ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A3R9ZLU8 | MNKKSKSIIIAFDGTAASGKGTVAKSLAEKLRYDYLDTGLMFRKVAYFSIKNKVNLSNIEKICELIDRIDFAKPIPLSEIYFDEVSDLSSKIAEFNIIREKLLNIQREFAKGKNGIVVDGRDIGTVVFPNADFKFFFDANIEERARRRYKQLQKMGKSIKLQKVLEYLKIRDKRDIERKSAPLLKADDSMLIDTTQMTIEESLNIILNKLKFK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 24529
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A0A0S7X6D2 | MIKGVGVDIIAVRRVEKMIKAHGEVFCARVFTRRETEYCQRFRRPEERFAGRFAAKEAVLKALGTGWRGGISWQDVEISQTRSGPPEVKLSGAAETEAKKLGVQKIYLSISHSRGYALAFAIAEGGT | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 127
Sequence Mass (Da): 14043
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L7PDR9 | MKHLVWASRELERFALNPGLLETKEGCQQIMEQLQSALNTGTEDLRSLFNTIAVLYCVHQRIEIKDTKEALDKIEEIKSKSKQKTQQAATDTGNSRSGSQNYPIVQNVQGQMVYQVMSPRTLNAWVKVIEEKAFSPEVIPMFTALSEGATPQDLNMMLNIVGGHQAAMQMLKDTINEEAAEWDRLHPVPAGPLPPGQMREPRGSDIAGTTSTPQEQIAWMTNNPPIPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQAAQPVKNWMTDTLLVQNANPDCKSILRALGPGATLEEMMTAC... | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins.
Subcellular Location: Virion membrane
Sequence Length: 379
Sequence Mass (Da): 42410
Location Topology: Lipid-anchor
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A0A1G0KBQ1 | MNNSIDPGAVAEFAVQTAEEAGRIALRYFRTDLDVTNKARKHAFDPVTRADREVEECIRARIRARFPAHRIVGEEFGAQGDETAPAWLIDPIDGTRTFISGSPMWGVLLGLIDGDTCVAGLMHQPFVGETFVGSSAGAFLVRDGQWRKLAVRGTQSLADATLACTHPGMFRTAPELAAFQRVESRCRLSRFGTECYGYCLLAAGFLDIVIEADLEPYDIVPLIPVVEAAGGVVSNWRGEPAIAGGSVVASATPALHEKVLQLLREAV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 267
Sequence Mass (Da): 28813
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A0A834GZW9 | MNAIQLEEKKKWEKELLREIQTEFYRRRKLACENNKVANREKEKLFLEKQETIHGEAKKSHWKAIAELIPNEVPTIEKRGKKEKAKQPSIAVMQAPNWASPFKDAPCTREAQA | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 113
Sequence Mass (Da): 13256
Location Topology: Peripheral membrane protein
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A0A1G0HMA8 | MDHELLKAMTFLAKQAGKSTLPFFYGNKALKIDYKNEEGRQSPVTVADKKANDIIVSGLGLMAEYPVLSEEGKHLPFKTRQSWQRYWLVDPLDGTKGFIHQQPEYTINIALIEDHQPLMGVVYIPVTDECFFGMRGHGAFKQVGDAAPVQIHTRLQTAKPMDILVGHFDHSKNLTSLLSLLKEHAGYHLIRLNSSMKFCRVAEGGGDAYARLGPTSEWDTAAGQAVLEAAGGLVVDTNGLLLRYNEKKSLINPMFCAVSQRSIIPSLLADIRHVQSLRELGSK | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 283
Sequence Mass (Da): 31375
Location Topology: Peripheral membrane protein
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E4TJ95 | MIEKLKRFYIDKDLTDEIEIDEDMYHHIKNVLRTKIGDKFIFINDSEVGEYQFYFGMKRSGIFTLNNKKSHEILDYKLNVYLGILQREYFDTVMEKLGEIGVTNVIPVITKRSIQTVNNNTVERIKKLLIKGALQAEHDFLPSLDAVLNISEITPNTDNNFLLYERKESKNRMEIGSKSVSLVIGPEGGFEEDEIELLSDKGFVPVSPIKGVLKAETAALLFAGYAKILIDTF | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A1J4XBY5 | MKTAAPETLRLRLQVGGEVQGVGFRPFVYRLALDLGLAGWVVNTAGGVVIEVEGGRERLADFETRLQSQPPKNARIEQFQRREIPPVGATGFVIGQSQGGEVTTRIGIDTALCPDCLRELFDPTDRRYLYPLITCTHCGPRYTITRQIPYDRANTSMASFPLCHACAAEYTDPLDRRFHAEPVACPECGPMARLLDETGQPLPGDCFVEAAGLLRQGKIVAVKGLGGFHLLVDALNPEAVARLRARKQREAKPLAVMGLNLPSLRRWLNVDPASQTLLEGVERPIVVVDPAKQEPWMEQVSPGGVGIGALLPYTPIHFLL... | Pathway: Protein modification; [NiFe] hydrogenase maturation.
Function: Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and t... |
E4TIG4 | MKLVFMGTPEMAVPTLDMILKEGFEVPLVVCQPDKPKGRGNKLQPSPVKEFALDHNLEVFQPEKIKNNPEAIEKIRSLKPDFLVVVAYGKILPKELLDIPTFAPINVHFSLLPKYRGAAPVNWAIINGEKETGVATMKMDEGLDTGDILLMKSIPIEKDDTTITLSEKLSKLGADLLIETLKNYHNITPTPQDHASYTYAPIIKKEDGKIDFTKNAEVIERMIRGFQPWPTAYCFYKGKMVKFFKAEVVKANGKPGEVVGVDKSSFLVACGEDSGLRILELQMEGKNRVDAKSFLTGNTINVGDLFE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A2N6LCD6 | MTKAPVAPVVLVILDGWGYCEETKGNAIAAAKTPVMDSLWAAYPHTLIRTSGKAVGLPEGQMGNSEVGHLNIGAGRVVPQELVRISDAVEDGSILKNSALVSICQEVRSRNGKLHIIGLCSEGGVHSHVSHLFGLLDLAKSQEISDICIHAITDGRDTAPTDGVNSIALIQDYIDRIGVGRIVTLSGRYYAMDRDRRWDRVQRAYDVMTKDSSGNGHSAVEVLQASYAEGVTDEFIAPVRIAPGTIEPGDGVIFFNFRPDRARQLTQAFVSPEFNGFERKLITPLSFATFTQYDPELPVKVAFEPQ | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 306
Sequence Mass (Da): 33234
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A0A924GZJ8 | MVTRIVASQVAKSAGKTARRAVRSVQTNATRAATGMLGMTGERMTKVDTAWLRMDSPSNLMMIVGVWTIQPGVRYEDLCQRVEERLLKYARFRQRVEQDTAGATWIEDEEFDIGRHVVREKLAKSAKGHEQQVLQDRVGELAMQPLDAGHPLWQIHLIEDYQGGSAMLVRIHHCIADGIALISVTMSLVDGGEPPPERKRKSGAATGTEDWIADTLIKPFTDMTVKALGAAGEGAVSALGMLRDPQKGMAGSLDLAKLAYQVVSDV | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 266
Sequence Mass (Da): 29079
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A0A1G0FFB0 | MMDESKSLKRMPVRFITIEEGGQRIDNFLLNYLKHVPKSHIYQLIRKGQVRVNKKRIDASYRLHEQDQLRLPPLYTKESEVKRAPDRLLRVIASQIIYEDNFFIVVNKPAGVAVHGGSGLSFGIIEAVRQIRPQEKHLALAHRLDRETSGCLLMVKKSSILREVHQLLREGGIEKQYFAFLKGPIRFKEKTIEAPLKKFNLQGGERVVRSSSEGKPAKTVFIVEKHFPLGSLVKAKPITGRTHQIRVHAALMKHPIAGDDKYGDKIFNKEIQKKGLKRLFLHSAYLKFTLPSSQQVYEFQSPLMQDLDDFLQKCGK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 316
