ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7R9NWH3 | MAGFVLKVKTKSGQMVVTSLNSKSTIADLKTTLSSLTNIKENCLHVLSGFPPKPLNLSPDEASLETCKITSGDTLIVEEKEPPIESVSFSSSLQEEARHHIITDQFASPGILMKKVVPADNSCLFTSLGFVLGGTYPLIKKIERPTKSCYIGDCKAILLYVRLPYNTILYYWSVWIALFLFGWKQKLCQGRCARGVGGSIQTIFLASDQRVLNEAYDIAKEAKSSRQFTDVDKFTLRCMVCSVFLTGQIQAQQHAKESGHMNFGEIK | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of u... |
A0A6B9M1D1 | IWINTTTYGLLISLISLFYLNQPNDXXXXXXXXXXXXXXXXXXXXXXXWXXXXXXXXXQHHLSKEPLTRKKLYISMLILXXXXXXXXXXXXXXXFFYILFEXXLIPTLIIITRWGNQTERLNAGLXXXXXXXXXXXXXXXXLLYIHNFMGSLNFLMIXXXIQXXXXXXXNIFLWLACMMAFMVKMPLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A6B9MA59 | MIWINTTTYGLXXXXXXXXXXXXXXXXXXXXXXXFFSDSLSAPLLALTTWLLPLMLMASQHHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTLIPTLIIITRWGNQTERLNAGLYFLFXXXXXXXXXXVALLYIHNFMGSLNFLMIQYWIQPLPNSWSNIFLWLACMMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRIXXXXXXXXXXXXXXXXXXSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAVLIQTPWXXXXXXXXXIAHGLTSSMLFCLANSNYERIHSRT... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A6A0GUF0 | MRRSKMRMRVRLAGLGVFVVVGMIVLYPSPLKTRHLNTIRSIFPQSKLTWQLQPAAAVSSPLNSSSSTTPTVVDTRDQVLANVHLPKSVPVQEPPVQSIPSPHLEGDSIKIEDKATPANFVDVPKVGALPKPASSSNVPWHENPDEVISPARLRERAAKFPPDSAIGRFMAEQSRRVEHIGRQCAMSRKEMPHEILGYEASVMAINAYAHLIFDRRNSLTFCPVYKAASTSWSNNLLQLSGLVPSKRRQPAAAIQNLLGQVFPRISGIAGPSLTKDTIKFMVVRHPFERLVSCYRDKFQDGLKDYYYEMYGEKMVHLYRP... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 407
Sequence Mass (Da): 45965
Location Topology: Single-pass type II membrane protein
|
A0A0D3FW43 | MAAAAGLFEELLIRFGDWIGEEMSIPHLFRCPISLDIFTDPVTLCTGQTYDRPCIERWLAAGHRTCPVTMQPLGDATALVPNRTLRHLIERWLSTDQHHHHHLPEPAAPAAEAEADAEEPSLAALKPLATSHRTLASPLAAAGHRSTPPRQASTSKSKQARKIQWQHARPSNKQVHEQ | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
EC: 2.3.2.27
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.
S... |
A0A2D0VM52 | SLLVRFLIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWILPPSAILLTLPFTLALFGVGDGALATGWTFYPPLSVQGGIGVDFAIFAVHLLGISSVHRSPKVIETNHNMFPPGMTLLKLPISLCG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A3S4U1V6 | MFGIEEKYRDLIRDGNENVKFLFLEGSFDLVLERMKQRKGHYMKTDMLKSQFDTLEVPQEDEPDVIHIDIDGSFETVVERCVYALKPLL | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 89
Sequence Mass (Da): 10514
|
A0A1L7WRG5 | MATQAPPEPQVPQPNGIPKISARKPHFGGSAKHIYDTVCVGFGTVGLGLAVALSDLTLDSLSNVLFLERSPRFSSNTASEEEYMQTTFAQDLVTLRCPTSPYTFLNYLAEKQSLESFLSSSNSLSPTRKAFGEYLEWSAEQFKDVVVYGEKVVNVEAVSIQGAGKLWVVTIQNTQTRDLGTLVCKRVVFATGREAKLARLSWKYEDFEKTGSTEVLPAIEQMREFCSPQSSQDEVLSTLAISSGKIAVSLMFESEGNTKRAAL | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 263
Sequence Mass (Da): 28811
|
A0A8J2VZM9 | MRKRKSLKKADEESDASEGGAEPEEFQDSGEDWTPDADSNEQPVRGGRKRTSKAAINNSKKKRKNSSSEESEGEGEEDDEAEDEEGELEDEEGSDDEKNGSDGNKSDSSQSKDIPKHFHSGNFVLLKSDVKWDGDTVISKLDELNLWKIDGKALLQKFIPMESNGKILHKCTCVYSGWNVDNRDNYYPITEILNRNPQTDSKEICVALDLNDLIMGIAIQSKKCAMCRTHIPRDYFDHPILLEKQPVDEIDEDCDNNKYQWYYEGRNGWWKYEERSNADLEAAFTSGVSECLLLLAGTIYCVDFQNMVQIRRSDPTKLRR... | PTM: Ubiquitinated; autoubiquitinated.
Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Catalytic Activity: S-ubiqu... |
A0A7R9FK99 | MILAKSAEEKSLPVELVDLSTYDPEDKLTEETSGQSLCVFVLPTHAEGKPPEAAAWFYKWLQEAAHDFRVERALLKGMKYAVFGLGNSQYADHFNEVGRSVDHWLHKLQAMRVAKLGAGDEDTVASRHGSIEADFDDWQNALMGCVEKWRAKSNCRCGGKSQPQEERIEEASSCDSQSDAGEASDSEWDSDPSQEVKSAVLDMEELGNFSSALRAARKRKESEESEGTREMITPLLRESLTKQGYKLIGSHSGVKMCRWTKSMLRGRGGCYKHSFYGIESHRCMETTPSLACANKCVFCWRHHSNPVGTEWRWKMDQPEE... | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylgu... |
A7SP58 | MKPAWEPEVKPDIFTLVLIISAPGNKRQRNAIRRTWGRAENWDCLRLYTNHEEYSYQSVFMVGSTTDAVDNFVMDEAETYNDLLLGNFNDTYSNLLFKSLMGLSWASNVVNCSYVIKTDDDVYLNMPKILQWLQTRNKTARLYAGKVASGWSPIRDPSNKNFIPYTDYAKKTLPDFCPGTFYVLSRNILHFLLGVARFIKPLQTEDVYIGMLVQAIGLDP | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 220
Sequence Mass (Da): 25258
Location Topology: Single-pass type II membrane protein
|
A0A8H4S4S0 | MLESPKAEITFDQVTNALKSVPDEEIFTRWPAPGIELMQAPAALIENFYIKRPNPEMYKVMKEHNALSQLSASLLAEAKVLESLSQHPHPNIIRYYGCRVLRGYFIGLVIDKHPHYLYTYLKNRVGTIEKRSFIAALESSLRHLHTHGLTHNDLTPRNILVSKEGMPVLIDFAGCQPIGTYLKHIRGTPGWINGEIKDHNTSKKEHDVSALAKISAWLDKPVFDQ | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
W6KVA0 | MIFCHRVFACLLPRWLSGHNQCISLEYDSCGHLYDDQRLKEVRHWDGVHMYHIAYYGYTHETLFVFFPFIPFMIRFVRWCIVRAFPLLYRLAPVSFYVSGLNIFASAGAGVVLRHLTILTMLGPETERTIQLWRRHRQGRHAGIGRGHLATVYEMDTERRSEDFKEAIPTSALCTAGTVPTLSSHHWGSIRGILQDNQYVVNLIYGVDDNHACKAAGILLNFPHAHAAAAFRVIQGYHGTVLDKLSPFLLTTSIHDTAGLTGCQTSHNVLSMFDTKDTKQGSHTYLPSLTSEAAREVVFRWRVVGGAVLVWLLTPAVVFT... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 714
Sequence Mass (Da): 81480
Location Topology: Multi-pass me... |
A0A6A3D0I8 | MSGRNMFPFTATQWEELEHQALIFKYVVSGIPIPPDLLFSIKRSCLNTRLFSRQPPPPHPHVGWNCFQVGLGRKVDPEPGRCRRTNGKKWRCSKEAYPDSKFCERHMHRGKKRSRKPAEVSTGTSSSTRANPSLSFMDYRRNSYVYGVKEEVDSHAHAVFSGASMDNSWQLTPLTTSSSSSKQNEYSYLKLQNNKDVGEAQKTVHRFIDEWPLKHGDP | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 218
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 24974
|
A0A7V0JUC8 | MRRLAELLQESNDAWAFTGAGVSTPSGIPDFRGPDGLWRKYDPGKVSSIDAFQRDPKSFYEFWSYRFQVMAAAEPNVVHRFLAWLEERGMLRGVITQNIDGLHRRAGSKRVLEIHGRADRGICTACGRVYPLGELLKRMEGDGVPRCDCGGLIKPDVVLFGEEMPPIFSQALEEVKKADLFLVLGTSLLVWPAERLVPLAARHGATVAIINRDPTPYDGLAEVVIRDDLVIVIQELWELLKGEGDDRREDR | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide... |
S0FWF4 | MMPCNLILIGYRCGGKTSVGKLLADLLSYDFVDTDICIESNCRSSIDVLVADRGWAYFRQKETQVLEQVLQGNNQVIATGGGMVLAPENRELIKTHGFVIWLAADVTTIVQRLETDPQTQATRPRFTSRSLKDETRDTLAQRIPFYKKLADMTVDTTVHPPQHIAEIIKRRLDHVRI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A6A2YTP2 | MQELWDDSVTPNKMLQQLTFSWFSQKYLAMKKRSEDVQRRVKEILEILKKVKGQARIQALKELRQVVQAYGTAHKTVMENGGVGLISFLLGPFTTHAVGSEIIGVLVNLNLDSNFKSDLLRPAKMSLMVDILNEWSIETKIKFPQLVELMPGLNNECLELVLYLLELFSKIPEGRLALKDCPRTIPNVVKLLMKASENCTQLALSILWAICKFAPEECASLALDAGLAAKLLLAIQSGCNPVLKQSENAGITRGGFENEELLKRVKEGSSFDSNGWFDKVSSTLAIPCNRKFVVDVTGRVTFETIRFILEFLLWKPSDGL... | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
EC: 2.3.2.27
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.
