ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9BZM6 | MAAAASPAFLLCLPLLHLLSGWSRAGWVDTHCLCYDFIITPKSRPEPQWCEVQGLVDERPFLHYDCVNHKAKAFASLGKKVNVTKTWEEQTETLRDVVDFLKGQLLDIQVENLIPIEPLTLQARMSCEHEAHGHGRGSWQFLFNGQKFLLFDSNNRKWTALHPGAKKMTEKWEKNRDVTMFFQKISLGDCKMWLEEFLMYWEQMLDPTKPPSLAPGTTQPKAMATTLSPWSLLIIFLCFILAGR | Function: Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27997
Sequence Length: 244
Subcellular Location: Cell membrane
|
Q9BZM5 | MAAAAATKILLCLPLLLLLSGWSRAGRADPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGNKTVTPVSPLGKKLNVTTAWKAQNPVLREVVDILTEQLRDIQLENYTPKEPLTLQARMSCEQKAEGHSSGSWQFSFDGQIFLLFDSEKRMWTTVHPGARKMKEKWENDKVVAMSFHYFSMGDCIGWLEDFLMGMDSTLEPSAGAPLAMSSGTTQLRATATTLILCCLLIILPCFILPGI | Function: Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27368
Sequence Length: 246
Subcellular Location: Cell membrane
|
Q6H3X3 | MAAAASPAFLLRLPLLLLLSSWCRTGLADPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGSKTVTPVSPLGKKLNVTTAWKAQNPVLREVVDILTEQLLDIQLENYIPKEPLTLQARMSCEQKAEGHGSGSWQLSFDGQIFLLFDSENRMWTTVHPGARKMKEKWENDKDMTMSFHYISMGDCTGWLEDFLMGMDSTLEPSAGAPPTMSSGTAQPRATATTLILCCLLIMCLLICSRHSLTQSHGHHPQSLQPPPHPPLLHPTWLLRRVLWSDSYQIAKRPLSGGHVTRVTLPIIGDDSHSLPCPLALYTINN... | Function: Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.
PTM: The functional form is cleaved C-terminally of the GPI-anchor and yields a 28 kDa protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37106
Sequence Length: 334
Subcellular Location: Cell membrane
|
Q9K3Z0 | MTDIAMLPESWREVLGGELQQPYFKELMEFVEEERANGPVYPPREEVFAALDATPFDRVKVLVLGQDPYHGEGQGHGLCFSVRPGVKVPPSLRNIYKEMHAELDTPIPDNGYLMPWAEQGVLLLNAVLTVRAGEANSHKSRGWELFTDAVIRAVAARTDPAVFVLWGNYAQKKLPLIDEARHVVVKGAHPSPLSAKKFFGSRPFTQINEAVAGQGHEPIDWTIPNLG | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25205
... |
Q8UCM8 | MEAGMAEAGVKLEDSWKHVLSGEFASPYMQKLKEFLLAEKTAGKRIFPKGAEYFRALDLTPLDEVKVVILGQDPYHGLGQAHGLCFSVQPGVRIPPSLVNIYKELQSDLGIRPVKHGFLESWAKQGVLLLNSVLTVEEARAASHQGQGWEKFTDAVIRAVNDECDHVVFLLWGSYAQKKAAFVDQRKHLVLRSPHPSPLSAHNGFFGNGHFSKANAFLVSHGRDPIDWQLPDVVEGDKNLL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 26719
... |
Q8X444 | MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQHGETPIDWMPVLPAESE | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25662
... |
B6EM11 | MTYFEAFFLALLQGFTEFLPISSSAHLILPSEVLGWSDQGLAFDVAVHVGTLAAVVMYFRKEVVTLLSAWTFSIVKKEHNKESKLAWLIILSTIPAAVCGLMFKDFIEVYLRSAWVIAITTIVFGLLLWWVDKNSTLVKDEYEMTWKKALFLGIAQAAAMIPGTSRSGITITAALYLGFTREAAARFSFLMSIPIITLAGSYLGLKLALSDAIIHFGFLGTGIIVSFISAYICIHFFLKLISSMGMTPFVIYRLLLGTSLLAWLALT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29519
Seque... |
A6TW45 | MTTFKAILLGIVQGLTEFLPVSSSGHLAVTQHLLGVPEDRILFLTILLHVGTLFSVFFVYADDIFMICKEFILMIVDLLTGKGIRVNNQYRKLGLLIIVATIPTGIIGLFFKDLFTSFYNSTLIIGISLLVTGTLLWTAEKVNTGKRDIKDMNWFDAVIVGLFQGLAITPGISRSGSTIVGSLFRGFNKELATKFSFLISIPAILGATVFEVKDVLEVGLGDFTLTMLIAGVLASFLSGVFAIRTLINFIKKEKLYYFSYYTWTVGSIVILFSLL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30322
Seque... |
B4RY28 | MTLFEIIILAIIQGVTEFLPISSSGHLLLPAELLGWVSQGLAFDVAVHVGSLLAVMIYFRQEIGQMTVAWVTQGFSKQQSTDSKLAWYVIVGTIPAVIIGFLMKGWIEENARTALVIAGTTIIFGLLLWYADATAKREQELEGLTLKQAIYIGLAQVLALIPGTSRSGITMTAGLMLGLKREACARFSFLLSIPVILGAGLLATLDLLSANEAVDWYALLYGAAFSFVSAYLCIYLFLSWIARIGMLPFVIYRLALGAVLLWFVFA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28991
Seque... |
A7H6N5 | MSLLAAVFLGVLQAATEFLPVSSTAHLLVFGELLGHDLADPRFRAFATIIQTGTTLAVLVYFRTEILSLLAAGLRSLARRRPLETPQSRLAWFIVLGTVPAAVLGKLFEERIEALGNWVIAGSLVVLGLVLLAAERYARHLRTVEDVGARDAVLIGLGQALALVPGSSRSGTTITAGMLLGFTREAAARFSFLLSVPIILGAGGYKLWKTVPVLRGEPSWALATLVGTAVSAVAGYLVIDWLLGWLRTRTTHLFVVWRIAAGVALAILIWQGVLPAGHASVSAPAVEAARAADPDAPLGAALRR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32162
Seque... |
B7GJC8 | MHIIELIKALILGLVEGATEFAPVSSTGHMIIVDDMWLKSSEFLGKYGANTFKVVIQLGSVLAAVVVFKDKFFELLYLRKGEVRKGPRLTLMHIFVGLLPAGVLGVLFEDYIDEHLFSTKTVLIGLVLGALLMIAADRFGKRTVAQTVDDITYKQAFIVGLVQCLSLWPGFSRSGSTISGGVLVGMSHRAAADFTFIMAVPIMAGASAISLLKNWQYITFDALPFFVVGFISAFVFALLAIRFFLRLINRVRLVPFAIYRIVLAAVIYVVYFA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30068
Seque... |
O67939 | MTEWQAVVLGIVEGISEFLPISSTGHLILTAHILGIKHTDFVKSFEISIQLGSILAVVVLYFNRLIRDYEIWKRIIAAFIPTGIIGFLLYKLIKGFLIGNDLVVVVSLILGGIILIFADTYCEKFCYLGDVRELPLRKAFMIGVFQSIAVIPGVSRSGSTIIGGMLMGLNRKVAAEFSFLLAIPTMFAATTYDLIKSGGSFNAQEWNILIIGFITSFITALIVVKWFLNFLKSHSLKIFGFYRILIGLVYAAFFLF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28466
Seque... |
P39438 | MLIDQYLDAALLGLIEGLTEFLPVSSTGHLIIFDTLLGFEGPPGKVFEVVIQLGAILAICTVYFARLWKVVTGLKDDPGARHFAMAVILAFLPAMVLGAALHGVIKAVLFNPTVVSIALILGGVAILMAERLVPAPRYHQIERFPAPLALKIGLCQCLALVPGVSRSGATILGSLLMGVDRRTAAEF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin (By similarity).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
