDKIVGGYIIPQTDVIVDTHAINIDNPHWVDSNSFDPHRHLGQKDSSRRYNMWRFGFGPRQCLGKNVADIILRIILCEMLNTYELGLLEEEGITGVKLQPDSWIGLPNGVVQMTPLKLDE
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Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56554
Sequence Length: 502
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1U9YI21
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MPINKFSARSLDNDVPNKPLIFVMEGRYQNWIKPIMLLECLEIDYDAACIDGPTTRTDWFTRLHPQRYVPAMIDVEDGQRVSSWDSSQMLQYLSNKYDAKRMWNGHNAAENLEICNWLTFETASLGPTAKYWVWYALRQGEEQNPKAQQKMYNDLRVQYSILDKHLAQPGQNWVGLKDRPTIADLAIYPFADDPTMARMGIDKKDFPSLKAWSEALSKVPGVAKAYAELDSRKEIAIGA
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Function: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 27441
Sequence Length: 239
Pathway: Mycotoxin biosynthesis.
EC: 2.5.1.18
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A0A1V6NXN7
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MAICIYEHDAAKIIPTLVSELPYSTTLLRRIQHGIAYPYETAHILATFPPGLTPEPGQPWLAARVDLFAGRTTQMIIYSSLEAEHTSIPPIVTVSDSTEILNVDSTSNNSKNNDTNDADNPDINSITKFIVSTFSASPPVLALARAQLLALLEYVKTNMLPFYLSYLAKSAQATSVAAETPPVSTSSVTSNNTSPTSVPLIPAPDPQAFLIGSLHTGLFSLLQQSGSYTLSNPIPNIRVHRFDDPPYYKYFFRRSEFSPEAVCGRSADLPFADLSLPSGYRFHDREGREGVLSKHLDLVQSRTHIPRPRAQLSKIPGMAVYLDSTSSDADEMPIAWGFLGVDGALVTLHVEPEHRGRGLAVPLSKAIMRRGMAVDGVFGAGSVNSEDSQTRERVGAWAHTEVAGYNNASRRVMEKIGGQVLTTVTWTVIELLD
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Function: Acyl-CoA N-acyltransferase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).
Sequence Mass (Da): 47180
Sequence Length: 433
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.3.1.-
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A0A1V6NWJ0
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MVFAMLVVCWSIFLGLWMLVSRLKQSRDKICPPKGPPRLPWIGNLHQFPLKLLHLRLTEWSRTYGGFYTLKLGPVTAAVITDRQIAKEAFDRNSAISSTRHTNYATEFVTDGTHLLTMKYGALWREERKILQQTLKGSVCDNDHMRLIDAEQTQLMRDLLVNPSDYSAYIKRASTSIITSLVFGIRTPSCATLHLQELDAINDDWLQLLVIGGALSEDVFPVLKYIPSAFLGTFTKRLKGIRRRMRRLYGTMLNQTITRQRESPAPPARSMIDAVLNQREHFNLTDRQIEVLAGVTLEGGFDTTTSMLLVFVQAMTLHPECQERAYVEINALCGRHRIPQWSDRNQLPYVNMLLKETMRWRPVTTLSPPHVLEKDTTIRGTFLPQGSMLILNTWGLHQDPNVFIDPDRFDPMRYEGYTKLAADYANAPDAATRDHYTYGIGRRICPGIHLADRSMFLAIAKLIWGFRFEPQRDEQGNSIPIDSNPVTGYTVDKVQISPKPFACAVIPRDKEGEKTILREFGVASEVFADYNLDENASL
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Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61279
Sequence Length: 538
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1U9YHZ6
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MLSRRARESNAWFLERFKRPLGRQGSKSNTNIDLATAENWLIRPEILSALKRNLQADFQSSHLSYAPGLGGTPELLSAISTFFNHFFSPTIPVAPEHIVTGAGCSSVLDTLINDICDDGDGLLVAAPYWGSFEVSSVLRNGVTLIPVQIKFHESHSAQGIVDAYRKAMENTSCKVRGLLFCNPHNPWGHILSVEVIDALLLFCEQADIHFVSDEIYALSTFGRMELPSGNLEHGEKFLSPATSFVSVLSRDLIKLGGCLITQANKELRMSQAILNNAKLCNAASAMVAPILGSTSQLSTLVNLNVQRMRKAARTAIQFAQFHGLTFCEPVAGVYIWLRLSEDCHTRDDEEEIVQRCTKHGALVGSGSDYSESQPGWFRLTFAIPDNEFLEGLNRIETAMGYKERFNGEMVQSSLGGFVSQLWKRFVLV
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Function: Aminotransferase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Sequence Mass (Da): 47334
Sequence Length: 428
Pathway: Mycotoxin biosynthesis.
