ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A4F7F6 | MRPGEIITGDGPVPLNPGRPRVRITVVNRADRAVQVGSHYHFAAVNEGLEFDRAAAWGHRLDVPAGTAVRFEPGVEREVRLVPVGGSRRVPGLRPEYAGELDGRGHEPTAPNYGEKGQGHFE | 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
|
P41021 | MSNNNYIVPGEYRVAEGEIEINAGREKTTIRVSNTGDRPIQVGSHIHFVEVNKELLFDRAEGIGRRLNIPSGTAARFEPGEEMEVELTELGGNREVFGISDLTNGSVDNKELILQRAKELGYKGVE | 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
|
P0A677 | MRLTPHEQERLLLSYAAELARRRRARGLRLNHPEAIAVIADHILEGARDGRTVAELMASGREVLGRDDVMEGVPEMLAEVQVEATFPDGTKLVTVHQPIA | 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
|
P08298 | MKLSPREIEKLDLHNAGYLAQKRLARGLRLNYVETVALIATQILEFVRDGEKTVAQLMCIGRELLGRKQVLPAVPHLVESVQVEATFRDGTKLVTIHDLFACENGNLELALFGSFLPVPSLDKFTENEEDHRTPGEIICRSENLILNPRRNAIILRVVNKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGNATRFEPGECKSVVLVSIGGNKVIRGGNNIADGPVNDSNCRAAMKAVVTRGFGHVEEENAREGVTGEDYSLTTVISREEYAHKYGPTTGDKIRLGDTDLFAEIEKDFAVYGDECVFGGGKVIR... | 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... |
D8JBB7 | MNYGKEQVAVYRTYANPLEGVRTIPESSFDGRDNILFGLEVRVQFEGEEFLPSFSEADNTTVVATDSMKNFVLHQAGEYEGATAEGFLHFVGTEFLETYPHVEAVTMSATEYPFDERPVPGDDGFDPSDLVFRVSDDESAFGEIYLEREGDELRFEEQTSGVTEIELVKVKENSFTGYVQDEYTTLPEREDRALYISLDVFWTYSDPEDALGDEPQRYVPAEQVRDIAQVVFHEVNSNSIQDLIYQIGLRVLERYPQLESVNFEANNRTWIEVRDDLDGDAKVLREPPRPTGYQQFSMDRSDLEEQ | 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... |
P25688 | MAHYHDNYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKLRGIRNIETFAMNICEHFLSSFNHVTRAHVYVEEVPWKRFEKNGIKHVHAFIHTPTGTHFCEVEQMRNGPPVIHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYQRRDVDFEAIWGAVRDIVLQKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLPSRL | 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 dea... |
P16164 | MAHYRNDYKKNDEVEFVRTGYGKDMIKVLHIQRDGKYHSIKEVATSVQLTLSSKKDYLHGDNSDVIPTDTIKNTVNVLAKFKGIKSIETFAVTICEHFLSSFKHVIRAQVYVEEVPWKRFEKNGVKHVHAFIYTPTGTHFCEVEQIRNGPPVIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYHQGRDVDFEATWDTVRSIVLQKFAGPYDKGEYSPSVQKTLYDIQVLTLGQVPEIEDMEISLPNIHYLNIDMSKMGLINKEEVLLPLDNPYGRITGTVKRKLTSRL | 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.
Subcell... |
P11645 | MATTKKNEDVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLSSKQDYVYGDNSDIIPTDTIKNTVHVLAKFKGIKSIEVFAMNICEHFLSSFNHVVRVHVYVEEVPWKRLEKNGVQHVHAFIHTPTGTHFCEVEQRRSGLPVIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYQHSQDVDFEATWDIVRDTVLEKFAGPYDKGEYSPSVQKTLYDIQVLTLSRVPQIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLSSRL | 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.
Subcell... |
O74409 | MSETTYVKQCAYGKTLVRFMKKDICPKTKTHTVYEMDVQSLLTGELEESYTKADNSIVVPTDTQKNTIYVFAKNNDVSVPEVFAAKLAKHFVDKYKHIHGAALDITITPWTRMEVQGKPHSHSFIRNPGETRKTHVVFSEGKGFDVVSSLKDVLVLKSTGSGFTNFHKCEFTTLPEVTDRIFSTSIDCNYTFKHFDTFEELAGFDFNSIYEKVKEITLETFALDDSESVQATMYKMADTIINTYPAINEVYYALPNKHYFEINLAPFNIDNLGSNCSLYQPQAYPSGYITCTVARK | 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.
Subcell... |
A2RJJ9 | MGENTVPQKSSDNVGSIVALMVALLVAIFAFQLNASMLSPALVTMQAQLHTTASSIALTQTIFFTAAALFALFLPRLADLIGRKKVLIGMLTLTMIGCLISGFATNVGILMIGRILQGAAGPVVPLCLIILHVKVRDEKRYAKLMAILTSINGGIAGVDALAGGWLVSHGGFRSVFFVMGITAALAILLVSFGTQESTAKDTPKMDWTGVILLVVAMGALLSAVNALQGSFGNLGLPNWLLASILALLGLICFVGFWQVEKRVNHPMVPIHYLKQRRTWGLLITTLLTMTGVFAIMNGIIPALGQDGKFGLGLGADMVSL... | 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 | MPEAFERYSSNPTYEPPWRKVRFIGIAGPSGSGKTSVAQLIVKALNLPHVVILSLDSFYKSLNAEQKKRAFNNDYDFDSPEAIDWDLLFVKLLELKQGRKVDIPIYSFNEHNRLPETNTLFGASIIILEGIFALYDEKIRSLLDVSVFLDTDSDVCLSRRLNRDINYRGRDIVGVLEQYNKFVKPSYENFVRRQLSYTDLIVPRGRDNKLAIDMVINFIRRTLSIQSETHVKNIDSLQQIVPTIPHLPLNLVQLKITPEISAIRTILINKNTHPDDLQFFLSRIGTMLMNLAGDSLAYEKKTITLHNGNQWEGLQMAKEL... | 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.
Subcellul... |
P27515 | MSHRIAPSKERSSSFISILDDETRDTLKANAVMDGEVDVKKTKGKSSRYIPPWTTPYIIGIGGASGSGKTSVAAKIVSSINVPWTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVKPTMKNADAIIPSMSDNATAVNLIINHIKSKLELKSNEHLRELIKLGSSPSQDVLNRNIIHELPPTNQVLSLHTMLLNKNLNCADFVFYFDRL... | 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.