P94507 | MTLWELFVAAILGIVEGLTEYAPVSSTGHMIIVDDIWLKSSNLMSEEAANSFKVVIQLGSILAVAIVFKDRILNLLGLKKNITSDQEQGHKLSIAQIAVGLVPAAVLGFLFEDYIDEYLFSVKTVAIGLIAGAILMLFADWVNKRKTATDTLDRISYKQAIAVGLFQCLSLWPGFSRSGSTISGGVILGLNHRAAADFTFIMAMPIMMGASFLSLVKHWDSLSSDLMPFFIVGFICAFVVALFVVRFFLRLINKIKLVPFAIYRIILGVILLLIMM | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30345
Seque... |
Q8A2U3 | MSWLEAMILGLIQGLTEYLPVSSSGHLAIGSALFGIQGEENLAFTIVVHVATVCSTLVILWKEIDWIFKGLFKFQMNDETRYVINIVISMIPIGIVGVFFKDYVEAIFGSGLMIVGCMLLLTAALLSFSYYYKPRQKDKISMKDAFIIGLAQACAVLPGLSRSGSTIATGLLLGDNKAKLAQFSFLMVIPPILGEALLDSVKMMKGEDVVGDIPALSLIVGFLAAFVAGCLACKWMINIVKKGKLIYFAIYCAIAGLAVIITQL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28563
Seque... |
A5UMH8 | MDIIQAIIIGIVQGLTEFLPVSSSAHLIFAQNALGVESSLAFDVFLHLGSLIAVLWFFRADIIRMIQAFLLSIGDIIQHRFKEGFYSDPYKRLVWYVIIATIPVGLVGVLFESQVESLFAGALYVPAFFLFVTGTILYLSQRMNSGEVDLSNLSLKESIFMGLGQACAILPGLSRSGTTIAAGLVIGLDKEFAAKFSFILSIPAILGAFVVQLKDIGTITDFNALAILFGFLAALISGYLAIKWLLELIQKRSLDIFAYYCWIVGIIVFMGSITHLF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30380
Sequence Length: 277
Subcellular Locati... |
Q2NIA2 | MLDILSAIILGAVQGISEFLPISSSGHLVLVPALLGIETGLAFDTILHIGTLVAIFTFFWKDIINLIKGFILSIIDLTEGVDIFKRELHRVPEKRFAWLIIVGTIPTGIMGILLKDAIETIFRGTLFVGIFLLVTAAVLYYSERHSSGQITQKDMSFKQALIVGICQGLAVFPGISRSGSTIASGLCLGLNREYAARYSFLLSIPAVIGAGLIQIKDIATLDASASVLLAGFISSVIFGYLSIKLLMKMIKGWSLDIFAYYCTIIGIITIILSVVL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29844
Sequence Length: 276
Subcellular Locati... |
O27479 | MVIIGTVPAGLAGVLFKDFFESLFSSLTAVGFFLLVTGFLLWGSENISRRVREKLPVEKLGVRESLIIGCAQALAIAPGISRSGATISAGLFLGFERELAARYSFLLSIPAILGAALIQIKDIGAGMNLLGASMVAGFAAAAVSGYIAIKFLLKLIKERDLYIFAYYCWALGIMILAAALI | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19211
Sequence Length: 181
Subcellular Locati... |
A0B9M2 | MDALQALVLGALQGITEWLPVSSEGQTMLAMISWLGMRPTDALSCSIFLHTGTMLAVLVRFRSRLLGMLNTESKLMRTVIVATLFTGITGVPLYMLFRDRFTGGEQATLLIGSLLIATGLMLRLRSSSTKDMEEISTKDMVLLGLAQGFSILPGVSRSGTTLTVLLMRGVKQDDALMVSFIISVPAVLGAIALDCLAGSPLSIRSLPGAVMLASSFITGYATMDVLMRFSRNVSFSWFCITMGMITLALTALPEVQ | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27511
Sequence Length: 256
Subcellular Locati... |
Q2RKY8 | MTVLQAIVLGLVQGVGEFLPISSSAHLILTPWFFRWPDPGLTFDVALHLGTLIAVVAYFWRDIIELVLSGLGQPRSQDGRLFWYLIVASIPGAIFGVLFEKQAETIFRSPLLIALTLTLMGLGLWWADRVGRKRRQLDDVNLFDGIIVGISQALAIIPGVSRSGITMTAGLLTGMERETAARFSFLMSVPIIAGAALLKLKELPLHEVNLAFIAGVLTAAVVGFLAIKFLLQYLRRGSYLLFTGYRILLAALIVAVFWLRR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28734
Seque... |
P60939 | MTAHLSYVEAVVVGAFQGVTELFPVSSLGHAVLVPALVGGRWAQDLSVSAHRSPYLAFIVGLHVATAAALLVFFWRDWVRILAGFFSSLRHRRIRTPDERLAWLIVVGTIPVGLAGLALEQLFRTTLGKPVPAAAFLLLNGVALYAGEVLRRRVAPVADEPAVPDAEQQHGDEASDNRLAQLPLRRGVLIGAAQILALLPGISRSGITIVAGLWRGLSHEDAARFSFLLATPIILAAGVYKIPELFGPLGAGIGGQVLAGSIASFVCAYLAVRYLTRYFQTRTLTPFAIYCAVAGGASLVWLALR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32549
Seque... |
O67914 | MIVELSHPLIKHKVNTARIQDTSAEKLRKTLKELGFMLVYEALKDILLEEKEVRTWIGNKRFNYLNEEEIVFVPILRAGLSFLEGALQVVPNAKVGFLGIKRNEETLESHIYYSRLPELKGKIVVILDPMLATGGTLEVALREILKHSPLKVKSVHAIAAPEGLKRIEEKFKEVEIFVGNVDERLNDKGYIIPGLGDIGDRLYAVSVY | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23533
Sequence L... |
Q9M336 | MACSIGNAFRCSSDTLRFAPRQQCSSRLNPNPSSFLSFNSSPILAQNLGASSSSLSRRTIRARTKMAASEASINGSNRMLVFVPPHPLIKHWISVLRNEQTPCPVFRNAIAELGRLLMYEASREWLPTVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGTETHWVK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Uracil phosphoribosyltransferase (UPRT) that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. Is probably the only functional UPRT, since the dual-domain proteins of the UKL... |
B9DTU7 | MGKCQVISHPLIQHKLSILRREDTSTKNFRELVNEIAMLMGYEVSRDLPLEDVEIQTPVAKTIQKQLTGKKLAIVPILRAGIGMVDGFLSLVPAAKVGHIGMYRDEETLEPVEYLVKLPEDIDQRQIFVVDPMLATGGSAILAVDSLKKRGAGNIKFVCLVAAPEGVKKLQEAHPDVDIYTAALDEKLNEHGYIVPGLGDAGDRLFGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22897
Sequence L... |
Q4JAV0 | MTLYVLSKPILLHFLTQLRSKNIDQISFRKNLVKLGRIIGYEIVNTLDYESIDVETPLGTKAKGIYIYDLENILIISILRAATPFVEGLLKALPTARLGVIAASRKEKEVQVGYPEDIPVDVYYMKIPQVSHKDTVIIADPMIATGSTMRKAIKSIVNSQPKRIYIASVIISEYGLKRLMEEFPFVDIFTISVDPEIDNRGFILPGLGDAGDRAFG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 24145
Sequence L... |
Q67TC9 | MSRVVVIDHPLIQHKLSIIRDKDTGPKEFRELVNEIAMLMAYEVTRDLPTEEVEVDTPIARARCRRLAGEKLGLIPILRAGLGMVQGILSLYPTARVGHIGLYRDPDTLKPVEYYCKLPTDLGERELLVLDPMLATGGSVVASLDLIKRQGGRRIKLLCLIAAPEGVQAVQEAHPDVDIYLAALDEMLNEHAYIVPGLGDAGDRLFGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23042
Sequence L... |