S... |
K9SE74 | MTDNAPTDNAPNGIEIDTETLITQLRQKQGTWVDWAIACQQLQKHGQSAQQIFEQTGFEPIQQNQIIVAVQVYAGLVEDNASEPTLNHFKQRGSDSLHELRILSKPDRLAVAELLVSRGMDSIAAKEAAKAVKEIQILSEAPSGFTRHPGDAIAYQAWKSAQNQRDPQQRAKFISKALQFAHSDTARTEVEKLLTGLVDPTVAKAPRLPIFRLEESDEMPRVLPLAGKLPLTVADLQAIPTVETIEPFRMVRTSGDFTWVALPGWQVVRRAIDAVVILADTDTFKEASGQEIRSSFPNQAEEILLLVDRAQVEWQSDRYY... | Function: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.
Sub... |
A0A6A3BY42 | MEKLDHIKSHLPSPSLSQISENEKNGFINLVSRYLSGEEQHVEWSKIQTPTDKVVVPYDALAPVPEDPAETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIQVRSGCTFLDLIVSQILNLNTKYGCSVPLVLMNSFNTHEDTMKIVENYANVNLKIHIFNQSQYPRLVAEDFTPFPCKGQPGKDGWYPPGHGDLFQSLKNSGKLDTFLSEGKEYVFVANSDNLGALVDLSILILISSALEILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDAHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADA... | Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
EC: 2.7.7.9
Subcellular Location: Membrane
Sequence Length: 976
Sequence Mass (Da): 107172
Location Topology: Multi-pass membrane protein
|
A0A0E9NF46 | MSNAGRWVKALFWGTVIAVGGHQLQYYIMPSEDELVKRLSPALKKEFLEQRQRRAAEDIDNGAQLMAHIRANAQKTEPAWKTDWGKKPDAAAQLDRETAAVVMTENALLYVWKLYDIP | Function: Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 118
Sequence Mass (Da): 13441
Location Topology: Single-pass membrane ... |
A0A1Q3RDY0 | MEIKKYDVIILGSGISSLFLANNLDVDLNVLILNSGQNRETNSYLAQGGIAAAVGVEDDWAHHFEDTMIAGHGQNNKELVELMVKSGPSVICDLVELGVSFDKNETGEFALGLEGAHSFPRIMKAGDHSGEAVMDALWRNLKNKPCLTFSEHTLAYRVDSYQEGFLVQTLSTQIEDSNEPCLGTFFCSKIVFATGGISKLYHRTSNKSIGYDGLALAIDLGLKLSHLSWIQFHPTVFYNLVGHQEGFLVSEAVRGESGMLLNQRGERFMNRYHPKLELAPRDVVSAAMIKEINGQEKPYLYLDVRHIGQKKMMQKFSKIT... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 495
Sequence Mass (Da): 55448
|
A0A7R9IQK6 | MAVEEIHLERCVPELFQDQSVLVTGATGFMGKVLVEKLLRSCSDIKHIYLLMRAKQKQELDDRFREFTSNRTGSDNPCAALVARLNGISVNPALGGGGNVAMKFVATVQCQRCHVLNWKARDADLTQTGLGLSNDDTATLMANVSVIFHCAATVRFDEPLRHAVLLNTRGTLELTRLAANMKNLQ | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 185
Sequence Mass (Da): 20370
|
A0A7R9NV93 | MRPCCSETTPTLWCPMGRVKEHETMLLRDNSHPLVCELHVAGYKFSVLNNAFLVHKGLKTAGSFHSDKDLDQERNRVLFRHFKLELREKYPESSRRCWCLGSRRWPLSWSIALSPVSSSGSSLSEPCQSRGCSLAREIAKKRTGSDEKDKWVGRGKDRQKESRQRMLRWDR | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(... |
A0A7R9P128 | MFGQYARTKQSGSLVLPAKLNMSGFKDEHNFDTLSVSECIVMGLSSKRKGRWRYRFWQKMFLTLIGLPLLVGLVLGFVAIFRAVFVTQLDGSMLHIIDDQETQDIVDESQSMERAERLAGALKIATISYDTDHQENENLLAFIRYLEKGFPLIHSRSFIKREVINKYSLLFTVQGLTRGKLPYLLASHLDVVPVDAKAWEFPPFSGRIVNRTYVYGRGAIDDKAGVMGIMEAVEYMLQKNQRPQRTFFMAFGHDEEVTPPSSPDNKPEDMIASTSQSPNSETNTMPLGTNLPNMVTRSGRVVHPPERLDL | Pathway: Amino-acid metabolism.