Subcellul... |
P09728 | MLRRGSLRNPLAICLLWWLGVVAAATEETREPTYFTCGCVIQNHVLKGAVKLYGQFPSPKTLRASAWLHDGENHERHRQPILVEGTATATEALYILLPTELSSPEGNRPRNYSATLTLASRDCYERFVCPVYDSGTPMGVLMNLTYLWYLGDYGAILKIYFGLFCGACVITRSLLLICGYYPPRE | 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
Seque... |
P09727 | MNLVMLILALWAPVAGSMPELSLTLFDEPPPLVETEPLPPLSDVSEYRVEYSEARCVLRSGGRLEALWTLRGNLSVPTPTPRVYYQTLEGYADRVPTPVEDVSESLVAKRYWLRDYRVPQRTKLVLFYFSPCHQCQTYYVECEPRCLVPWVPLWSSLEDIERLLFEDRRLMAYYALTIKSAQYTLMMVAVIQVFWGLYVKGWLHRHFPWMFSDQW | 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 c... |
Q9FMU5 | MSLSQNAPKSKGIKREELKKQYEDVEDEEEIGSDDDLTRGKRRKTEKEKQKLEESELVEMKKLENLIFGSLYSPVTFGKEEEEDGSALFHVDRSAVRQIPDYEDDGDDDEELSDEENGQVVAIRKGEAAWEDEEEKQINVDIASVNRLRKLRKEENEGLISGSEYIARLRAHHAKLNPGTDWARPDSQIVDGESSDDDDTQDGGVDDILRTNEDLVVKSRGNKLCAGRLEYSKLVDANAADPSNGPINSVHFHQNAQLLLTAGLDRRLRFFQIDGKRNTKIQSIFLEDCPIRKAAFLPNGSQVIVSGRRKFFYSFDLEKA... | 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 | MTSAYELVSDYQPAGDQPQAIKTLNEGLENGLAHQTLLGVTGSGKTFTLANVIAKSGRPTVIMAHNKTLAAQLYGEMKAFFPNNAVEYFVSYFDYYQPEAYVPTTDTFIEKDSSVNEHIEQMRLSATKALLERKDAIIIASVSAIYGLGDPQAYLSMMLHLSRGDIINQRDILRRLAELQYKRNDMAFERGTFRVRGEVLDVFPAESEHEAIRIELFDDEVERISKFDPLTGSIITKDMPRCTIYPKTHYVTPREKVLDAIEQIKVDLAERKKELLANNKLVEEQRISQRTQFDIEMMNELGFCSGIENYSRYLSGRPQG... | 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... |
B9KH59 | MQRFKISSEFNPSGDQPGAIDSLVRGISCGAKEQTLLGVTGSGKTFTMASVIEQTQRPAIIIAHNKTLAAQLHEEMRSFFPENAVEYFVSYYDYYQPEAYIPQSDVYIEKDALINDKIDLLRHSATRSLLERRDVVVVASVSCIYGLGSPELYSEMTVPIALGMKLDMCQLQERLVELQYKHGNRYERGSFSVQGDVLSVFPSHYEDRIWKISFFGDEVDSIQEVDPKSGMVTLKLEKIKIFPNSHYVTPRPTLLQAISEIEKELDECALQFKQCNKIVEADRIVERTRFDIEMMRETGTCKGIENYSRYLCGKEAGDPP... | 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... |
Q2GID5 | MRHFKITSEFDAAGDQPEAIRKLSEGIERGVREQVLLGVTGSGKTFTMASVIEKRQCPALIVAHNKTLAAQLYEEMRMFFPNNAVEYFVSYYDYYQPEAYIPHSDVYIEKDALINEKIDMLRHSATRSILERRDVIVVASVSCIYGLGSPELYSEMTIPLSIGMQIDLCQLKEKLVELQYKSGSQCERGTFSVKGDIVTIFPSHHEDHVWRISMFGDVIESIQEVDNNLGIAVANLEKVKVFPNSHYVTPRPTLMQALSRIEEELQECVINYRKNNKIIEAERILERTKFDIEMMKETGTCKGIENYSRYLCGKAAGEPP... | 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... |
Q81X47 | MERQFEIVSAYSPQGDQPVAIEKLVEGINSGKKKQVLLGATGTGKTFTISNVIKEVQKPTLVMAHNKTLAGQLYSELKDFFPNNAVEYFVSYYDYYQPEAYVPQTDTFIEKDAQINDEIDKLRHSATSALFERDDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEKDRNQLLRELVDVQYGRNDIDFKRGTFRVRGDVVEIFPASLDEHCIRIEFFGDEIDRIREVNALTGEVLAERDHVAIFPASHFVTREEKMKVAIENIEKELEERLKELNDNGKLLEAQRIEQRTRYDLEMMREMGFCSGIENYSRHLTLRPAGA... | 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... |
P56981 | MVEGRFQLVAPYEPQGDQPQAIAKLVDGLRRGVKHQTLLGATGTGKTFTISNVIAQVNKPTLVIAHNKTLAGQLYSELKEFFPHNAVEYFVSYYDYYQPEAYVPQTDTYIEKDAKINDEIDKLRHSATSALFERRDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEIERNALLRRLVDIQYDRNDIDFRGTFRVRGDVVEIFPASRDEHCIRVEFFGDEIERIREVDALTGKVLGEREHVAIFPASHFVTREEKMRLAIQNIEQELEERLAELRAQGKLLEAQRLEQRTRYDLEMMREMGFCSGIENYSRHLALRPPGS... | 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 ... |
Q884C9 | MSEFQLVTRFEPAGDQPEAIRQLVEGIDAGLAHQTLLGVTGSGKTFSIANVISQIKRPTLVLAPNKTLAAQLYGEFKAFFPNNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDHIEQMRLSATKALLERKDAIIVTTVSCIYGLGSPETYLRMVLHVDRGDKLDQRALLRRLADLQYTRNDMDFARATFRVRGDVIDIYPAESDLEAIRIELFDDEVESLSAFDPLTGEVIRKLPRFTFYPKSHYVTPRETLVEAMEGIKVELQERLEYLRSQNKLVEAQRLEQRTRFDLEMMLELGYCNGIENYSRYLSGRPSGAP... | 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... |
A1STV6 | MDKRFQLVSQFSPAGDQPQAIEQLINGLKSGLAFQTLLGVTGSGKTFTLANAIAKLNRPTLILAPNKTLAAQLYGEMKEFFPNNAVEYFVSYYDYYQPEAYVPSSDSFIEKDAAINAHIEQMRLSATKALLERKDVVLVASVSAIYGLGDPTAYLQMMLHLTVGEIISSREILQRLVDLQYNRNETELSRGTFRVRGEVIDIFPADSEKEALRIELFDDEVEQISVFDPLTGQGIDKLARVTVYPKTHYVTPREQILKAVDAIKVELNERKKEFLEQNKLLEEQRISQRTLYDIEMMNELGYCSGIENYSRYLSGRSEGQ... | 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... |
Q98I01 | MVSDFEPAGDQPTAIKDLVEGVDNNDRTQVLLGVTGSGKTFTMAKVIEETQRPALILAPNKTLAAQLYSEFKKFFPDNAVEYFVSYYDYYQPEAYVPRTDTFIEKESSINEQIDRMRHSATRSLLERDDVIIVASVSCIYGIGSVETYTAMTFQMQIGDRLDQRALLADLVAQQYKRQDINFVRGSFRVRGDTIEIFPAHLEDRAWRISMFGDEIEQITEFDPLTGQKTGELKSVKIYANSHYVTPRPTLNQAIKSIKEELKQRLVELERAGRLLEAQRLEQRTRFDLEMLEATGSCAGIENYSRYLTGRQPGDPPPTLF... | 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... |