Q31MH4 | MAPQLRIFVPPHPLIRHWLGIARDRQTPTPLFRTAIAELGRWLAYEAVREWLPTIPAAVQTPLAETPAEFVDFSQPLAIVPILRAGLGLVESVQQVLPTARIFHVGLKRDEVSLEPRCYLNHLPEQLEVNSRVLVLDPMLATGGSLLYTLDLLRDRGVSAEQVRVLSIVAAPPALQKLSQAYPALTIYSAIIDEQLNDKGFIVPGLGDAGDRLFGTP | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23903
Sequence L... |
P72753 | MASQLRVYVPEHPLIKHWLGVARDENTPPVLFKTAMGELGRWLTYEAARYWLPTVDTEVKTPLAIAKASLIDPQTPFVIVPILRAGLALVEGAQGLLPLAKIYHLGLVRNETTLEPSLYLNKLPERFAPGTHLLLLDPMLATGNTIMAALDLLMARDIDANLIRLVSVVAAPTALQKLSNAHPNLTIYTAMIDEQLNDRGYIVPGLGDAGDRCFGT | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23638
Sequence L... |
Q5JGQ6 | MKRDERWEGVYSFEDSPFIMEILTELRDESTGPIAFRKGLVKLGRYMAYEITKTMATEKVPIRTPLEETEGIIVKDRRNVVIITVLRAAIPLMEGLIKVFEHARVGIVSASRGKAPKFEIEMKYVKVPRIKAEDTVIIADPMIATGSTLIKVLDEVKKYGNAKRYVVVGVLAAPEGITRIKEAHPDVEMFVAAIDRELNDHGYILPGLGDAGDRAFGEPIRFEDGAPGGI | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 25570
Sequence L... |
A8ESZ8 | MKISKEKYASMYGPTTGDRFRLADTTLIAKIEKDYTIYGEESKFGGGKTVRDGMAQSPTAVDVADLIITNAIIIDYTGIYKADIGIKDGKILAIGKSGNPNLCDGITEGLEIGANTEILSAEGKIITAGGIDTHIHFISPGQINEALSSGVTTMIGGGTGPNTGTNATTCTPGEWNISKMIQSVDDLPLNFGFMGKGNSSSYEALKVQIEAGAMGLKLHEDWGSTPNAIDTCLSVADDFDVQVAIHTDTLNESGFVEATVGAFKNRTIHTFHSEGAGGGHAPDIMKVAGLSNVLPSSTNPTLPYTKNTIEEHLDMLMVCH... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 60814
Sequence Length: 566
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
A7HHN1 | MTRRMDRRQYAQVYGPTTGDRVRLGDTALVLEVDRDLTVYGDECVFGGGKVLRDGMGQAAGAPPEEVLDLVITNALVLDQGGVTKADVGIRGGRIAALGKAGNPDAMAGVTPGMTIGPGTECIAGEGLILTAGGVDSHIHFISPQQAYEAIASGVTTMLGGGTGPATGTNATTCTPGARHVALLLQATDALPVNIGLLGKGNAASPEGLAEQVRAGAVGLKLHEDWGTTPAAIDTCLRVADQLDVQVAIHTDTLNESGCAEHSIAAFAGRTIHTFHTEGAGGGHAPDIIRVCGEPNVLPSSTNPTRPFTVNTVDEHLDML... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 60120
Sequence Length: 571
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
Q88J04 | MSHISRQAYADMFGPTVGDRVRLADTALWVEVEKDFTIYGEEVKFGGGKVIRDGMGQGQMLAAEAMDLVLTNALIIDHWGIVKADIGIKHGRIAVIGKAGNPDVQPGVNVPVGPGTEVIAAEGKIVTAGGVDSHIHFICPQQVDEALNSGVTTFIGGGTGPATGTNATTCTPGPWYLARMLQAADSLPINIGLLGKGNASRPDALREQIAAGAVGLKLHEDWGSTPAAIDCCLGVAEEMDIQVAIHTDTLNESGCIEDTLAAIGDRTIHTFHTEGAGGGHAPDIIRAAGQANVLPSSTNPTLPYTINTVDEHLDMLMVCH... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 60531
Sequence Length: 567
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
Q0RQR9 | MIPGEILPGEDPVEINPGRPVRTVLVRNTGDRPVQVGSHYHFAAANPALDFDRDLAWGHRLAVPAGTAVRFEPGVEREVDLVPLTGARIVPGLRPESAGPLDGRAVRAGGAVRAGGAVRAGGAVVGDSPAATPGTTGATGDLPGYLGEGS | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 15182
Sequence Length: 150
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
|
Q2JES5 | MIPGEILTGDDPVEINAGRPVRTVLVRNMGDRPVQVGSHYHFAAANPALDFDRASAWGHRLAVPAGTAVRFEPGVEREIELVPLAGARVVPGLRPESAGPLDAASGTRIADTATIEDISGFQGEGS | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13178
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
|
Q5KYM0 | MIPGEYRLREEPIVCNRQKSATKLTVVNRGDRPVQVGSHFHFFEVNSFLEFDRQAAYGKHLNIPAGTAVRFEPGDAKQVELVPFSGERRVYGLNNMVNGPLDGNGKGGVRE | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 12386
Sequence Length: 111
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
|
B7K907 | MIPGEIITLPEDQEIILNAGRPTLDIMVSNKGDRPIQVGSHYHFLEVNEDLEFYEIDSESKNFIFIDRSNLHNKTRGMRLNIPAGTAVRFEPGDIKKVQLVPLAGTREIYGFNGKINGQLDSSVEQ | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 14183
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
|
Q9KG60 | MIPGEVIPANGEVVLNKGRRMVKVLVAHTGDRPIQVGSHFHFAEVNRSLHFDRQEAFGMRLNIAAGTAVRFEPGEEKEVDLVEIGGKRQIYGLNGWTDGAIDDENLPSFLASYQVSEDKEDEEK | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13792
Sequence Length: 124
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
|
Q75ZQ6 | MSDGLVPGEVIPGEGTVTLNEGRERTEVTVGNTGDRPSQVGSHFHFFEANAALEFDREAAMGMRLNIPAGTAVRFEPGDEQTVELVEIGGKRRAHGMNGLVNGSVDGETGDAVERMRAAGFGDTGEAAPDDGDTESDQ | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 14476
Sequence Length: 138
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
|
P18315 | MIPGEYHVKPGQIALNTGRATCRVVVENHGDRPIQVGSHYHFAEVNPALKFDRQQAAGYRLNIPAGTAVRFEPGQKREVELVAFAGHRAVFGFRGEVMGPLEVNDE | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11695
Sequence Length: 106
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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B3R3Z9 | MELTPREKDKLLIFTAALLAERRKARGLKLNYPEAVALITAAIMEGARDGRTVAELMHEGTTVLTREDVMDGIAEMIPEIQVEATFPDGTKLVTVHHPIV | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11037
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
|
E6Y5X0 | MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKV... | Cofactor: Binds 2 nickel ions per subunit.
