ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A3R9ZLU8 | MNKKSKSIIIAFDGTAASGKGTVAKSLAEKLRYDYLDTGLMFRKVAYFSIKNKVNLSNIEKICELIDRIDFAKPIPLSEIYFDEVSDLSSKIAEFNIIREKLLNIQREFAKGKNGIVVDGRDIGTVVFPNADFKFFFDANIEERARRRYKQLQKMGKSIKLQKVLEYLKIRDKRDIERKSAPLLKADDSMLIDTTQMTIEESLNIILNKLKFK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 24529
|
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
|
L7PDR9 | MKHLVWASRELERFALNPGLLETKEGCQQIMEQLQSALNTGTEDLRSLFNTIAVLYCVHQRIEIKDTKEALDKIEEIKSKSKQKTQQAATDTGNSRSGSQNYPIVQNVQGQMVYQVMSPRTLNAWVKVIEEKAFSPEVIPMFTALSEGATPQDLNMMLNIVGGHQAAMQMLKDTINEEAAEWDRLHPVPAGPLPPGQMREPRGSDIAGTTSTPQEQIAWMTNNPPIPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQAAQPVKNWMTDTLLVQNANPDCKSILRALGPGATLEEMMTACQGVGGPSHKARVLAEAMSQAQQPNIMMQRGNFKGQKRIKCFNCGKEGHLARNCRAPRKK | 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
|
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
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 26648
|
A0A1J4XBY5 | MKTAAPETLRLRLQVGGEVQGVGFRPFVYRLALDLGLAGWVVNTAGGVVIEVEGGRERLADFETRLQSQPPKNARIEQFQRREIPPVGATGFVIGQSQGGEVTTRIGIDTALCPDCLRELFDPTDRRYLYPLITCTHCGPRYTITRQIPYDRANTSMASFPLCHACAAEYTDPLDRRFHAEPVACPECGPMARLLDETGQPLPGDCFVEAAGLLRQGKIVAVKGLGGFHLLVDALNPEAVARLRARKQREAKPLAVMGLNLPSLRRWLNVDPASQTLLEGVERPIVVVDPAKQEPWMEQVSPGGVGIGALLPYTPIHFLLFHALAGEPSGWDWLERPCEILLVATSANPGGEPLVTGNAEALARLGGIADATLLHDRDIVIRADDSVVLGGRAPVFLRRARGFVPRPVARLEGGSDGVAFGGDLKNTLAFSRGGEIFLSQHIGDLDNGATVAFAEESLTHLLHVLDLHPQWVACDLHPDFRSTRLAEVFAARHGLPLIRVQHHHAHIAAVMAERGLQGPVLGVALDGFGWGEDDQPWGGELLRVDGDGSMRRVGHLRPVALPGGDRAAKEPWRMVVAWLVQALGDGALPELKRRFANRPLLEPLVQRLLAGKETATTTSCGRLFDAAAALILGDVDNRYEGQAPMLLEGAARHGVAGDFPPCDITCGVLDPTPLLLGVLRGQQGGLGVADAAVGFHAGLAKGISQWVLQAAKPENVTDVILGGGCWNNRLLTDAVRMQLELHGLSVTNASIIPGGDGGISAGQVWIAVMKQ | 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 transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide.
EC: 6.2.-.-
Catalytic Activity: ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + diphosphate + H(+) + phosphate
Sequence Length: 771
Sequence Mass (Da): 82695
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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 Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 307
Sequence Mass (Da): 34169
|
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
|
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
|
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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8033
Location Topology: Multi-pass membrane protein
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A0A2J0MDJ3 | MSQITDQIKDRVDIVELVREYVPQLKKTGASWKSCCPFHQEKTASFLVSPEKQIWHCFGCSKGGDVFGFIREIEGLEFPDALRLLAKRAGVKLEARNPEIESKRARLLEILRLSTAWYHQALLSAKTADKVRKYVADRAISDETRDIWQIGFAPDAWEAVSAYLKSRGYQDAEIAQSGLSSRNDRGGYYDRFRNRLMFPIKDVHGSVVGFTARKMNEEDVGGKYINTPESEVYHKSSVLYGLSSAKKSIRENDLAVIVEGNMDCVSSHQAGVENVVASSGTALTREQVCLLKRFTKNIALSFDPDAAGQDALSRGLEIAWQEEMLVKIIILPEKEDPDNLIKRDVDEWKDRIKKAVPFMDWVIARAEKQHDLTTAQGKREAAKIVLSWISRVPDMIEQTHYLQMLSSKINVSEEVLRSAIGKSHKSARWISGKTPPASPPEYKGGKIGDPNEYRRGNIYQKTIIRLFALMVCDKKSIKIDEDLLKSESLIKLYKMLDKLYDSSIEELDQDIQSISREIIILSEEARLELSPEVREEERLGLINRLSNDQRKAKLSILREKIRSSEQEGNEKALREYLGQFQDIQKE | 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-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 66717
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A0A2N6BYQ0 | KIIARAERFREDMVVVDTGTWQGDVHGRHILELHAEESTPDAPEMDIQEAGTVYTALVMGVRDYGAKCGFSKGVVGLSGGIDSAVTCAIACEAFGAENVLGVAMPSPYTSVDSIEDAKKLAENLGCRFEVIAISSVFSALKESLAHIFTASKNSARPTVDITEQNMQARIRGNLLMALSNKYGSLLLSTGNKSEMAVGYCTLYGDMSGGLAVISDVPKLLVYKLAQYINRSKNLIPARIISKPPSAELAPNQLDQDDLPPYEVLDPILQAYLEQNKSVAEIAAMGFERPTVEDIVKRIRTNEYKRKQAPLGLKVTSKAFGYGRRYPTAQNFKEEDAL | 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
|
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
Catalytic Activity: 2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 + succinate
