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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A8T2HYJ9 | MVNYEHMGGMREADPAAVAKLRNKLVDSSTTLSQKYRILFSLRNLAGSDAHEAMLLGLKDPSALFRHEVAYCLGQRQDPAAIQTLTTILQDTAEHPMVRHEAGEALGAIGKESCLAPLREHVDDQCLEVAQTCQLALQRIEYHLAEAEKHNTRNTSTEMQHPETESGPSPYLSVDPTPPAPDSIPSTDLRSCLLNDEERIFDRYRALFALRNRGGTEEVQALSASFKSNSALLKHEVAYVLGQIQDANTVSQLKIVLEDSKENPMVRHEAAEALGSIAAPECLDLLKQYTLDIDPIVADSCIVALDMLEHEQSGEFEYAKI | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Catalytic Activity: [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O
Sequence Length: 321
Sequence Mass (Da): 35462
|
F3BGD8 | MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHSPTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSSLGTVIIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTNDLPTKSLIGKRILYLEPHEHTHHAVLSLLTQWESNVTACFNETSFLDAIKNTEHKYDVCLIGHMASVDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLSKPLNHRKLCEVLAAPYRLDHPTHNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRDKAKTDTPQSPAPFQSSRIDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADASVTELQR | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 924
Sequence Mass (Da): 103366
Location Topology: Multi-pass membrane protein
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A0A8B8YBS5 | MVSCVRRSSLRRSRRRGGLARLPETPESASLVARSAMETLRKALIAGAVLGAGAGVGTALFVLVAPGEQQKQTMLKEMPEQDPQRRDEAARTKELLLASLQEAAATQENVAWRKNWMSGGGGKSA | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Subcellular Location: Membrane
Sequence Length: 125
Sequence Mass (Da): 13387
Location Topology: Single-pass membrane protein
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A0A075B060 | MPHIETNVFPDQINFSTVQQTLPPNYIIRPLRSNDFDKGFSQLLSQLTDIGDLSAQNFQDRFHEMLAMPGTYYIIVIENTTTQKLVASGSLILEKKFIHGNGLAGHIEDIVVDEKERGNSLGKKLIEQLRLTAIQLNCYKVILDCHEKTVGFYEKCGFKVKGVQMAYYKE | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 170
Sequence Mass (Da): 19358
|
A0A6A3NRF2 | MRLGYLLVVVVATLLAVSCDVTSAESSTPSTRLLRTAGEQTPERRLVNKLPASFVRDLLKDKTKLEGTLTSWQESGLGVKRLAKSLGLSSNWVKMLRNAKNHGKVDEVALLKLYRARVGPKAK | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 123
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 13503
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A0A6V2P2J7 | VETTLDTSLPWLDGGPRAAHPPRDMGFLLDATPLEWDESLEVIRYVREHGIAQFIHLYNRIKDIEGDRLLWGDEVEYAIFKLDAERGTVKLSLRGAEILAGLQEGERSVPVGQQCNWVPEWGSWMVEGTPGMPYSGYATDLLLVEKNMRTRRARLLAALAEDEICPTLPCFPLMGVGTFTDPPARPTPGLSDSLFVPDEIINPAPRFAALVKNIKRRRGSKVDIRVPRYRDEKTPDAARPVGCPPPATLEEALEMDEVYMDAMAFGMGCCCLQVTFQARDLSESRHLYDQLAVLGPIMLALTAATPIARGVLLDTDVRWDIIAQSVDDRTPAERGVAAGGGEGGGGHAAMAGHGTKRLHKSRYETISTYICNTVIGQDGQDSSTRAALKDLGRNDLEVPMDEEAYRTLTQAGEGQGGAESSIHVCVLTHSHAG | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 433
Sequence Mass (Da): 47303
|
A0A7J4L660 | MKTELIGKKIKIIESNNKNSIGKAGIVVDETKNMLSVEIDGKEIKVIKDQCVFEIEGKKISGKDIAKKPEERIKK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 75
Sequence Mass (Da): 8398
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A0A7J4P504 | MEIRVIENSKDKGKLSFLLKDSSAVFANTLRRLITDEVPVMAIEEVEFRDNSSILYDEMVAHRLGLIPLKTDLKSYKLVEKPEDRESLKCIVKLVLKAKGPCTVYSGDLKSKDPEIVPVDKGFPIVKLLKGQSLELEATALLGRGKEHTKFNPGHVYYRYKPVIEIGSVRNPEEVVDKTHGTVFAIKGGKLEVVKDNLFSVDLAGAAEEISQGAIKEGHDSDIIFTIESWGQLSCKEMVLRALDEFDAMLDELSEKVKSAQ | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 261
Sequence Mass (Da): 29092
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A0A7J4LCZ8 | MLKGVLSRISYFYEHRYKQLLILPVFLLLFSLFILGNNYAKTGEFIQTGVSLKGGTTISIAQSFDIKEFESFLTEKYPGSDLSVRSLSRAGTDVGMIVEASDVSSGDLLKSIEEKTGPLDKSLYTIDTTGPSLGKSFFKQAMIALLLAFLAISFVVYIYFRSFLPSFYAVFSVVADLLFAMTVFVLFGLKLTTGSIAAFLMLIGYSIDTDILLTTRVLKRKEGTVSERMASTIMTGLTMTLTAVVAVTIGYFFTESELLKQITFILAWGLPADIIYTWLFNAALLRMYVEKKEKQNEH | Function: Involved in protein export.
Subcellular Location: Cell membrane
Sequence Length: 298
Sequence Mass (Da): 33216
Location Topology: Multi-pass membrane protein
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A0A3D2NKW8 | MASNRATQDSDDLEALFDSIVSAHTQEEAGEGTHCLSQSAANDQSDANKEKSGKVINQLGQMTRTLHDTLRELGLNKAIEAAASSIPDAHDRLHYVATLTQQAAERVLNATEAAQPLVENMETEANRLAAQWKKLFDKQLDVADFKALALQTHAFLEVIPRQTKATNAYLLEIMMAQDFQDLTGQVIKKIIEVTQQMEQQLLSLLLENALPTDKKIEYSGLLNGPVIKPVGRADVVTSQDQVDDLLESLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 27596
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A0A075AQL0 | MKIQEFIDLICDQEAKESLGTIRTGVPPRSVAIANLNMSLKDIGIKDRDTITIENGNTFKRKTISNEMMVIRKMADDNSCLFSSIGYLLENKRACQADALRQKVVEFILSHPDDYNSVILGKNVSEYCQWISKPTSWGGAIEISIFSKLYKIQIASIDVKSLRVDLFGEEDSFPDRCYIVYDGIHYDCIVSTYSNNETAQDITIFSSKDDFALASAISVVEEISKKNMFTDLANFTIRCETCHSGFIGTDDAQRHAQETGHTNFAEFKN | 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 ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 269
Sequence Mass (Da): 30282
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A0A2E7FUX0 | MSMPSQPSSRWVFGYGSLIWRPGFVFERAERALLRGVHRRLCIYSHLHRGTAERPGLVFGLERGGACVGMAFKIAESDWDEVRDYLRAREQVTMVYVETHRPAKLANGEIVETLTFVADPHHPQYAGRLSLEEQFALVDGAVGEAGSNIEYVINTARHLKEMGIADRQVQALAAMIASKHAPAENQSAAG | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 190
Sequence Mass (Da): 21061
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T1UP47 | IGKAGNPDTMENVNPNMIIGASTEVHAGENLIATPGGIDTHIHFLSPQQIEHALYSGITTMIGGGTGPFDGTNATTVTPGAWNIERMLQATDNIPMNLGFFGKGNCSHLAPLKEQVEAGVLGLKVHED | PTM: Carbamylation allows a single lysine to coordinate two nickel ions.
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 128
Sequence Mass (Da): 13403
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A0A8B8WMG5 | MKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMIALAKGQRAEDGYVIDYELTDQEAWDLRVAGMKRRGTNVPKWMSIMTEQSVCHLQKVFERYKSYSPYDMLESIKKEVRGGLENAFLNRVQCIQNKPLYFADRLYDSMKGRGTRDKVLIRIMTSHSEVDMLKIRSEFKKKYGESLYYYIQQDTKGDYQKALLYLCGRDD | Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Subcellular Location: Membrane
Sequence Length: 222
Domain: A pair of annexin repeats may form one binding site for calcium and phospholipid.
