ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A7R8ZIF7 | MWQGALVLLLLWVQQHHCQHQECTALSREPGVCTDVNVCRPLRPVIDFIKDNTKPVSRRAAAVNFLRRSRCPSRGSQRRKVRHQFNRTCTTTIQADKVVGGKPANVGSWPWAALLVYDDKLAIRCGGLLIADGWILTAAHCVKNGISPPGSQRRKVRHQFNRTCTTTIQADKVVGGKPANVGSWPWAALLVYDDQLAIRCGGLLIADGWILTAAHCVKNGIRPNLVRLGDHDLFRTDDIEHRTYPVLRIIPHEDYGKPLRGDNDIALIEINQSQGYPGGQFSDVLQQVQLTVVPTDDCAAIFKRGNFGDVVDEHKLCAYEEGKDTCGGDSGGGLFLPRPTTPGEPLKYYVIGIVAFGFRCAEVGFPGVYTRVTDYLDWINARID | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 384
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 42548
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A0A7R8WH47 | QLLAPQHGIRINCKHHLSNYTYNKSDDPEMKSIIEKSWLQTRVYVIIADRDLTLDFIRTMYRMGYSTRDPYQVITLDYNNVYYPNGPSNQSFFYKWVDFHHLDLEHATEEQWRDYVEPFRHVLEITKLYPVDDGLDGDFGLNVKNRSVEAPFCVPYHRMLMNENEVPLTATYAYDAVSVYAKALAKVLQDFGEEGASNGTLVMKYVFNSTYESVMGLETHIDNSGDTEGNYVLLALRLQGRNFMDAEMTPVASFNYTGLESSGDSLPRVQFIGSGRIDWPHGVIPLSDPVCGYDGSRCLQTDWASPIVGSTIALFLLIVSALGVRYYFKEHGLEMQLWKVCPKDLEEVREFRHNQSCSSLSDPQSISRGSDSGAPGSPLGRKAHVRVYKRQRVYLKMICKEKVDLTQEIRRELVTLRQIRHENLVFFVGAVVEPGFVAVLTPYFPRGNLEDFIKCGTHFLDQTIFESLTFDLLQGMNYLHYSDIVSHGNLHPRNCLIDSRCVLQISDFGLHMFKATSVRLDPTDPQIVFRAPEFLKNLALPSPRGTQKGDVYSFAMVLYAMTTRKRPWANSSFSLSEIIARVISLDNFRPPIQDIPVPFSADHVVRAIRDSWSDNPEDRPDFKYLLRKFQEKSSRNPNIFDHVMELLSQYTERLEDQVKEKTKQLIMEQKRTEEEKRKTENLLYNMMPKTVAEDLIQGKAVAHSFTSVTIYFSDIVGFTELAARMKPEEVVSMLNGLYSLFDTVIETSYPGVYKVETIGDAYMVASGCPQVREASEHASEIAFLALHLLETTKDFDIPGRPSTEKLKLRIGIHSGPVCAGVVGRKMPRYCLFGDTVNTASRMESAGEEERIHVSAATRDLLESKGLFAIKERGDVFIKGKGVMRTYWLEGVKNPLNGWTPLIPSESDTTKTSPQKETLMDARMMNPTAFLVRRSATLNPASSNCGPSRIMNLYSWKNDDLRPIPASPPEANGTIPGILGRFDLLRLHPE | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
EC: 4.6.1.2
Subcellular Location: Membrane
Sequence Length: 989
Sequence Mass (Da): 112318
Location Topology: Single-pass type I membrane protein
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A0A3B9FGC6 | MATGDRLVGNTKAGNTEAGLGLTKQSLTSHLPVGAIVGAQGIKGQFKVKPFTSTPDALAAYGPVILDDGRQMQLQVTSVNAKGLAIVRAKGVDTRDAAEALRGTTLYVAREQLPDLDDDEIYHADLLGMMVSAEDGKPLGKIVAIHDFGAGEIAELAPDKGPTIMVPFGGENLITVDIKAGKIGLLVPDGLLDDQPE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 197
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 20496
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A0A6B0WMQ5 | MSTSRLSSSTRGRAGGPSASSGASSAPLLEIGRVGRPHGTSGEVTVTLVSNRPERLEPGSELQTDLGTLTVSSARPHNKRHLVAFDGIDDRSKAEALRGLVLKAAPLVDPDELWVHELIGARVVDQAGTDRGAVASVVANPAGDLLELTDGALVPLRFLVRSVPGERIDVDVPDGLFEAAT | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 181
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 18829
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Q57Y42 | MIKMSPLLLKAAVVTACLCSLAVATTVEEQTAPKPIENATTYQQELGGRGKVDSPIAPGDAVSITSGIKVMSVTTATAIIFLASAFGFSFAMYWWYVASDIKITPGKGNIMRNAHLTDEVMRNVYVISKRVSDGANAFLFAEYRYMGIFMLGFGALLYFLLGVAMSSPQGEGKDGRPPVAVEAPWVNAAFSLYAFVIGAFTSVLAGWIGMRIAVYTNSRTAVMATVGSGGSDDDVLANGSQSRGYALAFQTAFRGGITMGFALTSIGLFALFCTVKLMQTYFGDSAERLPELFECVAAFGLGGSSVACFGRVGGGIYTKAADVGADLVGKVEKNIPEDDARNPGVIADCIGDNVGDIAGMGSDLFGSFGEATCAALVIAASSAELSADFTCMMYPLLITAGGIFVCIGTALLAATNSGVKWAEDIEPTLKHQLLVSTIGATVVLVFITAYSLPDAFTVGAVETTKWRAMVCVLCGLWSGLLIGYSTEYFTSNSYRPVQEIAESCETGAATNIIYGLSLGYISVLPPILAMAFTIYLSHHCAGLYGYALAALGILSTMSIALTIDAYGPISDNAGGIAEMAHMGHEIREITDALDAAGNTTAAIGKGFAIGSAAFVALALYGAYVSRVGISTVNLLDARVMAGLLLGAMLPYWFSALTMKSVGVAAMDMVNEIRRQFQDPAVAAGTKEPDYESCVNIATGAALQQMVAPACLVMLAPIVTGILFGRYTLAGLLPGALVSGVQVAISASNTGGAWDNAKKYIEKGGLRDKSKGKGSPQHAAAVIGDTVGDPLKDTSGPALNILVKLMAIISVVFAPVVQSKLGGLLVK | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 826
Sequence Mass (Da): 85936
Location Topology: Multi-pass membrane protein
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H8ZL61 | LYFLFGAWAGMVGTALSLLIRAELNQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMVGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPTVSMYQIPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTAFFDPTGGGDPILYQHL | 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: Membrane
Sequence Length: 217
Sequence Mass (Da): 23226
Location Topology: Multi-pass membrane protein
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L2FW86 | MLYLVGLGLSDETDITVKGLEVVKKASRVYLEAYTSILLVDKAILESYYGREVVIADREMVESNSDEILRDAQTVDVAFLVVGDPFGATTHTDLVLRARELAIPVSTVPNASIMSGIGATGLQLYNFGQTVSMVFFLDNWKPASFYDRIRENRSIGLHTLVLLDIKVKEQSLENMARGRKIYEPPRYMTVGQCAAQMLEIEEEKGEGVYGPDSLAVGAARVGGKTEKFVAGTLKELCETDDILGGPLHSMVLLGRRAHELERDYIREFAFNKETFDKSWEVDYGKQ | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
EC: 2.1.1.314
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine
Sequence Length: 286
Sequence Mass (Da): 31858
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Q583T3 | MTKAVTEWPVNRVRQEFVSFFEQRGHTFVPSSAVVPHNDPTLLFTNAGMNQFKNLFLGTADPNTDFGRLTRAVNSQLCIRAGGKHNDLDDVGRDTYHHTFFEMLGSWSFGDYFKREAILWSWELLTEVYKLPKDRLYATYFEGDPANGIEADEESKQLWLQLLPASRVIAGNAKDNFWEMGDVGPCGPCSEIHFDRIGGRDAADLVNKDDPMVLEVWNLVFMQFERRAGGVIVPLPKMHVDTGMGLERLTSILQGADSNYDTDAWTPLFDTIQKVTGFEKSYAEVRHDTCDATVAYRAVADHIRCLTVALADGAMPDSVGRGFVLRRIIRRAVRYGVQFLGAKVGFFHQLVDSVVSSLGPFFKHIQEPRTVQRIKGVLADEETSFARTWETGLKHFNKAVAEAVNNVISGENAFILHDRYGFPVDLTSLLAEKANMSVDLEGFHATMKASQLSSGRVAAAKTFIDVHQLEELKAGGVSPTDDSAKYTWKKHVAEVKAIFDKKSGSFVDVLLPDSEMGPEDIGIILDVTNFYAEAGGQIYDTGCIVAAPDAIFDVRKVYNVGGYIVHVGGMRSVEDGAAAPIPVTASVELQVDYERRLPIAANHTSTHILNWCLRRVLEEEAKDNFMEVNQKGSLVTPEMLRFDFSYNNKVSLEDLIKVEKLINQIIQQGLEVYRKEIALDAASRIAGLRHMFGEKYPDPVSVISVGVPVEKLIAEPESEEWRAYSTEFCGGTHLSNTQDAQLAVILSEESLMKGIRRMVVATRDAARKAQEGGKALQQEYREIMSRPASDAVAKSLSVLNKKVGDSAIPLVVKNTLREEIDGSIKNVLGALKAQAAQMKEKATEAGRAAAEAYDASAGPLLVRHLTDTGADREALQAYADGFSKAVSGDVGLFLVGSDESKALALVSLPPAFVAKKLDAVSWAKTAVGKGGGKPSAAQSGFPAANTTQVLQKAEVEAAKMMAVLLN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Mitochondrion
Sequence Length: 966
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 105913
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A0A7R8WMY3 | MGYCRPAAKPAQEPQRHLPAQEPQRHLPAQEPPRHLNPNEEVIFPEARRAVAAIGSGNVHGLVVFKQANPSAPVIVDVDLQGLSPGYHGFHVHQFGDIRDGCKSAAGHFNPFKVTHGAPHDPVHQRHVGDLGNILADDYGRVRVLLEDKLLSLYDPQGHNEPSRNIAGEYLLEDKLLSLYDPQGHNEPSRNIAGRSVVIHAGVDDLGQGVGGAREGSLKTGNAGSRVACAPIVLANPATTA | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 241
Sequence Mass (Da): 25822
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A0A5A8DH59 | MTWAIVIYANWAVTLFVVPPWLGDSSVATYVLLGVFRLISFLGLFSHLRAVISNPGAVPPGARPTDPELGERQCRRCQAFKPERAHHCSICQRCIIKMDHHCPWVNNCVGLSNHKFFLLFLLYVCTLCAFAVVLVAGRVLACATAPKQASGTVDPGKGIPSTSSSRPAVCHVDAGSAIAVVMLVTLAFLFGIFTLCMMCDQYPALQDGMTMIDRYQARDRAGADSASIRRQRRSPGAALAEVFGGRASDGFQLHWLLPTAVRYPDPEAIAGYSMRTRGRRLAPKGAPVGGRLGAGPAGIDSDGEAEAMEDDAAGTDTDSDMFHNRRRF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 328
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 35474
Location Topology: Multi-pass membrane protein
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A0A182H1H7 | MNRMLWIDKENLVACFESGVIGQDLEREVRKLGFTMGHEPDSFEFSSLGGWVATRASGMKKNLYGNIEDIVVKVKMVTVKGVLEKSVAVPRISCGPDFNHIILGSEGTLGVVTEVVVKIRPLPETKKYGSLVFPDFGSGVRFLREVAKQRLQPASIRLIDNEQFAFGQALKPAGGVLSSISSALQKAYITGVKGMDMEKIAITTLVFEGTAKDVKLHEQKIFAIAAKHGGFSAGSTNGEKGYILTFVIAYIRDLALEFSVVAESFETSVAWDRCETLCTNVKNRISKECAKYNIKHYLVSCRVTQSYDAGACVYFYFGFNHTGFPDPVIIYETIEGHARDEILASGGSISHHHGVGKIRARWYPKTVSDVGVSLYRATKQELDPNNIFAVGNFLPELQTGHHGEHQQNPEGSSGQGTLMSKL | Pathway: Glycerolipid metabolism; ether lipid biosynthesis.