Q7UFR2 | MSITKLAPAAFDLHQPFPPSGDQPAAIAKLIEGIQSGKTAQTLLGATGTGKTYTMANVIASVQRPALILSHNKTLAAQLYGEFKEFFPNNAVHYFVSYYDYYQPEAYIPQRDVYIEKDSSINEEIDRLRLATTSSLVSRRDVVIVASVSSIYGLGSPDDYRQLVVDLHQGEQTRRDHLLLKFVDLQYQRNDIQFERGKFRVRGDSIELWPSYEEFAYRIEMWGDEIEKISLIKPTSGETIKTVEHLYIYPCKHFVMPEDRIQRAIRLLREELTQQLEIFQSQGKLLEAQRLSARTKFDLEMLAEVGHCPGIENYSRPLSG... | 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... |
Q1RHI9 | MSNFSIISDYKPAGDQPKAIDEIIKGLNNKKRSQMLLGITGSGKTFTMANIIERTNRPTLIMAHNKTLAAQIYSEMKSIFPKNAVEYFVSYYDYYQPEAYIPKTDVFIEKDSSINEQIDLMRHSATRSLLERRDVIVVSSVSCIYGLGSPDLYYQMTVNLEPGKSYPRDKLLNDLVNLQYERNDIGFERGCFRVKGDNVDVFPSHYSDKAWRLSFFGNELEYIHEFDPLTGEKLVKLDKAIIYGNSHFVMPKETVNKAISEIEEELQKRIAFLKSQDKLLETQRINQRTQYDLEMLTETGSCKGVENYSRFFTGRKAGEP... | 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... |
P0A5A4 | MSVHATDAKPPGPSPADQLLDGLNPQQRQAVVHEGSPLLIVAGAGSGKTAVLTRRIAYLMAARGVGVGQILAITFTNKAAAEMRERVVGLVGEKARYMWVSTFHSTCVRILRNQAALIEGLNSNFSIYDADDSRRLLQMVGRDLGLDIKRYSPRLLANAISNLKNELIDPHQALAGLTEDSDDLARAVASVYDEYQRRLRAANALDFDDLIGETVAVLQAFPQIAQYYRRRFRHVLVDEYQDTNHAQYVLVRELVGRDSNDGIPPGELCVVGDADQSIYAFRGATIRNIEDFERDYPDTRTILLEQNYRSTQNILSAANS... | 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... |
Q9CD72 | MSVHTTDAKPDSEVDRLLDGLNPQQRQAVVHEGSPLLIVAGAGSGKTTVLARRIAYLIAARSVGVSQILAITFTNKAAAEMRERVARLVGDHTGPSMWVSTFHSTCVRILRNQASLIGGLNSNFSIYDVDDSRSLLQMIGQDMGLDIKRYSPRLMANAISNLKNELIDAESAVANLSSDTDDLARTVATVYGEYQRRLRTANALDFDDLIGETVGILQAFPQIAEHYRRRFRHVLVDEYQDTNHAQYVLVRELVGHGARNSPDDMPPGELCVVGDADQSIYAFRGSTISNIEDFERDYPDTTTILLEQNYRSTQNILSAA... | 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... |
P53528 | MVMVVNPLTAGLDDEQREAVLAPRGPVCVLAGAGTGKTRTITHRIAHLVGAGHVATGQVLAVTFTQRAAAEMRSRLRALGAAVQAVSDFGVVRVLTFHAAAHRQLRYFWPRVIGDTGWQLLDSKFATVARAASSVRLHAGTDDVCDLAGEIEWAKASLIGPEEYVAAVAAIGRDTPLDAAQIASVYAAYEALKARGNGVPGVTLLDFDDLLLHTAAAIENDAAVAEEFRDRYRCFVVDEYQDVTPLQQRVLSAWLGDRDDLTVVGDANQTIYSFTGASPCFLLDFPRRFPDATVVRLERDYRSTPQVVSLANQVIAAAHG... | 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 | MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISL... | 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... |
P45612 | MSVDNLLDLLNDQQLAAVLNIDKPVRIIAGAGSGKTRVITTKIAYLIEKQNIDPSRILAVTFTNKAAKEMKERVLQITNNSFKSPFISTFHSWCSKVLRIDGKHIGLEDKFLIIDSDDQKRIIKSALKESNIELSENDKKTFDKKILYKIKEWKEELVDPSEAILNATSTLEKNFAVIYRLYQNTLLKNNSLDFDDLQIYVYRLFKQNNEILNKWRNAYDYVLVDEFQDTNELQFSLIKFLTINTNHLTVVGDPDQTIYSWRGAKLDIILNFNKTYSNAISIVLNQNYRSTKQILDISNSFIKNNKFREHKEIFTNNKSG... | 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 si... |
P47486 | MNEQQKQAISCGKGVNVVYSGAGTGKTTIITNRFAYLVNKEKVDPSRILAITFTKKAAKEMQFRILKLIDSSLAEKTNIYTFHSFCNKFLIQTLKKRFIIDDDISYFLKEFLADSKLDINLAKQIIDNFKNTFADFEINKLDQDERLISLCEHSLLNKDEEYSTLKTQLINAFISYEKNKILNNKLDFHDLLIKTCNLLSNDNDLLNQWSEQFQHILVDEFQDTNQIQYELIKMLVTKNKNLFLVGDNNQMIYRWRGAVNGIITALKHDFNVPKSNEFFINQNYRCDQNILAVANQILLKIMAYEKQVKTEKNLLFSTLN... | 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 si... |
F4IHS9 | MGEMKSMQMGVIGALFLSVASSVSIVICNKALMTNLGFPFATTLTSWHLMVTYCTLHVAYKLNFFENKPIDMRTVVLFGLLNGISIGLLNLSLGFNSIGFYQMTKLAIIPFTVLLETLFLNKKFSQKIKFSLFLLLVGVGIASITDLQLNFVGSVLSLLAIATTCVGQILTNTIQKRLNVTSTQLLYQSAPFQAAILFVSGPFVDKYLTSLNVFSFHYSPIVVGFITLSCLIAVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYTLLHDPFTPRNIAGILIAVLGMLLYSYFCSVASKSKQASSDSTFLGKDRDTT... | 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 | MSEGQKFQLGTIGALSLSVVSSVSIVICNKALISTLGFTFATTLTSWHLLVTFCSLHVALWMKMFEHKPFDPRAVMGFGILNGISIGLLNLSLGFNSVGFYQMTKLAIIPCTVLLETLFFRKKFSRKIQFSLTILLLGVGIATVTDLQLNMLGSVLSLLAVVTTCVAQIMTNTIQKKFKVSSTQLLYQSCPYQAITLFVTGPFLDGLLTNQNVFAFKYTSQVVFFIVLSCLISVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYVLLRDPFDWRNILGILVAVIGMVVYSYYCSIETQQKASETSTQLPQMKESEK... | 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 | MATPPKRRAVEATGEKVLRYETFISDVLQRDLRKVLDHRDKVYEQLAKYLQLRNVIERLQEAKHSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLAEALKFIDRKSSLLTELSNSLTKDSMNIKAHIHMLLEGLRELQGLQNFPEKPHH | 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 induc... |