Sequence Length: 319
Sequence Mass (Da): 36275
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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(+)
Sequence Length: 236
Sequence Mass (Da): 25760
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A0A3L6QNE5 | MVQRHPPAHRRVGRQQRNPRHEQQYLSVAGAVPDQRLRPRPVRRGRPRPVDDQRRRCSSGSGGRQRCRGVLLNTGNLVIRSPDGTTLWQSFDHPADTFLPGMKIRIRYDTRAGERLVSWKGPADPSPGAFSLGGDPDTFLQVFVWNGTRPIWRSGPWTGYMVSTQTAQYLTNTSVIVYLAVVNNEEEIYITFSLSDGAGHARYVLTDSGDYQLQTWNRSSSAWILLGWTKAPGGECASYGYCGLNGYCDITELPSTCKCLDGFEPTSLEDLRSGRFSQGCRRKAALLCSDGFLALPGISSPDKFVLVKNRSRHECAAECTRNCSCVAYAYANLSTSRTKGDLTRCLVWTGELIDTVKVGVGDGSNTLYLRIAGLDEGKMRTKRSHALKTVLPAVLISGLLILAAISLAWFKFKGRVNYGAKHKKLTLDDMSASDELGEGNHAQDFEFLSVRFEDIVDATCNFSEACKIGQGGFGKVYKAMLGGREVAIKRLSKDSEQGTKEFKNEVILIAKLQHRNLVRLLGCSVEANEKILIYEYLANGSLDATLFDNSIKMLLDWPMRLNIIKGVARGLLYLHQDSRLTIIHRDLKAANVLLDAEMRPKIADFGMARIFNDSQESANTHRVVGTYGYMAPEYAMEGVLSIKSDVYSFGVLLLEVVTGIRRSSSGGIMGFPNLIVYAWNMWKEGKARDLADPYIMGTCSLDEVLLCSHMALLCVQENPDDRPLMSSVVFTLENGSTRLPTPNNPGHYGQTSTSDVEQIRDRTENSMNSLTLTTIEGR | 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
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 26980
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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 | MDPEKGVFNLLLPFLLLRVCTSTDTITPNQSIKDGDLLVSNGETFALGFFSPENSNRRYVGIWYNKISEQTVVWVANREKPINGPSGVLFLNQDGNLAIYDNSQNITHWDTNISVAETGTNTSTFYSARLMDSGNFVLFQGDTVSNVVWQSFDHPTNTMLPHMKLGLDLRTGLDRILTSWKSRDDPGAGQYSYRVEPSGSPQLVLYNGSVRVWRSTPVWIENEMSGSPNTTYWFLFNASYIDNQDDVSTVYTLVNNSIASSKFVDESGSLQMVSWLGRWVRFYSVPEDQCDNYGRCGVYGYCDSNNGREFECTCLPGYEPRSTDEWYLQDASGGCVKKRQALAMWGNGDGFVKVAKAKMPDTSKALVWKSLSIQECKEKCLRNCSCTAYVVGGRGICITWYGNLMDVRRFPDGGQDLYIRVDAIELAQYLKKYRSLNGKKVAILVASVVLTSFLIISFVCWLVMKKTRRKFDLVA | 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 Location: Endoplasmic reticulum membrane
Sequence Length: 187
Sequence Mass (Da): 21081
Location Topology: Multi-pass membrane protein
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A0A6L4AJK2 | MGLSSRRRFILHATCGYLLFGSAWIFLSDRLLLSFTDVEALTRLSTAKGITFILLTALLLLIALSIIPDRTAEESRTRLRSADIARSSDRIPAWAAYLFAVAVTVAMLYVREAIAVSFDDRPMLVLFMPPIILSSVLGGFGPGLTATAIAAIGIDYWGIPPVASLRIEKEHDLFQWCLLIASGLLSSYLSELLHRARRQAERRRIRQEQAKEEIRRLNAGLEQRVAQRTAELVAANTELESFAYAVSHDLRAPLRAMSGFSQALIEDYGDQLQGEARMYLDQIIVGSRRMGELIDGLLALSRSTRGQLQRDAVDLSAMAGRILNGLKEENPSRQIEWRVEPDLAVSGDERMLEVVIRNLLENAWKYTEKKDKANIRVFTREEGGNRWYCIEDNGAGFEAAYAGKLFQPFQRLHRQDEYPGLGIGLATAQRIIHRHGGTIRGEGSPERGATFCFTLPHSGTTEIKEGQ | 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 + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+)
Sequence Length: 182
Sequence Mass (Da): 20767
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A0A0S7X4S4 | MKKAKILRKRYPKFVFEKYAWRISEKDLEISFKFKMGSDIKFNPKVVIKNVNKNQIKRVEDSVLNNLIFHLGLIELLSYWKTACPPEIEIRAGFLNGEQIKFWRDLILKGMGQFFYENRIDFTRPSFLKIKATADAVLIGYYKEKLENRILVPIGGGKDSIITLEILKNAKKNITCFSLSPTTATQKVMKIGGCKTPIIVQRKVDRKLLELNRKGFLNGHTPLSAYLAFLSILLAVIFDYKFITFSNERSSNEGNLKYLGKIINHQYSKSFDFEKRFREYSKEYLTKEVEYFSFLRPLYEIQISKLFRRYPKYFSSFISCNEAFKTYSGRREPIKTWCQKCPKCLFIFTALYPFLGKYRLFRIFKKNLFERIGFLPTMLRLIGEKKFKPFECVGTKKETLIAFYLSWRKEKRGKKPFLLRYFEKNILPKHPNLEKESKKIMNSWSDQHNLPKEFEKILKERVKY | 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(+) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Length: 464
Sequence Mass (Da): 55154
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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 | MGFVEVVGKFVFGGGDKASCERMKLMMSEWPLQKHVVFAQSRANMWKKNGSALRLQHHHYCDVSVRDSTIDQALFLALFLLQVSLCVVYPLELMIACIDRFGLGDYFQDSVTDPTLWYDENLEPKQKINLLEDFLLLVIQLATYPVFINSWDRYTEIETPRKITGDQLLAHLVGGGQLQEPDRECPWTVQCLKDEMYNEVDPYWKYYSRNDQPFSTTADFLGTHVVADIVHWAFAHSMHIATLEQWADAVQSAFPQDHTSSPVIPTWDLVLDYALHLSMLALSVKAQEFAQQSVYLKGSEGTNSTFQKLWVMQSDAAFQPFRARVDYILDTIVANIPPHYTADYRAHKESENPIALSRPAKPDSKASAAARQKAIMAKCATGGRTSW | 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.
