ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
E0Y3X0 | MAIEEKSTSAEPGPYDALSRFSSLTGEDDRKWWEHTGPVLEKVMRDSGYELQSQYIYLYFVQQHLIPYLGKFPTRGQDDHRWQSNLTPYKVPYELSWNVSHKVVRISWDPVCDASGTENDAFNKKAIHDCTRQLAELDSTVILDRYRLLHKDLVITDEEEQQLLRRDVLPKSGRGQHNLAVDFQEGGITLKVYFYPYMKFLATGTPIEELFFSAIEKLRIADIDEAVGMLKCFLSPKSDDGKPSVDEKVFPSLLACDLCDPSKSRIKYYVIDKWVKWERIANLWTIGGRRLEDPYCAKGLALLKELWDLLAIPEGDRGDI... | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan b... |
L7WR40 | MRDIRELLLVLFTSCLALGSVPSSFDGDRYCRCQPGEACWPSLADWQALNMSIQGTLVEVRPIGHVCHEPTYNKADCERVSKLSSNGTWRASQPGAQQEHAWEVSLSRNESCYVGPANPAEPCGQGRIPRYSAMVETTEQAQKAIRFARERRLRLVIKNTGHDSGGRSSAVDSFQILTQRLKDISFIEEFTPTLAETRGPSVRIGAGVLTKELYAVADEHGYTAMGGECATVGVAGGYIQGGGVSTALTPMMGLAADLVQEFEVISAEGSLVIANEFQNQDLFWALRGGGGGTVGLVTSITMPVFGAIPANISELSFESQ... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryp... |
I4AY86 | MTAPELRAPAGHPQEPPARSSPAQALSSYHHFPTSDQERWYQETGSLCSRFLEAGQYGLHQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVNFLSGSSQDPFNRIPIADLLAQLARLQLRGFDTQCFQQLLTRFQLSLDEVRQLPPDDQPLKSQGAFGFDFNPDGAILVKGYVFPYLKAKAAGVPVATLIAESVRAIDADRNQFMHAFSLINDYMQESTGYNEYTFLSCDLVEMSRQRVKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIMEGLARLKQIWSLLQIGEGSRAFKGG... | Function: Deoxybrevianamide E synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-t... |
A6R538 | MAPARPILLRFESRNGQFRLTVNPTDEFPSLLPKVLDNLPKNTAPPSIVLSNKPIGTGGQERNISTLKGVTIQRVGLSHGDKLFIGYEEETAVVNGSSSEHPSSISKSQNAPRRLDGVAVRQQEQAPPVPTPTSETLIKNPWEAVKQSPLDDRLDRKDGKISRGLDHKMCRHGPKGMCDYCMPLEPYAPEYLAEKKIKHLSFHSYLRKINSSTNKPELKSSYIPPLSEPDYRVKRDCPSGHPAWPEGICTKCQPSAITLQPQPFRMVDHVEFSSPDLINSLLDFWRKSGTQRLGFLYGTYEEYTEVPLGIKAVVQAIYEP... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71205
Sequence Length: 642
Su... |
Q74ZJ1 | MILRFRSKHGMQRVNCEGSEQFGTVLDRWVKLVHERAPREAMEVGVAERQIETRIAAEMAQKTVEQLGLKHGDMLSVSFKETGGSLAVAAAPERSSELAVDRELAREEGLIRRSHSRLCRHGDRGMCEYCSPLPPWDRGYQQEQNLKHISFHAHVKELNEHTNKKASGSTYIPPLSPPDFHVNKHCPAPHEPWPRGICSKCQPSAISLQQQEFRMVDHVEFQHSELVNEFINTWRSTGMQRFGYLYGRYARYDNTPLGIKAVVEAIWEPEQHDEQDGLTMDTVAVRVSVAAVDAIAADMGLMRLGMIFTDLTDSGSGDGS... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63253
Sequence Length: 563
Su... |
A1CS06 | MAATRPIILRFESRNGQFRLSVSPQELFPTLKQKILENLPKDVEPSSITLSNKPIGTGGEERSLDGLEGVSIEQVGLKHGDKLFVGYQERKGGETTPAKAHAAADSLRRLNGALVPQTETVTFRPPTSSSATVKNPWEVVQQSPLDDKLDKKDGKIQRPRDMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKINAATNKAELKSSFMPPLSEPYYRVRHDCPSGHPPWPEGICTKCQPSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGSQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDE... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75417
Sequence Length: 674
Su... |
Q5AA50 | MSSIILRFRSKDGMFRITTDSSSNFTLVLEQLIEKLSQSGNNGNGNGNNNKIDLQSLTIANKPQDKGKSSYEFQNQTVNELGLKNGDMLYVNYESVTNDSGPTTTATNTTTNTASGNTIPITGPVPSIPINSVVTSHGPLKVEELPIDQELDKEDGLITRPLSSMCRHGPKGMCEYCSPLPPWDENYRKDHAIKHISFHAYLKQQLEKLKSSGGSYFPPLDPVDYSIDLTCNQGHKPYPNGICSKCQPSPITLQLQKFRMVDHLEFADSFILNDFINVWRVSGVQRFGYLYGRYAKSEKTPLGIKAIVETIIEPPQHDEL... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67354
Sequence Length: 598
Su... |
P0CP30 | MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLFLSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRHGDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICSTCQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTV... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75103
Sequence Length: 693
Su... |
Q8TAT6 | MAESIIIRVQSPDGVKRITATKRETAATFLKKVAKEFGFQNNGFSVYINRNKTGEITASSNKSLNLLKIKHGDLLFLFPSSLAGPSSEMETSVPPGFKVFGAPNVVEDEIDQYLSKQDGKIYRSRDPQLCRHGPLGKCVHCVPLEPFDEDYLNHLEPPVKHMSFHAYIRKLTGGADKGKFVALENISCKIKSGCEGHLPWPNGICTKCQPSAITLNRQKYRHVDNIMFENHTVADRFLDFWRKTGNQHFGYLYGRYTEHKDIPLGIRAEVAAIYEPPQIGTQNSLELLEDPKAEVVDEIAAKLGLRKVGWIFTDLVSEDT... | Function: The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for t... |
A4RN19 | MLLRLRGPDGMLRIELDPKDTFNKLGQELMGKLPPTVDPATITVSNAPGSQGDKKLLKDIAKYKVEAIGLKHGDLIFVDYKHQGAEADGTANSDGASQPLTSTTNRLNGQPVLPTEDLPIDPLPTPAPGATIKNPWEVVRQSPLDDRLDKKDGKIPRKRDAMCRHGPKGMCDYCQPLDPFDAKFLAEKKIKYLSMHAHLRKINSATNKPELGSSFIPPLSEPYFRVKHDCPSGHPQWPEGICSKCQPSAITLQPQPFRMVDHVEFASPSIVDSFINTWRRTGGQRYGIMYGKYSEYEEVPLGIKAVVQAIYEPPQVDEVD... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74006
Sequence Length: 669
Su... |
Q9UTK3 | MSEPAVVSILDTDLYKLTMLQAVLEHYPDAQVSYKYTNRSPKMALNQEAYNWLREQIRGLRNLHLLPEEEQWLRKNCPYLKESFYEFMHEFEFDPENSISLNYDSETKDLSIFIHGLWKNTIFYEIPLLALVSESYFKFVDKDWSPEGQFEKAYEKGKRLIRAGCAFTDFGTRRRRDPHTQEIVLQGLMKAQEDFKGPGSFLGTSNVYFAAKYNLNVSGTVAHEWYMGIAAITQNYKQANRIASLKWVQTFGTSLLIALTDTFSTDVFLKSFTANSADDLANVFHGVRQDSGCAEEYIEKVVKHYKSIGVDPSTKVIVHS... | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM:... |
P39683 | MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKF... | Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate . Essential for growth under anaerobic conditions .