Q8UAW0 | MRHTWRWFGPVDKVTVQDAAQAGAEGIVSALHHITTGDVWPVDEITKRHEAIKAGGLYWDVVESVPVSEDIKTQTGDWKNHIANWQETLRRLSASGIRTVCYNFMPVLDWTRTDLRWETRHGARAMRFDLTDFAAFDIHILKRPDAKADYPDWLLEEAAKRFAEMPDTKIAALGRNIGAGLPGSADGYTLAQLLEKLRSYHGINRGRLQQNLIDFLSEVTPVAEEVGINICAHGDDPPWPLLGLPRILSTEADYAHMLSQVDSRANGVTLCTGSLGARADNDLPFIAGRFADRIHFVHLRNVTRDTDTVPCSFFEDEHLE... | 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 | MKETWRWFGESDPITLEHVRQTGASGVVTALHQIPDGTAWPAEEIAKRKAMIEAAGLEWSVCESIPMEQSIKRGDADAPKAIARWKDTLSRLGRAGVPVVCYNFMPVVDWTRTNLRWQARNTGLALRFEMADFVAYDVFILKRIRAAENYDPALVARAEERFAQMSEDEQSLLERNIIAGLPGGALVQTRQSIAALIASFDGIDSATMQGNLLAFLKEVVPVAEEVGVHLGIHPDDPPFSLFGLPRVVSTPADIRAILSAVESPNNGITLCTGSYGARSDNDLVAMAKEFASRVNFAHLRNVTVEADGSFFEDDHLDGGA... | 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 | MQMTFRWYGDSDPVTLEYIRQIPGVTGIVSAIYDIPVGEAWPYEKIVELKEKIENHGLSLSVIESVPVHEDIKLGLPTRDQYIENYKTTIRNLAKAGVKIVCYNFMPVFDWTRSSLDYALEDGSTALIYEEEKVRQMNPLHGELKLPGWDTSYEDGQLKNLFQQYQHMTEEDLWENLSYFIKAVIPAAENEQVKMAIHPDDPPWPIFGLPRIITNKENLERLIHLYDSSFNGLCLCSGSLGVKSTNDIPELIRYFGKKGKVNFVHLRNIKIIGEKSFQESSHRSEDGSLDMYEIVRALRDIDFAGPARPDHGRMIWGETG... | 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 | MNMTFRWYGRGNDTVTLEYVKQIPGVKGIVWALHQKPVGDVWEKEEIRAETEYIQSYGFHAEVVESVNVHEAIKLGNEERGRYIENYKQTIRNLAGFGVKVICYNFMPVFDWTRTDMFRPLEDGSTALFFEKAKVESLDPQELIRTVEEASDMTLPGWEPEKLARIKELFAAYRTVDEEKLWDNLSFFLQEILPVAEAYGVQMAIHPDDPPWPIFGLPRIITGEASYKKLRAISDSPSNCITLCTGSMGANPANDMVEIAKTYAGIAPFSHIRNVKIYENGDFIETSHLTKDGSINIQGVMEELHKQDYEGYVRPDHGRH... | 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 | MSFFGFGPAAELDIALTDGESRRRAEHKTEDGKKEKYFLFYDGETVSGRVTVNLRNPGKRLEHQGLKIEFIGQIELYYDRGNHHEFVSLVKDLARPGEISQSQSFDFEFTHVEKPYESYTGQNVKLRYFLRATLSRRLNDVVKEMDIVVHTLSTYPELNSSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIKHMEIDIIKRETTGTGPNVYHENDTIAKYEIMDGAPVRGESIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEIVLWRKGDIVRKSMSHQAAIASQRFEGTSHP... | 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 retrograd... |
O70410 | MASRQISLALGFLAFLWAVLGAQNKTEEVQCRLMAKFNLSGYVDAKNHSLVIAGLFPIHSRIIPVDEAILEPVSPMCEGFNFRGFRWMKTMIHTIKEINERKDILPNHTLGYQIFDSCYTISKAMESSLVFLTGQEEFKPNFRNSTGSTLAALVGSGGSSLSVAASRILGLYYMPQVGYTSSCSILSDKFQFPSYLRVLPSDNLQSEAIVNLIKHFGWVWVGAIAADDDYGKYGVKTFKEKMESANLCVAFSETIPKVYSNEKMQKAVKAVKTSTAKVIVLYTSDIDLSLFVLEMIHHNITDRTWIATEAWITSALIAKP... | 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 | MKLLTAFSPLVVLILFQEQISCYYLTKYASSGYYQDADFVIGGLFSLRVTDGDTFISRSGVEDTSHIAEYVFADLIKYYQHILAMVFAIEKINKDPNILFNKSLGFFLFNVNFIEMKAAEGSMALLSGESPPIPNYSCRPEKTDKLVAVIGGISTSISIQISRVLSLYNVPQISYAPFDQILGTRVQLQSPYQFSMHTAALYQGIVQLLLYFTWIWVGLVVPDDMRGELYLRDITKEMISHGICFAFAEKVTEYSSMDTVNWKHFMERLTLTPVIITVGDTHSLLRIVYFVIFYNLSGNVWITTSDWYITTLPFEQNLIY... | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96200
Sequence Length: 855
Subcellular Location: Cell membrane
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O94262 | MSEPKPMQMSVETETVLNVSQVQIPSSCDRKASLETLKTKKNAQKKKKISLPNVMTSKAAMFAARVASAVDQDPNDEESENFVYENLIPTNDDELHSPSASIHSFQTYNLPLEMLPTINHVPYYGSAGTNALNGGPLSNSRKLIPKRSAKFSSMVGSSDTRCNSPTTARGLATSPLQINPTTSKSPLLNKKLSSTSQEPFRTSRRSGQESGDVTTKMLRNLLHKRLWISFFFACFVVLSLVYFHYAVQPLL | 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: Sing... |
P0CM61 | MGSALSSCCSPRRKNAYEPLLLETEREAVADLLQYLENRSTTNFFAGSPLAALTTLSFSENVDLQRSAALAFAEITEKEVREVGRDTLDPVLYLLSSHDPEVQRAASAALGNLAVNAENKLLVVSLGGLEPLIRQMLSPNVEVQCNAVGCITNLATHDENKTQIAKSGALVPLTRLAKSKDMRVQRNATGALLNMTHSDENRQQLVAAGAIPVLVSLLNSPDTDVQYYCTTALSNIAVDAANRKKLAQSEPKLVQSLVQLMDSQSLKVQCQAALALRNLASDSKYQLEIVKFGGLKPLLRLLHSSYLPLILSAAACVRNV... | 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 | MGICSSTCCGGRARDGLYEPVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVFSENIDLQRSASLTFAEITERDVREVDRDTLEPILFLLQSPDIEVQRAASAALGNLAVDTENKVLIVQLGGLTPLIRQMMSPNVEVQCNAVGCITNLATHEENKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSPDVDVQYYCTTALSNIAVDASNRRKLAQSEPKLVQSLVNLMDSTSPKVQCQAALALRNLASDEKYQLDIVRANGLHPLLRLLQSSYLPLILSAVACIRN... | 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 | MGASCSSCCGGKSRDGLYDNVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVYSENIDLQRSASLTFAEITERDVRAVDRDTLEPILFLLQNSDIEVQRAASAALGNLAVNTDNKVLIVQLGGLAPLIRQMMSPNVEVQCNAVGCITNLATHEDNKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSTDVDVQYYCTTALSNIAVDANNRRKLAQTEPRLVQSLVNLMDSSSPKVQCQAALALRNLASDEKYQLEIVRASGLGPLLRLLQSSYLPLILSAVACIRN... | 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 | MGNCLSCCEKSKDEQYEPLLADREREAVADLLSFLEDRNEVNFYSEEPLRALTILAYSDNLDLQRSAALAFAEITEKDVREVDRETIEPVLFLLQSPDAEIQRAASVALGNLAVNAENKALVVKLNGLDLLIRQMMSPHVEVQCNAVGCITNLATLDENKSKIAHSGALGPLTRLAKSKDIRVQRNATGALLNMTHSYENRQQLVSAGTIPVLVSLLPSSDTDVQYYCTTSISNIAVDAVHRKRLAQSEPKLVRSLIQLMDTSSPKVQCQAALALRNLASDERYQIEIVQSNALPSLLRLLRSSYLPLILASVACIRNIS... | 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 | MGSCCSCLKDSSDEASVSPIADNEREAVTLLLGYLEDKDQLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEITEKYVRQVSREVLEPILILLQSQDPQIQVAACAALGNLAVNNENKLLIVEMGGLEPLINQMMGDNVEVQCNAVGCITNLATRDDNKHKIATSGALIPLTKLAKSKHIRVQRNATGALLNMTHSEENRKELVNAGAVPVLVSLLSSTDPDVQYYCTTALSNIAVDEANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLASDTSYQLEIVRAGGLPHLVKLIQSDSIPLVLASVACIRNIS... | 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 vac... |
