ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q3A247 | MKSPAPYIDHTLLKADATSAQIRQLCLEAAHWQFASVCIPPRFVSEAVACLADSQVAVGTVVGFPLGYDTAAVKRAATAQAVAEGVDEIDMVIPLGAALEGRLDMVREDVIGVLDAAAGRLVKVIIECCYLENARKVELVELLAEAGADYVKTSTGFAVSGAAEADIRLLHQAAGGRIKVKAAGGVRDWETCRIMLKAGAHRVGTSNGVQIIQQWQEAPEL | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23380
Sequence Length: 221
Pathway: Carbohydrate degradation;... |
Q5N4L8 | MAELSSDFDLAPYIEHSLLDPAATLEQIDQLCQEADRYHFAAVCLFPWVVRQAREWLNGRSPRLCTVIDFPNGASTAASKVYAAQEAVENGAQELNVVVNLGWLRSDRADLVHQELAEIVEATGVPIKAILEATRLNPSELEQLTDLCLDAGVTMLQTSTGWFGGATPALVQQLRQLTRNRVGIHAAGGIRTWDQAAALVEAGAIRLGTSYGPMILQQRLAASTPAPA | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24659
Sequence Length: 228
Pathway: Carbohydrate degradation;... |
Q9HKB7 | MKYSIEQVMRLVDHSGLKPYLTEKDIARLIEEAKDMGNYAVCIEPIYGKFAKEYLDEKRYKVKLDVTIDFPFGSLATSSRKKIIEDSDYADEVDIVVPMGYVKSHRWDYVDQDLTDVVKIAKDHDLVIKIITEDGYLTQDEKDRLYRSVIRAKPDFIKTSTGFANKDYCASLGNAAGATPDNVSLMSRIAEELGSDIGIKAAGGIHTYREIESIIDAAKRPIDPEKLRIGMSGTGKVFEEMKKIKK | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 27759
Sequence Length: 246
Pathway: Carbohydrate degradation;... |
C5A366 | MVGMDIAKYIDHTNLKPYATKEDIIKLCDEAIQYGFYAVCVNPYRVKLAKEYLSEKKADVKVASVIGFPLGATPTEVKVFEARKALEDGADELDMVINIGALKDGDYDYVKRDIEEVVKVAHEKGAKVKVIIETCYLTEEEKIKACELAKEAGADFVKTSTGFGTGGATVEDVRLMRKVVGPEMGVKAAGGIRTYEQALAMIEAGANRIGTSSGVRIVEGARNAE | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24420
Sequence Length: 225
Pathway: Carbohydrate degradation;... |
Q877I0 | MNKREIARYIDQTNLKPYATKEDIIKLCDEAIEYGFYAVCVNPYRVKLAKDYLREKNADVKVASVIGFPLGATPTEVKVFEAKRALEDGADELDMVINIGALKDKDYEYVKNDIAEVVKVAHERGAKVKVIIETCYLTEEEKVKACELAKEAGADFVKTSTGFGTGGATVEDVRLMRKVVGPEMGVKAAGGIRTYEQALEMIEAGANRIGTSSGVKIVEGAPDE | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Could be involved in pentose biosynthesis.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24506
Sequence Len... |
Q9X1P5 | MIEYRIEEAVAKYREFYEFKPVRESAGIEDVKSAIEHTNLKPFATPDDIKKLCLEARENRFHGVCVNPCYVKLAREELEGTDVKVVTVVGFPLGANETRTKAHEAIFAVESGADEIDMVINVGMLKAKEWEYVYEDIRSVVESVKGKVVKVIIETCYLDTEEKIAACVISKLAGAHFVKTSTGFGTGGATAEDVHLMKWIVGDEMGVKASGGIRTFEDAVKMIMYGADRIGTSSGVKIVQGGEERYGG | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 27285
Sequence Length: 248
Pathway: Carbohydrate degradation;... |
B0KA53 | MNIAKMIDHTLLKPNATKSEIEKLCNEAKEYGFASVCINPCFVDLAYSMLKDTDVKVCTVIGFPLGANTIESKVFEAVDAVKRGATEVDMVLNVSMLKSGDYDYVKKEIEEVVKAVKSYGDIVVKVILETCYLTDEEKVKACQLTREAGADFVKTSTGFGPGGATVEDVKLMRQTVGENFGVKASGCVRTAEDAKAMIEAGANRIGASAGVKIAEEWNKLKMS | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24114
Sequence Length: 223
Pathway: Carbohydrate degradation;... |
P02540 | MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQ... | Function: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mito... |
B0L3A2 | MTMFKGSNEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRELEIFIVLTDVPNYRLIKENSHLHTTIVDQGRTV | Function: Dual receptor for both endothelin-1 and the signal sequence of vascular endothelial growth factor A . Does not act as a receptor for angiotensin-2 . Does not bind the VEGFA mature protein (By similarity). May play a role in angiogenesis with a significant role in cardiovascular and neural development (By simi... |
Q2QKR2 | MNALYVTTVPKGYSSLSKCNHNEQDTAYRLWLCTHNHWTAPSGMRLQPLTSLGSKEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRGIGHITNSYKRPQAPAWPCLSSGTMGRSH | Function: Dual receptor for both endothelin-1 and the signal sequence of vascular endothelial growth factor A . Does not act as a receptor for angiotensin-2 (By similarity). Does not bind the VEGFA mature protein . May play a role in angiogenesis with a significant role in cardiovascular and neural development .
Locati... |
O34723 | MISIFIAEDQQMLLGALGSLLNLEDDMEVVGKGTTGQDAVDFVKKRQPDVCIMDIEMPGKTGLEAAEELKDTGCKIIILTTFARPGYFQRAIKAGVKGYLLKDSPSEELANAIRSVMNGKRIYAPELMEDLYSEANPLTDREKEVLELVADGKNTKEIAQELSIKSGTVRNYISMILEKLEVKNRIEAITRSKEKGWFK | Function: Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase.
PTM: Phosphorylated by DesK.
Sequence Mass (Da): 22177
Sequence Length: 199
Subcellular Location: Cytoplasm
|
Q8BVC1 | MKSLLSTLVIIMFLAHLVTGGWYVKKCANTLGNCRKMCRDGEKQTEPATSKCPIGKLCCVLDFKISGHCGGGGQNSDNLVTAGGDEGSSAKASTAAMVGAAAMAGTPTKTSAPAKTSAPAKTSTTTKASNAAKASTTTKASNAAKASAATMAGNTTKVSTAAIASTPAQASTPTKANST | Function: Probable component of sperm glycocalyx. Likely protects and facilitates transport of sperm in the female reproductive tract. Probably released from the sperm surface during capacitation.
PTM: O-glycosylated; glycans contain alpha(2,3)-linked sialic acids.
Sequence Mass (Da): 17709
Sequence Length: 179
Subcell... |
Q8WYQ5 | METDESPSPLPCGPAGEAVMESRARPFQALPREQSPPPPLQTSSGAEVMDVGSGGDGQSELPAEDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGAERDVRAECGLLLSPVSGDVHACPFGGSVGDGVGIGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGAGGFTAKAIVQRDRVDEEALNFPYEDDFDNDVDALLEEGLCAPKKRRTEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYL... | Cofactor: Binds 1 heme group per homodimer.
Function: Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to re... |
Q8EGF8 | MDFGLATTLYPDEYNYQTDAYSPTSSPVDLVQVIQQLHASLDPRTVFACYGKVLGQHLPIQGVRLQSEQHKLSWGKRYGISLKRQIICGGTPLTLQYQLLTPLTPSQSICLQEIEPLLLQPLLNAMQYQEMSMQAMFDALTGLGNRHYYSQSLKNAVARAQRKQGSVSLIVLDLDNFKKLNDKYGHKCGDYILKEFGDIIRSSIRSTDQAFRIGGDEFVVIVQGNIHAAGLLCERIVSATNTHASFHQFGVSCSLGAAEASETMEAEQLYEQADKTLYQAKASGRNCYKLSPTQLS | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules . May be involved in the regulation of formation of solid surface-associated biofilms and pellicles according to environmental conditions .
