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stringlengths 6
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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 Length: 224
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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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; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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P02540 | MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | 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 mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin.
PTM: ADP-ribosylation prevents ability to form intermediate filaments.
Sequence Mass (Da): 53629
Sequence Length: 471
Subcellular Location: Cytoplasm
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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 similarity).
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9677
Sequence Length: 85
Subcellular Location: Cell membrane
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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 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14117
Sequence Length: 127
Subcellular Location: Cell membrane
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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
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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
Subcellular Location: Cytoplasmic vesicle
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Q8WYQ5 | METDESPSPLPCGPAGEAVMESRARPFQALPREQSPPPPLQTSSGAEVMDVGSGGDGQSELPAEDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGAERDVRAECGLLLSPVSGDVHACPFGGSVGDGVGIGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGAGGFTAKAIVQRDRVDEEALNFPYEDDFDNDVDALLEEGLCAPKKRRTEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYLHRESRVVTWSRPYFLGTGSIRKHDPPLSSIPCLHYKKMKDNEEREQSSDLTPSGDVSPVKPLSRSAELEFPLDEPDSMGADPGPPDEKDPLGAEAAPGALGQVKAKVEVCKDESVDLEEFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAESERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVTIDGVTYGSGTASSKKLAKNKAARATLEILIPDFVKQTSEEKPKDSEELEYFNHISIEDSRVYELTSKAGLLSPYQILHECLKRNHGMGDTSIKFEVVPGKNQKSEYVMACGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRESSKMVKQETSDKSVIELQQYAKKNKPNLHILSKLQEEMKRLAEEREETRKKPKMSIVASAQPGGEPLCTVDV | 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 release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs . The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding . Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing . Involved in the silencing of embryonic stem cell self-renewal (By similarity).
Sequence Mass (Da): 86045
Sequence Length: 773
Domain: Both DRBM domains are required for efficient binding to pri-miRNA. The region between residues 276 and 498 has an autoinhibitory function on pri-miRNA processing activity.
Subcellular Location: Nucleus
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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-di-GMP + 2 diphosphate
Sequence Mass (Da): 32924
Sequence Length: 296
EC: 2.7.7.65
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P75908 | MEKDYLRISSTVLVSLLFGLALVLVNSWFNQPGVEEVVPRSTYLMVMIALFFIDTVAFIFMQLYFIYDRRQFSNCVLSLAFLSCLIYFVITVIIIQQIIEERLTSSVVQNDIAIYYLFRQMSLCILIFLALVNKVSENTKQRNLFSKKMTLCISLFFVFGGPIVAHILSSHYESYNLHIAELTNENGQVVWKASYVTIMIFMWLTLLSVNLYFNGLRYDIWNGVTVIAFCAVLYNISLLFMSRYSVSTWYISRTIEVVSKLTVMVIFMCHIFSALRVTKNIAHRDPLTNIFNRNYFFNELTVQSASAQKTPYCVMIMDIDHFKKVNDTWGHPVGDQVIKTVVNIIGKSIRPDDLLARVGGEEFGVLLTDIDTERAKALAERIRENVERLTGDNPEYAIPQKVTISIGAVVTQENALNPNEIYRLADNALYEAKETGRNKVVVRDVVNFCESP | 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-fold increase in c-di-GMP levels in vivo. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51783
Sequence Length: 452
Pathway: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.7.65
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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 residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to other classes of translation inhibitors. The c-di-GMP produced by this enzyme up-regulates poly-GlcNAc production as well as the biofilm synthesis protein PgaD, although c-di-GMP is probably not the main inducing principle. C-di-GMP is a second messenger which controls cell surface-associated traits in bacteria .
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Sequence Mass (Da): 33863
Sequence Length: 296
Domain: Contains an N-terminal CZB (chemoreceptor zinc binding) domain and a C-terminal GGDEF domain.
Pathway: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
EC: 2.7.7.65
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A0A0H3AFM6 | MKNWLCQAVRGEPMIELNRIEELFDNQQFSLHELVLNELGVYVFVKNRRGEYLYANPLTLKLFETNAQSLLGKTDHDFFHDDQLSDILAADQQVFETRLSVVHEERAIAKSNGLVRIYRAVKHPILHRVTGEVIGLIGVSTDITDIVELREQLYQLANTDSLTQLCNRRKLWADFRAAFARAKRLRQPLSCISIDIDNFKLINDQFGHDKGDEVLCFLAKLFQSVISDHHFCGRVGGEEFIIVLENTHVETAFHLAEQIRQRFAEHPFFEQNEHIYLCAGVSSLHHGDHDIADIYRRSDQALYKAKRNGRNRCCIYRQSTE | 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 activity.
EC: 2.7.7.65
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P16932 | MSLNDDATFWRNARQHLVRYGGTFEPMIIERAKGSFVYDADGRAILDFTSGQMSAVLGHCHPEIVSVIGEYAGKLDHLFSGMLSRPVVDLATRLANITPPGLDRALLLSTGAESNEAAIRMAKLVTGKYEIVGFAQSWHGMTGAAASATYSAGRKGVGPAAVGSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSGNLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLILDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAAIVTSAAIEERAHELGYLFYTTHVSDPLPAAVGLRVLDVVQRDGLVARANVMGDRLRRGLLDLMERFDCIGDVRGRGLLLGVEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGMGGVFRIAPPLTVSEDEIDLGLSLLGQAIERAL | 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 + dialkyl ketone + L-alanine
Sequence Mass (Da): 46444
Sequence Length: 433
EC: 4.1.1.64
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Q9S7D1 | MVKETLIPPSSTSMTTGTSSSSSLSMTLSSTNALSFLSKGWREVWDSADADLQLMRDRANSVKNLASTFDREIENFLNNSARSAFPVGSPSASSFSNEIGIMKKLQPKISEFRRVYSAPEISRKVMERWGPARAKLGMDLSAIKKAIVSEMELDERQGVLEMSRLRRRRNSDRVRFTEFFAEAERDGEAYFGDWEPIRSLKSRFKEFEKRSSLEILSGFKNSEFVEKLKTSFKSIYKETDEAKDVPPLDVPELLACLVRQSEPFLDQIGVRKDTCDRIVESLCKCKSQQLWRLPSAQASDLIENDNHGVDLDMRIASVLQSTGHHYDGGFWTDFVKPETPENKRHVAIVTTASLPWMTGTAVNPLFRAAYLAKAAKQSVTLVVPWLCESDQELVYPNNLTFSSPEEQESYIRKWLEERIGFKADFKISFYPGKFSKERRSIFPAGDTSQFISSKDADIAILEEPEHLNWYYHGKRWTDKFNHVVGIVHTNYLEYIKREKNGALQAFFVNHVNNWVTRAYCDKVLRLSAATQDLPKSVVCNVHGVNPKFLMIGEKIAEERSRGEQAFSKGAYFLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLNFLKGRDHADDALHKYKVFINPSISDVLCTATAEALAMGKFVVCADHPSNEFFRSFPNCLTYKTSEDFVSKVQEAMTKEPLPLTPEQMYNLSWEAATQRFMEYSDLDKILNNGEGGRKMRKSRSVPSFNEVVDGGLAFSHYVLTGNDFLRLCTGATPRTKDYDNQHCKDLNLVPPHVHKPIFGW | 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 (PSI) complex, especially to the PsaA, PsaB, PsaC, PsaL and PsaH subunits .
Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+) + UDP
Sequence Mass (Da): 91829
Sequence Length: 808
Subcellular Location: Plastid
EC: 2.4.1.241
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Q8W1S1 | MTNQQEQHIAIFTTASIPWLTGTAVNPLFRAAYLANDGERRVTLVIPWLTLKHQKLVYPNSITFSSPSEQEAYVRQWLEERVSFRLAFEIRFYPGKFAIDKRSILPVGDISDAIPDEEADIAVLEEPEHLTWFHHGQKWKTKFNYVIGIVHTNYLEYVKREKQGRVKAFFLKYLNSWVVGIYCHKVIRLSAATQEYPKSIVCNVHGVNPKFLEIGLRKLEQQKLQEQPFTKGAYYIGKMVWSKGYKELLKLLEKHQKELAELEVDLYGDGEDSEEIKEAARKLDLTVNVYPGRDHADSLFHNYKVFLNPSTTDVVCTTTAEALAMGKIVVCANHISNKFFKQFPNCRTYDDGQGFVRATLKALGEQPSQLTEQQRHELSWEAATQRFIKVSDLNRLSRADSNLSKRSVFASSSISVGKNLEDMSAYIHFLASGFEASRTAFGAIPGSLQPDEELCRDLGLSLNTPSPNTRKQD | 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).
Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+) + UDP
Sequence Mass (Da): 53907
Sequence Length: 473
Subcellular Location: Plastid
EC: 2.4.1.241
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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
EC: 3.8.1.5
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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
EC: 3.8.1.5
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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: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 33331
Sequence Length: 294
EC: 3.8.1.5
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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 | MNALAATNRNFRHASRILGLDSKIERSLMIPFREIKVECTIPKDDGTLVSYIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVADIPYGGAKGGIGCSPRDLSLSELERLTRVFTQKIHDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEYGKSIQGLTFVIQGFGNVGTWAAKLIHEKGGKVVAVSDITGAIRNPEGIDINALIKHKDATGSLNDFNGGDAMNSDELLIHECDVLIPCALGGVLNKENAGDVKAKFIVEAANHPTDPDADEILSKKGVIILPDIYANAGGVTVSYFEWVQNIQGFMWEEEKVNLELQKYMTRAFHNIKTMCHTHSCNLRMGAFTLGVNRVARATQLRGWEA | 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 | MSAKQVSKDEEKEALNLFLSTQTIIKEALRKLGYPGDMYELMKEPQRMLTVRIPVKMDNGSVKVFTGYRSQHNDAVGPTKGGVRFHPEVNEEEVKALSIWMTLKCGIANLPYGGGKGGIICDPRTMSFGELERLSRGYVRAISQIVGPTKDIPAPDVYTNSQIMAWMMDEYSRLREFDSPGFITGKPLVLGGSQGRETATAQGVTICIEEAVKKKGIKLQNARIIIQGFGNAGSFLAKFMHDAGAKVIGISDANGGLYNPDGLDIPYLLDKRDSFGMVTNLFTDVITNEELLEKDCDILVPAAISNQITAKNAHNIQASIVVEAANGPTTIDATKILNERGVLLVPDILASAGGVTVSYFEWVQNNQGYYWSEEEVAEKLRSVMVSSFETIYQTAATHKVDMRLAAYMTGIRKSAEASRFRGWV | 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. Wild-type cells are unable to utilize glutamate or glutamine as a sole carbon source; thus RocG does not function physiologically to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source . The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars .
Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 46553
Sequence Length: 424
EC: 1.4.1.2
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P24295 | MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPTTNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDSKLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW | 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
|
P29051 | MTMASKSDSTHDESGDEAADSTEPESALETARRQLYHAASYLDIDQNIVERLKYPKKVHEVTIPIERDDGTVEVFTGYRAQHDSVRGPYKGGLRYHPDVTRDECVGLGMWMTWKCAVMDLPFGGAKGGVAVNPKELSPEEKERLTRRFTQEIRDVIGPNQDIPAPDMGTDPQTMAWLMDAYSMQEGETTPGVVTGKPPVVGGSEGREEAPGRSVAIITQLVCEYYDQPLDETTVAVQGYGSVGANAARLLDKWGATIVAISDVNGAMYEPDGIDTASVPSHDEEPEAVTTYADTVISNEELLTLDVDVLIPAALGNVITKENAEAIAADLVVEGANGPTTSTADSILADRDVAVIPDILANAGGVTVSYFEWLQDINRRAWSLERVNDELEAEMQAAWRAVKDEYENRDVTWRDAAYIVALSRIAEAHEARGLWP | 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 | MNKHLLAKIALLSAVQLVTLSAFADVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGPDNQIWLTERATGKILRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYISGTFKNPKSTDKELPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLVIGPDQKIYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVLRLNLDGSIPKDNPSFNGVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNSDDEINLIVKGGNYGWPNVAGYKDDSGYAYANYSAAANKSIKDLAQNGVKVAAGVPVTKESEWTGKNFVPPLKTLYTVQDTYNYNDPTCGEMTYICWPTVAPSSAYVYKGGKKAITGWENTLLVPSLKRGVIFRIKLDPTYSTTYDDAVPMFKSNNRYRDVIASPDGNVLYVLTDTAGNVQKDDGSVTNTLENPGSLIKFTYKAK | 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
|
P18173 | MSASASACDCLVGVPTGPTLASTCGGSAFMLFMGLLEVFIRSQCDLEDPCGRASSRFRSEPDYEYDFIVIGGGSAGSVVASRLSEVPQWKVLLIEAGGDEPVGAQIPSMFLNFIGSDIDYRYNTEPEPMACLSSMEQRCYWPRGKVLGGTSVLNGMMYVRGNREDYDDWAADGNPGWAYNDVLPFFKKSEDNLDLDEVGTEYHAKGGLLPVGKFPYNPPLSYAILKAGEELGFSVHDLNGQNSTGFMIAQMTARNGIRYSSARAFLRPARMRNNLHILLNTTATKILIHPHTKNVLGVEVSDQFGSTRKILVKKEVVLSAGAVNSPHILLLSGVGPKDELQQVNVRTVHNLPGVGKNLHNHVTYFTNFFIDDADTAPLNWATAMEYLLFRDGLMSGTGISDVTAKLATRYADSPERPDLQLYFGGYLASCARTGQVGELLSNNSRSIQIFPAVLNPRSRGFIGLRSADPLEPPRIVANYLTHEQDVKTLVEGIKFVIRLSQTTPLKQYGMRLDKTVVKGCEAHAFGSDAYWECAVRQNTGPENHQAGSCKMGPSHDPMAVVNHELRVHGIRGLRVMDTSIMPKVSSGNTHAPAVMIAEKGAYLLKRAWGAKVURVDATWTLHRVI | 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 | MSKKKILITWPLPEAAMARARESYDVIAHGDDPKITIDEMIETAKSVDALLITLNEKCRKEVIDRIPENIKCISTYSIGFDHIDLDACKARGIKVGNAPHGVTVATAEIAMLLLLGSARRAGEGEKMIRTRSWPGWEPLELVGEKLDNKTLGIYGFGSIGQALAKRAQGFDMDIDYFDTHRASSSDEASYQATFHDSLDSLLSVSQFFSLNAPSTPETRYFFNKATIKSLPQGAIVVNTARGDLVDNELVVAALEAGRLAYAGFDVFAGEPNINEGYYDLPNTFLFPHIGSAATQAREDMAHQANDLIDALFGGADMSYALA | 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
|
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 Mass (Da): 34269
Sequence Length: 314
Pathway: One-carbon metabolism; formaldehyde assimilation via serine pathway.
