ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6FLR5 | MSPDPKYSAYLLDIEGTLCPLSFVKDTLYPFFVLHVQRIVYENFNEEHPKDEFIAEQLAKYDIKEEGQAGKNKLVEHLLDLVANDTKDSTLKALQGHVWEVGYNSGELEVPLYPDVIDFLVRNDGRGDDKVPVYIYSSGSIHAQKLLFGHVKNSGNSHAKIAGNWDLNRFIDGYFDINTAGKKTESNSYKKILDEIKMTDKPHDVLFLSDNAKELDAAKECGISVGLAMRAGNVTVPNAIDYKQYFQFTKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q2H683 | MAAAKKPRVVLLDIEGTVCPISFVKDVLFPYALSALPSTLAQEWDAPAFARYRAAFPAEHASTPSALAAHARDLMARDVKIGYLKALQGYLWEAGYASGALRAPLFEDVAPKVREWTSAAGEEGGVARVMIYSSGSVPAQKLLFRHTSGEPADLTDAITDYFDTVNAGPKTEPASYERIAAKYPEVPAGEWLFLSDNVREVEAAREAGMRACVVQRPGNAELPEDVRGRLEVVESFEEL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
C4Y3W1 | MSIALLDIEGTVCPITFVKDCLFPYFSKQYPSYLRDVSFPIDKSDGGLADVLAGFPKEAVASIDQLKNHIDDLVARDVKDPVLKSFQGLVWKEGYAKGDLKAPVYEDAIAFINRSKSVYIYSSGSVGAQKLLFSHVDVNGASVDLTPKLKGYFDITTAGFKQEKDSYLKIAADIGCDPADVIFYSDNVLEVKAALEAGMASKVVVRPGNAELSESDKKSYECISSFTAE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
B0WQG0 | MRYQQDTLFPYALKNVEEYLKANWNEDATKTVVAALREQADEDKKAEVEGALTIPAGDSEDIIPDIVKYVEWQTSRDAKTGSLKTLQGLVWAKGYKDGSIKGHVYDDVSKALEQWTEGGRKIYVYSSGSVDAQKMLFEHSEQGDLVKYLAGHYDTKIGAKTEKDSYEAILKNIEATAEEALFLTDVVAEAKAAKEAGLNVVVLERPGNAELSEDDRKEFTVVKSFADIPLESIVESANGAGAKRKIDEAQEEDEAQPPTKVVKKDENGDAAAKKDETAKVDEPAAKATNGDAAAKEEAAAPAEGKMEVDEAAAAAAPPAD... | Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
... |
Q55FM6 | MTPNIHTVILDIEGTTTPISFVHDVLFPYIRDNLVRHINQKWGSEELKQDIKELYKLYLEDNKASELVVNNQFNTPEILNPDDESTDKEKLIESVIRNVIYQMDNDRKSTPLKQLQGHMWLEGYENELVKGVVFPEVPKAFENWNLNHIDIYIYSSGSIAAQKLLFNYSNFGSLLPYIKGHFDTTIGGKLHPSSYEKILSTINNGSPNSYLFVTDSILEAKAARESGLNVCLSIRDGNPPIVDRELLNTFDQVSSFDQLFNKFNFKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
O29133 | MIIEDVHYRVVFDSRGNETVECEVVAGEVVAKAMAPSGASTGSGEAVVVSPYRYEEIEEEVSKAIIGMSVFDQESVDEALRELDGTDNFSRIGGNFAITASLAVAKAAAEILGLPLYAYVGGVFAKELPYPLGNVIGGGRHAEGSTSIQEFLVIPVGAKTFFEAQRANAAVHKQLKKIFKERGIFAAKGDEGAWAAQISDEQAFEILSEAIQRVEDELGVKVRMGIDVAATELWDGERYVYSDRKLTTEEQIAYMAELADRYDLLYIEDPLHEKDFEGFAELTKQVKCMVCGDDIFVTNPEIIKKGIEVGAANTVLIKPN... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 43420
Sequence Length: 399
Pathway: Carbohydrate degradation; gly... |
Q96X30 | MPISKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEAHELRDGDKTQWGGKGVLKAVKNVNETIGPALIKENIDVKDQSKVDEFLNKLDGTANKSNLGANAILGVSLAVAKAGAAEKGVPLYAHISDLAGTKKPYVLPVPFQNVLNGGSHAGGRLAFQEFMIVPDSAPSFSEALRQGAEVYQKLKALAKKKYGQSAGNVGDEGGVAPDIQTAEEALDLITEAIEQAGYTGKIKIAMDVASSEFYKADVKKYDLDFKNPESDPSKWLTYEQLADLYKSLAAKYPIVSIEDPFAEDDWEAWSYFYKTSDFQIV... | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 47305
Sequence Length: 438
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cyto... |
O02654 | MVIKKVHSRQIFDSRGNPTVEVDLWTDKGMFRAAVPSGASTGIYEALEMRDKDAKNYHGKTLFNAVGNVNKIIAPALVDKKMDEKDQTAVDNFLLALDGTENKNKLGANAILGVSLAVCKAGAAAKGVPLYRHIADLAGNKEVILPVPAFNVINGGSHAGNKLAMQEFMILPTGAKNFTEAMKMGTEVYHHLKSVIKKKYGQDACNVGDEGGFAPNILDNKEGLELLKTAIANAGYTAEIEIGMDVAASEFCKEKKYDLDFKNPDSNPNDWLTSDQLADVYKDFVKNYPVVSIEDPFDQDDWEAYTKMTKDMDIQIVGDD... | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 47426
Sequence Length: 434
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cyto... |
P15007 | MSWTASVFLRTSTTSMKFLRLRWPLPRIPQNKSANVAPRFRSKSAVSQLSSGFKFVQIRKSTCDSNEMTIKAIKARQIYDSRGNPTVEVDLTTELGLFRAAVPSGASTGVHEALELRDNDKANYHGKSVLKAVGHVNDTLGPELIKANLDVVDQASIDNFMIKLDGTENKSKFGANAILGVSLAVAKAGAAKKGVPLYKHIADLAGNKEIILPVPAFNVINGGSHAGNKLAMQEFMILPTGATSFTEAMKMGSEVYHHLKNVIKAKFGLDATAVGDEGGFAPNIQSNKEALNLISDAIAKAGYTGKIEIGMDVAASEFYK... | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 54310
Sequence Length: 500
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cyto... |
Q9CD42 | MPVIEQVGAREILDSRGNPTVEVEVVLIDGTFARAAVPSGASTGEYEAVELRDGDGRYGGKGVKRAVDAVLDEIGPVVIGLNANDQRLIDQELLDLDGTPDKSRLGGNAILGVSLAVAKAAADSAELPLFRYIGGSNAHILPVPMMNILNGGAHADTAVDVQEFMVAPIGAPSFVEALRWGAEVYHALKSVLKKKGLSTGLGDEGGFAPEVAGTTAALDLVTLAIEAAGFKPGADVALALDAAATEFYTDGIGYHFEGMTHTADQMTEFYADLLGSYPLVSIEDPLSEDDWDGWAALTASIGEQVQIVGDDIFATNPERL... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45202
Sequence Length: 429
Pathway: Carbohydrate degradation; gly... |