Catalytic Activity: 2 GTP = 3',3'-c-... |
P75908 | MEKDYLRISSTVLVSLLFGLALVLVNSWFNQPGVEEVVPRSTYLMVMIALFFIDTVAFIFMQLYFIYDRRQFSNCVLSLAFLSCLIYFVITVIIIQQIIEERLTSSVVQNDIAIYYLFRQMSLCILIFLALVNKVSENTKQRNLFSKKMTLCISLFFVFGGPIVAHILSSHYESYNLHIAELTNENGQVVWKASYVTIMIFMWLTLLSVNLYFNGLRYDIWNGVTVIAFCAVLYNISLLFMSRYSVSTWYISRTIEVVSKLTVMVIFMCHIFSALRVTKNIAHRDPLTNIFNRNYFFNELTVQSASAQKTPYCVMIMDID... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression leads to a strong repression of swimming; swimming returns to normal when residues 359-360 are both mutated to Ala. Overexpression also leads to a 20-f... |
P31129 | MIKKTTEIDAILLNLNKAIDAHYQWLVSMFHSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQHMHNCGRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQTGRNRCMFIDEQNVINRV | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules . May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when re... |
A0A0H3AFM6 | MKNWLCQAVRGEPMIELNRIEELFDNQQFSLHELVLNELGVYVFVKNRRGEYLYANPLTLKLFETNAQSLLGKTDHDFFHDDQLSDILAADQQVFETRLSVVHEERAIAKSNGLVRIYRAVKHPILHRVTGEVIGLIGVSTDITDIVELREQLYQLANTDSLTQLCNRRKLWADFRAAFARAKRLRQPLSCISIDIDNFKLINDQFGHDKGDEVLCFLAKLFQSVISDHHFCGRVGGEEFIIVLENTHVETAFHLAEQIRQRFAEHPFFEQNEHIYLCAGVSSLHHGDHDIADIYRRSDQALYKAKRNGRNRCCIYRQST... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Involved in biofilm formation . Catalyzes the conversion of GTP to c-di-GMP .
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Sequence Mass (Da): 37183
Sequence Length: 321
Domain: The disordered N-terminal region is not required for diguanylate cyclase act... |
P16932 | MSLNDDATFWRNARQHLVRYGGTFEPMIIERAKGSFVYDADGRAILDFTSGQMSAVLGHCHPEIVSVIGEYAGKLDHLFSGMLSRPVVDLATRLANITPPGLDRALLLSTGAESNEAAIRMAKLVTGKYEIVGFAQSWHGMTGAAASATYSAGRKGVGPAAVGSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSGNLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLILDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAAIVTSAAIEERAHELGYLFYTTHVSDPLPAAVGLRVLDV... | Function: The dialkylglycine decarboxylase is of interest because it normally catalyzes both decarboxylation and amino transfer. It may be more properly described as a decarboxylating aminotransferase rather than an aminotransferring decarboxylase.
Catalytic Activity: 2,2-dialkylglycine + H(+) + pyruvate = CO2 + dialky... |
Q9S7D1 | MVKETLIPPSSTSMTTGTSSSSSLSMTLSSTNALSFLSKGWREVWDSADADLQLMRDRANSVKNLASTFDREIENFLNNSARSAFPVGSPSASSFSNEIGIMKKLQPKISEFRRVYSAPEISRKVMERWGPARAKLGMDLSAIKKAIVSEMELDERQGVLEMSRLRRRRNSDRVRFTEFFAEAERDGEAYFGDWEPIRSLKSRFKEFEKRSSLEILSGFKNSEFVEKLKTSFKSIYKETDEAKDVPPLDVPELLACLVRQSEPFLDQIGVRKDTCDRIVESLCKCKSQQLWRLPSAQASDLIENDNHGVDLDMRIASVLQ... | Function: Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes . Specific for alpha-glycosidic linkages . Responsible for the final assembly of galactolipids in photosynthetic membranes. Digalactosyldiacylglycerol (DGDG) provides stability to the photosystem I (PS... |
Q8W1S1 | MTNQQEQHIAIFTTASIPWLTGTAVNPLFRAAYLANDGERRVTLVIPWLTLKHQKLVYPNSITFSSPSEQEAYVRQWLEERVSFRLAFEIRFYPGKFAIDKRSILPVGDISDAIPDEEADIAVLEEPEHLTWFHHGQKWKTKFNYVIGIVHTNYLEYVKREKQGRVKAFFLKYLNSWVVGIYCHKVIRLSAATQEYPKSIVCNVHGVNPKFLEIGLRKLEQQKLQEQPFTKGAYYIGKMVWSKGYKELLKLLEKHQKELAELEVDLYGDGEDSEEIKEAARKLDLTVNVYPGRDHADSLFHNYKVFLNPSTTDVVCTTTA... | Function: Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes. Specific for alpha-glycosidic linkages . During phosphate shortage, involved in the biosynthesis of digalactosyldiacylglycerol (DGDG) which rescues the limitation of phospholipids (Probable).
Catalyti... |
Q8U671 | MKEHRHMTEKSPHSAFGDGAKAYDVPAFGLQIHTVEHGSGAPIVFLHGNPTSSYLWRHIFRRLHGHGRLLAVDLIGYGQSSKPDIEYTLENQQRYVDAWFDALDLRNVTLVLQDYGAAFGLNWASRNPDRVRAVAFFEPVLRNIDSVDLSPEFVTRRAKLRQPGEGEIFVQQENRFLTELFPWFFLTPLAPEDLRQYQTPFPTPHSRKAILAGPRNLPVDGEPASTVAFLEQAVNWLNTSDTPKLLLTFKPGFLLTDAILKWSQVTIRNLEIEAAGAGIHFVQEEQPETIARLLDAWLTRIAGN | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalytic Activity: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 34390
Sequence Length: 304
E... |
P59337 | MSKPIEIEIRRAPVLGSSMAYRETGAQDAPVVLFLHGNPTSSHIWRNILPLVSPVAHCIAPDLIGFGQSGKPDIAYRFFDHVRYLDAFIEQRGVTSAYLVAQDWGTALAFHLAARRPDFVRGLAFMEFIRPMPTWQDFHHTEVAEEQDHAEAARAVFRKFRTPGEGEAMILEANAFVERVLPGGIVRKLGDEEMAPYRTPFPTPESRRPVLAFPRELPIAGEPADVYEALQSAHAALAASSYPKLLFTGEPGALVSPEFAERFAASLTRCALIRLGAGLHYLQEDHADAIGRSVAGWIAGIEAVRPQLAA | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalytic Activity: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 34089
Sequence Length: 310
E... |
P59336 | MSEIGTGFPFDPHYVEVLGERMHYVDVGPRDGTPVLFLHGNPTSSYLWRNIIPHVAPSHRCIAPDLIGMGKSDKPDLDYFFDDHVRYLDAFIEALGLEEVVLVIHDWGSALGFHWAKRNPERVKGIACMEFIRPIPTWDEWPEFARETFQAFRTADVGRELIIDQNAFIEGVLPKCVVRPLTEVEMDHYREPFLKPVDREPLWRFPNEIPIAGEPANIVALVEAYMNWLHQSPVPKLLFWGTPGVLIPPAEAARLAESLPNCKTVDIGPGLHYLQEDNPDLIGSEIARWLPGLA | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes primary, secondary and cyclic haloalkanes (chain length > C4).