PTM: Transiently phosphorylated on a His residue during the reaction c... |
Q06495 | MLSYGERLGSPAVSPLPVRGGHVMRGTAFAYVPSPQVLHRIPGTSAYAFPSLGPVALAEHTCPCGEVLERHEPLPAKLALEEEQKPESRLVPKLRQAGAMLLKVPLMLTFLYLFVCSLDMLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIHGGRDAPDLLKIITEPFTKLIIQLDESVITSIATGDESLRNHSLIQIWCHPDSLQAPTSMSRA... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity).
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pa... |
Q06496 | MMSYSERLGGPAVSPLPVRGRHMVHGAAFAYVPSPQVLHRIPGTTTYAISSLSPVALTEHSCPYGEVLECHDPLPAKLAQEEEQKPEPRLSQKLAQVGTKLLKVPLMLGFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKVITEPFTKLIIQLDKSVITSIAVGDESLRNHSLIRIWCQPETKEASTSMSRV... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic .
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane pro... |
O97704 | MISYGENLGGRAVSPLPVRGGHMMHGAAFAYVPSPQVLHRIPGTSAYGFPSVGPMALPEHGCPYGEVVEHHDPLPAKLALEDERKPEPGLIQKLRRAGVTLLKVPLMLSFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIVVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIRGGRDAPDLLKIITEPFTKLIIQLDKSVITSLASGDESLRNHSLIRVWCYPNPTEVPTPMPRA... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane prote... |
O95436 | MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTA... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75759
Sequence Length: 690
Subcellular Location: Apical cell membrane
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Q9JJ09 | MAPWPELENAHPNPNKFIEGASGPQSSIPDKDKGTSKTNDSGTPVAKIELLPSYSALVLIEEPPEGNDPWDLPELQDNGIKWSERDSKGKILCIFQGIGKFILLLGFLYLFVCSLDVLSSAFQLVGGKMAGQFFSNNSIMSNPVAGLVIGVLVTVMVQSSSTSSSIIVSMVASSLLSVRAAIPIIMGANIGTSITNTIVALMQAGDRNEFRRAFAGATVHDFFNWLSVLVLLPLEAATHYLEKLTNLVLETFSFQNGEDAPDILKVITDPFTKLIIQLDKKVIQQIAMGDSEAQNKSLIKIWCKTISNVIEENVTVPSPD... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75992
Sequence Length: 695
Subcellular Location: Apical cell membrane
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Q8N130 | MPSSLPGSQVPHPTLDAVDLVEKTLRNEGTSSSAPVLEEGDTDPWTLPQLKDTSQPWKELRVAGRLRRVAGSVLKACGLLGSLYFFICSLDVLSSAFQLLGSKVAGDIFKDNVVLSNPVAGLVIGVLVTALVQSSSTSSSIVVSMVAAKLLTVRVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATALLERLSELALGAASLTPRAQAPDILKVLTKPLTHLIVQLDSDMIMSSATGNATNSSLIKHWCGTTGQPTQENSSCGAFGPCTEKNSTAPADRLPCRHLFAGTELTD... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral (By similarity).
Catalytic Activity: 2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in)
Location Topology: Multi-... |
Q80SU6 | MPNSLAGGQVPNPTLDAFDLVDRSLRNAGISGSIPGLEEGGTDPWTFSPLKNADQLKEVGMASRLRRVVSSFLKACGLLGSLYFFICSLDILSSAFQLLGSKMAGDIFKDNVVLSNPVAGLVIGVLVTVLVQSSSTSSSIVVSMVASKLLTVQVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATAALERLSELALGAASLQPGQQAPDILKALTRPFTHLIIQLDSSVITSGITSNTTNSSLIKHWCGFRGETPQGSSEGCGLFSSCTERNSSASPEEDRLLCHHLFAGSKL... | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral .
Catalytic Activity: 2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane p... |
Q5SZA1 | MDEKPTTRKGSGFCSLRYALALIMHFSNFTMITQRVSLSIAIIAMVNSTQHQDPANASTEGPVMDLLSNQSRGIKDFSTRAAVYQWSTETQGIIFSSISYGIILTLIPSGYLAGIFGAKQILGAGLLISSLLTLFTPLAADFGVILVIVIRTVQGMAQGMAWTGQFTIWAKWAPPLERSKLTSIAGSGAAFGSFIILCVGGLISQALGWPFIFYIFGSIGCVCCVLWFTVIYDDPMHHPCISVREKEHITSSVAQQSSSPRRSVPIKAMVRCLPLWAIFMGFFSHFWLCTIIITYLPTYISTVLHVNIRDSGVLSSLPFI... | Function: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions . Mediates chloride-dependent transport of urate . Can actively transport inorganic phosphate into cells via Na(+) cotransport .
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 N... |
P58796 | MVKVNIIFYSMYGHVYRMAEAVAAGAREVEGAEVGIYQVPETLPEEVLEKMGAIETKKLFAHIPVLTREMNEEVLAGADALIFGTPTRYGNMTAQMRAVLDGLGGLWNRDAFVGKVGSVFTSSGTQHGGQESTILTFHVTLLHLGMILVGLPYSEKRQTRMDEITGGSPYGVSTIAGGDGSRQPSENELAMARYQGRHVTLIAKKIAGK | Cofactor: Binds 1 FMN per monomer.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 22604
Sequence Length: 209
EC: 1.6.5.2
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Q1QX85 | MGIRNTLDKLEPHFHQGGKYEKFYALYEAVDTIFYSPPSVTKSTAHVRDGIDLKRIMITVWLCTFPAMFFGMYNAGLQANMAIGDGFGALGGWREAVTMALAGSHDPGSIWANFVLGATYFLPIYLVTFAVGGFWEVLFAVKRGHEVNEGFFVTSVLYALILPATIPLWQVALGITFGVVIGKEIFGGTGKNFLNPALTGRAFLYFAYPAQISGDSVWVAADGYTGATALSTAAQNGMSAVQQAYSWWDAFLGFIPGSVGETSTLAILIGAAVLLITRIASWRIMLGVFVGMALTAMLFTAIGSESNPMFGMPWYWHLVL... | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
Q7UWS1 | MVEQYLSVFLKAVFVENLALAFFLGMCTFLAVSKNVKTAIGLGIAVIAIETITVPANQLIYSLLLKKGALTWVNDYLISTDTYNFAEVDLTFLGFISYIGVIAAMVQILEMFLDRFMPSLYNALGIFLPLITVNCAILGASLFMEQREYPFGESVVFGFGCGVGWALAIMALAGIREKLKYSDVPPPLRGLGITFITVGLMSLAFMSFSGIQL | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
Q56589 | MEHYISLLVKSIFIENMALSFFLGMCTFLAVSKKVKTSFGLGVAVVVVLTIAVPVNNLVYNLVLRENALVEGVDLSFLNFITFIGVIAALVQILEMVLDRFFPPLYNALGIFLPLITVNCAIFGGVSFMVQRDYNFAESIVYGFGSGVGWMLAIVALAGIREKMKYSDVPPGLRGLGITFITVGLMALGFMSFSGVQL | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
PTM: The N-terminus is blocked.