EC: 3.5.1.114
Catalytic Activity: (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine
Sequence Length: 310
Sequence Mass (Da): 35069
|
A0A8H8DCP2 | MDDTDKPDPILKQVPLIKNPSYQPPKAISLRTNYSKLLPTLSQTVIPPNLTISKEDIDKWTTEVDQFKNRIHSELREDDSVTNYETWIKEQSTKFAPGFDYPLPPNRKFDLIKNRNTFKNPVFAQWKVPTKAQRFVNLPLKDRCDLYFKSATAAEFDVNFWNSFKPDPHVYKRRKWIRDRTRSEKRKYKKTADWKEEYDRQIALEFATVAKEYSGLEHRMFDEVGHMKVFGKCFAGEVNNGNCEKPQQKLYPWLTNKLPLVTTVDGEVKSKQVEGCVTQSLVANEGQGIVIPTQSKHVDNVCRLMNSLIALENKLPIEIA... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 885
Sequence Mass (Da): 101772
Location Topology: Single-pass type II membrane protein
|
A0A662EYI6 | MKNKLVARILYEIADLLELEGVPFKPRAYRRAAQAVESCSTPIEDFVAAGKLSELSGVGKAIADKIEEIVKTGKLAYHEELKKKLPIDLYSLTRVDGVGPKTAKLLYEALGVRNLDDLERAARAGKIREIKGLGKKTEEKILRGLAEARRTEARMPLGHAYPIADELRRRLRKTGLFTRLEVAGSLRRGMETIGDLDILGTAPDPNAAAAAFVGLPDVEEVIAHGPKKSSVRLSSGLQVDLRIVPEESFGAALQYFTGSKAHDIALRARAVARGWKLNEYGLFDEGGKVLARKTEAEIYARLGLSFIPPELREDQGEIAA... | Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in ... |
A0A1H2XTL1 | MIGRISQMMQAQCAPGKGAALALSVTLGAAFCLPVGAAAQGQPAAPLIVLPVDDGPALSPEMQENLLDMRIGADRRRAPEPDVAPPPPLIASPLRALRVSDALRANVLRFSGERHVEDFSLFVADPDALPTGERALVLSMISSVNVLPERSEARVSINGTFVGALELANFTEFTPARFAIPAGALRAGHNDVQITVAQHHRIYCGPEASFALWSEIDLAGSGLSLGDTLQATGPEAFLMGLAAQAVQPGGVEVRGAEGLGAARSQWLSLISARLSNVMAGAPLVYRFTPYWSLEGEAAARARVTFVPGLANRVSFQRGAD... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 783
Sequence Mass (Da): 83413
|
A0A6A2WKP6 | MGLLKLLKLQLNDMHESQRNDRNQRGLGRDRGHGRGGSRSRLELLSKKEIVKGLPHINHPDQLCEGCLVEKQLRKSFPKESELRARKPLEFIHTDVCGPIKPISLGEPQREFETPPTSPTSTTQGDSSPSSSGSQSERVVQRTRNFRDLYEVLNECTKQNAKGDIERHKARLVAKGYSQKAGIDYDEMDVKSAFLNGVPEEKVYIQQPSGYEVKGHKDKVLKLKKALYGLKQIKDRDILIVCLYVDHLIFTGSNPSMFKEFKDVMMKEFEMTDMRIMAYYLGIEVLYTLGGLENLQTAKKYYASTIDLTGGKNTRALFGL... | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 465
Sequence Mass (Da): 52038
Location Topology: Per... |
A0A6A2XL12 | MAQLLKLSLFTYNSIQAFGWTISLFRILTSFIAINSVNGAYDCAGDLICQFVANLCILGSCTWSNRDCSKWSVVPLMQWGGRTHFLLAIVLRIHEVQEVPAVFITFFAWSLTEVIRYSYYALNIFGGCPSWLTYLRYTTFIVLYPLGLAPGERPALSFLLFFFSLKNEKRRTLSLLSKFPSPDRRETISGRPPSNPPPATTSGGRKLQNPPQIKAWFPLKLNPEFSFISLDEALVGPVIRVKFGESPNYVVTHPIVMTWGLCGTPGSFWRGSSQRRRCGGSGSSGGWDGIIQPLINLGFLLGSRFGFGCKWASGIGPVCK | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A6A2XMP7 | METDTFHSRSKNRTTRIGWCSATAVLGVHSQTRAQVGRGGLWEFNDGMARGDEEQRKDSRAFKDRLMVPVPKADSTDYRESSQPPFGPELKGIMVVQPDGPSFTVDGGRVRWANWDFHLSFDARVGPIVSLAAVYDTEKQRFRRVKYREFVSELFVPYIDLTEEWSYRTFFDAGEYGHGQCAVPLGTVRRTQFSWTHLFPAAMGCPLRSLTFSPSSNAMPVTEVRPDVSLVVRMVSTVGTYDYINDWEFRQIGSIKVTSSPRKSYWKVVSETAKTESDAKVKLGLQSADLLVVNPNKRTKMGNFVGYRLIPGLVEGPLLT... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 417
Sequence Mass (Da): 47492
|
A0A6A2ZPP9 | MLIALRLPSLLIICRVSNRGRSRVFGYFGFIVIAAVAGAITAVAGAIAAIADAIAAVAGNSDGGKTAISRSKSQSQTELDEPDARIADYFDIVAGTSTGGLIAAMLTSPNKDNRRQPIYEAKDIAKFYLENWPKIFPQDRF | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 141
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 15064
|
A0A1S9CB32 | MDNKVIIIISIVVVVLLLAIVGAVAAVLLLGGDKAPVVVDPNQRPEVVITVPLTTSLMVNVTDEDGKPHVARVHPAFELDASKDAYKELNETTLPLMEIRIRTEILNVVSKYPYEMLLEQGAPTRVAIDIKDAINTLLDTDIIFQVIWQDFIVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 154
Sequence Mass (Da): 16980
Location Topology: Single-pass membrane protein
|
A0A8B7PMZ1 | MQWHSTKLLLALLLVLPYVVLFTAYCWWGEDQKHVSPAIQRSAALAPRTPAAQRRGRHLASYCNSHAHLRTGRQSSRDIMVSRPHRLAWCKIPKVASTSVVQSLLKVLGCENLIEELGISGQHTALRRLMPHLSADEQPPDASTTFMVVRHPFLRLISAYRDKIATKSGKMVMAQFQKFRRLYNMPIISKYRQQEPHDKFYKDVPTFPEFVQYLLETPVEDYNEHWRPYHVICRPCDVPYNVVLKLESLDEDIQTLVFITGFPELAISKTHQSAAVIDEGLELRRASDLQSNQHPENFSTPPMENSERREHRSNDSIELK... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 366
Sequence Mass (Da): 42261
Location Topology: Single-pass type II membrane protein
|
A0A1T1CZI6 | MPAAGWGGAALLTSHVWLLWLHPLDWLGVPDAPSRLLTVLLWLLVGGGGSLAVGLWWWLARFYPLPQFRDALTMALLWGCGEVLLARGPLFWLGLSTVAAIHDRALAGLGSLAGPGGLAAVQVLVGWWLWRSCRTPSCQRSRWWAGGAVVVVALHGLGLVSLADTQGPSVPIGVLQPAIPTRQKFTWTAMAALERRLVLAMNRVAQKGAPWLLVPEGTLALDQSPPVVDGVGLVTGGFRRQQKGLRNSLLVYPVGAHDPAMALDKHRLVLLGEWLPWSGLLANAGLSAVGGLQPGPEERLLAGQPLPWQAGVAICYEISQ... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A3M7QPF3 | MNKELKEVRILMLGESGVGKTSLILSLVSEQFLDDTQDPNFDLPAKLEPITIPAEVTLEKIPGVIIDFSFREQNEQDLIDEIEKSSVICLVYSIENEDSKHKLSSFWLPKIEEIEDARFNSNSSFQDQNQFKRPIVLVGNKTDTDIERTSPTQDSVITQLVRSHSQIETCIMCSAKTLKNVPEVFYYAQKSVLYPTAPVFDVDKKQLTPLGIKCFTRIFKLCDMDNDGRLNDSELNEFQIRCFGVRLNSSSLQEVKSLLALNSENLIENEITLKGFLHLQMLFFKKGRHETSWTVLKKYGYSKNLSLSQDYTSINLKIPD... | Function: Mitochondrial GTPase involved in mitochondrial trafficking.