Sequence Mass (Da): 26080
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Q8M0U6 | GLVGSALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLASNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSLPVLAGAITMVLTDRNLNTA | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 192
Sequence Mass (Da): 20458
Location Topology: Multi-pass membrane protein
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A0A8U1EKI9 | MATTVNSGNAPVSDTQSSTSADPRYEGSTFQYSMLLEHLIGEKRPIKDLNPTVMGGLPNPMKTDDQKMIERGMESCAFKAVLACVGGFVLGGAFGVFTAGIDTNVGFDPKDPMRTPTAREVLKDMGQRGMSYAKNFAVIGAMFSCTECIIESGATIFSKLELRNAYHLVRICEGDELKTAFNTASGYYEYCFPGFGK | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Subcellular Location: Membrane
Sequence Length: 197
Sequence Mass (Da): 21338
Location Topology: Multi-pass membrane protein
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F0VNK4 | METKSEASGRDLRDPVLLSLLPRFSSVSSAGHSAESSLVPEPSRGSLQRSLRGARLHSVDPLDRGVCTPGIRSTANARGDVPPFSTVTSAFYRASFSFFRPPVLSLFPASSGVAFCSSELPNVSPKAVPSTSPRANPSSCPVSRPTVTSAGQGCPFGHGKSERAASDLVPAGPSDVSTDSSSSGTANAVSCPASVFGSVCPVEHGSSGASLSGNSAELPQECPMKRLPVRKSFFSSLFSSSPAPSSCPYGLGEGGENAQGVQVEVPAGLSDAREKSTIPSVSGENWNYPSEKQFYRVTRAKGHQVDPGDMPAIVAIHNAVNEQTWTEILRFEAFHQRECDTPKLVRFVGRPEELTFKARIKHFLGYERPFDRHDWLVDRCGTKVRYLIDFYDGRAPPEEEARGKVAIYIDARPDVLSPHGLRDRVRMFLTKKGWLQR | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 47155
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A0A959F1Z7 | MDILTLKALHVIGFVAWFTGLYYLGRLFVYHAEAGQKPANERDILQKQYQHMMKRVYKILCNPAMMLTWTFGIAMLALNPSYFKMGWLHIKLTLLVLLLVYHVYSKSMIRKMESGKSTMSDLRLRLYNEVPTWFLAGIVFTVVLGKAELLNYAYLGGGLIVFAALLYFGIRASQGKKAA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Location: Cell membrane
Catalytic Activity: 3 A + protoporphyrinogen IX = 3 AH2 + protoporphyrin IX
Sequence Length: 179
Sequence Mass (Da): 20454
Location Topology: Multi-pass membrane protein
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Q1W563 | LGQAGSLIGDDQIYNVVVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAADMAFPRMNNMSFWFLVPALIMLLSSSLVESGAGTGWTVYPPLSSNIAHAGSSVDFAIFSLHLAGVSSILGAVNFISTLGNLRTFGMMLDRMPLFNWAVLITAILLLLSLPVLAGAIT | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 167
Sequence Mass (Da): 17779
Location Topology: Multi-pass membrane protein
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F0VDV8 | MRLPRYAREASESASTLASPSGSTLAGESEGVALEDSKLTHSASCKGTNRDGVFCSETCDKDAGNAAFAPGTLRPNCPVHGQLFSESEVALCDAEPRSGGRCLVIFNTCVYDLSNFSHPGGSRLLKGHAGRDITEPFQEVGHSVHAFKLLDALCVGVVKERLDRHKQTVGERCLCGSGQAETATLSQLRYRGLAPGGDSSEAARQLGEHAGSTSPTATPSAHELIDFTKPLLPQVWRLSKTDYERLIEVPCMIEGSMTLMPYAWMEPLSQTRWWVIPLLWLPVVFWCIRENLKTLSPTCCFVSVSVGLALWTLLEYVMHRFLFHFPEQRLPDSRLIRIFHFLVHAVHHLLPLDPLRLVVPPALFVALASGVYGVFSLLLPQWAIQAGCPGALLGYIAYDVIHYSTHHMAFLQRVSHIREMKRYHMRHHFRYPLLGFGVSSKIWDWVFGTLLP | Pathway: Lipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 452
Sequence Mass (Da): 50231
Location Topology: Multi-pass membrane protein
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F0V9V3 | MVGTNAPSAQASCVQHVGGARTSVPRRRVTSGGGASNSAAQRPRGMPASSQGILRFYTDDTPGLKIGPQTVLIMTLCFMACVVLLHIAGKVHQTYGGEN | Function: Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 99
Sequence Mass (Da): 10269
Location Topology: Single-pass membrane protein
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A0A7J4V4Z2 | MAQKLKALRPSLREKKRYMVFQVISGRPVTAQEASDAIMGACRQFLGELGMSRAGIIMLHDKWQQASQRGVMRISHKEVQNVRTALMLVRSIGSREAVITTKGMSGILRKAVQRFLLAPEGQPPAVPG | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 128
Sequence Mass (Da): 14156
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A0A0D1ZR10 | MNVHSYCQWQTLGLVCTTKSTTLPNFPNSLGTNGSQFFVTTVKTPHLDGKHVVFGEVINGKNIVRKIENLPTQSDKPVHDVVVSDCGQLEGSAYSAATEKALDSTGDPYEDFPDDQGEGLKGEEYYKIGLDLKEYGNKAFKAGDVEVGIEKYQKALRYLNEYPATNDNDPKELQGNLDSLRFTLHSNSALLANKTKRYAEAQKWAGFAIDGMPKDAKDADKAKVYFRRGQARVALKDLEAGLQDFEQAAKLAPTDAGIKHELAKTKKTLQDSLRREKESYKKFFS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 285
Sequence Mass (Da): 31684
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A0A8T2HUT0 | MIGDVQLILQRGSAVLAAEATGLAFLRVVLPSTTGHLPFAARGIASSSARVAATESEKRAEKKAAETAEREMVAADEEFSAITDKIPQRPITVVEGTSYTVVIIAALGFAAAVIYAALNELIFSPKEYQCYTHTLNRIKDDPRITVRLGSPISAYGTESRNRAARQRIPHRVYNDSEGREHVQLQFHMRGPSGRATVNADMYKDGSEWRYHFLYLNVESPIQQQVVLVRPGQVDEY | 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: Membrane
Sequence Length: 236
Sequence Mass (Da): 26091
Location Topology: Single-pass membrane protein
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A0A7Z8Z8M8 | MKKTVIALLALVASSACSAATPWQKITQPIGGSAQSIGAFANGCIVGAQALPLNSVNYQVMRTDQRRYFGHPDLVRFIQRLSNQVYSRGMGTMLIGDMGMPAGGRFNGGHASHQSGLDVDIFLQLPQTRWSPAQLLKPQALDLVSGDGKRVVPARWSPQISQLIKLAAEDSEVTRIFVNPAIKQQLCLDAGSDRDWLHKVRPWFQHRAHMHVRLRCPAGSLECEEQAPPPAGDGCGAELQSWFEPPKPGSTPPVKKTPPPLPPSCQALLDEHVL | Cofactor: Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the active site. Zn(2+) ion 2 is bound at the dimer interface by residues from both subunits.
Function: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus.
EC: 3.4.24.-
Subcellular Location: Periplasm
Sequence Length: 274
Sequence Mass (Da): 29788
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A0A485KR35 | MESSLENDTSVQETASDAAACKLSAVRLGYWEDPFASMFAKPNRKMPIINRGYYARARSIELLIHRFFATPVATPSGGGNQPHTRQVIVLGAGQDSMFFRLKTQHPDLLATTMYVELDFPAVTRSKVRLCRRHKVLADALGPVETNETELKAQGYALLACDLRDLKTVQSKLATARINPQLPTLILSECVLCYMNAEDSLPLLSWIGASFADAAVVVYEQIRPHDAFGQTMVENIHMRGCDLKSIFSCVATILCFPPRHCRYPEADDQRRRFLDVGFAHVDCWDMNKVYYEYLDVTERKQKERLELFDEVEEFHMLQGHYCLVVASKQATSSIGDAVRLTANESSGVPPALSST | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 354
Sequence Mass (Da): 39678
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B0X8W2 | MLPKFFQRIARCESVYDVIYVKYLLYKFFGFTIFTVDGRPQDGKVKLTAWDVFSLVRVLAMEAVVFYVSYTTLQSRESTGSSILDNGTRYTFVGGSLYISLVTLLNYRRYRGVWKIFAKMDRFDGRAKQINAPVDQRTQQIRILQSIAGLIISFVLMTISGIAMVFWSEETSIYRWSIPVSVIFFNIPFLLMQHQVLIVTYLVYYRVQHLNATFEVHFIPQKEPTLVILAELPAPRSIHDKPTILHNLVIQWDEIRRIVQRISNEFYAQLIFVVLVSIMIVTFSLFALYRAFLTGDRVQMVRALMYMECDVFYLVMLVLFTWSADGIKREAVKTAVLAHKALRELENERVQDDLLLFSQMVNHQVPVIDCGVFRCDWKLVLSIFGTVTSYLVILIQFDASLVT | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 46792
Location Topology: Multi-pass membrane protein
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Q8MKK7 | MRIRSNPMPSRMVDILCFLIIAVFLPVVFMFEIVVVLPAFHEPGGFFHTFTFLMAMFLVFNIKGNMIACMMIDTSVNVKKVEPPSDQLNWRECGECQKLAPPRSWHCKACKVCILKRDHHCIYTGCCIGLRNHRFFMGFIFYLFVGSVYALVYNSIYMWVIHGHIYSNWVTVLKLACPMLHLLWLMESSSWPTMCPLF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 198
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23048
Location Topology: Multi-pass membrane protein
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Q3KNZ4 | MILVSTTSGIAACQVLIFREIHASLVPGPSERAGRRRRGHRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCWAPFFLVQLWAAWDPEAPLERPPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCAQRHTTHSLGPQDESCATASSSLMKDTPS | Function: Involved in renal water reabsorption. Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular Location: Cell membrane
Sequence Length: 160
Sequence Mass (Da): 17371
Location Topology: Multi-pass membrane protein
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A0A1I8N9E8 | MFNKNNTGAGGAGASGPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGEVWERAQRLHDKMQTNLSMARDRLHFLELRDEQLRMEALHLREEQQNKKQDNTRNRSNLKHRKTTTPSTTSKAASATKNVQVVQPMQMEYNSSNNNSSGGAAGASCSIPMVRINNTTKLRSIAAHNIRNNYNSNNASSNAGSPSATASGRKLTVSSKRPGNLAVVNKSQTLPRNLGSKNAIAGVSQRQPIKTAATPPAVRRQFSSGRNTPPQRSRTPISGIGGGSSGGGQSNSGASTPVVSVKGVEQKLVQIILDEIVEGGAKVEWSDIAGQEVAKQALQEMVILPAVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVAREMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDMETRELLLRRLLQKQGSPLDTDALKRLAKLTEGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRPITENDFHNSLKRIRRSVAPQSLTSYEKWSQEYGDITI | Function: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
EC: 5.6.1.1
Subcellular Location: Membrane
Sequence Length: 621
Sequence Mass (Da): 67747
Location Topology: Peripheral membrane protein
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A0A1D7W417 | MKPSFVQIAIVILIIVIIFGAPKLPALARSLGQSMKIFKSEVKDLRDDDEPKKTEPGELNREATENDTSTTAEAARKPEQPAKEKQDPQSHEK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 93
Sequence Mass (Da): 10341
Location Topology: Single-pass membrane protein
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A0A134BSZ8 | MTTIKIALLGFGTVAQGTFNLLQDNAELIKNRTGVNVEISKIYVRNPEKYSHITLPETAKYVTDIDEVLKDDSIQMVVELMGGTSFAKDCVEGALKAKKNVVTANKDLLAEAGPYLLDLASKNGVDLRFEASVLGGIPIIRTLYESLAGNRITEIIGIMNGTTNFILTKMSEEGLSYQDVLKEAQDLGYAEADPTADVEGLDAARKLAILASISFNRRIFFEDVTVEGITCIDTEDIKFGKEFGYNIKLLGIAKETAQGLSLNVYPAFIPTTHPLASVRGSYNAIYVKGNGIDDVMLYGRGAGSLPTGSSVVSDIMEVAKNVSYNETGRLKPFYYDQKDIYSPGKIQSSYYLRLAVDNKTGVLAKISAKLAEQKISVLSIVQRNMDPETAVLAIVTSKCPRSYILNLIDSFNSLRSVKAVNSVIRIMEA | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 429
Sequence Mass (Da): 46780
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A0A2I4HGT4 | MDRCYRLFPCLSDPARRSSLGLKLAMVMVHLVYAGILFLFDEDLIEKMKRVPWYIALYLLLFFATLVQYFITSCSSPGYVIDVMRTINVKDSVFQTPSMASKQPASSKNRSLVITVDGSQLGRNLLGSDTTSWSKLVMDLYPPGTSARTWTCSYCNVEQPPRAKHCHDCDKCVLQFDHHCAWLGTCIGQDNHCRFWWYICGEMALCIWTGILYISYLKSNISRAWWKDAIMILLLIALSIALIFLLLLLLFHSYLILTNQTTYELVRRRRIPYLRSIPERVYPFSKGICKNLYGFCCARSSIYSMDPLPTPQEIEEKLRPYTCLEVVTCRCC | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 332
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 38304
Location Topology: Multi-pass membrane protein
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A0A817CVQ3 | MNNNQIRPSLSPQDSATMLAQIQQKNPQMYARLQAMRSDLTETAYEQLLAAVAVSAANSNGQGHGHSHTHSSSCAHSNSQMHFSQPVPDVPPKPNAAEMNIVQAVQYNEIERVKQLIESGQADVNTPDSEACHLLHWASINNHVELVRYLIAKGATVDIIGGDLKSTPLHWALYSIVTYIYIYIHAGRQGAAETFFLLVDNGAAIDSRDINGVQPIHIAAQYGQIKILAYLLGSGVDVECHDGRDFTPLIYSCLGPPQNYVPLPNSSHVCCTQFLLTFGADVNYQEPTRRFTPLHFSINNLNSISFQVLLKNPQINVHLKNADNLDPSFFARIRQNLDAARMIDERVESSKVNIRPTFLRRYFTNEYNRRWLTRFFMFFVMTLIGLSANAHEYNYWIRIIFPIVVIFGCSHLFNYFVFDSYTKDNFAFSYVLSSSILMYVTYCVYLQENRFTIIDFIYHFSTFYGIYCLYCCKKLNPGFLKQQTMAIDGNNLSKEKICIAFARDPRWTLDHFCVTCLIRRPLRSKHCPLDGTCVMKFDHHCNW | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 543
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 62004
Location Topology: Multi-pass membrane protein
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Q9VRU1 | MVNVTEDVFANGAVNPFTKSKDTIKRFTLTNGAGMSVQLITRGATITSIKTPDASGQIDDVTLGFDDLAGYQSERNPYFGATIGRVCNRIANGSFYLDGKLVQVSKNRDNKFQLHGGFVGFDKAHWEVVEVRVDGVTLSHTNPDGHEGYPGKVTATASFTLSEDNCLHVQMSALADKTTPVNLTNHSYFNLAGHKSGANGLYEHTIEINAYGITETDQSSIPTGRITPVEGTGFDLRVSSNLGERLKALQPARGYDDNFCVTFSPPQPLAKVARATHPPSGRWLEVVSNQPGVQFYTSNFMPDVERGESPIPGKDGAAYAKHCAFCLETQKFPDSVNHSNFPSTILRPGESYQHEVIYKFGVSH | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 364
Sequence Mass (Da): 39627
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D6RHN2 | MATKCTKCGPGYSTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYSQVIHRLPMPYLKDELHHSGWNTCSSCFGDSTKSRNKLILPGLISSRIYVVDVGSEPRAPKLHKACH | Pathway: Organosulfur degradation.