Subcellular Location: Cytoplasm
EC: 1.1.1.29
|
P15877 | MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRSKRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGAVAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRFSPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALDAASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLIAINAENGKLCETFANKGVLNLQSNMPDTKPGLYEPTSPPIITDKTIVMAGSVTDNFSTRETSGVIRGFDVNTGELLWAFDPGAKDPNAIPSDEHTFTFNSPNSWAPAAYDAKLDLVYLPMGVTTPDIWGGNRTPEQERYASSILALNATTGKLAWSYQTVHHDLWDMDLPAQPTLADITVNGQKVPVIYAPAKTGNIFVLDRRNGELVVPAPEKPVPQGAAKGDYVTPTQPFSELSFRPTKDLSGADMWGATMFDQLVCRVMFHQMRYEGIFTPPSEQGTLVFPGNLGMFEWGGISVDPNREVAIANPMALPFVSKLIPRGPGNPMEQPKDAKGTGTESGIQPQYGVPYGVTLNPFLSPFGLPCKQPAWGYISALDLKTNEVVWKKRIGTPQDSMPFPMPVPVPFNMGMPMLGGPISTAGNVLFIAATADNYLRAYNMSNGEKLWQGRLPAGGQATPMTYEVNGKQYVVISAGGHGSFGTKMGDYIVAYALPDDVK | 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: 1.1.5.2
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Q75BS4 | MSEDWKKKLNIPKKDTRPQTDDVLNTKGNTFEDFYLRRELLMGIFEAGFERPSPIQEEAIPIALARRDILARAKNGTGKTAAFVIPTLEIVKPKVNKIQALIMVPTRELALQTSQVVRTLGKHCGISCMVTTGGTNLRDDIMRLNEPVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKSLVEQILSFLPQNHQSLLFSATFPLTVKEFMVKHLNKPYEINLMDELTLKGITQYYAFVEERQKLHCLNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQERNKVFHEFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIAAIPAQIDKSLYVAEDTSAVPVPFPLDTMQGNARAAQQMPHPQQQAQLGGMPQPIPQQIQPPLAHQQAQPPPQVYPPQMYHQGIPPQQFANPPQF | 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 mRNA nuclear export (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 54841
Sequence Length: 484
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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A1CJ18 | MADALASQLSNTTLGEANSETKWKEQLNVPAKDARPQTEDVTATKGLEFEDFYIKRELMMGIFEAGFEKPSPIQEETIPVALTGRDILARAKNGTGKTAAFVIPTLERINPKSTKTQALILVPTRELALQTSQVCKTLGKHLGINVMVTTGGTGLMDDIIRLNDAVHILVGTPGRVLDLASKGVADLSECPTFVMDEADKLLSPEFTPVIEQLLSFHPKDRQVMLFSATFPLIVKSFKDKHMRNPYEINLMDELTLRGITQYYAFVEEKQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHARMLQQHRNRVFHDFRNGVCRNLVCSDLLTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLINWEDRFNLYKIEQELGTEIQPIPQNIDKKLYVYDSPETIPRPISNPPQLRQATQSVTAERRHQNHANSGQYQFNRGRGSYRGRGQGQRRSVQNESNKFNHPQGQQSGKSQMAPVS | 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).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 56731
Sequence Length: 503
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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A2QY39 | MTDALASQLNNTTLGDASSDAKWKEQLNVPAKDARPQTEDVTATKGLEFEDFYIKRELMMGIFEAGFEKPSPIQEETIPVALTGRDILARAKNGTGKTAAFVIPTLERINPKSTKTQALILVPTRELALQTSHVCKTLGKHLGINVMVTTGGTGLMDDIIRLNDAVHILVGTPGRVLDLASKGVADLSECPTFVMDEADKLLSPEFTPVIEQLLSFHPKDRQVMLFSATFPLIVKSFKDKHMRNPYEINLMDELTLRGITQYYAFVEEKQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHARMLQQHRNRVFHDFRNGVCRNLVCSDLLTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLINWEDRFNLYKIEQELGTEIQPIPQNIDKKLYVYDSPDTIPRPIANPSQPQITAQAANANIGERRHNHHMNGGQYQYGRGRGSYRGGRGQGQRRNMQNETKFGTQGQSSGKSHPTQVS | 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).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 56685
Sequence Length: 505
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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P36009 | MAANSNSRVASNHTSKKQKVRRNIHPFTNNTRIKRASKIVKFNDSGEGDHVSDQRSNKENVLTYKSLKSRASDLLKMRETLPVYQHKREIMSYIESNPVTVLIGETGSGKSTQIPQFVLEKLYDTKKHGSIAVTQPRRVAAINLATRVAQEHGCKLGEQVGYSVRFDNTTTTRTRLKYLTDGMLLRELMMNSDLREYSVIVIDEAHERTVLTDLILGFLKSLIQGPRPDLRIIVMSATLQAEKFSEFFNNAPILFVEGRKFDVKQYYLKAPTDDIVDAVIRCCIQINQGEELGDILCFLPGQEEIDKAVTIMEKIAKYVSDEAPVPLIVPYPLYAALPAVQQSLVFAPIKGFKRKVVFSTNIAETSVTISGVKFVVDSGLRKVKVWRHQLGLATLLTVPISQASAMQRSGRAGRESEGKSFRLYCESDYVKLPKQSEPEIARSDVTSPVLMLKRYGVDDLLNWTWFENPGKEAIVMGLQELYELGALDTRGKITKRGQQMALLPLQPHLSSVLIKASEVGCLSQVIDIVSCLSVENLLLNPSPEERDEVNERRLSLCNAGKRYGDLIMLKELFDIYFYELGKSQDASSERNDWCKGLCISIRGFKNVIRVRDQLRVYCKRLFSSISEEDEESKKIGEDGELISKILKCFLTGFIKNTAIGMPDRSYRTVSTGEPISIHPSSMLFMNKSCPGIMYTEYVFTTKGYARNVSRIELSWLQEVVTNAAAVAKQKVSDSK | 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(+) + NADPH
Sequence Mass (Da): 33909
Sequence Length: 313
Domain: May be attached to the ER membrane by its C-terminus segment.
Subcellular Location: Endoplasmic reticulum
EC: 1.1.1.-
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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 covalent modification of cellular components . Also displays a minor hydroxysteroid dehydrogenase activity toward bile acids such as ursodeoxycholic acid (UDCA) and isoursodeoxycholic acid (isoUDCA), which makes it unlikely to control hormone levels . Doesn't show any activity in vitro with retinoids and sugars as substrates . Attenuates MDM2-mediated p53/TP53 degradation, leading to p53/TP53 stabilization and increased transcription activity, resulting in the accumulation of MDM2 and CDKN1A/p21 . Reduces proliferation, migration and invasion of cancer cells and well as the production of ROS in cancer .
Sequence Mass (Da): 29927
Sequence Length: 280
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.-
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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: 1.1.1.300
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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: 1.1.1.300
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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-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin. In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 29440
Sequence Length: 279
Domain: The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions.
Subcellular Location: Peroxisome
EC: 1.1.1.184
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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 the stereoselectivity of non-primate DHRS4s which produce 3alpha-hydroxysteroids and S-benzoin . Diplays low activity toward all-trans-retinal and no activity toward 9-cis-retinal as compared to non-primate mammals . In the reverse reaction, catalyze the NAD-dependent oxidation of 3beta-hydroxysteroids and alcohol, but with much lower efficiency . Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds .
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 29537
Sequence Length: 278
Domain: The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions.
Subcellular Location: Peroxisome
EC: 1.1.1.184
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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-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin. In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 29885
Sequence Length: 279
Domain: The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions.
Subcellular Location: Peroxisome
EC: 1.1.1.184
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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-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin . In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency . Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds .
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 29919
Sequence Length: 279
Domain: The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions.
Subcellular Location: Peroxisome
EC: 1.1.1.184
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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, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. No detectable activity on testosterone, progesterone or 3-oxo-desogestrel.
Catalytic Activity: a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH
Sequence Mass (Da): 26392
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 1.1.1.50
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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 on testosterone, progesterone or 3-oxo-desogestrel.
Catalytic Activity: a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH
Sequence Mass (Da): 1315
Sequence Length: 15
Subcellular Location: Cytoplasm
EC: 1.1.1.50
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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 tissue degeneration by inhibiting apoptosis .
Sequence Mass (Da): 12448
Sequence Length: 115
Domain: Contains two subdomains, SD1 and SD2. SD1 is composed of an antiparallel beta-sheet covered by an alpha-helix and displays a ferredoxin-like fold. SD2 displays a new protein fold made of loops connected by four disulfide bridges.
Subcellular Location: Secreted
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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 azelaic acid- (AA) induced systemic acquired resistance (SAR). Component of plant systemic immunity involved in priming defenses in a AA-dependent manner, by modulating production and/or translocation of a mobile signal(s) during SAR. Is able to bind with high affinity monoacylated phospholipids, mainly lysophosphatidylcholines .
Sequence Mass (Da): 10702
Sequence Length: 102
Subcellular Location: Secreted
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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 molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism (By similarity).
Catalytic Activity: a (4R)-4,2'-dihydroxyisoflavan = a pterocarpan + H2O.
Sequence Mass (Da): 20698
Sequence Length: 188
Subcellular Location: Secreted
EC: 4.2.1.139
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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 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family .
Sequence Mass (Da): 21521
Sequence Length: 193
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
Subcellular Location: Secreted
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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 molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism (By similarity).
Catalytic Activity: a (4R)-4,2'-dihydroxyisoflavan = a pterocarpan + H2O.