Function: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Catalytic Activity: a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+)
EC: 2.5.1.26
Subcellular Location: Peroxisome
Sequence Length: 422
Sequence Mass (Da): 46352
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A0A0D5YHV6 | MSEAQFDLIVIGAGPGGYVAAIRAAQLGLKTAIVEERHLGGICLNWGCIPTKALLAGAELATQFKHARQFGFQVSQLDFDIQKLVQHSRQVSAQLVQGIDYLLKKNQVTVFNGRAQLTAKEKLEVTDAQGNSQALSAPHIILATGAKARHVPQLPVDGTYVWSYKEALVPEQLPKSLLVVGSGAIGSEFASLYQDLGCQVTLIDLAKQILPTEDAEVAQFVRKQFEQKGMKVLTDAVVQSIQIENEQVHCVVETANDVQTLVFDRVLSAIGVQPNTTGLGLERLGVELNPQGFVAIDDYCKTNVAGLYAIGDVAGAPCLAHKASHEAIICVEKIAGVANVHSLDRSQIPGCIFTHPQVASIGLTENAAKAKNLPIRIGKFSLTANGKALAIGDASGFVKTVVHAETGELLGAHMVGHEVTEHIQGFVIAKYLEATDESLAQVIFPHPTLSEAMHESILASMQRAIHM | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 467
Sequence Mass (Da): 49961
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H9TA35 | TLYLIFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSSVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGRDPILYQHL | 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: Membrane
Sequence Length: 218
Sequence Mass (Da): 23328
Location Topology: Multi-pass membrane protein
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A0A335KBH6 | MKKSLSVILITIFLDAVGIGLIMPILPELLRSLAGAEAGGVHYGALLAVYALMQFIFTPILGALSDRFGRRPVLIISIAGATADYLLMAAAPSLLWLYIGRIFAGITGANMAVATAYVSDITPAHERAKRFGLLGAVFGIGFIAGPVIGGVLGEWNLHAPFFAAAFMNGINLIMTAVLLKESKHSNKMTEKVQEQSILKKLSYLITQPNMAPLLGIFLIITLVSQVPATLWVIYGQDRYGWSIFIAGVSLASYGICHSIAQAFAIAPMVKRFGEKNTLLCGIACDAIGLLLLSIAVEEWVPFALLPLFALGGVAVPALQAMMSRGISDERQGELQGLLSSFNSLGAIIGPVLVTSLYFMTQASAPGMVWALAAILYVITLPLLLKYRLNKYSGVP | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 395
Sequence Mass (Da): 42144
Location Topology: Multi-pass membrane protein
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A0A249A504 | MQNEVILTMKNISKSFAGVNALKGVELTLRKGEVHALMGENGAGKSTLMKCLLGVYQADEGEIIYKGQPVRFESVLEAQKAGISMIFQELNLIPHLTVAENIFFAREPLKHGLVDKDKMVEESAKLLNFFEIDVDPNDEVRMLSVAKQQMVEIAKALSFDVEVLIMDEPTSALTEKEIDKLFELVDRLRAKGVSIVYISHRMEELKRICNHITIFRDGTYVSNHKFNEITMDEIITKMVGRSLDNHFPPKTAVVTNDIILSIMNAERKGVFEPLNFDLRKGEILGITGLVGAKRTELARAIFGADPLDSGEIFVHENKVSIKDPSDAIKAGIAYLSEDRKLNGVAVRMSIRENITMASMDKVANQIGVISYDEEEKASKTFIDKMEIKTPTIEQKVQNLSGGNQQKVVIGKWLFREAKVMIFDEPTRGIDVGAKYAIYQLLDELAANGVGVIVISSELPEVLGVSDRIIVMREGRMTGMLETKKTNQEEIMHYATGVKNMFAREYGVEK | Function: Part of the ABC transporter complex LktBD involved in leukotoxin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.
EC: 7.4.2.5
Subcellular Location: Cell inner membrane
Sequence Length: 509
Sequence Mass (Da): 56893
Location Topology: Multi-pass membrane protein
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A0A8C0Z090 | MAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVSAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHSRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDSPGVVTCLDEARHGFESGDYVSFSEVQGMVELNGSQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLLASLAEPDFVMTDFAKYSRPAQLHLGFQALHQFCAQHGRPPRPRNEEDATELVALARAVNARALRAVQQDSLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEALTEDKCHPRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATLLRSVQVPEFTPKSGVKIHVSDQELQSANASVGEGVWPDGQESPLHLSPARARMMTAISIWISLWLLPTSGQRTMTFPLRTGIR | Pathway: Protein modification; protein ubiquitination.
EC: 6.2.1.45
Catalytic Activity: ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
Sequence Length: 833
Sequence Mass (Da): 92410
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A0A1B8J6E7 | MNTFGRLLRVSTFGESHGEGIGCVIDGFPAGVAIDLAFLDSEMQRRRGGRTAYATPRKEDDAVQILSGVFEGKSTGAPIALFIANNNTKSKDYSDIQSVFRPGHADFTYHHKYGVRDYRGGGRSSARESAARVASGAFAKMLLNEFGVVCESGILHIGECLGSEIDFAHARESEIFALDRHQEEAQKQAILQAKKAGDSIGGCALIRARGEAKILRGLGEPLYYKLDAAIGAMMMGLNGVKAVEIGDGVESSRRRGSQNNDKMDSRGFLSNHSGGMLGGIGTGEDIVVRVYFKPTPSVFVAQETIDASGNERELLLKGRHDPCIAVRGSVVCESMLALIIADMLLLRATERIENLKAIFDEK | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 362
Sequence Mass (Da): 39063
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A0A3E0RKF4 | MSAYMIIFITGSYLAFLFFVAQWGKNAGKAFLEKYSAVFYALGICVYATAWTFYGSIGRAATHGLDFLAIYLGPILFLPIWWTVMRKIIRISKAQHLNSLSDFITARYGKSWFLAVLTTVLVVMAITPYLALQIKAISSSANVLLNDSNSAPIDIDLASTILLFIFAMFYGIRFAFDPKQRNGLVATIAFESTIKVLTAFICGGVIVYTSFKGPSSIYQEGTSVGLSQLLSIQSSSDWMLMLLISGFAFFLLPRQFQMAVVSNKKEKDLKTAVWLIPLFLLLMNWWVVPIALGGHLQLPQGTNPDYFFLDLALNTSPVLAGFVFIGGFAAATSMIIVSSSALSSMISNSIIMPLFLNRKDSSRETITPIVAQRIGLFIVFALAFSYHAIIVQKESLVSIGMISFIGIAQLAPGFLAALYWRNATSKGVMAGLSLGFILWLTAFGVPQWLGSRSDEILLFNVFEQWSPLANITFISLGLNGLVMSAVSLMDTPSKLERNQAEIFYNILSIEPGLYENSNSTSGKITFERLEKLLFRYLPEELVSETLFRRYTINRINPKPFDTVPAHLISYAERLLTQMMGPATARIALNKEFESETIDLFDIQDILQETRETKKLNTALKEKSDRLAKLTGELTQANDQLHSMGKLKDDFLYTVTHELRSPLTAIRAQIELLRDEEEMPKEIRDQFLDATIGECVRLTSLISNVLDIEKFESGNQQLSLSKVDLRKTLATILETQLIVAEREGISIAIDGPEEVWTLADEKRITQVIINLLSNAFKYAEKTVEVCFKEDAQDWHVHIIDDGPGVPLEAVPHLFKKFYQSDDQTVKKRVGTGLGLAISDNIIKAHKGALNLTSNTPEGRTTFTFKISKYGNN | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 871
Sequence Mass (Da): 97125
Location Topology: Multi-pass membrane protein
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A0A4P9JF96 | IGTLYLVFGAWAGMIGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLTSSALEGGAGTGWTVYPPLAGNLAHAGASVDFAIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG | 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: Membrane
Sequence Length: 225
Sequence Mass (Da): 24152
Location Topology: Multi-pass membrane protein
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A0A2R7ZYZ1 | MKKILIWILCIFLLAVGAMGAYAYKVYHDVTKTTDKMYKKVDKEETRKTPINIEKGEPFSVLLLGVDTGDLGRTEQGRSDSVMVVTVNPEKNETKIVSIPRDTYTEIVGHGTTDKINHAYAFGGTTMAINTVQNLLDIPIDYYIEINMQGVKEIVDAVGGVDVESPLDFTQDNIKFTKGPVHLDGEKALAYSRMRYEDPTGDYGRQGRQRQVIEAIVKKAANFSTLTRYKDILNAMGNNMATNLTFDDMMDIQGKYKAAAGNVEQIQMQGTGEMINGVSYQIIAPEELQKISENLKIQLGL | Pathway: Cell wall biogenesis.