Function: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria. Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport.
Catalytic Activity: H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 + hydrogen sulfide
EC: 1.8.3.4
Subcellular Location: Nucleus
Sequence Length: 123
Sequence Mass (Da): 13666
Location Topology: Peripheral membrane protein
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B0WY73 | MKMRTTIKVFKFHASDWIFYLGLGFIVTLCVTFVVFLVHIRHRQKLPSYGMGRTAPDPQHTYTHEFQKKLTHNSTGGHATPDINIRVNNYEYSNGSTMEAPKIPGQNVPLLLPRSISSEHHYDEPQFASSYSTPIDSKNHEKVTTTLANGGANPAPVTTTNLYHQQKHYQQLQQQIHLYQQQQQPHPSPVASLKGPQHHLQQQQQQQQQALLQSQLSSLQKASSQQYMSTDSLVTNSNTNTSNSTYAVATTDSLETSSSTGTMHKSNSMRQVVTSDGGWLELDHLQTSLSIPEGALPESLKINVFLAVMYDSKDTILVENQITHISPTVVCGPAKSSFSKPLILKVPHCAEDVGNWKISLFYKEEVTNCWKKIASSENDVPSPQAYIQLDLKNAYIMTRKLGKYILGGENLSPEVSVMKRLKIYMFGPSRKPETDFNIRVYILEDYPSALEHCSIIESRMGYFMIGQSSPFHFLNNKENLILRINCSGGWTSKQDTALQRIPFNHVWKNMSILHCEFQLQKLVNELPCLRVELAAEQENGTKVLITSVAFS | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 551
Sequence Mass (Da): 62130
Location Topology: Single-pass type I membrane protein
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A0A1E3A7I4 | MTTEQVMEVMKEAMLVAFEMAGPLLILSIIVGLIVAVFQAATQIHEQTLTFVPKLIVIAVVLLATGSWMLNTFDGFVQRLFEIMASL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 87
Sequence Mass (Da): 9585
Location Topology: Multi-pass membrane protein
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A0A2I4DM93 | MGSPSTGETTRIAARASMIDSLKGCALLGSQIDKAELRRRLLMPQYLRLAVRDSIRSKDPTAGMTWMHDRGGDEENLEPPEAPMIVFINPRSGGRHGPVLKERLQQLIAEEQVFDLADVKPFEFVQYGLKCLEMLADLGDSCAKETREKMRVMVAGGDGTVGWVLGSLGELKKQGREPFPPVGIIPLGTGNDLSRSFGWGGSLPFAWKSAVKRSLHKAITGPICRLDSWHILLSMPVGEVADPPYSLKLTEECALDEGLEVEGELPDKVTCYEGVFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPITNKLIYSGYSCTQGWFFTPCASSPSLRGLRNILRIHVKKVNCSEWEEIPVPSSVRAIVTLNLHNYGSGTNPWGNLKPEYLEKRGFVEAHPDDGLLEIFGLKQGWHASFVMVELISAKHIAQAAAIRMEFRGGEWKDGYMQMDGEPWKQPMSKDYSTFVEIKRIPFQSLVIGGE | Function: Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack.
EC: 2.7.1.107
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 480
Sequence Mass (Da): 53381
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A0A448NWG2 | MCDDGRVSETTNTDLDSCSPPPADGWVALTPAGRAVARAVGHDPAGTLLASDVDGTLSPIVADPTRAAVSERARRALAGLDGRVGTLAVITGRPVARAREMVDVDRRGGLDHLVMLGLYGVERYDVGTGQLQVPEPPAVMGQARHRLQEAVDRAVAADPAMAGTMVEDKGSAVVLHTRRAVEHDRALALLGPVARDLAGELGLAVEEGRDVVELKAWQTTKGDALRRLIAERMPSVLLMCGDDLGDLPAMAVVEEWIGEGRPGARVVSWSAEQPRVARSADVLCDGPEGVAAFLDEISGRITESSTM | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 307
Sequence Mass (Da): 32300
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A0A815F1D0 | MLISVILIPVFLIRARNVINIRLAAQVLNPILNLFGIKYRIENAKVLDKEESCVIVANHQSSIDFIGMMRLWPEHIRYCTILAKKELIWALPFGFAAWLTGLEFVDRKNRERSSETMRQVTKKVQDKSLRLWVFPEGTRNMADTFLPFKFGAFRLAIEAQVPIVPIVFSSYKPIYNVDKTSKNYYWRQGCVTIKCLEPINTKGMTIEKDLQQLTEMTRQRMIEAHQTIQTTTSQNKKNN | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 239
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 27799
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B0W2L5 | MIHWKVALLCTLVVASSARQIVQKSEEGHEREHYHRSSNLHVKPVKQAFTEAELESKYWNDAAQESLGAKLKKEEVSKVAKNIIFFIGDGMSPQTVAATRMYLGNENEQLSFEKFPYLGQAKTYCVNRQVADSACTGTAYLSGVKINYGMLNVAASVPRYDCDYEKTNETEIFGIMKWAQDAGKATGIVTNTRITHASPAASYAQSATRGWEYDVEVRAAGCDQEKTMDIAQQLVRNEVSKNFKVAMGGGRRYFLPRDVNDGEGARGYREDGKNLVEEWLETHKEMGESEFVWNREQLLAVDPKKTEYLLGLFEASHMKFNLVVEEQNAQDMEPTLAEMVEAAVKVLQESEEGFVLFVEGGLIDLAHHDTMARMALDETAEYSKAIEHARKLTSEDDTLIVVSSDHSHTMTYNGYPTRGNDILGIGDVSDRDRLPYTTLSYANGPGYGVTYNVANVAERLDISEYDFTRYNQRYLATVPLGSETHGGEDINVYASGPFAHLFVGNYEQSTLPHLMAYAGNFGEFYREIEEDKDKEDDDDDAGSSLVVSVPVVLIAVIVGLLMRP | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 564
Sequence Mass (Da): 62970
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A0A450XBE8 | MNTKSPMISDHRHYARHFSVVILSILLAACSLLPKSPLIQVTDPFATWQARSRKLTNIEEWSAAGRIAIRAEDDAWNVNMRWQQKIDDYRIRFNAPLALGAAEITGDPYGVRLRTTNRRTFFATDPESLLWDTLGWHIPVSGLRYWILGMTDEDAPVDGLEIDAAGRLEQLHQSGWKIRYLGYRRFKDMDLPIRLELKNDRLDVRIRISRWVLAPAPESIRSTSKGSSEASPQSNEPQPGKSGTKKVR | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 248
Sequence Mass (Da): 28307
Location Topology: Lipid-anchor
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B0W3C7 | MGITGLIPFLEKASRKCHLRDLRGQCVAIDSYCWLHKGAFACAEKLVRGEATDVHIQYCLKFVNLLLANEIKPILVFDGRHLPAKAGTEAKRRESRDSSKKRAAELLRMGKVEEAKSFLRRCVDITHSMALELIKECRKRNVDCVVAPYEADAQLAFLNKKGIAQVVITEDSDLMLFGCSKVLFKLDLTGSGLLIEREKLAVAMGCKEEKFTFDKFRYMCILSGVIIWTRFRGLGCQGEEVCTDNGGHGYSKGAGQDSGLQVSEEYKDSFLKADATFRHMVVYDPTERKQTRLNDPEEVGTDPELCCNAGTFLEDKIALQLALGNVDPFSMKQLDNFHPDDPGCQPTGGKTSSWNQSSVTKHASVWKTNYVPRPAAPDKRQNFATQTSQKPKEFIKRPVPNPDFEEGEKNETIDDVLHAYGIKPKDDPPPLKRLCLTLSTDKRTKPVNFDEVEALDASPSKTKRNPFVVNSTSSNRRSTPADQLLSPTKLTPETSSLLRNVSPVKRIEFKPTEKLSRFKRTVFANEGQKIISRFFSAGAVNTSVSPKTAPTTPKKASSPLKQETNLYLMSPEAKLAHRGEQTPTKKRKSSERTEISDSPNPPCKVEPAVEQVDSGFVEEPETGFSSSQKENEDEQKGTSSRLALDFGRKEPSRFGRESAGQNEDVGVVKMEEQDDDDVVEIVETNEVKTELAVVSSQTMRSSAAETKAGSSSQQKKNVACRRVGLAKGKAVMDTGPTQSGTTKKSAKSEVVVWERGPLNLQIARFVIFSCDLGRVVRASLKLCYKVKRNVDS | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 792
Sequence Mass (Da): 87842
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A0A2S2PZQ5 | MANVTHVDLNNFISKTMHTFSNLINQELKFDEVADSWVFMRTPWPMFIILAAYLLFVLKLGPNMMKNREPYNIKHIMMIYNLAQTAYNIYIISAVFLIPGTYTYLLNIVCIPDETESNRFYKRQFYIQSWHFVISKVFDLLDTVFFVLRKKQSHVSFLHVYHHVNMVVTTWIFLRFIKGQQGALCGIMNATIHAIMYSYYFLAALGPQVQKYLWWKKYVTCLQIVQFIVGIIYGVYLFIYDCDFPRLFSIYMIFDVLLFLYLFVAFYNRTYNQKQKSQ | 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: 278
Sequence Mass (Da): 33220
Location Topology: Multi-pass membrane protein
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A0A1I8N2C0 | MLATALIWIAALLAVIGPLPLTVDGRRHNLKILGLFPHPGISHFHFFHPILRGLAERGHDVTVVSHFPDKSPPVGYTDIPLTGKETLANSVDLKVFENRRFYNHFLEFFLLYEWGKEACNHTLRSEALYKVMRQKVRYDVILLEQFNSDCMMGVAHMLQAPVIGLSSCAMMPWHYERMGMPIIPSYIPALFLGQSEDMSLGGRIANWISFHALNLMYKVFSIPAADALVQYKFGHDVPSVGELVKETTLMFVNQHFSLSGAKPLPPSVIELGGVHIQKAKPLDVDLQKFLDNADNGVVFISWGSMIKAETLPVAKRDAIVRAVKRLKQRVIWKWENETLANKPDNMYISKWLPQRDILCHPNVKVFMTHAGLMGSSEAAYCGVPVVATPMYGDQFLNAAAMKQRGMGVVLNYEDIDENTVLKAIKKVLEKQYYDNAKMISYAYKHRPNTALDTAIWWVEYVANTEGAPLLKSSSTYMSRFVYYSLDVYTVLGLVVLTSVVTWGLLMRKLKTATRNRGTTKVKSN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 524
Sequence Mass (Da): 59100
Location Topology: Single-pass membrane protein