EC: 3.6.5.-
Subcellular Location: Membrane
Sequence Length: 698
Sequence Mass (Da): 80404
Location Topology: Single-pass type IV membrane protein
|
A0A498JKA6 | MMPAKSKDEDPHIKHGAQTVLQPICSQPWWRGVGNGSASSLVDHSNSMVMNGAMQAQPNARLDGGGANFHKELRTTVGSQSDGNNGSENEHIKSVSSSVVPALGEHVDPNSQMELVGHSIVMSSYPYSDPQYGGMLTPYGPQAMLPPHFYGMHPGRMPLPLDMEEEPVYVNAKQYHGILRRRQSRAKAELEKKLIKARKPYLHESRHLHALRRARGCGGRFLNTKKQDANDENSSLEKGMNLDGNHSAQSAKSGFEYRPNTSNGNVDSSNVQQDGSGPWFRTHNHHTHSNGNGNDHGPSSAYPSTFGDSRENMQLKGLSR... | Function: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Location: Membrane
Sequence Length: 688
Sequence Mass (Da): 75742
Location Topology: Multi-pass membrane protein
|
A0A3M7SUY5 | MSSQIPPALSASKKNTFAYVTIKDRLPVTITKAIDYLSRFRNELAQRYSEDIMSDLKNAIELLSQLRYELTTDKNLKEITDSGSDSTLWNTALEELKSQIGPDNCTWFKSPWLFAECYVYRRIREAMLLCTTSLKDYDPYEKSKLESHEQSLKSVFQLITNLCPLNFNEEKQNESLMRERFREIMEALLWANKNDLSLSSGNDVSSKIHNLIELLDSFRPNVLCDHTEELWQFLKQLKSKKEHDNVCIDIVLDNCSIELAADLILCDFLLRNEFVHKIRLHGKAFSWFISDVTRSDFNFLIQQLQSSNSLIINNFLRRLN... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
A0A7S0RDP1 | TPMTHGAYLLATFQEVLETMNGSNYQEAYNDAVQFRSEARTLFRLGVLSMREAVVAEDLHAQVVAEALRMAPPGDLPEDFLAAARASTAIYHVNMSIFRSAPDTWAIGQVFPIMPLH | Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
EC: 4.1.1.19
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Length: 117
Sequence Mass (Da): 12939
|
A0A2P4WAU8 | MQVQETSKTIAVDKRYKGIMDVLTRVPKEQGYSALWRGNLANVIRYFPTQALNFAFKDTYKNIFQKGVDREKEFWKFFAGNLASGGAAGATSPDGKQLNFFASWAIAQVVTVSSGILSYPWDTVRRRMMMQSNRKDILYKNTMDCLKKIMRDEGTMALYKGALSNVFRGTGGALVLAIYDEIQKHI | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 186
Sequence Mass (Da): 21045
Location Topology: Multi-pass membrane protein
|
A0A1F3J3G4 | MAQVIPNLSMIVAVDSKNGIGIRNTLPWHLSDDLKRFKEITTDHTVIMGRNTWFSLPKRPLPNRRNVVLSPDPLGETGAEEVRSMDEVFDLCKGDTENFVMGGASMYEQLLPHTSKLYLTCVDGEYEADTFFPELNEKEWELVDESDIMVDSKSGIEYQYLVFVRI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A8B7P9T3 | MSSKEEWAAHLEVSELLHAIHRGVGCPPPAVDNAAVDNAAVDKAAVDNAAVDNATVDKAAVNKAAVDNATVDRAAVDNATVDNAAVDSAAVGNATANGAVKSLYTMPLKKILLWTTFWKSYKYYETFFARLHKQQCEVNACVVTHDRSQLSSADVVVFHTNDFLQSTPLPDPRPLAQPWLVFSLEAPPVQAHQGIGRIDWGRLNNVVNWTMSYRRDSDVVAPYGVVVKRTIPEIWRRDHDYTSGKKFEKMTAWMVSHCQTHSRRESYAAELSKYIPMDVYGSCGNKSCGLSLVHRNIGKFNSSDCDQVTGEYYFYLAFEN... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 470
Sequence Mass (Da): 52552
Location Topology: Single-pass type II membrane protein
|
A0A8B7P0X7 | MSLLTNFHFIMAVVYGYSSYFYVYGVVQPAEITAAQKSTYGAIKYLTYWDLLVQCAFFTLCFLSNVFSSAQQNKRKTAPEKILDFLFSSIVFPLALFTDTTFWGLYFTDRELVFPKVYDDFYPSWLNHVVHSLPLAAALLEMLCVQRSFPSYKKGFLCNSLFLAIYLSWVLFIAHTTGDWVYPVLAKLPTPQRSLFIFGLFVLMWLCYSVCRILYSFKWRQPARSEKKVHQKKNK | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 235
Sequence Mass (Da): 27435
Location Topology: Multi-pass membrane protein
|
A0A6A2YMY3 | MALGKYGRVDNSTTGNRRSSSSSYGSTVTKVVFVGFCLVGLWMMSSSSVVPDQNMDDVAHEKKIHIDDQGTGNLNTQENNGNTEESKLDESEKDKKQLDSEVERTNNNSGENFPKDASGAKDGDNNNSGENLPKDASGAKDGGTGNLNTPETEESESDESKKDKKQLDSEGGQTRVSENKTTEESNLDDSKKDKKLLDTEGGQRNNNDENLGGSGGSEENPNDKKSDPGESNEKAVSNENDKKSDSGSGEKKPDEKSSETNVDQNEKNEYNKKDSEGGLSNNNSGKDSEVNPDEKKSISEEGNNNAVFNDKNVNKSDSGG... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 657
Sequence Mass (Da): 72150
Location Topology: Single-pass type II membrane protein
|
A0A498KFU4 | MAENFAVPKYWTTLSLVLGFMMLSATGTSLLLPSLGDIESLLLNDTGSINSTSTDYGHIVYEFAAAVLNPTSPNDIVSLILSANNNSAPVSVAARGQGHSVRGQALTSGGVVINMTALIRNGSRIVVSESPSLGSYADVGGEQRWVDVLRATLERGLTPVSWTDYLYLSVGGTLSNAGISGQTFLYGPQINNVYELDVVTGKGELVTCSSKKVPELFYAVLGGLGQFGIITRARIPLAPAPKRAKWVRMMYSNFSAFSRDQEHLMAPNGFDYLEGFLLMKQGPLDLSFYPLLDQPRIAALINRYGIIYYIEAAKYYDDST... | Catalytic Activity: A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
EC: 1.5.99.12
Subcellular Location: Nucleus
Sequence Length: 885
Sequence Mass (Da): 100032
|
A0A8B7NTA0 | MENSTHIQTGTKHVLSEDSNEKAAKKRVLPTFPIIPSSRFGTTTAPTLRHPLFIGDFSLDGDRKFHHDRRSLGFISIDWDQSQTKKVEYDLNIAMDKVKRKDYQRCVRENLDNLLMWILLNRYKFAVSPPPPPPPTAPMPSQHSSSQAPQQGGQPHSSSHGDATKSARPNPVRGASVDSLQNPLAASGPITSLSTDFVTYRGLLRDLMCSPYQKEGWIILATKFRRTIYLCGIDSVEKQLEKENETENQKRLCSWGFKFEQFMTDGADPNEGHDENKEYCCVLRSRLASHSLVYGAEVDGADPTRYNPPHGHLTPFVELK... | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 454
Sequence Mass (Da): 51408
|
A0A8B7NWV5 | MARVGLILNVVLVCLVTASNAIGETNYMFKSGVFASISNVEDLLHPEGEIMRRLEKYYMSAENTLESLKRYIEAWRALDFESLLGEDSLSKDRYYERKRLGFRMKEGELRLQLRKLQSKTATSKNKRGDDFPLANFLHQDEKENETSTEDIESQIVKVQSEIQLVQAEYDKYDVKTHKKTSAAVTRMSAGGVQHPVDTYLLMKRLTKEWHDIEKSLLKLHNDTFKVLDDGDHDREKYNFPVAADLNGAAVALIRLQDLYDLNMKEFGDGLIPAAVTNSNHDIRSLGKLRTWDYILLGKEAVKLGYNKRAIQWFKLAVKNS... | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 631
Sequence Mass (Da): 72590
|