Sequence Mass (Da): 36302
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A0A1G0K5J6 | MIYGVGIDVVEVRRIEDSMARFGRRLAEKILSAEECLEYDQSPRKARFLARRFAAKEALVKALGTGFRAGLFPGAISVTHDALGKPDFRLTTPISSALEQRGICKSHLSITDEREYALAYVLLESN | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 126
Sequence Mass (Da): 14018
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A0A554K3T7 | MGITIMDPASAQLLSIALVMAVGTIAPALAIGLIGSKGTDAIGRNPEAAPKVQTAMILGIAFAEAIAIYALVVALILKFV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A2J0MDJ3 | MSQITDQIKDRVDIVELVREYVPQLKKTGASWKSCCPFHQEKTASFLVSPEKQIWHCFGCSKGGDVFGFIREIEGLEFPDALRLLAKRAGVKLEARNPEIESKRARLLEILRLSTAWYHQALLSAKTADKVRKYVADRAISDETRDIWQIGFAPDAWEAVSAYLKSRGYQDAEIAQSGLSSRNDRGGYYDRFRNRLMFPIKDVHGSVVGFTARKMNEEDVGGKYINTPESEVYHKSSVLYGLSSAKKSIRENDLAVIVEGNMDCVSSHQAGVENVVASSGTALTREQVCLLKRFTKNIALSFDPDAAGQDALSRGLEIAW... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 586
Domain: Contains an N-termi... |
A0A2N6BYQ0 | KIIARAERFREDMVVVDTGTWQGDVHGRHILELHAEESTPDAPEMDIQEAGTVYTALVMGVRDYGAKCGFSKGVVGLSGGIDSAVTCAIACEAFGAENVLGVAMPSPYTSVDSIEDAKKLAENLGCRFEVIAISSVFSALKESLAHIFTASKNSARPTVDITEQNMQARIRGNLLMALSNKYGSLLLSTGNKSEMAVGYCTLYGDMSGGLAVISDVPKLLVYKLAQYINRSKNLIPARIISKPPSAELAPNQLDQDDLPPYEVLDPILQAYLEQNKSVAEIAAMGFERPTVEDIVKRIRTNEYKRKQAPLGLKVTSKAFG... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 337
Sequence Mass (Da): 36673
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G4T4A0 | MITENAAQSEQSEDFYQSRNGSKPKIIPRVDPVVYAQTANPGLIAEDLQARYEQQGFLVIDNVFNEREVDCFKQELKRLNDDEKIKASAEAITELSSDELRSLFKIHEVSPVFKRLAADNRLAGLAQHLLNDRVYIHQSRLNYKPGFRGKEFYWHSDFETWHVEDGMPRMRALSMSIILTENDQHNGPLMLVPGSHKKFVVCEEETPENHYSVSLKKQEYGIPSDECLASLVADGGIVSANGKPGSVLIFDSNVMHGSNSNITPWPRSNLFFVYNAINNRVTWPFCGLLPRPEYLCSRKNIRVIEPRPFIAAADQLIYA | Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
EC: 1.14.11.55
Cata... |
A0A1G0JXV4 | MPHQWQEFSDRQALCSELAATMGAGLAQALAQAPSAGLIAAGGTTAPPVLERLAAMDLDWARVWVTVSDERWVNAEHEASNERMVRDKLLRGPAARANFIPIYSDHASPEAAETHCHERLTAMPWRNSLCMLGMGTDGHAASLFPGTAALTDALNVNFGRLCKAVYPEASPIAGPYPRMSLTLMALIQTRHIYLVITGAEKRAAFDRALLGKEEREMPVRAILRQSKTPVSVYWAP | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A3L6QNE5 | MVQRHPPAHRRVGRQQRNPRHEQQYLSVAGAVPDQRLRPRPVRRGRPRPVDDQRRRCSSGSGGRQRCRGVLLNTGNLVIRSPDGTTLWQSFDHPADTFLPGMKIRIRYDTRAGERLVSWKGPADPSPGAFSLGGDPDTFLQVFVWNGTRPIWRSGPWTGYMVSTQTAQYLTNTSVIVYLAVVNNEEEIYITFSLSDGAGHARYVLTDSGDYQLQTWNRSSSAWILLGWTKAPGGECASYGYCGLNGYCDITELPSTCKCLDGFEPTSLEDLRSGRFSQGCRRKAALLCSDGFLALPGISSPDKFVLVKNRSRHECAAECT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 778
Sequence Mass (Da): 86316
Location Topology: Single-pass type I membrane protein
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A0A554MQY8 | MKLHRFYIDHPLDQEFFEIIDEEILHQAKDVFRFASGDNFVLWNGRGREILAVLDDYTKGALSVHSVQSIENKNELPVRLVLYCAVLKADHFEWVVEKTTEIGVSLIVPILSERTVKMNLRADRLAKIAKEAAEQSCRAKVPGIAVPISLDKAIAEFGEGMNYVFHSGPNLQSIQLNKKSDQGSVGLWIGPEGGWSEAEIKKFEYLGSSRKDFSFASLGKTILRAETAAICACFSIAQKYN | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A346DZB0 | MMRLIRGIYNLKNEYRKCVLTIGNFDGVHLGHQMLLKRLCIEGSNYNVKTMVILFEPHPLEVLKPFTPFIRITSFREKIKYLSTLGIDLVLCIRFKLDFASLNGEFFIKNFLINNLSIKLLIVGDDFCLGVKRHCDVKHLKKLGLKYGFNVININTYLYNKIRISSSLIRKYLYVNNFDFVKLLLGRSFMISGRVVKGNAIGCNVIGYPTANISIRHTTFPLRGVYAVKIYGLFLEPIYGIANIGTCPTFYGTKLKMEVHLLDIFINLYYYRIDVLFCCKIRDEKFFYSIDKLKKQISNDIMVVKKYFKLKI | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 312
Sequence Mass (Da): 36336
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A0A011P339 | MITANAVTKRYPEGHEALKNVSFEITAGEMVFLTGHSGAGKSTLFKLLAAIERPTSGSIVINGQNLAALRKSAIPYLRRKLGLIFQDQKLLFDRSVLDNVLLPLSIVGHPVKDAPRRAQAALAKVGLPNRAKAFPITLSGGEQQRLAIARAVVNRPAIILADEPTANLDAASAIEIIDIFRAFQQVGVTVVIATHDPLIMARVNPRILRLDQGQMSEPASTPSADGVAP | Function: Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring.
Subcellular Location: Cell inner membrane
Sequence Length: 229
Sequence Mass (Da): 24493
Location Topology: Peripheral membrane protein
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A0A522WNK2 | MVLEARDLSYAYPGGVVALDGLSLRIGRGRKLAVLGPNGAGKSTLLLHLNGTLKPQDGQVLLDGRAGVYSRAGLAEWRRRVGLVLQEPDDQLFAATVAEDVSFGPLNLGLDEAATRARVAEALAVLGITDLAGRATHMLSFGQKKRAAIAGALAMRPEVLLLDEPVAGLDHQGARRLLDALGRLSAAGTTLVFTTHDVDLAWAFADEVALFTGGRVMRYGPAAEILADRDALAAAGLEPPLLLELGFRTREEALAGRT | Function: Part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 258
Sequence Mass (Da): 27176
Location Topology: Peripheral membrane protein
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A0A834G600 | MDPEKGVFNLLLPFLLLRVCTSTDTITPNQSIKDGDLLVSNGETFALGFFSPENSNRRYVGIWYNKISEQTVVWVANREKPINGPSGVLFLNQDGNLAIYDNSQNITHWDTNISVAETGTNTSTFYSARLMDSGNFVLFQGDTVSNVVWQSFDHPTNTMLPHMKLGLDLRTGLDRILTSWKSRDDPGAGQYSYRVEPSGSPQLVLYNGSVRVWRSTPVWIENEMSGSPNTTYWFLFNASYIDNQDDVSTVYTLVNNSIASSKFVDESGSLQMVSWLGRWVRFYSVPEDQCDNYGRCGVYGYCDSNNGREFECTCLPGYEP... | Function: Involved in sporophytic self-incompatibility system (the inability of flowering plants to achieve self-fertilization).