O07783 | MNVRRALADTSVFIGIEATRFDPDRFAGYEWGVSVVTLGELRLGVLQASGPEAAARRLSTYQLAQRFEPLGIDEAVSEAWALLVSKLRAAKLRVPINDSWIAATAVAHGIAILTQDNDYAAMPDVEVITI | 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 protei... |
P96917 | MSTTPAAGVLDTSVFIATESGRQLDEALIPDRVATTVVTLAELRVGVLAAATTDIRAQRLATLESVADMETLPVDDDAARMWARLRIHLAESGRRVRINDLWIAAVAASRALPVITQDDDFAALDGAASVEIIRV | 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 | MVAKGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPGLLTSIYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIVEIAEEGDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLVLTKEFGLIKIKELYEKLDGKGRKIVEGNEEWTELEKPITVYGYKDGKIVEIKATHVYKGVSSGMVEIRTRTG... | 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 Activi... |
P31406 | MAGGIELAKKAIRSLKNYDEHENRYGSIFSVSGPVVVAANMLGCSMYELVRVGHEELVGEVIRIHQDKCTIQVYEETSGLTVGDPVQRTGKPLSVELGPGLAETIYDGIQRPLKQIFDKSQSIYIPRGINTESLNREHKWDFTPNKDLRIGDHVSGGDVFGSVFENSLFNDHKIMLPPRARGTVTYIAEAGSYHVDEKLLEVEFNGKKHSFSMLHTWPVRAARPVADNLTANQPLLTGQRVLDALYPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDLIVYVGCGERGNEMAEVLMDFPELTIDINGKPEPIMKRTTLV... | 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 ... |
A3DNQ6 | MSLGITGKIYRVSGPLVIAENMRGSKVYEVVEVGSDRLIGEIIGVEGDKAIIQVYEDTSGLRVGDPVYGTGYPLAAELGPGLVGSIYDGIQRPLPLLQELVGFFVKRGVKAKPLPRNKKWHFKPLVKQGEKVGPDDVIGYVEETPVIKHYIMIPPDTHGVVEEIVGEGEYTIVDPIARINGKEIVMLQKWPVRKPRPYREKLEHREPVLTGQRVIDFFFPLAKGGKAAIPGGFGTGKTVTLQQLTKWSAVDIAIYVGCGERGNEMADALHSFRRLVDPRTGKALVERSVFIANTSNMPVAARETSIFLGATIGEYFRDMG... | 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 | MADPRVPSSYNVTPRIRYNTVGGVNGPLVILDNVKFPRYNEIVTLTLPDGTQRSGQVLEARGNRAVVQVFEGTSGIDVKKTKVEFTGESLKLGVSEDMLGRIFDGSGRAIDKGPKVLAEEYLDINGSPINPYAREYPQEMISTGISAIDTMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVQRQGITNKGVHDGHEENFSIVFGAMGVNLETARFFTRDFEENGSLGRTTLFLNLANDPTIERIITPRLALTTAEYYAYQLEKHVLVILTDLSSYCDALREVSAAREEVPGRRGFPGYMYTDLSTIYERAGRVAGRN... | 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 intracellu... |
Q9C9Z8 | MNDADVSKQIQQMVRFIRQEAEEKANEISISAEEEFNIERLQLLESAKRKLRQDYDRKLKQVDIRKRIDYSTQLNASRIKYLQAQDDVVTAMKDSAAKDLLRVSNDKNNYKKLLKSLIIESLLRLKEPSVLLRCREMDKKVVESVIEDAKRQYAEKAKVGSPKITIDEKVFLPPPPNPKLPDSHDPHCSGGVVLASQDGKIVCENTLDARLDVAFRQKLPQIRTRLVGAPETSRA | 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: 23... |
P0CAN7 | MNDADASIQIQQMVRFIRQEAEEKANEISISSEEEFNIEKLQLVEAEKKKIRQEYEKKEKQVDVRKKIDYSMQLNASRIKVLQAQDDIVNAMKEEAAKQLLKVSQHGFFNHHHHQYKHLLKDLIVQCLLRLKEPAVLLRCREEDLDIVESMLDDASEEYCKKAKVHAPEIIVDKDIFLPPAPSDDDPHALSCAGGVVLASRDGKIVCENTLDARLEVAFRNKLPEIRKSLFGKVGAA | 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: 23... |
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 compartmen... |
A7TMI5 | MSVDKRTLIAVIGDEDTTTGLLLAGIGQITKETNEKNFFIYEDGKTTKEQILNNFINYTQERQDIAILLINQHIAEKIRSDIDNYTNAFPAILEIPSKDHPYDPEKDSVLKRVRRLFGE | 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 compartmen... |
P39111 | MAEKRTLIAVIADEDTTTGLLLAGIGQITPETQEKNFFVYQEGKTTKEEITDKFNHFTEERDDIAILLINQHIAENIRARVDSFTNAFPAILEIPSKDHPYDPEKDSVLKRVRKLFGE | 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 T... |
O82628 | MESNRGQGSIQQLLAAEVEAQHIVNAARTAKMARLKQAKEEAEKEIAEYKAQTEQDFQRKLEETSGDSGANVKRLEQETDTKIEQLKNEASRISKDVVEMLLKHVTTVKN | 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 | MPGKMVVILGASNILWIMFAASQAFKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKPFTVEISPG... | 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... |
Q9M2D2 | MYQSMNLSVSSNFTHRSLLESRFPIFSTGFRKSVNLKPPRVSSGPESNDSGHETLTDKLIHLLRAVPDWADEIKERGMQQKRSLYTHEKWVEHRSSLRHVRHLLSSFSSRVILSLIPPVFFFTSVAVVIASYNSAVALDWLPGIFPILRSSSLPYQLTAPALALLLVFRTEASYSRYEEGRKAWVGIIAGTNDLARQVICSVDSSGDELIIKDLLLRYIAAFPVALKCHVIYGSDIARDLRNLIEADDLSLILQAKHRPRCVIEFISQSIQLLKLDDAKRDLLESKMLHLHEGIGVCEQLMGIPIPLSYTRLTSRFLVFW... | 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 a... |