A0A662F4L0 | MNSRFFHFGEDNRGGYHFDPRALPENVRLLGNGQLGGKARGLLFVIDHLRHGGRLTDYDPLIGFPDSFIITTDVYDEFMEENRLGESVLARCAGEISTEELQARIVAAHFPDEARARLAEFIAAEHRPLVVRSSSVMEDNPNHSFAGIYLSEFLGNTGSDADRLEALVGAVKRVYASTFGRNARAYRKRHGLPWEKEKMAILVQNMIGRHYPHSLFYPLIGGVAFSLNFYPWSDRLRPEDGVVRLVVGVGTRAVGREYARVFSPVMPGLRPEGSDTKAIIRYSQETVDVLDMQSGRLGQRKLHQLDNPLLAEVCSVVSPD... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 581
Sequence Mass (Da): 64467
|
A0A8B7PJY0 | MFLEXQPEVSGGNLGATYKFDQYHLHWGADDARGSEHTINNFRFPMELHLVHHNTKYASFNASLEHRDGVAVLGVLFVISELDNPLLQPLIDHLMSITEAGQEDIAVDLYPLASLLPQDRSRFYRYHGSLTTPMCNEVVTWTIFDDYLPVSDAQMARLRSLSNIEGNPLVNNFRPNQPLNGRAVYRSFLY | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 190
Sequence Mass (Da): 21650
|
A0A7C4TK19 | MVSDMFRGIKQYKTLLVEVVCILILTISLAVGSYLRLQPVYNALKYGYGPTLYEMDPFLNYWIVSKLYENGLTYYTSLTSENPVTKIFWYPYGRDIPATELPVLPYISLFTYYIAHAVNPSVTLYEWLVYLPVVLYIISVVGIYLTVRELYGPLPATIASLTASLMFIDRQVAGFTVKYVLGLAFIFPAIYFHVRAFKRDSTTSALLCGIVLGISAISWAGFNLVLAAIFLQYVLTPLIRGSMDMRYFKLWVYEMLPLTLIILLTPSYYNGYEYLIRNAGLMIPLGTIVLVIALTIFYLPRLGIVRRNSKLYKPRFIYFS... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A165B9P2 | MSDHPDEFFLYYKMTDLAKSSKKSSNEAAGWDIYAAEMHEIPLHSRAVVGTGVVIDPPKHTYTRIAPCSRLAARGIDVGAGVVDPNYTGELKVVLINTTDFIFSVKPGDRIAQIIFEYYAEGLPSQSYQPL | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A6A3CTA2 | MAASVANYDYIVDWEFQTDGLIRIKVGPSVILMVKGTEYDNMNQVEENLFGTLLSENVIGVIHDHFITFYLDMDIDGSDNSFVKLDIKRQDTSPGESPRKSLLLGSGTPSDTRWFLPATPLVCSTTTIRRRGEVHSQLTRFGFRVYITEASNGLVDCLITRARVTTLLLFGPKENKDIVVWYTLEFHHIPCQEDFLIMPKTASSSFDLKPFFESNPILRSPPNVEKDLPACRAAA | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 235
Sequence Mass (Da): 26468
|
W6KY06 | MSFYNRLALALGLNFFLRSITFTLTVYLTRILLPSQSGMGFVYTLYVDFVLFTARDAIRSVSSRTNLRKPKHASEDSPLSAQEGCKNPENIPNTEDSTPFSGKAIREVVNLSLLSVPLAFIIVVILEISVSMTGLHILPSLWANAWKTTSQPLMQSQVQGSKLHAFWMHFIVPIYPELIVWLSIVIRLLSEPCVALVHSLNMIHVVVIAEFFSITGRQVTVISLIHFYGMHSSWDTRMFFALGQLACSVANISYYALLLSGRPSVWRWLGGSTSMDQLRVVSLSKGALQTWRQAIIPFPWCDIEFRKIISTCYAELHLLG... | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 661
Sequence Mass (Da): 73793
Location Topology: Multi-pass membrane protein
|
A0A3M7S429 | MSKFRTQFDFSRISKELYQWFPGHMAKGLKKMHEHLPSVDAVIEVHDARAPFTGRNLQFRQSVVGNKPYAYVLNKADLTDLKDKKTITSKLAKEGYSPVYFTNLRDSADKTYRKILPDITSQIENQFRFNRELATDYHLLVVGVPNVGKSTLINKLRNFHLKKGNAVKVGSEPGITRAVQSKVKINQNPLVFIYDTPGVLEPTFENIETGFKLACLNCVKNHQVNSDILADYLLFRLNKSSNFKYVEYYGLKEPSDTIFDVLLHIAKKTNKIKIMKGFDNSMKKIYDIDAAGHMMIKHFFDGHLGKSMLDEDIVLQEEEE... | Function: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 329
Sequence Mass (Da): 37749
Location Topology: Peripheral membrane protein
|
A0A3M7R4V1 | MQQINSSNRKSQSNNLNVPKSGFINVLDYKNTEELSQYLKYLDQNKTAYNSYFKWKKYVLFKDRLVHNNFCDMCLMLNLENEMPIHLKQILFNSFFCKSEIILNLILNLTLALLIFEGQDFISTI | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 125
Sequence Mass (Da): 14815
Location Topology: Single-pass type II membrane protein
|
A0A6A3BUU8 | MIFHFFWLCSIIKGFNYAVSFSNKVSAVPRFPSFKDAAQDDGPRKAAHDPIMSSGFMAIPPADSNQKPFSGITKEWYQIFGAPSQLTVFYAGSVCVYDDVSPEKAQDIMLLAGNGSSAAQSKTTLKTQAQTSVPRPSTSDAFPGGGSSGSNELTAATRIGAVPSASNQPEPPKFVNSVGSAMTTLIPAASLARFLEKRKERVTNTSPYSMSKKSPESMPLGSDGASFSDLRQINPLNATHLDRLAAIDDVR | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 251
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 26793
|
A7S034 | MATVNKEVKKVNTLDKKKLGKGKATVITHVVVKKPEVTEKSEKKGELMEGDIDAMEYSSEEEKEEEDLESTYAGYKTKKKKELQPVDHKTVVYQPFRKDFYVEVPELAKMTPEETDEFRLSLENIHVRGKNAPKPVKTWAQTGVQLKILDVLKKNSYEKPTPIQAQAIPVIMSGRDMIGIAKTGSGKTLAFLIPMFRHIKDQPPLEREEGPIAIVMTPTRELAIQIHRECKKFCKPNNLRCVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLTANNGRVTNCQRCTYLVLDEADRMFDMGFEPQVMRIIDCIRPDRQ... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 794
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 89376
|
A0A7C0XNP8 | SRLINELRSFLANMGNGDVKLVVEEKADAKYVVVSAASIIAKHLRDTHIRLLHTIYGDFGSGYPSDPKTISWLSTAIRTGEIPPIIRRSWYTVRRLGLRVNQDLLKWAKK | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 110
Sequence Mass (Da): 12474
|
A7RKP9 | MISASPIVKTLHPIIGVLAQESTGRISNDGEGQYVVQAYTEMMQNAGARVVPFLINKTDEEVDKLFNSINGLVLPGGHVRLQDSNYGKIGKRLYELAVEANNKGSVFPIWAECLGFELLALCASGRGVTHGQFDEALFEYTDAKNYSVPVQLVKDYTKSRFLGTASPDMIGYLNNSLKAFNNHDKALTPKTFNKFPGIKNDYRIITVNRDRVNTEYISTMEGKKWPFFLLDWHPTKPMFPWMETYAQYDHSQQAIAITQFMASSFVNIARMSDHTFPNPQEELLSLIENYTPTLTKDRGNVYFFPMPTKTPQMEEE | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 316
Sequence Mass (Da): 35779
|
A0A8B7NH88 | MVCSTDTHIDPKSFYDPDSPRPMRSFVGQYWYQASCTVLGFGVACLHNFIRKRPVFAGLPRHAAFTLIGFGAGTWINNFIKRRSAERDYFYYQYMCDHPEDFPLIERKKFKDVMKHWTPVR | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A6I1EIS3 | MFKRHLLILCTTLAGAVGLTGCSTVTDTVSSAWESATDFVPYFLKPYRADVHQGNLVTSEMALQLEKGMTDAQVQFLLGVPLVQDQFHQGRWDYVYYLRRGDGEEQIRRLSVYFNADRRVDHWTSDPMPDEQQADQLILGTIRSFEPRPPKTIIPPAQPNSSPSTTDANETGTREAQSPDNAAHQPAAE | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 189
Sequence Mass (Da): 21123
Location Topology: Lipid-anchor
|