Catalytic Activity... |
P80472 | MIPAQFTYRRVSSVDEALAAVAEHGD | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: a quinone + an aldehyde + H2O = a carboxylate + a quinol + H(+)
Sequence Mass (Da): 2834
Sequence Length: 26
EC: 1.2.5.2
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P80704 | MYAFSYSTPRTLDEVSAAS | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: a quinone + an aldehyde + H2O = a carboxylate + a quinol + H(+)
Sequence Mass (Da): 2096
Sequence Length: 19
EC: 1.2.5.2
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Q38946 | MNALAATNRNFRHASRILGLDSKIERSLMIPFREIKVECTIPKDDGTLVSYIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVADIPYGGAKGGIGCSPRDLSLSELERLTRVFTQKIHDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEYGKSIQGLTFVIQGFGNVGTWAAKLIHEKGGKVVAVSDITGAIRNPEGIDINALIKHKDATGSLNDFNGGDAMNSDELLIHECDVLIPCALGGVLNKENAGDVKAKFIVEAANHPTDPDAD... | Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 44699
Sequence Length: 411
Subcellular Location: Mitochondrion
EC: 1.4.1.3
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P39633 | MSAKQVSKDEEKEALNLFLSTQTIIKEALRKLGYPGDMYELMKEPQRMLTVRIPVKMDNGSVKVFTGYRSQHNDAVGPTKGGVRFHPEVNEEEVKALSIWMTLKCGIANLPYGGGKGGIICDPRTMSFGELERLSRGYVRAISQIVGPTKDIPAPDVYTNSQIMAWMMDEYSRLREFDSPGFITGKPLVLGGSQGRETATAQGVTICIEEAVKKKGIKLQNARIIIQGFGNAGSFLAKFMHDAGAKVIGISDANGGLYNPDGLDIPYLLDKRDSFGMVTNLFTDVITNEELLEKDCDILVPAAISNQITAKNAHNIQASI... | Function: Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. W... |
P24295 | MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMP... | Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 49296
Sequence Length: 450
Pathway: Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 1/5.
EC: 1.4.1.2
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P29051 | MTMASKSDSTHDESGDEAADSTEPESALETARRQLYHAASYLDIDQNIVERLKYPKKVHEVTIPIERDDGTVEVFTGYRAQHDSVRGPYKGGLRYHPDVTRDECVGLGMWMTWKCAVMDLPFGGAKGGVAVNPKELSPEEKERLTRRFTQEIRDVIGPNQDIPAPDMGTDPQTMAWLMDAYSMQEGETTPGVVTGKPPVVGGSEGREEAPGRSVAIITQLVCEYYDQPLDETTVAVQGYGSVGANAARLLDKWGATIVAISDVNGAMYEPDGIDTASVPSHDEEPEAVTTYADTVISNEELLTLDVDVLIPAALGNVITK... | PTM: The N-terminus is blocked.
Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 47459
Sequence Length: 435
EC: 1.4.1.2
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P13650 | MNKHLLAKIALLSAVQLVTLSAFADVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGPDNQIWLTERATGKILRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYISGTFKNPKSTDKELPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLVIGPDQKIYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVLRLNLDGSIPKDNPSFNGVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNSDDEINLIVKGGNYGWPNVAGYKDDSGYAYANYSAAANKSIKDLAQN... | Cofactor: Binds 1 PQQ group per subunit.
Function: Oxidizes glucose to gluconolactone.
Catalytic Activity: a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone
Sequence Mass (Da): 52773
Sequence Length: 478
EC: 1.1.5.2
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P18173 | MSASASACDCLVGVPTGPTLASTCGGSAFMLFMGLLEVFIRSQCDLEDPCGRASSRFRSEPDYEYDFIVIGGGSAGSVVASRLSEVPQWKVLLIEAGGDEPVGAQIPSMFLNFIGSDIDYRYNTEPEPMACLSSMEQRCYWPRGKVLGGTSVLNGMMYVRGNREDYDDWAADGNPGWAYNDVLPFFKKSEDNLDLDEVGTEYHAKGGLLPVGKFPYNPPLSYAILKAGEELGFSVHDLNGQNSTGFMIAQMTARNGIRYSSARAFLRPARMRNNLHILLNTTATKILIHPHTKNVLGVEVSDQFGSTRKILVKKEVVLSA... | Function: Essential for cuticular modification during development.
Catalytic Activity: a quinone + D-glucose = a quinol + D-glucono-1,5-lactone
Sequence Mass (Da): 68434
Sequence Length: 625
Subcellular Location: Secreted
EC: 1.1.5.9
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P36234 | MSKKKILITWPLPEAAMARARESYDVIAHGDDPKITIDEMIETAKSVDALLITLNEKCRKEVIDRIPENIKCISTYSIGFDHIDLDACKARGIKVGNAPHGVTVATAEIAMLLLLGSARRAGEGEKMIRTRSWPGWEPLELVGEKLDNKTLGIYGFGSIGQALAKRAQGFDMDIDYFDTHRASSSDEASYQATFHDSLDSLLSVSQFFSLNAPSTPETRYFFNKATIKSLPQGAIVVNTARGDLVDNELVVAALEAGRLAYAGFDVFAGEPNINEGYYDLPNTFLFPHIGSAATQAREDMAHQANDLIDALFGGADMSYA... | Function: Active on hydroxypyruvate and glyoxylate.
Catalytic Activity: (R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH
Sequence Mass (Da): 35115
Sequence Length: 322
Pathway: One-carbon metabolism; formaldehyde assimilation via serine pathway.
EC: 1.1.1.29
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Q59516 | MTKKVVFLDRESLDATVREFNFPHEYKEYESTWTPEEIVERLQGAEIAMINKVPMRADTLKQLPDLKLIAVAATGTDVVDKAAAKAQGITVVNIRNYAFNTVPEHVVGLMFALRRAIVPYANSVRRGDWNKSKQFCYFDYPIYDIAGSTLGIIGYGALGKSIAKRAEALGMKVLAFDVFPQDGLVDLETILTQSDVITLHVPLTPDTKNMIGAEQLKKMKRSAILINTARGGLVDEAALLQALKDGTIGGAGFDVVAQEPPKDGNILCDADLPNLIVTPHVAWASKEAMQILADQLVDNVEAFVAGKPQNVVEA | Function: Plays a central role in assimilation of carbon. It converts hydroxypyruvate to glycerate as a key step in the serine cycle, and may also play an important role in C2 reactions, by interconverting glyoxylate and glycolate.
Catalytic Activity: (R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH
Sequence Ma... |
P15877 | MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRSKRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGAVAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRFSPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALDAASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLIAINAENGKLCETFANKGVLN... | Function: GDH is probably involved in energy conservation rather than in sugar metabolism.
Catalytic Activity: a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86747
Sequence Length: 796
Subcellular Location: Cell inner membrane
EC: 1.1.5.... |
Q75BS4 | MSEDWKKKLNIPKKDTRPQTDDVLNTKGNTFEDFYLRRELLMGIFEAGFERPSPIQEEAIPIALARRDILARAKNGTGKTAAFVIPTLEIVKPKVNKIQALIMVPTRELALQTSQVVRTLGKHCGISCMVTTGGTNLRDDIMRLNEPVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKSLVEQILSFLPQNHQSLLFSATFPLTVKEFMVKHLNKPYEINLMDELTLKGITQYYAFVEERQKLHCLNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQERNKVFHEFRQGKVRTL... | Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and m... |
A1CJ18 | MADALASQLSNTTLGEANSETKWKEQLNVPAKDARPQTEDVTATKGLEFEDFYIKRELMMGIFEAGFEKPSPIQEETIPVALTGRDILARAKNGTGKTAAFVIPTLERINPKSTKTQALILVPTRELALQTSQVCKTLGKHLGINVMVTTGGTGLMDDIIRLNDAVHILVGTPGRVLDLASKGVADLSECPTFVMDEADKLLSPEFTPVIEQLLSFHPKDRQVMLFSATFPLIVKSFKDKHMRNPYEINLMDELTLRGITQYYAFVEEKQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHARMLQ... | Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).