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: 387
Sequence Mass (Da): 43955
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A0A3R9ZRJ2 | MYKLTDKLSEYSNKVSESKHKLFGLIADNISNIITTKIFNIRNKELRKLKTELDKDTIPKEVSMYKYDFKVQIIASLFYWVLLASILWAMIYLKNQGLITIGDFAFVFGIIFAASNELWHAILNFRDLHASIGDLKQSFTILEEKHDLINKSSSKKIAIRNGKIEFNNVKFGYIREKLILNNFNLIIQSGEKVGLVGVSGVGKSTIVNLLLRFFKVNSGKILIDGQNINDIKEEYLYDYMSIVPQDIMLFHRSIKDNILQGNKKATVQDMIIAAKHANTDEFIQNLPNKYDTIIGERGIKISVGQRQRIAIARALLKASPILIFDEATSALDSITEKCIQETTQNIIKKSDKTLIVIAHRLSTLKNLDRILVIDNGKIIEEGSHKDLMLKENGKYRKLWNLQSDFLIF | 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 | MFFSLFFVQLFPSLVSTFNPSKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYKRAIELQPHFPDAYCNLANALKEKGSVAEAEECYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVTIVADQLEKNRLPSVHPHHSMLYPLSHNFRKAIAERHGNLCLDKINVLHKPPYEHPKELKASEGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFTDLSQVPCNGKAADRIHQDGIHILINMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDRETSPIEVAEQYSEKLAYMPNTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVTMKCPDGGDNVDSSAGLSMPVIPMNTIAEAV | 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(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 316
Sequence Mass (Da): 33801
Location Topology: Multi-pass membrane protein
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A0A2N6BZP3 | MFSKIGTRLTSAFIALAVLPILFLGTFIAQKTYSAARENAISVTQQTALRVAGEVESFIRDKAGHLELLTKVHGLQGLPRVEQRRILQELLLFQNAYDEISLLDNQGRELIKVHRTRIISDTDLASRANNREFQASMQTRKPYFGPVLFRPGTGEPYMICAVPLFDTKSGAITGLLVGDLRLKKMWDLLAAIKHRPGENVYIANQQGLIIAHKNPSIVLRGTRTTFDLAGAEHNMENHIGLFTDEAIIGDHDIFLGEQRLHVISEWQKENALSLAYRMLLVIGSGTLAALSAAILLVIPVVSAIVRPIRKLAATARRIEQGDINEEAGITNNDEIGELARAFNRMTAQLRTSVTALRTEVAERADIQKALQRELLINESLAAVSKVMLASDDINEIAQEVLQRAQALTDSEHGYVGYIDPRTASLVTPTITAMLGKECRLMEQNNRLEFPAEPGGHYGHLWGVSLNTKEAFIANTPASHPAADGCPEGHVPLVRFMSVPVLFNNRLIGQISLANGPIDYERRDIEAIERLARLYALALNRVHTLQEKEQLISNLRQSQKMEAIGTLAGGIAHDFNNMLTPILGYSEIALLRLKPGDDLFEHIEAIHLAANRAKELIKQILTFSRQQEHELVPVTMQPILRETIKLLRSSLPTTIELREDIAPECGAIMADLTQLQQVVMNLGTNAYHAMDDAGGILSISLRQAEITPTDPLARQGLPPGRIACLEISDTGSGMDGATLQRIFEPYFTTKEKGKGTGMGLAMVHAIISNHKGHINVYSEPGRGTTFKIYLPVIPAAEQGREQEKSAPATGGSEQILLVDDEEPIVLMLRDMLRNLGYQVTAITRSPEALDVFQAHPDKFDLVITDQTMPELTGGQLAKEMLAIRADLPIILCTGFSEILTEEMARQIGIRQYIMKPVIIQELAQKIRAVLETD | 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
Sequence Mass (Da): 28375
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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 | MWKKRNGAVWFLVKLCGINYFWKNDMMFKKIAAVILISFLLSYCDNKKVESVKLPPKNDSILKYLSIAFDESLPYKIRYENNFKALRIIEKQNNDSINRYYFFKVAGRFWNMKDTIDYKKITSFLIKQSESALDTFSMAKACSYMGDYFVLMNKPDSSYYYFDKSIKFYNKIKNSEEILEPLFSKAQIQHKYTDYLGYEKSAFDILRIIKGRPNKIELRYEANNLLGIAYGELSEFELSRKYYNIALSLCADKSIPLKNHFKAATLNNLGRMCTCQKKYKISKIYCEIGLKEANLRKDNPSTYAMLLSNLGHAKFRLNELDDLPDLFYQSLKIRDSLNDAVGVYNCYAHLAEFYLLKNDNIKALDFAKKTYKLTKENNFPRDQMYAVRILTKADPSKAFEYLQEYYRLFDSIEIADRRIKNKFARIEFETDNLIQQQKQLKAENAKKDRKLITVASLFGLALLLMIITYLLNRQRLKNRELAILRRQQQSESELYELRLAHQQQHDQGRQQEKKRIARELHDGIMGKLSAIRMNLFVLTKRTDPETIQKSLAHIDTLREVEQEIRNIAYDLGQTAFADSNDFIPVLRNMLQSAETATGMQTTLITEESIAWQDLDNNSKMQLYRILQEALQNTVKYAGASSLSVTISQANNILSIEINDNGKGFDKKNTGKGLGLRNMKERARELQGKLKIESKPNAGTTLTLTFPLTIK | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 710
Sequence Mass (Da): 82625