A0A6A0HDZ4 | MANQDAYIAALESKLAELSGIEVDQIRKNQLANAADEARSIQQMAEYVAGITVQQVAVAAQPSVLHPQIDLIFDHIKAELGENKGEHALPPLQYDYKGLEPHISGLIMEIHHTKHHQGYINNLKAAAAKLDEARAKNDIAACNALFPALKFNGGGHLNHTIFWTNMAPNPTGTPTQPTGDLLAAIDAKFGSFQNFQVQK | Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 199
Sequence Mass (Da): 21637
|
A0A7R9FGK4 | MAQLIRDIIHGYHDVMDNKSDPRVNQWSMMASPFPTLAICLAYAYFAKVLGPRLMENRKPFNLRNVLIVYNFLQTIFSSWIFYEDYLVNSYVRPAKTDRKLRSGSLKGLSRSGPHSFWSPRT | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 122
Sequence Mass (Da): 14236
Location Topology: Multi-pass membrane protein
|
W6KG87 | MSVDSPKYRQKLKLSALHIFWIFLYHAFISFSLRTQESPDEWWQSAEVAYYLVFGKGELTWEWREGIRSVCFPLLYAIPFYLLKIIGTDTAFMVYAAERIVQAIIATGISYTIFSLGAIIDHALDEDLRNVDSDANKDDYRLVTHLKDLLLSIKAWPRQNAHKNPTSFIICPSVAWTALYFSLTHGYLICDGARAYSNVAEALFIMLALIQIENEIRFLIFADLACMLRVTSAITLFPIFIFHVVRLGRSYGRCRILRYLAQTCFAVAITIPFMATLDYMLYRRWIFTPLQFYKYNVSMNISTFYGTHMWGWYFIAGIPV... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 607
Sequence Mass (Da): 70442
Location Topology: Multi-pass membrane protein
|
A0A6A3AEZ8 | MSDGNHDSDRPRDPKDADILEMKDSETYGKGNDEHPNMQNIIQMNSREKEQYNQKTDSHDQRFQSQSHKVTDEKVKQMRDQVIRAKVYLNFAQPGHNNHLLKELRTRIKEVERTVGEASMDSELPRRVSQKMRSIEVLLAKATEYFSLQPEERQFPNQKKINDPDLYHYAVFSDNVLACAVVINSTISSAKEPEKIVFHVVTDYLNLPAISMWFLLNPPGKATIHIQSIESFDWLSTKYNSTLKEQKSYDPRFTSAINHLRFYLPDIFPALNKIVLFDHDVVVQRDLIEIWSVDMKGKVNAAVETCLESEASFRSMPILL... | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 456
Sequence Mass (Da): 52985
Location Topology: Single-pass type II membrane protein
|
A0A3M7PQF2 | MSLFKSLKFNFFLAFLIRVLFTFYGFYHDDQASKIKLKKQIPKYTDIDYQVFTDAASYVYKNESPYLRDTYRYTPLLSYLMLPNIFLLESFGKFLFVLFDLLCGFLILKINELNLANEDKNLYSILFWFYNPITIAIASRGNAESLMSFLVLNFVYFLKRKNFILSGLFYGLAIHFKIYPVTYALALILYVSQFNQLIKKKKILSIVKSILFNINLVKFGLSALALLILLTCFFYLKYGYIFLYETYLYHLVRKDVRHNFSPYFYMLYLTDTTELGFISYLSFLPQMMLILSASFYLHEHIELCLFFITFTFVTFNKVCT... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum mem... |
A0A8B7NZG9 | MMRVVVLASLLSACAAHGIGKPQWEYSGKEGFDHWAEEFPSCNGSQQSPINIDPFFTTVGAFEPLYFSHYHEIPEAESITNNGHSVEVKIKSKNQPQVSGGNLGATYTFVQYHIHWGADDLRGSEHTINHVRYPMELHLVHHKNEYGNLTAALEHPDGVAVLGLLFVISEYDNPSLAPLISHLLSHTAVGEQNVTKDLYPLTSVLPRDLSRFYRYRGSLTTPKCNEVVTWTIFDDHVPVSDKQMARLRSLSDTEGDPLVNNFRPNQPLNGRIVYRSFLK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 279
Sequence Mass (Da): 31353
|
A0A6A2YRB9 | MPKNFSSNCSGAAGKGGQHHFDTRKGGQFTTFIKLLQATQVADQLNNELSTPNPNDGLTIFAPSDNAFSGLKTGTLNSLSDQQKLQLVQFHILPTLMSTSQFQMASNPLRTQAGDVKGGKFPLNVTAAGNQVNITTGVVNATVANTVYSDRRIAVYQVDQVLLPLQIFGTTPVPAPAPDVPDKDVSVSSPKASKGADTDSGGAVSLKFSSMAMVSFGSAFFGTIFWGFEQKDVRRSCLPNTEEESVEVETPRVIREEDLEIMDRCVMVKLISYKLADCEFKLLDDKQSIMRRTPWSFDAPLISIIVMSWNCRGLGNPTTV... | Function: May be a cell surface adhesion protein.
Subcellular Location: Cell membrane
Sequence Length: 518
Sequence Mass (Da): 56938
Location Topology: Lipid-anchor
|
A0A3M7RXL7 | MFDLVDFHSSEYSFSGTAKKLDSLVSDNFTSFTSMHSALFKQGSIGSVTLSVVLVVANVFVLVSSGAKFLNITLQMHLGICLAITHTSAKSSTAQALNSILVRTFGQIHAWIYQTTIVTDTNGTQAERKIEQLEGFLEHETIFIGGSMSSGTSLVRSLLDVNPSVKCGPETKFIQLILDFMKKMYKNDKTSLWFMKAAGIKNNTLDKSVGLAIYYVMLSNIRWNEDNRDSYNQCLRTGPHFCMVLRYDSLVKNPEKETRKMTDFLGVKWSKRMLKHQKYIGSKWIGNVPGYQKNLIKDTIDMLTLQNN | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
EC: 2.8.2.20
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Sequence Length: 3... |
A0A238F5P0 | MVPSPLLASSAGPVSSFVDALPLPSMPSSMLQWTVGVSPLSTHTEVVSALAVYLAVIFGGQYLMQDRKAFRKSCFFEGRGCGALCVSRAACLVCLIGSERGGGTSIGWTFFRAGAAATPRRARKGRASSARAPGCIHCIHAQRKTSPDDEEDSHTERVLCCAPFVQTPSAATTATTAGPCRAQPTDHRLTRRRPSIRVHACLGLGEVREAIFALTQFKWLFMLHNFLLSAGSGLVLALMLEEIIPILYQHGFFYAICHTSAWTSRLETYYIINYYFKYWELADTVFLVVKKKPLQFLHVFHHTATAALCYTQLNGRTSVS... | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 450
Sequence Mass (Da): 49932
Location Topology: Multi-pass membrane protein
|
A0A0E9N7Q8 | MQGAPVTHLGSALSITDVHTESCCPDQPPTSVSFEYEIIDRDTITSKPFDAEMSHDQGDEEERSCLVLYASQTGNSEDIAHGIGRMLERMHIKRRVCAMDQCDLMDLMNENYVIFVASTTGQGDIPDNMKLFWPAILRRSLPPTLLDHLSFALFGLGDSSYPKYNFTAKKLYRRLIQLGARPMVERGEGDESHPQGIDAGFAPWLKDLRQVMEVELPLPSGLETIPDDQHLPPTYKIQFGENAPSMKTASPRRLGLTFSATVTKNDRITADDHWQDARHIVFSISAPDLAYDPGDIAVLWPENPRNEVDRLIEVCKWQNI... | Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides ... |
A0A1I4EV51 | MPASFATNPLNYILRSESWACKRLQPHEGKIVCIRIPPIAHFKMIVLANGEMQSNMDNLEADTTLSILPAILPGLIMHDESAYDGISISGDALFAEDLITVSKYLKPNFEQALSKILGDIPAHRITKAKDSFCQWHIHLVKNLSDALGEYWQEERPIIAKSNAIKDFSRQLNELKHDVNQLEHRINQIFLKDTLNNR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A6A3A1I2 | MNCSSLVLDPCPVATSGWGYRSRILHFQPLRRNFVVCSLKPVSSSSLSVAESAASESLSRIGSLSQVSGVLGSQWGDEGKGKLVDILAEHFDIVARCQELFLYGYTYIFLRIIIFFLLRFKRVELMLDIQSTIRRDRILPFTLSLGILIVETPCVIGNGVVVHLPSLFKEIDRLEANGVSCKARILVSDRAHLLFDFHQEVDGLREAELNKSFIGTTRRGIGPCYSSKMNRIGIRVNFNYTPEMLKQEVENYKRYAERLEPFIADTVHVMNESIAQKKILVEGGQATMLDIDFGPFVTSSSPSAGGICTGLGIAPRVVGD... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP... |