Cata... |
A2QY39 | MTDALASQLNNTTLGDASSDAKWKEQLNVPAKDARPQTEDVTATKGLEFEDFYIKRELMMGIFEAGFEKPSPIQEETIPVALTGRDILARAKNGTGKTAAFVIPTLERINPKSTKTQALILVPTRELALQTSHVCKTLGKHLGINVMVTTGGTGLMDDIIRLNDAVHILVGTPGRVLDLASKGVADLSECPTFVMDEADKLLSPEFTPVIEQLLSFHPKDRQVMLFSATFPLIVKSFKDKHMRNPYEINLMDELTLRGITQYYAFVEEKQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHARMLQ... | Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).
Cata... |
P36009 | MAANSNSRVASNHTSKKQKVRRNIHPFTNNTRIKRASKIVKFNDSGEGDHVSDQRSNKENVLTYKSLKSRASDLLKMRETLPVYQHKREIMSYIESNPVTVLIGETGSGKSTQIPQFVLEKLYDTKKHGSIAVTQPRRVAAINLATRVAQEHGCKLGEQVGYSVRFDNTTTTRTRLKYLTDGMLLRELMMNSDLREYSVIVIDEAHERTVLTDLILGFLKSLIQGPRPDLRIIVMSATLQAEKFSEFFNNAPILFVEGRKFDVKQYYLKAPTDDIVDAVIRCCIQINQGEELGDILCFLPGQEEIDKAVTIMEKIAKYVS... | Function: Probable ATP-binding RNA helicase. Required for 18S rRNA synthesis.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82713
Sequence Length: 735
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q96LJ7 | MAAPMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQGRLDVLVNNAYAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQDPVLKQFKSAFSSAETTELSGKCVVALATDPNILSLSGKVLPSCDLARRYGLRDVDGRPVQDYLSLSSVLSHVSGLGWLASYLPSFLRVPKWIIALYTSKF | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of steroids (estrone, androstene-3,17-dione and cortisone) as well as prostaglandin E1, isatin and xenobiotics in vitro . May have a role in steroid and/or xenobiotic metabolism .
Catalytic Activity: 17alpha-estradiol + NADP(+) = estrone + H(+) + NA... |
Q13268 | MLSAVARGYQGWFHPCARLSVRMSSTGIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYSTRL | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of dicarbonyl compounds. Displays reductase activity in vitro with 3,4-hexanedione, 2,3-heptanedione and 1-phenyl-1,2-propanedione as substrates . May function as a dicarbonyl reductase in the enzymatic inactivation of reactive carbonyls involved in... |
O75911 | MVWKRLGALVMFPLQMIYLVVKAAVGLVLPAKLRDLSRENVLITGGGRGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQTAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVEAVQLNQALLLLPWTMHALVILKSILPQAALEEIHKFSGTYTCMNTFKGRT | Function: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33548
Sequence Length: 302
Subcellular Location: Membrane
EC: 1.1.1.... |
O88876 | MVWKWLGALVVFPLQMIYLVTKAAVGMVLPPKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGTYTCMNTFKGRT | Function: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33652
Sequence Length: 302
Subcellular Location: Membrane
EC: 1.1.1.... |
Q8SPU8 | MLKVGLPLGACARSWKSVRMASCGMARRNPLDNKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDRAVATLKGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGVDILISNAAVSPFFGSLMDVPEEVWDKILDVNVKATALLTKAVVPEMAKRGGGSIVIVSSIAAYSPFPSLGPYNVSKTALLGLTKNLALELAESNVRVNCLAPGLIRTSFSRVLWEDPARQESIKATFQIKRIGKPEECAGIVSFLCSEDASYITGETVVVAGGSLSHL | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces all-trans-retinal and 9-cis retinal. Reduces 3-ketosteroids and benzil into 3alpha-hydroxysteroid... |
G5EGA6 | MPSNCRRFEGKVAIVTAATKGIGLAIAERLLDEGASVVIGSRNQKNVDEAIEYLKNKGLTKVAGIAGHIASTDDQKKLVDFTLQKFGKINILVNNHGINPAFGHILEVSDQVWDKLFEVNVKAGFQMTKLVHPHIAKEGGGAIIFNASYSAYKSPPGIAAYGVTKTTLVGLTRALAMGLAKDNIRVNGIAPGVIKTKMSQVLWDGGEDAEKELTDIQEIALGRLGVPDDCAGTVAYLASDDSSYITGEMIIIAGGVQARL | Function: Catalyzes the reduction of isatin, 4-oxonon-2-enal, 9,10-phenanthrenequinone, menadione, 2,3-hexaenadione, 3,4-hexanedione and 2,3-heptanedione.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 27590
Sequence Length: 260
EC: 1.1.1.184
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Q9BTZ2 | MHKAGLLGLCARAWNSVRMASSGMTRRDPLANKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGIDILVSNAAVNPFFGSIMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLTKTLAIELAPRNIRVNCLAPGLIKTSFSRMLWMDKEKEESMKETLRIRRLGEPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones . Reduces 3-ketosteroids and benzil into 3beta-hydroxysteroids and R-benzoin, respectively, in contrast to... |
Q99LB2 | MQKAGRLLGGWTQAWMSVRMASSGLTRRNPLSNKVALVTASTDGIGFAIARRLAEDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGIVCHVGKAEDREKLITTALKRHQGIDILVSNAAVNPFFGNLMDVTEEVWDKVLSINVTATAMMIKAVVPEMEKRGGGSVVIVGSVAGFTRFPSLGPYNVSKTALLGLTKNFAAELAPKNIRVNCLAPGLIKTRFSSVLWEEKAREDFIKEAMQIRRLGKPEDCAGIVSFLCSEDASYINGETVVVGGGTPSRL | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces all-trans-retinal and 9-cis retinal. Reduces 3-ketosteroids and benzil into 3alpha-hydroxysteroid... |
Q8WNV7 | MRAAGQLLRACSQTWKSVRMASTGVERRKPLENKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQENVDRTVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVNLHGGVDILVSNAAVNPFFGNIIDATEEVWDKILHVNVKATVLMTKAVVPEMEKRGGGSVLIVSSVGAYHPFPNLGPYNVSKTALLGLTKNLAVELAPRNIRVNCLAPGLIKTNFSQVLWMDKARKEYMKESLRIRRLGNPEDCAGIVSFLCSEDASYITGETVVVGGGTASRL | Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones . Reduces all-trans-retinal and 9-cis retinal (Probable). Reduces 3-ketosteroids and benzil into 3alpha-hy... |
P80702 | MSIIVISGCATGIGAATRKVLEAAGHQIVGIDIRDAEVIADLSTAEGRKQAIADVLAKCSKGMDGLVLCAGLGPQTKVLGNVVSVNYFGATELMDAFLPALKKGHQPAAVVISSVASAHLAFDKNPLALALEAGEEAKARAIVEHAGEQGGNLAYAGSKNALTVAVRKRAAAWGEAGVRLNTIAPGATETPLLQAGLQDPRYGESIAKFVPPMGRRAEPSEMASVIAFLMSPAASYVHGAQIVIDGGIDAVMRPTQF | Function: Catalyzes the reversible interconversion of hydroxy and oxo groups at position 3 of the steroid nucleus. Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, includin... |
P80701 | QVIAITGSASGIGAA | Function: Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. No detectable activity... |
Q9VAK8 | MASPVVSLLLVGICALAFVHVARSECCTSRELVEFKMDRGDCEAVRAIENYPNGCEVTICADGVAQLGAYCGQGSCNIFGCNCDGGCLSGDWSQEFVRRNQQYGIQIIKVTRLPF | Function: Cytokine which promotes survival following infection by Sindbis virus by suppressing the immune deficiency pathway . Following infection by the enteropathogenic bacteria E.carotovora limits intestinal stem cells proliferation . When secreted from muscle or adipose tissue, can attenuate age-related intestinal ... |
Q8W453 | MASKKAAMVMMAMIVIMAMLVDTSVAIDLCGMSQDELNECKPAVSKENPTSPSQPCCTALQHADFACLCGYKNSPWLGSFGVDPELASALPKQCGLANAPTC | Cofactor: Binds 1 zinc ion per subunit.