Loca... |
Q68D85 | MTWRAAASTCAALLILLWALTTEGDLKVEMMAGGTQITPLNDNVTIFCNIFYSQPLNITSMGITWFWKSLTFDKEVKVFEFFGDHQEAFRPGAIVSPWRLKSGDASLRLPGIQLEEAGEYRCEVVVTPLKAQGTVQLEVVASPASRLLLDQVGMKENEDKYMCESSGFYPEAINITWEKQTQKFPHPIEISEDVITGPTIKNMDGTFNVTSCLKLNSSQEDPGTVYQCVVRHASLHTPLRSNFTLTAARHSLSETEKTDNFSIHWWPISFIGVGLVLLIVLIPWKKICNKSSSAYTPLKCILKHWNSFDTQTLKKEHLIF... | Function: Triggers NCR3-dependent natural killer cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 50827
Sequence Length: 454
Domain: The C-terminal part is similar to retroviral Gag protein. This putative protein seems to be the result of a fusion between an Ig-like domain-con... |
P22736 | MPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQ... | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' . Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain . Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK ac... |
P12813 | MPCIQAQYGTPATSPGPRDHLTGDPLALEFGKPTMDLASPETAPAAPATLPSFSTFMDGYTGEFDTFLYQLPGTTQPCSSACSSASSTSSSSSSATSPASASFKFEDFQVYGCYPGTLSGPLDETLSSSGSEYYGSPCSAPSPSTPNFQPSQLSPWDGSFGHFSPSQTYEGLWAWTEQLPKASSGPPPPPTFFSFSPPTGPSPSLAQSSLKLFPPPATHQLGEGESYSMPAAFPGLAPTSPNRDTSGILDAPVTSTKSRSGASGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKSAKYICLANKDCPVDKRRRN... | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' . Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain (By similarity). Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cyto... |
Q04913 | MPCIQAQHGSLSQCAGPCDNYVPDILNSEFGKFTMDLVNSEIAASTSLPSFSTFMDGYTGEFDAFLYQIPSSNQQSSLKVEEFQVFGCYPGSFTNQLDETMSSSGSDYYGSPCSIPSPSTPGFQNPQLPTWECSYGAYSPTQNYDNMRHWTEQQKNSISQQTFFSFGTPAHSPNMAANPLKIAPATHRLDQQLVDTDVFALAQNSSAGFPAVPLGQAPGVLDSSVLLDSPLSPSKTRSPSSNEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLVVGMVKEVVRTDS... | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'.
Sequence Mass (Da): 64383
Sequence Length: 577
Domain: The NR LBD domain may bind the lipid A moiety of lipopolysaccharide (LPS) in the cytosol.
Subcellular Location: Nucleus
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P43354 | MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPTTPGFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRF... | Function: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development . It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity).
Se... |
Q06219 | MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPSTPSFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRF... | Function: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development . It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons .
Sequence Mass (Da... |
Q92570 | MPCVQAQYSPSPPGSSYAAQTYSSEYTTEIMNPDYTKLTMDLGSTEITATATTSLPSISTFVEGYSSNYELKPSCVYQMQRPLIKVEEGRAPSYHHHHHHHHHHHHHHQQQHQQPSIPPASSPEDEVLPSTSMYFKQSPPSTPTTPAFPPQAGALWDEALPSAPGCIAPGPLLDPPMKAVPTVAGARFPLFHFKPSPPHPPAPSPAGGHHLGYDPTAAAALSLPLGAAAAAGSQAAALESHPYGLPLAKRAAPLAFPPLGLTPSPTASSLLGESPSLPSPPSRSSSSGEGTCAVCGDNAACQHYGVRTCEGCKGFFKRTV... | Function: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner. Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the p... |
P51179 | MPCVQAQYSPSPPGSTYATQTYGSEYTTEIMNPDYAKLTMDLGSTGIMATATTSLPSFSTFMEGYPSSCELKPSCLYQMPPSGPRPLIKMEEGREHGYHHHHHHHHHHHHHHQQQQPSIPPPSGPEDEVLPSTSMYFKQSPPSTPTTPGFPPQAGALWDDELPSAPGCIAPGPLLDPQMKAVPPMAAAARFPIFFKPSPPHPPAPSPAGGHHLGYDPTAAAALSLPLGAAAAAGSQAAALEGHPYGLPLAKRTATLTFPPLGLTASPTASSLLGESPSLPSPPNRSSSSGEGTCAVCGDNAACQHYGVRTCEGCKGFFKR... | Function: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner . Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the ... |
P07071 | MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHESGIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVASHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEYEVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEEGVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDSTGNEILDGRNNLGVVTLNLP... | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Sequence Mass (Da): 67957
Sequence Length: 605
EC: 1.1.98.6
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P28903 | MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASYNKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQESILRNRIAGLGK... | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair . Can reduce each of the four common ribonucleoside triphosphates .