A0A8B7NPT0 | MLRNISKLLRKTACQFGISDLRGTARMPLKNKFSTSAAGCIQAVSSVSHRRKPNAMAYALLIIPGSAFCLGCWQVYRRQWKLRLINELQDKMALPPIELPNDLSMLQDLEYRKVLVKGTFDHSKEMLYGPRPALYDGRYKETGSLVSSGSSGFCIITPLKLSETGETILVNRGWVPKKFKNAKTRLQGQVEGEQEITGVVRLQENRSPFMAKSSAQNQMFLYRDVETMSAMTGSLPVFLDACTGVPGGPMAGQTRVSIRNEHLSYLLTWYSLSFITSFLWYRKYINPRAFI | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 291
Sequence Mass (Da): 32825
Location Topology: Multi-pass membrane protein
|
A0A0E9NMG1 | MASLLRRQCLRAPASIRSVRFNSSGGKVTGDTTLNQVQQTTDAPQTPTDPTLTTEALTADVFSGAPEELHARTVRIYQPSRNVMQSGKGRAGGWKLDWEILDKGNRYEHTPLMGWAASADYMQGTHLKFKTKEDAMHFAEKQGWDYYVQEPRQAVFRPKAYANQFTYSYGKLKYVHTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A6A2XNQ2 | MISKLEAAGLSFVGRDETGRRMEIVELPSHPYFIGVQFHPKFKSRPGKPYALFSGLIAASCEQLELFLNKSDHVSNGVANGVNTGKANLKVWQNGNCFKSANGSLNGVYSNGNGVHH | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 117
Sequence Mass (Da): 12662
|
A0A6A2WWP3 | MSNERTVIAIIRAARPSFRNDQDKVAFAVHATFLSAGFVLTATGPAALGDNVFSSTSTDEVGTDNWNEFEDHYAFVYTNPEKGWKKILVKCLVMNRKLLVETLAEDSSQPLHLEIDIDDYVGENTSGNYSALYKNLEKLVNGLEKEVISKLNCSTVDTPSSVRGEGSRHNRPDVTINEPRGPQIHPSGVVIPPVNPIGGSDLVPGPGAGMYPTRGGFGGDGSMLLGPNDPRWFGGVGGEHGFPGAQPGIPPGARFDPYGPPGVPGFEPSRFTRNPPRRPGSGIHPDLEHFGAHPPRKQRRTTEALYSSAIDEMAGTRYHI... | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 478
Sequence Mass (Da): 51072
Location Topology: Multi-pass membrane protein
|
A0A6A2ZYS7 | MLAVYGCCLLRLQGLPISCAGHAARMVPPYDQTKYARIGSAIEYAVLHLKVQEIVVIGHSARGGIKGLMSFPYDGNTPTEGLEIIFYSDFIEDWVKIGMPAKTKVRAEHGSEPFGGQCAHCEKEAVNVSLGNLLSSPFVRGGLVKKTLAIKGGYYDFINGTFELWSLEFQLSNPLSV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 177
Sequence Mass (Da): 19299
|
A0A1W1VQL6 | MNMKRSISIMTLLLLLFTLVPQATFANDLKLESPSVILIDAESGKILYEKDPHVERAPASVTKLMTLLVAIEAIKDGRGNFEDVVVASEHASQYGGSQIYLEPGEEMKLKELLISIAVGSANDSCVAVAEHLYGSEESFIKAMNEKAKELGLKHTQFQNTNGLKAEGHYTSAYDMAMIAKEGLKHKELLQLTSIKHYKLRENTEKPFQLDSTNKLLWWYKGADGFKTGWIGEESGFCLASTAKRDSLRLISVVLGAQERRGNFRDAMTLFNYGFAGYKYQEFMKKGQEVGQINVDKGEQDFVTAVTKDNVGTIIAKGKDK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
E3RKK1 | MTRAQQTISIAMLLTSIYLALFLQVIPLPEKIQAEVVPVLPFWALISFGSYLLFKLGWGVFTFNDVPEAHAEIMQQIAEARKDLSAKGVDVGED | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 94
Sequence Mass (Da): 10451
Location Topology: Multi-pass membrane prot... |
A0A1T1D165 | MPILAAAGVRDSKTLKPTHRQRLLPIIRRLATDLGLGQASAREIHQQGIRAATELAMIRALQRLSRVPQLVLVDGNLKLRPWHNRQQTVVRGDQRCLTIACAS | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 103
Sequence Mass (Da): 11476
|
A0A6A2ZUI4 | MVGAEPKLMENGEGKPLSVDDLIRFIRSVVISNEKQEEASPFYVLDLGAVRSLVHTWFHNLPLVQPFYAVKCNPDPVFLKEMADLGTGFDCASSAEIETVLSLGVSPDRIVFANPCKPVSHIKYAAKCALLIRVKVPETSGATFQFGSKFGALPAEIIPLLRASQEAKLQVIGVSFHIGSRAINFNAFEDAIEVAKTAFNTAAKLGLPNLRILDIGGGFTSGPQFTEAASALKLALQKHFPVGVAEGLKIMAEPGRFFSNSSFTLATSIIGKRVRDGIKEYWIDDGVSGSMNFLKYDHDEVVCTPLITGKNSRRKEMKTW... | Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
EC: 4.1.1.17
Catalytic Activity: H(+) + L-ornithine = CO2 + putrescine
Sequence Length: 382
Sequence Mass (Da): 41669
|
A0A6A3BJ06 | MINVNKLTPNSMGQHVPMSSRSSGRSPTEVPANIRDCSLNSPTLSTIALFVGNVEKDHPDDIPRARDGFDTVIKAKAAVDSNPRCRNKVTCAEILALATREVVLLVSPQYYVCQPRSLSDRYDRVIRCTHLRVLPLRSFFSNRIYNFSPRNPIDPTLNIQYAMQLRQMCPRIVDPTIAINMDPNTPGTFDNVYYKNLQQEGSLHLRSGTVFGSEVEKHRQPFASSNAAFNQAFVAAVTKLGRVGVLTGNQGEIRRDCTRPN | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 261
Sequence Mass (Da): 29133
|
A0A117LNK5 | MNLATTALLGFGLSMDAFAVSIVISFCVMKLKNVHVLRVAGSFGFFQAAMPLFGWLAASGFAESIRPWDHWLAFLLLAGVGAHMVREGLEKSVSCPNWPDPTKGKALFALSVGTSIDAFAAGAGFVGLRVDIIRTVTVIGLMTFGISVVGMLFGDRLGKHSGKRMLVVGGLVLALLGLKILLEHLIA | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 19788
Location Topology: Multi-pass membrane protein
|
A0A6A2Z4H7 | MSSDPKKYSKAFLGKPNAEYCAWILDSDKWGGAIELSILADYYGCEIAAYDIQTTCCDLYGQEIDIGSLDIGDFLAIGAMFAATDSVHTLQVISQDETLLLYNMDFGECCK | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of u... |
A0A6A2X2F9 | MGGYALGSAFDSKSGQMIMVALLLMLGSFFVGNLFGNNAPIYISQVSETSSSLASSSSSSPGGGTHFKHGAAEYIQRLGNMATDKTGDLRSAGVVQVLDVGCGVASFSAYLLPLGGILLKEVSRLLRPKGYFVYSAPPAYRRIKIIRFRLPSGSKMKIRHAFSIMQNATTQKLPPSLSVCQFISDSLSRIASVEKNLARIPISARPSSLLLEADDVSKKIYGT | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 223
Sequence Mass (Da): 23790
Location Topology: Single-pass type II membrane protein
|
A0A097ZLM8 | XGAADMAFPRLNNMSFWFLVPALVLLLTSALVESGAGTGWTVYPPLASNVAHAGSSVDFAIFSLHLAGVSSILGAINFISTLGNLRVFG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0D3FD47 | MTAESAAVSVLWLCTMAIVCAGFPANDGSLHPNFYAATCPQAETIVRQEVTRALYTNIGFAAGLVRMHFHDCFVRGCDGSVLLESTSDNVAERDSPINNPSLRGFEVIDAAKARLEAACPGVVSCADVLAYAARDGVALTGGPRYDVPGGRRDGTASLEPEVADNIPAPTFTLDQLTQSFAAKGLTQEEMVTLSGAHTVGRAHCTSFSDRLYNFSATGAADPSVDPALLPQLRRACPAAGPDGAVDAGLVVPMEPRTPNGFDALYYWAVLRNRALFTSDQALLSSPPTAAQVRQTAYGGYPWKLKFAAAMVKMGQIEVLT... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A7X7PBF7 | MTWIQAIVLGAVQGLTEFLPISSSGHMRIVSAIFFGDDAGASFTAVTQLGTEAAVLVYFARDIARIVTAWFRGLFNREHRGDLDYRMGWYVIIGTIPVGVLGFLFKDEIRT | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 111