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A0A078KA89 | MGNIFLFGVITFRLVVLVTYIYLKNNYNIILANINTYFLFYSISFLLYLISSLCNPGYITACPTRYIARDISDEFKKNIYNKKNTEKTQPFYNFSTSDEDKSTISNISSSAPSLTLSKNDIYDELTSLTILHNLPNDIVLTEKCIKKKEKYKKLNNLASYTHKNYDKEQISISPVKNKYNKKNINTKLNNIYLEFFLKQKKNISLYATNIKKKKNNKIKKLYKYKPVFINNVNKINNTKINIFNKITQKKTNVIKTETNKYYDSTLYKINSSNIIFSKNIKYEKNNSLTNPFYIYRDNIYQHNIKLNYCIHCDIVQILRTKHCKYCKQCIKTYDHHCLWINNCVGENNRLFFFLYLYFENITIFLTLRHVTKIVCSLVPRPRYILLCWLVVLIFILAIFLIIIFFLALYHTYLCMVNETTLENLSRDILTDSKNDKEKGKRKYNNTCFFISYTKNIFIYFFYLPIRFFIPTKIKKQLLFSIFHKTGINLGIDDEIIWRPTKNKSMWKKKGKKKGKKKEKKRKKKGKKKEKNKIISKLCVISQF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 543
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 64677
Location Topology: Multi-pass membrane protein
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A0A183E3E6 | MRRRRKSVCLFQRILAAGAGAVSLAGAGLLYALESAVKVEAYEHFPHPAPLPWTHKRLFGTIDMASFACHSMKWIAYRHLIGNIMSEEEAKAEAAAVVMPDFDEAGNAIERPGEINDHLLSPYPNAAAAKAANGGTFPPDLSMLLLTREGAEDYVFALLTSYHDPPAGLKLDAGKYYNPYFPDGVIGMPQQLFDGGMEFKDGTPATASQQAKDICTFMRWTAEPFYERKKRLFLKTLLFLPLVTFILVYGKRHIWTFIKGRRSVWKTVKGRERPGT | Cofactor: Binds 1 heme c group covalently per subunit.
Subcellular Location: Membrane
Sequence Length: 276
Sequence Mass (Da): 30786
Location Topology: Single-pass membrane protein
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A0A937Q1L7 | MKFWRKTRPSFWDKREIAPGASTHQFNYRRIWKLAVLLTGGVALVPLIFITVVNYEAMQDAIASEFLLRTTRIVSNTRRAISFFLSERKSALDFIVHDNSFESLNNKERLAGILENLKRSFGGGFVDIGVVDSSGFQNNYVGPYKLEGKNYSGQEWFKQVVDSGMHISDVFLGYRKVPHLVIAVKGINQNGSFYVLRSALSIAPFEGLLSNLELGGMGDAFMINHQGILQTPSRYHGNVLQKLFLLVPKNSPKTEVLEEKNRFGQDLLIGYRYIDDTPFILMIVKKKEELMRPWYRTRLRLIAFLLISVTVILTVILGTATYMVRRIQIADEKRVITLHQVEYANKMASIGRLAAGVAHEVNNPLAIINEKAGLIKDLFAFRGEYVTDHKLIGLVDSILASVKRAGTITRRLLNFSRNLEAGIEPINLKEVILEVLSFMGKEAELRSIEIAMDVSEDIPKFETDRGRLQQILLNIVNNAFAALNDGGHLDIKANREDRDHVSVIITDDGCGISKEDLNRIFEPFFSTKTGQGGTGLGLSITYGLVQEIGGKISVRSELGRGTSFGISIPIKWEKNKK | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 577
Sequence Mass (Da): 64785
Location Topology: Multi-pass membrane protein
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F9D2X1 | MPAGQSRLTKEERMCSKKLIEVLFKGGQSRSMSAFPLRVVYMLLAEGGTADDGILSEMLVSVPKRCFKRAVKRNHVKRQVREAYRRHKTLVGQPAAIAFVWLDNKLHASEEVERKVVNLLRRVGERIQQEAKV | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 133
Sequence Mass (Da): 15188
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Q9XZ68 | MDFTTFVKPSNGGGDSGGGGDADGGGQKLQFWKHVEYIENHGKQEDDYEYCMTEFLRMSGIYWGTTALDIMGQLERLERKSIIEFVKRCQCPNTGGFAPCEGHDPHLLYTLSAIQILCTYDALEEIDREAVVRFVVGLQQPDGSFFGDKWGEVDTRFSFCAVASLTLLGRMEQTIDVEKAVKFVLSCCNQTDGGFGSKPGAESHAGLIYCCVGFFSLTHRLHLLDVDKLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLTIMGRLHWISSEKLQQFILSCQDTETGGFSDRTGNMPDIFHTLFGIGGLSLLGHSGLKAINPTLCMPQYIIDRLGIKPQLLPRP | 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-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 347
Sequence Mass (Da): 38542
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A0A347VRP1 | MLEIEVLKILKDSKNLLAFSHGCDSSALFFILLNLNIDFDIAIVNYNVRKQSKDEVRNTRSLARKYNKKCYVLESNILDFISFNENKNSKDSIESNAKNTQDSIESIDNFASNFELKARQIRYNFFFNLLDSKNYKNLITAHQLDDKIEWFFMRFLSGSGINSLLGFESVESRFYGGKEFKIIRPLINVSKSEILEYNKINNIEYFIDKSNENTKFFRNYVRAKITKNIESRFYKNIKKSFEYLQKEKEILYPKVMICVDFNLFYCKNSNFKSALHRIYIIDKLSKRLGYVLSSKQKNEIDELFFNLDFGREPYKECVMGEKIIIAINEQFLFVGFKLCNKDSKKVIESRIPKKFREIYRKQKIPPKIREIMYYSEITFL | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 45192
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A0A1D7W1G7 | MVEYQVMLNSSAVAQQIARGLASSGVTEVVIAPGSRSAPLIYALAPLAEAGVIRTHVRIDERDAGFLALGLARGLRAKQSRAGGVRTRAGTAGGRDGAVALVTTSGSAVANLHPAVLEASYGHLPLIAITADRPARLRGTGANQTIDDQSQVLSDVRVRIDVPAGSADAGQLFAEAVAHSLGLVTDPGSGRDLVTGAASDTESESGTGEVGPVQFNVQFDVPLVPTVTELAEWKAAVQSLAAKSANEASKSAFAGSDAVSYSDSAKDISVRILPGTVIVAGDAGGHAATALKSLAEEHAIPVLAEPSSPLTSELRDSSVVVPAHARVLSEREDLRTAIRTVIVHGKPTLTRPVAALLADSEVLVQRLPDDVDAVSLSARSSESPSVDEVAGSGGDSTVSDVAAAPNTVSGGTPLHPSMDTGWRDEWVRAGEAIIAESRRTREVESTQSSARAITEELANRDINLFAASSNTIRYLSEATDVRAHVHASRGLAGIDGLISTATGLSLGLGEQVVLVIGDIAMLHDVGGLLTPSAEEGGDVIIVVLNDDGGAIFSGLEHSQEHVAPYLERYFTVPHGRDFKNLAVGYGWEYSRVGSRKESSLLDDFIAEFDSNSEVDSTSEIGTAARGVDGLESNQVTRMRRGRRIIEVDLT | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
EC: 2.2.1.9
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Length: 650
Sequence Mass (Da): 67573
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A0A6G1FU29 | AEAKNKRNREIAVHHARLIQAQKDAEARILESIEELIEFPLSKDADPANPAASDLQRIQTLLAAFQPSDFDDLLEERRCADLCAYVLCPRQPRRQLGDSEFDLVWGVADMKILPHRNTKLWCSPECAKRAIYIKVQLIEEPVAFRKSGATPPISILKETSGDDPVVPDIRKPTADRNPDLSRALAQLALERGDKISSTRATDLMQSDIVEKPVSGAPAAPTQLAATGYGSIEGYIP | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 236
Sequence Mass (Da): 26033
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A0A351VM96 | MLKKGLVGKIAAVFGMVAVAAGIAFASSHGGAGVTPDEALQKLMDGNKRYVGNQMTGAKLSDSAARASLAKSQKPYAIVLTCSDSRVPPEIIFDNSLGEIFVIRVAGNIPDPVVLGSIEYAVEHLGSPLVMVLGHERCGAVTATVGAKGKSTGSANIDAIVKTIAPNIKSAVKNCEACKGDAKCADINKDAFIECVTDANARTVAANLTKKSKIIKHMAAEKKIKIVVAKYDLDDGLVTVFK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 242
Sequence Mass (Da): 25155
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A0A6G1FY73 | MFNQNDRTFGGGQGHHRYGMQHTHLQNLGGVHQHQNFPHGSHARGQNSAHRYTSSGTPLSLAHQYDRHAHEEPSGSHIEELDESGNEQWKEHIKAYREYMQSGTPHYHAKTFARRPPPDIVKVNAADEDNEDPDDRSRAAIAKPKERSAWAGLDLSGQGLRLLSSALFRFEFLEELHLDHNKLVRIPPEIGRLKNLIHLDISNNLLVELPGEIGLLSNLQELLLFDNSLEHLPVEIGYLFRLRILGIRGNPIDHDVGPEIKEAGTENLIKYYRNRITPPPHPDRDWIGFFETSDQSQETFTALSYNILCQRAGTSAHHGCVPDKALSWDYRRDLILRELENFESDFICLQEFDAITHEDFRQRLRELGYASYYSQRTRSRYLNGEQARLVDGCGTFWKTDKYISLASETLRFGELGLNDQSVKKSADYINRVWQKDHIALVNLLENRVTGTRLILVNAYIFWNPKFKDVKLIQVAVLLREITQLAEQWADLPPVRDKRSRPSDVPDAPDAPDQEFAPSSKYTNSTDIPLVICGDFNSEPTSAVYDLVARGSLPAHHDDLDGRDYGPFSTAGMSHPLTLKSAYGAVGELPFTNYTPDYQGVLDYIWYSSNTVRVKGLLGEVDREYLRKVPGFPDWNFPSDHLPLVAEFAVTPRRKGAGKM | Function: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Cytoplasm
Sequence Length: 659
Sequence Mass (Da): 74995
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B0W2Q2 | MNWCSEYFDRKASNPIESLVRQSTKVPCPYKKAGCTWLFGSSDMRSHLEECKFRPYRCIASKLNVLTCPWEGMQFQIEDHLMEDHAKLGEPFTYFQESEIPFSEQSSKGGIKLVDAFSKKFLFYFLSSAKARVAYFMIVYFGRREEARQYYYEFEIRSKSDSELRKIKFVQNCVSDCEDLSRCIVEEDCVAVSFKTIRHFLHEGTIPFRFIVKKKDDEPGKEGRERKLSDGSVTKPNKPRPTPFNFSEKGKLKPNLRRSTSSGSFSGGGGQSGPGKSGGAKKASEEAPSRKTSAPAQVGTSGVQRSPEFSSINRMGVSGQDSPIVHQEPCPLLTPSINRLDASTSEHSPAVVNRPPPGECKTTANVCRMYTQPYKTKDDRLYLQRYPTDCLSKPVFRR | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
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.