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 475
Sequence Mass (Da): 53500
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A0A0Q3Q5T3 | MVGVVGKYKVPNISLDVLKPSFAEILLESHMVMIQGNTALKPKDNEVTSKPWHWPINYQGLRFSGVNETDYRVYLLGNPVIWWLNLITIGLYLLITVFTAVALKRGVQLTSELKGITWDTLLKFFAGFWTPSATARKVYGAGFLALVLLIIYSFYLFHPLSYGIVGPMASDPSSPMAGLRWMDSWEF | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A6L4AJK2 | MGLSSRRRFILHATCGYLLFGSAWIFLSDRLLLSFTDVEALTRLSTAKGITFILLTALLLLIALSIIPDRTAEESRTRLRSADIARSSDRIPAWAAYLFAVAVTVAMLYVREAIAVSFDDRPMLVLFMPPIILSSVLGGFGPGLTATAIAAIGIDYWGIPPVASLRIEKEHDLFQWCLLIASGLLSSYLSELLHRARRQAERRRIRQEQAKEEIRRLNAGLEQRVAQRTAELVAANTELESFAYAVSHDLRAPLRAMSGFSQALIEDYGDQLQGEARMYLDQIIVGSRRMGELIDGLLALSRSTRGQLQRDAVDLSAMAG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 467
Sequence Mass (Da): 52148
Location Topology: Multi-pass membrane protein
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B0DDS1 | GSGNDRVQISVQDSSGTNNANFATPPDGQPGQCRMYTWTYTTPNRDGALENDIVVHEMTHGITNRMTGGGTGSCLQTTEAGGMGEGWSDAMAEYVWSEQKSATITDYVMGDYVTNNKNGIRTHPYSTSATTNPLRYSSIKTLNEVHNIGEVWANMLHNVYAALVGAHGFSTTAKTNPDGTQGNVVFLHLFLDALRLQPCNPTFVTARDAWIQADQNRYGGANKCLLWKAFASRGLGVNAK | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 240
Sequence Mass (Da): 26003
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A0A3L6R4L4 | MNSISNELPAQIVGNQNTDTRRDTPGLDRLPRRFHDPCIAVSMCHIITISRRMNNGKTTEIQHEEVHILRLEVIDKCFGHETVDEEIVDALESEAAKLNEEWCTLALKRLKEASPLALKVSLRSGLPHPDQCPLFDQEEEIVYPYHMCILDAILAQHTKASLSRGFVRVSWALNFMSYQQIC | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A0S7X4S4 | MKKAKILRKRYPKFVFEKYAWRISEKDLEISFKFKMGSDIKFNPKVVIKNVNKNQIKRVEDSVLNNLIFHLGLIELLSYWKTACPPEIEIRAGFLNGEQIKFWRDLILKGMGQFFYENRIDFTRPSFLKIKATADAVLIGYYKEKLENRILVPIGGGKDSIITLEILKNAKKNITCFSLSPTTATQKVMKIGGCKTPIIVQRKVDRKLLELNRKGFLNGHTPLSAYLAFLSILLAVIFDYKFITFSNERSSNEGNLKYLGKIINHQYSKSFDFEKRFREYSKEYLTKEVEYFSFLRPLYEIQISKLFRRYPKYFSSFISC... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes epimerization of the terminal L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
EC: 5.1.1.23
Catalytic Activity: ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate = AMP + diphosphate + H(+) ... |
A0A7W0IQJ7 | LDGMATWMRVQAQEEMFHGMKIYDFVNERGGRAVMQAIDQPPAEWVSALAVFENALAHEQKVTSLINNLVDLSMAERDHATTIFLQWFVTEQVEEEATATGVVNKLKMVGHDASSLFALDQELGQRIFTLPAEAAN | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
EC: 1.16.3.2
Subcellular Location: Cytoplasm
Sequence Length: 136
Sequence Mass (Da): 15180
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A0A4T0FKM6 | MLEEEQFASNKADYVWSLIIMSTLLLAISPLLNLPFLSTALSSALVYVWARSHPNAQIGLLVFLIRASYLPWAIVLLSWLITGRASAARTELAGIAVGHVWYFSKSIWPKELAARGRPLLPTPRILTDTFNH | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 132
Sequence Mass (Da): 14731
Location Topology: Multi-pass membrane protein
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A0A1E3IKL2 | MGFVEVVGKFVFGGGDKASCERMKLMMSEWPLQKHVVFAQSRANMWKKNGSALRLQHHHYCDVSVRDSTIDQALFLALFLLQVSLCVVYPLELMIACIDRFGLGDYFQDSVTDPTLWYDENLEPKQKINLLEDFLLLVIQLATYPVFINSWDRYTEIETPRKITGDQLLAHLVGGGQLQEPDRECPWTVQCLKDEMYNEVDPYWKYYSRNDQPFSTTADFLGTHVVADIVHWAFAHSMHIATLEQWADAVQSAFPQDHTSSPVIPTWDLVLDYALHLSMLALSVKAQEFAQQSVYLKGSEGTNSTFQKLWVMQSDAAFQP... | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A3R9ZRJ2 | MYKLTDKLSEYSNKVSESKHKLFGLIADNISNIITTKIFNIRNKELRKLKTELDKDTIPKEVSMYKYDFKVQIIASLFYWVLLASILWAMIYLKNQGLITIGDFAFVFGIIFAASNELWHAILNFRDLHASIGDLKQSFTILEEKHDLINKSSSKKIAIRNGKIEFNNVKFGYIREKLILNNFNLIIQSGEKVGLVGVSGVGKSTIVNLLLRFFKVNSGKILIDGQNINDIKEEYLYDYMSIVPQDIMLFHRSIKDNILQGNKKATVQDMIIAAKHANTDEFIQNLPNKYDTIIGERGIKISVGQRQRIAIARALLKASP... | Function: Part of an ABC transporter complex. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Membrane
Sequence Length: 408
Sequence Mass (Da): 46650
Location Topology: Multi-pass membrane protein
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A0A2D4JG75 | MFFSLFFVQLFPSLVSTFNPSKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYKRAIELQPHFPDAYCNLANALKEKGSVAEAEECYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQI... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
EC: 2.4.1.255
Subcellular Location: Mitochondrion membrane
Sequence Length: 630
Sequence Mass (Da): 70389
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B0D3V3 | PESWEHNISSMTTPANGQSSCPVHNPSTHATTNSGQATTHVGNEDACPVDHTSLSSIPKVQDGKWVYPSEAQFFSAMQRKNHNPQATDMKTVVPIHNAVNERAWGEILKWEAGRGGDACGGVSLVNFKGKPGERSLKARWRTLLGYSPPFDRHDWVINRCGTPMRYIIDFYTGHNPGSPNSNLSFFLDVRPALDSWEGVKMRTERFFSRWFK | 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: 212
Sequence Mass (Da): 23760
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A0A4V0XDX1 | MIRDQQRPVPIPSALITLLVGMALVLAGLWVGYNVSMLPIDASSNAPVYDALFKVLFSIGTVLFLGIVGVLIFSLVRFRRRRGDSSDGAAIEGNLPLEIVWTAIPAVVVLFVGIYSYDIYERMGGMTPLNDHGAMHTAQPAGDHHHHGGTHGSKQAILASSSSAPAATADQEPGRVWAGIGTNTGEEQTLTVDVTAMQFAFIFHYPEGNIVSGELHIPADRPVSLNMEARDVIHAFWVPQFRLKQDVIPGQPTLLSFTATRPGTYPIVCAELCGPYHGGMRSSVVVHQPADFDAWLSKNTPPVPATVASSGSTPTA | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A2N6BZP3 | MFSKIGTRLTSAFIALAVLPILFLGTFIAQKTYSAARENAISVTQQTALRVAGEVESFIRDKAGHLELLTKVHGLQGLPRVEQRRILQELLLFQNAYDEISLLDNQGRELIKVHRTRIISDTDLASRANNREFQASMQTRKPYFGPVLFRPGTGEPYMICAVPLFDTKSGAITGLLVGDLRLKKMWDLLAAIKHRPGENVYIANQQGLIIAHKNPSIVLRGTRTTFDLAGAEHNMENHIGLFTDEAIIGDHDIFLGEQRLHVISEWQKENALSLAYRMLLVIGSGTLAALSAAILLVIPVVSAIVRPIRKLAATARRIEQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 932
Sequence Mass (Da): 102900
Location Topology: Multi-pass membrane protein
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A0A6G8PVN4 | MLRVGFVDGLSCLPLRMGLQATGGLDGVELVGGAPDETDAMLLSGELELGLVSSASWEGNRDRLWRVPGYGIASDGPVMDALLAVRRGRSLREARSVALASEAATSHGLARVVLERVCGASPRYEVVSPRPGWALAEYDAALFVGEAALEARRLGGVDTVDLGEVWREYASLPMVYAVWASRGDPARYGFWADRVALAVGWAELHADEVVEEARRRGAPATPEDLREYFSAIGYRVGLREGEGLKRYLAESRLLSAGPFGRVSA | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.2.1.151
Catalytic Activity: chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O
Sequence Length: 264
Seq... |
A0A511RGA6 | MRTADLDVLFSKLSRLFSDGPQAEVFSRLLPHAVVRLAAGRPVTPVELAAATGRTAAEVGRLLQQLPGVEMDDAGNLVGMGLTLRPTPHRFEVEGRSLYTWCAFDALLFPVILGKTVRVRSPCPGTGAPVRARVSPAGLEELDPPEAVVSLRVPDTFENLRGSFCGFVHFFRSAAAAADWLRSRPDAVVLSVDEAFALGRRLAYDRFGVGSS | Function: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase.