P75189 | MSAQTGTDLFKIADLFAYQVFDSRGFPTVACVVKLASGHTGEAMVPSGASTGEKEAIELRDGDPKAYFGKGVSQAVQNVNQTIAPKLIGLNATDQAAIDALMIQLDGTPNKAKLGANAILAVSLAVAKAAASAQKTSLFKYLANQVMGLNKTEFILTVPMLNVINGGAHADNNIDFQEFMIMPLGANSMHQALKMASETFHALQKLLKQRGLNTNKGDEGGFAPNLKLAEEALDLMVEAIKAAGYQPGSDIAIALDVAASEFYDDTTKRYVFKKGIKAKILDEKEWSLTTAQMIAYLKKLTEQYPIISIEDGLSEHDWEG... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 49228
Sequence Length: 456
Pathway: Carbohydrate degradation; gly... |
Q98Q50 | MSEIVKIKALEVLDSRGNPTIQVEVHTISGAYGKALVPSGASTGSREALELRDESTKYKDNWYASKGVQKAVDNVNNKIADLLIGQNVLDQRNIDNIMIEADGTENKSKFGANAILGVSLAAAHAGANFLQIPLYRYIGGINANMLPLPMLNVINGGEHASNTIDFQEFMIMPMGAKTFKESLQMANKVFHNLAKLLKKAGHGTQVGDEGGFAPNLKNHEEVLDFLMQAIEVAGFVASTSKEKGIAIAIDAASSELYDQSTGKYTFKKLKQAIKTKQPGFENVEKTKLDFTSDELIAYYGELISKYPIISIEDGFAESDW... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 49878
Sequence Length: 456
Pathway: Carbohydrate degradation; gly... |
Q566N0 | MQISAYLCALIACCGLTLSAPTANNKSSSEAPPLLLVSFDGFRADYLNKYSFPNLEKFFSDGVLVHELTNVFTTKTFPNHYSLVTGLYAESHGMLASIMYDPVAKKHFSIKNDSDPFWWDEATPIWVSVEESGYHAASAMWPGSDVNIQNHTLKYTFKYDSRVSFKERLGNITQWMTTDKSLKFASLYWEEPDFSGHTYGPDNTTEMARVLKEVDGHVGYLMEELDRMELWGKINVIITSDHGMAQCSEERIIRLDDCVSPSSYTLVDLTPVAAIIPLEDKTTVYNNLSSCHVHLKAYMKNDVPDRLHYKNNERIQPIIL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thro... |
Q9Y6X5 | MKLLVILLFSGLITGFRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSNPPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADE... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thro... |
Q9EQG7 | MIPEFLLASCTLATLCHSAPFSLQPEEQKVLVVSFDGFRWDYLYKVPTPHFHYIMKNGVHVNQVTNVFITKTYPNHYTLVTGLFAENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPGADVKIHDSFPTYYLPYNESVSFEDRVAKIIEWFTAKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHGMTQCSKQRVIELDRYLDKEHYTLIDHSPVAAILPKEGKFDEVYDALAGAHPNLTVYKKEEIPERWHYKHNDRVQPIVAVA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates . Lacks lysopholipase D activity. May play a role in neuronal cell communication (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54387
Se... |
F1N5C8 | MAGKLGVLLLALVLSLAQPASARRKLLVFLLDGFRADYISDEALESLPGFKEIVSRGVKVDYLTPDFPTLSYPNYYSLMTGRHCEVHQMTGNYMWDPDTNKSFDLGINRDSRLPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKSVPTDINFVNAVSGALDVFKSGQADLAAIYYERVDVEGHHYGPSSPQRKDAVKAVDTVMAYMTKWIQERDLQDDLNVIIFSDHGMTDISWTDKVIKLDNYINLRDLQQLKGRGPVVSLWPAPGKHSEIYNKVRRVEHMTVYAKEDIPSRFYYKKGKFVSPLT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty ac... |
Q5BKW7 | MTRTLLKIYTLFILLLCRQRDANRKLLVFLIDGFRHDYMDDLHNLPGFREIVENGVKVDYLTPDFPSLSYPNYYSLMTGRHCEVHQMTGNYMWDTDTQKEFLIGTNPDSRLPMWWDGSEPLWVTMQKLGKKVYMYYWPGCEVTILGVRPTFCEEYVYNPSEKNLTDSMENALNALKSSKADMAGIYYEKIDVEGHHFGPRSPEIQRAIRSLDQAFQILNQKIREKNMRDTINVVLFSDHGMTQLKWMEKIIELDNYINMSHIIKMMDRGPVVSLWPKQDKFEEIYQNLSTADNMNVYKKHEIPDRFHYKNGQFVSTLTLV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty aci... |
Q6UWR7 | MAVKLGTLLLALALGLAQPASARRKLLVFLLDGFRSDYISDEALESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSFDIGVNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSFKSGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIFWMDKVIELNKYISLNDLQQVKDRGPVVSLWPAPGKHSEIYNKLSTVEHMTVYEKEAIPSRFYYKKGKFVSPLT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty ac... |
Q8BGN3 | MAAKLWTFLLGFGLSWVWPASAHRKLLVLLLDGFRSDYISEDALASLPGFREIVNRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPRTNKSFDIGVNRDSLMPLWWNGSEPLWITLMKARRKVYMYYWPGCEVEILGVRPTYCLEYKTVPTDINFANAVSDALDSLKSGRADLAAIYHERIDVEGHHYGPSSPQRKDALRAVDTVLKYMIQWIQDRGLQQDLNVILFSDHGMTDIFWMDKVIELSNYISLDDLQQVKDRGPVVSLWPVPGKHSEIYHKLRTVEHMTVYEKESIPNRFYYKKGKFVSPLT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty ac... |
Q6DDP3 | MAKYSTLSLILLTLSLLPPSSARPKLLLFLIDGFRFDYISDGELQHLPGFRHMVERGVKVDYMTPAFPSLSYPNYYTLMTGRHCETHHMTGNFMWDPKKNISFDIGANEDSRLPQWWDGAEPLWVTMEKAKRKVSMYYWPGCEVEIRAIKPNYCREYFYYPSEAEFGKSVTDALQSLTRGNAEMAAVYYERIDVEGHHHGPWSEERKNVTRELDQILWHLHQQIREMGLESELNVILFSDHGMTDVFWMDKVIELKNYIDMQDIIQMKDRGPVVSLWPAEGKLSKVYEELRAVQHMNVYQKEDIPERFHYKKGTFVSPLT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiester phosphodiesterase. Has a lysophospholipase C activity (By similarity).