Function: Putative lipid transfer protein required for systemic acquired resistance (SAR) long distance signaling. May interact with a lipid-derived molecule to promote long distance signaling associated with SAR. Together with AZI1, required for glycerol-3-phosphate- (G3P) and a... |
A0A1V1FH01 | MAKSTTFFISLTLPFLLLSVVTATYYQSMSPTVLGFQEEKFTHLHFYFHDVVTGPKPSMVIVAEPNGKAKNSLPFGTVVAMDDPLTVGPESDSKLVGKAQGIYTSISQEEMGLMMVMTMAFSDGEFNGSTLSILARNMIMSEPVREMAIVGGTGAFRFARGYAQAKFYSVDFTKGDAIVEYDIFVFHY | Function: Involved in pterocarpan phytoalexin biosynthesis . Catalyzes the last step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions . Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two mol... |
Q1ZZU9 | MGGEKAFSFIFLLFLCFFLANLSASSAHPPRQKLKQRIPCKQLVLYFHDVVYNGHNKANATASIVGAPQGADLVKLAGENHFGNVVVFDDPITLDNNFHSPPVGRAQGLYVYDKKDTFHSWLSFSFTLNTTMHQGTLIFMGADPILIKNRDITVVGGTGDFFMARGIATIATDSYEGEVYFRLKVDIKLYECW | Function: Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism (By similarity). Also involve... |
I1JNN8 | MAKSTFFVCLNLSLLFSLVTATYYSSLTPTLLGFREEQFTHLHFFFHDVVTGPKPSMVFIAEPNGKAKDALPFGTVVAMDDPLTVGPEQDSKLVGKAQGIYTSISQEEMGLMMVMTMAFTDGDFNGSTISVLGRNMIMSEPVREMAIVGGTGAFRFARGYAQARFYSVDFTKGDAIVEYDVFVNHY | Function: Involved in pterocarpan phytoalexin biosynthesis . Catalyzes the last step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions . Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two mol... |
P37202 | MSTVSGLKRPQSSEKNHRDRVFVRATRGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPILSEKPMFLEKFGHHYLIPDSNIFYHCIDALEHPNNFFDVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIKIVLLTDDRENARLAAEQGIQVSTLKDYVQYLPDSEILLDMVSAIADAIASKEQVESGTKNVYELHWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWK... | Function: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elim... |
Q8TBM8 | MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKDSTSGSGEGGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSV... | Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway . Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities . Can... |
Q8IXB1 | MGVWLNKDDYIRDLKRIILCFLIVYMAILVGTDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYESWNYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNSIQTAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDGLVNVGWMDCATQDNLCKSLDITTSTTAYFPPGATL... | Function: Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR.... |
Q9NVH1 | MATALSEEELDNEDYYSLLNVRREASSEELKAAYRRLCMLYHPDKHRDPELKSQAERLFNLVHQAYEVLSDPQTRAIYDIYGKRGLEMEGWEVVERRRTPAEIREEFERLQREREERRLQQRTNPKGTISVGVDATDLFDRYDEEYEDVSGSSFPQIEINKMHISQSIEAPLTATDTAILSGSLSTQNGNGGGSINFALRRVTSAKGWGELEFGAGDLQGPLFGLKLFRNLTPRCFVTTNCALQFSSRGIRPGLTTVLARNLDKNTVGYLQWRWGIQSAMNTSIVRDTKTSHFTVALQLGIPHSFALISYQHKFQDDDQT... | Function: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63278
Sequence Length: 559
Subcellular Loca... |
Q7ZYZ6 | MKGLSGSRSHHHVVTCDPSFESMGHHLDHKPYLISQIDNPHPVDHSYYSQRSPYQPDCVVPYGTFPRRHYSSQHELKDEMAVVPYSGGGVPASKGQQRLPVALLDQFDRQLPVPRDGYHTLQYKRAAAALEQRSDSPGRIRHLVHSVQKLFTKSHSLEGPHHGHGHGKGSINGGKASPDGEPPAIRHRKRSKSRERCKSAEPKNRTPPSGYWSSDELEREACLFHHGPPGVMTMGRHPDKSQSQYFLEAYNTINDQALKNSRSNNDLGKCSTCTSIPLSVDASQLVKKSSWSSSLTVSRARQVYQKASVNVDKALVKAEA... | Function: Part of the postsynaptic scaffold in neuronal cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 110828
Sequence Length: 999
Subcellular Location: Cell membrane
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P97836 | MKGLSGSRSHHHGITCESACDSLSHHSDHKPYLLSPVDHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDESALVPRTLATKANRLPTNLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGASKGGVNGGKASPDGSQTVRYGKRSKSKERRSEPKARSNASNASPTSPSWWSSDDNLDGDMCLYHTPSGVMTMGRCPDRSVSQYFMGAYNTISEQAVKASRSNNDVKCSTCANLPVTLDAPLLKKSAWSSTLTVSRAREVYQKASVNMDQAVVKSEACQQERS... | Function: Part of the postsynaptic scaffold in neuronal cells.