Sequence Mass (Da): 20511
Sequence Length: 186
Subcellular Location: Secreted
EC: 4.2.1.139
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P37202 | MSTVSGLKRPQSSEKNHRDRVFVRATRGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPILSEKPMFLEKFGHHYLIPDSNIFYHCIDALEHPNNFFDVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIKIVLLTDDRENARLAAEQGIQVSTLKDYVQYLPDSEILLDMVSAIADAIASKEQVESGTKNVYELHWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWKTEAEEIADDDEDVVVSTAAEPDSARINDLELITKRNAHPTAKVVGILKRNWRPYVGHVDNATIAQSKGGSQQTVLLTPMDRRVPKIRFRTRQAPRLVGRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRPFPKAVLDCLPEEGHNWKVPADKTHPLWKNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQKMQDPLTQGMRVLLKLSKILKQKRMDEGALNLASPEVRIQTDNETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAFPQTAVLRRHAAPPLTNFDSLQDILRVCKGMHLKCDTSKSLAKSLDECVDPKEPYFNTLLRILTTRCMLSAEYFCSGTFAPPDFRHYGLASPIYTHFTSPIRRYADVLAHRQLAAAIDYETINPSLSDKSRLIEICNGINYRHRMAQMAGRASIEYYVGQALKGGVAEEDAYVIKVFKNGFVVFIARFGLEGIVYTKSLSSVLEPNVEYVEDEYKLNIEIRDQPKPQTVQIQMFQQVRVRVTTVRDEHSGKQKVQITLVY | 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 elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by dis3 (By similarity). Implicated in mitotic control. Essential for cell division and spore germination. May be involved in regulating protein dephosphorylation during mitosis.
Sequence Mass (Da): 110138
Sequence Length: 970
Subcellular Location: Cytoplasm
EC: 3.1.13.-
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Q8TBM8 | MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKDSTSGSGEGGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG | 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 also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers . While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 . When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42516
Sequence Length: 379
Subcellular Location: Endoplasmic reticulum membrane
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Q8IXB1 | MGVWLNKDDYIRDLKRIILCFLIVYMAILVGTDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYESWNYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNSIQTAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDGLVNVGWMDCATQDNLCKSLDITTSTTAYFPPGATLNNKEKNSILFLNSLDAKEIYLEVIHNLPDFELLSANTLEDRLAHHRWLLFFHFGKNENSNDPELKKLKTLLKNDHIQVGRFDCSSAPDICSNLYVFQPSLAVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNFPANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFIEDLMNPSVVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRFFPPKSNKAYHYHSYNGWNRDAYSLRIWGLGFLPQVSTDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYFYERAKRNFQEEQINTRDAKAIAALISEKLETLRNQGKRNKDEL | 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. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.
Sequence Mass (Da): 91080
Sequence Length: 793
Domain: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.8.4.-
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Q9NVH1 | MATALSEEELDNEDYYSLLNVRREASSEELKAAYRRLCMLYHPDKHRDPELKSQAERLFNLVHQAYEVLSDPQTRAIYDIYGKRGLEMEGWEVVERRRTPAEIREEFERLQREREERRLQQRTNPKGTISVGVDATDLFDRYDEEYEDVSGSSFPQIEINKMHISQSIEAPLTATDTAILSGSLSTQNGNGGGSINFALRRVTSAKGWGELEFGAGDLQGPLFGLKLFRNLTPRCFVTTNCALQFSSRGIRPGLTTVLARNLDKNTVGYLQWRWGIQSAMNTSIVRDTKTSHFTVALQLGIPHSFALISYQHKFQDDDQTRVKGSLKAGFFGTVVEYGAERKISRHSVLGAAVSVGVPQGVSLKVKLNRASQTYFFPIHLTDQLLPSAMFYATVGPLVVYFAMHRLIIKPYLRAQKEKELEKQRESAATDVLQKKQEAESAVRLMQESVRRIIEAEESRMGLIIVNAWYGKFVNDKSRKSEKVKVIDVTVPLQCLVKDSKLILTEASKAGLPGFYDPCVGEEKNLKVLYQFRGVLHQVMVLDSEALRIPKQSHRIDTDG | 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 Location: Mitochondrion
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Q7ZYZ6 | MKGLSGSRSHHHVVTCDPSFESMGHHLDHKPYLISQIDNPHPVDHSYYSQRSPYQPDCVVPYGTFPRRHYSSQHELKDEMAVVPYSGGGVPASKGQQRLPVALLDQFDRQLPVPRDGYHTLQYKRAAAALEQRSDSPGRIRHLVHSVQKLFTKSHSLEGPHHGHGHGKGSINGGKASPDGEPPAIRHRKRSKSRERCKSAEPKNRTPPSGYWSSDELEREACLFHHGPPGVMTMGRHPDKSQSQYFLEAYNTINDQALKNSRSNNDLGKCSTCTSIPLSVDASQLVKKSSWSSSLTVSRARQVYQKASVNVDKALVKAEACQQERSCQFLQLWKCVFVELSVCLDADMHVWAKVCDVASLLNRQVPQDEWGGFPLGKDEDIPCRRMRSGSYVKAMAEDDSGDSDGSPKPSPKMQARRASYLKATQPSLTEMTTLKISQEHSPKLQIRSHSYLRAVSEVSINRSLDTLDPKALLASPQYRSRNESYMRAMSTISQIEAMCESVFNEMESHAVDALDLPMPGCFRMRSHSYVRAIDQGCSQDDDSPLLPASPPRTTTTVRTIQSSTVSSCITTYKKTPPPVPPRTSTKPFISITAQSSTESAQDAYMDGPGTRGEPVLHSGLSNSTESIDSMKALTAAIEAANAQIHGPASQHVSNSTMTISTAPPSPLPLPVPVPVPIPIPALEDVRRDVLRKSRCLSIGIQSKFQSVGVQVEEEHGVTTAVQADLDTPDYTPADSPVTDFPAAGCLSRQYSRDAATSTVSIQGSGNHYHACTSDDYEDVGFDPSILPPPDPWIDSVIEDSLEVVGRSVCQRDGRWFLKLLQAETERMEGWCRQMEHDEKENKMPDEVLGKIRGAVGSAQLLMSQKFQQFRELCEENLNPNAHPRPVAQDLAGFWDMLQLSIENISLKFDELHQLKANNWRPLDPPERKERRLPPPVPKKPPKAHPPLARDRSLESTEKQRQEARKRLMAAKRAASVRQNSATESADSIEIYIPEAQTRL | 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 | MKGLSGSRSHHHGITCESACDSLSHHSDHKPYLLSPVDHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDESALVPRTLATKANRLPTNLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGASKGGVNGGKASPDGSQTVRYGKRSKSKERRSEPKARSNASNASPTSPSWWSSDDNLDGDMCLYHTPSGVMTMGRCPDRSVSQYFMGAYNTISEQAVKASRSNNDVKCSTCANLPVTLDAPLLKKSAWSSTLTVSRAREVYQKASVNMDQAVVKSEACQQERSCQYLQVPQDEWTGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPMPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTGVIKLSSAVEVSSCITTYKKTPPPVPPRTTTKPFISITAQSSTESAQDAYMDGQGQRGDMISQSGLSNSTESLDSMKALTAAIEAANAQIHGPASQHMGSNAAAVTTTTTIATVTTEDRKKDFKKNRCLSIGIQVDDAEESEKMAESKTSSKFQSVGVQVEEEKCFRRFTRSNSVTTAVQADLDFHDNLENSLESIEDNSCPGPMARQFSRDASTSTVSIQGSGNHYHACAADDDFDTDFDPSILPPPDPWIDSITEDPLEAVQRSVCHRDGHWFLKLLQAERDRMEGWCKQMEREERENNLPEDILGKIRTAVGSAQLLMAQKFYQFRELCEENLNPNAHPRPTSQDLAGFWDMLQLSIENISMKFDELHQLKANNWKQMDPLDKKERRAPPPVPKKPAKGPAPLIRERSLESSQRQEARKRLMAAKRAASVRQNSATESAESIEIYIPEAQTRL | 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 bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Sequence Mass (Da): 9276
Sequence Length: 79
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Subcellular Location: Cytoplasm
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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 bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Sequence Mass (Da): 9009
Sequence Length: 78
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Subcellular Location: Cytoplasm
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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 bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Sequence Mass (Da): 8735
Sequence Length: 78
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Subcellular Location: Cytoplasm
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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 bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Sequence Mass (Da): 9259
Sequence Length: 80
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Subcellular Location: Cytoplasm
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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 bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Sequence Mass (Da): 9139
Sequence Length: 79
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Subcellular Location: Cytoplasm
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M2Y2F4 | MVEIQSQNEHHKFWANHLLPQFRRYIAEIGAYTSKQQDEHVKFFDSLLPHLGPRLPHPHTKAVLTVANMPLGFSVNLSDARKPIARMEIEPLDDTSGSAEDLFAANCIPACFTTLVKGMTTRVDTRWAHQLRQAFTPTSEESAIAKPRLRPGIERVSLAYFGITFDGDNRAMKYCTSHWPKFLGTATAESNDATSADAFLFSAIRRLKPGGEALAPSLDAIQHYFQNERHAKLPSPILFVGLDCIDPSRARIKMYGRTHSTAFSNVRNIMTLGGRALTAETTEFLARLRSIWHLLLNDPKAKDDEDYDRPPLDPNSLRTGLLVSFEVSALVSTPDIKVYVPFWQYHETDVQAINNLEQIFSLLGWDWGSGKYGDLLRKTFVGTDLAATQNHDYVSFNYSKRQGSYMTMYHVPPRPESTTA | 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) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway (By similarity). In addition, the cluster also includes the tryptophan dimethylallyltransferase dma1, the FAD-dependent oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1 and the methyltransferase DOTSEDRAFT_139328; the latter 2 being not present in all CPA-producing fungi but involved in additional modifications that occur in biosynthesis the of a range of CPA and CPA-like products (Probable). Further studies are required to clarify whether the CPA-like hps1-dma1 cluster is functional or a non-functional relic reflecting evolution of D.septosporum (Probable).