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2... |
Q9L646 | MTPHVMKRDGCKVPFKSERIKEAILRAAKAAGVDDADYCATVAEVVSSQMNARSQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIQREKRGRLNQEIRGLVEQTNSALLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTESYNKHRKTADEWQIPDAEGYARSRTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQASILRNRIAGLGK... | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Sequence Mass (Da): 79959
Sequence Length: 712
EC: 1.1.98.6
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P07075 | MNYDRIYPCDFVNGPGCRVVLFVTGCLHKCEGCYNRSTWNARNGQLFTMNTVKELASHLSKSYIQGLTLTGGDPLYPQNREEISNLVSWVKARFPEKDIWLWTGYKFEDIKQLEMLKYVDVIIDGKYEKNLPTKKLWRGSDNQRLWSNTDGVWKHD | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as c... |
P45080 | MNYLQYYPTDVINGEGTRCTLFVSGCTHACKGCYNQKSWSFSAGVLFDDVMEQQIINDLKDTRIKRQGLTLSGGDPLHPLNVETLLPFVQRVKRECPDKDIWVWTGYKLDELDKQQRAMLPYIDVLIDGKFIQEQADPSLVWRGSANQIIHRFKL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as c... |
Q7WZY5 | MKSISNRDKLQDLLTQYYLNTNEKMVFLNSTGEVIALNEAAEEVFADDNDYSQMTNAVCRRCEGYSNEYDIMSCENCFLEALEIGKGSFQVFIRTKDNKIQPYTASYELIDHEKGIYAFTLHNVSPQIQRQERMYQRKMMQKTISAQENERKRISRELHDGIVQELINVDVELRLLKYQQDKDELIDNSKRIEGIMSRLIDDVRNLSVELRPSSLDDLGLDAAFRSYFKQFEKNYGIHVNYHTNFSAQRFDNEIETVVYRVVQEALFNALKYAQVDIVEVSLQLNENNIIAEVSDRGVGFKRGDDPKGTGLGLFGMNERA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the... |
P46011 | MSMQQETSHMTAAPQTNGHQIFPEIDMSAGDSSSIVRATVVQASTVFYDTPATLDKAERLLSEAAENGSQLVVFPEAFIGGYPRGSTFELAIGSRTAKGRDDFRKYHASAIDVPGPEVERLALMAKKYKVYLVMGVIEREGYTLYCTVLFFDSQGLFLGKHRKLMPTALERCIWGFGDGSTIPVFDTPIGKIGAAICWENRMPSLRTAMYAKGIEIYCAPTADSRETWLASMTHIALEGGCFVLSANQFCRRKDYPSPPEYMFSGSEESLTPDSVVCAGGSSIISPLGIVLAGPNYRGEALITADLDLGDIARAKFDFDV... | Function: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN) or allylcyanide and no activity with indole-3-acetonitrile. Not associated with auxin production but may be involved in cyanide detoxification.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Locat... |
Q6H849 | MAMVPSGSGGGPPVIAEVEMNGGADSGAATVRATVVQASTVFYDTPATLDKAERLIEEAAGYGSQLVVFPEAFVGGYPRGSTFGFGANISIGNPKDKGKEEFRKYHAAAIEVPGPEVTRLAAMAGKYKVFLVMGVIEREGYTLYCSVLFFDPLGRYLGKHRKLMPTALERIIWGFGDGSTIPVYDTPLGKIGALICWENKMPLLRTALYGKGIEIYCAPTADSRQVWQASMTHIALEGGCFVLSANQFCRRKDYPPPPEYVFSGLGEEPSPDTVVCPGGSVIISPSGEVLAGPNYEGEALITADLDLGEIVRAKFDFDVV... | Function: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN). Not associated with auxin production but may be involved in cyanide detoxification (By similarity).
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 38676
Sequence Length: 362
E... |
P33036 | VSYNSKFLAATVQAEPVVLDA | Function: Acts on many kinds of nitrile compounds such as aliphatic, aromatic, and heterocyclic mononitriles or dinitriles. Prefers S-(-)-2-(4'-isobutylphenyl)-propionitrile to R-(+)-2-(4'-isobutylphenyl)-propionitrile as the substrate.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): ... |
P20960 | MQTRKIVRAAAVQAASPNYDLATGVDKTIELARQARDEGCDLIVFGETWLPGYPFHVWLGAPAWSLKYSARYYANSLSLDSAEFQRIAQAARTLGIFIALGYSERSGGSLYLGQCLIDDKGQMLWSRRKLKPTHVERTVFGEGYARDLIVSDTELGRVGALCCWEHLSPLSKYALYSQHEAIHIAAWPSFSLYSEQAHALSAKVNMAASQIYSVEGQCFTIAASSVVTQETLDMLEVGEHNASLLKVGGGSSMIFAPDGRTLAPYLPHDAEGLIIADLNMEEIAFAKAINDPVGHYSKPEATRLVLDLGHREPMTRVHSK... | Function: Nitrilase that acts mostly on arylacetonitriles.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 38908
Sequence Length: 356
EC: 3.5.5.1
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P10045 | MDTTFKAAAVQAEPVWMDAAATADKTVTLVAKAAAAGAQLVAFPELWIPGYPGFMLTHNQTETLPFIIKYRKQAIAADGPEIEKIRCAAQEHNIALSFGYSERAGRTLYMSQMLIDADGITKIRRRKLKPTRFERELFGEGDGSDLQVAQTSVGRVGALNCAENLQSLNKFALAAEGEQIHISAWPFTLGSPVLVGDSIGAINQVYAAETGTFVLMSTQVVGPTGIAAFEIEDRYNPNQYLGGGYARIYGPDMQLKSKSLSPTEEGIVYAEIDLSMLEAAKYSLDPTGHYSRPDVFSVSINRQRQPAVSEVIDSNGDEDP... | Function: Specific for the herbicide bromoxynil (3,5-dibromo-4-hydroxybenzonitrile); converts it to its metabolite 3,5-dibromo-4-hydroxybenzoic acid.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 37802
Sequence Length: 349
EC: 3.5.5.1
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P54845 | MALPPSPLAMEYVNDFDLMKFEVKREPSEGRPGPPTASLGSTPYSSVPPSPTFSEPGMVGATEGTRPGLEELYWLATLQQQLGAGEALGLSPEEAMELLQGQGPVPVDGPHGYYPGSPEETGAQHVQLAERFSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLTSSGPGSGDPSHLFL | Function: Acts as a transcriptional activator which regulates the expression of several rod-specific genes, including RHO and PDE6B . Functions also as a transcriptional coactivator, stimulating transcription mediated by the transcription factor CRX and NR2E3 . Binds in a sequence-specific manner to the rhodopsin promo... |
P54846 | MAFPPSPLAMEYVNDFDLMKFEIKREPSEGRSGVPTASLGSTPYSSVPPSPTFSEPGMVGGGEAPRPGLEELYWLATLQQQLGSDEVLGLSPDEAVELLQNQGPVSMEGPLGYYSGSPGETGAQHVQLPERFSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLTSGGPGSDDHTHLFL | Function: Acts as a transcriptional activator which regulates the expression of several rod-specific genes, including RHO and PDE6B. Functions also as a transcriptional coactivator, stimulating transcription mediated by the transcription factor CRX and NR2E3. Binds in a sequence-specific manner to the rhodopsin promote... |
Q9VMA0 | MELVKRGFLRACKNHSYLSFELIDDILAPLCANHKTTKPGSKEAIRALVAEINDTISDLGQLLVFIKYPVKAEEYLVYAKTDATPDSVANTGLTAEECQYFSKLLDKIASEEDCHIAWNDAYNDIVLQASSKPLKKSRMQELLQKWIQMGYFMEVTDRIYLGPRSLVELSFYLSSNHADNIKNCTLCKCLVLWDIRCGSCNIQYHRGCIQTYLQRRDICPSCGNLWTTPIRRSIG | Function: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination . The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (By similarity).