EC: 4.99.1.2
Catalytic Activity: an alkylmercury + H(+) = an alkane + Hg(2+)
Sequence Length: 212
Sequence Mass (Da): 22845
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A0A2S1SEX1 | MWKKRNGAVWFLVKLCGINYFWKNDMMFKKIAAVILISFLLSYCDNKKVESVKLPPKNDSILKYLSIAFDESLPYKIRYENNFKALRIIEKQNNDSINRYYFFKVAGRFWNMKDTIDYKKITSFLIKQSESALDTFSMAKACSYMGDYFVLMNKPDSSYYYFDKSIKFYNKIKNSEEILEPLFSKAQIQHKYTDYLGYEKSAFDILRIIKGRPNKIELRYEANNLLGIAYGELSEFELSRKYYNIALSLCADKSIPLKNHFKAATLNNLGRMCTCQKKYKISKIYCEIGLKEANLRKDNPSTYAMLLSNLGHAKFRLNEL... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A7S0W604 | EAQAMVPNTSETMLSKALAFGTIACASAFQAPAGFSQPKLRQATTGVTMMAEGSRREVLEGAAIAGAAVTLVPGAASAKEAKAVKNTVENEGFVDPRTYGKRFSLAPKIVISDERGGCSRKAIEYEGLPAGNINDEMCITVKMRQIPADLGAAKLVFDAFGGKGTGYRKA | Function: Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
Subcellular Location: Plastid
Sequence Length: 170
Sequence Mass (Da): 17689
Location Topology: Peripheral membrane protein
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A0A3L6QXB9 | MEGAACLLQRLPPLPPAPLACHHARQLPPRPLAGEAGKERKSNANMVLDRWKLLQESLKAIIKRTVDNLPSEITEYVKEQFINPSERCSTSPLIDSSLKIYWEQTTKVARKRSWAESQESCISQMQWPQRNSGELGSSSCLRVQSISEEPRGVESRALGHWPAHCKLRVSFAAERKGRRFLSGGAAPVGRQPVSQIRRPREKVAFGARVGILCATAFQAIKRGDPWDGPAEGCQASSRRIANESKKCWHHAKLSVDGLVKCEKWIQDDEGRSEESKTSWWLNRLIGRTRTVPIDWPYPFVEDPPHGRNEINVELKKEAEF... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 432
Sequence Mass (Da): 48864
Location Topology: Single-pass type II membrane protein
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A0A0S1SR19 | MIAEEMHSRLEALRDAFLQENAKLNLSAFRTPEACWTGNILDSLAALETEPLRTLSPSPNPNPNPHPHPNPNPHPHPAPSILDLGTGGGFPLLPLALCLPQCSFVGMDATQKKIAAVQRIIDALQIPNVSLICGRSEELARESAQREQYDVVLVRALAELNVLLELAAPFVNVGGTILCWKSLTIDQELHDSLLARSELSCQIEQPYAYDLGSAWGKRQILVFRKRAKTSKKYPRAVGEPKKTPLL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 27061
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Q9J0G5 | MRVKGIRKNYQHWWRWGIMLLGMWMICSAAEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPIDPNPQEVFLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLKCTDLNDTNTNNSSTSENNTNPTISGGEGMGEGEMKNCSFNVTTNIRDKVQKEYALFYKLDIIPIDNTSYALRHCNTSVITQACPKVSFEPIPIHYCAPAGFAILQCNDKKFNGTGPCSNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVLRSENFTNNAKTIIVQLNASVEINCTRLNNNTRKSIRIGPGS... | Subcellular Location: Cell membrane
Sequence Length: 679
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 76738
Location Topology:... |
A0A843ABD1 | MKNQSNQSVIILCGGMSKRMGQDKGSMKIQETPMIIHVLEAITPQINEVIIVLNDRDRIAKYKSIIDSYLKKLNKKFNFNLIFLEDEIKNKGPMSGIMTGLKNISSEYGLILPCDSPFISNEYIKNMFEILNEIKSLYNNVDGIIPFHFKKKLENEDKNEKNNIKTNKKTNKKNNKKVNGKLNRKTKENDNKKDNKNEIDIPKSGFYKEGVMKNFIIENTEPLHSIYKKNTYKTIESLLEQNEMKVKSLIKSINSYFILIDEYKDNSTNKKLNYNISSSNFKNINYKKDINEIN | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A3L6RT13 | MVMLTVEAKIDSENSSRNTRTTVNSAGSHVLDSGDSSDKEHEKELNAAQSILLEEPTCIEESRLDGKTKENKIISTPAATVNNSKETAIESSKPEGVQSICLNSTRMIGEDHFKGISKPPIKHVYTRSKKQQVTEAINKSSLNKLDKGMGPESSNATRNWVSEMECKRELNIEEMTLTGVRKMSEEVGTCKEKEDNSVTLAAITINSKEKKISEDSSKTETAQLVPTHMKDIVALMLGSAFEGVSMDHTGPGRVRFHVKQYASRIDTRVPQNFEDNVTYESFSEMGLHENLLKGIYQYGLKTPSMVLRRGIVPLCKGLSV... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 504
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): 56171
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A0A1J4XRB5 | MPTGVRVVTEIQLSVAEIYRSLQGETSRVGCPTVLVRLAGCPLRCVWCDTPGALLSEQGKPMSVEAILAAVAQAGAGDVLLTGGEPLVQEGAIALLGRLVDTGRRALLETSGALPIHAVPRGVKIIMDLKAPGSGMVEHNRLANLGLLGPEDEIKIVVADRADFDWAVALCRQHRLTERVGSVLLSPAAPDTSPRELAQWILDSRMNLRLQLQMHKIVWGSDAQGV | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A514YM49 | MLPLDIAAIVGLIVASIAAIIVWAIVFIQYKQIRKQKKIDRILERIRERAEDS | Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... |
A0A1Y6EFB1 | MAWPEQLVTLVQYPASIVLLMLLLERVLVWSPLWHPLSLVRLFAQQLQLRVLRPQRDASGQQLLAGVLATLVLLTLVLFPAWWLLDVSDFPSALGAFLLLISLHTSPQTALVKAIAKALQRDQKNVARTLLNRLDSRDNKRLSPIGIIRAAADNQLLSWVQHTLAIILAYLIGGAVLALAVRVLTLLASQWPLEDPRYRYFGQIPHRLSQLALLLPMLLAALLVIILSTLVRGPRLLRTLRQQQWQHWWLPEACWLFGCARLLGIPLGGPVQYRNERTRRARFGPAVANPKAILFALRFTRIADALVLLTSLAFAALQLL | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 320
Sequence Mass (Da): 35956
Location Topology: Multi-pass membrane protein
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B0D525 | DRVLLSVQHDGLKNNATFATPADGQSGKCQLCSPSKYQPKRDAAFANGIIIHEFTHGLTNRLTGGGTASCLQSLEAKGLGEGWSDAVAEYIPILWAFQTSAPIQAFSAGVWVTGNTGRWYPNSTTYSSLKTLTEVHKIGAVWANILHHVNAALVDKYGFSATAMTNPDGSEGNITFFHLLIDALALQPVNPTFAFARQAWIQADANRYNGANEEILWSTFANLGLGVGAADYNDSK | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 236
Sequence Mass (Da): 25350
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A0A942R661 | MKSVHHKYMQLAIEQARKAFSNGDVPVGAVIVRNEEIIGTGYNMVEKMGDPTLHAEIIALREASENIGAKFIYDSTLYVTLEPCVMCVGAIVLARLKCIVFGADDLKMGACGSLFSIPAEPQLNHRVEVIGGINSTACSKLLSDFFEQIRIKKEN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 155
Sequence Mass (Da): 16974
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B6DR40 | MGARASILSGGELDRWEKIRLRPGGKKQYKLKHLVWASRELERFAVNPGLLETSXGCXXILXQLHPALQTGSEELKSLYNTVAVLYCVHQRIEVRDTKEALDKIEEEQNKSKKXVQQAAAAAXPGNSSQVSQNYPIVQNLQGQMVHQPITPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPPAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGDIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKVLRAEQASQDVKNWMT... | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins.