P04014 | MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRAL... | 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 ... |
P50760 | MDDDKGTDTTDAKEGCSGWFMLEAACSDDSDLDNSLEKLFEDGTESDVSDLINDDDTAAQGNSRELLCQQQSEECEQQIQYLKRKYFSPKAVQQLSPRLQSMNISPGHKSKRRLFVEHDSGLECSLNEAEDLTEEVEVPASAPAPAAQGGVGSGHYTSLLRCNNVKAVLLGKFKDAFGVSYNELTRQFRSNKTCCKHWVLAIYAAKDELIDASKQLLQQHCTYLWLQTFSPMSLYLCCFNVGKSRETVMRLLSSMLQVNENHILSEPPKIRSMIAALFWYKGSMNPNVYAFGEYPEWIMTQTMIHHQTADSVQFDLSEMI... | 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 ... |
P22156 | MMEALAERLSALQDRILELYEADSKDLKDQIEHWKCVRQECAVLYKAREVGFSHLNHQVVPSLTVSRAKAHKAIEVQLALESLQNSEYNNEEWTLQDASLEMWHTEPKGCFKKTGVPVTVLFDCDKDNTMEYVLWGHIYVWGDNGWVKTFGEADNWGLHYTVAGEKVYYVQFYEDAKKYGHGNGNGDGYEWEVHVGGTVMHYSDSVSSATHCDKLPTVEIVSGLQHINPSPPPANPSAKENVWSSPAKRVRRSDSGGDPVRALDGKSRSVLCGSAHNNATGSSGDSDYTPIVHLKGESNCLKCLRFRLGKHKHLYINISS... | 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 t... |
P11329 | MKMSAASDHLLAAQETQMQCIEKDSRLLQDHACYWGAVRREKLLLYAARTKGLKTIGCVPVPPCSVTAEQAKQAICMQLIVEELLHSPWAKEPWSLTDLSWERYQAAPKGCLKKGARVVEVEYDGNSSNKTWYTAWSTVYVRGTEEEGWETAVCAADGQGIYYCAGMSSKVYFETFETDARRWSRTGHWTVRDNDVIYHSTFGAPPHSRNDRDCIEGFWSDAGERRGSRGSDTTDRALPYPAARQSPICRPVRTGENRSRAVHRQAPYSAPSSPGSSVGPDSPSESSRQVPLVLLPGPSDPAPPSPDSTDVIAEGDKEPE... | 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 t... |
P06926 | MANDKEIAQTESGSHPKDLKETLQEKKPSQPSLSLLCSAPPPAVPSEQASVGYGTVLARTPTIFLQARGALFSALPPPRAGHGTGGLGIKAGRRGAVARLHRGRTSDSPKAHHQ | 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.... |
P11301 | MANDKEIAQTEFPHQKDLKETLQEKKPSQPSLSLLCSAPPPAYPSEQASVGYGTVLARTPTIFLQARGALFSALPPPRCRARYRWTWHQGRKKKKINRPTQQRRNL | 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.... |
Q07852 | MADKALHTPPPSTLRNNSYPGPPPATPKLPSRRALLEGGNRGNPTRPPPRPLKPREYDYDEDDEKENQGPGQEKPPAKEEEEEEEEEERPNWDLHHLLQKWGADIDKLKDKVCRDLDSYKQKLGIRL | 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.... |
P06924 | MTDPNSKAPRLQGRQEDKQTQTPPPRPPPPPQPPLTPRPDSSPHQNSHNKPKPEEEGTDGGPPASQGDRKRSKGDQGPDTGPGLGPGRGPSPKPTPLGPPPGPGPRRSPRLGPLQADRDPEEGPQPPAEGEVEGHPGGDQGHPPPPPPAPHNGHSGHEPKVQQPEGPEGREGHEEGAVGGEGGDEEGHPPPPPPPTNGHEGGLLSSVASLLVKWEGHFDQLVQSIQDDLEDYWKKLATPQ | 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.... |
P25485 | MHGNRPSLKDITLILDEIPEIVDLHCDEQFDSSEEENNHQLTEPDVQAYGVVTTCCKCGRTVRLVVECGQADLRELEQLFLKTLTLVCPHCA | 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 ... |
P17387 | MRGETPTLQDYVLDLQPEATDLHCYEQLPDSSDEEDVIDSPAGQAEPDTSNYNIVTFCCQCKSTLRLCVQSTQVDIRILQELLMGSFGIVCPNCSTRL | 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 g... |
Q80901 | MIGKEATIPEIVLELQELVQPTADLHCYEELSEEETEEERPHIPYKIVAPCCFCGSKLRLIVVATPIGIRSQEELLLGEVQLVCPNCRGKLRHD | 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 ... |
A0A1U9YI05 | MARPWLSASVLITAVILLVDYLNYYRLRKRLGGIPVVGDASYFWRRIRWTESDTNFQKVIQHGYDTFSKKAKPFAFWGQHEDFILVLPPGSCEEVKHLGPEKLNFLQAVEDSYHFKLHTNILGRSHVDAVRQSVNKNMNQLHEIVVKKAEETIPKLFDDIAASNEPFAAFLTIWHLVHIVSASYLVGTEFCANEEYLQAIEYYCINVPNFIYGYFWVPVPLRRLYWYLSPQGYKVRACKAKLKTFIVPKIRETISAWQNGQKSSSYTLLGAMLDLKAQKGQIKRDPTAMTKAELERQIDIFSDEMIFTGFDSAGPVACMV... | 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 synt... |
A0A1V6NVX3 | MHPSARLYNNIALWFYDYLVHSIFMVYGWHCPTKSVGLPFFSSHVGPKHMDVGVGTGYFPVAVRKSSRKRNGQLKPQWPQKLMLVDLNPNCTAMAATRVGAPDCTETLTADVLQPIPAAGKHETFDSLSLMNVLHCLPGTSESKAQAFGHLKPFLKEDGVLFGSTILGRGVEHNRFGRLVMWLSNSLGIFHNYGDHPDDFVRALQKDFNQVEHVVVGRVLLFTAKEPN | 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 ve... |
A0A1V6NWP3 | MTFRVIIVGGGVAGLTLASAFEKAGIDYILLECRPAFDVAVGASIALSPNGARILDQLGAWEKWLKIAQPLVRWGDRNSKGELIMPRSASTPLAKALTGYDMTFGLRRSLLQTLYDNIEDKSMLLPKKSVINVTCSQEGVAVQCADGCSYEGDILVGADGTYSKVREYMWRLADRDEPGLMDPDKKAMTAEYQCLFGISKASGSIAIGDADFIYDHDRSSFIFSDNCGRICYFILQKMDRVYEMVEIPRFSQANAQAYAQRHADIQIRPDLTFGNLYEHSESSILVALEEAKFKQWSWGRIVCVGDSIHKMTPNLGAGAS... | 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... |
A0A1V6NZ11 | MLCWELANRRKRIGPNRFGFPIAILTRQQLIEVLYTALSDKSKVKTGKKVVRIESEERRITTWTEDGSEYEGELVVGADGVHSVTRSEMWRAADNQQPGFIQEEEKYSLSAEYSCIWGLSTPVPGIRQGEQIIRSYDRLTFLIFPSQNGCLGWFAIQKLNRKHVYPDIRPFSQKDTLARCEALRDLPIWNDVKFGDLLTLTEVCAMTPLEENLFQTWNYGRILCIGDSISKLTPNIAQGANTAIEGAAAVANGLHQLLHHNGLNQPSYDEIQEVLGRYSQSQRKRMKKLHWISHMVTRLQSREGLINKFVGRYIYSHTGN... | 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... |