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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 | MEGAACLLQRLPPLPPAPLACHHARQLPPRPLAGEAGKERKSNANMVLDRWKLLQESLKAIIKRTVDNLPSEITEYVKEQFINPSERCSTSPLIDSSLKIYWEQTTKVARKRSWAESQESCISQMQWPQRNSGELGSSSCLRVQSISEEPRGVESRALGHWPAHCKLRVSFAAERKGRRFLSGGAAPVGRQPVSQIRRPREKVAFGARVGILCATAFQAIKRGDPWDGPAEGCQASSRRIANESKKCWHHAKLSVDGLVKCEKWIQDDEGRSEESKTSWWLNRLIGRTRTVPIDWPYPFVEDPPHGRNEINVELKKEAEFFGDIVIVPFMDSYDLVVLKTIAICEYAVHVVSARYIMKCDDDTFVRLESVMAEVKKIRSGMDYPIYANGPGYVISSNIADAILSEFLNHKLRLFKMEDVSMGMWVERFNLDA | 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 | MRVKGIRKNYQHWWRWGIMLLGMWMICSAAEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPIDPNPQEVFLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLKCTDLNDTNTNNSSTSENNTNPTISGGEGMGEGEMKNCSFNVTTNIRDKVQKEYALFYKLDIIPIDNTSYALRHCNTSVITQACPKVSFEPIPIHYCAPAGFAILQCNDKKFNGTGPCSNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVLRSENFTNNAKTIIVQLNASVEINCTRLNNNTRKSIRIGPGSTFYATGAIIGDIRQAHCNISREKWNDTLKQLVIKLGEQFGNSNIIVFKQSSGGDPEIVMHSFICGGEFFYCNTTQLSNSTWQRSDGTWNRTGGLNETKENITLPCRIKQIINRWQEVGKAMYAPPISGLIRCSSNITGLLLTRDGGNENNGTNGTETFRPEGGNMKDNWRSKLYKYKVVRIEPLGIAPTRARRRVVQREKRAVTFGALFLGFLGAAGSTMGCTSMTLTVQARLLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNTSWSNKSENEIWDNMTWMEWDREINNYTNLIYDLLEKSQNQQEKNEQELLELDKWASL | 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: Peripheral membrane protein
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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: Cytoplasm
Sequence Length: 294
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 34202
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A0A3L6RT13 | MVMLTVEAKIDSENSSRNTRTTVNSAGSHVLDSGDSSDKEHEKELNAAQSILLEEPTCIEESRLDGKTKENKIISTPAATVNNSKETAIESSKPEGVQSICLNSTRMIGEDHFKGISKPPIKHVYTRSKKQQVTEAINKSSLNKLDKGMGPESSNATRNWVSEMECKRELNIEEMTLTGVRKMSEEVGTCKEKEDNSVTLAAITINSKEKKISEDSSKTETAQLVPTHMKDIVALMLGSAFEGVSMDHTGPGRVRFHVKQYASRIDTRVPQNFEDNVTYESFSEMGLHENLLKGIYQYGLKTPSMVLRRGIVPLCKGLSVIHQSLFGTTVTLCCGVLHQLDYASEECQALILVPTYNLAQETKKIYTIIQYLPTKIQVGLFSTTFSNEALETSRRFMDKPATIIVPRGEELKDIMQYCLKVDNEEKKLSEIYALFEDCRGQKVIMFVNTKDKVMLLTEEVGKHYTVSASHDDMDQHARDIAIEKFESGSSTILIATDLRGTNAV | 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 all 7-deazapurine-containing compounds.
EC: 4.3.99.3
Catalytic Activity: 6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+)
Sequence Length: 226
Sequence Mass (Da): 24101
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular Location: Host membrane
Sequence Length: 53
Sequence Mass (Da): 6089
Location Topology: Single-pass type I membrane protein
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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 | MGARASILSGGELDRWEKIRLRPGGKKQYKLKHLVWASRELERFAVNPGLLETSXGCXXILXQLHPALQTGSEELKSLYNTVAVLYCVHQRIEVRDTKEALDKIEEEQNKSKKXVQQAAAAAXPGNSSQVSQNYPIVQNLQGQMVHQPITPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPPAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGDIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKVLRAEQASQDVKNWMTETLLVQNSNPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQATNSATIMMQRGNFRNQRXNVKCFNCGKEGHIAK | 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 | MTPKGISPTWPPASGISVLLKNSGLIFSFSRRGSMPRRGIMARCLLISLGFVLLWPCWASAFDRQGREQENIFVLHSYQSGLGWVEDVNDGIYKILLAKDQHNLELYMEYMDAQRLDEPNIFNRLREQLRRKYGRLTFTAVIAVDDIAIDFLARHHAEIFPGAATIFCGKAGGEPIDEYGREGFAGVVEHIDVAATLQVGLDLFPATERVVVINDRSVDGLLLDPLFRRQEENFPHLQFDFVTPVSMDELVEEVKLLSGNTLVLLGNFTRDERGQIFSNTRASWLIASRCKVPIFSMWDFYLGSGPMGGRMVSGKAQGELAAQLAMQVVWGDLLPGQTKTLTTDNHYAFSYNEMRWFDISYGALPDKSTVTQEPQSVLWKYKKLGWSVLGIALALEAMVIVLSVLIYRSKKAEAALEEHRNTLEEVVHQRTLELSSTNKVLHNEIEERKKVEAALLESEEVLHQLSNNLLTVQENERQRISAELHDELGQSLAALKLQLRGVVRGLDSQPVETLQAECEELRSSINHIIENVRRLSRNLSPLLLDDLGIDAALEHLVSSFAKFSGLEADIDLMEINTYFGQNSQRMIYRIVQESLNNMSKHAQATAFGVQIEKRQNRIFLVVKDNGKGFNVEEIFSSISPEKGMGLTAMAERVRILRGSFDVESEPGCGTAIHVTIPV | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 678
Sequence Mass (Da): 76150
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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 the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Subcellular Location: Cell membrane
Sequence Length: 287
Sequence Mass (Da): 31645
Location Topology: Multi-pass membrane protein