Function: May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 301
Sequence Mass (Da): 33520
Location Topology: Single-pass type II membrane protein
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A0A1B8J6L9 | MADSSANANASDAKSSIDASLKALERKCNGGDVDSCSELASMYYEGEKIAQDYVKAAEYTTKACDLGHARECRRIGYLYNYGQGVKQDYIKARELYQKACDGGDAGGCFNLGNLYAEGQGVRQDYAKAREYYQKACDGGDAGGCLNLGNLYNDGQGVKQNYPKASEYYQRGCDDGDADGCFGLGLLYKNGQGVKQNYTKASEYYQRGCDGGNAGGCFNLGNLYNDGQGVKQNYTKANEYFQKACDGDIAGGCFNFGVSYYNGRGIRQDYTKAKEFMGKACDFGYQRGCDIYKDLQNWGY | Function: Hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
EC: 3.5.2.6
Subcellular Location: Secreted
Sequence Length: 299
Sequence Mass (Da): 32695
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K8Z6W9 | MADIQKPTPVLLAEGPAFVFEFISQCELPTDRGLFHLRAYRYTHKTGRRQVVEPVVLFQGEHRGGKQVWVRVHDQCLTSEVLGSRRCDCKEQLEMALDRIVGNGSEGGLVIYLPQEGRGIGLANKVAAYALQEQGLDTVDANLFLGFGDDERTYDYVSFILQDLGIESIRLATNNPFKTRSLRAAGVQVDGVDGLQPSANRHNLHYLRTKILKMEHAMELRLGGGEGREGEREEGGSLDGTEAATTPEVLTESDRNSLSSEKERILDQEGLEEELEEEREEGGRRGNGEGSVEDKVGAGVSAGTLARSEGPQTGEAGEKAAKAAAAAAAAAAEAEKKLQAPGYCFGKATVEAAINAVAAGKMVVVVDDEDRENEGDIIIAADKVTTEAMAFIVRHCSGVVCVSLEGEDLDRLALPPMIAENEDPKHTAFTVSVDYKHNTTTGISAHDRAATLRALADPASRASDFTRPGHIFPLRYSPGGVRNRRGHTEAALDLSKLAGRRPVGVLCEICSEDGSMARLPELREFCARHNLVLTSIADLVAYRVEHEGS | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Length: 549
Sequence Mass (Da): 59340
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D6XGL4 | MLRRTFFRLSLDNRENIIRIFTEMADLNNALGEKYKVQSYNRAVRSLKTHLDLPLRTVEDLEKFPGIGSKLLKKAEEIIRTGKLDELEKKTKPKLKAIQELTQIHGFGPRAAATLFDREGIFTVEDLIEKADQIQLTEQQRVGVRYFHDINEKIPMHESILHENFLRECALRRLGSDYEIQICGSYRRRHPFSGDIDAILARSLNAPPLDAPVTTTGVLTILVEYLQEQRYLEATMALGPLKYMGMGRLPPRTTGGATKTYKARRVDIRLIETKSVPTALLTFTGSKNFNVIMRQAAISKGYLLNEYGLFKVGTSDEVRVLQERVRARKAAGLSKSQMKQEDPYSSSSVTEEGAEPFVSSISGNSAKMETLGMTKEELEAKRVHVTCEKDVFDVLGMPYAKPENRDP | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 407
Sequence Mass (Da): 46102
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A0A286MU39 | DQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFIWAVLITAVLLLLSLPVLAAG | 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: Membrane
Sequence Length: 155
Sequence Mass (Da): 16503
Location Topology: Multi-pass membrane protein
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A0A7V0L327 | MVIYEKRILGIDFGRRRMGIAISDPMRIVAQGLETITYHSSKDLWDKLEAVLTRYEIEKIVVGIPLNLNGSESDISLLVKKFSELLTKRFKIPVEFWDERFTSKTAQETLIQMGKSPGRNKKKVDQIAAVLILQNYLDRHSNL | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 143
Sequence Mass (Da): 16479
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A0A7R8ZUA5 | MDSIKVFCPGSVANVSCGFDVLGIALDEPGDIMTVEKIKEPKVVIEHLDAFNLPTEPEMNVAGKAALAILEDLNPGFGFKITIDKKIHPGSGIGSSSASASGVVFAINQLMDQSIDEAQQMEYAMIGEYVASGSYHADNVAPALIGGIILIRGYKPLDYIKLPTPKELWMTVITPKIQIRTYDARRVLKRRVELKDAISQCGNLAGLIAGIYTEDYDLIGRSLKDVLIEPQRAALIQGFDELKASAIAHGALGSGISGSGPSVFAMSRGEDPARNVAAGFDKYYSLNGHPEKVSFRKAVIQSLAPDRGLYFPEEIPQLDAALLSNFRKMDKADVCTEAIAGFVGGDIPKEELKRIVSETINFPTPVVKVNDRIHTLELFHGPTLAFKDVGARFMARCLQYFLKDENRKTTILVATSGDTGGAVANGFLGVEGISVVILYPKGKVSPLQEKQLTALGQNIKALEVDGNFDDCQDLVKAAFIDPEINEKLGLTSANSINVARWLPQMFYYINALQQVPEDASVTFCVPSGNFGNICAGIMAQQLGFPIHHFVAATNVNDVVTRYLSGEEYQPKPTIPTLSNAMDVSSPSNFVRIEKIFGGREAMKKILSAYRFDDAQTQAQMKKTYAEDGYLLDPHGAVGLGYFLVSKKAPDSILLGGDKKEDSASIAVDGMSGVVGGLAGTQVLDKDDDDDDSENEGGSPLLNSFSDEDLENESDKPKDSTQNNNNTAGLAVAGAAAGVAAQNSPNQKEAKNTQSTKADSDGDGVPDSEDNCADVAGILENKGCPEVNLSADEKEAFNKAVGSVEFETASAQIKNSSLSKLDQVVSILKKHPEIKLSVFGHTDNTGDENKNLELSKARAESCINYIKTKGIAGDRLSAKGFGSSRPTADNSSEEGRKENRRVEFNLY | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
EC: 4.2.3.1
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Length: 906
Sequence Mass (Da): 97327
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A0A2K5E885 | MDRSRLSVTILLVLSIFIQSNARGQSLKPEPFGRRTRAVETNKTLHETKTRFLLFRETNRGCQIQINRLDRLQECGFNSSLPLVMIIHGWSVNGILENWIWQLVAALKSQPAQPVNVGLVDWITLAQNHYTIAVRNTRLVGKEVAALLRWLEESVQFSRSHVHLIGYSLGAHVSGFAGSSIGGTRKIGRITGLDPAGPLFEGSSPSDRLSPDDANFVDAIHTFTREYMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQAIKCSHERSVHLFIDSLLHAGTQSTAYLCRDMDSFSQGLCLSCKKGRCNTLGYHVRQEPRSQSKRLFLVTRAQSPFKVYHYNFKIHFINQSEKPIETTFTMSLLGTKEKMQKIPITLDKGIASNKTYSFLITLEVDIGELIMIKFKWESSAVWADVWNTVQTIIPWGTRPRHSGLLLKTIRVKAGETQQRMTFCSENTDDLQLHPTQEKIFVKCELKSKKSKQNIR | Catalytic Activity: 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+)
EC: 3.1.1.3
Subcellular Location: Secreted
Sequence Length: 499
Sequence Mass (Da): 56531
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A0A1S8D9I9 | MSGQFEPLATQGAPQGTAAGGTLAQERGTPGQAGTPGLGAVYDIPVQVSAVLGHATMQVSQLLKLGRGAVVELDRKLGEAVDIYVNNRLVARGEVVMVDDNRLGVTMTEIVKTDRS | Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular Location: Cell membrane
Sequence Length: 116
Sequence Mass (Da): 12045
Location Topology: Peripheral membrane protein
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A0A7R8W1G8 | MEQAAWRNSSHSSSVVQTQMATPPITNPPCHGVTGPISCAPPSPGDLELTDKLDLTLKKMGIYEEEEDLTRRMEVLDTMNTLVKKWVRDLCISKNMPENIADTVGGQIRTFGSYRLGVHSKGADIDTLCIAPRNVERSDFFTSFFELLKQTPGVTDIRKIEEAFVPVIKFKLQGIELDMTFARLAFKEIPDDFDLSDDNILKNLDAKCVRSLNGCRVTDEILRLVPNRESFRLALRAIRVWAKRQGIYSNVLGYLGGVSWSMLVARVCQLYPNACAATIVLKFFMVFSQWDWPHPVLLKAQENTNLGFPVWDPRVNVADRYHLMPIITPAYPQQNSTFNVSRSTRTVMTKAFKEGLEIAKVIFTNQCSWDQLFEPINFFAKYKHFIVLIVSSLTPEDQLEWHGMVESKIRHLIATLERNEHIELPHVNMYSYPPPDKNKEKTCSMWFIGLEFAKVENLNIDLTYDIQQFSRHVSQSSRMRDGMRMEAKYVKKRQLTDYLPDLVLPKTNRRTTSSSSLNASRTSSSSLSLPTSPPSQATMTPNGDVPPSSPLRSGGDAVMTDASENSCEVPDAASTVAASLVLNAANLSSPSRKRGQQDSEGDSGGSMNSSQSAMAGVPQDTVLKNSGSIEEETMEKEQESKRARFGSPARAAVPFSSNLPHSSSIDFSNKPPRVVASTVPTSEGSTVVSL | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 690
Sequence Mass (Da): 76838
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U5HIK7 | MFKCNCAVSTLPLSTRCSTAVASVASWTGTSSIAGSRYASTTRRHLAIDSWVQQRSTGFCPSRSNRAFVTETSGLWSLRRLAASPPHHRTFASTSHSSAASAQQSQAYADARKAHYQQRNRSLLLYSSATIVLVTTASYLAVPLYRVFCSATGYGGTPATDKSRFGAERLIPVVETERRIRVQFNADSSDSLPWTFTPQQKEVRVLPGETALAFYRAKNNSTEDIVGIATYNVTPNNIAPYFAKVECFCFEEQRILAGEEVDLPVFFFIDKDFLEDPLMRDVQEVTLSYTFFRARRDHFGNLVPAEAELSR | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 311
Sequence Mass (Da): 34636
Location Topology: Single-pass membrane protein
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A0A7R8W5S4 | MYNRKPFDLQRALISWNWFLAAISTFTAVKGLAFLLDEYYHQELSTMLCFMPINNVTCKAATIHGIMFALSKVVELGDTAFIVLRKKPLIFLHWYHHVTVLLSPKEVANVSSQFPKGAGHVTHHRHTLENDQFLKVPNFQAKGWLVCRNEKCPCVCLSVRDCILTNTDLLVTVSLYASYCILFIWFFYRAYLGEGKGVKRRRLADITMKNLMGSEDKHQKTS | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 25537
Location Topology: Multi-pass membrane protein
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A0A4S2JFZ1 | MGGISVAQLLIIGVICVLVFGTKKLRTVGSDLGYALKSFQKAMRDEPETTQATTVKNEETVQTQTRVENKID | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 72
Sequence Mass (Da): 7871
Location Topology: Single-pass membrane protein
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A0A7S4E9N8 | MARTKTPPPPPAHQMRQTTLFDALPRARPQQPQARRAHEPDALDQKLDLALSAVFGHQGFRPGQRATCRAAAQGRDCVVILPTGGGKSLCYQLPAVITRGVTIVVSPLLSLIEDQVSTLISLERCGGVPAAHLTSSTKETTSRAILRELHSAAEGRVDYPTLKLLYVTPERLALSENFRDVLEKLHRANLLARIVVDEAHCVSEWGHDFRPDYRKLGQLRSFLPGVPFMALTATATQACESDLRKSLKIKPTAHAHRTSADRPNLRFGVRDFSDCSPVNAAASFFLSHTSRVDGVWAPPDATPPKPSPRQERHTRRVALMASGPRTHPHTGTPSPLPPHAADAYNAQEDVRDAVVDFVRRRAGQCGIVYCMTQADAEACADHLTDKLKDVGTTAHHYHAGMTQLQRRVVQAAWQQGKLDVVCATIAYGMGIDKADVRYVVHASLAKSLEGYYQEAGRAGRDGRASECLMLYRDQDVGKVQKLLRGFGRKKRRGPKLQRDLDRLDDMARYCGMKDGCRRRQLVGHFGKDPGPSSGGGPCCDLCDARNPALRPPAPPPKPPAVRKRGPPVPQPRVRKAPEVVDLLGDSDDEVLASKRARA | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 598
Sequence Mass (Da): 65557
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A0A0N4VDQ3 | MIRFTTVFHFVVTVIYIIGAIEDVAVISGPALPIPGNYFSKIVWLTIIDLAVGTLFWGLYLTNRDFIVPKGFADPMEVHPYFNHILVRNFLKVLHTLPVVAMFLDRVFWDHGRTKRKKAIIAMLAFIIIYIHSCDTRNFWVLAVWYIKHAIYDPQNVVSFIWWYGACHVVFRR | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 173
Sequence Mass (Da): 20231
Location Topology: Multi-pass membrane protein
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A0A1B8J7B8 | MPYFKKSKSSDKGTLNPNHLAILGALFFAIFSISQAIGAESTQPRPNVSGKKANIDAKAIVNKLLEAKCRNGDMKLCDEIGNAYHDGYQVKKNYAKAMEFWQIGCKGKRFSSCNSIATLYFTGRGVQKDYVKAMEYYQKACNGGLAIGCYNLGIYYYKGYGVGKNIPKARFFFQKACDGMHANGCSAVGFFYDKGIGGTQQNPIKAREYYQQACELKSSPGCLRMGEIYLKGEGVRQNLKIAKEFFGKACDSGNQQGCDIYRKLQDQGY | Function: Hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
EC: 3.5.2.6
Subcellular Location: Secreted
Sequence Length: 269
Sequence Mass (Da): 29835
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B7X6S6 | MSRGNDPNPFDEEEPEVNPFSNGGSAPASKSRFPQMIASSLGFGQKHDATIDIPLDSTNGSNKKQKELANWEADLQRRERDIKRREDAVAGAGVPTDDRNWPPFFPIIHHDIANEIPAHSRKLQYLAFASWLGIVFCLAFNVLAVTICWIRGGGVKIFFLAIIYALMGCPLSYVLWYRPLYNAMRTDSALKFGWFFMFYLIHIGFCILAAIAPPIVFHGKSLTGILAAIDVFSDHVLVGIFYLIGFAFFCLEALLSLWVLQKVYMFFRGHK | Function: Probably involved in membrane trafficking.