Subcellular Location: Virion membrane
Sequence Length: 405
Sequence Mass (Da): 44980
Location Topology: Lipid-anchor
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A0A2N6BXD6 | MTPKGISPTWPPASGISVLLKNSGLIFSFSRRGSMPRRGIMARCLLISLGFVLLWPCWASAFDRQGREQENIFVLHSYQSGLGWVEDVNDGIYKILLAKDQHNLELYMEYMDAQRLDEPNIFNRLREQLRRKYGRLTFTAVIAVDDIAIDFLARHHAEIFPGAATIFCGKAGGEPIDEYGREGFAGVVEHIDVAATLQVGLDLFPATERVVVINDRSVDGLLLDPLFRRQEENFPHLQFDFVTPVSMDELVEEVKLLSGNTLVLLGNFTRDERGQIFSNTRASWLIASRCKVPIFSMWDFYLGSGPMGGRMVSGKAQGEL... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A4Y7JHQ3 | MNVVPVRSANTPSVILDRGFAGVLHDWCEPFPTYPRTYDMLHANGLLTYYKSENCEISDLFLEMNRILRPEL | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 8332
Location Topology: Single-pass type II membrane protein
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A0A5C8PGF2 | MTTRRRLPWQDPAGRFSPFKLAVFVLLFVPAIVIAARYESGVLGARPVNEAVHQIGNWTLKLILISLAISPGRAILKWPRLMQVRRMVGVAAFTYAAIHLTLYAADEAFDLRKVGLEIVLRIYLTIGFSALLILAALAMTSTDGMMRRLGAPRWRRLHQLAYVAALLGVVHFFMQTKANSAEPYVMAGLFAWLMGWRLLAWRGLRDARWARWWPMILAVLAAAGTAIGEAVYFWIRLGVPPSRLLAANITFTAGIRPAVVVFAICMAAAVAGVLRPPASTRVSPAAD | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
A0A1V6Z205 | MQLTMATVCQIPFSHYQALMKAVSEMYHKRNMLAASLGQTKAKERGYATSAKMGHSSAVDTQVNAEITDLKRKDCSRRSSDLQNYSRSHETDQLLSLIRTIETGVPLEPNQVKSLGELLEQEIGVLSEGLKGRCTLTNNHYPQNLTIRNICDFMALPTLVYELEYPRTKKIDWLYVAEKILATFGIIVVMIAVSQSWIYPVVMDTVRMKEEGMTAQQRLQEFPWVLGDLLFPFMMEYLLAFYVIWECVLNAIAEITMFADRGFYSDWWNSVSWDQFARDWNRPVHNFLFRHVYHGSISEYLSLTVALTVAVEVYISRPEH... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 527
Sequence Mass (Da): 59582
Location Topology: Multi-pass membrane protein
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Q1W264 | MRVMGILKNCQQWWIWSILGFLMLMICSGMGNLWVTVYYGVPVWKEAKATLFCASDAKAYEREVHNVWATHACVPTDPNPQEINLENVTESFNMWKNDMVDQMHEDVISLWDQSLKPRVKLTPLCVTLNCTDNLNNTKSNSNNTSNSTNGTRNNNMYGEIKNCTYNVTTVLKDKKKSEYALFYKLDVVPLVPLKEQENRQENKLNVSRSNYSEYRLINCNTSAVTQACPKVSFDPIPIHYCAPAGYAILKCKNKTFNGTGPCNNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVHLNESVEINCT... | Subcellular Location: Cell membrane
Sequence Length: 680
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 76895
Location Topology:... |
A0A7S0VYP4 | MSRLSAWAVLAAVWAGYASAFIPSAPSGVVGLRKGGLAPSGRMGEGITAPLPSNGLKGRAQLRMTLADPSAAAPEEGKKVAESEGVFRYFSTDAPGGAKRFRIVLMAGFETFNRELYKQAAAKAVEQCAGLEIFVFTDADIDAHPEALASALDGADAFFASLIFDFNQVNWLRGRIADIPNRFVFESALELMSSTQVGSFNMKAQPGKKQGMPPAVKSLLSKFSSTREEDRLDGYTSFLKVGPKVLKFIPVDKAQDMRRWLSTYAYWNAGGLPNVVTMLCELGRELGGLSPAYQSPPAAVPAGEQEEGGLAGLIQRAVRL... | Pathway: Porphyrin-containing compound metabolism.
EC: 6.6.1.1
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Length: 674
Sequence Mass (Da): 72901
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A0A7S0W4G6 | EDKPSTPSKAEGAKKGRKQAAATPSKAAEADVGDKEPSVSAADKIQKMKASRKKAAAQLDSAWVPDDVKKLYKLYLDAKKQLDHAWGQTPVKFMRMILAAIVVIVLYGYCTEFNHYSQQMSWGMSNPSIMFKAQLRNGQNVIIDDYREAYWWLRDNTPQDARVMAWWDYGYQIAGIANRITIADGNTWNHEHIATLGKCLSSEESAAHKIVRHLADYVLVWTGGGGAAPRGPPISSP | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Locati... |
A0A1C6C2G0 | MFITRTISGIVLLAVTMCAIIASGPLLYLFMLLISLVGMYELYRVFQMEKKIPALVGYLTAIGIESVILAGKNDLVVLILVLGFLAMMVSYVATYPKFTAEEIAKATFGMVYVALMMSFIFQTRISNDGAYTVWLIFISAWGCDTCAYLVGRAIGKHKMTPVLSPKKSIEGAVGGIIGSALIGALYGTIFKTNLTEFSNPAVFCAIIGACGGFISMFGDLSASAIKRQYQIKDYGNLIPGHGGIMDRFDSIIFTAPLIYILVTLLQRIA | Pathway: Lipid metabolism.
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: 269
Sequence Mass (Da): 29159
Location Topology: Multi-pass membrane protein
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A0A834LFK7 | MLLLTDQPQPNPDGDDDEPNPNLNNSPIEKHHSPNQQPQLHYLPSLQSTVVIRQLPSQGLSFQLWPAATSLFSLLDLHRSHPYASPLSSLSLSSPPRLRILELGSGTGLVGITAALTLSADVTVTDLPHVLPNLEFNARANSDVLARHGGSVEVAALCWGEVDQMEGLVGREYDLVLGSDVVYHDHLYDPLLRTLGFFLVKGRRTVFVMAHLRRWKKEAVFFKRARKMFDVDVIHRDGPSHGSRVSEPSPVYTIDQALSAMGFGKFQGYVLAYAGLGWVAEAMEMMILSFIGPTVKYEWALSPGEESVTTSVFAGTLLGA... | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 672
Sequence Mass (Da): 73247
Location Topology: Multi-pass membrane protein
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Q2EQ46 | MAGRSGDSDEALLQAVRIIKILYQSNPYPEPKGTRQARKNRRRRWRARQAQINQISQRILSSCMGRPEEPVSFQLPPIERLHIDCSEGTTEGVGSP | PTM: Asymmetrically arginine dimethylated at one site by host PRMT6. Methylation impairs the RNA-binding activity and export of viral RNA from the nucleus to the cytoplasm.
Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry ... |
A0A841ENG8 | MIPFVFIAFIVLTVISACVVLWSNNVLYAAFSLLLTFFGIAALYVLVGADFIAITQLLVYVGGILVLLLFGVMLTNQNGNKENGKNDIIGTNTNRLIGFAVAFGLFALLFFTFAKANFVNIQSNLFESIETFSTTQNIGVLLMTDFVLPFEVSGVLLMATLIGAAYLSSKTKV | 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 i... |
A0A0G1A8S5 | MLHKINPNYLTGFGLTIVPFMIVAQQIGGIDGLGICLTLLVLREATDIADGQLARYTNQITTFGKLFDPLVDSLARYLLFLGFMASGWMPLWMAAIIFSRDIVVAYTRVFAASYGIVMAARSSGKYIKAIPQAVAQITTVLGYLLVECGLKLPIENISWVLLFIATVATASTAFDYIYAAWTQIRNKPVPL | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 20975
Location Topology: Multi-pass membrane protein
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A0A1M5QZ18 | MKKTLMLLYGIIAYAIFFGTFLYAVGFVSSWFVPKHIDSPPQSSLGFALLVNAGLLSLFAIQHSVMARPAFKRWWTQFVPTPIERSTYVLLASLCLILLFWQWQPMGGVIWTVESEGAATFLKSLSMLGFGIVLVSTFLINHFDLFGLRQVWLNFRGEKYTDLPFRTPFFYKYVRHPLYLGFMIAFWATPVMTAAHLFFAIMTTLYMLTAIQFEERDLVTHFGVRYKDYKRSAPMLIPFTKASKAKKADRETSEVTV | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 257
Sequence Mass (Da): 29572
Location Topology: Mult... |
A0A834HFB8 | MTVPSSHYFIYIEHNSYLIGNQLSSACSDVSIIKAWKRAVRVIELDIWPNSTKDDVHVLHESVLAPHVSIFKGRGCMSIFVSDNGKSNHNLDDEDNDNCDKSLHASEPPLGEMDMSKILFTKGNRAVLARSSQLLVGLMMNMSNANEKLAASLCTHFAGAKHPHRATDVAAIVGKPFSPTFETRIRASPFNHFILTFLWSPYPSMGLA | 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(+)
EC: 3.1.4.11
Subcellular Location: Cell membrane
Sequence Length: 208
Sequence Mass (Da): 23027
Location Topology: Peripheral membrane protein
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A0KKR7 | MIPMIPPILDFATGRLAGAELVEKSTTLADLQGLFVDPHAEAALPSETRLYRVAMLPGHGGEGDLNMGVTYLEAGRVGQEFFMTRGHLHARAEQAEYYFGLCGQGVLLLQDMAGVCRLERVFAGSVHHIPGHVAHRLINTGETQLSALAVWPAVAGHDYGALGARGFDLRVLAGEDGTPRIVTSAGQAT | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 189
Sequence Mass (Da): 20099
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A0A0E4GBY6 | MGNSLAKIGIDVVFSKLGVVVAQWFVATPYAIRTFQQAFNSIDPRMEKVAKTLGYSPAQVFLKVTIPLTKMALVGGIMMSWARALGEFGATAMLAGITRMKTETLSIAVFLNMSIGDMNFAIATAIVMLFLALSLLIIVKTLVKNEVQL | Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 149
Sequence Mass (Da): 16133
Location Topology: Multi-pass membrane protein
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U1HW77 | MCQISAAASWLEQLQLIHGDLRPINILLDHRSNVKLCDFDNAYHFGEYIVGAHQPYYKMSKQGHFGKAGVGTEQFAVGSCFYFILTGDDPDFLLDADGEYASCSIDGFLMFNTLLQKCWNMEYASVADLKTEVVSKVEEVEHLELGKDSKIMGMEEFKNRVKECKDYLARCKLDFDGDT | 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... |
A0A0M3SH03 | GCVVWAHHMFTVGMDVKSTVFFSSVTMIIGVPTGIKVFSWLYMLASSNVSNNDPIVWWIVAFIFLFTIGGVTGIVLSSSVLDSLLHDTWFVVAHFHYVLSL | 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... |
B3VFD6 | MRVKGIKKNYQHLWRWGTMLLGILMICSATDNLWVTVYYGVPVWKETNTTLFCASDAKAYDKEVHNVWATHACVPTDPNPQEVKLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNATDNSTTNNSTTNNSGMKMETGEIKNCSFNITTSIRDKMQKEYALLYKLDIVPIDNDNTKDNTSYRLISCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCTNVSTVQCTHGIRPVVSTQLLLNGSIAEKEIVIRSDNITDNAKTIIVQLNKTVQIICTRPNNNTRKSIPIGP... | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system.
Function: Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp... |
H1LGM2 | MNDYLVKATTTDGMFRAYAITAQQMVATAQGDHDTWAASSVALGRTLIATTMLATSVNKNDEAITVKINGQGPAGEIVADADSKGNVKGFIHNPHVQLPNDGKHQMTSGKAVGVNGFLEVTKTSEGEDPYTSSVPLTSGEIGDDFTYYLAQSEQIPSAVGVSVFVNGDDMIGAAGGYLIQALPGAKDEAINKVIDHIQAMPAISETLLDGEAPETILEQVFGKGSLHFLTKLPVAFYCNCSKIKFGRDLEGLPVSQLETMLKEDKGIDVTCNFCESKYHYNADELATIIAAAKSRPKKTN | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversi... |
A0A084GX20 | MAGGLSGKTILITREETQATTFAAKIKKAGGVPVAAPLISFEKAKDIHKLKEAVRGIKAEDCLVFTSMNGVLFFFDFLKEHGFPCDFLSHCTFAAVGRKTRQLIEDRGYTVRIMPKEYVAERLAEEIAGSIRPFQHIYLFRGNLAREILMKELTLKGFSVTDLTLYETIHNTEDGNRIEQLLEEQKLDYITFTSSSTVDAFMKVMKNKNLDTLLKGVTLVSIGPITHKTLKKYGYDGIVSDPYTIDAMIDRIQTHAERQE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A554MP01 | MSFNFVYICPSCPFPPFGIPYKNTLLVLFIFCMQITLMEAKVSANHAKYIPIMLSVGKEKTDGWVVEGEKKSLALAVADPKKLNRRSWSMLIRRVISMAKAHHVKNICLNLVDFKFSHLKMSWEDLVEEITVNLKLANFEFVRYKTKPEEGWNWVKEVALITPEDSSRRSPATRGTEADKSAKAEIKKGLERGVILADEINNTRVLANTPGGDITPESLAEEAIKAAKGLPIKVEVLGVEKMTELKMGGLLGVGKGSHFKPRFIIMEYFGGKKSEKPVVMVGKGVTFDTGGLSLKPAPSLLDMHMDMSGGAACIHALVAA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xa... |
A0A834LDA8 | MPKPKASLKARYATDKLGVVGTLAVDAGDFRLLASATDTTFVGGPSLNGLSLSIEKPGSFFIDYDVPKQDVLFQFMNTVRVLDKPLNLTYTHEKGMNQTAFNGTLMLDPANELSANYGFDSGNCRLKYTYTHGAKTTFEPSYDFAQNSWDFTVSQKLFDDDILRASYETSSKVLGLDWSRNSMLNGTLKWMFDFNSLCGLVKSSSFQNDSLLIGFFEMSEMVSLCISASVNLAEKRKVPKFCAESSWNFDM | Function: High-conductance voltage-dependent solute channel with a slight selectivity for cations transporting triosephosphates, dicarboxylic acids, ATP, inorganic phosphate (Pi), sugars, and positively or negatively charged amino acids.