EC: 2.6.1.-
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A0A1U9YI27
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PIVSKMALLDDNLSKALKLLADVPLIDGHNDFPYFIRGWFPEQIDSLDCRNVRIAHTDLERLNQGRVGGVFWSAYVPCPDRHAKNDFVVDAQYESLRATMQQIDIIHTLIERYSDRLGLARTSSEVWEVFRSGRIASLIGVEGLHQIANSPGVMRNLYRLGVRYITLTHDSNNLYADSTNSSGPFHGGLSRDGISIVKEMNRIGMMVDLSHTSVATQKHVLAISKAPVIFSHSSCASVTEHPRNSPDDVLDMLKANGGVFMITFIRKPTDAESPTLEKVADHVQHVGDRIGYEHVGIGSDFDGVMLTASGLDDVSKFPLLIAELLKRGVSDHSIKNMIGLNVLRVMDSVEEVSMKMKETGEEMLHEVFEEIWDEKMRDEVRKTRDIFD
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Function: Dipeptidase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Sequence Mass (Da): 43458
Sequence Length: 388
Pathway: Mycotoxin biosynthesis.
EC: 3.4.13.19
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A0A1U9YI11
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MTNTERSSSWKASSIPDQPMWYFGYGSNMKASSMADRKVTPLSTKIVTVPTHFVTFDIFGIPYSEPSYASLEQFPDGGTGKLDLVHHISRTQVLPACGVAHLLSPNDFHRLLVTEGSGVVYNLVEVQAYEMNKDGQPIPAPFTVHTLKAKWPQRPNGTPSARYMVRFLGLLSSSTYYQY
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Function: Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid
Sequence Mass (Da): 19953
Sequence Length: 179
Pathway: Mycotoxin biosynthesis.
EC: 4.3.2.9
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A0A1U9YHZ8
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MAVALFPILPIGCLLIYIIFKLWTRDERLKHLPPGPKGLPVIGNMLDMADTDKMMKKSKDWADEYGEIFYTKVGLYNFVWLSSPNAVRELMDKKGSIYSSRPPSPMINMVSNGERLNFLPYGHKWRTIRNILHSALNLETSSTYKPVQDFESKQALWEILHAKDDMEFNDINRRYSTSTIMTITYGLRVPTLQHPLYQDILTIVRHFSLATAPGEWVIDMVPMLADIVPQFLLQNWKNVARKWYKEDSEIYLALYNKLMDDIKRGTAPDCFLKDMAREKLKKNPIADTTAAFAAGALIEAGSDATTTALNNVVLACLLYPEIVKGAHEELDRVVGSDRMPEFSDEPNLPYIRGIAKETLRWRASTKVGPAHATTQDDWYNGYFIPKGTGVVLNWWAIHMNEKRWKDPERFDPTRYLEDTLTEAESMAQPNPELRDHFTFGAGRRNCPGVHIAHNSLFINIARIFWAFNKQKSKDADGKILEPSTAAQPGFLLTPVKFPCHFEARSDKHARIIEERWTEAQEKGIDGWKGKKESSSEENRGVSSR
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Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62188
Sequence Length: 544
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A1U9YI02
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MEAALKKLNIALQEAIDSFEGPLNQERLNELQTTESLPNKEVWSLASQTIDLADKIIHRLQPPSLQLAESFLAYLDTKCLWAAVSHDIPDLITAGGPQTVQELAKKSGLQSIRLKQVMRVLHNNGIFEYKPTTQKYSNTPSSTLLAKDHWTQWHLWVDLYGNEHYKAAEGIPDAIREGQTRCAAQIQYDTDESMFRYFARNGLQEKFHKTLGAGAVAQAPGMMADYNWGELDDAVVLDIGGGGGDFITSLLREHPSMRGGLFELDSVIEMVRPKYRDASGEFADVGDRMVDLHVGDFRVEVPAYEVYTMKWCLHNWLDEDVVKILSAVRRAIKVTPRARMVVVESVLKDGRSSRIWRFGDLTMMAGANGQEREEEDWRGLAAKTGWNIHSISPLRNAWAAAIDLRPC
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Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Sequence Mass (Da): 45770