A0A1U9YHZ9 | MLSEMLGEIAALPMVSLLGAALIVVSVLGRRLLVSNIAWAITGQTPAKSLAKRSRLPGLPFKFPNGQGTEKFFGGRSAARRWRIQYGPIYAIWAGLKREVVLSTPEHVQAFYKDSHLHVKATDNNSGWLFAELLGSCVGVVSQGRWKRVRRPFEHPFSRPESLTRPKAFIHEARDYFAVLNPNIQELTINTSNDLKHCPFFMVASIFFGIHTTAQRDELKQLGPPREELFRHAFMGGMNRYAITKYLPGSALALLRQFQGKWEGFVKAAYNRSIQTGDGTIVPLFEAVNRGEMSMQELLQTLDESLFANLDVTAHAVSWN... | 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 synt... |
A0A1U9YI21 | MPINKFSARSLDNDVPNKPLIFVMEGRYQNWIKPIMLLECLEIDYDAACIDGPTTRTDWFTRLHPQRYVPAMIDVEDGQRVSSWDSSQMLQYLSNKYDAKRMWNGHNAAENLEICNWLTFETASLGPTAKYWVWYALRQGEEQNPKAQQKMYNDLRVQYSILDKHLAQPGQNWVGLKDRPTIADLAIYPFADDPTMARMGIDKKDFPSLKAWSEALSKVPGVAKAYAELDSRKEIAIGA | 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 syntheta... |
A0A1V6NXN7 | MAICIYEHDAAKIIPTLVSELPYSTTLLRRIQHGIAYPYETAHILATFPPGLTPEPGQPWLAARVDLFAGRTTQMIIYSSLEAEHTSIPPIVTVSDSTEILNVDSTSNNSKNNDTNDADNPDINSITKFIVSTFSASPPVLALARAQLLALLEYVKTNMLPFYLSYLAKSAQATSVAAETPPVSTSSVTSNNTSPTSVPLIPAPDPQAFLIGSLHTGLFSLLQQSGSYTLSNPIPNIRVHRFDDPPYYKYFFRRSEFSPEAVCGRSADLPFADLSLPSGYRFHDREGREGVLSKHLDLVQSRTHIPRPRAQLSKIPGMAV... | 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 ... |
A0A1V6NWJ0 | MVFAMLVVCWSIFLGLWMLVSRLKQSRDKICPPKGPPRLPWIGNLHQFPLKLLHLRLTEWSRTYGGFYTLKLGPVTAAVITDRQIAKEAFDRNSAISSTRHTNYATEFVTDGTHLLTMKYGALWREERKILQQTLKGSVCDNDHMRLIDAEQTQLMRDLLVNPSDYSAYIKRASTSIITSLVFGIRTPSCATLHLQELDAINDDWLQLLVIGGALSEDVFPVLKYIPSAFLGTFTKRLKGIRRRMRRLYGTMLNQTITRQRESPAPPARSMIDAVLNQREHFNLTDRQIEVLAGVTLEGGFDTTTSMLLVFVQAMTLHPE... | 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 t... |
A0A1U9YHZ6 | MLSRRARESNAWFLERFKRPLGRQGSKSNTNIDLATAENWLIRPEILSALKRNLQADFQSSHLSYAPGLGGTPELLSAISTFFNHFFSPTIPVAPEHIVTGAGCSSVLDTLINDICDDGDGLLVAAPYWGSFEVSSVLRNGVTLIPVQIKFHESHSAQGIVDAYRKAMENTSCKVRGLLFCNPHNPWGHILSVEVIDALLLFCEQADIHFVSDEIYALSTFGRMELPSGNLEHGEKFLSPATSFVSVLSRDLIKLGGCLITQANKELRMSQAILNNAKLCNAASAMVAPILGSTSQLSTLVNLNVQRMRKAARTAIQFAQ... | 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 i... |
A0A1U9YI27 | PIVSKMALLDDNLSKALKLLADVPLIDGHNDFPYFIRGWFPEQIDSLDCRNVRIAHTDLERLNQGRVGGVFWSAYVPCPDRHAKNDFVVDAQYESLRATMQQIDIIHTLIERYSDRLGLARTSSEVWEVFRSGRIASLIGVEGLHQIANSPGVMRNLYRLGVRYITLTHDSNNLYADSTNSSGPFHGGLSRDGISIVKEMNRIGMMVDLSHTSVATQKHVLAISKAPVIFSHSSCASVTEHPRNSPDDVLDMLKANGGVFMITFIRKPTDAESPTLEKVADHVQHVGDRIGYEHVGIGSDFDGVMLTASGLDDVSKFPLL... | 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 spe... |
A0A1U9YI11 | MTNTERSSSWKASSIPDQPMWYFGYGSNMKASSMADRKVTPLSTKIVTVPTHFVTFDIFGIPYSEPSYASLEQFPDGGTGKLDLVHHISRTQVLPACGVAHLLSPNDFHRLLVTEGSGVVYNLVEVQAYEMNKDGQPIPAPFTVHTLKAKWPQRPNGTPSARYMVRFLGLLSSSTYYQY | 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 sy... |
A0A1U9YHZ8 | MAVALFPILPIGCLLIYIIFKLWTRDERLKHLPPGPKGLPVIGNMLDMADTDKMMKKSKDWADEYGEIFYTKVGLYNFVWLSSPNAVRELMDKKGSIYSSRPPSPMINMVSNGERLNFLPYGHKWRTIRNILHSALNLETSSTYKPVQDFESKQALWEILHAKDDMEFNDINRRYSTSTIMTITYGLRVPTLQHPLYQDILTIVRHFSLATAPGEWVIDMVPMLADIVPQFLLQNWKNVARKWYKEDSEIYLALYNKLMDDIKRGTAPDCFLKDMAREKLKKNPIADTTAAFAAGALIEAGSDATTTALNNVVLACLLYP... | 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 synt... |
A0A1U9YI02 | MEAALKKLNIALQEAIDSFEGPLNQERLNELQTTESLPNKEVWSLASQTIDLADKIIHRLQPPSLQLAESFLAYLDTKCLWAAVSHDIPDLITAGGPQTVQELAKKSGLQSIRLKQVMRVLHNNGIFEYKPTTQKYSNTPSSTLLAKDHWTQWHLWVDLYGNEHYKAAEGIPDAIREGQTRCAAQIQYDTDESMFRYFARNGLQEKFHKTLGAGAVAQAPGMMADYNWGELDDAVVLDIGGGGGDFITSLLREHPSMRGGLFELDSVIEMVRPKYRDASGEFADVGDRMVDLHVGDFRVEVPAYEVYTMKWCLHNWLDED... | 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 ver... |
A0A1U9YI04 | MTEHTVSHANGSDLENAKKTYMLANNQKEIERMKNQHEWIKGSFGGLVKAPIDFDKKNQSILDSATADGTWLMDVRSLFPPETELIGFDIAPELYPPEGTRPRNVELVTADLLQGLPAQWIGRFDLVHQRFVFPNFETEVIREVLGRLMQCVKPGGWIQLVEPCAGENVSGPEPKWFLLLHKLANQFMRSAVPRDAILAILHEEGFVNINIESLDIVIGKHQRNKEMDARGRRSMRDSVSNMYPMITAEQLGMPKEEARAVLDKFEADMQKYRTAVRHVIIWAQRPE | 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 ver... |
A0A1U9YHZ1 | MATPMIYDALIIGGGPAGLAASLALARVCRTSMLFDSGEYRNEGAKEMHTFLSRDGIPPHDFRATCLQQLEKYKDYAYVTNTKITDIANTDVAPGLKGFKAVDFTKKEFFGRKLVLATGTEDVLPTHIEGYKENWPVHIYQCPFCDGFERKSYPIGLLTFPNPSYSHLALMLRPLNKDITIYSNGPVPTDEPTQTALKMVLAAGVKLDERPVRRLINNGDGPENGISIEFTSGATVKLGMLYHRPPTRSRAANLILQLGLETNAIGDVITDTMMLKTNVPGCVSAGDTQENMKQASVAAATGTRAAASIVFQLADEDGKK... | 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 . Th... |