Subcellular Location: Membrane
Sequence Length: 251
Sequence Mass (Da): 27950
Loca... |
A0A0P1FMP5 | MPDPRFSALLLILAGPFMGSFLALLADRLPRGEDVIVKPSHCRDCNARLRLRDLLPVLSFGLTRGRCRHCGAAIPPVTLYSEIIATGAAILAVLAGGGTIDIWLSAGFLWLLLVLTLCDLQWFRLPDLLTGMLFLITLGMAVRGGAMDQALIGAGLGAGAFLALRLGYHAIRGREGLGLGDVKLMAGLGAFAGPLDLPLLVLIAAFGALAVAGGGYLLDRTAQDTPLAVRKLPFGSALCAAAAILWLLRAGV | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
D6NUR6 | MRVMGXRKNYQELWTWGTXLXGILMICSATEQTWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTDPNPQEVVLENVTESFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX... | Subcellular Location: Cell membrane
Sequence Length: 855
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 96544
Location Topology:... |
A0A2G2KG02 | MISSKQYFILTCILFLSACFPSFSQSPIDSVKKLITENKTEEALNISIAQLEIVEASRNTPLQIKWNSQIGKILRNNQNFESALKYYKIAKKLSIKLNDSLAIANSIFNIGSMQIFEYSIASYNAGNSEVSVDKRDLAFESFYYLLDEFKNVKGTEKIFAKTYANLTGLHSYTEEYDKADFSAHKAIAYFTTLNDTLSVIGVQNNLAVSQIYRKEYNKAERTFLSALPLLKDTTNLKILDYKISNLNNLSQIYAFKGNHEAALAKLEESFILKNILNKKKSSLAIAEIEEKYSQEKALAIQVKKSEKMLLWFTLFTATFL... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A929S100 | RTLLSASASGASSATSAMAIALNPNYASASWVTNQYDRFVRGQTALSQPDDAGVVRVDEKTGLGVAISTDANGRFTKLDPATGAAQALAESYRNVCTVGARPLAVTDCLNFGSPEDPDAMWQLVEAITGLADACKVMGIPVTGGNVSLYNSHGKVKGLLDSSINPTPVVGVLGVIDDVTRANPSGWQEEGLALVLLGETYDELDGSAWARVVHRHLGGLPPKVDLEAEMALGNVLLALSEARTPSGERLISAAHDCSAGGLVQTLLEGSLRCGVGVSVDIANAATAAADGAGLDDFTFLFSESGARCVIAVPEGALPAVY... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A1Y6EXL0 | MGILGSFQEYFNVLVERVSLSESMLRLLISSLILFTALLILRWIIRRFIRRTVKSVELRQRWLRQTRNAILLLLVLGLVLIWGNELRTLALSLVAIAVALVVATKELILCVTGTIVKNGANSFNLGDRIQVKDFRGDVIAQNMLATTILEVGPGKLTHQRTGRMIVVPNALFVSEPVINESYTHDYVLHVFTVPFKREENWRAAQQALLQATNEHCAPYLENVRAHMKRESQSRGLTSPSVEPRVSLQVPNAGEIHLIVRIPTKSENRSAIEQSILTDVFTNNDFSVKKDSGTEEKGIEKTNADNPDT | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
U1GPS2 | MAKTTVILSFACRGCRGSVLQSFTSTFLENPPLRPFQPPRLLPAARYSHARFMLADHSTQPTPSSDQSEDSNASVSLSPPNSVASSSDPIPWYLQVDTPQPPTPSHPFADRQIIPDLPEDSPAILSPMLEYLSVDTGLDNLTLLDLRSLDPPPALGANLLMVLGTARSVKHLNISADRFCRWLRSNYKLRPYADGLLGRNELKLKLRRKARRTRLAASVGNTMYEKGGRADDGITTGWICVNVGQVEEGHSKDVPEQARAAAESDMREHEDDAVPEFGIEEDDGGATMETGHKRELMGEVTAETGTKLEEEEYINPEQSI... | Function: Mitochondrial mRNA stabilization factor.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 412
Sequence Mass (Da): 45717
Location Topology: Peripheral membrane protein
|
A0A0E9LZ46 | MQNTTFHKYHGTGNDFVIVDNRDGAFDANDTLFVKYICHRRFGVGADGFMLLEKSKKHTFSMRYYNSDGNESTMCGNGGRCIVAFAHKLGLVPTGELFEFEAIDGLHEAGYDPEHIRLKMIDVSGIEEMAGGYFLNTGSPHFVSYTEDLDAVDVFTLGRSSVTIRCLEKVGVM | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
EC: 5.1.1.7
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Length: 173
Sequence Mass (Da): 19254
|
A0A554MR88 | MPLLPGRVLAEKILDELRIEISSKQLKPILAAILVGQDPSSKTYIALKQKACQKIGVEFRLFKMRKNTTQKKLSAQIQNLNEDKTVHGILLQLPLPAQLNPNQAIQAIDPEKDADGFHPANLEKFLRGDPDAILSPVPAGIKILLESTGQNLAGKNALITSNSEIFSKPILKILADKNIGGSWKSCRDTDIFDATKNADIFVTACGKPQWIRGENIKKGAIIIDVGINKIAPRKIVGDVDIDSVKNRASLVSPVPGGVGPLTVAFLLKNVMQLSEI | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A6G9KNW8 | MRVMGIPRNCQRWWMWGILGFWMLLMCNVMGNSWVTVYYGVPVWQEAKTTLFCASDAKAYEREVHNVWATHACVPTDPNPQEMVLENVTENFNMWKNDMVDQMHEDIISLWDQSLKPCVKLTPLCVTLNCSNVNATVNGTMNGEVMNCSFNITTELRDKRKKEHALFYRLDIVQLDDENSSYRLINCNTSAVTQACPKVSFDPIPIHYCAPAGYAILKCNNKTFTGTGPCNNVSTVQCTHGIKPVVSTQLLLNGSLAEGEIIIRSENLTNNVKTIIVHLNESVEIECTRPSNNTRKSVRIGPGQTFYATGAVTGDTRQAH... | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system.
Function: Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp... |
A0A7S0VPA0 | MHLTSVAKGAALLAGLMACMPEGADAFAASPASLARLGGRAPAVNFASAAQKGGRAPLTGLKMSLSKDDKLGPFLESEKNLDHVFRNNKMWVVEQTRNDPDFFLRMSTGQSPKFLWIGCSDARVPANEIVGCGPGELFVHRNIANLVVNNDNSIQSVFQYAVEYLQVEHIIVCGHYQCGGVAASLNNADLASPLEEWVCNIRDVYRLHKEELDAIKSPEQRKRRLVELNAREQAVNVYKAAVVQRRRVYTHMKTGLAQPKVHAVVFDPKTGNLKRINTFEGDEQIDELHEVYDLYDAQTAAEFWENEEEYPKRENTPRKL... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 343
Sequence Mass (Da): 38129
|
A0A5E4XR93 | MTSRAPRAPAPSSAVNSSAGAAGTDLRAVASPVAPCAILTRPDGQAQSLAARLHAEGIDTLEFPLLHIAAQADPAALSALDDALRSLTSYALTVFVSPNAVVHALSRLVHLQSVSGATDDGKTTVRWPETLPVAVVGPGSAQALAEAGIAAPTHRVIVPPGGPEARFDSEALLEQLDLPALAGRRVLLVRGDGGRELLADTLRANGTQVDIVSAYTRRAPEPDAAAWAALEARLASPLVSAQRCAWVLTSSEAVRHLATLLAARYGTRDGVHTPGTPQVLAQILSAPCFTSHTRIADAARSAGFDRITQCAPGDDNLLAA... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A7S0VZ50 | VWAHHMYTVGMDVDLKAYFVAATMVIAVPTGIKIFSWIATMWGGSIDFTVPMLWAIGFIFLFTVGGVTGVVLANAGIDHALHDTYYVVAHFHYVLSLGAVS | 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... |
D7S0R6 | MRVMGMQRNSRHLLLRWGIRILGMIMICRTAGQLWVTVYYGVPVWKDAETTLFCATDAKAYKTEMHNVWATHACVPTDPNPQEIMMENVTEDFNMWKNNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCGKVKNDTRDELRNCSYNMTTELRDRRQKVFSLFYRLDIVEIENNRTNNRTNNTEYRLINCNTSAITQACPKVTFEPIPIHYCAPAGYAILKCNNESFNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAKDQVMIRSENITNNAKNIIVQFKGSVQINCTRPNNNTRKSVHIGPGQAFYATDIIGDIR... | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system.