Sequence Length: 407
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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A0A1U9YI04
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MTEHTVSHANGSDLENAKKTYMLANNQKEIERMKNQHEWIKGSFGGLVKAPIDFDKKNQSILDSATADGTWLMDVRSLFPPETELIGFDIAPELYPPEGTRPRNVELVTADLLQGLPAQWIGRFDLVHQRFVFPNFETEVIREVLGRLMQCVKPGGWIQLVEPCAGENVSGPEPKWFLLLHKLANQFMRSAVPRDAILAILHEEGFVNINIESLDIVIGKHQRNKEMDARGRRSMRDSVSNMYPMITAEQLGMPKEEARAVLDKFEADMQKYRTAVRHVIIWAQRPE
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Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Sequence Mass (Da): 32745
Sequence Length: 287
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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A0A1U9YHZ1
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MATPMIYDALIIGGGPAGLAASLALARVCRTSMLFDSGEYRNEGAKEMHTFLSRDGIPPHDFRATCLQQLEKYKDYAYVTNTKITDIANTDVAPGLKGFKAVDFTKKEFFGRKLVLATGTEDVLPTHIEGYKENWPVHIYQCPFCDGFERKSYPIGLLTFPNPSYSHLALMLRPLNKDITIYSNGPVPTDEPTQTALKMVLAAGVKLDERPVRRLINNGDGPENGISIEFTSGATVKLGMLYHRPPTRSRAANLILQLGLETNAIGDVITDTMMLKTNVPGCVSAGDTQENMKQASVAAATGTRAAASIVFQLADEDGKKALAEAHL
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Cofactor: Binds 1 FAD per subunit.
Function: Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins . 11'-deoxyverticillin A is required for normal conidiation . The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable).
Sequence Mass (Da): 35527
Sequence Length: 327
Pathway: Mycotoxin biosynthesis.
EC: 1.8.1.-
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Q9I6M7
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MRQRDLKFTFVVGEGKLAFDVVEFELEEALCEPFRLNLKLASDKNAIDFKQVLDQPGTFTLWQDGRPARYVHGIVSHFTQGSSGFRRTRYELLLEPQLARLELCCNWRIFQEKSVPEILQALLKEHRVLDYEQRIYHEHLPREYCVQAGDSDHYLHDRLAFEEGLVYYFRFDEHRHTLVCSDRLYVQERIAGGPVLFSAQPEGDNPQPVLHSFRYSENVRTARQTQRDYSFKRPTYDQEHHLAGEALEHQGSSYERYDYPGRYKRSGAGRPFTESRLRGHRRDARVASVSGDDPRLIPGHAFALEGHPRADFNAWWRPVRVVHRGTQYAGQEEESADAPLGVSYDLRAELVPEDVEWRPAPLPRPRIDGPQIATVVGPAGEEIHCDEWGRVKVQFPWDREGRHDEFSTCWIRVAQNWAGADWGHMAIPRIGQEVIVDYLDGDCDQPIVTGRTYRATNRPPYALPDHKILSTIKSKEYKGSRANELRIDDTTAQISAALMSDHGASALHLGYLTHPRPEGGKPRGEGFELRTDEHGAVRAAKGLLLSTEEQLRAGAGHLDRGVVVQVLEAALELARELGDYAGEHQGVGHDAAPQQTLQEAVRDLGHGANDESGKSNGGKPAIALSGPAGIAAATPASLTLAAGEHVDSVARQNQQVTAGQKVVINAGSDIGLFAQGGELRQITHQGPMLLQAQKNDIRLEAKQSVEVSASQQHVLVTAKEHITLMCGGAYLTLKGGNIELGMPGNFVVKAAKHSHVGAASLEAELPQFEVGETQRRFVLKQLDGQTAMPNVPYTITMANGEVIEGVTDAEGATQLLQKDAMNIAKVDMKHTKSPASAVAGIAAAVGAAVAVGKLLGGPDAEAGRALSEGEISLAKGVFGDSIDYSTVRLRDEDYVPWQGKDYVMAPNGHIYFGEELRGVADWSLESLQRQGLFIHEMTHVWQHQHGVNVLLVGAYQQARQFLLGDQYAYRLEPGKTLKDYNIEQQGDIVRDYFLEKNEFGEASANSRFAGVLKNFPTGY