Sequence Mass (Da): 47348
Sequence Length: 420
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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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 mediated through preventing the SIN activator, plo1 kinase, from localizing to the SPB.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30597
Sequence Length: 267
Domain: The FHA domain is required for the proper localization at the SPB.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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P38823 | MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNGLGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQTEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPIIRTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVKSSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLKANAFNKEALSRIKNLQKLTTGLEQEDCSICLNKIKPCQAIFISPCAHSWHFHCVRRLVIMNYPQFMCPNCRTNCDLETTLESESESEFENEDEDEPDIEMDIDMEINNNLGVRLVD | 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 regulating septin ring deposition at the bud neck .
PTM: UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306. Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase in association with UBC4.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 46098
Sequence Length: 416
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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P53924 | MYTPIPANTPAPTAPTSSMTSNSSSASNANTTSSSGINPRNRASGTPSNERARPASGISSFLNTFGIRQNSQTASSSAAPDQRLFGTTPSNSHMSVAMESIDTAPQQQEPRLHHPIQMPLSAQFHVHRNYQLPISISLTAPTTTDHQQSSAHNFEGNNVGNVQESLNQRQPNGTNNTTTSIISMAPAATTRNIVGGADGSTIVNNSQEMYKNLRHLIYAANQPNGTEILHLDLPATSAEESNNMFNVDEVTLKQRKDKHGLFSIRLTPFIDSSSTTNQGLFFEPIIRKAGPGSQLVIGRYTERVRDAISKIPEQYHPVVFKSKVVSRTHGCFKVDSQGNWYIKDVKSSSGTFLNHQRLSPASSLSKDTPLRDGDILQLGMDFRGGTEEIYRCVRMRIELNRSWKLKANSFNKEALQRLQNLQKLTTGIEEEDCSICLCKIKPCQAIFISPCAHSWHFRCVRRLVMLSYPQFVCPNCRSSCDLEASFESSDEEDESDVESEGDQLVDQLSVLMETSKDVDSHP | 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: UBC4-dependent autoubiquitination occurs at Lys-211, Lys-258, Lys-288, Lys-310, Lys-333, Lys-343, Lys-346, Lys-366, Lys-406, Lys-412 and Lys-423. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-258, Lys-310, Lys-346 and Lys-366. Lys-211, Lys-256, Lys-288, Lys-310, Lys-343, Lys-258, Lys-366 and Lys-412 are also ubiquitinated in trans by DMA1 E3 ligase in association with UBC4.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 57584
Sequence Length: 522
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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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-adenosyl-L-homocysteine
Sequence Mass (Da): 32255
Sequence Length: 285
EC: 2.1.1.72
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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 | MEFTECKTTFIHLPDKSFLYDVFVSVYNFYHPIHAYLSIFLCVLGTIANFCNIVVLTRRTMRTPVNMILTAMASCDTVVLFSNLIYTTHYSFVAFKFCHPKHWSYSWALFLIAHAHLSLVAHSSSVWLSVMLALVRYVTLRSRGNMGGMQVTLRHSYYAVAVTVSLVAVLNAPNFLNYKINEQPLNETCTDLDPMFWNSPAYLPGIADIAKANSCLVFRLSYWISGMVFKVLPCALLSLFVWLLLRILREVRENRQRLLKNSQHRPPNQTTTRNGQRLSISVAGNEKLGRNGSLRGRGERVDRTTHMLLAIVAVMLVTELPQGIMAVLSGMCSEEFRIYIYNNLGDILDLFSLCGSCCSFIIYCSMSGQFRNEFHRVFVPAKVRCLRMSSPSIRRPSDAYSTTKMTFLKPNEKNGNGMNGNGTYSEDTRSASVKMVGIQVRRNSTEITRMTGCDSITPCSPMPTSFPSSPLPPIRSGEDESTDETSHLLNSSGPNSTASADGIRGHFQNI | 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 | MLTQESEDLLKQIEKLSPDFFYFKSNSLVYRAILETVNPIDKIALVSLLTALNTNNLIRQLGRLETIMKLIENSPASNIIYEYSKVILDNYVKRLLLKSGDSLCLISCSKKQITQSVITSVASQLTIAYEILEDEGTYTLAEIFASLLVSLDTKKKISINSGIFSGFWQLDLITNGFQKSDLIIIAGRPSMGKTAFAINITRHIIKTSQYYVILFSLEMSTEQLLRRILAQECHLNSQKIQSGQLTNVEWQRIVEESKILANLNFYIDDSAEISCDIIKVKVKLLRLQGKKIKLIIIDYLQLLQESKKSENRSQELSLITRSLKILARELNLPILVLSQLNRNLESRHNKRPLLSDLRESGCISKFSHIMWSHVSKPLFNFSIKKSHMHNFNKNIYQLLDQGEAFISRQDKKTTYKIRTNSEKYLELTSNHKILTLRGWQRCDQLLCNDMITTQIGFELSRKKKYLLNCIPFSLCNFETLANINISNFQNVFDFAANPIPNFIANNIIVHNSIEQDADLVIMLYRESYYNKEMEMEDMTEIIVAKHRNGPLGTFQLKFDANLANFLNV | 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 | MAEFEERPRLSIGEEEAPPYPLEKLTGGRRTRAQIHALHQQAGRVPPQAVELEQAVLGAMLIEPEAIPRALEILTPEAFYDGRHQRIFRAIVRLFEQNRGVDLLTVTEELRRTGELEQAGDTIYLSELTTRVASAANVEYHARIIAEKLLRRMIEVMTLLVGRAYDPAADAFELLDEVEAEIFRLSDVHLRKAARSMNEVVKETLERLEAIHGRPGGITGVPSGFHQLDALTGGWQRGDLIIIAARPSMGKTAFALSCRNAALHPHYGTGVAIFSLEMGAEQLAQRLLTAEAASMPRRPAPDGCATRTGVSWPARRPLSDAPIFIDDTPSLGVLELRAKCRRLKAEHDIGLVIVDYLQLMQASHMPRNANREQEIAQISRSLKALAKELNVPVVALSQLSRAVETRGGDKRPQLSDLRESGCLAGDTLITLADGRRVPIRELVSQQNFSVWALNPQTYRLERARVSRAFCTGIKPVYRLTTRLGRSIRATANHRFLTPQGWKRVDELQPGDYLALPRRIPTASTPTLTEAELALLGHLIGDGCTLPHHVIQYTSRDADLATLVAHLATKVFGSKVTPQIRKELRWYQVYLRAARPLAPGKRNPISDWLRDLGIFGLRSYEKKVPALLFCQTSEAIATFLRHLWATDGCIQMRRGKKPYPAVYYATSSYQLARDVQSLLLRLGINARLKTVAQGEKGRVQYHVKVSGREDLLRFVEKIGAVGARQRAALASVYDYLSVRTGNPNRDIIPVALWYELVREAMYQRGISHRQLHANLGMAYGGMTLFRQNLSRARALRLAEAAACPELRQLAQSDVYWDPIVSIEPDGVEEVFDLTVPGPHNFVANDIIAHNSIEQDADVVLFIYRPERYGITVDENGNPTEGIAEIIIGKQRNGPTGTVRLAFINQYARFENLTMYQPEPGTPLPETPDETILPSGPPDEAPF | 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 Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 104883
Sequence Length: 941
EC: 3.6.4.12