PTM: Ubiquitinated by TRIM3; leading to proteasomal degradation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 110178
Sequence Length: 992
Subcellular Location: Cell membrane
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A9VKV4 | MAEFKEQVLDILEEVCENDIVKENLDVQLFEEGILDSFAVVSLLVEFQERLEIEVSISDFDRDEWATPNMVIKKLEEIR | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
P39579 | MDFKQEVLDVLAEVCQDDIVKENPDIEIFEEGLLDSFGTVELLLAIENRFDILVPITEFDRDVWNTPNNIVNQLSELK | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
Q830N2 | MNIQETVLNILEDITGTDEVVNNQDIQLFEEGLLDSLATVQLLVEIEGQLGIQVPVSDFDREVWGTPKQIIQQVEALQ | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
Q1G852 | MDIQKQIVDILAEATGEDFSDNMDQELYESGIMDSMTTVQMLLTLQETFDITVPVSEFNRDDWNTPNKLVEQVKKLQDEE | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
Q9CG51 | MKEQIFDIIETVSGTDEFREDLDMDLFEEGILDSMRAIMLIVELEGAFDISLPPSEMDREDWNTANKIAARVQEKKDEN | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
M2Y2F4 | MVEIQSQNEHHKFWANHLLPQFRRYIAEIGAYTSKQQDEHVKFFDSLLPHLGPRLPHPHTKAVLTVANMPLGFSVNLSDARKPIARMEIEPLDDTSGSAEDLFAANCIPACFTTLVKGMTTRVDTRWAHQLRQAFTPTSEESAIAKPRLRPGIERVSLAYFGITFDGDNRAMKYCTSHWPKFLGTATAESNDATSADAFLFSAIRRLKPGGEALAPSLDAIQHYFQNERHAKLPSPILFVGLDCIDPSRARIKMYGRTHSTAFSNVRNIMTLGGRALTAETTEFLARLRSIWHLLLNDPKAKDDEDYDRPPLDPNSLRTG... | Function: Tryptophan dimethylallyltransferase; part of the hps1-dma1 gene cluster that probably mediates the biosynthesis a derivative of cyclopiazonic acid (CPA) (Probable). The hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) nps1 might incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) a... |
Q10322 | MTKSVEGYLKEQELAAETDSEKDDDKISIRLTNFVGPNAHSFSFDPLVRYWNRKQNNLPIYIGRYTERYNGGDVSAIVFRSKVVSRRHAQIFYENNTWYIQDMGSSSGTFLNHVRLSPPSKTSKPYPISNNDILQLGADYRGGHEVNYRCVRARVELNNSWKIKLSPYNLNEFKRMQELVLCGSSESGPPECCICLMPVLPCQALFVAPCSHSYHYKCIRPTLNESHPYFSCFICRKYHDLEAPVEEGDESLNDLLRNATVKDDASE | Function: Probable E3 ubiquitin-protein ligase which is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is compromised. Inhibits the septation initiation netwok (SIN) during spindle checkpoint activation. The effect appears to be m... |
P38823 | MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNGLGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQTEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPIIRTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVKSSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLKANAFNKEALSRIKNLQKLTT... | Function: E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes . Involved in nutritional control of the cell cycle . Targets the G1 cyclin PCL1 for destruction . Required for proper spindle positioning, likely regulat... |
P53924 | MYTPIPANTPAPTAPTSSMTSNSSSASNANTTSSSGINPRNRASGTPSNERARPASGISSFLNTFGIRQNSQTASSSAAPDQRLFGTTPSNSHMSVAMESIDTAPQQQEPRLHHPIQMPLSAQFHVHRNYQLPISISLTAPTTTDHQQSSAHNFEGNNVGNVQESLNQRQPNGTNNTTTSIISMAPAATTRNIVGGADGSTIVNNSQEMYKNLRHLIYAANQPNGTEILHLDLPATSAEESNNMFNVDEVTLKQRKDKHGLFSIRLTPFIDSSSTTNQGLFFEPIIRKAGPGSQLVIGRYTERVRDAISKIPEQYHPVVF... | Function: E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.
PTM... |
P21311 | MSTILKWAGNKTAIMSELKKHLPAGPRLVEPFAGSCAVMMATDYPSYLVADINPDLINLYKKIAADCEAFISRARVLFEIANREVAYYNIRQEFNYSTEITDFMKAVYFLYLNRHGYRGLCRYNKSGHFNIPYGNYKNPYFPEKEIRKFAEKAQRATFICASFDETLAMLQVGDVVYCDPPYDGTFSGYHTDGFTEDDQYHLASVLEYRSSEGHPVIVSNSDTSLIRSLYRNFTHHYIKAKRSIGVSAGESKSATEIIAVSGARCWVGFDPSRGVDSSAVYEVRV | Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 on both strands. May play a regulatory role in the functions of the retron.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenos... |
Q96GE9 | MGSRLSQPFESYITAPPGTAAAPAKPAPPATPGAPTSPAEHRLLKTCWSCRVLSGLGLMGAGGYVYWVARKPMKMGYPPSPWTITQMVIGLSENQGIATWGIVVMADPKGKAYRVV | Function: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12257
Sequence Length: 116
Subcellular Location: Mitochondrion inner membrane
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Q9CQ00 | MGSSFSGSTEFSAPAPPTVSTAVPANPPAKSAVPASPARDPELKTCWSCRVLSGSTLFGAGTYVYLVARRPLKQGIPPGPGTVLQMVIGISIACWGVVVLVDPKGKSHPVI | Function: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11344
Sequence Length: 111
Subcellular Location: Mitochondrion inner membrane
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Q20929 | MEFTECKTTFIHLPDKSFLYDVFVSVYNFYHPIHAYLSIFLCVLGTIANFCNIVVLTRRTMRTPVNMILTAMASCDTVVLFSNLIYTTHYSFVAFKFCHPKHWSYSWALFLIAHAHLSLVAHSSSVWLSVMLALVRYVTLRSRGNMGGMQVTLRHSYYAVAVTVSLVAVLNAPNFLNYKINEQPLNETCTDLDPMFWNSPAYLPGIADIAKANSCLVFRLSYWISGMVFKVLPCALLSLFVWLLLRILREVRENRQRLLKNSQHRPPNQTTTRNGQRLSISVAGNEKLGRNGSLRGRGERVDRTTHMLLAIVAVMLVTEL... | Function: G-protein coupled receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57249
Sequence Length: 510
Subcellular Location: Cell membrane
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P51333 | MLTQESEDLLKQIEKLSPDFFYFKSNSLVYRAILETVNPIDKIALVSLLTALNTNNLIRQLGRLETIMKLIENSPASNIIYEYSKVILDNYVKRLLLKSGDSLCLISCSKKQITQSVITSVASQLTIAYEILEDEGTYTLAEIFASLLVSLDTKKKISINSGIFSGFWQLDLITNGFQKSDLIIIAGRPSMGKTAFAINITRHIIKTSQYYVILFSLEMSTEQLLRRILAQECHLNSQKIQSGQLTNVEWQRIVEESKILANLNFYIDDSAEISCDIIKVKVKLLRLQGKKIKLIIIDYLQLLQESKKSENRSQELSLIT... | PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 65370
Sequence Length: 568
Subcellular Location: Plastid
EC: 3.6.4.12