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Function: Part of the H2 type VI secretion system (H2-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection . Forms the spike at the tip of the elongating tube probably formed by haemolysin co-regulated protein 2b/Hcp2b (Probable). Allows the delivery of the Tle3 antibacterial toxin to target cells where it exerts its toxicity . Additionally, acts directly as an effector and promotes internalization by interacting with the host gamma-tubulin ring complex . Elicits toxicity also in the bacterial periplasm and disrupts bacterial cell morphology. Toxicity is counteracted by a cognate immunity protein .
Sequence Mass (Da): 112964
Sequence Length: 1019
Domain: The C-terminal region is part of a wide family of metallopeptidase effectors.
Subcellular Location: Secreted
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A0KJB0
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MADSTGLQFTVKVGALPESTFVVAEFALDEALNRPFNLRLELASAQPDIDFGAVLDQPCELLVWYNGELQRRVCGVVSDFAQGDSGFRRTRYQLMVQPALWRLSLRQNCRIFQAQKPDEILSILLQEHGITDYAFALKNEHAKREYCVQYRETDLDFVNRLAAEEGMFYFHEFEAGKHRIVFADDAAALTAGPELFFNLGNRSLEQGPYVRQFHYREAVRPSDVELKDYSCKTPAYGLSHKKQGSELEHQRDTYQHFDYPGRYKQDPSGKAFAQHRLDALRNDAVAGQVKSNCAALLPGQTFSLTEHPNGSLNTDWQIVRIRHTGEQPQALEEEGGSGPTVYHNEFGVVKASTTWRARIGSPEAPHKPMVDGPQIAMVVGPDGEEIYCDEHGRVKLQFPWDRYGSSNDQSSCWVRVSQGWAGGQYGMMAIPRIGHEVIVSFLEGDPDQPIVTGRTYHATNRPPYELPANKTRTVLRTETHQGEGFNELRFEDQAGQEEIYIHGQKDLNVLIENDAAWHIKHDQHTDIDNERVTRVRKVPGEEGAPPSLGNDHLTVEGEKRDHIKADYSLTVDTSMHQKLGQSWLTQAGQEVHVKAGAKVVLEAGSEITVKVGGCFIKVDGGGVTLVGPTIKMNSGGNAGSGSGWAGKVPKSMEGMLDSPHTRWMKFYHLDSELMPLAGTPYKAVLSDGSVREGTLDGEGMALLEDVPAGTASVTYDLQDTFADLPRESISALTGHLDSLSDEG
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Function: Part of the type VI secretion system specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection. Acts directly as an secreted effector with an actin ADP-ribosyltransferase activity that disrupts the host actin cytoskeleton, leading to a decrease in host cell viability and an increase in apoptosis.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 82412
Sequence Length: 743
Subcellular Location: Secreted
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K7WKL8
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MADSTGLQFTVKVGALPENTFVVAEFALDEALNRPFNLRLELASAQPDIDFGAVLDQPCELLVWYNGELQRRVCGVVSDFAQGDSGFRRTRYQLRVLPALWRLSLRQNSRIFQAQKPDEILSILLQEHGITDYAFALKNEHAKREYCVQYRESDLDFVNRLAAEEGMFYFHEFEAGKHRIVFADDAAALTQGPELFFNLGNRSLEQGPYVRQFHYREAVRPSDVELKDYSFKTPAYGLSHKKVGAELTHQRDTYQHFDFPGRYKEDPSGKAFAQHRLDALRNDAVAGQAKSNCAALLPGQSFSLTEHPNGSLNTDWQIVRIQHTGLQPQALEEEGGSGPTVYHNEFGVVKASTTWRARIGSPEAPHKPMVDGPQIAIVVGPDGEEIYCDEHGRVKLQFPWDRYGSSNDQSSCWVRVSQGWAGGQYGMMAIPRIGHEVIVSFLEGDPDQPIVTGRTYHATNRPPYELPANKTRTVLRTETHQGEGFNELRFEDQVGQEEIYIHGQKDLNVLIENDAAWHIKHDEHTDVDNERVTRIKANDHLTVEGEKRDQIKADYSLTVDTSMHQKLGDSWLTQAGQEVHVKAGAKVVLEAGSEITVKVGGCFIKVDGGGVTLVGPTIKMNSGGSPSSGSGWGGKSPVDPLGVSVPPKPKVPLTPAQLATMKSAAPFCEECEKCKEGGCEI