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 51486
Sequence ... |
Q6UWV6 | MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFH... | Function: Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract . Has also phospholipase C activity and can also cleave phosphocholi... |
Q03137 | MAGIFYFILFSFLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEASQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRESQFGKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEEQNGECQACKIGYYKALSTDASCAKCPPHSYSVWEGATSCTCDRGFFRADNDA... | Function: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ... |
P54755 | MGLRGGGGRAGGPAPGWTCLLLCAALRSLLASPGSEVNLLDSRTVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGRPASSFELKFTLRDCNSLPGGLGTCKETFNMYYFESDDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDVGACIALVSVRVYYKKCPSVIRNLARFPDTITGADSSQLLEVSGVCVNHSVTDEAPKMHCSAEGEWLVPIGKCLCKAGYEEKNNTCQVCRPGFFKASPHSPSCSKCPPHSYTLDEASTSCLCEEHYFR... | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... |
Q60629 | MRGSGPRGAGHRRTQGRGGGDDTPRVPASLAGCYSAPLKGPLWTCLLLCAALRTLLASPSNEVNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDENGRSIKENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAIFPDTITGADSSQLLEVSGSCVNHSVTDDPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQAPSPVTNVKKGKIAK... | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... |
Q61772 | MVVQTRFPSWIILCYIWLLGFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIVENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAP... | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... |
O09127 | MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPP... | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... |
Q5JZY3 | METCAGPHPLRLFLCRMQLCLALLLGPWRPGTAEEVILLDSKASQAELGWTALPSNGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSSIPGAAGTCKETFNVYYLETEADLGRGRPRLGGSRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRRGFHLAFQDVGACVALVSVRVYYKQCRATVRGLATFPATAAESAFSTLVEVAGTCVAHSEGEPGSPPRMHCGADGEWLVPVGRCSCSAGFQERGDFCEACPPGFYKVSPRRPLCSPCPEHSRALENASTFCVCQD... | Function: Receptor for members of the ephrin-A family. Binds to EFNA3, EFNA4 and EFNA5.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 109716
Sequence Length: 1008
Domain: The protein kinase domain is ... |
I6YGS0 | MGAPTERLVDTNGVRLRVVEAGEPGAPVVILAHGFPELAYSWRHQIPALADAGYHVLAPDQRGYGGSSRPEAIEAYDIHRLTADLVGLLDDVGAERAVWVGHDWGAVVVWNAPLLHADRVAAVAALSVPALPRAQVPPTQAFRSRFGENFFYILYFQEPGIADAELNGDPARTMRRMIGGLRPPGDQSAAMRMLAPGPDGFIDRLPEPAGLPAWISQEELDHYIGEFTRTGFTGGLNWYRNFDRNWETTADLAGKTISVPSLFIAGTADPVLTFTRTDRAAEVISGPYREVLIDGAGHWLQQERPGEVTAALLEFLTGLE... | Function: Could be involved in detoxification of extraneous host-cell epoxides. Catalyzes the hydrolysis of epoxide-containing substrates.
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 35097
Sequence Length: 322
EC: 3.3.2.10
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P54762 | MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACT... | Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway dow... |
B0XMC1 | MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADA... | Function: Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA . Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis . Plays an important role in growth, morphogenesis and maintaining mitochondrial function including ... |
B0YA65 | MSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKPSDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAIILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMKDGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLFDEEIAPIQLPGFRGKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAPNSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPALAIPKALKHAGVGQDAIDAFE... | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Probable). In this module, the cytosolic acetyl-CoA ac... |
I1RY81 | MANLPPVYIVSTARTPIGSFLGSLSSQTAVQLGSVAIKGAVERAGIKPEDVDEVFFGNVLSAGVGQGPARQCALGAGLPQTVIATTVNKVCASSLKAIILGAQNIMLGTSDIVVAGGTESMSNTPHYLPNLRNGAKYGDQTLVDGVLKDGLTDSFKKDHMGISAELCVDDHDLTREAQDEYAINSYKKAQAATEAGLFTEIVPVEIPGGRGKPAIKVERDDEVKNLNVDKLKAMRPAFKPDGTVTAPNAAPINDGAAAVVLVSEAKLKELNLKPVAKILGWGDAEREPERFTIAPALAIPKAIKHAGLTAEQVEYYEINE... | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG10B catalyzes the formation of aceto... |
Q4WXT8 | MSARPQNVGIKAIEVYFPSQCVDQAELEKFDGVSEGKYTIGLGQTKMSFCDDREDIYSIALTTCSSLLRKYNIDPKSIGRLEVGTETLLDKSKSVKSVLMQLFAPHGNTNIEGVDTVNACYGGTNAVFNSINWVESSAWDGRDAIVVCGDIALYAKGAARPTGGAGAVAMLIGPDAPIVFEPGLRGSYVTHAYDFFKPDLTSEYPVVDGHFSLKCYTEAVDACYKAYAAREKVLKAKVQNGTNGVENDETKTPLDRFDYVLFHAPTCKLVQKSYGRMLYNDYLANPSHPAFAEVPSELRDLDYEKSFTDKTVEKTFMGLT... | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg13A and erg13B condense acetyl... |
Q4WKA5 | MAPRKDFEDKATVPIQPVPGKRGYEFGGPLGAFVFIFGLSTLIYCLTFLCNDVSGCPVPSLLNPSTLSLDKLKEEAGWPQEGLKAFFDVRVTVWVLSYYVLSLVLYVFLPGEVVEGTELACKGRLRYKFNALPSAILILGGLALGTYMHGADFVVWTFLWDNYVQIITANLIICVVLAIFVYARSFSIPAPGQPNPELRELAPGGHSGNALYDFFIGRELNPRVQLPIPFVDEASRTIDINVWCEMRPGLLGWIILNLSNIARQYRTYGYITNSIVLSTVFQTFYVLDALYMEPAVLTTMDVIMDGFGYMLSFGHLVWVP... | Function: Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol . The third module or late pathway invol... |