Catalytic Activity: S-ubiquitinyl-[E... |
Q8WV22 | MQGSTRRMGVMTDVHRRFLQLLMTHGVLEEWDVKRLQTHCYKVHDRNATVDKLEDFINNINSVLESLYIEIKRGVTEDDGRPIYALVNLATTSISKMATDFAENELDLFRKALELIIDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQNKWLIEKEGEFTLHGRAILEMEQYIRETYPDAVKICNICHSLLIQGQSCETCGIRMHLPCVAKYFQSNAEPRCPHCNDYWPHEIPKVFDPEKERESGVLKSNKKSLRSRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity... |
Q9D720 | MQGSTRRAGAMTDVHRRFLQLLMTHGVLEEWEVRRLQNHCYQVHDRNATVDKLEDFINNINSVLESLYIEIKKGVTEDDGRPIYALVNLATTSVSKMATDFAENELDLFRKALELIVDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQSKWLIEKEGEFTLHGRAILEMEQFIRESYPDSVKMCNICHGLLIQGQSCETCGIRMHLPCVAKYFQSIPEPHCPHCNDYWPHDIPEVYNPEKEREAGISKSSRKSLRTRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity... |
Q5RAZ5 | MQGSTRRMSVMTDVHRRFLQLLMTHGVLEEWDVKRLQRHCYKVHDRNATVDKLEDFINNINSVLESLYIEIKRGVTEDDGRPIYALVNLATTSISKMATDFAENELDLFRKALELIIDSETGFGSSTNILNLVDQLKGKKMRKKEAEQVLQKFVQNKWLIEKEGEFTLHGRAILEMEQYIRETYPDAVKICNICHSLLIQGQSCETCGIRMHLPCVAKYFQSNAEPRCPHCNDYWPHEIPKVFDPEKERESGVSKSNKKSLRSRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity... |
Q53EK2 | MEKERQDGLSDKHKFILQYIMCRTAGVDNEQVRELVQEQYGETATVEDVINELNNSLHNFDFKIKRVQDQLDGRLTLHFQNLSGDPVSQMATPYPPVQIELMRKIIEWIMKCDDYQYSLTTLQIQKLSRKEMGLAPSVIESHLHTFERDGWLRQREGIWTFTNHALAELDAYLHNEYESNLYECNACREIVIAGYVCDCGYCLHVYCCKHLAHVNCINCNTPWANATVIGRW | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role ... |
Q6PAF4 | MADRINESHQRFLQALMSHGIMEGSAVRALHRHCCELHKVHYMHDKLDDFVGVLNRHLQPLFMTIEKGVGEEDGLTYYALVNRVENDITKMASDYAENELELFRKTMELIILSDNGFATSISILNLADELQSKKMKKKEVEQLLQSFVQEKWLIGRNGEYTLHTRCIMELEHYIRNTYQDVAKICNVCRKVAIQSQLCENCGIPLHLQCAGKYFHGKANPTCPNCNESWPHEIPDLNQVSSQGPSHSQTETVRGRNQRSKNTSTASRTSR | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity... |
Q07913 | MEVHEEQVSAPVTGDATAKYLLQYILSARGICHENALILALMRLETDASTLNTEWSIQQWVDKLNDYINAINVKLNLLGYKIIRINHGIGRNAVTLKAKQNFESFEDNTAIRAHNNDYAVLQSIVLPESNRFFVYVNLASTEETKLATRFNQNEIEFMKWAIEQFMISGETIVEGPALETSIIVKEVNRILVAATGDSNLAKWRKFSTFTVGSTNLFQFQELTATDIEDLLLRLCELKWFYRTQEGKFGIDLRCIAELEEYLTSMYNLNTCQNCHKLAIQGVRCGNESCREENEETGENSLSQIWHVDCFKHYITHVSKN... | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Catalytic Activity: S-... |
Q8GYH7 | MASASSSDGVAGRIQNASLVLVSDNSSTLADIRKAVAMMKNIAVQLEKENQTDKVKDLENSVAELLDLHSDCNHRSTAIQSVANRYQPVEQLTDFKKLLDDEFTKLKATPSSVPQNDHLMRQFREAVWNVHHAGEPMPGDDDEDIVMTSTQCPLLNMTCPLSGKPVTELADPVRSMDCRHVYEKSVILHYIVNNPNANCPVAGCRGKLQNSKVICDAMLKFEIEEMRSLNKQSNRAEVIEDFTEDVDED | Function: E3 SUMO-protein ligase that modulates cell cycle progression and functions as a repressor of endocycle onset in meristems. May function downstream of the meristem patterning transcription factors PLETHORA 1 and 2 (PLT1 and PLT2) in root meristem development. Modulates the expression of the mitotic cyclins CYC... |
Q32KY9 | MPGRSTSSSSSGSTGFISFSGVESALSSLKTFQSCISSGMDTASSVALDLVETQTEVSSEYSMDKAMVEFAMMDRELNHYLKAVQSTINHVKEERSEKIPDLKLLVEKKFLALQNKNSDADFQNNEKFVQFKQQLKELKKQYGLQSDREADITEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKVCGHTYEEEAIVRMIESKHERKKKACCPKIGCSHVDMRMSDLIQDEALRRAIESHKKRRRQSN | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to dou... |
Q96MF7 | MPGRSSSNSGSTGFISFSGVESALSSLKNFQACINSGMDTASSVALDLVESQTEVSSEYSMDKAMVEFATLDRQLNHYVKAVQSTINHVKEERPEKIPDLKLLVEKKFLALQSKNSDADFQNNEKFVQFKQQLKELKKQCGLQADREADGTEGVDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKKKAYCPQIGCSHTDIRKSDLIQDEALRRAIENHNKKRHRHSE | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination . Is not be required for the stability of the complex . The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to d... |
Q91VT1 | MPGRSSTSSGSTRYISFSGIESALSSLKNFQSCISSGMDTVSSVALDLVETQTEVSSEYSMDKAMVEFAKMDRELSHYVKAVQSTINHVKEERPEKVPDLKLLVEKKFLALQDKNSDADFKENEKFVQFKQQLRELKKQYGIHADRENDLTEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKMCGHTYEEEAIVRMIESKHKRKKKACCPKIGCSHTDMRMSDLIPDEALRRAIESHNKKKKRHSE | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to dou... |
Q4PIR3 | MSEAQLKTSLEALSQNLLPGNQNHCSFDFQLKEIDDSIKQVIKCALVAAEIKNNECLDMLDSGIRELLDAKQRLLLMQQSVDTLANKTSENISDFENKSLLDIYTQIFKELIQEYEEKSDYGKYGTQGEYIEFKKTIWHEQNTDGSDFPSMKTFFNVMNTEEQEADEVMVYSATFDNRCPLTLQPIVHPILSTACNHFYEKDAILSLLNPTCVCPVVGCEARLQRSLLKEDEILERRLRRAQEISNLKEA | Function: Acts as an E3 ligase mediating SUMO/Smt3 attachment to other proteins. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand brea... |
Q7ZXH2 | MSGRSAPVVSFSSVDNSLSSLKNCQGYLHTGMDITVSVALDLLETGCESTEVDAMESVMLEYSAMERDLKQYIHAVEETVQKLRREQMEQVPDLQSLVQEKYATIQKKNDDEDLKKNDRFVQFKDQLREMRKQMGEKEEGDAAFENVDEDIAVLPSQQNLTCPITQMEMTNPVKNKVCGHTYEKEAIERMIQDRHQKKKRVKCPKVGCVHSDMQISDLVPDTALKRTIDILNKQKGRH | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to... |