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Function: Part of the type VI secretion system specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection. Acts directly as an secreted effector with an actin ADP-ribosyltransferase activity that disrupts the host actin cytoskeleton, leading to a decrease in host cell viability and an increase in apoptosis.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 75614
Sequence Length: 681
Subcellular Location: Secreted
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W7E4C5
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MDLYISNYTSDDDMAILRRRWIELLPLVVGDIVHVENPEGYSYLLDPIIPGPGYVVTWYHQLHCLFFLMSEYDRLLRHGPNGKERSIPAGSSSIHTRHCFEILRHSILCHLDMTLEGGSAPFFNGTTGFGHAHVCQNRQEAIDWMEKNRANDNRMIIRA
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Function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . The role of vicYa within the pathway has still to be determined . The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
Sequence Mass (Da): 18326
Sequence Length: 159
Domain: The 2 HXXHC motifs are conserved in ustYa family proteins and might form active sites.
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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W7E0Q5
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HLVSLQVYHYLHCINALRRAAYQHVYGAPTKEHLNHLDHCIDMLRQAAQCQSDLTPMLYFNPENDPNTMLIKSHQHSCRRFDLVNEWAMARSQCKGNTTCAIEVGKQVGGEM
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Function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . Within the pathway, vicYb catalyzes the oxidative cyclization of the core peptide . The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
Sequence Mass (Da): 12865
Sequence Length: 112
Domain: The 2 HXXHC motifs are conserved in ustYa family proteins and might form active sites.
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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W7DZP2
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MLTKSRLQVFHELHCLNFLRKLIYPDVYGKIDYKGQIHANHCIDHIRRIAECGSNATPVVYTGYKNGNLYSEPETYTCRNFTLIRQWAEMKKIQNTQ
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Function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . The role of vicYc within the pathway has still to be determined . The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
Sequence Mass (Da): 11450
Sequence Length: 97
Domain: The 2 HXXHC motifs are conserved in ustYa family proteins and might form active sites.