I1RR90 | MAVKPKQPPAQEQHGYEFFGPPGAFAISFFLPVLVYVFNFVCNDISGCPAPSLLQPKTFSLDALKQEVGWPHNGVAGLVSWNGTLAVIGYNVLSLILYRVLPAIEVEGTQLSSGGRLKYRFNTLYSSTFTLAVLAAGTIAQGAEFPVWTFMSENFIQILSANIIYSYLVSTFVYVRSFSVKHGNKENRELAAGGHSGNILYDWFIGRELNPRIEIPLIGEVDIKEFLELRPGMMGWIIMNCSWCAQQYRNYGFVTDSSILITAVQALYVFDSWWNEPAILTTMDITTDGFGMMLAFGDIVWVPYVYSLQTRYLSVHPVSL... | Function: Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol (By similarity). The third module or lat... |
Q4WBI8 | MDSLNSSYPQSAMATYSDLLDLAAQQQPHLSGLERLWWAHYAYWDNNIVATATGIITFLAHEIIYFSRCLPWIIADSLPSIFLKYKIQDQKPPPSAAEQWACTKYILLIHFVVELPLIVLFHPMMELCGLSFTIPFPDLRTLTAQIIIFFLLEDTYHYWLHRAMHWGPLYRSIHRIHHQYAAPFGLTAEYASPWETLLLGLGTIGPPLLLALMDCNVHLVTVLAWVTLRQFQAIDSHSGYDFPWSLRRILPFWGGADWHDDHHRYFWGNYSSSFRHWDVLMGTVAGPEAREKRRAEREKRQA | Function: Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Erg25A is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol . The third module... |
Q4W9I3 | MNSTLYSTSPGTYWEQYEEVSQHSAHLNVVERLWSAWYAWMQNDVLATGIMSFVMHEIVYFGRSVPWILIDTLGLFKNYKIQNNKIPSLREQWDCAKFVLLSHFTVELPQIWLFHPMAQFFGLSTSVPFPSVWTMMYQIAIFFVLEDTWHYFSHRALHWGPLYKAIHKIHHQYSAPFGMAAEYASPIEVMILGFGTVGCPILWCALTGDLHIFTMYVWIVLRLFQAIDAHSGYEFPWSLHHFLPFWAGADHHDLHHEKFVGNYSSSFRWWDYLLDTEYTPEALKRRREGKLTKKAQ | Function: Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Erg25B is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol . The third module... |
Q8EW66 | MKYGIVSIVGKPNVGKSTLLNNIFEREVVISSNKPQTTRNMIEISYDSIEDCVINFIDTPGLHNPKNKLDLFLNSQVKASLKKSDLVLFLFDLSRDFDSEDEECLKVLKDFNCNNVVLVLNKRDLKSEEEIKNAKQSISKMFDFTNVLEINSKSKEDVSVLLNTIKEHIKEYEGEKKDLELLKKEVSDKFFVSELIREIIINSFRQEIPYGVAILIDEMKYEQDKNLLTIVYSIIVEKESQKPIIIGKGGSMIKKINISLRERLSDIYDCKIFTNSYVKVKKDWRNNETQIKELGYKK | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34509
Sequence Length: ... |
A1U2V4 | MTDITRPENPESRCGFVAIVGRPNVGKSTLLNHILGQKLSITSRKPQTTRHQVLGIKTEGPVQAIYVDTPGMHEDEPRALNRYMNKAAASALIDVDVVVFVVDQLAWTSADEMVLEKLKRVKCPVILAVNKVDKLEKRELLLPHLEALSKKRDFAEIIPLSALKETNLEPLESAVGRFLPESVHFYPDDQITDRSERFMAAEMVREKITRQLGAELPYSVAVEIEEFKHQGNTLHVSALILVEREGQKKIIIGDKGERLRSIGQEARVDMERMFGSKVMLRLWVKVKRGWADSDRALKSLGMSDF | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34418
Sequence Length: ... |
P47627 | MKVLKVGVLGPTNAGKSTLINFLHNDDSLMVSSMNNTTLLSISTEVINQANKNIVFIDVPGFTEKKHSNYELITKEIRKALSGIDVLLLVVRSDQNNKIEFLKTQLQQLKRYQNLTRIFLINKFHQKSLSEVNKAIILEEFKPQKTIEINLLKFDKNLFWSIFKQVELRYNIFRKDINFIDANNDDFKILEGLREQIIFYCKNEIPHIARIEIIEKSFNKEKNLLKIHLVISVPKLSQKKIIIGKNAEMIKAIGIATRKKLLNHFDCDIFIDIFVKTEKQKLPVYSFLSK | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33722
Sequence Length: ... |
Q98QI1 | MKILFSTIIGRPNVGKSTLLNNILEYDLAIVSSKPQATRDQIMGIYSDDDYQLIFTDTPGIYKTKTKFGENLNAQSYESLKDIDLVIFLSPANEEIGPGDEFICEKIKNFTNKIALITKIDLENSEEVLKKKAEKLKSLGFKEIFAISSKDHGSIKKLINEIKKYSYEGERQFDEDMITEKSEKFIAKESIREACIDLLEQELPHSILVEIDSFSEEEREEKNLVEIHSTIYVNKESQKGILIGKGGSKIKKIGISARKKIQRKLGVNVKLFLKIKVKKNWVNQEKIFKKFDN | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33550
Sequence Length: ... |
P18074 | MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVP... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription b... |
O00835 | MSSGDSNLKRRRGGNTGQSSKSYNTWTDYEEDLEESGEFNQSIKKTTNTSSATLTSSEEKGSLLDYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTGFIINKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNSDQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFRNDTVNPNLNIDLKPTTMIRP... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... |
Q02870 | MGPPKKSRKDRSGGDKFGKKRRAEDEAFTQLVDDNDSLDATESEGIPGAASKNAETNDEQINTDEYGAKDYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEYLKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEDFIQGTLDGKAITQFGTKLPPGATDKPTPDPAAAAGADGTTAVPEDITDFYEKIDKEEEDEDEANLKTVSFEVAQEKIEVIQKRCIEIEHPLLAEYDFRNDTNNP... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... |
P19447 | MGKRDRADRDKKKSRKRHYEDEEDDEEDAPGNDPQEAVPSAAGKQVDESGTKVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCIHLEYPLLAEYDFRNDSVNPDINIDLKPTAVLRPYQ... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... |
P49135 | MGKRDRVDRDKKKSKKRQYEEEEEDEDDIPGNESQEAVPSAAGKQVDESSTKVDEYGAKDYRQQMPLKGDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIIQFIKLCTVSYGKVKLVLKHNRYFVESSHPDVIQHLLQDPVIRECRLRNAEGEATELITETFTSKSAISKTAAEGSGGPSTSQGVDAQATSDIPKDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCICLEYPLLAEYDFRNDTLNPDINIDLKPTAVLRPY... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... |
O13768 | MSLKRKNNAREGTPDEDLEEYSDYSDVDNYGEEDDDSYKPAPRIRINNNKTKAQTTTNSNEARQSGISAMFGQNDFSNLLGLKLDHTARPLWINPIDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDNVEDKKDITNDSSKETAEKSSSDELFSAVVGLQEEEDDEDAVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRNDNINPDLPIDLKP... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH... |
Q13216 | MLGFLSARQTGLEDPLRLRRAESTRRVLGLELNKDRDVERIHGGGINTLDIEPVEGRYMLSGGSDGVIVLYDLENSSRQSYYTCKAVCSIGRDHPDVHRYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQTADVFNFEETVYSHHMSPVSTKHCLVAVGTRGPKVQLCDLKSGSCSHILQGHRQEILAVSWSPRYDYILATASADSRVKLWDVRRASGCLITLDQHNGKKSQAVESANTAHNGKVNGLCFTSDGLHLLTVGTDNRMRLWNSSNGENTLVNYGKVCNNSKKGLKFTVSCGCSSEFVFVPYGSTIAVYT... | Function: Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent mann... |
G4SW86 | MSEQESRDNAAVDAVRQKYGFGFSWLVLMIALPPLVYYLWICVTYYQGELVFTSDAAAWRRFWSHVAPPTWHAAGLYAAWFLGQAALQVWAPGPTVQGMKLPDGSRLDYRMNGIFSFLFTLAVVFGLVTMGWLDATVLYDQLGPLLTVVNIFTFVFAGFLYFWGLNGKQWERPTGRPFYDYFMGTALNPRIGSLDLKLFCEARPGMIFWLLMNLSMAAKQYELHGTVTVPMLLVVGFQSFYLIDYFIHEEAVLTTWDIKHEKFGWMLCWGDLVWLPFTYTLQAQYLVHHTHDLPVWGIIAIVALNLAGYAIFRGANIQKH... | Function: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast.