Function: Urea hydrolase involved in recycling metabolically derived urea generated internally or externally (By similarity). Is able to impair growth of the phytopathogenic fungus Penicillium herguei, and shows entomotoxic activity by inhibiting diuresis in Malpighian tubules... |
Q9SR52 | MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGDKSVAELMDIGRQLLGRRQVLPAVLHLLYTVQVEGTFRDGTKLVTVHEPISLENGNLELALHGSFLPVPSLDKFPEVHEGVIIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVNIGGNKVIRGGNGIVDGLVDDVNWTVLMETMERRGFKHLEDIDASEGIAGEDPRFTTMISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLR... | Cofactor: Binds 2 nickel ions per subunit.
Function: Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 91024
Sequence Length: 83... |
Q6A3P9 | MHLIPKELDKLVISQLGFLAQRRLARGVRLNHAEAAALISSNLQELIRDGHYSVADLMSIGKTMLGRRHVLPSVVHTLVELQVEGTFPTGTYLVTVHHPISSDDGDLEKALYGSFLPIPPADTFPDPNPDDYLPEKMPGAVLPVKNERITLNDGRKRIRLKVMSKGDRPIQVGSHYHFIETNPQLHFDRLRAYGYRLDIPAGTSVRFEPGDTKTVTLVEIAGNRIIKGGNSIASGKVDISRAEEILQRLQVEGFAHVPEPAPTADSALIAPFTMDREAYARMFGPTTGDLVRLGLTNLWVRVEKDCTVYGDECAFGGGKT... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 90912
Sequence Length: 838
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
P07374 | MKLSPREVEKLGLHNAGYLAQKRLARGVRLNYTEAVALIASQIMEYARDGEKTVAQLMCLGQHLLGRRQVLPAVPHLLNAVQVEATFPDGTKLVTVHDPISRENGELQEALFGSLLPVPSLDKFAETKEDNRIPGEILCEDECLTLNIGRKAVILKVTSKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGTAVRFEPGDCKSVTLVSIEGNKVIRGGNAIADGPVNETNLEAAMHAVRSKGFGHEEEKDASEGFTKEDPNCPFNTFIHRKEYANKYGPTTGDKIRLGDTNLLAEIEKDYALYGDECVFGGGKV... | Cofactor: Binds 2 nickel ions per subunit.
Function: Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism . Is known to be highly toxic and lethal when given by intravenous route, producing convulsions and other signs of central nervous system intoxication associated with the high ... |
O13465 | MHLLPRETDKLILTTLGTLAQRRLARGLILNRAETIALISSQLQEFVRDGRHSVAELMDLGKKMLGRRHVRKGVPESIHTIQVEGTFPDGVFLVTVDDPISSDDGDLNNAFYGSFLPIPSADVFPAAPEPADTLLGALICRKETVKINASRRRFRLEVKNAGDRPVQVGSHYHFLETNPALIFDRLLSYGYHLDIPAGTAVRFEPGEKKTVTMVEFGGKKIFHGGSGLGNGSFDENLRETKVKEMVEKGGFGHKEQEKIEEGPVTEMNREVYASMFGPTTGDKIKLADMDLWIEVEKDYTVYGDECKFGGGKVIRDGGGQ... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 90475
Sequence Length: 833
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
O32033 | MGKNPVVIGIAGGSGSGKTSVTRSIYEQFKGHSILMIQQDLYYKDQSHLPFEERLNTNYDHPLAFDNDYLIEHIQDLLNYRPIEKPIYDYKLHTRSEETVHVEPKDVIILEGILVLEDKRLRDLMDIKLYVDTDADLRIIRRIMRDINERGRSIDSVIEQYVSVVRPMHNQFVEPTKRYADIIIPEGGQNHVAIDLMVTKIQTILEQNAIL | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 24487
Sequence Length: 211
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
Q59190 | MAKIIGISGGSGSGKTTVVSKISEFIPEFVLISQDNYYKSVGDYEHEFSKVNFDHPDAFDNNLFYEHLKNLKKNSPIDMPLYDFINHKRQLKTVLVVPTPVVIVEGIMIFVEERVRNLIDLKIYIDTPNDIRFIRRLRRDISKRGRTVESVIDQYLNTTRWGYYRFIEPTKEYADLIIPEGGHNDKALYVLSTFLKSLSKEGLDFT | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 23874
Sequence Length: 206
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
Q9Z7H0 | MLMMLMMIIGITGGSGAGKTTLTQNIKEIFGEDVSVICQDNYYKDRSHYTPEERANLIWDHPDAFDNDLLISDIKRLKNNEIVQAPVFDFVLGNRSKTEIETIYPSKVILVEGILVFENQELRDLMDIRIFVDTDADERILRRMVRDVQEQGDSVDCIMSRYLSMVKPMHEKFIEPTRKYADIIVHGNYRQNVVTNILSQKIKNHLENALESDETYYMVNSK | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 25758
Sequence Length: 222
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
B5ZBE2 | MNAKSPILVLIAGASGSGKTTFANEIVARIPQNTTSVIICQDSYYISNSQLNKNERRLINYDHPSSFEWDLMREQLSDIKKRKKIKVPIYDYKTEIRLDKTIDISDVDVIVFEGIYAIYDDVINQIADLKVFIETPKDECLIRRILRDVNERNRSFESVITQWRSTVSPMYDQFVEPSKKNANVSVLWNEHNRVALHLINKWINNIH | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 24103
Sequence Length: 207
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
Q9KT67 | MSENNQCVIVGIAGASASGKSLIASTIYNELRAKVGDHQIGVITEDCYYKDQSHLSMEERVKTNYDHPSALDHDLLCQHLQMLARGEAVEVPEYSYTEHTRTEQTTTMTPKKVIILEGILLLTDPRLRDLMHATVFMDTPLDICLLRRVKRDVQERGRTMESVLKQYQETVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLKS | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 24228
Sequence Length: 213
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
P09703 | MTTSTNNQTLTQVSNMTNHTLNSTEIYQLFEYTRLGVWLMCIVGTFLNVLVITTILYYRRKKKSPSDTYICNLAVADLLIVVGLPFFLEYAKHHPKLSREVVCSGLNACFYICLFAGVCFLINLSMDRYCVIVWGVELNRVRNNKRATCWVVIFWILAVLMGMPHYLMYSHTNNECVGEFANETSGWFPVFLNTKVNICGYLAPIALMAYTYNRMVRFIINYVGKWHMQTLHVLLVVVVSFASFWFPFNLALFLESIRLLAGVYNDTLQNVIIFCLYVGQFLAYVRACLNPGIYILVGTQMRKDMWTTLRVFACCCVKQE... | Function: Interacts with the host Gi complex without activating it, thereby probably interfering with the chemokine-Gi signaling . May also function as a G protein sink to sequester G protein from the cell surface via internalization . Plays an important role in spread of HCMV via the extracellular route.