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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Q05934
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MRAMDTQVQSAERGLVLPPMNSTVSSATAATTATNTDTDTDGDRDEERESLAEDGSEWVPAYMLTRDRSRYLGHFLGVDKMLEAVKCKYCGVIIRRQGNSISMAEASQTHLWSTHKIDPNANYYSGWTGVEAGSTFMVRPPLKNHQGGSATTNSIANLLEIDEDFLKRTREKEMALPLVQSLAIIIASENLPLSFVDNTAVRLLINQNANSLSFIDHDLILNAIRSIAYNLDRIIQRTALRNNSDLSLIIDKNYLLMDPTDRSNQLSNRLKNQLFEMQKINFFSLSHSVWNNTISILSIQYYDDFHSQVKTLPLIIQNLHEYNNDPKLSIPAQLLKISQELPGLQNTVISITLPRSQIVDLLNVMDSQPFFPNTYTNAKNYYHNCIISIINSAILPLFGTPKSADITHPRQSSFSKEPLTLLDSLIDLSNIDISNSIFSRINSFLDDLQSNSWQLDKFRSLCEKFGFEFVCSKFDLSRYSTATVSLQTFLNLRPIIEEYQSSIQIEKFNEIDFQIIDYLLITLNSINRILKFFTSSKSLNFTYVLFAIMSIEKHLLSTLGSLQFQRLIAPFETFLSKIQEFKTILFSDDMNLLAMFLCPAILFEREVLEYSFHTISLSEIVDKLSTSIFSLLKRFLNLHTIGNVNNSHNTSNHSNMNIHTDNQTNNINNRSGNNSDNNDNEHDNDNDNHSNSNTPASRIDIDPTGGENSVLPEQQPQNSNNNLSFGSLSDTHHLSDSTISKEIDSIFLQIIQEDLYDYLSTVNSIVPISYRSYCEQSNFIRDSGRFKKRIITEDSIIGELEQPMNFIEELLDIHVPVCNAFWSQYLDNDAGPIIRILFKIMQCQSSSSIRGEYSFLNDFIPRVHPDLTQEIIKIKLFNDQFVASKVDYDLDTLQTASQYLP
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Function: Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A.
PTM: Glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 102500
Sequence Length: 901
Subcellular Location: Cell membrane
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P27426
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MASKDSDVRCVKCQSLKPTTPLTGQDRCARCVAINELKPWISTCNINPCYDGDLSESNETIEMMDINSCREDTPSDAESETRFMPFVAHSKQPKHTSKNPTKGEIQYFPVEKCKDIHRVENQSSIDEEGKQCWICRDGESLPEARYCNCYGDLQYCHEECLKTWISMSGEKKCKFCQTPYKVNRQLSLKRGLPGYWDRDDRFVFIAGFIGMGTILAGWIASFFYLLVVLCGKYFTYKDVMIVVGGLAIIQVVGLMFSLFMYFQIGNLLRQYINYMTETNIDPLRT
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Function: Controls the expression of later classes of genes and also of the IE genes (Potential). E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32693
Sequence Length: 285
Domain: The RING-CH-type zinc finger domain is required for E3 ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
EC: 2.3.2.27
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P03169
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MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEETSVMLAKRPLITKPEVISVMKRRIEEICMKVFAQYILGADPLRVCSPSVDDLRAIAEESDEEEAIVAYTLATRGASSSDSLVSPPESPVPATIPLSSVIVAENSDQEESEQSDEEEEEGAQEEREDTVSVKSEPVSEIEEVAPEEEEDGAEEPTASGGKSTHPMVTRSKADQ
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Function: Plays an important role in transactivating viral early genes as well as activating its own promoter, probably by altering the viral chromatin structure . Expression of IE1 and IE2 proteins is critical for the establishment of lytic infection and reactivation from viral latency (By similarity). Disrupts PML-associated ND10 nuclear bodies by interfering with host PML and SP100 sumoylation thereby altering the regulation of type I and type II interferon-induced gene expression . Promotes efficient viral growth by interacting with and directing host SP100 to degradation, leading to enhanced acetylation level of histones . In addition, functions in counteracting the host innate antiviral response. Inhibits the type I interferon pathway by directly interacting with and sequestrating host STAT2 . Also targets type II interferon pathway by repressing IL6- and STAT3 target genes . Repression of STAT3 genes is due to STAT3 nuclear accumulation and disruption of IL6-induced STAT3 phosphorylation by IE1 (By similarity). This repression is followed by phosphorylation and activation of STAT1 . Inhibits host ISG transcription by sequestering host ISGF3 in a PML- and STAT2- binding dependent manner . Alters host cell cycle progression, probably through its interaction with host E2F1 or RB1 that overcomes the RB1-mediated repression of E2F-responsive promoters . May act as a E3 ubiquitin ligase targeting several host proteins including HES1 and SP100A for ubiquitination and subsequent proteasomal degradation . Impairs the radial migration of immature neurons by downregulating Gap junction alpha-1 protein/GJA1 also via ubiquitination and degradation .