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O30477 | MAEFEERPRLSIGEEEAPPYPLEKLTGGRRTRAQIHALHQQAGRVPPQAVELEQAVLGAMLIEPEAIPRALEILTPEAFYDGRHQRIFRAIVRLFEQNRGVDLLTVTEELRRTGELEQAGDTIYLSELTTRVASAANVEYHARIIAEKLLRRMIEVMTLLVGRAYDPAADAFELLDEVEAEIFRLSDVHLRKAARSMNEVVKETLERLEAIHGRPGGITGVPSGFHQLDALTGGWQRGDLIIIAARPSMGKTAFALSCRNAALHPHYGTGVAIFSLEMGAEQLAQRLLTAEAASMPRRPAPDGCATRTGVSWPARRPLSD... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
PTM: Upon expression in E.coli this protein undergoes self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Catalytic Activit... |
Q9ZD08 | MVRNKINNDDNLSIPRVLPSNIQAEQMLLGAIITNNALLSYVSEFLRNEHFFEPIHQKIYDAIEKIIEKGLIATPITLRSMLTQDALFKEIEGEGYLAKLITMSMMVINPIDYGKIIYDLAIKRNLINIGEEVVNNAYNSSLAVAAKEQIEYAEAKLYDLTKEGLNEKSFTKVGISISESLASINRAMKNNDHVIGISTGLLDLDNKLFGFHNSDLIILAGRPSMGKTAFAINLALNTCNNMRLKNIRDNQEIKSVGFFSLEMSSEQLTTRLLSLCAEIDSTALRTGMLSEDKYNRLRKEANTLSELQFFIDDTPALSIS... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
... |
Q55418 | MAANPALPPQNIEAEECILGGILLDPEAMGRIIDLLVVDAFYVKAHRLIYEAMLSLHGQSQPTDLMSVSSWLQDHHHFEAIGGMVKLTQLLDRTISAVNIDRFAALIMDKYLRRQLIAAGHDIVDLGYETSKELETIFDESEQKIFRLTQSRPQAGLVPLSETLVNTFIELDKLHEKLSSPGVETQFYDLDAMTGGLQRADLIILAGRPSMGKTAFGLGIAANIAKNQNLPVAIFSLEMSKEQLALRLVASESLIDSNRLRTGHFSQAEFEPLTAAMGTLSSLPIYIDDTASISVTQMRSQVRRLQSEQKGPLGMVLIDY... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Catalytic Activity: ATP + H2O = A... |
O83097 | MPGMPNPTQELKGKIPPHNLEAERAVLGAVLLDDSALSTATEQLSASSFYSAAHQRIFQALVELSDLGQRPDILVLSEHLRSCEALDFVGGSAYVASLTDAVPSAANVEYYTRIVCDAAMRRSLLKVARIITAEAFNDTVSGNIVLETAQREIYDLTNARRVATFKLLKNLIPDLVNTIETRYRNQSDLVGIATGLTALDNLTGGFQNSELIVIGARPSMGKTALAMTMASNIAIRQRIPTAFFSLEMSNLLLMQRLIAAESGVSATNLRKGLLQLSDFGRIQNAAGEMYDAPLYIVDVPNMKLLDLRAVARRLCVQEKI... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 47796
Sequence Length: 438
EC: 3.6.4.12
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P49519 | MEKINLKTGRLIVEKYLPHNFLAEKIVLSSLLISSEAIETCLRSLTIDAFYFKNHREIYKAILIMYKKNTPIDIVTLNTFLQNQGLLPKIGGIKVLIELVNQLPNLVYLEEYIRIIQDKYVRRSLIKLGYEAINSGYITNISLEEILISLEKQMFSLTNEIKNQDVFSSVDLFSQILLELKYKSSKPVLAGLSSGFYDLDSLTQGFQKSDLIIIAGRPSMGKTAFCLNIATNIVKKYKLPILFFSLEMSKEQLAYRLLSAEALINPMRLRNGHLNKKDWLKLHRIIKNLSSLPFFIDDTPNLSIQAIRSKVKKLLFEQNT... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 52320
Sequence Length: 455
Subcellular Location: Plastid
EC: 3.6.4.12
|
P74143 | MDNLRLHPDTIQEIKQRIDIVEIIGDYVVLKKRGRDHLGLCPFHDEKSPSFSVSPAKQMYYCFGCGAGGNAFNFLMELGKRSFTDVALDLARRYQIQIQTLEPAQKQELQRQLSLREQLYEIMAVAAGFYHHTLFQPQGQEALTYLDQKRCLSSATIQEFQLGYAPAGWETLYRYLVEQKRYPVAAVEQAGLIKARQSGTGYYDQFRHRLMIPIRDVQGKTIAFGSRTLGNDEPKYLNSPETPLFHKSKTLFGLDQAKTAIQKVDEAILVEGYFDVIALHESGIKQTVAALGIALSRDQVQSLMRFSQSKQIIFNFDADK... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 73079
Sequence Length: 635
Domain: Contain... |
Q5JH14 | MKRKKTVLQQILSEKRKKVKEGDSMSGKDEFGTTKYVIYAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIRVEVHNKAGKTYGTITVPSSLDRVETAVLAAALETIDRVGPAEARIKVLRIEDVRATKRKYIIERAKEILETLMEQEIPETQEITEEVKKAVRAKELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLKHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADVDYVARAPEGKEVEELTKKEIVKALRSKVPAEQVINEMFNKGRSFYELIRERESEGE... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction betwee... |
Q9X1G3 | MIPREVIEEIKEKVDIVEVISEYVNLTRVGSSYRALCPFHSETNPSFYVHPGLKIYHCFGCGASGDVIKFLQEMEGISFQEALERLAKRAGIDLSLYRTEGTSEYGKYIRLYEETWKRYVKELEKSKEAKDYLKSRGFSEEDIAKFGFGYVPKRSSISIEVAEGMNITLEELVRYGIALKKGDRFVDRFEGRIVVPIKNDSGHIVAFGGRALGNEEPKYLNSPETRYFSKKKTLFLFDEAKKVAKEVGFFVITEGYFDALAFRKDGIPTAVAVLGASLSREAILKLSAYSKNVILCFDNDKAGFRATLKSLEDLLDYEFN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 65133
Sequence Length: 565
Domain: Contain... |
O83505 | MARISAHVIDAIADRVDLVSLVGNYTHLERRGDDWWGRCPFHHERTPSFHVVPDKKMYYCFGCGVGGSTIKFFMEIEKIDFHEAAVRLAKRAGIEMSFEDGVHAPSAHASFTMQLCEVYQRIAETFHHVLMHTAQGARARAYLASRKVTDDSIRTFKLGYAPPDPVWLFQFLRHKGYSPEFLARSGLFAKKSERIAVFSDRIMYPIADRYGQVIAFGARALGTAPAKYLNTADMPQYKKGEHLFAFHCALSQMRKTRAAIICEGYMDVIAFHQAQLTYAVAPLGALLTKSQARLMRSFVDRIYMCFDADGAGRAATYKAI... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 67893
Sequence Length: 605
Domain: Contain... |
Q9PPZ6 | MSKITNNVFLTIRNAINISDVIQNYIKVIKKGNNYWAICPFHNDTNESLSINDKKQIFKCFACNHAGDVIKFVAEYKKISYALAAQEIVQLMNLDLNLLNHLQKISPQEIKKNKVFDLNKQIQKWFINFLNNKNNIHVIDYLTKRNLNKNDLAYFKIGYAPNNDELLNLIKSNYNNLIQENDEFELNKLIENSFLVIDKNGNYHDFFNDRIIFSIYDHLNNVVGFSGRIITNEKTPKYLNTKTTAVFKKDEVLYNFHNVITIENNHQLFIVEGFMDVITIHKSNKPNVVATMGVELTNKHLELIKSYGIKDLILCFDNDQ... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 75391
Sequence Length: 641
Domain: Contain... |
O85213 | MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRM... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
B9KFK6 | MELNYYEILEISQTSDKETIKKAYRKMALKYHPDRNQGDKEAEEKFKLVNEAYEVLSNDEKRSIYDRYGKEGLKGQAGGFGGFGDVDLGDIFSSFFGDGFGFGSSTRKKEKGNKYPQDLKITTKISFKEAVFGCKKKIDFSYKSFCKSCKGSGSENGKLDTCPHCGGKGQVGVRQGFMTFVQSCDHCKGSGQIIKDKCKTCHGNGYEEIKDHIELDIPEGIDSGMSLRVQNKANELPNSSQRGDLYIKIIVEDDDKFIRHDDDIYTIVPVFFTQAALGKTIKVSTIRGEADLKLPVGAKDKQKFELTNEGVKNIHNGKLG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P22305 | MRDYYEILGVTRTIDEAGLKSAFRKLAMEHHPDRNGGCENAAGRFKEINEAYSVLSDPQKRAAYDRFGHAGVNGPQGGPGGFGGQGFDASDIFNDVFGDVFGEMFGGGRRQSNAPQRGQDLRYDLEITLEQAYAGAEVEITVPAAMTCEVCEGSGAKPGTSPSVCGTCGGAGRVRATQGFFAVERGCPRCGGSGRLVLDPCSNCHGHGQVRRERILSVRIPAGVDDGARIRLAGEGDAGARGGPRGDLYIFLSVTPHELFERDGLDLLCTVPVPMTTAALGGEIDAPCLLGGESCDGECKVKVHVPEGAQTGKTVRLKGK... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