Sequence Length: 398
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Sequence Mass (Da): 45068
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Q9VPX8 | MIEVLCLLLGRILLLLVGGYELMWRLRERLNALAVRSYDLWRSKAAREAHERRVLADCRSQLTKTPQHLVLVISPVDAGVDAVLLSRIFDFALDVGIKHVSLYDRRTKGRGYVDMADLCRSTNADTGSCLKWPPVASPSKLENQPKNGQKTNGYVNGSHSPQLQLHQISASDGHALIADVCRELYEDSKTELVQSLLKQKREALTEQISDMLSKRLGFEAPEPELGIVFARQTCTYGLLPWHARFTEFHTHPSGRHFDVETFASILCKYSRCEQRWGT | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 278
Sequence Mass (Da): 31475
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Q76NQ0 | MYVSKFEASMATNFVIYLALGALLCLATANGEIVNTNVERTLDLTSQLVKTTTKISAEDSAGKPIVEYVFFTSEPSLAYIDVKDASDKSVPFKRNEPVKGEQSFTFTFPRAAAKQTFIVETVASKGIRPHPEEIRQNDKQFVKYTGNLHLYSKYRTNSQKTNVKLSSSNILSHTQVKPFSVSSNKITLGPYENVEAFSQEPLVIHYENSAPFVTVNTLERTLEISHWGNIAVQESIQMTHTGAKLKGSFSRYDFQKEGRSGLAALKSYKTYLPASASGVYYRDTNGNISTSNMNAVRDFIELELRPRFPLFGGWKTQYTLGYNVPSYEYMFNDGNKYQLKMHLIDHIYDNMAIDEATIKIILPEGSSDIRLSTPYSISRLPNELVHTYLDTIGRPVVSFSKSNLVESHISDFTLHYSFSKTSMLQEPLLVSGFIYIIFLFTIVFLRLDFSITSHAHKE | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 458
Sequence Mass (Da): 51710
Location Topology: Single-pass type I membrane protein
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A0A2I4EFW2 | MASGGGNTVEWQVRPPNPKNPIVFFDITIGNIPAGRIKMELFADIAPKTAENFRQFCTGEYRKAGLPVGYKGCQFHRVIKDFMIQAGDFLKGDGSGCISIYGHKFDDENFVAKHTGPGLLSMANSGPNSNGSQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNRPKLACIIAECGEM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 188
Sequence Mass (Da): 20471
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A0A089QJB6 | MEWKIGDIVIPNQVVVAPMAGVTNVAFRMICKEFGAGLVVCEMISDKGIHFRNKKTLDMLFVDPTEHPVSVQIFGGSKETLVEAAQFVAENTATDIIDINMGCPVPKVTKTDAGARWLLDPDKIYEMVHAVTSSIDKPVTVKMRTGWDEDHILAVENALAAEEGGAKALAMHGRTRKQLYTGHADWGILKEVADHLTKIPFMGNGDVRTPEEAKKMLDEVGADAVMIGRAALGNPWIVKQTTHYLETGEILEEPTPAEKIKVAKEHLHRLVKAKGEVIGPKEFRSQAAYYLKGIPRSARTKAALNSADTEAEMIDIFDNFLADTLARQAV | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 330
Sequence Mass (Da): 36213
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B0X677 | MAAAFQRRVHISVDDNITEDNADTDNDSISLTNDETEEEDDDDPPPSVQEVTLVTSSSLDRQDTVDSLVIEEASGREEPVAPPEDEVGLDALSANLADDHEETIRPAVVRAAAEAVLPTGWSMQLAPNGRVFFIDHNEKKTSWVDPRTGRASPMPNASSSAAISDSRRPEDGLAPLPEGWEERVHTDGRIFFIDHNTRTTQWEDPRLSMPNVAGQAVPYSRDYKRKYEYLKGQLRKPANVPNKIEIKVRRASILEDSYRIINSITKVDLLKTKLWIEFEGEAGLDYGGLAREWFYLLSKEMFNPYYGLFEYSAMDNYTLQINPFSGLCNEDHLHYFKFIGRVAGMAVYHGKLLDAFFIRPFYKMMLQKPIDLKDMEAVDMEYYNSLLWIKENDPSELMLTFCVDEETFGYTSQRELKPNGADIEVTNDNKDEYIKLVIEWRFVARVKDQMQAFLEGFGQIVPLNMLKIFDENELELLMCGIQSIDVKDWKRNTLYKGDYFANHVIIQWFWRAVLSFSNEMRARLLQFVTGTSRVPMNGFKELYGSNGPQMFTIEKWGTPENYPRAHTW | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
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 Length: 568
Sequence Mass (Da): 65306
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A0A0K1R1V8 | MGMSNVNRMTWRLWSLQSSASLLSLVILSVLAIAAAFDGLGYPCYYAILVDYTTLNVSNYGSWEPAITPVLFLERLEMAFYVYATVVLLMAFGIYLLIGVILVGRLDVIDIKKFTRLVASNHLVFVLGFMFWAFGVFINLLAFKTIVLAAAFHTIYYGLLILFVIYSTTRGVSPNMYHTSNAMVKQPHKQLYNLVVYGKGVVINCLHICFALSTLMQCLLIELVIGNNFRLKIADVISIGIGLFCTLVVIFMLVSEIVLVRYVSGTIGIPLGAILASILIGIPTLRYETKFSYIINGETKRLNQLVSGLLGAVAVLAVILVIVRFIRLVITNRRDNTSVYRKSKQLKAKMERLQRKKAPLPSLPTNDNIPLLEVGENEEDIYDVIDSDRESTDEESVIYENVNPTYVTFLRP | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Subcellular Location: Virion membrane
Sequence Length: 412
Sequence Mass (Da): 46141
Location Topology: Multi-pass membrane protein
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Q9VG87 | MATDVQSFYKDKTVFLTGGSGFLGKVTIAKLLCTTEVKRIYVLLRAKRGQEMRERCAAWDKDPVFGNLMKTNPEALKRVVPCGGDCQEPDLGLSNSDRQVLIDEVQIVIHTAATVRFVEPLHIALAVNTRATRLMIQLAKEMSHLESFVHVSTAYSNCVVEHVSERFYPEHLTCPAEKILELLESISPELLDKMAPALMGKYPNTYTYTKALTEQVIQKEAKDLPLSIFRPGVIIASYKEPMPGWIDNLYGPIAVLYGAAFGILHITLLNLKAQAGIVPVDYCVNMVLTCAWNTARDTSIKLSPEPPIYNFTPNNDNLITWGGFRDKAARLRYTYPLTKMMWLPFLHCTTIPWLFRFTAIFYHLLPGYAIDLALRLWGKKPRMIKLYDKIHKNIDILAPFVITSWSFDTVNTRKLWAKMSVEDQKLYDFNMSSVDWDDYFLQALAGVRIYLAKEEPGQEVVERGRKIYKRFEFLHRLLQFTLCGGAALILWSILKRLLGSFV | 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: 502
Sequence Mass (Da): 57235
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B0WII5 | MDSMIRYISPVNPAVFPHLASVLLLIGIFFTAWFFVFEVSRPKLGGKEGVIFKELLISLFASIFLGFGILFLLLSVGIFV | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Membrane
Sequence Length: 80
Sequence Mass (Da): 8912
Location Topology: Multi-pass membrane protein
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A0A1C0W104 | MYVVIEGIDTSGKSTQIQELKLALQEAIFTFEPGATPLGKKLRKILLEDSIELDSRAEMLLFLADRAQHTHEILKANPDKLIISDRSLISGMAYAKDFDFETLKAFNLFATQGILPQKVIFLELQKEDLQQRLQSKNEDKIEQRGLEYLLELQQRTKAIIKKLQLPYISINANLPKTTITQQIINFIKE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 189
Sequence Mass (Da): 21659
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A0A1L9D043 | MFRITKEFHFSASHQLKSLPSDHQCNRLHGHNYIVEVELSGEELNEHGFVRDYHELAPLKRYIDDHFDHRHLNDVLGHDRVTAECLAKHFYDWCKDRLPETSAIRVSETAKTWAEYRP | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 118
Sequence Mass (Da): 14041
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A0A0T5YYC5 | MAKDAAKEDLELGDEKPGKKKLIIIIAVAAVLLLGGGAAAYFLLMGDEAPTEEEVAQEQEQAKEEGPAAEVEKGPPQYHALDPVFVVNLPGKPSLIQVGVTVRVRSDQMVEFLKHNDPMIRHHFLDLLGAKDGKVLKNREAKEALQQEMLDKLNGIVKELDGPGEVEALYFTNFVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19383
Location Topology: Single-pass membrane protein
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A0A485KM72 | MQRIAARSARPWLYMVTPSISSSDKLVSMVEKALVGGVNIVQLRNKLFAADSAELKAMAVALRTLTRSYNVPFIINDHVSLALEVGADGAHIGQEDTTIADATALIDAENATAFLLGVTVRDAAQAALACKAGAAYLGVGPVYSSSTKQNANNGQTIGLDGLRAVVQTAQEYDVPVVAIGGIDIGRVGPCMATEAAGVAVVAALSGSADVEAAARALSAAVHQTRREC | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 228
Sequence Mass (Da): 23435
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A0A2I4DH32 | MSRTTVELDFFGMEKESSSSSSSSSKSQFQKFLDRQRSFRGMPSAISMINPEVLKSVIASTANQGSEACNAIPSKNLVSVPSSPVLPVYTPPIVRPSSENLPDTAPLTIFYNGTVSVFDVPQEKAENILKLAVEGTLNPKVAVPSSDQQQLLDSLGGGIADLGIPRRKSLQRFLEKRKERLTCVSSPYACYT | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 192
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 20848
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A0A2S2QV25 | MDIISIIKKKCQKEELTKDEMTFFIKCIVNGSIDQCQIGAMLMTLYLNDMTNIEVSNMTMAMANSGKILDFKSSSFVVDKHSTGGVGDKVSIPLVPALRATEEDFVIPMVSGRGLGFTGGTLDKLESIPGFSAFSFDYKQLFNIGNEFGCFIVGSDDLSPADSILYRARDVTATVDNSGLIIASIISKKAAAGIKYLVLDIKIGSASFFHSVDEAKTFGKQFVLVAKLMGIECRALMTRMSAPIGNYVGNSLEILESVNCLKGEGPRDLQNLVELIGGHLLHMTHKVNTVEEGRKRIAESLNNGTALEKFKQMLIKQNIDEMIADGICYGRTIAILPMAKHETKIKSQSSGYVKKINGMIIAEICNKLGAGRQFSNQQIDPAVGVQLLVKIGDYIKNDTQCIILYHNEIDLDKSFLISLQNSIELTDKVVQPENILLGIIDCNS | Pathway: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2.