Function: Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp... |
A0A7S3MXA6 | VSFPIPILRLINSKVLFYCHYPDKLLSTQRSSSIMRFYRFFLDTFEELTTGMAQTIVVNSGFTQQVFLDNFPIIGASKSKKSDEVVKQDGLLIASHMPRILYPPINLKVFEKSENYSSQKIEDLLEGKITPGKTHVLTSLNRYERKKNIPLALKAFANFLERTSQKTGKAESEIDATLVVAGGWDPRVEENVGHEKELRQLAKELGITAKMVFLKSISNDQRLMLLENTNVLLYTPENEHFGIVPVEAMHMGCIVMACNSGGPLESVANGETGFLNPPKPDLWGEKIFGLLEASPDPERVKKMQAAAKKRVKDNFVMDVF... | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-al... |
A0A0D0D2F1 | MLSRSTALALAGLAATVIAASCDIYASGGTPCVAAHSTTRALFSSFNGPLYQVTRSSDNSVMDIRTLSAGGVANAASQDSFCSGTTCTISIIYDQTSRANHLTRAPGGGAASGADNLAVANAAPVHLNGQKVYGVFIPPGTGYRNDVATGTATGDEAQGMYAVLDGTHFNGGCCFDYGNAETSNDDTGNGHMEAIYFGNSRTWGTGAGNGPWVMADLENGLFAGSTAGNNPALPTITDRFVTAVVKGQPNNFALKGGNAASGGLTTFYNGPRPNVSGYNPMKKEGAIILGIGGDNSRGAQGTFYEGVMTSGFPSDATESQ... | Pathway: Glycan metabolism; L-arabinan degradation.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 332
Sequence Mass (Da): 33740
|
E4THV1 | MHKKSIELLNKAIAEEMTALQQYIYFHFHCDDQDLDILSTIFRQNAIQEMIHVERFAERILFLKGEVEMKASQDVQKITDPEEMLKMATKLEEDAIILYNKFANECAQHGDSVTKQLFESVIAEEERHYDDFDKESENIQTYGKEYLALQSMERAKKRGIPRPTTPVE | Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
EC: 1.16.3.1
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Le... |
W7DJ52 | MRRVVVLTREAEKNEIAQKKLENASIPTISIPLIETTPLKVDEKMKFSDYDWLFFTSQNAVHYFFWQYKTCPATVKIAVIGTKTEEALIEKGFHADFLPSKFETDIFIHEWLEQVEGKSSILFPQSLKGRSVISDLLSQKGFIIKRLFLYDTVMPQNAPLALKKLFAEESYFYITFASPSAWKNFKKICEETAFNGHYQIVSIGPVTSDIIRRDGYHVAFQPEIYTMDALLDLLIKEFLKNEF | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
X0KYY2 | MVYVSEYKPPHKLTAPHLRLDLEHEAAVYERLKPIQGVHVPVFLGAIDLRSMNKTYYYDHRVYVVHMTFLSWGGCSIDRAQRIGGMDRSLEDEAIRSLRAMHREGVIHKDVRLANMLFNPETNRVMVIDFERALLLKPPRRPLAQLVPNKRAWKSERMDAKKVTGDSSKRSRPSQSFSEDIWLAKTAFLEWNAGPWTRVARAPC | 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... |
A0A257RRR1 | MSVKVLVVDDSATMRELISAVLRRDPHIEVVGHAADPLEARTAIKQLNPDVITLDVEMPNMNGLEFLEKIMRLRPTPVIMVSSLTQAGASVTLRALECGAFDCVAKPTNGDYHDFNQLAEKVRAAAKSRVQPRSFAPAPPVTPDRNGRFAPDGRVVAIGSSTGGVEALIAVLSQFPANCPPVLITQHMPATFTKSFADRLNRLCAPEVAEAEDGMLVLPGHIYLAPGSAHLEIANSSKPRCRLHDGERVSGHRPSADVLFGSVARVIGARSLGVILTGMGRDGAQGLLEMRQAGAETIGQDEASCIVYGMPKVAFEIGAV... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A6G8PZA2 | MATADLYKALEVSKGATQDEIRRAYRRLARKYHPDANPNDKGAEERFKEIQHAYEVLSNPEKRREYDEGPRSFFGQSTQGTQTNLRDFGDLSDIFGSFGDVFGGASGGARGRPQAVRGDDVTVTVNLKFKEALEGVTTRVSAPVEDSCEDCRGTGAAPGTAPRPCPECGGRGVRSRDQGFFALSEPCGRCGGEGTVVEKPCRRCSGAGRLRKNRQVSVRIPAGAKTGTRVRLAGRGSAGRKGGPPGDLYVTTRVEEHPVFERRGDDFVVEAPVSFVEAALGRRSRCQGPRVGR | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0KN88 | MQRGFSMGTTLTRWLTILLTGLLLQACGFQMRGTAIPPELMTMKVVGDNKSDFYRLVTTRLKAAGVQLADKEGIPVLTLSGVGSTSQVASVDSIGQAREYVLGYNTQFTVSMPGKPTQVFPIAFNRSFLNKPDAALASSREQEQLGKEMQEQAANLVIRQLSQVKF | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 166
Sequence Mass (D... |
B9V668 | MTVMGIKKNYQNLWKGGILLLGILMIYSTAGQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEIELKNVTENFNMWKNDMVEQMQEDIISLWDQSLNPCVKLTPLCVTLHCTNYTRNHNNSTSANSTRVENKGEIKNCSFNTTTGIRDKIKKEHALFYTDDVVPIEDNNDSISYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAMLKCKDKKFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEKDVVIRSENFTDNTKNIIVQLNKTVQITCIRPNNNTRKSITIGPGRTFFAA... | Subcellular Location: Cell membrane
Sequence Length: 637
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 70950
Location Topology:... |
A0A7S3MY64 | MSEAFAYGMSNKATLNKLQGMLVFNSVLYVTAVVTLSGKFGIIGLVYANCVNMGVRGVMSLVISVKAQNEMITDQNKKISLLAIVLRVLSHKFFAGILVLGAGAVFLTNLGLDFALQKTMRKRASSRGRPTTSWLSKSS | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 14994
Location Topology: Multi-pass membrane protein
|
A0A522W0R6 | MAGRLKLSPSVKGRCSQAIMPALMLRQFRLWRTDTQPIAFASWACADDAVAARLEAGKRTLTAAEWQSGERKVTVDLIRPLWWPGGVRAGAAGGVGMIQVMEGWCPMPGRGRWRGAIPSTTSRSR | Function: Involved in fatty acylation of protoxin at internal lysine residues, thereby converting it to the active toxin.
EC: 2.3.1.-
Subcellular Location: Cytoplasm
Sequence Length: 125
Sequence Mass (Da): 13652
|
F1B0H7 | MRVMGIQRNYQHLLTWGTMILGIIIICSAAENLWVTVYYGVPVWKDAETTLFCASDAKGYETEKHNVWATHACVPTDPNPQEIHLENVTEEFNMWKNNMVEQMHTDIISLWDQSLQPCVKLTPLCVTLNCSSINNRDNITGEMEEIRNCSFNTTTVLRDKRQQVYSLFYKPDVVPINGSQGNSTYSEYRLINCNTSAVTQACPKVSFEPIPIHYCAPAGFAILKCKDERFNGTGPCKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX... | Subcellular Location: Cell membrane
Sequence Length: 853
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 96866
Location Topology:... |
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