Subcellular Location: Cell membrane
Sequence Length: 271
Sequence Mass (Da): 30529
Location Topology: Multi-pass membrane protein
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A0A380Y0J4 | MKPKKQLSTITPYHPGKTIEEVKRTYGLNHVVKLASNENPYGCSHYVQKSIMSELNKLSFYPDSRADRLREKLADSIGVNEDQFIFGNGTDELIRMICRAYLGSDTNTVMSDLTFSQYKRNAIIEGAEVREVPHVNGRHNIMGMIDATDKKTTVVWICNPNNPTGEYVRKNELITLLDELNKDILVVCDEAYYEYVDADDFPDTVSLMNKYPNLMILRTFSKAYGLAALRIGYGICKTEVINVLETVRETFNTSRLAQVAAVAAFEDQSFIKECHEKNRRELQQFYSFCWRFGLSYFPTQTNFIFIDMKRDTDSLANRLLSKGFIIRPGSEFACPTSVRITIGSSAQNDDLIAHLSQLLQMSEMIEK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 367
Sequence Mass (Da): 41883
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F7D8V3 | MKPSGEDQAAPAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHLVEDLIISELRERFPSHRFIAEEAAASGAKCVLTHNPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 288
Sequence Mass (Da): 31332
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A0A7R8WDM9 | MARLRVRTFLLYLMVGSLACTVILYLSTPSLLDGSDTGDAGSSMGQTQETLASLLDGSDTGDAGSSMGQTQETLASLLDGSDTGDAGSGASHRPDPPPQLPWFFEHGSVAWPSRSTDKLKVWPHEDPGDRIVAQLSLTSTKDAPIKRIKLDSKFRREVALDNFGFLKEKCPVDRCQFSKDDETADVVIFKDWVPDRPPGRSNQIWVLYMLESPFHTAHGKKNAVNWTATYRHDSDLVAPYDKWVYYDPRVKRKQVQKNYATGKTKKVAWFVSNCGAKNGRLEFAKELSKYIDVDIYGRCGKRMCSRWDPKCFNLLNSDYKFYLAFENSNCRDYITEKLFKNGLSHDILPIVIFSHDILPIVMGAHPEDYARATPVHSFIHVEDFAGPKELADYLHHLDRNDDLYNEYFEWKGTGEMINTAFWCRLCAMAHEPSVTKSYDVNEWWRGNGACRRGSWTNDKLAETTRWWKGWTKGLEPDDLKYDLKPDGGGRILKDPSGSSDSEGLASPLSTSNKGSDVERSGLGAERS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 527
Sequence Mass (Da): 59337
Location Topology: Single-pass type II membrane protein
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A0A3C0M764 | MSARADDNNKDTKSVPATPPKRVSAMEFIAQVRQETAKVTWPTRKETTTTSIAVLIMVVLAMVFFFTVDWVIGRVVAFVLNLV | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 83
Sequence Mass (Da): 9257
Location Topology: Single-pass membrane protein
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A0A2P4RD70 | MSRLIVVSNRVAPVAEGQGTAGGLAVGVFDALRETGGIWFGWSGETATTVSHEPNIVTKGNITYATVGLNRKDYDQYYRGFANATLWPIFHYRVDLSRYERQEYHGYRRVNAQFAHQLKALVQPDDILWVHDYHLIPFAAECRALGLTNRIGFFLHIPFPSPEILTTIPPHEDLMRALCAYDLVGFQTETDRVAFYDYIEREARGYIEQKEQNGPVHAYGHTLRAEVYPIGVHPDEIAQQAKASLARRNPFARHASVRGERIAPQGQGQGQQPTKLIMSVDRLDYSKGLPERFRAFEQLLDDFPDHRRHVTFIQIAPTSRQDVQSYQQIRQRLEAESGRINGKHSELDWTPIRYINKQYERRVLMALFRSSQIGYVTPLRDGMNLVAKEYVAAQDPEDPGVLVLSRFAGAARELDAALIVNPYDTRGMAEALNRALTMPLEERKARYAHMMDRLRAANLTIWRERFVADLRNASPQ | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor.
EC: 2.4.1.15
Catalytic Activity: D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP
Sequence Length: 476
Sequence Mass (Da): 54337
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A0A3C0MHW7 | MWVPLTPSWIRSLVWGITALRLLSIRPLIPALGFMAMTRLDLRLLLVSIAMALLAGASFARAQPAEAPFSPQSTTQTVTIGPDGTIQTAARQLLFMEYETGEVLYEKDGYTPMKPASMAKLMTTAVLFEKLKTQELGLDTLFTVSETAWRISVGQRAASSKMFLEVGKKVRLEDLLRGIIIQSGNDATLVAAEGVAGSEEAFAGLMNETAQKIGLKSSTFRNSSGLPHPEQWVTAHDLALLARHIISGYPQQYRYYAEREFKFAGIVQANRNPLLARFPGADGMKTGHTAESGYGLVGTAIRDGRRIIMVINGLTSEAERAAEASRLMEIAFNEFRSYALFSKGEQVGEAEVFAGLNSAVPLLINRDVRVTLRRDARAGLKAVIRYDGPLEAPVARGQAAGVLEISAPGMDTISVPLSTGKASARVGILDTVQLGLKDLLAGGTQVPSNTLP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Length: 452
Sequence Mass (Da): 48735
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A0A0N4V6A6 | MMESKLGDADSVIVTGSNLKNQAEKAAQKNPDQLDAYLFDITLLLAIQNEDGIPQLPAGYRARPLHSKDIDMNYFALLEQEEDSFHLDKKAFTEKWGIIIATVTLVIELKYIHALGTRGRVESLIVDSNHRGFGLERVLGTYAFKLARLLSVYKVTVGCSDNLIALFENCGFRKDIGNNVMSQHLDSFCKEEELAKCFRSEGVELFNASILQELDLSKMPELRQNLKVRPLRVDDWGRGYLNVLEQLTVVGAVLETDYRERFKSMQSSTLSRYFVVVIEDLDLKRLVASGTLYIDLHGNEAHGHFEDIVVSENYRGRKLGQYLCTCLLELARRVGIRRLTLEARDRVLEFYKKYGYRRVANLMSYKFCE | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 369
Sequence Mass (Da): 42200
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A0A0N4VK13 | MIYFCTLLALLCLNYEVILADSETLKALWNLEEMAICRLHYNALVYNNYGCWCGVGGSGEPVDGIDRCCMHHDECYDMAVNKKLCRNVPFEYIRDYSWQCVNGEPVCKENMNECQAALCKCDKTVVDCWGQFPKPAIKSSCEKRRKNKTFKGIKSVSTL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 159
Sequence Mass (Da): 18179
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U5H733 | MAPPKSRYRGSTSKGSTTHRHSTRGGGSSSTRSRTDRNVYGGVSGIEVPASAVDQEGNSEEDEGNDVDGLPREGKRLPVAMWDFDHCDPRKCSGKKLARLGLMKELRVGQKFQGVVMSPKGTQVVSPSDRDIVASSGVAVVECSWARLEEIPFHKIKSPHERLLPYMIAANPVNYGKPYKLTCLEAVAAALYICSFPTQAEELLSKFSWGHSFWEINGPIISRYQTCSTPESVLEMQEVIIEEMKKEEEERRREKERVEEEGDLLVLNPNHMRGAWRPHHSDEEEGSGEEDDGGGSEDGEDKVDTVTTAVGRTRLD | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
Catalytic Activity: N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-carboxypropyl]pseudouridine(1191) in yeast 18S rRNA + S-methyl-5'-thioadenosine
EC: 2.5.1.-
Subcellular Location: Cytoplasm
Sequence Length: 316
Sequence Mass (Da): 35033
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A0A0N4VNI9 | MTLLSLFTVFHAAFRLVPSPVGTTAQQIASRITVVWLVLYVSRSSFGVPLILIAWSITEVVRYSFYATKILDKTPEFLKWMRYSFFIVLYPVGALGEILIVLAALPEVAVKKQLTLEMPNSFNIGFSFWWFLVVFAAFYPFGFPPLYKYMFRQRNKVLCVEASKKRE | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 167
Sequence Mass (Da): 19269
Location Topology: Multi-pass membrane protein
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A0A7C6XC53 | MTMPPHGQPDEWIRVSIQVTPAAVEAAGELLRAAGCSGWENPAPDTVAGYFPADGRAEERIAALQEQVRALDQYGLDPGPALVTAQAVPARAWEEVWKEYFRPARIGRVIVAPTSEKVTLGEGEVVVRIDPGMAFGSGAHATTRLCLLALQQELRAGGRVLDLGTGSGILAIAASLLGASRVLAVDNDPEVVPIAQENAELNGKAAEITICEGDITTVEESGWDLVLANIAPGPVLQAAPRVAGMLAEGGVYVGAGIPAERADEVEAGLTSAGFRVERVLREAEWVAIVARPAGAAAAST | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 31163
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A0A0N4VMG5 | MKAKIKNLENFRNSKKKKLLTTQLLPTTMTLEDVNKHRSDIRSPPGSKRRFKRNGVSRAAKLWPNARIPYTISSQYTSHERALLARAVKEYHDKTCIKFVPRTSGEDDYLFIGKVDGCFSEVGRTSGVQVLSLDNGCLEYATIIHEMMHVVGFYHEHERWDRDDYIDIIWQNIDRAALDQFGKVDLSKTSYYGQPYDYKSILHYDSLAFSKNGYPTMLPKQKGYASTIGNAKDFSEIDLAKINRMYDCQNKQYGGIRFADCEDRITVCWWSQDRCHSPRLHNMMKALCAKTCNFC | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 295
Sequence Mass (Da): 34189
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A0A8T0H829 | MDLGEVTGMDLGEVTGMDLGEVTGMALGEVTGMALGEVTGMLRIEALSGFLRKGELLVKQLKTVDTPLMTCLLGGPPHTGKSTIAAKIAIDSGFSIETVSAETMVGLQESTKVSRIVEVFEDAYKSPFSIIILDDIERLIEYVPIGPRRFSNLILQTLLVLVKRNPPKGKKLLVIGTTSCERAIVEDMGFLKAFNVHFEVPTLKPTDMVEVLKQQNFFYSWDIDNAVEALGSEIPIKRLLKLMEMAILGKECNDADAIREGRQKIDIYHFYDCVRVFEP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 30802