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A0A1V6Z205 | MQLTMATVCQIPFSHYQALMKAVSEMYHKRNMLAASLGQTKAKERGYATSAKMGHSSAVDTQVNAEITDLKRKDCSRRSSDLQNYSRSHETDQLLSLIRTIETGVPLEPNQVKSLGELLEQEIGVLSEGLKGRCTLTNNHYPQNLTIRNICDFMALPTLVYELEYPRTKKIDWLYVAEKILATFGIIVVMIAVSQSWIYPVVMDTVRMKEEGMTAQQRLQEFPWVLGDLLFPFMMEYLLAFYVIWECVLNAIAEITMFADRGFYSDWWNSVSWDQFARDWNRPVHNFLFRHVYHGSISEYLSLTVALTVAVEVYISRPEHSSKRSILLLTDVIGHRFINAQLIADQLAANGYMVVMPDLFHGDPVPLNNRPASFDLMTWLKGPPGHLPDCVEPMVRAILQEMKSNMGCARVGAIGYCFGAKYAVRLLQPGFCDVAYVAHPSFVDAEELQAIKGPLSIAAAETDSIFPASKRHESEDILAKTGQPYQINLFSGVEHGFAVRADITKPTIRFAKESAFLQAVAWFDQYL | 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 | MRVMGILKNCQQWWIWSILGFLMLMICSGMGNLWVTVYYGVPVWKEAKATLFCASDAKAYEREVHNVWATHACVPTDPNPQEINLENVTESFNMWKNDMVDQMHEDVISLWDQSLKPRVKLTPLCVTLNCTDNLNNTKSNSNNTSNSTNGTRNNNMYGEIKNCTYNVTTVLKDKKKSEYALFYKLDVVPLVPLKEQENRQENKLNVSRSNYSEYRLINCNTSAVTQACPKVSFDPIPIHYCAPAGYAILKCKNKTFNGTGPCNNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVHLNESVEINCTRPNNNTRKGVRIGPGQTFYATGDIIGDIRQAYCEINKNDWNKTLQKVGERLQKHFPNRTIKFERSAGGDLEITTHSFNCRGEFFYCNTSSLFNGTYKANSNSTNSTSKVNETITLPCRIKQIINMWQGVGRAMYAPPIAGTITCKSNITGILLTRDGGSGDNETEEIFRPAGGDMRDNWRSELYKYKVVEIKPLGPAPTEAKRRVVEREKRAVGIGAVFLGFLGAAGSTMGAASITLTVQTRQLLSGIVQQQSNLLKAIEAQQHLLQLTVWGIKQLQTRVLAIERYLKDQQLLGMWGCSGKLICTTAVPWNLSWSNRSQEEIWENMTWMQWDRELTITQTQYIVCLKNRKTSRRKMKKIY | 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: Peripheral membrane protein
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A0A7S0VYP4 | MSRLSAWAVLAAVWAGYASAFIPSAPSGVVGLRKGGLAPSGRMGEGITAPLPSNGLKGRAQLRMTLADPSAAAPEEGKKVAESEGVFRYFSTDAPGGAKRFRIVLMAGFETFNRELYKQAAAKAVEQCAGLEIFVFTDADIDAHPEALASALDGADAFFASLIFDFNQVNWLRGRIADIPNRFVFESALELMSSTQVGSFNMKAQPGKKQGMPPAVKSLLSKFSSTREEDRLDGYTSFLKVGPKVLKFIPVDKAQDMRRWLSTYAYWNAGGLPNVVTMLCELGRELGGLSPAYQSPPAAVPAGEQEEGGLAGLIQRAVRLFTSLFTAEAGEVEASAPPPTAPGVQEAPSRGLVHPERPGHYFPSPRAYLDWYHDRFPESRGRKVVAVLLYRKHVVSDLPYIPELVSHMEGEGLLPLPFFITGVDAHIAVRDSLTSVWERDAVQAGEVPPNPTLSQDAVDVDAVVSTIGFPLVGGPAGSMEGARQADLAKQILTAKNVPYFVAAPLLIQDVKSWHESGIGGLQSVVIYSLPELDGAIDAIPLGGLCCGDRDFCESRRDLKGCQREAGEIRLVKERLSRLTQRVKKWTALRAKREADRRVAVVLYGYPPGIGATGTAALLNVPRSLLKLLKRLQGEGYDVGEVPEDEEDLLRMCREADEVADTGRAYRNEEYKEGG | 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 Location: Membrane
Sequence Length: 237
Sequence Mass (Da): 26294
Location Topology: Multi-pass membrane protein
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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 | MLLLTDQPQPNPDGDDDEPNPNLNNSPIEKHHSPNQQPQLHYLPSLQSTVVIRQLPSQGLSFQLWPAATSLFSLLDLHRSHPYASPLSSLSLSSPPRLRILELGSGTGLVGITAALTLSADVTVTDLPHVLPNLEFNARANSDVLARHGGSVEVAALCWGEVDQMEGLVGREYDLVLGSDVVYHDHLYDPLLRTLGFFLVKGRRTVFVMAHLRRWKKEAVFFKRARKMFDVDVIHRDGPSHGSRVSEPSPVYTIDQALSAMGFGKFQGYVLAYAGLGWVAEAMEMMILSFIGPTVKYEWALSPGEESVTTSVFAGTLLGAYSWGLISDHFGRRQVFLPLSCPLFCLYLHIAFSVSVLKGLLSIAIVTSGAGFLSVFSPNYVSLVVLRCLVGFGLGGGPAFSSWFLEFVPAPNRGTWMVIFSTFSTFGTVLEASLAWIIMPRLNWRWLLAVSSVPSSIALLFYGPTPESPRLTLSLWLLFFGNAFSYYGIVLLTSELSSGQSKCRHSIGLHSEKIRGSSLYVDVFITSLAELPGLVLSAILVDRIGRKLSTVIMFALGCIFLLPLVFHQKEILTCLLFGVRMCIMGTITVANIYAPEIYPSSIRATGYGLVSAVGRICGMICPLMAVGLVTGCHQTAAILLFEAVMVVSGLSVMLLPLETNGTELTDIVGVPE | 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 a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm.
Subcellular Location: Host cytoplasm
Sequence Length: 96
Domain: The RNA-binding motif binds to the RRE, a 240 bp stem-and-loop structure present in incompletely spliced viral pre-mRNAs. This region also contains the NLS which mediates nuclear localization via KPNB1 binding and, when the N-terminal sequence is present, nucleolar targeting. These overlapping functions prevent Rev bound to RRE from undesirable return to the nucleus. When Rev binds the RRE, the NLS becomes masked while the NES remains accessible. The leucine-rich NES mediates binding to human XPO1.