P38632 | MALNDNPIPKSVPLHPKSGKYFHNLHARDLSNIYQQCYKQIDETINQLVDSTSPSTIGIEEQVADITSTYKLLSTYESESNSFDEHIKDLKKNFKQSSDACPQIDLSTWDKYRTGELTAPKLSELYLNMPTPEPATMVNNTDTLKILKVLPYIWNDPTCVIPDLQNPADEDDLQIEGGKIELTCPITCKPYEAPLISRKCNHVFDRDGIQNYLQGYTTRDCPQAACSQVVSMRDFVRDPIMELRCKIAKMKESQEQDKRSSQAIDVL | Function: Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5 and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand brea... |
Q9Y7U4 | MSQLSFTGKSSSKGRSRLTQEVRPTASQIIADEEASDLDEYEEDLEGSGNEDDFGPSMSRSSRGRKRRKGDPLELQSQFEERNETDAINFQLLVRNVVRYAICSQTSHNTITRKDIVQKAFPEGTSRNLFQSVFEEADRQLQLSFGFRLVAVTQSNRKKDMAVSQLRRPATSNANSSNLHRYWVLRSTLPMELQKDSRLIVDSVLDTAYYGFLMTVIAFIAVSHCSVGHSELQSFLQELLTEEETTPLHLDITRSLSLLVRQGYLDRVKDDTHNQFVYYIGSRAVTEISIEGLKSFVTEFFPDSDIDMDALLTEYRQEYQ... | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role ... |
P03535 | MDKLADLNYTLSVITSMNDTLHSIIQDPGMAYFLYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVIKYCIVTIINTLLKLAGYKEQVTTKDEIEQQMDRIVKEMRRQLEMIDKLTTREIEQVELLKRIHDNLITRPVDVIDMSKEFNQKNIKTLDEWESGKNPYEPSEVTASM | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associate... |
Q45UF1 | MEGTSESPVLDEFEVNNNDYDNDFISRFSQNPLNAFSLFTDGNLQEYFMNNSLEKIVIHVVLIVISLCGIKAQTSKIIYVVRLLFWKIYNVINNLVNKVINREKIINHQVVDNRFREFEERFRLLLLQHDKNIAKQDDIVQYNKLDNFAESIKSEFNLKVAEMERRFQELKWRCDMIANKAMNTIVLANTVDSNNKDEKIVFDEGSVVQYNRE | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associate... |
Q9YS17 | MEFINQTFFSDYSEGKIDTIPYALGIVLALTNGSRILKFINLLISLLRKFIITSKTVIGKFKIENNTSHQNDDIHKEYEEVMKQMREMRVHVTALFDSIHKDNMEWRMSESIRREKKREMKASTAENEVKIHTNDVNICDTSGLETEVCL | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associate... |
Q9NPB1 | MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRARFPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMASLQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDITGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC | Function: Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Sequence Mass (Da): 25862
Sequence Length: 228
Subcellular Location: Mitochondrion
EC: 3.1.3.... |
Q8CHQ9 | MAAYHIRQYQEKDHKRVLELFSSGMKELIPAAIRQMLTLPHSLLLLPGVPVTIVLMSASWLLATLYSFLFLLCLWLIFWISCRNYVAKSLQADLADITKSYLNAHGSFWVAESGDQVVGMVGAQPVKDPPLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLQFARDQGYSDVVLETGSVQHSAQALYQAMGFQKTGQYFVSISKKLMGLSILQFSYSLPFASGPGYSGKYLKKGPIPC | Function: Probable acetyltransferase (Probable). Has no detectable histone acetyltransferase activity towards histone H3 or H4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26424
Sequence Length: 238
Subcellular Location: Membrane
EC: 2.3.1.-
|
Q9JIY8 | MAPYHIRKYQDSDHRSVVDLFRRGMEEHIPATFRHMLLLPRTLLLLLGVPLTLFLASGSWLLVLLSILTLFLSLWFLAKYTWEKHVMNCLHTDMADITRTYLSSHSSCFWVAESRGQTVGMVAARPVKDPLLQKKQLQLLHLSVSLQHRREGLGKAMVRTVLQFAQMQGFSEVVLSTSMLQYAALALYQGMGFQKTGETFYTYLSRLRKSPMINLKYSLTSREGDL | Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25956
Sequence Length: 226
Subcellular Location: Nucleus membrane... |
Q9QXS4 | MAPYHIRKYQDSDHRSVVNLFCRGTEEHISASFRYMLLLPGTLLILLGVPLTLFLASGSWLLVLLSTLTLLVSLWLLAKYPWEKYTAMCLHSDMADIPRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDPLLQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEFFYTFVSRLRNSPMICLKYCLTSALNDLKT | Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26038
Sequence Length: 228
Subcellular Location: Nucleus membrane... |
O60178 | MKFGCVQFFPKLGKVNENIVHLRQLLDQHSEALQSVKLLVFPEMCLTGYNFKNSESIQPFLENVTSNHCPSIQFAQEVSEQYRCYTIIGFPEFQNSNGISTLYNSTALISPKKELLNVYHKHFLFETDKSWATEGKGFSFEPCIPELGPISMAICMDINPYDFKAPFEKFEYANFILRELEHQQMVSSNVSRPIICLSMAWLVSDDKVIDASLPDIKNLHYWTTRLSPLINSNTDAIVLVANRWGKENDLNFSGTSCIMELSQGRAILHGVLKAAENGIVVGELEK | Function: Deamidates N-terminal Asn and Gln. Component of a targeting complex in the N-end rule pathway (By similarity).
Sequence Mass (Da): 32427
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 3.5.1.-
|
P54989 | MGANKQMNLGFLFQISGVHYGGWRYPSAQPHRATDIQYYAEIVRTAERGKLDFCFLADSIAAYEGSADQQDRSKDALMAAEPKRLLEPFTLLAALAMVTEHIGLVTTATTTYNEPYTMARLFASLDHITNGRAGWNVVTSANLAEAHNFGRDGHVEHGDRYARAEEFINVVFKLWDSIEDGAYLRDKLAGRYGLSEKIHFINHIGEHFKVRGPLNVPRPPQGHPVIVQAGSSHPGKELAARTAEVVFTAQQTLADGKAFYSDVKGRMAKYGRSSENLKVLPGVVVYVAETESEAKAKYETVSNLVPPDFGLFMLSDLLGE... | Function: Hydroxylation of nitrilotriacetate.
Catalytic Activity: FMNH2 + nitrilotriacetate + O2 = ammoniodiacetate + FMN + glyoxylate + H2O
Sequence Mass (Da): 50529
Sequence Length: 453
EC: 1.14.14.10
|
P54990 | MADQIRSATEGGDPTSDPKGFRRALGTFPTGVTIVTAPGVDGPAGVTANSFASVSLDPPLVLWSIGHTSRSHSKFQQSATFAINILADDQVGVSQVFAGGSADKFSLVDWHTGRTGAPLIDNALAYFDCVCEARHEGGDHTIMIGRVVDFGRAEGSPLAFSQGRYGVTLDHPEAAKARDHKSEEYGLDDLPFLSLIAKAHYKEDADLEEQRSAAGCTPVGSKILAGLYGSAPLTADELARRMYLDRREVVDSLNEFVADGHVESCDSGRFALTESGKQRRRRMIEYVSRYQDEQLASISRSDLGVATRVLQAFLAGPGRG... | Function: Catalyzes the NADH-dependent reduction of the FMN cofactor of the nitrilotriacetate monooxygenase subunit A.