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A9XIE9 | TLYFIFGIWAGMIGTSLSMIIRTELGMPGSLIKNDQIYNVMVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLNFLLLGSMVENGTGTGWTVYPPLASNIAHMGSSVDLSIFSLHMAGMSSIMGAINFITTFINMKSKNINFDQISLFAWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPTGGGDPILYQHLF | 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: 219
Sequence Mass (Da): 24006
Location Topology: Multi-pass membrane protein
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A0A5A8DFG6 | MATATAGPKPKLYFAGSIRGGREDAALYMRVIQGLAERGNEVLTEHVGKASLDMMGEGDLTEQQIFERDMAWLRSSDAVVAECTVPSLGVGYELGLAESLGIPVLVLFRPSAERSLSAMLRGNSKFTVHEYADVDGELFAAISAFLEVHGVPTA | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Catalytic Activity: a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase
EC: 3.2.2.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 16476
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A0A183VQL6 | MNQILSGILKFTKVGKDAYLKQLKGLGEKTKPLAAVISCVDSRVIPSKFLCSNIGELFIERNPGNFICFENSALSQFSEVCVTPGFIDFILFRCKINDIIICVLTNLVEFATKILFNNQLIYF | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 123
Sequence Mass (Da): 13805
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A0A0N4V648 | SFDRRSIFQFSKHDFDVSWDSSQEKKPVLETPVWLEAKEESRQEVIDLLGNKGEMKETIDDEDRYCDLNLLKEMLSAKSVFDELSDRALVEARSRANPYETIRCGFFQNRAAMKAANMDAVFNYLFTGEGENLLKKNPIDLNEDGTMKKGVNTDRSKPLFYFADVCAGPGGFSEYVLWRKGFYNAKGFGFTLKGKDDFKLERFTAASPNYFEPFYGELGTGDVTKPKNIESFEKVGFENCGVHLMMADGGFSVGGEENIQEIRSKRLYLCQFLVALSIVREGGVFFCKLFDVFTPFSIGLIYLMYIAFQRISLHKPNTSRPANSERYIICEKLRLTEAELVKKYFTWINNKLDKFNEEKKKNDVYEIFPAEVIDIEKMDVIFSFLKNQILYLNKYKVFAKDQGKIDLDQGKLRDECMEYWNLPKVDRRGKSRIDHRRIPMIPSLTRFIIPQKKPVFRILDAAVIDGDYVDSLSFDERMNAAKKMCSAVMVHEQTKNQCPIFAAEVRNYY | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.57
Subcellular Location: Nucleus
Sequence Length: 509
Sequence Mass (Da): 58926
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A0A8J5V4N1 | MGSSRRRVRSASCAMPMSASASSPAPTISMTAFPKTSSLKNLHRPPLVSTDPPRPLRFLGFHELYLYLLSLSLRLGSHGDIDLPYLDPLLQGPLATLPIQLRTHDGGGVRPRGPEVAPAVGVLRKAGARVQLVPGFVPFLWVPFYPLANIKNCETKDPLEGGGILAPLHAVAPPGTDLRLADAQKISIEKSKYLGVFGYEPHSVLPIGVAADLVGFMPLPKIKVLASSAVFYTPFLRLIWMWLGLIPATRKNFQSYLGAGYSYIIVPGGVQEILRMDHDSEVAFVESRKGFVKIATLLWFMVLEKLSLCVVSVGNKEIYSSCNKMSFSLEMKKCIFLNLYFYYINYFACVLADLSTREKFLLQKHKVTCQ | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 370
Sequence Mass (Da): 40862
Location Topology: Multi-pass membrane protein
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A8B4E2 | MDFPLSLLDANVSKAIFILLQGEPEQASLWSLILQLRTPGQGSSFASCASLIYKDLKGLSSWITEAAFIPFLRRLGFCSLYLSYGHDVLLELFKYPIVLTSTVSGKRVLLSEPQMPLAFPPCLHDKSVSSMVRASTVQYASNCLEEFISMIQEHPMNVRFIFFCKTRPYIRAFHSLALLGSATAIWHLSLLPSQCLTAFYQANPLVTFKFPYNAFSTRSFSSLLQLCTSRGRLMPNNAINSNAKARITRLISIFRSKMKRLSHNLTFLKDKKPQSLLQSFGFDTHFRVFLDETGTLRHAPLPLSVHKITLYLMLYCKSISAFSILGKRNARTFHSHLFRFISQPMNGFMTLQELTSSISTKEFLLPATTVSKAEGEVRHHLLAYFVVYLMDFVILPALYQSFSAVSMHTELSNRIETANSMVPALLSRSLWVSYKNYLIKSSARLEIAATYEFVCSLSNLHSIPLTNEDAVNRIFWKQVSPGRLSFVYKSNGRVRPLCNFSFCSRRHRVSLNSFLRSALQVIIFELERPRNRYLQAHLAKNLGHIAVDYAAWLDATYTENPEAQIYMVTTDMITAFESVSVPRLLYYISHYIVTGNAYVVLTYKEIAPSKMPKIRTVALPCQHNGCVSMDSISRYLLCKETPKKQPNSMLCPMHARIYKREDIIKMLELHLLNPLVIHEGGVYRLTSGIPQGSVVSTVLFNCYSSLLHVQLLNTGIVSSRLFFYRTFVDDWLLLTTSIALLDAYIEYLNIMRDHGAYFRLSCFTKPHKNSPFAPIATLDCSREPIPKKSLYTPNLNQDMYKLDVPRYCGYIFLENVAIIDVLKWFSSTRTNGSPSYPMIFGSGISVMQRLRLVFKKRIRDLRCFIERSIQAPDPRIKVDGSILYAYIRAVTFCILCYTRNIRYSESLRTLLRSTFCSLKATVWRHSTSRAIFIHVSKRIILHVYGHNPRIRGLLLGMLSR | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.49
Subcellular Location: Nucleus
Sequence Length: 960
Sequence Mass (Da): 109696
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A0A7S4A3H7 | MGRRDDHHQLEEGCELMLDWRKLHKVATCGDDVVPVAVQDADTREMLILAYANEHALAEARRRGVCVLWSTSRRKLWIKGETSGDVLDLVEIRVNCEQNSLLYLVKPRRTGACHTRGPDGRTRRSCFYRALEGDAWLVKRPSPKSVGYSPEAVFGAFLLGFLLSKAKAPRLPTWLFGAARN | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Length: 181
Sequence Mass (Da): 20434
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A0A0R3R815 | MLGIPFLDSAFLKIFSPTTYDDRIDRLNYFVTSSLLTFFAILVSAKQYVGSPIQCWVPMEFKGGWEQYTEDYCFIQNTYWVHFDDPVPEDVNDRHGAEIGYYQWVPIMLVLQALMFFIPEWIWKTLNKQSGLDLDTIVKGAKSLRSSKCNERKKELEKLASFVEECLEFDTPRHQKRFFCFNYGYSLGSYVTLLYLLMKSLFLINIFSQFIILNNFLGTSHSLWGFQVIF | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 230
Sequence Mass (Da): 27039
Location Topology: Multi-pass membrane protein
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A0A356U0N4 | MTSCWINVVGTGAWGTALACHFAKFGSVHLVARDEARAAEITHKHMSPRLPDITLPNQVQLGHHIQENILTCFALPFGHLEAYLEQGHDHDGLIIAAKGITANGKLAPQLLAQHNISNYCIMSGPSFAGDLAAGRPVALALASEPLDVASNLAARFHDKSMRIYPDDDPLGVSLGGAVKNVVALACGVARGAGLGDSAVAALAARGFAEIRRLGLAIGCRPETLMGLAGFGDLFLTASSLQSRNMQFGIALGQGCSTDEAAARVFGVVEGADTLTGLLALASQQEIELPIALGLAELLKGKFGVHDLIKALSARPMAMGS | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 320
Sequence Mass (Da): 33257
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A0A183WP34 | MLGSQFALAMRFVDHVYENQVVQDLTLKIVLPETVSDVQFVPPFPVREQYFENMKTYLDTTGRTVIVIKGANLVEEHIQDFKDEKSELRLRAQTLVDEAQALLSRRSSLYQSYEDILLKYKGSKNSTQFTADRRKLETDHKSVTQQLLSVQNKMADLYTDGVEKVS | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 166
Sequence Mass (Da): 19139
Location Topology: Single-pass type I membrane protein
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A0A1S8D371 | MTPGSLAWDATARLTAPFWRLHLRRRARRNKEIPARLQEREGGGAARPPGRLLWLHGASVGESLSILPLIEALARRDPALRFLVTTGTVTSAELLMRRLPETLRPRLQHRFVPLDVPDWADRFLQGWRPDAGVFVESEIWPNLLAATRRARIPMLLVNARLSERSARGWRWAPGLAREAFSTFRLVLAQSEADAARLRAAGAGEVRVAGNLKYAASPLPADAAELARLRRLVGDRPVLFAASTHAGEEGILALTHERLARRLPGLLTVIAPRHPERGAELAASLPGAVRRGAGGEPGPETGLYLVDTLGELGLFYRLAGAAVIGKSLLAPGGGQNPLEPARLGCPILLGPHMGNFADVTARLLAAGGAVQLPPAPAADPAMLADAAHGVLTDTRRADLLRQGAARVAEGASGLAEDVARTIAELLPQPPTPGTPRECQEERT | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 442
Sequence Mass (Da): 47315
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A0A2A4LPS8 | MSNKTPRNILKINSSARYEGSISRGIVDELIEKLTSNNENIPVVDRDVIKGIEFIDETWVSGNFTQKEARSEIQINKLSYSDALVEEIITADTLVIGVPIYNFGIPAPLKAWFDQIARSNLTFKFIDTGPVGLMTGKKAYVVITSGGTQSNSEVDYATGYMKQVLEFIGIEDVEFIIADQLLAGEEAKLKAVHEQIAAL | Cofactor: Binds 1 FMN per subunit.
Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
EC: 1.6.5.-
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Length: 199
Sequence Mass (Da): 21961
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A0A356U0L1 | MEQFATREFMLRALSALVMVPLAVSSLYVGGALFHGLILALACVMALEWSSVTSISQRGPMAPLVFVVALTVAVSVSDMQLGLLLWPFGALFLWILAQNQRRCVHVMGFAYITIPVLALIILRQEPEHGFSLLLILMVVVWCADTFAYLGGRIIGGPKLWPSISPSKTWAGAITGFAGGLLGGNILCAIGFEVQSCLLVSAVLALASIMGDLMESFFKRFYGQKDSSNFIPGHGGLLDRVDGIVVAAPVLWVLVFLGVAI | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 260
Sequence Mass (Da): 27870
Location Topology: Multi-pass membrane protein
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A0A0R3R501 | MLTVESWQTLFDPVFCRMRTSTPREYNDALMRSENIERNLPKHSTVTTVTRSGDHLWIPYRLYSFDNIWIARSARFLVTPSFFNLLHRILYTYVEHQQLNEAIFQTTVYFLTLMVKFVTSKQFSCFAEEKSKLPSSVQEILSGQRNPVSAILSVFTDFADFGGRQMPSVITLLLEYLRKMNNENAISAEHDHFMAHCISKQLSLVPVSLDFISGYAIDYIGRLFCLLHHNCEKIRDVLDKFIAEHQVEMLKSDKLEKKHCGDSPSKLAHRSAAKRRQEALMIAHKKKNAILMKKLMAKEGLTQTQMDAMDTTENSPVRYYRCPICNDTTASTLADPIGLMSRIVVNYGWFSFNCTVTFSLKVAVEHSLPEDCPSLSLMEIGEKGVHTNRMMLKIFSASRRSLLQTRFPKYADLIQAPTGIEVRTCGHYAHVGCYKAYVQTLLESPPPSLDPLEARMEISCPLCRAPVHTLLPLAPDTGVERIRFV | 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: 485
Sequence Mass (Da): 55396
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A0A3D1G625 | MRLNIAAIGNGRNAAEQSLALDWLNRLPFRGQLNEFTSRKPAGPARCLDESTRILSSLPDGALLIALDPGGKDTSSEAMAALIRRYRDDGRRDAVFAIGGADGHHPDLIARADHVIAFGRQTWPHMLFRAMLAEQLYRAEMILAGHPYHHA | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 16635
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A0A0D4BRU4 | DGLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKARRALRLEDLRIPPAYAKTFLGPPHGIQVERDKLNKYGRPLLGCTIKPNLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 157
Sequence Mass (Da): 17881
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A0A061HH50 | MIVSGTWAAAPLPSMIKNQRGYCKIDGASQTLRNLAFSQILLAFLTLTTAHVQIINRISSSHPVWIWFTAACLQDGKGKLHKYIIRFIVIYGLVQAGLYSSFLPPA | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 106
Sequence Mass (Da): 11721
Location Topology: Multi-pass membrane protein
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A0A7S4ECU6 | MDDLGAMNYSLTLLEQEECESVCARFLIDDFSTVPAAQLAQMRREGLLDEENRPRLMREKHVQYLRKGLAGLSGGFVALDASRPWLVYWIIHALDLLEALDDDAEIKQRCISTLRACRAEGAFGGGPRQLAHLAPTYAATLALCCIGSNEAFETIDRPALYQFLLSMKDASNGFRMHDDGEVDVRGTYTAIAVAALTNVLTPQLVEGVAEYAASCQTYEGGFGGEPGVEAHGGYGFCAIATLCILDACHLVDLDALDAWVARRQTSIEGGYQGRANKLVDACYSFWQGGTAQLSAHARRGDPHHIEAPQGVRWRPGTTSADVPAATPIQEIVDPIKLQRYILLCAQVFPDGGLRDKPGKGRDYYHTCYALSGLSASQHPDCTAPATVSGSPANLLPRTHPAFNCRPEKVSRMLDHFSGLPDL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
EC: 2.5.1.58
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]
Sequence Length: 422
Sequence Mass (Da): 45872
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A0A2A5GX16 | MMLWVEKFVKQWKGMEFRKMKNKIITGFLVVTISLMALPSYASDLGFVLNLFGAKGSVSIDIIPKRKYVERRRYYYVEQPRYRQYETNYNRMYNHVNWCYDNYKSFDEGTNTWQPYYGSRKFCRSPFIR | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 15757
Location Topology: Single-pass membrane protein
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A0A183W9Y0 | MFIGFLCRCFDDVRVFPNLSDRNAVEICPDMLCLTQVLCKRISQTGGAALLIDYGHEGEKGDTFRVSF | Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subcellular Location: Mitochondrion
Sequence Length: 68
Sequence Mass (Da): 7634
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A0A5A8C1W3 | MASFDDNTSVERRRGNAPRAKFSEERELKADPVWLKRERVQPILRDFCSHLMMPWQRCRAETRFASWKCGVEKHAWEECMEHEFARAMRQKLQGKL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Membrane
Sequence Length: 96
Sequence Mass (Da): 11553
Location Topology: Peripheral membrane protein
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A0A158Q9Y8 | MLRDVCVDPDYNRFCRITFLKAAFRKQLQKKRCPICKEMVAFGIYQRHVNSCVSDPDDEECRVSFFLFLAQFFGYFCYHIVRILGDEFDFELEEALRLLQAPCLKNVAKKFKINFSSSKEEITIKLISMSKQKNIFGSPINSYFSIKEEMGHCYRLREDVEKFFNCVFTLFSPSDMNSALLIDDPNTNLASQLLFLLLEVRLEKIHFKLMLLNTRGSLWDRLALNLDSHLRDKADAFEVIQTGIADPDIGDKDRLLLQVSFLCEIDVLLAYNDGANFLVQRKNLGDQRTNHFVTQRNGESYHCPVEQVALNYYISEEGYKEGVHAEGGVWHFFYGLLCYDIIFDHDVGDVWFSETQCHPSDLNTRSFYTTRRARFEERFKKIERTKVEELINLVIPVYEEHFGETNSEISWECFTNLDQIKVRFLQCCPPRVLAAVFRRITTDYRNCRSGFPDLTLWNHLTKKLLVAEVKGPGDKLSTKQILWLQYFRKHRVEAHVCHVAGRPISF | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
EC: 3.1.4.1
Subcellular Location: Nucleus
Sequence Length: 506
Sequence Mass (Da): 59191
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A0A061HI17 | MNEKERPTKRLRCSNSTGSDKVPKDEKGHAKKLDLYGLERASGDEGELDDDEPSANHRTTDLENALPTIPTDVETIRHYEALRGDESFPEELKRLRDSETWVKGESSIYVDAFNLALKTVLEEEHHLFTAQELEVFACWRSLDFGAQYLSTALWHRVRALRYGEDISNLPSAIESLQRFQTLSQVSEKPSSSKAGLPDLEELDLDGGFTWADSSTTAITTMEEAASLLSLDELKLVSREAKVSGRNKAELLRALAKMSKSQSALCWRDSKELESKSPHSPKFNKSNGLATEGLEVTPEQYFYQKIMTILGPCIRLSQPILRLFERVHLVFYRSTEWTDKSLTTVILARISRQRFPRYIVCRTANVFSSRSDLLEYESALKQQYRLVQILEKNGRLSDSEQEESLTILEQVYPRWRRLVEVEEKREASIIEGERGAYLRRFSPAWVYTRIIHKILSVLGRRKDYDREYSIITELLEQTLFHTARRGVWYQRKALLEEHYLFKIRPASGISDINSLKKYWKRMALQT | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
EC: 3.1.4.1
Subcellular Location: Nucleus
Sequence Length: 525
Sequence Mass (Da): 60659
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A0A6B0WIF1 | MRQILDPAGELVGPAPDLDDTQLVEMFRLLLTTRMADEKLLNLQRQGRMPAYYQVSGQEAHVGAALALRESDWLFTAYRELGMWLARGMSPLATVGLWMGVPDDDDLWDVNRYRVTRLNATIGTHLPHAVGFGYAERLQERDTVAMVVFGDGATSESDFHAAMNFAGVWKTPTVFLCQNNQVAQSTTIDKQTAAATLAAKADGYGFCGERVDGMDPLAMYQAAREAVERAASGGGPTLIEMLTYRFAPHSTYDGTPVYRTTDEESQWRQRDPITRMRAFLVNKGLWETGQEDDMRAGISANLEAFVDQLEARAPVSRHYSPRQLFARAPASLAEQLHREQQDAGEAPAALEPDEVWAVAEDPSPTGETRRLDMTEALKLTLHAAFERDQSLVTLGEDVGVEGGVFRITEGMHERFGADRVIDTPLCETGIMGTAVGMAMAGLRPVAEIEFAGFVYPAFDQLIGHVARIRWRYRGHLTAPVVARLPVGTNLDNHEFHTDSPESLFTHAPGLVVVYPSNPYDAKGLMESALASDDPVVFLEPISLYRGLKQDVP | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 552
Sequence Mass (Da): 60873
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A0A7S4A7T4 | MYCAISGEVPQQPVVSRKTGHLFERRLIEKALQASENRCPVTGEELKPEDLLPVACDLAQRPRPLSATSLPAMLAMFQNEWDDLVVESHATRKQLHATRRELSHALYQHDAACRVIARLTKERDDALALARSGQGVVVTQQVDQAALEQAYACLQDYWKATSKTRKKRKAPAQLASASQIKTWSPQKPAKVLGSASGLAHDVKSGSTLVWGPQGIAYCSSAKKPLVVDKPTSGACFLPQGLLTCGDNITIYSSSMEEQGTIQGTYQSVDAHNTGKYAVALKATGAWSLISLEAKTVLAESSVDPGDAATSSIKFHPDGMIVAAAISTNGAHRVKVWEVKDQKPVHAFDGHSAPISSVAFSENGYHLASCDEGGTVKLWDLRKLKELKSFQVDGAGASVAFDSSGKYLVVSTTTNVVVREVKPWSDLVSVETSSIGACFLTDAQGVVAVDGGGGLVSIGK | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
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.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 459
Sequence Mass (Da): 49001
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A0A0N4V071 | MFSVLVMVVVYQKNPMHTLEVSVFLFFLFYSMGSVSIELYWDHAPKTCRNFAELARRGYYNNTIFHRIIAGFMVQGGDPTGTGRGGASIYGDVFPDEIDDRLKHTGAGVISMANAGPNTNGSQFFITLAPAQHLDGKHTIFGRVAAGMKVVQRMGMVDTDNSDRPKSEVRLIRATPRDDSRI | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 182
Sequence Mass (Da): 20196
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A0A7S3A887 | MEVQEAVYRMEPPGVKLFEALHKMVVGIVRGVQEAENPGKAFETFWSKNGLEPVMMWMKEQRQKRHLNEITPPESFVDVDVGTGHLIADSGLSLQDDDVKLAIVTTASLPWMTGTAVNPLLRAAYLSRLKKQVTLLVPWLSPSDQKEVHPDGKVFESPKEQEAYVRSWLKNRVGFESDFKLRFYPGYYEREKGSIFAFGDITEYVPDGEAQVAVLEEPEHLNWYHVGRRWCDKFNHVVGIVHTNYLEYVRREEGQFKSNMLKLFNDWVVRAAGVHTVVKLSDAVQEFKNSENITCFVHGVSPKFLEVGRMVSERFSELESVKATFVSCITSSETSRESLAAEPSPLDENAFPGFDKGCYFLGKVLWGKGYSELLNLMQSCGRNVDVDVFGGGPDLQEVENEAERRHLRLHFRGAKDHGDVDFHRYKVFINPSMSDVVATTTAEALAMGKFVICADHPSNAFFRQFRNCLVYRNAAEFSNCLTKALSEEPAPLLPQELRDLSWEAATERFLLVAEPQREQQDRQMPKMLDDITAKAIWHTHQGLQHFEAYRVAIGAPPGTSSRMPDLNDVKRFEMRPAPRGPVFPDSSRDRLMFNLSSKVAKVSTSNGRPRDGKCTGTCAAETGSDSSAAAAAARKTLRLKMEDLPRSAVLLR | Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+) + UDP
EC: 2.4.1.241
Subcellular Location: Plastid
Sequence Length: 652
Sequence Mass (Da): 73523
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A0A086ZRN2 | MLEHCRGLWKKLIEPIAKACVSMHLSANAITVTGSILAIGLSILIGVTGNIIPLVFLLALVVMFDSLDGSVAMLTNGGTKFGAFLDSTLDRIADWAVLIGCILIFYLHHGWWTKNALRGDMVSEVGIACALVGIMTSFVTSYARARAESVGYEAKNGIATRADRLCIILVGMLITGLTHQGVWLAVAMVLLAVLGLITVFQRIFEVRRQMRGNTVPVGDANAPEHDTVR | Cofactor: Contains a di-nuclear catalytic Mg(2+) center.