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Q9ZD08 | MVRNKINNDDNLSIPRVLPSNIQAEQMLLGAIITNNALLSYVSEFLRNEHFFEPIHQKIYDAIEKIIEKGLIATPITLRSMLTQDALFKEIEGEGYLAKLITMSMMVINPIDYGKIIYDLAIKRNLINIGEEVVNNAYNSSLAVAAKEQIEYAEAKLYDLTKEGLNEKSFTKVGISISESLASINRAMKNNDHVIGISTGLLDLDNKLFGFHNSDLIILAGRPSMGKTAFAINLALNTCNNMRLKNIRDNQEIKSVGFFSLEMSSEQLTTRLLSLCAEIDSTALRTGMLSEDKYNRLRKEANTLSELQFFIDDTPALSISAIRTRARRMKRKHNLGILFIDYLQLIRGVSKSENRVNEISEITQGLKAIAKELNIPVIALSQLSRAVELREDKKPMLSDLRESGTIEQDADIVMFIYREEYYLTRKEPVAGDAKHAEWLDKLNKVYNIADIIIAKHRNGPVGNVSLYYDSQFSKFGNLEKRTFNSI | 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
Sequence Mass (Da): 54940
Sequence Length: 486
EC: 3.6.4.12
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Q55418 | MAANPALPPQNIEAEECILGGILLDPEAMGRIIDLLVVDAFYVKAHRLIYEAMLSLHGQSQPTDLMSVSSWLQDHHHFEAIGGMVKLTQLLDRTISAVNIDRFAALIMDKYLRRQLIAAGHDIVDLGYETSKELETIFDESEQKIFRLTQSRPQAGLVPLSETLVNTFIELDKLHEKLSSPGVETQFYDLDAMTGGLQRADLIILAGRPSMGKTAFGLGIAANIAKNQNLPVAIFSLEMSKEQLALRLVASESLIDSNRLRTGHFSQAEFEPLTAAMGTLSSLPIYIDDTASISVTQMRSQVRRLQSEQKGPLGMVLIDYLQLMEGGSDNRVQELSKITRSLKGLAREINAPVIALSQLSRAVESRTNKRPMMSDLRESGCISGDSLISLASTGKRVSIKDLLDEKDFEIWAINEQTMKLESAKVSRVFCTGKKLVYILKTRLGRTIKATANHRFLTIDGWKRLDELSLKEHIALPRKLESSSLQLMSDEELGLLGHLIGDGCTLPRHAIQYTSNKIELAEKVVELAKAVFGDQINPRISQERQWYQVYIPASYRLTHNKKNPITKWLENLDVFGLRSYEKFVPNQVFEQPQRAIAIFLRHLWSTDGCVKLIVEKSSRPVAYYATSSEKLAKDVQSLLLKLGINARLSKISQNGKGRDNYHVTITGQADLQIFVDQIGAVDKDKQASVEEIKTHIAQHQANTNRDVIPKQIWKTYVLPQIQIKGITTRDLQMRLGNAYCGTALYKHNLSRERAAKIATITQSPEIEKLSQSDIYWDSIVSITETGVEEVFDLTVPGPHNFVANDIIVHNSIEQDADLIMMIYRDEYYNPDTPDPGVAELLIVKHRNGPTGVVKLLFKPEFTQFLNLQRSNDY | 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 = ADP + H(+) + phosphate
Sequence Mass (Da): 97813
Sequence Length: 872
EC: 3.6.4.12
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O83097 | MPGMPNPTQELKGKIPPHNLEAERAVLGAVLLDDSALSTATEQLSASSFYSAAHQRIFQALVELSDLGQRPDILVLSEHLRSCEALDFVGGSAYVASLTDAVPSAANVEYYTRIVCDAAMRRSLLKVARIITAEAFNDTVSGNIVLETAQREIYDLTNARRVATFKLLKNLIPDLVNTIETRYRNQSDLVGIATGLTALDNLTGGFQNSELIVIGARPSMGKTALAMTMASNIAIRQRIPTAFFSLEMSNLLLMQRLIAAESGVSATNLRKGLLQLSDFGRIQNAAGEMYDAPLYIVDVPNMKLLDLRAVARRLCVQEKIQIIFVDYLGLIVADNPFAPRYEQFAAISQSLKSLARELDIPIVALSQVGRPAEGSAPNLADIRGSGAIEQDADVVMFLHRDRNETETQLILAKQRNGPIGTVELEFQASFTRFVCKSP | 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 | MEKINLKTGRLIVEKYLPHNFLAEKIVLSSLLISSEAIETCLRSLTIDAFYFKNHREIYKAILIMYKKNTPIDIVTLNTFLQNQGLLPKIGGIKVLIELVNQLPNLVYLEEYIRIIQDKYVRRSLIKLGYEAINSGYITNISLEEILISLEKQMFSLTNEIKNQDVFSSVDLFSQILLELKYKSSKPVLAGLSSGFYDLDSLTQGFQKSDLIIIAGRPSMGKTAFCLNIATNIVKKYKLPILFFSLEMSKEQLAYRLLSAEALINPMRLRNGHLNKKDWLKLHRIIKNLSSLPFFIDDTPNLSIQAIRSKVKKLLFEQNTIGLVVIDYLQLMQSSTLKSSNRVQELSQITRSLKNIAREFNVPVIALSQLSRNVENRIIKRPILSDLRESGSIEQDADLVLMLYRDQYYNSNNENDEQLDITELILAKQRNGPIGTIQLKFDANYTKFFDYILKD | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 52320
Sequence Length: 455
Subcellular Location: Plastid
EC: 3.6.4.12
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P74143 | MDNLRLHPDTIQEIKQRIDIVEIIGDYVVLKKRGRDHLGLCPFHDEKSPSFSVSPAKQMYYCFGCGAGGNAFNFLMELGKRSFTDVALDLARRYQIQIQTLEPAQKQELQRQLSLREQLYEIMAVAAGFYHHTLFQPQGQEALTYLDQKRCLSSATIQEFQLGYAPAGWETLYRYLVEQKRYPVAAVEQAGLIKARQSGTGYYDQFRHRLMIPIRDVQGKTIAFGSRTLGNDEPKYLNSPETPLFHKSKTLFGLDQAKTAIQKVDEAILVEGYFDVIALHESGIKQTVAALGIALSRDQVQSLMRFSQSKQIIFNFDADKAGINATQRAIQEIEPLVYSGQVNLRILNLPAGKDADEFIHSSAENKEIYQTLVKQAPLWVDWQIQQLLKQKNLKDPLDFEQVARGMVDILKRLTDQNKRAYYLQLCGEILSQGDSRLISLQVNNLSSQLTYGDRPGKNGSRHWQAKDPTSSLLEKAEALLLKIYLHCPQERPTIDQILTENDLLFSFAHHRLLWQKIDQVREYFNLDSDPDNQLPLLVQLAYLEQEGDFNSVESLFQLTETSAEDLFRANLRIPEAIAIMEKVPWESYQKHCFGKLQQLDPRTQAEDFRYYQEQWQKAHQEIQRLESQRLNQPLN | 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: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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Q5JH14 | MKRKKTVLQQILSEKRKKVKEGDSMSGKDEFGTTKYVIYAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIRVEVHNKAGKTYGTITVPSSLDRVETAVLAAALETIDRVGPAEARIKVLRIEDVRATKRKYIIERAKEILETLMEQEIPETQEITEEVKKAVRAKELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLKHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADVDYVARAPEGKEVEELTKKEIVKALRSKVPAEQVINEMFNKGRSFYELIRERESEGERQPRQVTKPEPEVVKAQPKAETPEEKREPATVVRPSAEKIVKPIETSKSAPELEEFREFIERVKKDGIALLLDENKNVIAEIPVRELTNQLKERKDVYAVVFNGVITQRLIDTVSESGVKYIVGARKYNVVRRPVSLKIITFAE | 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 between heteromeric, adenine-rich transcripts and the exosome.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 52133
Sequence Length: 464
EC: 2.7.7.101