B3EE31 | MKKDYYEVLGVSRSASKDEIKKAYRKLALQYHPDKNPDNKDAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGAGGAYAGGATDFNDIFSAFNDMFGGGRARGGGAPFGFEEVFGGGGGAGRRGRTSAGISGTDLKIRLKLTLEEIAKGVEKTLKIKKQIVCKECNGSGSKTGATEPCQTCHGSGEVRQASKTMFGQFVNITACPTCGGEGRVVKDRCTACYGEGIKQGDVTVKVTVPAGVQDGNYLTLRGQGNAGPRGGAPGDLIVVIEEKPHELFRRDGNDVIFNLALSYPDLVLGTKIDVPTLDGAVKLT... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q9PK53 | MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSEGARQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGAKTSKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSECRGQGRIKDKRSVHVNIPSGVDSGMRLKMEGYGDAGQNGAPAGDLYIFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLNIPEGIQSG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P0CW07 | MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGH... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
B0JW23 | MPTDYYEILGVSRDAGKEDIKRAYRRLARKYHPDVNKEPGAEEHFKEINRAYEILSEPETRNRYDRFGEAGVSGGAAGFDPDNMGGFADIFETIFSGFGGMGGQATARRRTGPTRGEDLRLDFRLKFREAVFGGEKEIRIRHLETCQTCKGSGARPGTSSRTCTTCSGTGQVRRATRTPFGTFAQVSVCPTCDGAGEVIEEKCDVCGGSGRRQETKKLKITIPAGVDNGMKLRVAREGDAGLKGGPPGDLFVYLTVETDAEFQREGNDIKSDITISYIQAILGCTIKVNTVDGQEDLTIPAGTQPNTVLILENKGVPKLG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q7NBW0 | MSSKRDYYEILEVSRSATQQDIKKAFRKLAMKYHPDRNKDSDAEEKFKEVNEAYEVLSDEEKRKLYDTYGHEGLNASGFHQGGFNPYDVFNSVFSGFDFEGGFGDVFSQFFGGGGSGFHNQEYIEEVDVNLVHEIKINFLEAANGCIKNVKYTRQVTCPDCNGSGSADGDVITCSDCNGEGFLVEQRRTLLGMFQTKKTCPSCKGEGQTIKNKCKKCKSRRMVDEVVERKVSIDSNVFYQDVVIVRGEGHIYKNLVGDLFLRVKIEPSRVFELRDNHVVVNVLVDPLVAITGGTILIPTLKEIKEINLKAGTKNGDIITI... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P47265 | MAAGKRDYYEVLGISKNASSQDIKRAFRKLAMQYHPDRHKAENETTQKQNEEKFKEVNEAYEVLSDEEKRKLYDQFGHEGLNASGFHEAGFNPFDIFNSVFGEGFSFGMDGDSPFDFIFNRSKKRQQQIVVPYNLDIALVIEINFFEMTNGCNKTIKYERKVSCHSCNGFGAEGGESGLDLCKDCNGNGFVIKNQRSIFGTIQSQVLCSTCNGQGKQIKVKCKTCRSNKYTVTNQIKEINIPAGMYSGEALVDESGGNEFKGHYGKLIIQVNVLASKIFKRSDNNVIANVLVDPMVAIVGGVIELPTLEGIKEFNIRPGT... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q9HJ83 | MAKDYYKILGVDRNATDEEIKKAFRELAKKWHPDLHPENKQEAEEKFKEISEAYEVLSDPQKRRMYDQTGTVDFGAGGQNFNWDNFTHYSDLNDIFNDIFGGNFASDFFSGFGRGQREEQYDLDLYTNLDITLEDAYYGTEKRIKYRRNAMCPDCNGTGAKNGKLITCPTCNGTGQQRIVRGQGFFRMVTVTTCQTCGGRGRIPEEKCPRCNGTGTVVVNEDISVKIPKGATDNLRLRVQGKGQSYNGRTGDLYVVLRVRNDRNVQRINDDLMIDQKINFAQAALGDTIEVNLFREKYSLKIPEGTQPGEVLRIKGAGMP... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q9WZV3 | MKKEKKDYYEILGVPRDATQEEIKRAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPTYQETESGGFFDDIFRDFENIFNRDIFDVFFGERPHQEERREYARRGEDIRYEIEVTLSDLINGAEIPVEYERYETCPRCGGTGVEPNAGYMDCPSCGGTGRIREERRSFFGYFVSERTCERCGGTGKIPREYCHECGGSGRVLRKVRRTVKIPPNVEDGTHLRITGGGNAGYYGGPYGDLIIIVRVKPDPRFKKSGSDLVYDVTIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVF... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q8DKR7 | MARDFYEILGVSRSADAEELKRAYRRLARKYHPDVNKEPGAEEKFKEINRAYEVLSDPQARANYDRFGEAGVSGVGAAGFSDFGIGDMGGFADIFETFFGGFTTSSRRQQGPTRGEDLRYDLKLEFREAVFGGEKEIRINHLETCKTCQGTGAKPGTRPVTCSTCGGVGQVRRSARTPFGSFTQLTTCPTCGGSGVVIEDRCESCGGQGHIQVSKKLKITIPAGVDNGTRLRVSGEGDAGLRGGPPGDLYVYLFVQPDPEFQREGNNILSRIKISYLQAILGCRISVSTVDGEAELKIPAGTQPGTVLVLEGRGVPRVGN... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q73Q15 | MPASKRDYYEVLGVDKKASNDDIKKAYRKLAIKYHPDKNQGDKAAEEKFKEATEAYEILIDEKKRSMYDQFGHAGVDGMSGGGGYDPSAFQGFEDIFGGSFSDIFENLFGGGFSSRSSGFGGRHAGPVRGSNLRYDLQISFVDAVYGKKAELSYTRNEKCSECHGTGSESGSSKRMCPDCKGTGQVRQSTGFFSISRPCPTCGGEGSIIEKPCKKCGGNGLERKKQRIIVTIPAGVENGKRITIPSQGNAGQAGGDYGDLFVFIFVQAHPYFERNGIDLYCAVPISMTQAALGGEINIKSLDEKTLRLKIPAGTQNGKLL... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q83MZ4 | MEDLYGILGVDHNASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALL... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q39079 | MMGQEAAPTGPPNRELYALLNLSPEASDEEIRKAYRQWAQVYHPDKIQSPQMKEVATENFQRICEAYEILSDETKRLIYDLYGMEGLNSGLELGPRLSKADEIKEELERIKRRNEEAKKMAHFQPTGSILFNLSVPHFLVGDGIMRGMVMASQVQSQLSKDDAIAIGGNLAANEKSGGGVATAILRRQISPVSSIEFVASTGLQSLIGVQTTRQLTIHSTATINISKSLSDGSINLTNTWTRQLSETSSGNIELALGMRSAITVGWKKRDENVSAAGDFKIESGGLGASARYTRKLSSKSHGRIVGRIGSNALEIELGGG... | Function: Plays a continuous role in plant development probably in the structural organization of compartments (By similarity). Seems to be involved in resistance to oxidative stresses mediated by thiol-oxidizing agents such as diamide.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59232
Sequence ... |
Q9ZSY2 | MSAKKLEGSSAPANRRDPYEVLCVSKDANDQEIKSAYRKLALKYHPDKNANNPDASELFKEVAFSYSILSDPEKRRHYDNAGFEALDADGMDMEIDLSNLGTVNTMFAALFSKLGVPIKTTVSANVLEEAMNGTVTVRPLPIGTSVSGKVEKQCAHFFGVTISEQQAESGVVVRVTSTAQSKFKLLYFEQDSSGGYGLALQEEREKTGKVTSAGMYFLHFQVYRMDTTVNALAAAKDPESAFFKRLEGLQPCEVSELKAGTHIFAVYGDNFFKTASYTIEALCAKTYEDTTEKLKEIEAQILRKRNELRQFETEYRKALA... | Function: Plays a continuous role in plant development probably in the structural organization of compartments (By similarity). Seems to be involved in early gravitropic signal transduction within the gravity-perceiving cells (statocytes), where it influences pH changes and auxin distribution. Probably affects the loca... |
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