Catalytic Activity: 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,... |
Q75D30 | MNDKVAATLVLVVTYSIVGASLWCLTYAWHDETKLYYWCIVQLLPVMLWVWCVISWCGAQLFGYAKRGKAD | Function: Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins.
Location Topology: Multi-pass membrane pr... |
O44406 | MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGL... | Function: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) . Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) . Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA-mediated gene-... |
Q7SEY9 | MKPASRLFYLSLFALWSPEAQCKSDESCAISPKAIVSDACASYSTLEQLNRDIKPALEDLTRTTDFFSHYRLNLFNKECPFWNDENGMCGNIACAVETLDNEEDIPEVWRAKELGKLEGPRAKHPGKSVQKEEPKRPLQGKLGEDVGESCVVEYDDECDDRDYCVPDDEGASSKGDYVSLLRNPERFTGYAGDGAKQVWDAIYRENCFQKSSFPKSASLGDTYSVPKNPAAQDFRAVMQAAGRQHMLEQQREQNPLVPFVTKTGLESEDECLEKRVFYKIVSGMHASISTHLCWDFLNQTTGQWQPNLSCYINRLHKFPE... | Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly pdi1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on pdi1 to transfer oxidizing equivalent. Does not oxidize a... |
Q03103 | MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNE... | Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidi... |
Q09216 | MLRRRGGPNELRDELNNSKNQPEDDQRTKRGRESIGFRHWIYFVLTVAIVYAGVVALHRKMPAVRDGTSFEDFSEQRARVLLKQLTALGSRPSGSDNLEVKAFGMIQDRIGKIHSVVDEVGVNRLESDVQRPSGCFDLKFLSSFTLCYHKITNVVVRIGPKKGPSGNSLLLNCHFDTMPDTPGATDDAVACTIMMDVLEVLAHSKTELENDVVFLFNGAEENFLQAAHGFINQHPWRHDIRAFINLEGTGSGGREILFQAGPGNSWLLQTYLENAPHPFCSVLAQEIFQSGIIPSDTDFRIFRDYGRISGLDIAYTKNGW... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102122
Sequence Length: 895
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.-.-
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Q18600 | MSTGIRRRHADEKKNILEKESLQNDETQREMEKDISLLRPAHWNFIGLFFLVLIIGTTFLHKCLPEPKDPNQEETQFSEKRAVKVLQELSDYGWKPAGSYNCEELTRNRILKELNDIRSQNQNVENLRFDIDTQYVSGCFDIPAHDTEGMNICYRNVSNVMARLGKGEKKDKISVLLNCHYDSWPTSNAGSDDLSSCALMLELIRLYSKNPHLLNHDVIFLFNGAEESSLLAAHGFITQHSWRHEIRAFINLEASGSGGRELLFQAGPANQWLLNSYLEAAIHPHCSVIGQEVFQSGVYPGDTDFRIFRDHGRVPGLDLA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101896
Sequence Length: 895
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.-.-
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Q05359 | MLLTSLLQVFACCLVLPAQVTAFYYYTSGAERKCFHKELSKGTLFQATYKAQIYDDQLQNYRDAGAQDFGVLIDIEETFDDNHLVVHQKGSASGDLTFLASDSGEHKICIQPEAGGWLIKAKTKIDVEFQVGSDEKLDSKGKATIDILHAKVNVLNSKIGEIRREQKLMRDREATFRDASEAVNSRAMWWIVIQLIVLAVTCGWQMKHLGKFFVKQKIL | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24723
Sequence Length: 219
Subcellular Location: Endoplasmic reticulum membrane
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P39704 | MIKSTIALPSFFIVLILALVNSVAASSSYAPVAISLPAFSKECLYYDMVTEDDSLAVGYQVLTGGNFEIDFDITAPDGSVITSEKQKKYSDFLLKSFGVGKYTFCFSNNYGTALKKVEITLEKEKTLTDEHEADVNNDDIIANNAVEEIDRNLNKITKTLNYLRAREWRNMSTVNSTESRLTWLSILIIIIIAVISIAQVLLIQFLFTGRQKNYV | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24064
Sequence Length: 215
Subcellular Location: Endoplasmic reticulum membrane
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Q12403 | MSNLCVLFFQFFFLAQFFAEASPLTFELNKGRKECLYTLTPEIDCTISYYFAVQQGESNDFDVNYEIFAPDDKNKPIIERSGERQGEWSFIGQHKGEYAICFYGGKAHDKIVDLDFKYNCERQDDIRNERRKARKAQRNLRDSKTDPLQDSVENSIDTIERQLHVLERNIQYYKSRNTRNHHTVCSTEHRIVMFSIYGILLIIGMSCAQIAILEFIFRESRKHNV | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26511
Sequence Length: 225
Subcellular Location: Endoplasmic reticulum membrane
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P11474 | MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALR... | Function: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Req... |
O08580 | MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVTLASGPAPARCLPGHKEEEDGEGAGSGEQGSGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAPVNALVSHLLVVEPEKLYAMPDPASPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGDLGAALLQLVRRLQALRL... | Function: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Req... |
O95718 | MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLEL... | Function: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity . Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryoni... |
Q61539 | MSSEDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGIALSTHANGLDSPPMFAGAGLGGNPCRKSYEDCTSGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYNCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSENSPYLNLPISPPAKKPLTKIVSNLLGVEQDKLYAMPPNDIPEGDIKALTTLCELADRELVFLINWAKHIPGFPSLTLGDQMSLLQSAWMEILILGIVYRSLPYDDKLAYAEDYIMDEEHSRLVGLLDL... | Function: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcriptional activity . Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryo... |
P62508 | MDSVELCLPESFSLHYEEELLCRMSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSF... | Function: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements (By similarity). Induces the expression of PERM1 in the skeletal muscle.
PTM: Acetylated by PCAF/KAT2 (i... |
Q5RAM2 | MSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLL... | Function: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle (By similarity).
PTM: Acetylated by PCAF/KAT2 (i... |
P05432 | MSTAGVAAQDIRVPLKTGFLHNGQALGNMKTCWGSRNEFEKNFLNIDPITMAYNLNSPAPEHLTTLGCASPSAPGSGHFFAERGPSPKSSLPPLVIPPSESSGQREEDQVLCGFKKLSVNGVCASTPPLTPIQSCSSPFPCAAPCDRSSRPLPPLPISEDPSLDEADCEVEFLTSADTDFLLEDCVPSDFKYDVPGRRSFRGCGQINYAYFDSPTVSVADLSCASDQNRVVPDPNPPPPQSHRRLRRSHSGPAGSFNKPAIRISSCTHRASPSSDEDKPEIPPRVPIPPRPAKPDYRRWSAEVTSNTYSDEDRPPKVPPR... | Function: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratin... |
Q38846 | MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHAR... | Cofactor: Binds 1 copper ion per dimer.