Catalytic Activity: FMNH2 + NAD(+) = FMN + 2 H(+) + NADH
Sequence Mass (Da): 34496
Sequence Length: 322
EC: 1.5.1.42
|
Q5S7W5 | MAQPELLWAAAGLMLLGVAVSACVRCQLYATKRGKDGSQGSRLERPQRFEVIRSCSAVTRRPERIKEPEHLARKAPEELSTSCHVGFESSAEPRYQNFLTEDCLHEDAAYVEPVPLDYYSHNRFFSPPNDEDSHSYQNVIIGDPCSSELDDAEDYENSTAIEVWKVQQAKAMLYAESQDEEPDYVNTDPTIDAVVLSK | Function: Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells. May also be involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these ... |
Q9GZY6 | MSSGTELLWPGAALLVLLGVAASLCVRCSRPGAKRSEKIYQQRSLREDQQSFTGSRTYSLVGQAWPGPLADMAPTRKDKLLQFYPSLEDPASSRYQNFSKGSRHGSEEAYIDPIAMEYYNWGRFSKPPEDDDANSYENVLICKQKTTETGAQQEGIGGLCRGDLSLSLALKTGPTSGLCPSASPEEDEESEDYQNSASIHQWRESRKVMGQLQREASPGPVGSPDEEDGEPDYVNGEVAATEA | Function: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these ... |
Q9JHL0 | MSAELELLWPVSGLLLLLLGATAWLCVHCSRPGVKRNEKIYEQRNRQENAQSSAAAQTYSLARQVWPGPQMDTAPNKSFERKNKMLFSHLEGPESPRYQNFYKGSNQEPDAAYVDPIPTNYYNWGCFQKPSEDDDSNSYENVLVCKPSTPESGVEDFEDYQNSVSIHQWRESKRTMGAPMSLSGSPDEEPDYVNGDVAAAENI | Function: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these ... |
O64876 | MIYVGGVQFLDESSSFSLSSSSQGSSLLVDVMSHPVITLASDSFKNLEEKNVSFDESDSESSTKDRYVYIFQREFAVVNPALVDFVGTDEATTCVGLVIRNRKSGMTSVAHMDSPEIVDLGISQMLLLVLQDDVDAELDVHMVGGYEDVDIKNADGVGDYAKPEGYSFPLCCKLVETLQKRRENFHIQTLFILGHNTKLDSQANTCPIFNGCLVNTSTGAILPASFNRTSRCPDEIVRRIRVSSSFEDSSWKGKLLDTYDTKTDRFIIAPCRWTMRLIEYVWELNQLTDEEILTNCSTSPSAEGPDFVNSLRRNWGYLLK... | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by t... |
Q96AB6 | MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGS | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by t... |
Q64311 | MPLLVDGQRVRLPRSAVELVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQDDDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAGGPMISIYDAKTEQLRIGPCSWTPFPQVDFWLQQDDKQILESLSTSPLAEPPHFVEHIRSTLMFLKKFPSPENILFPGNKALLYKKNKDGLWEKISSPGS | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by t... |
Q9BV86 | MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR | Function: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala... |
Q8R2U4 | MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR | Function: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala... |
B8JM82 | MEFSGTHQAFRNRWAKTDDEMCKHSMSFHLHKTLRKEFFASYLYLLEQIPLVKLYALTCEYIKGEKQFYYRAQNFYKDVPPSEEGMMGDFVEISDIDLEGSRQFLKKFVGPGKAGTKCALDCGCGIGRVSKGVLFPVFESMEMLDMMEEFILHAHECYLGDYADRVESYYLYNLQEFIPPRKKYDVIWMQWVACHLTDKDLMEFLMRAKESLRPNGVIIIKDNMARQGCKLDPIDSSIIRHLDIMNGIIQRAGLNILDVEKQEGFPEAIVPVWMIAMR | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-L... |
Q5VVY1 | MAHRGAHFAFRSRWQKTDDELCRHSMSFILHKAIRNDFFQSYLYLLEKIPLVKLYALTSQVINGEMQFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFVGGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEAQNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNVAREGCILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFALHSDRHS | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-L... |
B2RXM4 | MAHLGAHFAFRSRWQKTDDELCRHSMSFILHKAIRNDFFQSYLYLLEKIPLVKLYALTSQVIDGEMQFYARAKLFYQEVPATEEGMMGNFIELSNPDIQASREFLRKFVGGPGRAGTGCALDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSYLQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKDLLAFLSRCRDGLKENGVIILKDNVAREGCIFDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQEGFPEQCVPVWMFALHSDRHS | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-L... |
Q5PP70 | MDICGVDSEGKEFNSVQEMWREEIGEGDETKKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVNNVGANQHLVALDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPGGFFVVKENLAKNGFVLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALTVDTPPKIHRTRSKTRSNRPQIIK | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
Q9N4D9 | MSSSSSSRIHNGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNLFGYFDYALDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLKDNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALKPQHTGFTNN | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
Q55DH6 | MTIKNEEQQQQTNKLKYPKNLLSSGLDGEGNTYINIEDLWKKELEGKDNKMEDKWYKSADEYWKGVEATVDGMLGGLAQVSPIDVVASKVFIQDFIKGTDSRPPINLNLALDCGAGIGRVAKEFLLPIGFKNVDLVEQNKLFLDKAKSDNFKDDNRVENYYAVGLQDFTFEKKYDCIWIQWVIGHLHDLDFIEFLKKCMDSLTPNGIICIKDNCAKKRFIMDKEDNSVSRTEDHLKYLFDQAGCKLLKSMVQPNFPKELFPVLMFALERK | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
Q6NN40 | MTTTLEEQLSDKLQMMDETTDKVQGSSKQKDDSSIAASSDAKTASPSSSDSSTKVAAPESEFYNKAQKYWSEVPATVNGMLGGLGYISAIDIQGSNVFLREIRVPGNRLALDCGAGIGRVTRNLLIPRFSCVDLVEQDPAFADKAREYCTSEDGSRGKVGQIYNVGLQKFTPTQQYDLVWTQWVLGHLTDRDLVSFFRRIKQGLAPGAFLCLKENVSSSKKTVEDRNDSSVTRPLDSYEHFLKEAGFRIVRKVKQQNFPKGLFPVYMIACKPVSKE | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