Function: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.
EC: 2.4.2.4
Catalytic Activity: phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine
Sequence Length: 444
Sequence Mass (Da): 48590
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A0A2I4HSS0 | MSRATVVLDFFGMEKESPHSSSSSSSSKSQFQKFLDRQRSFRGMQSAISKINPEVLKSVIASGSANQGSETGTPIPTKNSVSVPSSPALPVYAPHTLRPRTPESLPDTAPLTIFYNGTVSVFDVPRDKAENILKLAVEGRSDPKVAVPSSDQKQLLETLDGDLPIARRKSLQRFLEKRKERLTCASPYACYT | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 192
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 21003
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Q8INR5 | MSTVLAQKLWCTLWSAGSLGRFAQHMSNAAHQVSCIGSEEQRVYEEPHVIFQNWLMAAQKEAPQVRPRLACMATVDKSGEPVTRLTSIEEVNSHGITFFTTLGSRQAGEISANPHVSLHFNWAPLMRSVRIAGSAHQLTEEQVRDQFRRFPRHVQMSITHGPRYAAAEWQSRSGFFARIGQRLNTWLGKQPEEIPMPHNWGGYILTPSLYEFGMLSGEKAGRTRVRFRRCLEMPRGTRVGHVQAERQDWVYDSCDEN | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Sequence Length: 257
Sequence Mass (Da): 29294
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A0A2S2QWJ2 | MTIENELIRLSVDDFPPRNKPLIAKYLRSFAFPVLSKLSPFNISKTGSYLEGNKNSILQKYGADAEKDITSVLTKLNTLRKEILSNAPFRELISDNVDVQIWNKLLEDYSDEDGKRPTWMFTNWLYCECYIHRRLFEAFETSIYLKTYDPFYEQKMKGLVSCEDAMKILGQFLINYFNKSEVEIKNLREDLPKIIKCALWGNRCDLSQTGGDAIAQTESPLKLVDSLQDLMLVDESSKAVDFLCNSLSITNDDKILDIILDNAGYELFTDLCLADYLVTYKFVNIVRFHGKAIPWFVSDVTNQDFITTIDYIANKSTCEGLKELGKRWESYMKSGQWKFECEQFWTLPFHFGQIKLLDIELYNKLSQSLLIISKGDLNYRKLVGDVFWEPTVPFSQAVGNFKPSKLIALRTLKSDITCGLPEGLAESISKNDPDWLKIGKYAVIHVDGI | 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 in hexose phosphate metabolism. Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Possibly methylates PCNA, suggesting it is involved in the DNA damage response.
EC: 2.1.1.-
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 449
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence Mass (Da): 51568
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A0A6J0T6A6 | MADDQPLTRVTCTAPVNIAVVKYWGKRDEDLILPINSSLSVTLHQDQLKTTTTAAVSRDFTEDRLWLNGKESDIEHPRLQSCLREIRRLTRKRCSESNGEGNSDRPPLSLTYKVHIASENNFPTAAGLASSAAGYACLVYTLAKLYGVEGELSEVARQGSGSACRSMFGGFVQWLMGEEADGKDSVAQQVAPETHWPELRILILVVSAEKKPVGSTAGMQTSVKTSLLLKHRAKALVPERMAEMIRHIQQRNFEAFGKLTMQESNQFHATCLDTFPPLFYLNDTSKQVIALVHRFNAHYGKTKVAYTFDAGPNAVLFMLEETVDEFVEVVRRSFPPANNGGQFVKGLPVEAATPSEELLSAVVRDPAPGALRELLLTKPGPGPMLVGDPSAHLLGPDGLPRSYS | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Function: Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis.
EC: 4.1.1.33
Catalytic Activity: (R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate
Sequence Length: 404
Sequence Mass (Da): 44290
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F0TEE5 | MEKSFVFKFMGLNFDLTGIIGSTLMALTVFFICFWLARKVELKPNKRQNVLEYLLEFTNGIVKDNVSDVDAQNHLSLYAFVLFLFIWFMNQLGMFLEVKVDDWVFVKSPTADPVATMSFAMMTLLLSFTFGVQRFGVGGYLKNYTQPVGFMLPINLIEEFTNFLTLSLRLYGNIYAGEVLLTLIGNDLAHAGGPFTLILAAPLAMIWQGFSVFIGSIQAYVFVTLSMVYIGKKVTTE | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 237
Sequence Mass (Da): 26729
Location Topology: Multi-pass membrane protein
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A0A1I8NHF1 | MCSMRLSGISWHSRRKTSCCTFSLGMLDNFCGTNGGSITEQPIQNVCHWDPTAILSEPYLAAGQGHGCLVLNRNIKSPSHVVKALWQNASVRCCVDGGTNKWLNFIRNELQNDCSIKLPDLITGDFDSISQETEEYFSSRGVKRIHTPDQNNTDFTKAVDVLKPIIREKKLRDIIVLHDTSGRFDQIMSNINTLFTRNDDFCNIYLLGSCSLTWLLRPGKHSIVIPPHLVEEQRWCSLLPIGHEATNVTTKGLKWNLKNSPSYFGGLVSTSNTYASTHIEIETNSTLVWSMGVFYFGDD | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 299
Sequence Mass (Da): 33581
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B0X4L8 | MTRRSHQNTPSSSINIRLIPFQLAGLCPFSPTSPALTIALLVWTFANLTLVVILLVKVTGSASLLFMDPDGGKGHQLNPILLIKSSFTIAAHVLVLVETLIQHVTFRRVEERLESTDKSLSMVGSKSGPSQRKLLFYLVICATSEVGNFWLAQPLYRTAWYTTVASQAVIRLKHLQHMQYVEGLSIRFRVLKKQLQQFVTTTNAAKDEEKARYSGGKFASHAKQQHSIDGNLPDCLRKVFIIKSTYLALWDAGQLLAGAFTLAQLANLLQNFVQCTCDLYTIYSHLYRNDHHFGDIFDTVLGLIPTLVALLLVLGSCEACRTQVSNEVTFENLIFLFEK | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 339
Sequence Mass (Da): 37903
Location Topology: Multi-pass membrane protein
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A0A945LSD8 | MSTDSYTLPCVPLRDVVLFPHVSTPIFVAKGRALITVESLPPSATKLLLVAQRDARDEDPEPEGLYEVGTEAEILQVMRLSDGTIKLLLEGVSRCHVNEFYFEGDSLWADVRPIDDSEVESIDLLARCRGLMALFEDYLRVNQRIPHEVYAAIEGLGSVSAITDAVAANLPINNAERQHLLETFDPADRIKALTTLIDKEIELLKVERKVRSRARRQMNRNQKEFYLTEQLKAIQRELGNSDGVAGDGEELRQIAQKVRLPKEVSEKVEKEITRLEMMTPLSPEASVVRTYVEWLLEIPWANKTRDRNNLKEASNILENEHFGLKKVKERILEHLAVKILNNKIRGPILCFVGPPGVGKTSLGKSVANALGRKFIRVSLGGVRDEAEIRGHRRTYIGALPGRIIQSMKKAGTKNPVFLLDEIDKMGADFRGDPASALLEALDPEQNKNFNDHYLEVDYDLSQVFFITTANSTDVIPPALLDRMEVIRLAGYTEEEKLEISKRFLIPKQREEHGLEESKIQISDDATLRVIHEYTRESGVRNLERTLGNICRKVARNLVESSTGKVKRSKSQKGGNSKRPGQGKLVAVKPEALEKYLGARRYTPDRPETRAGVGVATGLAWTSMGGVLLPLEVSVFPGKGGLILTGKLGDVMKESARAAISWLRSHPKEYGVQSNFYEKKDMHIHFPEGAIPKDGPSAGITMAVALVSALSGRKVRHDIAMSGEITLRGRVLPIGGVKEKLLAARRGGIPEVILPEENRKDVVELEAETPLGLNIHFVDNVEQVVEKCLLPQPVRKRDSSSSKTDIKSKRVGSMIGVGAKRRGPSVPKSPATSSKKGGGAAARRTR | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
EC: 3.4.21.53
Subcellular Location: Cytoplasm
Sequence Length: 845
Sequence Mass (Da): 93589
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A0A2S2QMV1 | MPVKDMAYFMYNLFRLKKYLKYIFIIILFLIYYFGVFTHFFELDYFTDFEYPLGTNISKCIINMRSGNSDQLPCIKINPFEYDLLLANNNKCDKNIHLLILVKSSLNNFERRSVIRKTWGFESRFSDVFTKTVFVLGKSYDIDLEKRITDEHKQYGDIVQYDFIDQYFNNTIKTLNAIKWASTHCNNSRFYFFSDDDMYVSIKNLLRYLRNPFEYPHYLNQEIKGKQSQHNLPSDIELFTGYVFNSYPLRHQISKWYVSLNEYPYHMWPPYVTAGAYVLSHAVLIKFHYGSYYTKLFRFDDIYLGLLAKKLNISPLHCKYIYFYKKYYSPSSYKYVIASHGYDNTEELYNVWLEQKSYGNA | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 361
Sequence Mass (Da): 43426
Location Topology: Single-pass type II membrane protein
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A0A351KHB1 | MEEINVHTSKNYKIFFSNVRDKLQNLIDEYGIKDIYLITDKNIYNLYANEFSYFKGIKGLYIINPGEENKNKDTVFDIYNDMLSKDCNRKTSIVSLGGGVVGDIAGFVASTFMRGLKFINIPTTLMAQCDSSVGGKNGFDFNGYKNIIGTFYQPEFVFVDTNFIHTISCQDYKNGLAEIIKYGFIYDDTFFDYIDANKEQIKKRNEDVINTMVYRSLKIKSDIVCMDEHDNGIRQILNFGHTIGHGIESASNFSIKHGEAVAAGMLIESYLSLKCSLLSTHEFKRLLDIINYFEMPTYFDDMNEKSIMKSMLKDKKRNDSKINFILPERIGSAIITDKLSQNTVEDILIKWVGKKLW | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