Function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
PTM: Autophosphorylated on both His and Ser residues in th... |
Q8RY71 | MAPTLQGQWIKVGQKGGTGPGPRSSHGIAAVGDKLYSFGGELTPNKHIDKDLYVFDFNTQTWSIAQPKGDAPTVSCLGVRMVAVGTKIYIFGGRDENRNFENFRSYDTVTSEWTFLTKLDEVGGPEARTFHSMASDENHVYVFGGVSKGGTMNTPTRFRTIEAYNIADGKWAQLPDPGDNFEKRGGAGFAVVQGKIWVVYGFATSIVPGGKDDYESNAVQFYDPASKKWTEVETTGAKPSARSVFAHAVVGKYIIIFAGEVWPDLNGHYGPGTLSNEGYALDTETLVWEKLGEEGAPAIPRGWTAYTAATVDGKNGLLMH... | Function: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Converts glucosinolates both to epithionitriles and to simple nitriles in the presence of myrosinase . Promotes the formation of epithionitriles after hydrolysis of alkenylglucosinolates containi... |
Q9YHT3 | YEVGMMKGGIRKDRRGGRMLKHKRQREENDSRNAGALTEARSTALWPSPLMIKHSKKNSPALSLTADQMVSALLEAEPPVVYSEYDPSRPFNEASVMTLLTNLADRELVHMINWAKRVPGFVDLALHDQVHLLECAWLEILMVGLVWRSMEHPGKLLFAPNLLLDRSHGKVVEGFVEIFDMLLAASSRFRMMNVRGEEFVCLKSIILLNPGIYTYLSSTLKSVEERDHIHRVLDKITDTLMHLMAKSGLSLQQQHRRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPAAKGSPPSEDDPLN... | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 39560
Sequence Length: 349
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
Q91424 | GHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRILKHKRQREEHDNRNAGAIVERRSPNLWPSPLMITHNKKNSPALSLTADQIVSALLEAEPPVVYSEYDPSRPFSEASMMTLLTNLADRELVHMINWAKRVPGFVDLSLHDQVHLLECAWLEILMIGLVWRSVEHPGKLLFAPNLLLDRNQGKCVEGFVEIFDMLLATSSRFRMMNVQGEEFVCLKSIILLNSGIYTFLSSTLKSLEEKDHIHRVLDKIIDTLLHLMAKSGLSLQQQHRRLAQLLLILSHFRHMSNKGM | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 35202
Sequence Length: 307
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
P49884 | MTMTLHTKASGMALLHQIQANELEPLNRPQLKIPLERPLGEVYMDSSKPAVYNYPEGAAYDFNAAAPASAPVYGQSGLPYGPGSEAAAFGANGLGAFPPLNSVSPSPLVLLHPPPQPLSPFLHPHGQQVPYYLENESSGYAVREAGPPAYYRPNSDNRRQGGRERLASTSDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRNEAVPSGDMRAANLWPSPIMIKHTKKNSPVLSLTADQMISAL... | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... |
P06212 | MTMTLHTKASGVTLLHQIQGTELETLSRPQLKIPLERSLSDMYVESNKTGVFNYPEGATYDFGTTAPVYGSTTLSYAPTSESFGSSSLAGFHSLNNVPPSPVVFLQTAPQLSPFIHHHSQQVPYYLENEQGSFGMREAAPPAFYRPSSDNRRHSIRERMSSTNEKGSLSMESTKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGEMMKQKRQREEQDSRNGEASSTELRAPTLWTSPLVVKHNKKNSPALSLTAEQMVSALLEAEPPI... | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 66746
Sequence Length: 589
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
P03372 | MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALL... | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... |
Q9YHZ7 | MSEEQARAEAPAGARQRRRSELEGYSVSLASLKLSPMYPEEEQRTTGGISSTAHYLDGTFNYTTNPDATNSSVDYYSVAPEPQEENLQPLPNGSSSPPVFVPSSPQLSPFLGHPPAGQHTAQQVPYYLEPSGTSIYRSSVLASAGSRVELCSAPGRQDVYTAVGASGPSGASGPSGAIGLVKEIRYCSVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYVCPATNQCTIDRNRRKSCQACRLRKCYEVGMMKGGFRKERGGRIIKHNRRPSGLKERERGYSKAQSGSDVREALPQDGQSSSGIGGGVADVVCMSPEQV... | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 67671
Sequence Length: 617
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
P49886 | LFAPNLLLDRNQGKCVEGMVESFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGME | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... |
O24602 | MASRMGMVAIVSLFVCALAASTSVNANVWQTDDIPVVNSNMVRHSNMERQQQQGGFIGHRPRLASFNRASNQDGDRKRTVPSGPDHMHHSIPSHTPQHPPVYVQALYEDDRSRTSSGPSKSIGPPPLSDRY | Function: Extracellular signal peptide that regulates cell fate.
PTM: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-84 enhances binding affinity of the ESR1p peptide for its receptor.
Sequence Mass (Da): 14432
Sequence Length: 131
Subcellular Location: Secreted
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P38117 | MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (Probable). Requ... |
Q9DCW4 | MAELRALVAVKRVIDFAVKIRVKPDKSGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEIIAVSCGPSQCQETIRTALAMGADRGIHVEIPGAQAESLGPLQVARVLAKLAEKEKVDLLFLGKQAIDDDCNQTGQMTAGLLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVVKAGDLGVDLTSKVSVISVEEPPQRSAGVKVETTEDLVAKLKEVGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (By similarity). ... |
Q7F9U3 | MKILVAVKRVVDYAVKVRVRPDRTGVETASVKMSMNPFCEIAVEEALRLRESGAATEVVAATVGPSQSADTLRTALAMGADRAVHVLHDPDPSRPLLPLAVAKILRALALQENPGLVILGKQAIDDDCNQTGQMLAGLLNWPQGTFASKVILNKEKATVEREVDGGIETISLDLPAVITTDLRLNQPRYATLPNIMKAKSKVIKKVTPEDLDVDIRSDMEVVEVTEPPKRKAGVILSSVDELVDRLKNEARVL | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
Q6UAQ8 | MAELRALVAVKRVIDFAVKIRVKPDRTGVVMDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPAAEAHHLGPLQVARVLAKLAQKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKAGDLGVDLTSKLSVVSVEDPPQRVAGVKVETTEDLVAKLREIGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase. Required for nor... |
Q9UTH2 | MSKIRILVGVKRTLDYMLKPRINATKTAVDLSGQKMSINPFCDIAVEEAIRMKETLKNRIEDTLVVTAGQTSSEPILRQCLAKGIGRAALINVGEKELEPLSVAKLLKATVEKEKSNLVLLGKQAIDDDAHQTGGMLAAMLGWPQFTSASKVRIEGDKVIVTREIDGGEETLSSTLPAIITTDLRLNVPRFANLAKVMKARKAPLGKMSPEDLGVTIDQRLQTVSVSEPVQKRQNIMVKSVDEMVKTLKELGAL | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
Q0AZ34 | MNLKVLVCVKQTFDTEAKIELKDGKIADAGINLIINPYDEVAVEGAIQLKEKGVAKEIVVVAAGSDKAMDAIRTALAMGADRGILVQQDTAADEFARAVALAEAIKGENPDIILAGHVAADDGSSQVPTRVAEILGLPHVNVITAVEIAGGKATCTSEADGGTQVTEVSLPAVISSQVSWNEPRYPSMKGIMAAKKKPVATAAAAAAESKVKILEFSLPPAKAAGIKIEDEPEVCATKLAEWMKNTVKVEVK | Cofactor: Binds 1 AMP per subunit.