Sequence Mass (Da): 10886
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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 in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 173
Sequence Mass (Da): 18743
Location Topology: Multi-pass membrane protein
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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: Multi-pass membrane protein
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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 N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 179
Sequence Mass (Da): 20292
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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-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: 101
Sequence Mass (Da): 11212
Location Topology: Multi-pass membrane protein
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B3VFD6 | MRVKGIKKNYQHLWRWGTMLLGILMICSATDNLWVTVYYGVPVWKETNTTLFCASDAKAYDKEVHNVWATHACVPTDPNPQEVKLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNATDNSTTNNSTTNNSGMKMETGEIKNCSFNITTSIRDKMQKEYALLYKLDIVPIDNDNTKDNTSYRLISCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCTNVSTVQCTHGIRPVVSTQLLLNGSIAEKEIVIRSDNITDNAKTIIVQLNKTVQIICTRPNNNTRKSIPIGPGRAFYATGEIIGDIRQAHCNLSSRNWEITLQKVAEKLREQFRNKTIAFNQSSGGDPEITMHSFNCGGEFFYCNTTQLFTWNTTQLVNNTWDSTWNGTAEPNRTITLPCRIKQIINMWQEVGKVMYAPPIRGTIKCSSNITGLLLTRDGGNNKNETKNETEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGAMFLGFLGAAGSTMGAASVTLTVQARQLLSGIVQQQSNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTAVPWNVSWSNKSLEQIWDNMTWMEWEREINNYTREIYTLIEKSQNQQEKNEQELLELDQWASLWNWFDITKWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPAQRGPDRPGEIEEEGGERDKDRSGRLVDGFLAIIWADLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWELLKYWWNLLQYWSQEIKNSAVSLLNATAIAVAEGTDRIIEVSQRAFRAILNIPTRIRQGLERALL | 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, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Subcellular Location: Cell membrane
Sequence Length: 870
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5). Coreceptor usage of gp120 is determined mainly by the primary structure of the third variable region (V3) in the outer domain of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and macrophage tropism), is used to trigger the fusion potential of the Env complex, and hence which cells the virus can infect. Binding to CCR5 involves a region adjacent in addition to V3.
Sequence Mass (Da): 99038
Location Topology: Peripheral membrane protein
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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 irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 31969
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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 + uroporphyrinogen III
Sequence Length: 260
Sequence Mass (Da): 29278
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A0A554MP01 | MSFNFVYICPSCPFPPFGIPYKNTLLVLFIFCMQITLMEAKVSANHAKYIPIMLSVGKEKTDGWVVEGEKKSLALAVADPKKLNRRSWSMLIRRVISMAKAHHVKNICLNLVDFKFSHLKMSWEDLVEEITVNLKLANFEFVRYKTKPEEGWNWVKEVALITPEDSSRRSPATRGTEADKSAKAEIKKGLERGVILADEINNTRVLANTPGGDITPESLAEEAIKAAKGLPIKVEVLGVEKMTELKMGGLLGVGKGSHFKPRFIIMEYFGGKKSEKPVVMVGKGVTFDTGGLSLKPAPSLLDMHMDMSGGAACIHALVAAAKLKVKKNLVVLVPAAENMVSGESYRPNDILTMMSGKTVEVLNTDAEGRIILADGLHYAHRYAPRLIVDVATLTGASLAALGQYGSGIFTKDESLSDKFCKWGEEVGNRVWPLPLWDEFADEIKSSFADLSNIGSVRWGDASHAAAFLSSFAGDFPWIHLDMAPRMVATKADHLAKGAMGEPVRLLVKVMENY | 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 Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 513
Sequence Mass (Da): 56330
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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
Location Topology: Multi-pass membrane protein
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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 release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 252
Sequence Mass (Da): 26333
Location Topology: Multi-pass membrane protein
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D6NUR6 | 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 | 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: Peripheral membrane protein
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A0A2G2KG02 | MISSKQYFILTCILFLSACFPSFSQSPIDSVKKLITENKTEEALNISIAQLEIVEASRNTPLQIKWNSQIGKILRNNQNFESALKYYKIAKKLSIKLNDSLAIANSIFNIGSMQIFEYSIASYNAGNSEVSVDKRDLAFESFYYLLDEFKNVKGTEKIFAKTYANLTGLHSYTEEYDKADFSAHKAIAYFTTLNDTLSVIGVQNNLAVSQIYRKEYNKAERTFLSALPLLKDTTNLKILDYKISNLNNLSQIYAFKGNHEAALAKLEESFILKNILNKKKSSLAIAEIEEKYSQEKALAIQVKKSEKMLLWFTLFTATFLAVIIFGNVLYRNSKLKSRNLALILIKKELEKTNQIEKLQNETQNKVLTATLDARVTERKYIAQVLHDSVSSLLSSASMHLLVIKKKSKDHIEEIDKSRHIIREASDKVRDLSHKLISAILLKFGLVTAAQDLCEKYSNSDLNFELKSEGDVPRFDQDFEIKLHNIIQEITNNIIKHSGATNATIAINYINDIIAIDIEDNGVGFDVKSTKSKNGVGLNLIKSRIKTLKGKFDLSSTKKTGTKIHIEVPVIMV | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 572
Sequence Mass (Da): 64652
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A0A929S100 | RTLLSASASGASSATSAMAIALNPNYASASWVTNQYDRFVRGQTALSQPDDAGVVRVDEKTGLGVAISTDANGRFTKLDPATGAAQALAESYRNVCTVGARPLAVTDCLNFGSPEDPDAMWQLVEAITGLADACKVMGIPVTGGNVSLYNSHGKVKGLLDSSINPTPVVGVLGVIDDVTRANPSGWQEEGLALVLLGETYDELDGSAWARVVHRHLGGLPPKVDLEAEMALGNVLLALSEARTPSGERLISAAHDCSAGGLVQTLLEGSLRCGVGVSVDIANAATAAADGAGLDDFTFLFSESGARCVIAVPEGALPAVYAAAEAEGVKAARIGTTGGDLFAITGHDILSQDLGAPMVLELAEVGLAVERVLPDLFN | 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 conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 377
Sequence Mass (Da): 38582