PTM: Sumoylated by host PML/nuclear domain 10 (By similarity). Sumoylation abolishes the interaction with host STAT2 and thus the IE1-mediated repression of interferon-stimulated genes .
Sequence Mass (Da): 55179
Sequence Length: 491
Domain: The N-terminal region is required for nuclear targeting . The C-terminal 16-amino acid is termed the chromosome-tethering domain (CTD) and is required for the association of IE1, host PML and host STAT2 with the mitotic chromosomes . Targets host nucleosomes by directly binding to the acidic pocket of core histones .
Subcellular Location: Host nucleus
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P19893
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MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFEQVTEDCNENPEKDVLAELGDILAQAVNHAGIDSSSTGPTLTTHSCSVSSAPLNKPTPTSVAVTNTPLPGASATPELSPRKKPRKTTRPFKVIIKPPVPPAPIMLPLIKQEDIKPEPDFTIQYRNKIIDTAGCIVISDSEEEQGEEVETRGATASSPSTGSGTPRVTSPTHPLSQMNHPPLPDPLGRPDEDSSSSSSSSCSSASDSESESEEMKCSSGGGASVTSSHHGRGGFGGAASSSLLSCGHQSSGGASTGPRKKKSKRISELDNEKVRNIMKDKNTPFCTPNVQTRRGRVKIDEVSRMFRNTNRSLEYKNLPFTIPSMHQVLDEAIKACKTMQVNNKGIQIIYTRNHEVKSEVDAVRCRLGTMCNLALSTPFLMEHTMPVTHPPEVAQRTADACNEGVKAAWSLKELHTHQLCPRSSDYRNMIIHAATPVDLLGALNLCLPLMQKFPKQVMVRIFSTNQGGFMLPIYETAAKAYAVGQFEQPTETPPEDLDTLSLAIEAAIQDLRNKSQ
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Function: Stimulates viral early and late gene expression and thus play a crucial role in the regulation of productive infection . Selectively drives host RNA Pol II transcription initiation at a subset of viral early-late and late promoters without substantially affecting Pol II transcription of expressed host genes. Mechanistically, forms a repressive complex at the major immediate-early promoter region involving direct association with host nucleosomes and TBP. Concerning activation, stimulates transcription by binding nearby, but not within, core promoter regions. In addition, activates quiescent cells to reenter the cell cycle and up-regulates several E2F-responsive genes, which are responsible for pushing the cell into S phase . In S-phase, inhibits cellular DNA synthesis and blocks further cell cycle progression.
PTM: Phosphorylated by host CK2 at Ser-203 and Ser-205; leading to enhanced SUMOylation.
Sequence Mass (Da): 62875
Sequence Length: 580
Domain: The SUMO-interacting motif (SIM) is required for efficient transactivation function.
Subcellular Location: Host nucleus
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Q8QME4
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MSRQINANTPVSRRRSGLRGRRLSYSPEDAVPTPAPRFSILEARRAADRPAEERMRAWHVIGDTSEPVTLRFVHNNAQYTVHGNAPFNTADFQEERDSQETEAANRAHQRAVHLHEHLHEVQETAAPLPNYSPVHSPDLTVMEDLETPRQRFETMFHAVDAESEDEAVPLPQVDMAVFCHICSCFFTDIKNYNSSFVTTSECNHAVCFKCYTSIMFDKELFKCSMCNRATPTCRVYNHKGFVELLPTRAVRDKQAIKTHWAQLLDNNMSDSKVPEQNDVQKLQAELAELRAEMASMRAEMASKQLGATMALENRRGSSSSGASSSSTSTSSSSSSSWLWECLLNTRNY
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Function: RING-finger E3 ubiquitin ligase that plays an important regulatory role during the initial stages of infection. Migrates to specific nuclear foci early in infection supposely to prepare the sites for viral replication by targeting and ubiquitinating host proteins.