Function: Part of an electron transfer flavoprotein involved in syntrophic growth of S.wolfei with butyrate. Probably receives electrons from butyryl-CoA dehydrogenases, and transfers them to the membrane-bound quinone oxidoreductase Swol_0698.
Sequence Mass (Da): 26280
Sequence Lengt... |
P42940 | MSAKQQLRILVPVKRVVDFQIKPRVNKTLTGIETSGIKFSINPFDDIAVEEAIRIKEKNKSLVESTHAVSIGSAKAQDILRNCLAKGIDTCSLIDSVGKENIEPLAIAKILKAVVEKKGSNLVLMGKQAIDDDCNNTGQMLAGLLNWPQATNAAKVEFLDNGRVQVTREIDDGEEVIEASLPMVITTDLRLNTPRYVGLPKLMKAKKKPIEKLDIAKDFPEINIEPQLKIVSMEEPKTKSPGVKLNSVDELIEKLKEVKAI | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
P41212 | MSETPAQCSIKQERISYTPPESPVPSYASSTPLHVPVPRALRMEEDSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPRILFSPFFHPGNSIHTQPEVILHQNHEEDNCVQRTPRPSVDNVHHNPPTIELLHRSRSPITTNHRPSPDPEQRPLRSPLDNMIRRLSPAERAQGPRPHQENNHQESYPLSVSPMENNHCPASSESHPKPSSPRQESTRVIQLMPSPIMHPLILNPRHSVDFKQSRLSEDGLHREGKPINLSHREDLAYMNHIMV... | Function: Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
PTM: Phosphorylation of Ser-257 by MAPK14 (p38) inhibits ETV6 transcriptional repression.
Sequence Mass (Da): 53000
Sequence Length: 452
Subcellular Location: Nucleus
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P0A0L2 | MKKTAFTLLLFIALTLTTSPLVNGSEKSEEINEKDLRKKSELQGTALGNLKQIYYYNEKAKTENKESHDQFLQHTILFKGFFTDHSWYNDLLVDFDSKDIVDKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLTEEKKVPINLWLDGKQNTVPLETVKTNKKNVTVQELDLQARRYLQEKYNLYNSDVFDGKVQRGLIVFHTSTEPSVNYDLFGAQGQYSNTLLRIYRDNKTINSENMHIDIYLYTS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules . In turn, ... |
P20723 | MKKFNILIALLFFTSLVISPLNVKANENIDSVKEKELHKKSELSSTALNNMKHSYADKNPIIGENKSTGDQFLENTLLYKKFFTDLINFEDLLINFNSKEMAQHFKSKNVDVYPIRYSINCYGGEIDRTACTYGGVTPHEGNKLKERKKIPINLWINGVQKEVSLDKVQTDKKNVTVQELDAQARRYLQKDLKLYNNDTLGGKIQRGKIEFDSSDGSKVSYDLFDVKGDFPEKQLRIYSDNKTLSTEHLHIDIYLYEK | Cofactor: A zinc-binding site contributes directly to formation of the homodimer.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates... |
P0A0M0 | MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is necessary for interaction with host MHC class II molecules.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via th... |
A2RQG7 | MFCLNTFKSRWPREFQNLKKKKKKTCVKLSIPIRSVTGDAASLTVVVTMYKRDDYVRNKPGGVFSRWQGFARSMLLPKPFSETAELRRTVADYSLISRGLAPKILREAKGNREDLRVGKDFVGSRYRVQESIQGLGVAVNIHDADDISHGQTESIRTRLRSYGRPVPLLKKLGDNASQTITQKKTGGRSKDKKHGFEEERDVSRVEAEENNTNSVHASVLRLSRSRPQPVLERHDDIVDGSDSASVCGVLQEDGTTCLTAPVTGRKRCTEHKGQRITCAPPVKNPPCEEETEEICGVILPEMVRCRSKPVSGRKRCEDHK... | Function: Transcription regulator that negatively modulates gibberellin-mediated developmental processes. May act as transcriptional repressor of giberellin controlled genes. Binds DNA without sequence preference.
Sequence Mass (Da): 49323
Sequence Length: 440
Domain: Contains a bacterial GIY-YIG-like domain.
Subcellul... |
P10229 | MPLRASEHAYRPLGPGTPPMRARLPAAAWVGVGTIIGGVVIIAALVLVPSRASWALSPCDSGWHEFNLGCISWDPTPMEHEQAVGGCSAPATLIPRAAAKQLAAVARVQSARSSGYWWVSGDGIRACLRLVDGVGGIDQFCEEPALRICYYPRSPGGFVQFVTSTRNALGLP | Function: Important virulence factor of HSV neurotropism. Seems to be required for glycoprotein B-induced fusion. Dispensable for growth in vitro (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 18180
Sequence Length: 172
Subcellular Location: Virion membrane
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Q6UDL6 | MRPNGARTQTAPPPAAAEGTADVHGNGEAATIQLDGQPSAPSPPLTTVFEATDDYKARRRNLESEPPFEVRAILDDELSDYPVAAPLDAVPQKHSCCCGVCLRRCAFVLTGMAVGMLLAAALLATIAAFAVPESVWTGGVCERGWVQHMGVCYKPGRTPPPSSAADGNFSAATFAGANTNCAAAGGSIVSSDQALSFLVLLSKTASGPNSAPPRGSWWTTHSGSCAIVHYAPSSTLEVYGNTSSLQSLALRTRDALDVSIAEDTQCSGSAGVMCAAAPAPPTALKYAQALRAILTLGVRAE | Function: Seems to be required for glycoprotein B-induced fusion.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30945
Sequence Length: 301
Subcellular Location: Virion membrane
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L7MC74 | MAHKIAIGLVCVLYALHIMSAVCEVSEQEGVGEDNATEDEDYEDFFKPVTCYFANSTVGPLRPPNCTVVCTNNTAWWNDTKSDGGHCYSEYRPEKRTHSREIYNCTIGVCGNGTCIANHTYADCW | Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL2, CCL3, CCL3L1, CCL7, CCL8, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL18 and CCL23 . Binds to CCL8 with 1:1 stoichiometry and disrupts CCL8 homodimer formation .