Location Topo... |
P69332 | MTPTTTTAELTTEFDYDEDATPCVFTDVLNQSKPVTLFLYGVVFLFGSIGNFLVIFTITWRRRIQCSGDVYFINLAAADLLFVCTLPLWMQYLLDHNSLASVPCTLLTACFYVAMFASLCFITEIALDRYYAIVYMRYRPVKQACLFSIFWWIFAVIIAIPHFMVVTKKDNQCMTDYDYLEVSYPIILNVELMLGAFVIPLSVISYCYYRISRIVAVSQSRHKGRIVRVLIAVVLVFIIFWLPYHLTLFVDTLKLLKWISSSCEFERSLKRALILTESLAFCHCCLNPLLYVFVGTKFRQELHCLLAEFRQRLFSRDVSW... | Function: Binds to a great number of different CC-chemokines including CCL5/RANTES, CCL2/MCP-1, CCL3/MIP-1-alpha as well as CX3CL1/Fractalkine . Transduces signals resulting in the activation of MAP kinase signaling pathways and augmentation of intracellular calcium ion levels, leading to alterations in chemotactic beh... |
O14053 | MPFAEKKRRTYENAVKPLRKSRIYAPFRSIGHVSNAVPFDIEARGTHFLVTTSVGNTFQTYDCEKLNLLFVGKQLDKEITCLKSFKDFMLVAAGSKIFAYKRGKIIWDIDVEQEHGTVTHLDAFGEWIIACTSSRHVYVWKHASKYSVPELHTTFLPNTNADITSLLHPSTYLNKILLGFSDGALQIWNLRVSKRVHEFQEFFGDGITSLTQAPVLDVLAVGTISGRIVIFNLKNGSILMEFKQDGQVLSCSFRTDGTPILASSNPIGDLSFWDLSKRRIQNVTYNAHFGSLPKIQFLNGQPILVTAGPDNSLKEWIFDS... | Function: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Sequence Mass (Da): 100570
Sequence Length: 902
Domain: The WD repeats are grouped into two tandem seven-bladed beta-propeller regions.
Subcellular Location: Nucleus
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Q06078 | MSIDLKKRKVEEDVRSRGKNSKIFSPFRIIGNVSNGVPFATGTLGSTFYIVTCVGKTFQIYDANTLHLLFVSEKETPSSIVALSAHFHYVYAAYENKVGIYKRGIEEHLLELETDANVEHLCIFGDYLCASTDDNSIFIYKKSDPQDKYPSEFYTKLTVTEIQGGEIVSLQHLATYLNKLTVVTKSNVLLFNVRTGKLVFTSNEFPDQITTAEPAPVLDIIALGTVTGEVIMFNMRKGKRIRTIKIPQSRISSLSFRTDGSSHLSVGTSSGDLIFYDLDRRSRIHVLKNIHRESYGGVTQATFLNGQPIIVTSGGDNSLK... | Function: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Sequence Mass (Da): 104791
Sequence Length: 939
Domain: The WD repeats are grouped into two tandem seven-bladed beta-propeller regions.
Subcellular Location: Nucleus
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B7KC96 | MNLFHLQAPFQATGDQPQAIAQLVNSIEKGNRFQTLLGATGTGKTFTIAATIEKIGKPTLVLAHNKTLAAQLCNELRQFFPENAVEYFISYYDYYQPEAYIPVSDTYIEKSASINDEIDMLRHSATRSLFERRDVVVVASISCIYGLGMPSEYLKASIGLEVGKEINQRQLLRDLVSVQYSRNDLDLQRGRFRLRGDVLELVPAYEDRVIRVEFFGDEIDAIRYLDPVTGNSLQSLERVNIYPARHFVTPDDQLEAACQGIELELEDRLEELEKQGKLLEAQRLGQRTRYDLELLREVGYCNGVENYSRYLAGREPGQPP... | 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... |
Q9HMT9 | MSDASGPLQPDRPEADVPFRVEAPFDPAGDQPDAIAELVAGYEQGAQQQTLLGVTGSGKTNTVSWVVEELQQPTLVIAHNKTLAAQLYEEFRSLFPDNAVEYFVSYYNYYQPEAYVEQTDKYIEKDASINDEIDRLRHSATRSLLTRDDVIVVASVSAIYGLGDPRNYEEMSLRVERGQSIGRDQLLAKLVDLNYDRNDVDFTQGTFRVRGDTVEVYPMYGRYPVRVEFWGDEIDRMAKLDPLEGTVESEEPAVLFHPAEHYSVPDAEMEQAIERIRTDMHERVRHFERTGDMVAAQRIEERTTFDLEMMAEAGYCSGIE... | 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... |
P94846 | MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNET... | 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... |
Q31ES7 | MAKKFEIVSQYEPAGDQPVAITQLVEGLEDGEAFQTLLGVTGSGKTFTMANVIAKVQRPTIILAHNKTLAAQLYGEMKSFFPHNAVEYFVSYYDYYQPEAYVPASDTYIAKDSSVNEQIEQLRLSATKALMERKDVVLIATVSAIYGLGDPDQYLKMILQLRLGDTISQRDILQQLTTMQYTRNDVELWRGCFRVRGDVIDVFPAEAEEYAVRIELFDDEVDSLAWFDPLTGEVLTRPTRITVYPKSHYVTPKERVLQTIEQVKVELVSRLEELRSLNKLVEAQRLEERTRLDIEMMSELGYCSGIENYSRYLSGRASGE... | 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... |
Q56998 | MTIAIRTTLDEPENHSDFVPHRPSRPEKTEPSKPFRLVSDYEPAGDQPQAISALCKDIQKGERDQVLLGVTGSGKTFTMAKVIEKLQRPSLILAPNKILAAQLYGEFKRFFPENAVEFFVSYYDYYQPEAYVPRTDTYIEKDSAINEAIDRMRHAATRSLLEREDVIIVASVSCLYGIGSVDTYSSMTFRLLKGQLVDQREIIRRLVALQYKRNEVAFGRGSFRVKGDTLEIFPSHYEDMAWRISFFGDEIEEISEFDPLTGVKIAKLDQIKIYANSHYVTPEPTLKAANNAIRRELDNRLREFKAEGKLLEAQRLEERT... | 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... |
Q8ZIC5 | MQTLNRRDFPGRSHPDKIIQFGEGNFLRAFVDWQIDLLNEHTDLNAGIVVIRPIDTDFPPSLSTQDGLYTAVIRGLNEQGEAVRESRLIRSVNREINIYRQFDDYLALARDANIRFMFSNTTEAGIAWNEADQFSDAPPSSFPAKLTRLLFERFEHFDGAADKGWVLLPCELIDYNGEALRELVLRYASHWQLPAAFTHWLTENNTFCSTLVDRIVTGYPRDEVAALQTELGYQDSFLDTAEYFYLFVIQGPQGLAQELRLDQLDLNVRIVDDIKPYKERKVAILNGAHTALVPVAYLSGLDTVGQTMDDAQISRFVEKT... | Catalytic Activity: D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH
Sequence Mass (Da): 54907
Sequence Length: 483
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 1.1.1.58
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A8FHC4 | MKAFLNEQFLLNSPTAEKLYHEFAKDLPIIDYHCHLSPKDIYENKTFRNITEAWLYGDHYKWRAMRANGIPETHVTGDASDYDKFLAWAKTVPMTIGNPLYHWTHLELRRYFEVQDLLNEKNADTIWQKVNEKLQEEGFGARDFIMKSNVETVVTTDDPIDSLQYHQKLREEGFSVQVLPGFRPDKALDIANDLFEKYVHELAEASAISIQSYQDFLNALRARIDFFHEHGCLISDHAINEMTYEETTQEEVETIFHKRMSGYPLTEKEKIKFKTETFIMLGQAYCERGWAMQLHINALRNNNTKMFERLGPDTGYDAMN... | Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Mass (Da): 55773