Sequence Mass (Da): 12301
Location Topology: Multi-pass membrane protein
|
C2M9F2 | MSNFTTRLISGTIYVALIVLVLVLSMVWGLWVLLSFFAVAGLIEFNQLTRVNRPYIFRIVLDCAAAVWLLYATAQSGMAITLGLGIYIPYLLYLLYVVCRSTFLPHQDMLRSLGNSLIGQLYIAVPLALAIRLTLTINSFFPITHYNGLLLLAIFIFIWVNDTGAYLVGSRWGKTPLAPSISPKKTVEGSIGGLLLALLSAVILRLLLFPELSWLHILLIAAVVAIFGTIGDLFESSLKRQAGVKDSGKLIPGHGGILDRIDSLLLAVPAVYLLLRLLDLY | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 281
Sequence Mass (... |
A0A979FNU6 | MTISYTAQVATSSRGFGCFWKLLFRWQGSIYKLVWHELVIYCLAYTTISLIYRLALDDPQRRQFEAVALHIEAFINLIPMAFVLGFYVSIVIKRWWDQYITIPWPDTIAVFVSTNVHGQ | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 119
Sequence Mass (Da): 13940
Location Topology: Multi-pass membrane protein
|
A0A6A3CQA7 | MSCFTSKYADELAKNAAYIGSPGKGILAADESTGTIGKRLSSINVENVEENRRALRELLFTIPGALQYLSGVILFEETLYQKSAAGKPFVDVLKEGGVLPDIKVDKGTLELNGTNGETFTQGLDGLAQRCQKYYEAGARFAK | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 142
Sequence Mass (Da): 15329
|
A0A6A3CFN8 | MKLRRTSLSINYTPKNHNTNPTQLQANLTLLLILKAHFLVYAFLWLGLAATAFSLPPKFYDKVCPQALPAIRKVVEAAVHRERRIGASLLRLHFHDCFVNGCDGSLLLDWTPAFVTKKNARGNLDSVRGFEVVDQRVKWI | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A7RPT6 | MFNCKTYFSVFTVDESIALMRRGSELIKLRSASKKYPRTYFLDSELANISWTPSKKGDRAKIPVNTVKEIREGTVSDAFSQCSEVFPEERCFTLIHGESFATLDLVAANREEAMHWMIGLRYLMAQHYGENEPTRRQKARDLWLRGIYTAADKSGDGLLSIDEVYFLMHKLNVKISNRQVRENFKAADTDTVNSSGLLDFEEFANFYKSISTRRELYMLLLKYGNSKENMTVQELLNFLRIEQRVTECDEEYCSNIIQTYEPADSNKKNMLLGIDGFTSYLLSADGEIFNPEHSDVYQDMTRPLSHYFIASSHNTYLTGD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
EC: 3.1.4.11
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+)
Sequence Length: 877
Sequence Mass (Da): 101146
|
A7SM11 | MLLLRDDSTHDNEVWCPKPYTIFKLLLSARFCSAFLSNISDCDETFNYWEPTHFLLYGSGFQTWEYSPLYAIRSYGYLTLHTIPGLLQVHLLKANKLLVFYFLRFILSIMCAACETYFYRGVIQQFGSYVSQLAAVFIVFSTGMFISAAAFLPSSFAMYMMLLSYGGWFAGNYPVAIVTTAAGALIGWPFSAALGIPIAWDVVIRQRRIRYFIEWCLISLIAILVTLVYVDTYFYGKMVITPLNIVMYNVFGKGGADLYGVEPWTYYFRNGFLNFNIVFLLAFLVLPIVVIPSSILPIWLPISGMYIWIAIFFTRPHKEE... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 566
Sequence Mass (Da): 65635
Location Topology: Multi-pass membrane protein
|
A0A7R9FKN3 | MGCEITTCSFVTAPLTSHSQPVPDRRKELFLFVTALEQVQRNLAPRLFHRLRCNRSGVTLLLVSLSHAALEQVQSNLVPRLCDKLRCNRSGATLFLYAPKIFWCSRTVERKWIRFVLVTALRSVWLISPRPPPIHYRSFFEKRLIRKERIQVSGQAGDACPNVDSLQTLPSVNPIRFTLTAIAVLENNCLFCSISRVGMSMADLTMGKHFGELAYLRGIVQYRLSPFEQRAFAGAFTKGLWNIPVRIRASIFRVAPPFILGYLVYSSVERKHEQLMRKNPDDFKDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
A0A8B7P605 | MGHSKKKAKTGASRKDGYYKLAKEKGYRARSAFKLVHLNSICDNFFKNAKVCIDLCAAPGSWMQVAREFMPQGSVIVGVDLHPIKAIPKTLSIQGDITTQSLRAELRNTLKNYKADVVLHDGAPNVGKNWTQDAYDQNVLVLHACKLACEFLRYGGHFVTKVFRSKDSTKLEYVFKNLFKDIKCTKPQASRYESAEIFYVCKFYKVRPDDKVDPQFFDAKHVFAEVEPTEAKRVNLNRPEKVKKKSEGYEDGAEILYSESTVTDFIESTRHEELLQKTSKLVIDERWQDHPSLTKEIIACCQDIKVLGRKELKMLLIWRK... | Function: Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Catalytic Activity: a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: ... |
G9JWI6 | MQLLPLQPSRPHVSASSRLLQSFLTLTLVFILFPPHVAGQGVFEVKLRRVWNPGGRNFTRQCCSGMEVDGKCALPCRTYVRACLRQYSPGHPTDCTFANMLTSELGQDSFTAPRDHVIRFDIASSWPGSFSMIVELRSLEPGGLIARTEIRRETFFPGKLWANTSHIGVSSNFSLSFRMVCNPNQYGDSCSKFCEPRDDKFGHMTCDANGTHVCLPGWQGLPYCTTPVCSKSCRPNGNCVSPDRCSCQGGWTGPQCNQCVPHPACVHGTCNKPFDCICTPGWGSLYCDLELDYCGRNNPCINGASCKNTNPGQYKCICKP... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 613
Sequence Mass (Da): 66983
Location Topology: Single-pass type I membrane protein
|
A0A0D3HD82 | MVIHMDLKTWSCELFPCLLMVGFASLAHSDFLHCQLTTTSLPDHTLREQNDVTSASSSTSMNEPKFGIIEILPIVLQKGVLRTNCIDSRDRTNRAQIVDGLVGLGRQLKALVQTKGLEIHIEEPLSSTLMLFYEEMGDALALQFTGSAAQNKEFWKQKGQWSAMNKLTRNIQHFVSNAYMDSEKQNSPNIRNSTAVQPSNNLKNLQHI | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate
Subcellular Location: Vacuole membrane
Sequence Length: 208
Sequence Mass (Da): 23361
Location Topology: Peripheral membrane protein
|
A0A0E9NJY0 | MAHMATLRSISMRQVASAARPRNAAIAPASLRFIRIRSSSNPAPAVPEAAPVKESKPVTETPLPESSSFSGQNTAQPEPEILSKDQAADKSKPAFDGMPSAADMLDALEGAKAEGVKDEGAKESSSEEEPRGPKKDYVSSLDRKREQRAQFAMYGFLGALIGAGIYMGRPFDDAVEAQRHKDVPNDYNPLSFWERLRARWTAQTEYYTKPAFEKLLPEPLPAPYQRPYTLLLDLDDLLIHSEWNRETGWRIAKRPGLDYFLGYLSQYYELVIFTSQPAGIAMPVVDKLDPYKSYISAALFRDAALYKDGKYIKDLTYLNR... | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 545
Sequence Mass (Da): 61200
Location Topology: Single-pass membrane protein
|
A0A6A0HAG0 | MTEHIRMSGMYWGITAVDLLGCLGRMDHTEIVSFIQQCQDKTSGGIAPSIQHDPHMLSTLSAVQILVLLDSVSSIDVEGVVRYVSGLQNSDGSFNGDKWGEVDTRFSFCAVACLRLLVSGGELNRVDFDTLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLTLLNRLHWINPDKMRTFILATQDPETGGFTDRPGDVPDLYHTLFGLAGLSLLGDTSLKRINPVFCMPQYVIDKLNISIQIVGDD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-ger... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.