Sequence Mass (Da): 13925
Seq... |
Q08CB3 | MVTAFLNERQATTEEMALVSNALAAYSFIADQPERAALYFVCGVCLGLVLTLIALVVQISCRTDCKTQQAPKKTGKTVENTSDTSDSDSDWDNTSDLSARRHRRFERTLGNVFTSAEELERAQRLEERERIIREIWMNGQPDMPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17374
Sequence Length: 153
Subcellular Location: Endoplasmic reticulum membrane
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Q9H8M9 | MRLPLSHSPEHVEMALLSNILAAYSFVSENPERAALYFVSGVCIGLVLTLAALVIRISCHTDCRRRPGKKFLQDRESSSDSSDSEDGSEDTVSDLSVRRHRRFERTLNKNVFTSAEELERAQRLEERERIIREIWMNGQPEVPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17470
Sequence Length: 152
Subcellular Location: Endoplasmic reticulum membrane
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Q91WM6 | MKLPLSPSTEPVATEPLGMALLSSILAAWSYISENPERAALYFVSGVCIGLFLTLAALVMRISCHTDCRRGPRRRCLQDRECSDSSDSEDGSEDTASDLSVRRHRRFERTLNKNVFTSAEELERAQRLEERERIIREIWMNGQPEVPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17810
Sequence Length: 156
Subcellular Location: Endoplasmic reticulum membrane
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P54521 | MGEAAYVTVSALTKYIKRKFDVDPHLENIWIKGELSNVKIHTRGHIYFTLKDENARMQSVMFARQSERLPFKPENGMKVLVRGGISVYEPSGNYQLYAKEMQPDGVGALYLAYEELKKKLAGEGLFDDRYKKQIPAFPATIGVVTSPTGAAVRDVITTLKRRYPLVKVIVLPALVQGENASRSIVTRIEEANEKEICDVLIVGRGGGSIEELWAFNEEIVARAIFASNIPIISAVGHETDFTISDFVADIRAATPTGAAEIAVPHTTDLIERTKTAEVRMTRAMQQHLGQKKERIQTLQSSYAFRFPKRLYAQKEQQFDL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5104... |
A1UTK7 | MADFFTEKPVATNVAEFSVSEIANALKRVVEDKFGYVRIRGEISGYRGAHASGHAYFALKDDKARLEAVIWLSVMKKLSFPPEEGMEVIAVGKLTTYPGSSKYQIVIEALEPTGVGALMTLLENRKKKLAEEGLFDAANKKPLPYMPKIIGVVTSPTGAVIRDIIHRIFDRFPLHILVWPVRVQGETCGREVASAVEGFNALFLGGGIPKPDLIIVARGGGSLEDLWGFNDEAVVRAVYASAIPVISAVGHETDWTLIDYAADWRAPTPTGAAERAVPVKLDIEVHLASINSRFRVGLARYFDFHQQKLRALVRGLPTVD... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5331... |
Q6FZ30 | MNLFFEKTEATNVAEFSVSEIAGALKRVVEERFGYVRVRGEISGYRGAHASGHVYFSLKDDKARLEAVIWRGIMEKLKFPPEEGMEVIAVGKLTTYPGSSKYQIVIEALEPTGVGALMTLLENRKKKLADEGLFDEAKKKPLPYMPRIIGVVTSPTGAVIRDIIHRISDRFPLHILVWPVRVQGDTSGREVADALKGFNALPFGGLVPKPDLIIVARGGGSLEDLWGFNDEAVVRAVYESALPVISAVGHETDWTLIDYVADWRAPTPTGAAERAVPVKLDLEVQVASLGARLRMGLARYFDFHQQKLRALVRGLPTVDQ... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5331... |
Q7VVB6 | MTIGLSVTNDVFARDILTVAQLNQAVGQLLERSIPSLWVRGEISNFTQAASGHWYFTLKDSRAAVRTVMFRSRAAQVGFVPRPGDQVEVRARVSLYEPRGDYQLQADGMRRAGVGNLYEAFLRLKAQLQDEGLFDPQRKRQPARLPRAIGVVTSLHAAALRDVLSALARRAPQVPVIIYPAPVQGADAAARLAARVAQANQRAEVDTLLLVRGGGSIEDLWSFNDEALAREVAASDIPVISGVGHETDFTIVDFVADLRAPTPTAAAELACVPRGDLLAALRHTAEWLARAQQRRLDQAAQRLDRAAAMLTSPAQRLAHQ... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5027... |
C0ZC06 | MALQDILSVSDLNRYIKLVLEKEPHLQDIWVRGEISNFTHHSSGHMYFTLKDKQSRIKVVMFASYNRFLRFLPKDGAKAIVRGSISAYERDGAYQFYAKEMQPDGLGSLYLAFEQLKEKLAQEGLFAAERKRMLPRFPKRVGVVTSPTGAAIRDICTTIRRRYPQAEIVLSPAVVQGADAPASIVSAIRIMNDQPDIDVLIVGRGGGSIEELWAFNDENVARAIATSLIPVISAVGHETDVTIADFVADVRAATPTAAAELAVPHYLEWVERVRQLEIRMHRAVRGTMTEQRNRLTRLGNSYAMRQPERRLEEAAERLDR... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5240... |
A6X3A0 | MGSDSSFTGASSNVAEYSVSEISGALKRTVEDTFGHVRVRGEISGYRGPHSSGHAYFALKDDRARLEAVIWRGSMSRLRFRPEEGMEVIATGKLTTYPGSSKYQIVIEQMEPAGAGALMALLEERKRRLATEGLFDPAVKQLLPFMPRVIGVVTSPTGAVIRDIIHRIADRYPLHVIVWPVRVQGETSGPEVAAAVDGFNALPDEGNIPRPDVLIVARGGGSLEDLWGFNDEIVVRAVAASHIPVISAVGHETDWTLIDLAADIRAPTPTGAAEMAVPVKADLLATLAGQSARLSSAMSRFIDLKRQAHRSAARALPSAD... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5788... |
Q5FJG6 | MAENKYLTVTDLNYYITQKFKNDPYLHKVFLQGELSNFRYRRNSHQYFSLKDEKSKINVVMFRSYFDKVKFKPEEGMKVYVTGYVSVYGPQGSYQFYAENMEPAGLGALYEQLKQLQVKLAKEGLFNPEHKKKIPRFPDRIAVVTSASGAVIHDIMVTANRRFPHAEIDLFPAQVQGDTAAESLVRAMRQIAAEGDKYDVMIIGRGGGSLEDLWPFNEEEVVRQVYNMQMPVISSVGHETDTTLCDLVADARAATPTAAAEYATPNLMDELAGIHQLQSRLFSSMQTIIRQKRDRLNRIQNSIIMREPTRLYDQQIETVD... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5260... |
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