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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 conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 308
Sequence Mass (Da): 34648
Location Topology: Multi-pass membrane protein
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U1GPS2 | MAKTTVILSFACRGCRGSVLQSFTSTFLENPPLRPFQPPRLLPAARYSHARFMLADHSTQPTPSSDQSEDSNASVSLSPPNSVASSSDPIPWYLQVDTPQPPTPSHPFADRQIIPDLPEDSPAILSPMLEYLSVDTGLDNLTLLDLRSLDPPPALGANLLMVLGTARSVKHLNISADRFCRWLRSNYKLRPYADGLLGRNELKLKLRRKARRTRLAASVGNTMYEKGGRADDGITTGWICVNVGQVEEGHSKDVPEQARAAAESDMREHEDDAVPEFGIEEDDGGATMETGHKRELMGEVTAETGTKLEEEEYINPEQSIEDQDNNYIGFGSRSSAPRIVVQMFTEEKRAELDLEGLWQDRTTRRSRKAVIANEDAETALEGQSMVEEEEEEDDDLSSMVSDPRRAQSERAM | Function: Mitochondrial mRNA stabilization factor.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 412
Sequence Mass (Da): 45717
Location Topology: Peripheral membrane protein
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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
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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 + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 276
Sequence Mass (Da): 29959
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A0A6G9KNW8 | MRVMGIPRNCQRWWMWGILGFWMLLMCNVMGNSWVTVYYGVPVWQEAKTTLFCASDAKAYEREVHNVWATHACVPTDPNPQEMVLENVTENFNMWKNDMVDQMHEDIISLWDQSLKPCVKLTPLCVTLNCSNVNATVNGTMNGEVMNCSFNITTELRDKRKKEHALFYRLDIVQLDDENSSYRLINCNTSAVTQACPKVSFDPIPIHYCAPAGYAILKCNNKTFTGTGPCNNVSTVQCTHGIKPVVSTQLLLNGSLAEGEIIIRSENLTNNVKTIIVHLNESVEIECTRPSNNTRKSVRIGPGQTFYATGAVTGDTRQAHCNITKEKWKETLDKVKEELQKHFPNKNITFAPASGGDLEITTHSFNCRGEFFYCNTSNLFNSTNLFNSTDNSTDVGKEESNSTITLQCRIKQIINMWQGVGRAMYAPPIEGNITCKSNITGLLLTRDGGNSDNDTETFRPGGGDMRDNWRSELYKYKVVEIKPLGVAPTKAKRRVVEREKRAVGIGAVFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLKDQQLLGIWGCSGKLICTTAVPWNNSWSNKSQEEIWGNMTWMQWDREINNYTNTIYKLLEDSQNQQEQNEKDLLALDSWKNLWNWFDITHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLIPNPRGPDRPGRIEEEGGEQDRDRSVRLVNGFLAIAWDDLRSLCLFSYHQLRDFILIVVRAVELLGRSSLRGIQKGWEALKYLGSLVQYWGLELKKSAISLLDTTAIRVAEGTDRIIEVVQRICRTIRNIPRRIRQGFEAALQ | 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, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Subcellular Location: Cell membrane
Sequence Length: 853
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5). Coreceptor usage of gp120 is determined mainly by the primary structure of the third variable region (V3) in the outer domain of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and macrophage tropism), is used to trigger the fusion potential of the Env complex, and hence which cells the virus can infect. Binding to CCR5 involves a region adjacent in addition to V3.
Sequence Mass (Da): 96683
Location Topology: Peripheral membrane protein
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A0A7S0VPA0 | MHLTSVAKGAALLAGLMACMPEGADAFAASPASLARLGGRAPAVNFASAAQKGGRAPLTGLKMSLSKDDKLGPFLESEKNLDHVFRNNKMWVVEQTRNDPDFFLRMSTGQSPKFLWIGCSDARVPANEIVGCGPGELFVHRNIANLVVNNDNSIQSVFQYAVEYLQVEHIIVCGHYQCGGVAASLNNADLASPLEEWVCNIRDVYRLHKEELDAIKSPEQRKRRLVELNAREQAVNVYKAAVVQRRRVYTHMKTGLAQPKVHAVVFDPKTGNLKRINTFEGDEQIDELHEVYDLYDAQTAAEFWENEEEYPKRENTPRKLFNRMPTGLSAAKQSVSLPSSDDE | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 343
Sequence Mass (Da): 38129
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A0A5E4XR93 | MTSRAPRAPAPSSAVNSSAGAAGTDLRAVASPVAPCAILTRPDGQAQSLAARLHAEGIDTLEFPLLHIAAQADPAALSALDDALRSLTSYALTVFVSPNAVVHALSRLVHLQSVSGATDDGKTTVRWPETLPVAVVGPGSAQALAEAGIAAPTHRVIVPPGGPEARFDSEALLEQLDLPALAGRRVLLVRGDGGRELLADTLRANGTQVDIVSAYTRRAPEPDAAAWAALEARLASPLVSAQRCAWVLTSSEAVRHLATLLAARYGTRDGVHTPGTPQVLAQILSAPCFTSHTRIADAARSAGFDRITQCAPGDDNLLAALKTWADPIQVKHDDR | 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 + uroporphyrinogen III
Sequence Length: 335
Sequence Mass (Da): 34771
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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-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: 101
Sequence Mass (Da): 10993
Location Topology: Multi-pass membrane protein
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D7S0R6 | MRVMGMQRNSRHLLLRWGIRILGMIMICRTAGQLWVTVYYGVPVWKDAETTLFCATDAKAYKTEMHNVWATHACVPTDPNPQEIMMENVTEDFNMWKNNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCGKVKNDTRDELRNCSYNMTTELRDRRQKVFSLFYRLDIVEIENNRTNNRTNNTEYRLINCNTSAITQACPKVTFEPIPIHYCAPAGYAILKCNNESFNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAKDQVMIRSENITNNAKNIIVQFKGSVQINCTRPNNNTRKSVHIGPGQAFYATDIIGDIRQAHCNVSGTEWNKTLGEVVKQLRTYWNRTIIFTNSSGGDLEITTHSFNCAGEFFYCNTSGLFNSTWYTNGSTQGVTNDTIQLQCRIKQIINMWQRVGQAIYAPPIPGVINCSSSITGMILTRDGGNNNNGANGNETFRPGGGDMRDNWRSELYKYKVVRIEPLGVAPTKARRRVVQREKRAVGMGAVFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIEAQQHLLKLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNNKTQSEIWDNMTWLQWDKEISNYTELIYKLIEESQIQQEKNEQDLLALDKWASLWNWFDISNWLWYIKIFIMIVGGLIGLRIVFAVLSVINRVRQGYSPLSFQTHTPSPGELDRPGEIKEEGGEQGRGRSIRLVSGFLALAWDDLRSLCLFSYHRLRDFILIAARTVELLGHSSLKGLRLGWEGLKYLWNLLAYWGRELKISATNVLDTVAIAVAGWTDRVIEIGQRLCRAFLNLPRRIRA | 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, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Subcellular Location: Cell membrane
Sequence Length: 846
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5). Coreceptor usage of gp120 is determined mainly by the primary structure of the third variable region (V3) in the outer domain of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and macrophage tropism), is used to trigger the fusion potential of the Env complex, and hence which cells the virus can infect. Binding to CCR5 involves a region adjacent in addition to V3.