Sequence Length: 478
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
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O34808 | MEPFMGKNFLLKNETAVSLYHNYAKDMPIIDYHCHLSPKEIYENKTFQNITEAWLYGDHYKWRIMRANGIEETYITGDAPDEEKFMAWAKTVPMAIGNPLYNWTHLELQRFFGIYEILNEKSGSAIWKQTNKLLKGEGFGARDLIVKSNVKVVCTTDDPVDSLEYHLLLKEDKDFPVSVLPGFRPDKGLEINREGFPEWVQALEDAAAISITTYDEFLKALEKRVRFFHSAGGRVSDHAIDTMVFAETTKEEAGRIFSDRLQGTEVSCEDEKKFKTYTLQFLCGLYAELDWAMQFHINALRNTNTKMMKRLGPDTGYDSM... | Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Mass (Da): 54612
Sequence Length: 473
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
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Q8A9J2 | MKNFMDENFLLQTETAQKLYHEHAAKMPIIDYHCHLIPQMVADDYKFKSLTEIWLGGDHYKWRAMRTNGVDERYCTGKDTTDWEKFEKWAETVPYTFRNPLYHWTHLELKTAFGIDKILSPKTAREIYDECNEKLAQPEYSARGMMRRYHVEVVCTTDDPIDSLEYHIQTRESGFEIKMLPTWRPDKAMAVEVPADFRAYVEKLSAVSGVTISNFDDMIAALRKRHDFFAEQGCRLSDHGIEEFYAEDYTDAEIKAIFNKVYGGAELTKEEILKFKSAMLVIFGEMDWEKGWTQQFHYGAIRNNNTKMFKLLGPDTGFDS... | Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Mass (Da): 54317
Sequence Length: 468
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
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Q82ZC9 | MKWGFRWYGAAGDAIPLKHIRQIPGITGVVGTLLNKLPGDVWTVAEIQALKQSVEQEGLALLGIESVAIHDAIKAGTDQRDHYIDNYRQTLRNLGKCGISLVCYSFKPIFGWAKTDLAYENEDGSLSLLFDQAVVENMQPEDMYQLIHSQSKGFRLPGWEEERLQQFQELKAMYAGVTEEDLVENLRYFLERVIPVCEEENIKMGIHPDDPPWEIFGLPRITKNLADLKRILSLVDSPANGITFCTGSLGADPTNDLPTMIREIGHRINFVHFRNVKYLGEHRFEETAHPSVAGSLDMAELMQALVDVGYEGVIRPDHGR... | Function: Catalyzes the dehydration of D-mannonate.
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 40282
Sequence Length: 357
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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O05616 | MFPKNAWYVACTPDEIADKPLGRQICNEKIVFYRGPEGRVAAVEDFCPHRGAPLSLGFVRDGKLICGYHGLEMGCEGKTLAMPGQRVQGFPCIKSYAVEERYGFIWVWPGDRELADPALIHHLEWADNPEWAYGGGLYHIACDYRLMIDNLMDLTHETYVHASSIGQKEIDEAPVSTRVEGDTVITSRYMDNVMAPPFWRAALRGNGLADDVPVDRWQICRFAPPSHVLIEVGVAHAGKGGYDAPAEYKAGSIVVDFITPESDTSIWYFWGMARNFRPQGTELTETIRVGQGKIFAEDLDMLEQQQRNLLAYPERQLLKL... | Cofactor: Binds 1 [2Fe-2S] cluster.
Catalytic Activity: H(+) + NADH + O2 + vanillate = 3,4-dihydroxybenzoate + formaldehyde + H2O + NAD(+)
Sequence Mass (Da): 39491
Sequence Length: 354
Pathway: Xenobiotic degradation; vanillyl-alcohol degradation.
EC: 1.14.13.82
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P29753 | MKKIAVLFGGNSPEYSVSLTSAASVIQAIDPLKYEVMTIGIAPTMDWYWYQGNLANVRNDTWLEDHKNCHQLTFSSQGFILGEKRIVPDVLFPVLHGKYGEDGCIQGLLELMNLPYVGCHVAASALCMNKWLLHQLADTMGIASAPTLLLSRYENDPATIDRFIQDHGFPIFIKPNEAGSSKGITKVTDKTALQSALTTAFAYGSTVLIQKAIAGIEIGCGILGNEQLTIGACDAISLVDGFFDFEEKYQLISATITVPAPLPLALESQIKEQAQLLYRNLGLTGLARIDFFVTNQGAIYLNEINTMPGFTGHSRYPAMM... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Required for low-level resistance to the glycopeptide antibiotic vancomycin. Probable D-alanine--D-alanine ligase of altered specificity. It may synthesize a dipeptide or a depsipeptide which is incorporated into peptidoglycan precursors and not recog... |
Q91ZD4 | MDTESQYSGYSYKSGHSRSSRKHRDRRDRHRSKSRDGSRGDKSVTIQAPGEPLLDNESTRGDERDDNWGETTTVVTGTSEHSISHDDLTRIAKDMEDSVPLDCSRHLGVAAGAILALLSFLTPLAFLLLPPLLWREELEPCGTACEGLFISVAFKLLILLLGSWALFFRRPKASLPRVFVLRALLMVLVFLLVISYWLFYGVRILDARERSYQGVVQFAVSLVDALLFVHYLAVVLLELRQLQPQFTLKVVRSTDGASRFYNVGHLSIQRVAVWILEKYYHDFPVYNPALLNLPKSVLAKKVSGFKVYSLGEENSTNNST... | Function: Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocard... |
P74945 | MTISIYSHTFQSVPQADYVSLLKLRYKVFSQRLQWELKTNRGMETDEYDVPEAHYLYAKEEQGHLVGCWRILPTTSRYMLKDTFSELLGVQQAPKAKEIYELSRFAVDKDHSAQLGGVSNVTLQMFQSLYHHAQQYHINAYVTVTSASVEKLIKRMGIPCERLGDKKVHLLGSTRSVALHIPMNEAYRASVNA | Function: Required for the synthesis of N-(3-oxodecanoyl)-L-homoserine lactone (ODHL), an autoinducer molecule which binds to VanR.
Catalytic Activity: a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine
Sequence Mass (Da): 22127
Sequence Length:... |
Q47744 | MSIRILLVEDDDHICNTVRAFLAEARYEVDACTDGNEAHTKFYENTYQLVILDIMLPGMNGHELLREFRAQNDTPILMMTALSDDENQIRAFDAEADDYVTKPFKMRILLKRVEALLRRSGALAKEFRVGRLTLLPEDFRVLCDGTELPLTRKEFEILLLLVQNKGRTLTHEIILSRIWGYDFDGDGSTVHTHIKNLRAKLPENIIKTIRGVGYRLEESL | Function: Member of the two-component regulatory system VanS/VanR. Activates the transcription of vanH, vanA and vanX in response to vancomycin which results in vancomycin resistance.