Pathway: Lipid metabolism.
Function: Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation.
EC: 2.7.8.-
Subcellular Location: Cell membrane
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + 1D-myo-inositol 3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H(+)
Sequence Length: 229
Sequence Mass (Da): 24663
Location Topology: Multi-pass membrane protein
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M7YHH2 | MAAATAMVIMLAALAILAPSARGLDRAEFPPGFLFGAATSSYQIEGAYLEDGKGLSNWDVFTHTQSREINDGRNGDVADDHYHRYMEDVEIMHDLGVNSYRFSISWARLLPRGRLGGVNTAAIAFYDRLIAALLEKGIEPFVTLHHFDLPHELETRYGGWLGAGIREEFDYYADVCFKAFGDRVKFWTTLNEPNLFTKFAYMLGMYPPKHCSPPFGTCNSGNSRREPYVAAHNMILSHAAAVDNYKRNYQATQGGSIGIVIAMKWYEPLTNSTKDILAARRALSFEVDWFLDPIFFGDYPREMREMLSSNLPKFTSEEKRLLQSKADFIGVNHYTAIYAKDCISSPCDIKTYEGNAMVQAVGERDGVAIGRPTAFHGYYDVPEGMELIVKYVNQRYENTPVYITENGYSQLSDNSMEELINDVGRVNYLQGYLTCISSAVRKGANVHGYFVWSLMDNFEWGFGFTVRFGIYHVDFETQERTPKMSGKWYRDFLTGSRPVDQAQTLRADS | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 509
Sequence Mass (Da): 57580
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A0A0R3RC17 | MLCEVLHIFQEQVIERLLKFQDVIVQAPTGSGKTLAYILPLFTILWKKKXXXXXXXXXXXXXXXFFDVWPENEIGAVVIVPSRELAKQVGAICKLFADALSFSMRVMIGGKKGKSNSKADQCLSAAVIIATPGRLQSLISSNSDFKKALKALEVLIIDEADRYTDSSFKAGMTEILESLPKQRRTGLFSATQAKEMEEIVKFGLRNPTQITITNCGAMLDSVDSVEAISPNTL | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 233
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): 25656
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A0A1A7ZN69 | MSPSLRGCVGIVAMQVIRAVSFRCRRYEQSEWGWKEREKREEMNDERAWYLLARDADSTPVAFSHFRFDVECGEEVLYCYEVQLESKVRRKGLGKFLIQILQLIANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDETSPSMSGCCGDDCSYEILSRRTKHGEASAGHTHGGSHCGGCCH | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 181
Sequence Mass (Da): 20743
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A0A3C0M866 | MRNIFGELPETLPFWHPAVLIATWFGAGLLPIGPGTWGSAAALPFGWALMVLGGPMLLAVAIAVVFAAGWWAADVFVRELKADDPPEVVVDEVVAQWLVLTITPLTIEGYLSAFLLFRFFDTFKIWPASWIDEQVSGAAGVMLDDFVAGLFAFAGMAAVLYVQSL | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
EC: 3.1.3.27
Subcellular Location: Cell inner membrane
Sequence Length: 165
Sequence Mass (Da): 17832
Location Topology: Multi-pass membrane protein
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A0A183WVD2 | MVIGFNVSNFKVSISNIVFHAGLISIFYLYFVYWCRLDMFTTLGYLSILGIPTFLAGNSVLRAQVIAKQTAGAGGSSSTSAAATNLHTANVKK | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 93
Sequence Mass (Da): 9968
Location Topology: Multi-pass membrane protein
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A0A061HMW2 | MRVWDIARVAQKNTAMISDRGNGNPIDSGKAAPVKIVRRSTRTSSGEPVKYFVQTRKIGQFFKPESSESGSKRCRSPDLAQDDDSTVPERDLKRLRISSTAKETVSGGGTAPTSTQVGPLTPALVDRTGDGSEATPTAVNDEDADDTGTSELSIVYRDRQKTFIATKPHGRSISEETTALELLQGIRDSILAHQSLFKEARILHRDVSINNIILTDPAVNNGRYGLLIDLDLAISLNDVNRDRDVQNTTGAMEYIALGILEDIIFETGKGYLHTYRHDLESFFYVLVSACIRFGWGDKKSGRPYILASWYTGTVKQMYDAKYGAMGSKFFQNLILNHFSARSTGVDTSTNPFADEVYDLILKAFDDEIKGIKLSAGDEAVPDLKERMPLTPRADTETLSAEG | 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: 402
Sequence Mass (Da): 44258
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A0A0R3Q890 | MSASTIIDVHTHVVPEEFPPYIGHRLGARWPSMAPAHACHQHVMLNGRVYRTVSHQCWDCAVRLADMEAMQVGRQVLSPMPELLSYWLDGDDAQVLARYLNEQIAAMVQRAPERFSGLGTVPLQDVDRAIAELDHAVHGLGLAGVEIGSNIDGVALGDARLLPFFQAAERWGVAVFVHALRPAGMERLVGPPILEQVLAFPGEVGLAAASLLTGGTLQACPRLRIAFSHGGGTLAMLLPRLQFGWETFPALRERMAVPPVEAARFIYVDDLVYDATAIEHLVRTFGATQVMVGSDYPFAIMDRHPAERLGALPFDGPTRRRLSQENAEHWLGLRAARTEG | Pathway: Secondary metabolite metabolism; quinolate metabolism.
Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
EC: 4.1.1.45
Catalytic Activity: 2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-aminomuconate 6-semialdehyde + CO2
Sequence Length: 340
Sequence Mass (Da): 37225
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A0A0R3RAS3 | MDRYERNHDIACYCMLQVHGKIAILSVFIHIVLLYSIFDIYYSSPLVTGLHPYPITNGKGLADRLVIFSADGLRADAFFNHPEKSPFLHEIINSGKSCWGVSVSHVPTESRPGHVAMLAGFFEDVSAVARGWKHNPVPFDSIINRSREAFAFGSPDIVLMFTNDVSHATAMVYSSKLEDFQQNDAAQLDRWVFREIEVNRLVFFLHLLGLDTNGHGYKPQSDKYIDNIAVVDAGIARVVQLLNNYFADNRFVSLKNFVDSLGQ | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
EC: 2.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 263
Sequence Mass (Da): 29614
Location Topology: Multi-pass membrane protein
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A0A950QBC7 | MNYRHAYHAGNFADVHKHVALVAIIQHIKKKDQPFAVVDAHAGRGLYDLAGTEASKTGEALDGIGLLRDHQPQSPAVAEYLTVAQAFGSNRYPGSPLIAASLLRKQDRLIAIENQPGEFSSLRQALAFYPNARAIEGDTALKLRGLLPPKERRGLILIDPPYEISQELEQISGIVGDALRRFATGIFVIWHPLKFTQPIATLCGELGHAGAARALHLAFDRGRQESDSERALSAAGLLVINPPFGFERTFGEAAQELLTVLRRGPGADARATWMRKD | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 277
Sequence Mass (Da): 30225
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L2FHA3 | MKYSVALTLTTMVVGIAAAPAAQAAPKEHNLARAEHGYFDLIHKLARAEKANPSKTKSAKKPKKTHATKTRSPGSIITSAPGNGTASFAIAAASNGTSGGNIPAASGTSVLKAAQTIAAGESFDGGMKMFDRGVSCTGQAEGGDSDSVFILEKGASLSNVIIGPNQIEGVHCNGGCTLTNVWWSAVCEDAFTIKKQDAGETTKITGGGATGAEDKVLQHNGAGTLSVSGFTVSDFGKLYRSCGNCKTMYERHVIFDDINASSGKLLAGINSNYGDTATFTNVVAKSVSEVCTEFKGNDSGDEPTEISSGPSTACKYSTSDVTSS | Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
EC: 4.2.2.2
Subcellular Location: Secreted
Sequence Length: 324
Sequence Mass (Da): 33199
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A0A1E7REM8 | MFIEVALQQMPEKLQQLCQILQRASELLEQEYQDYIAGAAFEIQQKADQSPVTQADLKCNAMIQSQLQHITPQLPILSEEGEHQLRHQWSQFWMLDPLDGTKEFLHQTGEFTINLSLIDQGESVISALAVPLQHKIYITQKDLLPFRWQWHQEKKVIVTQYQRQFRYQETLRIAMSRRPERSPIYAEFLTFLEQHHINYQKIMAGSAYKFCMMLEDQIDIYPRFHPTCEWDTAAGQGLLKSIGGEVYSLKHQPFYYNQRKQLLNGNFIALRYADDWQKISQFIALLSRNN | 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: 290
Sequence Mass (Da): 34200
Location Topology: Peripheral membrane protein
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L2FN25 | MMPRRRSRYVLLVAFVMAFMLYQVFKNPEWDATSYTGSIKPNEPAKGKTEPAKQPPVNEPPANKPLNNNPPPDSEHPHDQEEDEPEQNPMRQTAKQTVVKIPQLKTETPKKGIPTKSANTPTMPVYNPDNEPEVTKAAKIPVEDEFHAKKPPGRPNADNAESSASTTTSQIHWHKVKEHFPVPTDKIIPLPTGKPKDIPRIQYKFEPETTAVKEKRERRLAQIKAEMVRSWGGYRKYAWMHDELSPVSARYRDPFCGWAATLVDGLDTLWIMGMKEEFDEAAKAVKDIDFTFSPTRRDIPVFETIIRYLGGLLAAYDVSGGKKGGYDVLLDKAVELAEILMGVFDTPNRMPILYYNWQPQYASQPHRAGNVGVAELGSMTMEFTRLAQLTGESKYYDAIARITDAFEDLQNRGTTLNGIFPEQLDASGCNRTAEAIRYQEEQAAAAAASAAAVAAHMKEPEGHKPAVDEKRDEPVAPRETGLSKRAVRVTEDGESVVKNANVDKEEAFPKPIVNEQPLYPGNSGRRPSPTSPEEKSEWECIPQGLAPGGWGYEQYSMGGSQDSTYEYFPKEYLMLGGLEPKYKTMHEKTVAAVKKWLLYRPMVPKERDILFSAKVSTAGDPEYDARVEYEVTHLTCFIGGMFGLGSKIFDRPEDLEIAKKLTDGCVWAYESMPSGIMPEGASVVPCASLESCPWNETLWWEHLDPSAAWRDAQVKEWEERQKEKKNEELRRAAAVDRLSVDKAMPPPAEEKKVDPLADVKVPKDQPKKVNDVKKTEWPAPEPGLNKSPSNVDEHLLKKRAPPASEDPRKGTSEEKASNSLKDKLNINSDASDSGTVSNDAPVSGGIVGTIPVYEEEIPDPKPKSHKEYVKIMLDEEKIPPGFVNINSRRYILRPEAIESVWYMYRITGDPIWQEKGWNMWQAIIKATRTEHGASAVDNILSSSPEPVDEMESFWVAETLKYFYLLYSEPDLISLDDYVLNTEAHPFKRPV | Pathway: Protein modification; protein glycosylation.