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Q9X1G3 | MIPREVIEEIKEKVDIVEVISEYVNLTRVGSSYRALCPFHSETNPSFYVHPGLKIYHCFGCGASGDVIKFLQEMEGISFQEALERLAKRAGIDLSLYRTEGTSEYGKYIRLYEETWKRYVKELEKSKEAKDYLKSRGFSEEDIAKFGFGYVPKRSSISIEVAEGMNITLEELVRYGIALKKGDRFVDRFEGRIVVPIKNDSGHIVAFGGRALGNEEPKYLNSPETRYFSKKKTLFLFDEAKKVAKEVGFFVITEGYFDALAFRKDGIPTAVAVLGASLSREAILKLSAYSKNVILCFDNDKAGFRATLKSLEDLLDYEFNVLVATPSPYKDPDELFQKEGEGSLKKMLKNSRSFEYFLVTAGEVFFDRNSPAGVRSYLSFLKGWVQKMRRKGYLKHIENLVNEVSSSLQIPENQILNFFESDRSNTMPVHETKSSKVYDEGRGLAYLFLNYEDLREKILELDLEVLEDKNAREFFKRVSLGEDLNKVIENFPKELKDWIFETIESIPPPKDPEKFLGDLSEKLKIRRIERRIAEIDDMIKKASNDEERRLLLSMKVDLLRKIKRR | 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: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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O83505 | MARISAHVIDAIADRVDLVSLVGNYTHLERRGDDWWGRCPFHHERTPSFHVVPDKKMYYCFGCGVGGSTIKFFMEIEKIDFHEAAVRLAKRAGIEMSFEDGVHAPSAHASFTMQLCEVYQRIAETFHHVLMHTAQGARARAYLASRKVTDDSIRTFKLGYAPPDPVWLFQFLRHKGYSPEFLARSGLFAKKSERIAVFSDRIMYPIADRYGQVIAFGARALGTAPAKYLNTADMPQYKKGEHLFAFHCALSQMRKTRAAIICEGYMDVIAFHQAQLTYAVAPLGALLTKSQARLMRSFVDRIYMCFDADGAGRAATYKAILLCRSLGFEVRIVELNGGTDPAECACIEGEDALRKSVERSTTDAQYLIRCARHEHSHLGADDTSRAVSFLFPYLSVLDSAIQREQVMQDIAMAFGIRIQAVHADYLRYVSRTTQKGTTGNCVLSVQGTAIQVKEPATGVRTAQLRLVLAVVANPELFELLRESVCADDFEDPMAKELFIILEECYRADTRASPHVLSCCTTDELRKLVSEAIVCGEFSCNAPQIVRDGVALVRRNRLLKERESLVGRLRRFGDASSGEECGSMQELMMEKQRVDEELERLKGVRK | 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: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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Q9PPZ6 | MSKITNNVFLTIRNAINISDVIQNYIKVIKKGNNYWAICPFHNDTNESLSINDKKQIFKCFACNHAGDVIKFVAEYKKISYALAAQEIVQLMNLDLNLLNHLQKISPQEIKKNKVFDLNKQIQKWFINFLNNKNNIHVIDYLTKRNLNKNDLAYFKIGYAPNNDELLNLIKSNYNNLIQENDEFELNKLIENSFLVIDKNGNYHDFFNDRIIFSIYDHLNNVVGFSGRIITNEKTPKYLNTKTTAVFKKDEVLYNFHNVITIENNHQLFIVEGFMDVITIHKSNKPNVVATMGVELTNKHLELIKSYGIKDLILCFDNDQAGFLATKKQIMKLINSPFNIFIVNHKDNDCKDMDEYANKHGYSATSKLLDQQLHISEFLLLEISNTNKSTPSLKHSYKQECFTIIKKYGDIFYVDKYVDFMKQTFSIEENLLKKVIEELLINKQCNSIQNKKNIQSYQKQTQLTNKLTTSNPKVILTKIDKHFNHLVVIILMNRVFLNRLDTQVRNRLTKEQSLVINIIEDFYLYHFKINNILKNTDSFIEFINKNYSKYTNVINQLTKMVQIIKYNPKFDNIVAFELAKNNFIYEWLNNQIKRLKLINLNLNMNNNQEQIINNEKLIKQYNDEKILLDNLINASLFHKNQ | 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: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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O85213 | MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRMGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKITNWFKS | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 41523
Sequence Length: 373
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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B9KFK6 | MELNYYEILEISQTSDKETIKKAYRKMALKYHPDRNQGDKEAEEKFKLVNEAYEVLSNDEKRSIYDRYGKEGLKGQAGGFGGFGDVDLGDIFSSFFGDGFGFGSSTRKKEKGNKYPQDLKITTKISFKEAVFGCKKKIDFSYKSFCKSCKGSGSENGKLDTCPHCGGKGQVGVRQGFMTFVQSCDHCKGSGQIIKDKCKTCHGNGYEEIKDHIELDIPEGIDSGMSLRVQNKANELPNSSQRGDLYIKIIVEDDDKFIRHDDDIYTIVPVFFTQAALGKTIKVSTIRGEADLKLPVGAKDKQKFELTNEGVKNIHNGKLGSHIVQIEIKFPKNLTDEQKNLLLQLEKSFGLADEEAFIEQESLFDKIKSWFSH | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 41954
Sequence Length: 373
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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P22305 | MRDYYEILGVTRTIDEAGLKSAFRKLAMEHHPDRNGGCENAAGRFKEINEAYSVLSDPQKRAAYDRFGHAGVNGPQGGPGGFGGQGFDASDIFNDVFGDVFGEMFGGGRRQSNAPQRGQDLRYDLEITLEQAYAGAEVEITVPAAMTCEVCEGSGAKPGTSPSVCGTCGGAGRVRATQGFFAVERGCPRCGGSGRLVLDPCSNCHGHGQVRRERILSVRIPAGVDDGARIRLAGEGDAGARGGPRGDLYIFLSVTPHELFERDGLDLLCTVPVPMTTAALGGEIDAPCLLGGESCDGECKVKVHVPEGAQTGKTVRLKGKGMPSLRSRQRGDLVVELFVETPTHLSARQKELMRELAGLCGEKQNPKSANFVGKAKRFWEEVTGS | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 40965
Sequence Length: 385
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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B3EE31 | MKKDYYEVLGVSRSASKDEIKKAYRKLALQYHPDKNPDNKDAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGAGGAYAGGATDFNDIFSAFNDMFGGGRARGGGAPFGFEEVFGGGGGAGRRGRTSAGISGTDLKIRLKLTLEEIAKGVEKTLKIKKQIVCKECNGSGSKTGATEPCQTCHGSGEVRQASKTMFGQFVNITACPTCGGEGRVVKDRCTACYGEGIKQGDVTVKVTVPAGVQDGNYLTLRGQGNAGPRGGAPGDLIVVIEEKPHELFRRDGNDVIFNLALSYPDLVLGTKIDVPTLDGAVKLTIPPATQPESMLRIPGQGIGHLRGSGKGDQLVRVNVYVPKDLSHHEKELLKELKKTAAFSPSGSNNDKEEKSFFEKARDIFS | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 42913
Sequence Length: 401
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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Q9PK53 | MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSEGARQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGAKTSKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSECRGQGRIKDKRSVHVNIPSGVDSGMRLKMEGYGDAGQNGAPAGDLYIFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLNIPEGIQSGTVLKVRGQGFPNVHGKARGDLLVRISVETPQHLSNEQKELLRKFSETEKAENFPKKRSFLDKIKGFFSDFAV | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 42074
Sequence Length: 392
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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P0CW07 | MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGHGKGDQLVRVIIRTPTKLTQEQKDLLHQFEYLSNGKKPEAEERSRSDKQKSEKPRKSKGLFEKVKDAFES | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 42990
Sequence Length: 389
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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B0JW23 | MPTDYYEILGVSRDAGKEDIKRAYRRLARKYHPDVNKEPGAEEHFKEINRAYEILSEPETRNRYDRFGEAGVSGGAAGFDPDNMGGFADIFETIFSGFGGMGGQATARRRTGPTRGEDLRLDFRLKFREAVFGGEKEIRIRHLETCQTCKGSGARPGTSSRTCTTCSGTGQVRRATRTPFGTFAQVSVCPTCDGAGEVIEEKCDVCGGSGRRQETKKLKITIPAGVDNGMKLRVAREGDAGLKGGPPGDLFVYLTVETDAEFQREGNDIKSDITISYIQAILGCTIKVNTVDGQEDLTIPAGTQPNTVLILENKGVPKLGNPVSRGDHRITVKISIPTRVTGEERELLEKLAKVRGETVGKGGIEGFLGNIFHK | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 40698