Q9I6M7 | MRQRDLKFTFVVGEGKLAFDVVEFELEEALCEPFRLNLKLASDKNAIDFKQVLDQPGTFTLWQDGRPARYVHGIVSHFTQGSSGFRRTRYELLLEPQLARLELCCNWRIFQEKSVPEILQALLKEHRVLDYEQRIYHEHLPREYCVQAGDSDHYLHDRLAFEEGLVYYFRFDEHRHTLVCSDRLYVQERIAGGPVLFSAQPEGDNPQPVLHSFRYSENVRTARQTQRDYSFKRPTYDQEHHLAGEALEHQGSSYERYDYPGRYKRSGAGRPFTESRLRGHRRDARVASVSGDDPRLIPGHAFALEGHPRADFNAWWRPVR... | 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 ... |
A0KJB0 | MADSTGLQFTVKVGALPESTFVVAEFALDEALNRPFNLRLELASAQPDIDFGAVLDQPCELLVWYNGELQRRVCGVVSDFAQGDSGFRRTRYQLMVQPALWRLSLRQNCRIFQAQKPDEILSILLQEHGITDYAFALKNEHAKREYCVQYRETDLDFVNRLAAEEGMFYFHEFEAGKHRIVFADDAAALTAGPELFFNLGNRSLEQGPYVRQFHYREAVRPSDVELKDYSCKTPAYGLSHKKQGSELEHQRDTYQHFDYPGRYKQDPSGKAFAQHRLDALRNDAVAGQVKSNCAALLPGQTFSLTEHPNGSLNTDWQIVR... | 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 dec... |
K7WKL8 | MADSTGLQFTVKVGALPENTFVVAEFALDEALNRPFNLRLELASAQPDIDFGAVLDQPCELLVWYNGELQRRVCGVVSDFAQGDSGFRRTRYQLRVLPALWRLSLRQNSRIFQAQKPDEILSILLQEHGITDYAFALKNEHAKREYCVQYRESDLDFVNRLAAEEGMFYFHEFEAGKHRIVFADDAAALTQGPELFFNLGNRSLEQGPYVRQFHYREAVRPSDVELKDYSFKTPAYGLSHKKVGAELTHQRDTYQHFDFPGRYKEDPSGKAFAQHRLDALRNDAVAGQAKSNCAALLPGQSFSLTEHPNGSLNTDWQIVR... | 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 dec... |
W7E4C5 | MDLYISNYTSDDDMAILRRRWIELLPLVVGDIVHVENPEGYSYLLDPIIPGPGYVVTWYHQLHCLFFLMSEYDRLLRHGPNGKERSIPAGSSSIHTRHCFEILRHSILCHLDMTLEGGSAPFFNGTTGFGHAHVCQNRQEAIDWMEKNRANDNRMIIRA | 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 endop... |
W7E0Q5 | HLVSLQVYHYLHCINALRRAAYQHVYGAPTKEHLNHLDHCIDMLRQAAQCQSDLTPMLYFNPENDPNTMLIKSHQHSCRRFDLVNEWAMARSQCKGNTTCAIEVGKQVGGEM | 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 vicA... |
W7DZP2 | MLTKSRLQVFHELHCLNFLRKLIYPDVYGKIDYKGQIHANHCIDHIRRIAECGSNATPVVYTGYKNGNLYSEPETYTCRNFTLIRQWAEMKKIQNTQ | 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 endop... |
Q05934 | MRAMDTQVQSAERGLVLPPMNSTVSSATAATTATNTDTDTDGDRDEERESLAEDGSEWVPAYMLTRDRSRYLGHFLGVDKMLEAVKCKYCGVIIRRQGNSISMAEASQTHLWSTHKIDPNANYYSGWTGVEAGSTFMVRPPLKNHQGGSATTNSIANLLEIDEDFLKRTREKEMALPLVQSLAIIIASENLPLSFVDNTAVRLLINQNANSLSFIDHDLILNAIRSIAYNLDRIIQRTALRNNSDLSLIIDKNYLLMDPTDRSNQLSNRLKNQLFEMQKINFFSLSHSVWNNTISILSIQYYDDFHSQVKTLPLIIQNLH... | 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)... |
P27426 | MASKDSDVRCVKCQSLKPTTPLTGQDRCARCVAINELKPWISTCNINPCYDGDLSESNETIEMMDINSCREDTPSDAESETRFMPFVAHSKQPKHTSKNPTKGEIQYFPVEKCKDIHRVENQSSIDEEGKQCWICRDGESLPEARYCNCYGDLQYCHEECLKTWISMSGEKKCKFCQTPYKVNRQLSLKRGLPGYWDRDDRFVFIAGFIGMGTILAGWIASFFYLLVVLCGKYFTYKDVMIVVGGLAIIQVVGLMFSLFMYFQIGNLLRQYINYMTETNIDPLRT | 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 Ac... |
P03169 | MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEET... | 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-as... |
P19893 | MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFEQVTEDCNENPEKDVLAELGDILAQAVNHAGIDSSSTGPTLTTHSCSVSSAPLNKPTPTSVAVTNTPLPGASATPELSPRKKPRKTTRPFKVIIKPPVPPAPIMLPLIKQEDIKPEPDFTIQYRNKIIDTAGCIVISDSEEEQGEEVETRGATASSPSTGSGTPRVTSPTHPLSQMNHPPLPDPLGRPDEDSSSSSSSSCSSASDSESESEEMKCSSGGGASVTSSHHGRGGFGGAASSSLLSCGHQSSGGAST... | 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. ... |
Q8QME4 | MSRQINANTPVSRRRSGLRGRRLSYSPEDAVPTPAPRFSILEARRAADRPAEERMRAWHVIGDTSEPVTLRFVHNNAQYTVHGNAPFNTADFQEERDSQETEAANRAHQRAVHLHEHLHEVQETAAPLPNYSPVHSPDLTVMEDLETPRQRFETMFHAVDAESEDEAVPLPQVDMAVFCHICSCFFTDIKNYNSSFVTTSECNHAVCFKCYTSIMFDKELFKCSMCNRATPTCRVYNHKGFVELLPTRAVRDKQAIKTHWAQLLDNNMSDSKVPEQNDVQKLQAELAELRAEMASMRAEMASKQLGATMALENRRGSSSS... | 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: ... |
P07167 | MTWDRLLPSRKFLLAINSWYVLALVVAAISFAVLAIGPWKNEKSIEAILTELQSIDVDCALLQRNVLRAHAGLLRNYRPLMVPLGRVRSSIANLQQLFKKARVEDVGELSELLARLKSSINTTDAAVASFGAQNVVFEDSLATFNQSISSLLRTSDSRDLNAAKVPELGYLMLQFSFRPNTELALQITQSLDQLQMSTNADKVAIQEVVRNGRVILGVLPRLNETVKLVQASGTFENTKKLQRAYLEADSLARVVEQRVRTFLGAVSVFFCFGIVILVHKLRRRTDRLARRLDFEEVIKKIGVCFEDSTETKQSLKSSAE... | 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
|
P10799 | MNGRYSPTRQDFKTGAKPWSILALIVAAMIFAFMAVASWQDNATTQAILSQLRSINADSASLQRDVLRAHTGTVANYRPIISRLGALRKNLEDLKQLFRQSHIVSESNAAQLLRQLEVSLNSADAAVAAFGAQNVRLQDSLASFTRALSSLPGKASTDQTLEKPTELASMMLQFLRQPSPAISFEISLELERLQKQRGLDEAPVRILAREGPIILSLLPQVKDLVNMIQTSDTAEIAEMLQRECLEVYSLKNVEERSARIFLGSASVGLCLYIITLVYRLRKKTDWLARRLDYEELIKEIGVCFEGEAATTSSAQAALRI... | 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
E... |
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