Q10CT5 | MDSRGFDSEGREFSSATEMWAHEIGAAADAPVSAAVAEPAPAPAAGSNGVAGEEEAGGGGKREEWYSKAIAYWQGVEASTEGVLGGYGCVNDVDVKGSDAFLRPLLAERFGAARRHLVALDCGSGIGRVTKNFLLRHFNEVDLVEPVSHFLEAAQENLTECMEVGEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFVLKENIARNGFVLDKEDNSITRSDAYFKELFKKCGLYIHSIKDQSDLPKELFAVKMYALVTEKPKIQKNGKRRRPKNSPRMIRS | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
O13748 | MDPEKFYSDAIDYWNGVQPTVDGMLGGLGTGRIPQTDVVGSRTFLNRLNYRIGKIENLVAADCGAGIGRVTENVLLKIASHVDLVEPVENFISTAKKQLATKPCSFINVGLQNWTPEKNRYGLIWNQWCLSHLTDEDLIAYLSRCCEAIQEKGVICVKENVSSFEDTFDPIDSSVTRCEQSLKSLFKKANLVVVAETLQHGFPEELFPVKMYALVPHSS | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
P38340 | MDVPADSHIKYEDAIDYWTDVDATVDGVLGGYGEGTVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHVELAELKDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNGTIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALKPMPN | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- ... |
Q7NH22 | MTVRLLLASASPRRRELLSQIGVAFEVKPSAFEERMDPALPPEQLVVQNALGKALNVQKRAPAELILGADTVVVFNRRIYGKPTGPADAGRMLGELQGQWHTVYTGIALVEERRWRVAERATRVKLRAMTPAQIAAYVAGGEPLDKAGSYAIQGLGAALVEQIDGCYSNVVGLSLPLLVDLLAEFDRRVF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20692
Sequence Length: 190
... |
Q5FS71 | MTASPSSAEGSSGLPDRPKLVLASASPRRLSLLEQIGIVPDAVVSADIDEEPRPGELPRPLAQRLARQKAEHVAAQRTDAALVLGADTVVSVGRRVLPKAEDEKTARACLKLLSGRRHKVLTAVVLRPSAGWPQGTPCERLVETSVIFHRLTDAQIDALIAQGDWQGKAGGYAIQGAAAAHIRQIGGSYSAVVGLPLFETAQLLRGQPVGKPSGGWIA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22919
Sequence Length: 218
... |
Q0BTC5 | MMPDQPATACPLVLASASPRRAALLAQIGVIPALTLATDIDETPLKGEVPLKGEVPRLLSRRLAQGKADTAIRVLREQSDAPLAAPFILAADTVVAVGRRALPKAETEAEARQCLTLLSGRRHHVWTTVVVIAPDGKRAERIVESAVTFNRMTDLQQEAYIASGEWRGKAGGYAIQGLAAAYIRFLSGSYSNVVGLPLFETAQLLRGLGFRSL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22807
Sequence Length: 213
... |
Q2SBH1 | MFDGNPGRRRLVLASGSPRRREMIAGLGCEFSIASADIDESVRPSEAAADYVERLAKEKATAVFEARGDQQDIVVLGADTTVVAGGDILGKPVDFDDAKAMLRRLSGTWHEVLTSVALVAAEGCKVTTTLSRVRFRELSEQEIQRYWDSGEPADKAGAYGIQGLAGSFVERVEGSYSSIVGLPLCETVVLLKEFGIKIWSD | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21715
Sequence Length: 201
... |
Q9K8H3 | MKPLILASGSPRRKQLLEQMNVPFTVCKSTIDETFDPTFPPDEVVQQLARQKAQDVAKKHEDSFILAADTIVVFQGRILGKPATEQEARQMLSQLSDQSHEVLTGVALLHQGQVETFVETTEVRFWPLTDTEIETYLQTGEPFDKAGAYGIQGLGAYLVKELKGDYYNVVGLPLSRTVRALKVHGFSTRF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21240
Sequence Length: 190
... |
Q31FH4 | MKRRLYLSSSSPRRKELLDQAGIPFDLVNAPVEETGLPNESPESFVLRMAVEKALSGFNKVPGKNVWVLGSDTIILKDGKVFGKPKHKMDAYRMLMSFSGEEHTVMTSIAIVNDGAVYSDVCQTNVFFRPISDSEFEQYWATGEAEDKAGAYGIQGQAAKFIEKIEGSYSAVMGLPLYELDKLLRESNFYSE | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21408
Sequence Length: 192
... |
Q0C2H1 | MPGSAPLILASASPRRLELLAQIGIVPDRVAPTDIDETRRKAESPRELALRLAREKAAACDAEGAFVLAADTVVALGQRNLEKAADETEAADFLRLLSGRAHQCITGVAVRAPSGQIVSRAVLARVKMKRLTEAEIAAYVASGDWKGKAGGYGIQGAAGGFVTAINGSYTAIVGLPLYETKSLLEGLGYRR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20071
Sequence Length: 191
... |
Q5QWE2 | MRLLLASSSPRRRELLTLLHRPFDCEVPEVEELRGANENAGDYVTRLAEEKAQTVAQRQQTPCLVIGSDTLISFKGQVLEKPESYEHFSQMMKQLSGQTHQVLTSVSVCQWNGHKVVARETALVTTQVEFAALSQGEIDAYWATGEPHDKAAGYGIQGYGGKFVKRIEGSYFAVVGLPLYETEQLLRMFEMTGEVDER | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22184
Sequence Length: 198
... |
Q1IV55 | MLRYNLGMGLILASASPRRSELLRKARMVFRVEPAHVPEVHTAGEDPKQYAQRLARDKARAVAAKYPNDFVIGADTIVVADAHVLEKPADEADAARMIRMLSGHTHEVTTGVCLCGPNVEIVETETTRVTVAEISDEEIADYIHTGEPMDKAGAYGIQGMFSRWVTGIEGDYFNVVGLPIARVYRMMRRAGVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21268
Sequence Length: 193
... |
A9KHL6 | MYQIVLASGSPRRKEILSQVGINFTVCVSNMEEITSETLPENIVMELSKMKAHDIAKQYETNTIIIGSDTIVAYKNQILGKPKNEDHAKEMLQLLSGVTHEVYTGVTVIIKNDSGEVEERTFFEISKVTVSDLTEEEIMDYIKSKEPMDKAGAYAVQGRFAAHVTRIEGDYYTIVGLPIARLYQEVKKFGIDLVKQM | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22171
Sequence Length: 197
... |
Q38YR2 | MFILASQSPRRQALLKRVVNDFEVQPAQIDEHETPLTAPGDYVQTLAQRKGEAVAVQYPTATILAADTAISFQGTLYGKPKDRQDAYEMLRQLSGQTHQVYTGLWLMKDGLVQQKVVQTDVTFWHLSTAEIEQYLDQNEYADKAGAYGIQGAGALLINKVNGDFYNVVGLPVSTVARMLQN | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20092
Sequence Length: 181
... |
Q1MQH1 | MTQQRVSSVFIETVPIVLASASPRRRSLLEQLGLLFKIVSVDSEPLPLSSEHPLEYVIRAAKVKAFAAAALEPRSVIIAADTVVIYTKDDVFEIIGKPQSGNDSFSMLSRFQGGKHQVITGCCIVWPLEENITSVQYEIFYDTASIQFGQWDKDILSSYVSTGESNDKAGAFSIQGIGAFLIDIIEGNYTTILGLPLPQLVKRLLKRKAIKVVLNKNSEETISSDFLTYSR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 25506
Sequence Length: 231
... |
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