Sequence Length: 374
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q7NBW0 | MSSKRDYYEILEVSRSATQQDIKKAFRKLAMKYHPDRNKDSDAEEKFKEVNEAYEVLSDEEKRKLYDTYGHEGLNASGFHQGGFNPYDVFNSVFSGFDFEGGFGDVFSQFFGGGGSGFHNQEYIEEVDVNLVHEIKINFLEAANGCIKNVKYTRQVTCPDCNGSGSADGDVITCSDCNGEGFLVEQRRTLLGMFQTKKTCPSCKGEGQTIKNKCKKCKSRRMVDEVVERKVSIDSNVFYQDVVIVRGEGHIYKNLVGDLFLRVKIEPSRVFELRDNHVVVNVLVDPLVAITGGTILIPTLKEIKEINLKAGTKNGDIITIANGGINLKLDSRVYGANYNQKGDLIVVINYARPSEYSKQEITKLKEFIKPNKEVNLYETLMKKELNNKDSQ | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 44083
Sequence Length: 391
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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P47265 | MAAGKRDYYEVLGISKNASSQDIKRAFRKLAMQYHPDRHKAENETTQKQNEEKFKEVNEAYEVLSDEEKRKLYDQFGHEGLNASGFHEAGFNPFDIFNSVFGEGFSFGMDGDSPFDFIFNRSKKRQQQIVVPYNLDIALVIEINFFEMTNGCNKTIKYERKVSCHSCNGFGAEGGESGLDLCKDCNGNGFVIKNQRSIFGTIQSQVLCSTCNGQGKQIKVKCKTCRSNKYTVTNQIKEINIPAGMYSGEALVDESGGNEFKGHYGKLIIQVNVLASKIFKRSDNNVIANVLVDPMVAIVGGVIELPTLEGIKEFNIRPGTKSGEQIVIPNGGIKFSKSFKRKAGDLIIIISYARPCEYTNLELKKLREFIKPNQEVKQYLNTLKNEYKT | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 43746
Sequence Length: 389
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q9HJ83 | MAKDYYKILGVDRNATDEEIKKAFRELAKKWHPDLHPENKQEAEEKFKEISEAYEVLSDPQKRRMYDQTGTVDFGAGGQNFNWDNFTHYSDLNDIFNDIFGGNFASDFFSGFGRGQREEQYDLDLYTNLDITLEDAYYGTEKRIKYRRNAMCPDCNGTGAKNGKLITCPTCNGTGQQRIVRGQGFFRMVTVTTCQTCGGRGRIPEEKCPRCNGTGTVVVNEDISVKIPKGATDNLRLRVQGKGQSYNGRTGDLYVVLRVRNDRNVQRINDDLMIDQKINFAQAALGDTIEVNLFREKYSLKIPEGTQPGEVLRIKGAGMPHLNGHGSGDLLVRVNVEVPKRLTQKQKDLIREIFDIKENHRSWFH | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 41584
Sequence Length: 365
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q9WZV3 | MKKEKKDYYEILGVPRDATQEEIKRAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPTYQETESGGFFDDIFRDFENIFNRDIFDVFFGERPHQEERREYARRGEDIRYEIEVTLSDLINGAEIPVEYERYETCPRCGGTGVEPNAGYMDCPSCGGTGRIREERRSFFGYFVSERTCERCGGTGKIPREYCHECGGSGRVLRKVRRTVKIPPNVEDGTHLRITGGGNAGYYGGPYGDLIIIVRVKPDPRFKKSGSDLVYDVTIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVFRLKGKGLPNRYGRRGDLIVNVHVEIPKSLSREERKVLEELAKKRGVTIG | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 42358
Sequence Length: 369
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q8DKR7 | MARDFYEILGVSRSADAEELKRAYRRLARKYHPDVNKEPGAEEKFKEINRAYEVLSDPQARANYDRFGEAGVSGVGAAGFSDFGIGDMGGFADIFETFFGGFTTSSRRQQGPTRGEDLRYDLKLEFREAVFGGEKEIRINHLETCKTCQGTGAKPGTRPVTCSTCGGVGQVRRSARTPFGSFTQLTTCPTCGGSGVVIEDRCESCGGQGHIQVSKKLKITIPAGVDNGTRLRVSGEGDAGLRGGPPGDLYVYLFVQPDPEFQREGNNILSRIKISYLQAILGCRISVSTVDGEAELKIPAGTQPGTVLVLEGRGVPRVGNPVARGDHLITVDVEIPTHITHEERELLEKLAKIRGERLGKGGLEGFLGSLFGG | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 40261
Sequence Length: 373
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q73Q15 | MPASKRDYYEVLGVDKKASNDDIKKAYRKLAIKYHPDKNQGDKAAEEKFKEATEAYEILIDEKKRSMYDQFGHAGVDGMSGGGGYDPSAFQGFEDIFGGSFSDIFENLFGGGFSSRSSGFGGRHAGPVRGSNLRYDLQISFVDAVYGKKAELSYTRNEKCSECHGTGSESGSSKRMCPDCKGTGQVRQSTGFFSISRPCPTCGGEGSIIEKPCKKCGGNGLERKKQRIIVTIPAGVENGKRITIPSQGNAGQAGGDYGDLFVFIFVQAHPYFERNGIDLYCAVPISMTQAALGGEINIKSLDEKTLRLKIPAGTQNGKLLRIRGEGVPTGIGRKGDLYIQIQVQIPSKLSSNSKKLLQEISAIEGENENPNLIPLKDLP | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 41084
Sequence Length: 379
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q83MZ4 | MEDLYGILGVDHNASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALLKKIMPNPPKPKLAKRTSGFFSWLKNKFT | 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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 38520
Sequence Length: 348
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
|
Q39079 | MMGQEAAPTGPPNRELYALLNLSPEASDEEIRKAYRQWAQVYHPDKIQSPQMKEVATENFQRICEAYEILSDETKRLIYDLYGMEGLNSGLELGPRLSKADEIKEELERIKRRNEEAKKMAHFQPTGSILFNLSVPHFLVGDGIMRGMVMASQVQSQLSKDDAIAIGGNLAANEKSGGGVATAILRRQISPVSSIEFVASTGLQSLIGVQTTRQLTIHSTATINISKSLSDGSINLTNTWTRQLSETSSGNIELALGMRSAITVGWKKRDENVSAAGDFKIESGGLGASARYTRKLSSKSHGRIVGRIGSNALEIELGGGRQISEFSTVRMMYTVGLKGIFWKVELHRGSQKLIVPILLSAHLAPVFATGAFIVPTSLYFLLKKFVVKPYLLKREKQKALENMEKTWGQVGEARARAEKAQQLLQTVATRKKNRQVETDGLIVTKALYGDPKAIERRNEGVEGLDSGVIDVTVPMNFLVSDSGQLKLHEGVKKSGIMGFCDPCPGQPKQLYIAYTYHSQPFEVIVGDYEELSIPQEGQ | 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 Length: 538
Subcellular Location: Membrane
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Q9ZSY2 | MSAKKLEGSSAPANRRDPYEVLCVSKDANDQEIKSAYRKLALKYHPDKNANNPDASELFKEVAFSYSILSDPEKRRHYDNAGFEALDADGMDMEIDLSNLGTVNTMFAALFSKLGVPIKTTVSANVLEEAMNGTVTVRPLPIGTSVSGKVEKQCAHFFGVTISEQQAESGVVVRVTSTAQSKFKLLYFEQDSSGGYGLALQEEREKTGKVTSAGMYFLHFQVYRMDTTVNALAAAKDPESAFFKRLEGLQPCEVSELKAGTHIFAVYGDNFFKTASYTIEALCAKTYEDTTEKLKEIEAQILRKRNELRQFETEYRKALARFQEVTNRYTQEKQTVDELLKQRDTIHSTFSVVKTPSGNNLSNGSSSKAQGDESKGDGDSAGEEGGTENRDKSKRKWFNLNLKGSDKKLG | 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 localization and/or activity of auxin efflux carrier components (PIN proteins) or other proteins involved in lateral auxin transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45484
Sequence Length: 410
Subcellular Location: Cytoplasm
|
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