Sequence Mass (Da): 95911
Location Topology: Peripheral membrane protein
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A0A7S3MXA6 | VSFPIPILRLINSKVLFYCHYPDKLLSTQRSSSIMRFYRFFLDTFEELTTGMAQTIVVNSGFTQQVFLDNFPIIGASKSKKSDEVVKQDGLLIASHMPRILYPPINLKVFEKSENYSSQKIEDLLEGKITPGKTHVLTSLNRYERKKNIPLALKAFANFLERTSQKTGKAESEIDATLVVAGGWDPRVEENVGHEKELRQLAKELGITAKMVFLKSISNDQRLMLLENTNVLLYTPENEHFGIVPVEAMHMGCIVMACNSGGPLESVANGETGFLNPPKPDLWGEKIFGLLEASPDPERVKKMQAAAKKRVKDNFVMDVFASNLDKYVQEMQPLSGFNYMAGTILFFMSVAWGVLMSCKVLLFGA | 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-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+)
EC: 2.4.1.132
Subcellular Location: Membrane
Sequence Length: 365
Sequence Mass (Da): 40947
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A0A0D0D2F1 | MLSRSTALALAGLAATVIAASCDIYASGGTPCVAAHSTTRALFSSFNGPLYQVTRSSDNSVMDIRTLSAGGVANAASQDSFCSGTTCTISIIYDQTSRANHLTRAPGGGAASGADNLAVANAAPVHLNGQKVYGVFIPPGTGYRNDVATGTATGDEAQGMYAVLDGTHFNGGCCFDYGNAETSNDDTGNGHMEAIYFGNSRTWGTGAGNGPWVMADLENGLFAGSTAGNNPALPTITDRFVTAVVKGQPNNFALKGGNAASGGLTTFYNGPRPNVSGYNPMKKEGAIILGIGGDNSRGAQGTFYEGVMTSGFPSDATESQVQANIVAAKYTT | 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
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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 Length: 168
Sequence Mass (Da): 19705
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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 + uroporphyrinogen III
Sequence Length: 243
Sequence Mass (Da): 28145
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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 N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 204
Sequence Mass (Da): 23623
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A0A257RRR1 | MSVKVLVVDDSATMRELISAVLRRDPHIEVVGHAADPLEARTAIKQLNPDVITLDVEMPNMNGLEFLEKIMRLRPTPVIMVSSLTQAGASVTLRALECGAFDCVAKPTNGDYHDFNQLAEKVRAAAKSRVQPRSFAPAPPVTPDRNGRFAPDGRVVAIGSSTGGVEALIAVLSQFPANCPPVLITQHMPATFTKSFADRLNRLCAPEVAEAEDGMLVLPGHIYLAPGSAHLEIANSSKPRCRLHDGERVSGHRPSADVLFGSVARVIGARSLGVILTGMGRDGAQGLLEMRQAGAETIGQDEASCIVYGMPKVAFEIGAVSRQLSLGKIADHILRSANLHHRERV | 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 residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 345
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 36933
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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 with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular Location: Cytoplasm
Sequence Length: 293
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence Mass (Da): 31681
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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 (Da): 18148
Location Topology: Lipid-anchor
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B9V668 | MTVMGIKKNYQNLWKGGILLLGILMIYSTAGQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEIELKNVTENFNMWKNDMVEQMQEDIISLWDQSLNPCVKLTPLCVTLHCTNYTRNHNNSTSANSTRVENKGEIKNCSFNTTTGIRDKIKKEHALFYTDDVVPIEDNNDSISYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAMLKCKDKKFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEKDVVIRSENFTDNTKNIIVQLNKTVQITCIRPNNNTRKSITIGPGRTFFAAGDIIGDIRQAYCNISGTKWNDTLKQIVIKLKEQLEKLGNKTNKIAFKQSSGGDPEIVIHSFNCGGEFFYCNTTQLFNSTWFTNGTWINGTVLNTNDTDKGNITLPCKIKQIINMWQEVGKAIYAPPIKGPINCTSNITGIIITRDGGNNTGENKNKTFTETFRPGGGNMRDNWKSELYKYKVVQIQPIEIAPTRAKRRVVQREKRAVGALGAVFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQNNLLKAIEAQQHLLQLTVWGIKQLQARVLAVKRYLRDQQLLGIWGCSGKLICTTAVPWNANWSDRSVDDI | 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: Peripheral membrane protein
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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
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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
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F1B0H7 | 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 | 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: Peripheral membrane protein
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