EC: 4.2.3.4
Subcellular Location: Cytoplasm
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Length: 357
Sequence Mass (Da): 40947
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I2CSU1 | MSNYAAAFTGEIFQCDTTESFSTDVVYGLVVSVTSTPSSSVTVGGLLLNPKVGTSAGTLISGTYSLASLYLGRYSSSCFMEPTGGLIVSSGTESSVECDMAWMLETPAPSIVSRQSVCEPLATGIVSIDAMIPIGRGQRELIIGDRQTGKTSICLDTIVNLKYEKVLSVYVPVGQKAASVLDAYQQLVKRDVYQALAIVMASASTSAVMQYLSVYAGTALAEFFMYNLSLPVFIAYDDLAKQASAYREISLLLRRPPGREAFPGDIFYVHSRLLERSAKLNYACGSGSITAFPIVETLAQDVSAFIPTNLISITDGQLFLSTDLFNQGIKPAIDVGISVTRVGSAAQQDQMKMVAGRLKLTLAQFVELEAFSQFASDLGEDTARALANGRRIREVLKQDVASPMSIPQQCAVLSLAGSGVLARIPSDSLVKVFLGYFLSLPSWCFLYVSTKVLAVALIDYVVSK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
EC: 7.1.2.2
Subcellular Location: Plastid
Sequence Length: 464
Sequence Mass (Da): 49702
Location Topology: Peripheral membrane protein
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A0A1I8MLG9 | MLEFLNKSSLVIIFNCQSFYTGCRRMYRVEDNRLFTFSRICDEIAEERSYLNKAQILEKFFKKGCNNKEFKGDLLLWVRMLIPSDSQRVYNLQNKQMLKLFSRLFNTDTREMQLDLEQEGDVSETLRKFFENSNKLKPQKDSSLYLQDVEEFLVKLEQRSKEDEQTVLLKELCKQATSQDLKTIIRIIKQDLRMNAKASHVLAAFGPMAYSSYQATRDLAAVVKQFAFNKKQNNNILTAAAAPKAKKGKASAVSVQVMTPISPMLANACNSVEEAFRKSPSGLFSEIKYDGERVQIHKQGNEFKFFSRNLKPVMEHKVKRFKEMIPKAFPGAGDMILDSEIILVDTITGELLPFGSLGAHKKKEYQHAEVCLFVFDCLLFKGEDLTTTPLRQRRKILEDNITPIKSYVQLSESHFLKTKTELSLMTAKVLRAHLEGVVLKDPSGIYQPGKRGWLKVKKDYLFGGRMADTADLVVLGASYGSGKQGGVLSIFLMGCYDERDHLWKTVTKVHTGLDDQTRLEMHDHLMKLMERSDAKHLPTWFLCNKPLVPDFIAKDPKLMPVWEITGAEYTKSGEHTASGISIRFPRITRLRSDKTAKEANNLEHLENMYEASKNNVNVDLLIKGCDDEPEDKVKINSKINLEGCITTPKREIKKEPLDESPQSSSSKKKLTTPSSTSNKKRKSTEPPEEELFVENKKVKIEKDIKENKKVKDERDTKRDSKTSVKKQLTLDFVIKKEIKSETTDEKPSTSAAAANSLKREIKQEPDEYSGTSSKNVRQMDVEPSVTKKSRLFKNITVYFNDVSDVNNLKCLLEANGGSVTTNKKLANLVLHETCKANITPSNCRSQYRLSCHHLSKQWLLDCLKENTLLNYGLYAVVYTSKK | Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 882
Sequence Mass (Da): 100614
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A0A6P9E321 | MRSAQLDEANREAEFSEAISRLTRVPSRLKVAVDEDFLLFFQMQVPGKLFPAELGTRSQILVSVHFPSHLQTCSPTERDPEMKPLCFQPSGAQQQPRPFADRPFLEPAIHKADYGQHKLLSFASQLGPQKNKQLAFADTIWEEGMSDEPPQVTVERIRQRQSRLESGLLHPCPSCPAFFGEGRIYSSRNVLQVLHFLGRQLFQLLWGPRRVQISAWGVNLVSDGSLEEFGTLEIRTMMEQLSDLSWQLCALEEQSGSWHQKELFLYAMLVSAWLFNMWMWLRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface.
Subcellular Location: Membrane
Sequence Length: 283
Sequence Mass (Da): 32578
Location Topology: Single-pass type IV membrane protein
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A0A2S2QXH7 | MNGYKFFLFGCLFTSLTWSLSLFMYWKLNTKPDSYSQVKLYRRENTFEYVKKQKSKYFKSHVDNSDLEDLGIIKTDEDLVIRDKGYIDHGFNALVSQRLGNYRKSLPDTRHKLCSVIQYDQNLPTASIVICFYNEHPQALFRTIQSVIRRTPKELLHEVILINDYSDKPNLHEIVEQYLKDEKLLKVVNLKKTNKREGLIRARLFGANLATGQVLIFLDSHVEVNIDWIQPLLTRIHNNRTQIIAPIIDIIQPDTFEYKSSPLVRGGFNWGLNFKWDSLPKGTLTTDKDFVKPIKTPTIAGGLFAVNRDYFNEIGQYDSGMNIWGGENLELSFRVWMCGGSLYIEPCSRVGHVFRKHRPYSAPNHEDTMARNSLRLANVWMDDFKKFFISKRMDLLRLDYGDISERKALRTKLGCKNFNWYLENVYPEMLLPTDEADQLSKKLENVEKPVFQPWNKRVRNYIAKFLLNLSGTNLCIHPSKGHQIKHSGLVLRSCIRNKEQIWYETDKEELVLSKLLCLDSGSGKPAIEKCSETGSSQRWKHSDDKGTALYNLAAGTCLSVNEKRINAEILMNICNKEDTFNKWNLIIV | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 588
Sequence Mass (Da): 68256
Location Topology: Single-pass type II membrane protein
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I1XMN7 | MVNIEIDGIPLKVDSAKMIIQAADEAGIDIPRFCYHKNLSIVANCRMCLVEVDKARKALPACATPVAEGMKVFTQSEMALAAQRGVMEFLLINHPLDCPICDQGGECELQDLSLGYGSGISRFSEKKRVVKDKDIGPLVQTDMTRCIHCTRCVRFGQEIAGIKELGATGRGEHMEIGTYVEHSLASELSGNIIDLCPVGALTSKPFRYKARAWEMTSHPSIAIHDALGTNVEIHTRQNEVMRVVPRDNESINQSWISDRDRFSYLGLKHPDRLLHPMIKQNGEWQTTDWQTALEFAVEGLKHVKIKNGADQIAGLISPMATLEEAYLFQKWLRNFGSHNIDHRLRQQDFNDIGHEQFSPVSLAQVEQSDAIVLLGCNVRGEAPLLAHRIRQSACAGGLITDINFFKTDLLMPVERQVVVNSTQLFSLLRGVAKALLHLDATLAKEWEHLVSEKAASATEQNIAMQLANANQPLIVVGAIANQHPQASVIRAMAALISKLTGAQLLILPEANSQALHLAGAIPYSEMMTGSKPGLDAKTVWDEQLRAYVLFNIEPEFDCSNPSAAQLALQRAGFVVAINSFHCNSLHEYADVLLPLAAFAETSGTFVGMDHQWQSFTGAVSPPGESRPGWKILRVLGNISKFSGFDFVSSEGVRQELEDQLNRHSSAKNSLYLPTEILPSKAVQLISEVPIYRTDSLVRHSKALQLTPENQFLDIVRIHPDQAKKSGVNQGDPVLIQQGDFTVTTTVLIDEQVAEGMVYLSAASPLAAKLGMAFGQVQLSAVTEMANA | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 787
Sequence Mass (Da): 86385
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A0A485KVL4 | MKHPSPPPPPESKGSSGAEDDDGDSPKTRPPRITGLDAPHSRDQFISCSGHVVSGLAFYAAMGCMLLPQTFAPSPTHTEDYELWKWIVLMAHVVLNALLVCAWVSCETCNPGDEGSSWLGVSLQGPRWEKSRYCAVCRKTVPGMDHHCTWLNTCIGRKNYAQFFTIAVCGVVIFSIQAFVAVYCTSVWRDWAAPRQVDFAVGSAAQACFILCALVSVPCLVMYTTLLAFHVYLFCLGYGTYDYFLKRRDALRAERRKKRNAQMELARQIEAIEALGKDASAAVVV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 285
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 31480
Location Topology: Multi-pass membrane protein
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A0A7J4JL85 | MARPVFPPAFSKRLLTLEGIYFGSGLESPLKSALSQAIDGKLSPTALGEGLRQILSGQATDAQTACLLTCLRLQGLEAPQLVAAVLALQEFMHAIHPNGDQPLLDIVGTGGDQAGTFNVSTASMFAAAGAGCRVAKHGNRGFTSKTGAADVLEKLGVNIGLSPAASARLLEETGACFLFAPTFHPALAYVAGVRRELGFRTLFNLLGPLANPANASTRLVGANSPENARVLAKALQRLGLAHCLVVHGSQGTASRAPGLDELSTLGKNLCIEVKGKASKEFFLRPAEFGFKPAALADLQVHSVDESAAAVLSVLRGEAGAKRDVVLFNAGAAIHVNGLAGSIAEGMALARGSIDSGQALEKLEQLKVKSNALA | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
EC: 2.4.2.18
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate
Sequence Length: 373
Sequence Mass (Da): 38460
|
A0A485KZX7 | MHRLECVVQQYAWGKKGTNSVVANLKAASDKTFRVENDQPYAELWMGTHPNGPSSLADTSQLLSEWIKENPSALGTSIGDIPYLFKVLSVNKALSIQAHPDKDAAKRLHRDFPHIYKDENHKPEMTIAVTRFEALCQFRPMDQIIDSIQHVDELRLLVDPAVAQALVDARDLPTLRAFFRAMIYCDPEKAKTAINTLRARLESQRESLTPLEALVLRLNEQYPSDIGVFCPYILNYVVLEPGDAVFLGANEPHAYLSGECIECMACSDNVVRAGLTPKFIDKATLCEMLTYNVGSPPVCRGNALDAYLTQYESPVPEFQVQRLGLPAKTTYNLVAAPGPSILLVFGGHGFSVVNGKESDVATGQVFFVPAGQAVTLTSRDELVIFRASPNEGAASDAKLRSSRSQSLEDLTQNRRSKR | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 418
Sequence Mass (Da): 46183