PTM: Phosphorylated by VanS.
Sequence Mass (Da): 25336
Sequence Length: 220
Subcellular Location: Cytoplasm
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Q9XGM1 | MAGQNARLNVVPTVTMLGVMKARLVGATRGHALLKKKSDALTVQFRALLKKIVTAKESMGDMMKTSSFALTEVKYVAGDNVKHVVLENVKEATLKVRSRTENIAGVKLPKFDHFSEGETKNDLTGLARGGQQVRACRVAYVKAIEVLVELASLQTSFLTLDEAIKTTNRRVNALENVVKPKLENTISYIKGELDELEREDFFRLKKIQGYKRREVERQAANAKEFAEEMVLEDISMQRGISINAARNFLVGGAEKDSDIIF | Function: Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).
Location Topology: Peripheral membrane protein... |
P39942 | MSGKDRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNRIEHVIIPRIERTLAYIITELDEREREEFYRLKKIQEKKKILKEKSDKDLEQRRAAGEVIEPANLLAEEKDEDLLFE | 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 and in some ... |
P87220 | MSGAGNREQVFPTRMTLGVMKSKLKGAQQGHSLLKRKSEALTKRFRDITQRIDDAKRKMGRVMQTAAFSLAEVQYATGDNISYQVQESVQKARFTVKAKQENVSGVFLPTFDSHINEDVNDFKLTALARGGQQVQKAKLIYSKAVETLVELASLQTAFIILDEVIKITNRRVNAIEHVIIPRTENTIAYINGELDEMDREEFYRLKKVQEKKQEAAAAAEQEEALAKAKAEGATDELAIQQDVEALDIKADKEEVDILQEKEDDVIF | 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... |
Q01278 | MSQVHALSDDQVGQELRKMTAFIKQEAEEKAREIQIKADEEFAIEKSKLVRQETDAIDSAYAKKFKQAQMSQQITRSTMANKTRLRVLGARQELLDEIFEAASAQLGQATHDLGRYKDILRDLILEGFYAMNEPELVIRARQADYDAVREAAGWASAQYKHKTDKDVKATIDAENPVPEGSAGGIIIVGGNGKIDIDNTFEARLTLLKDSALPAMRKALFGENPNRKFFD | 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... |
P23956 | MSEAKNGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEMIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDGISLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK | Function: Proton-conducting pore forming subunit of the V0 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 intracel... |
Q43362 | MSDLCPPTAPFFGFMGAAVALIFANLGAAYGTAKSGVGVSSMGVMKPDLVMKSIIPVVMAGVLGIYGLIIAVIIGNGVKGPEGGKPQYSSFTGFAHLAAGLACGLSGMAAGIAIGIVGDAGVRASAQQAKLYVGMVLILIFAEALGLYGLIVGLILTSKEAPCS | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16252
Sequence Length: 164
Subcellular Location:... |
P54642 | MFQLLSFLLSGEATAVERIITDACPVYAPFFGAMGVTAALVFTVMGAAYGTAKASVGISNMGVMKPDLVIKAFIPVIFAGVIAIYGLIICVILVGGIKPNANYTLMKSFTDLGAGLTVGLCGLAAGMAIGIVGDSGVRAFGQQPKLYVIMMLILIFSEALGLYGLIIGILLSSVSDTYCPGQALVPLNSGNVIGKN | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20149
Sequence Length: 196
Subcellular Location:... |
P23380 | MSSEVSSDNPIYGPFFGVMGAASAIIFSALGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGALEEPSKYSLYRGFIHLGAGLAVGFSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVAIYLYTK | Function: Proton-conducting pore forming subunit of the V0 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... |
Q24808 | MSVLLRSVTELCPVYSPFFGSMGITASIVFTVFGGAYGTAKSSVGISSVGVMKPEFIMRSLFPVVFAGVIGLYGLIVCIVLFINVNKSEYSLNRAFLDLGAGLTCGLCGLASGMSIGISGDCGVRGAAQQPKLFVSMLICLIFSEALALYGFIVALIMAATGDNSCVATASTSSSS | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18103
Sequence Length: 176
Subcellular Location:... |
Q43434 | MSSTFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16659
Sequence Length: 165
Subcellular Location:... |
P27449 | MSESKSGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEQIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDDISLYKSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK | Function: Proton-conducting pore forming subunit of the V0 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 intracel... |
Q41773 | VPVVMAGVLGIYGLIIAVIISTGINPKAKPYYLFDGYAHLSSGLACGLAGLAAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAD | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11043
Sequence Length: 109
Subcellular Location:... |
P63082 | MADIKNNPEYSSFFGVMGASSAMVFSAMGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDGITLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK | Function: Proton-conducting pore forming subunit of the V0 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... |
B2D0J4 | MEVLVQLALLLVVHGSLVVLVAGKSVPRVIDQDLERYEPLEEEDHRGARVPFNLEETYDQSFRANSFNGTWKTDREILYSDNYVGDIRLFDVTTGSGTVLLDSSVTADFDKASVMFSFDNSHVAIGHDYVNGFRYSIHQKCTVYNIKSRTFTDIANGDRIPLFKWSPTRNALIYVHKNDIYYQVFFEGGSDTRRITNTGVPDIVFNGIPDWVYEEEVLGSPVAFWISPDGRHLAFATFNDTNVRDIVISKYGSPGNSRDQYPNEIRIKYPKAGTTNPFVSLSVIDLHDPSSKLIDLPPPVDVVGADNVLYTANWRRDGEI... | Function: Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process promelittin into its active form and/or modulate the chemotactic activity of immune cells after the insect sting.
Catalytic... |
Q07943 | MTNSLLICFTILGLAASSPTKPIGDIRIVGGEDIVITEAPYQVSVMFRGAHSCGGTLVAADIVVTAAHCVMSFAPEDYRIRVGSSFHQRDGMLYDVGDLAWHPDFNFASMDNDIAILWLPKPVMFGDTVEAIEMVETNSEIPDGDITIVTGWGHMEEGGGNPSVLQRVIVPKINEAACAEAYSPIYAITPRMLCAGTPEGGKDACQGDSGGPLVHKKKLAGIVSWGLGCARPEYPGVYTKVSALREWVDENITNLRLKHILRRF | Function: Responsible for the degradation of vitellin in eggs at the head pigmentation stage.
PTM: Cleavage after Arg-27 leads to beta-VTN protease and subsequent cleavage after Arg-89 leads to alpha-VTN.