EC: 3.2.1.-
Catalytic Activity: 3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Sequence Length: 990
Sequence Mass (Da): 111250
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E5LG28 | ASLFFICMFMHIGRGMYYGSYKSIKTWIMGVMIMLTVMATAFLGYVLPWGQMSFWGATVITNLLSAIPYLGESMVKWIWGGFAVDNATLTRFFTLHFLMPLIVLVMSSLHIFFLHKKGSNNPLGISSNIDKIPFHPYFSIKDLMGFTIAMMMFLILNLMEPYILGDPDNFIPANPLVTPAHIKPEWYFLFAYAILRSIPNKLGGVIALIMSILILLTLPFS | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 25013
Location Topology: Multi-pass membrane protein
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U5KT30 | TLYFIFGMWSGMVGSAMSLIIRIELGQPGSFIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRLNNMSFWLLPPSLTLLLMSSMAESGAGTGWTVYPPLSSNISHSGASVDLAIFSLHLAGVSSILGAVNFISTIMNMRPTGMTPERIPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLF | 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: 219
Sequence Mass (Da): 23672
Location Topology: Multi-pass membrane protein
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A0A5N3UNF3 | MLVHLWGPRKIISFLGCSVQLFIFLFLGTTECVLLTVMAFDRYVAVCQPLHYATIIHPRLCRQLAAVAWVMGLVQSAVQTPPTLRLPFCPHRQIDDFVCEVPSLIQLSCGDTTYNEIQLAVSSVIFLVMPLTLILISYGAVARAVLRINSAVAWRKALGTCSYHLIVVTLFYSLVIAVYLQPKNPYAQKRGKFFGLFYAVGTPLLNPLIYTLRNKEVKRALRRLLGKDRDSRKN | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 234
Sequence Mass (Da): 26402
Location Topology: Multi-pass membrane protein
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L2FV06 | MDTMEPEQTPFSSVTTHTSKIQRQYQALLDQSTPFVLYRWVGTGVCLLVFFARVFVAQGWYIVAYALGIYLLNLFLAFLQPKFDPSNEALDNEMEDGGVGILPTKQDEEFKPFIRRLPEFKFWYWATRAILIAFFCSWWEIFNVPVFWPVLVMYWFILFFLTMRKQIQHMIKYRYVPFTFGKKNYAAKNNS | Function: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 22731
Location Topology: Multi-pass membrane protein
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A0A077TJD9 | MVMFLFLFMLACLKINMSYGSMYSIILPTYNEKNNVPYIIYMIIEELSKHNINYEVILVDDNSKDGTADAYKKLQSIFSNEKLLLLEREKKSGLGSAYMDALKLVSGDYVIIMDADLSHHPKYIYEFIKKQKETNCDIVTGSRYNKQGGIFGWGFKRILISRVANFLTQFLLFINLTDLTGSFRLYKTDVLKEVIQKVQGKGYSFQMEVIVRAHKSGKTIEEVGYIFYDRLFGESKLSSNEIIKYLFSLLHLFWTL | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Catalytic Activity: a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP
EC: 2.4.1.83
Subcellular Location: Endoplasmic reticulum
Sequence Length: 256
Sequence Mass (Da): 29710
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A0A183VWD1 | MGINRALVTNQLTNTTESPSLPYRTEMQKQLRSGQVSEFENSFLWRASVVLMAKEKNDGDFTSTQSTAGHSLGSTSEVNTRPYCSNIIGTSAANQSSHRSGRFGTYFNSNQQNHLSNLGRLQRHMAVIPRPPQNFQPNTQKRRTDNFNEFYTPSSIDSFNNDPFWSTVVRLLLSHANLKQELEIEFDGEEGTGLGPTMEFYALLSAELRRYSHGLWVTDDRDTINETKKLSSISHEDSINHNENPQDDSLEDKSQNDFYDERQMDLPFSNAFLCLLCNNGKASELNNLINDSKSDEDGSRTRSNWFYNTLDIKHFTEIYPERGKFILQLKKYQYMKSELWHKYNGDELIQKDLELQTRLFATDLESLCLTMSFPSVSKVSKLLQ | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 384
Sequence Mass (Da): 44088
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A0A7S4A4D2 | MTGRAAPTPDASPRDVAVDDEQQTPRHGLVYRVGSKRKDEDRAVAGEHVTCGGERFAYFAIFDGHGGKDAADRCQATLHDQISRRAPDTTKATDALSEGLRRACWELDEDLGSAHVDAGTTATILCIGRSTATLGWVGDSTALVVDMTSPKPAWATPKHNPQNPSEVARMKAEWGARREFLLYESPDGEDQAYNEAMDAFTTTYEKRLADHFRAQNLPPLRPNLIRDSMRRETLINDRCDRVNTMRRKQSFEAVTKFGKVVSGQDMDATIDMKRHDSNFTRRTSPEDGRPRGPVVVGANWRGRRPGTTVGGASTCVTRSIGDWDASRAVIPEPETKTWDTSSVFDRVVLASDGLWDLVSFDAAATCMRSVDDPQKAAHLLLKRAKSESARRGYSGLKDDTTILVVDINPNALKVTETAQGCACVVS | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 426
Sequence Mass (Da): 46739
Location Topology: Peripheral membrane protein
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A0A0R3QP58 | MGINVQSLTQMACDARMMDADARAATVQTIAGHMEDALEIQREVTDVSGMCVSKRWGSYVTCLYVFIKTLYLINVVGQIFLLNTFLGTDNIFYGFHILKDLLNGREWEVSGNFPRVTMCDFEVRVLGNVHHHTVQCVLMINMFNEKIFLFLWFWYFMVSIVSMFSVGHWMLMSFLPGQHMKFIRKYLKATDLATDRQSVKKFVHKFLGYDGVFCMRMISAHAGDIMATELIVALWHNFNDRVRKSPIEMFEGGVTQSPSKLDANFKTWLLGQTRNKPPFDGSNPTRSKKRRKSDGYFTFV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 300
Sequence Mass (Da): 34604
Location Topology: Multi-pass membrane protein
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A0A023HCH2 | MNNIFERIRLILNKQFRFSLNQIQPETEFENELGIDSREFFELINEFESAFNIEINAEEVATLVTIQDAINYIETKIIS | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Location: Plastid
Sequence Length: 79
Sequence Mass (Da): 9359
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A0A0N4UT49 | MTSPIDSLDGLWGWDANFVGKELCGRDLKHYSGNKGVPQTLVCHDMMGGYLPEESVDGCEVVDGIKPYILMHWWYVDIFTYFSHHFISIPPVGWISQAHDHGVLVLGTFITEGDRGADRCKAIFKNATTVRKTVEKMVKLATVYNFDGWLINIENKIEAENLPMLELFLATLTTRMHIRMGERSRVIWYDAVTVEGKLRWQDQLNDLNKLWFDVTDGIFLNYTWRPHELKESQEIAGSRCHEVFVGVDCFGRGNYGWNCYKAFAHARAANLSVAMFAPGWIAEQFQQSDLIPNSMNYEIKILELGKIMHSSYITLNQIPESLNKFFQFYNMLEAGTQPYYLESNAFPHASRPALVLPDTGNYK | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Subcellular Location: Cytoplasm
Sequence Length: 363
Sequence Mass (Da): 41576
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A0A5A8BZC9 | MRAALAARCRFPPRAGVTTALGAARSAHVRGLKVFVGISGGVDSSVAAAVVKDQGHDVVGVFMRNWDSADEAGQAVCPQDADLESAQAVAQHLGIPLVERGFEPEYWASVFEPFLSAYAEGRTPNPDVACNRHVKFGAFHDWCMRQGADMVATGHYAGLEGGPSAPCADGPSGRGASVPAAPTDGDALALRAWEDPASVEAAVAASGGRAVSLCPAPAPGPGFRALTHAADPLKDQSYFLCGVRAPVLETVALPLGAMCKGAVRTEAAARGLPTASRRDSTGICFIGKRSMRSFLPQYLQPTAGAFVDAETGREVGRHPGAELFTVGQSARVSGASSRLYVLSRDVADGTVWVVRSWDHPALFAAGLLLAGEPGLPPEAAAMAADADLMPVEQIGGILPRATGAGATAGAGAGGAAPEQPLPARVGAEAARASRSAGAHPAGSAAPWDGRGFNWLLPSDWPGFAELAAGRGVRALAKLNNRMPAAAGTLWLCRGSHGRTRLGLRLDLPHRAVSAGQVAALYVPGGAGGRLVCAGGTEIEAAGPSLAELGAVGVRPGREELSKAGVSRPELGTTWQAGVETGAGTLARWSVSESLESHGWTA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
EC: 2.8.1.14
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Length: 601
Sequence Mass (Da): 61321
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