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A0A485L9H6 | MGDGGGYKLTVADLIKLIETPRESIEEALKQAGGTEGIAAGLRSSLTFGLDTSKTDDMMSREKAFGRNYVEPPKPASILELMWEAFHDTTIIILTLSGLVSLILGLTLEGGSTEWIEGCSIMFAVLLVVMVTAINDYQKEKQFAALNAVKEDEKIKVIRDGAPCEVSKFHLLVGDVVRVDLGDILPADGLIFDESEIKIDESTLTGESDLMKKSRHELPVMFSGTRVMEGVAKMLVVCVGVNSQSGIISALVQGKGSEEEKKKKKPPKESAVGPVNEVEVAKKEQEEEYEEATESPLQGKLNILTVLISKFGMTTSIIVFLAMTIEFSVETFGSGNASWDKKYVTEYLHFFITAITVLVVAIPEGLPLAVTISLAFSVKKMLLDNNLVRHLDACETMGSATTICSDKTGTLTTNRMTVMQCWVGGREYSAASQLQGEISDSLKEAFAHGISLNSTAEILPPKVAGQPFEHTGNKTECALLTFCKDLGVDYSTVRKSNVIGHMLTFSSKKKRMSVVAERGVNSRVFCKGATEVVLGLCSKMKRLDGSVAELTNAEKDEIGRNIIEKYANQGYRTLCLAIRDLDISTEEVKQWADDDIETDLTCIAIVGIEDPVRPEVPGAIALCHRAGIVVRMVTGDNIMTARSIAAKCGILRSDENAITMEGAEFRKRVLDADGKIIQSEFDKIWPMLRVLARSSPKDKYTLVTGLKLSNLKDYGPQVVAVTGDGTNDAPALKKADVGFAMGICGTAVAKDACDIILMDDNFTSIVNAVKWGRNVYDSIAKFLQFQLTVNLVAITLAVIGAVVEKESPLSAIQLLWVNLIMDTFASLALATEAPTAALLERKPYPRTQPLLSKTMIKHVIGQGVFQLVVLLVLLFQGEKIFGIPSGRAKDNGGKSDPSIHFTMIFNTFVWMQLFNELNCRKIHDEINIFSGISQNAIFFNVSVFQVIFQVIIIQIGGQAMSCVALDAIHWIYCLAIGALSLPLGLVLRLFKPPKWMKWISDDV | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 1003
Sequence Mass (Da): 109465
Location Topology: Multi-pass membrane protein
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A0A6J2MUB5 | MGKLMVLTLLGAGLALIGERVWMLRQKLNAFREVEPVDPHNCHLIEGIENGSEDIDILPSGLAFISSGLKYPGMPCFAPDEPGQIFMMDLNEQNPRVQALTISDGFDKASFNPHGISTFIDKDHTVYLYVVNHPHMESTVEIFKFEEQQHSLVHLKTIEHELLKSVNDIVVLGPEQFYATRDHYFTNFLSLLEMIMDLHWTYVLFYSPKEVKIVAKGFNFANGITISPDKKYVYVADVMDKNIHVMQIHGNWDLTQLKVIQLDTLVDNLAVDPDTGDIWAGCHPNAMKLFLYNHDDPPGSEVLRIQNVLSEKPSISTEYANNGSVLQGSTVASMYKRTLLIGTIYHRALRCVL | Cofactor: Binds 2 calcium ions per subunit.
EC: 3.1.1.2
Catalytic Activity: a phenyl acetate + H2O = a phenol + acetate + H(+)
Sequence Length: 353
Sequence Mass (Da): 39889
|
A0A377HQE5 | MLENIRIVLVGTTHSGNIGSAARAMKVMGLKHMVLVAPECKVDGQAIALAAGASDIANNARIVDTVEEAVADCALVIGTSARNRSLEWPMLDPRECGIKAIEEAPQHPVAFVFGRERTGLTNEELQACNFHVAIPANPAYSSLNLAMAVQTLCYEARMAWIDSQAYKGEVKEQSYPLAEDLERFYVHLEQVLDKTGFINKSHPGMVMTKLRRLFNRARPESQELNILRGVLSSVEKQMKEAQK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 26791
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Q9VQK9 | MFLMTAGTSNFLSAAWRSEAEESKSKENGSLCCCEYVAEDSRERSHILGCCCNCVDFDLVCTRLVTCRAIDRRNIDGMLIAFQDRLRLPWRGGAKRISPAAVAPAFIVPLMLGLATLNSKTAIVLMLTLVGFTIWGMELAKRTATRTNFFLSWLVFSVFYMIIIFEFQVPLLELAPEENYALMFFSCAALYCLYSAKALSPLNLVSAQYGTTPKDELPGIAEASSGEEQAEAQTTLQMESVLSLDDDEVGDMDTAERSGLMHGQPNICEICRKVTPRRAYHCPVCGTCVKRRDHHSYWLNCCIGERNYVWYIVGLALSEIALLLGANLTLTSICHPFMVVRPLGYPVLLPDDCSEVFEGFDLGISFVVACYALLISSYIAFILARQAYLWWKGSTLHEYKRTSNAAGRNRIWSNWRAILK | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 420
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 47014
Location Topology: Multi-pass membrane protein
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A0A2I4E350 | MYSNFKEQAIEYVKQAVQEDNAGNYAKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDDGGPGSASNGGDAAVASRPKTKPKNGEGGGDGEDAEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEAESTFFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLSGQRGEGNESEASRRIKTEILVQMQGVGHNDEKVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLKARQHIFKVHLGDTPHNLTEIDFESLARRTEGFSGSDISVCVKDVLFEPVRKTQDAMHFVKTPNGMWVPCGPKQQGAVQITIQELEAQGLASQILPPPISRTDFDKVLARQKPTVSKTDLEVHEKFTREFGEEG | EC: 3.6.4.6
Subcellular Location: Endosome membrane
Sequence Length: 435
Sequence Mass (Da): 48372
Location Topology: Peripheral membrane protein
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A0A6J2LU38 | MDIKIGNKPAGCIQMLLHSDVVPMTTGLLSMANSGPNTNGFQFFLTCDKTDWLDGKHVVFGEITKGLDVLWKIEAQGSKDGKPKEKVIISNCGEYV | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 96
Sequence Mass (Da): 10472
|
Q9VB73 | MTRITWRGHSTQELLSILRLRWSYMKHCWHSLTFNAHMNSSYASDVCLTPIFWFVDNYTHCLGPFFVVGVAALTTSVVSIAYWIGLPFWWAKSQLVTYFLLIVGNWLLLNVVFHYVMAVITPAGHPPEGVSLVEAVSMCGKCIAPKPPRTHHCSICNRCILKMDHHCPWLNNCVGYGNHRYFFLYMTYTTLGCLFLILFGLEIGHKYLWLDHGENWTEIEPLEGQPVKFNLSGHIIPVTHPNEYDEFVLPPAVHNLPTPIVDTDAASPGRRRALWFMAFTNVAVVLALGSLSIWHAKLITRGETSVEAHINEAERKRHLQQQRIYINPYNFGTKKNWKLFLGLVRGRSFWRTVLLPSWHKPEGTGLSFHTVNDAPFEDEWP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 381
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 43802
Location Topology: Multi-pass membrane protein
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A0A183EVY9 | MLQIVVLTSIDPAVSNLRRDVRPAHYDASKHEHVIENNYCNICLIYVSVILFDSTCKHCRTCNKCVPGFDHHCKWLNNCIGAPNYRWEIIS | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 91
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 10517
Location Topology: Multi-pass membrane protein
|
A0A163KK98 | MTRAQQTISIAMLLTSLYLAVFMELISFPEKFQKEVVPVIPFWALISFGAYLLFKLGWGVFTFNDVPQAHAELMTQIKEARADLRAQGVDVGADD | 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: 95
Sequence Mass (Da): 10667
Location Topology: Multi-pass membrane protein
|
A0A4U8T4E0 | MSFIVAFMESKNGIFMQKSYKNNNVIKSRTLSKDSKSYKIYKDSNISNNFGKKVSKLDSNISNNLCEKVSNLDSKDSNISNNSLDSKNYDISNKNYKKIAIFGGSFSPIHNGHIEMVKLALKKLDIDKLIILPTFQNPLKDSSIFSPQTRLEWVKEVFLDSNIMDTKDSKENIESRFYKNNEITNLDSKKLENIESNSKDSNLTPVFLESIAKKILISDYEIAQNRAVASIESILHFKNLYNAKKIYFLIGGDNLFQLPKWKDFEKLKKVTEFVVFTRKDSINLNSPCGEKIDLQHIESKRQDSKKNIESNQKDSKKYYDFANKHNIKITLLDFNFNISSTEIRKNIESNIDFIPQKVRDSVILEINK | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 368
Sequence Mass (Da): 42499
|
A0A1I8MV56 | MPPTKEINYKSIWSIEPAASSSSRPPNPNTQCSQRNTKEAYLEAVRIILLLLDNIINHPNENKYRTIRIENKTIKEKLLTLEGCVELLTSIGFQRSDDQYTLPNDSSLELIRSYRDALSKRREFWMNRKEDDALQAIPTNLSNINPATSLSAPIQASKPYRQRISFPRFLRTSNQFLASLEQYSDAVMQYEDEQLLAAGRQLIPIDELTQRASENYLRIQEESSKAVEEGKPAPKEPGIRDLILVELVAWFKNDFFEWVNCLPCKVCGSEESKLSRTVQEGDVRVEVGICCGQETKFHRYNDIAELLVSRKGRCGEFANCFTFLCRCLDYDARIVHPLFDHVWTEVYSDTEKRWIHVDPSDNVVDSPLMYQHGWKRNIDYVFAYSCDDIQDVTWRYCNNHKETLQKRRFCTESELIEALITIRKKRQANLSDERKKMLSQRCMVELIELTLERKPTENELKGRSSGSLAWRQSRGEHSFDNIFEFTLLEEEINQKQFNLRYSCSTDNYERYIKDSTGLCRTISNYKTWQSCQHSSKNILRKVERDWKMVYLARQEDSPYGELVWKFNFNDTPLKVKSYKLTLEKKTFGEGQVEVILRDSQTKEILKTLVNCKSFEICAKLSGGKGDVAWQHAQLLRQSLHSSEYPFELQLEFE | Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
EC: 3.5.1.52
Subcellular Location: Cytoplasm
Sequence Length: 653
Sequence Mass (Da): 76256
|
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