Sequence Mass (Da): 28521
Sequence Length: 264
EC: 3.4.21.-
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P11473 | MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGL... | Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells . Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR . The VDR-RXR heterodimers bind to specific response elements on DNA and activate the tran... |
P48281 | MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMIMKRKEEEALKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPIRADVSTGSYSPRPTLSFSGDSSSNSDLYTPSLDMMEPASFSTMDLNEEGSDDPSVTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTLDDMSWDCGSQDYKYDITDVSRAGHTLELIEPLIKFQVGLKKLNL... | Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (By similarity). The VDR-RXR heterodimers bind to specific response element... |
P13053 | MEATAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMIMKRKEEEALKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSYSPRPTLSFSGNSSSSSSDLYTTSLDMMEPSGFSNLDLNGEDSDDPSVTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLN... | Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells . Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (By similarity). The VDR-RXR heterodimers bind to specific response elements on DNA and ac... |
O13124 | MEFMAATTSIADTDMEFDKNVPRICGVCGDKATGFHFNAMTCEGCKGFFRRSMKRKAMFTCPFNGDCRITKDNRRHCQSCRLKRCVDIGMMKEFILTDEEVQRKRQMINKRKSEEALKESMRPKISDEQQKMIDILLEAHRKTFDTTYSDFNKFRPPVRENVDPFRRITRSSSVHTQGSPSEDSDVFTSSPDSSEHGFFSASLFGQFEYSSMGGKSGELSMLPHIADLVSYSIQKIIGFAKMIPGFRDLIAEDQIALLKSSVIEVIMLRSNQSFSLDDMSWTCGSEDFKYKVDDVTQAGHNMELLEPLVKFQVGLKKLDL... | Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transc... |
A0A443HK79 | MPAYLLLLACNVLLVLGAHVQRELVLTWEEGAPNGQSRQMIKTNGQFPSPTLIFDEGDDVEIVVRNYMHENTTIHWHGILMQDTPWSDGVPGLSQKPIEPGESYVYRFTAYPPGQYWYHSHSRATLLDGLYGALFIRRKPGTAGPWAMISEDPEDIAAMERASNNPHIMMLSDWDYYNSTQYKEADANSRLQIFCVDSILLNGKGSVYCPGHQWLIDKQIPFMHKSWPNDTITDKGCFPFVPSTEGPWLADGNVSAIPPGLQEGCVPYSGPTEAIEVDPADRWASVNWIGGSTFKTLQPTIDEHEMWIYEVDGHYIEPRR... | Function: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity . The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units t... |
A0A443HJY8 | MAEEIKLTPLETFAQAISASAKTIATYCRDSGHPQLSDDNSSGLTGDVLPPSAPQAVTAARQTILEASYRLQQLVTEPSQYLPRLTVYPQHLAALRWLCHFRIPELIPVQGTRTYYELATEAKVPLHQLQSIARMAITGSFLREPEPNIVAHSRTSAHFVENPSLRDWTLFLAEDTAPMAMKLVEATEKWGDTRSKTETAFNLALGTDLAFFKYLSSNPQFTQKFSGYMKNVTASEGTSIKHLVNGFDWASLGNAIVVDVGGSTGHASIALAESFPDLKFIVQDLPMVTSTSKDNREKTPLPETVASRISFESHDFFKPQ... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity . The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units t... |
Q07853 | MTDRAPHYGLLGLLQTPTQPPKDNPPKLPEKQRRRGRDTTRNRRLFASDGPTDEEGPEVPEIPPSDEEKENRPEPLPVVENGWHSFLRETLEHQLGRLQREVNQDFEDLYRRLGIHP | 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.... |
P06459 | MADDSALHKKYPFLNLLHTPPHRPPPLCPQAPRKTQCKRRLGNEHEESNSPLATPCVWPTLDPWTVETTTSSLTITTSTKDGTTVTVQLRL | Function: Associates with keratin intermediate filaments in certain epithelial cells in culture.
PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability.
Sequence Mass (Da): 10173
Sequence Length: 91
Subcellular Location: Host cytoplasm
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P0CK45 | MPNLWFLLFLGLVAAMQLLLLLFLLLFFLVYWDHFECSCTGLPF | Function: E5 can induce cellular DNA synthesis. It seems to interact with a 16 kDa cellular protein. E5 seems to activate the PDGF receptor.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 5210
Sequence Length: 44
Subcellular Location: Host membrane
|
P15692 | MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQE... | Function: Participates in the induction of key genes involved in the response to hypoxia and in the induction of angiogenesis such as HIF1A . Involved in protecting cells from hypoxia-mediated cell death (By similarity).
PTM: Produced by use of an alternative upstream CUG codon and post-translationally processed into t... |
Q00731 | MTDRQTDTAPSPSAHLLAGGLPTVDAAASREEPKPAPGGGVEGVGARGIARKLFVQLLGSSRSVVAVVCAAGDKPIGAGRSASSGLEKPGPEKRGEEEKEEERGPQWALGSQEPSSWTGEAAVCADSAPAARAPQAPARASVPEGRGARQGAQESGLPRSPSRRGSASRAGPGRASETMNFLLSWVHWTLALLLYLHHAKWSQAAPTTEGEQKSHEVIKFMDVYQRSYCRPIETLVDIFQEYPDEIEYIFKPSCVPLMRCAGCCNDEALECVPTSESNITMQIMRIKPHQSQHIGEMSFLQHSRCECRPKKDRTKPEKKS... | Function: Participates in the induction of key genes involved in the response to hypoxia and in the induction of angiogenesis such as HIF1A . Involved in protecting cells from hypoxia-mediated cell death .
PTM: Produced by use of an alternative upstream CUG codon and post-translationally processed into the N-terminal N... |
Q9XS49 | MSPLLRRLLLAVLLQLAPAQAPVSQPDAPGHQKKVVSWIDVYARATCQPREVVVPLNMELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIQYPSSQLGEMSLEEHSQCECRPKKRESAVKPDRASTPHHRPQPRSVPGWDPAPGAPSPADITHPTPAPGPSAHAAPSAASALTPGPATAAADAAASSVVKGGA | Function: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis (By similarity).
PTM: VEGF-B186 is O-glycosylated.
Sequence Mass (Da): 21655
Sequence Length: 207
Subcellular Location: Secreted
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P49765 | MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA | Function: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.
PTM: VEGF-B186 is O-glycosylated.
Sequence Mass (Da): 21602
Sequence Length: 207
Subcellular Location: Secreted
|
P49767 | MHLLGFFSVACSLLAAALLPGPREAPAAAAAFESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYKCQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPTNYMWNNHICRCLAQEDFMFSSDAGDDSTDGFHDICGPNKELDEETCQCVCRAGLRPASCGPHKELDRNSCQCVCK... | Function: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentia... |
P97953 | MHLLCFLSLACSLLAAALIPSPREAPATVAAFESGLGFSEAEPDGGEVKAFEGKDLEEQLRSVSSVDELMSVLYPDYWKMYKCQLRKGGWQQPTLNTRTGDSVKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPTNYVWNNYMCRCLAQQDFIFYSNVEDDSTNGFHDVCGPNKELDEDTCQCVCKGGLRPSSCGPHKELDRDSCQCVCKNKLF... | Function: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentia... |
O13880 | MASEWPETSRASSVEENPKLNIPEIVESVSDSKPSLKNQFSTTVIDSSDLNVFNDGAETTVKEQEFTSSELRRLQKLRLKMDLRIIPCLWILYFLSCCLRFTVSLSFTMNTAQGHSLIQTLSGYSAHYLALGLALFYVGYIIFEVPSNLMMAFIEPRIWVSRIQLTIGVVGACHAVLGTKHGNAQSYVALRFFLGVAESGLWPGLAYYMSRWYRGKHLGKRIGWYYTAAQIAAAAVSLVSAGFQKMDGARGLYGYQWMFLIWGVVAIAQALSIPWWLPAVASKEHRKSLSSFIPLPKWMKTLSPQRIGFLTPADKSLHSR... | Function: Involved in uptake of biotin and desthiobiotin with the concomitant entry of protons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62822
Sequence Length: 568
Subcellular Location: Membrane
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