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 39281
Sequence Length: 348
Subcellular Location: Host nucleus
EC: 2.3.2.27
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P07167
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MTWDRLLPSRKFLLAINSWYVLALVVAAISFAVLAIGPWKNEKSIEAILTELQSIDVDCALLQRNVLRAHAGLLRNYRPLMVPLGRVRSSIANLQQLFKKARVEDVGELSELLARLKSSINTTDAAVASFGAQNVVFEDSLATFNQSISSLLRTSDSRDLNAAKVPELGYLMLQFSFRPNTELALQITQSLDQLQMSTNADKVAIQEVVRNGRVILGVLPRLNETVKLVQASGTFENTKKLQRAYLEADSLARVVEQRVRTFLGAVSVFFCFGIVILVHKLRRRTDRLARRLDFEEVIKKIGVCFEDSTETKQSLKSSAEAALGTIENFFEANQCVLGLVNVTENEIAETFSASAPPPSWNERRIRKIVSLVQADEHGSIFRDYPARKASCFNEDAPGRWALVAFKVSDRLVAVFGLRFDRDPVQPASSEVQLMELAAGCVSHYVVIRCKQTQRDILERRLKHAERLEAVGTLAGGIAHEFNNILGVILGYAMAQNILHRRTYARHYIDRINAESNRARLIIDQILALSRRRERTARPFNLSALVREIAPSLRVALPSEVEVDFNIQSAQMIVEGNPLEIEQILMNLCKNAAEACIGTGRIEDSVYRSFVWKHKVLANGTIPAGDYILLSFEDNGGGIGQAALPHIFEPFFRTRAQCGGTGLGLSTVHGHVSAMAGFVDVISTVGRGTRFDIYLPTSAKKPVNSESFFGPEKIPLGSGEIVAVVEPDPVTLERYEETIAAFGYEPVGFNTFKGLTDWVLAGKEADIVLIDHSSFLDGERVGSWVATLEKVPIIMIGQHQKNVSISADGEASNHFLQKPVSSKALAYVVRANIRTE
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Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92444
Sequence Length: 835
Subcellular Location: Cell membrane
EC: 2.7.13.3
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P10799
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MNGRYSPTRQDFKTGAKPWSILALIVAAMIFAFMAVASWQDNATTQAILSQLRSINADSASLQRDVLRAHTGTVANYRPIISRLGALRKNLEDLKQLFRQSHIVSESNAAQLLRQLEVSLNSADAAVAAFGAQNVRLQDSLASFTRALSSLPGKASTDQTLEKPTELASMMLQFLRQPSPAISFEISLELERLQKQRGLDEAPVRILAREGPIILSLLPQVKDLVNMIQTSDTAEIAEMLQRECLEVYSLKNVEERSARIFLGSASVGLCLYIITLVYRLRKKTDWLARRLDYEELIKEIGVCFEGEAATTSSAQAALRIIQRFFDADTCALALVDHDRRWAVETFGAKHPKPVWDDSVLREIVSRTKADERATVFRIISSKKIVHLPLEIPGLSILLAHKSTDKLIAVCSLGYQSYRPRPCQGEIQLLELATACLCHYIDVRRKQTQCDVLARRLEHAQRLEAVGTLAGGIAHEFNNILGSILGHAELAQNSVSRTSVTRRYIDYIISSGDRAMLIIDQILTLSRKQERMIKPFSVSELVTEIAPLLRMALPPNIELSFRFDQMQSVIEGSPLELQQVLINICKNASQAMTANGQIDIIISQAFLPVKKILAHGVMPPGDYVLLSISDNGGGIPEAVLPHIFEPFFTTRARNGGTGLGLASVHGHISAFAGYIDVSSTVGHGTRFDIYLPPSSKEPVNPDSFFGRNKAPRGNGEIVALVEPDDLLREAYEDKIAALGYEPVGFRTFNEIRDWISKGNEADLVMVDQASLPEDQSPNSVDLVLKTASIIIGGNDLKMTLSREDVTRDLYLPKPISSRTMAHAILTKIKT
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Function: Activates VirG, by phosphorylating it, in the presence of acetosyringone or hydroxysyringone.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91640
Sequence Length: 829
Subcellular Location: Cell membrane
EC: 2.7.13.3
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