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Q9WVS9 | MLFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEDLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLNSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLESLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGVEESLPETAADKSQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRPHLPAHEKMTQRRSSFSSQSINSQSVGSSLTQPAMSQAANLPIPQGMSQFQLSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNLGSVQLSSGNSNIQQLTPINMQGQVVPVNQIQSGVNAGHVSTGQHMIQQQTLQSTSTQSQQSVMSGHSQPTSLPNQTPSTLTAPLYNTMVISQPAAGSMVPIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQALSVTQQQQQQQQQQQQQQQQQPQQAQQPQSQQSSQDQPHPSVQQPAQLTQPPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQQQQLHRHRTDSLTDPSKVQPQ | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'. The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (By similarity). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity).
PTM: Ubiquitinated, leading to its proteasomal degradation.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 97004
Sequence Length: 862
Subcellular Location: Cytoplasm
EC: 2.3.1.48
|
Q8GHB2 | MPALPIDQEFDCERFRADIRATAAAIGAPIAHRLTDTVLEAFRDNFAQGATLWKTTSQPGDQLSYRFFSRLKMDTVSRAIDAGLLDAAHPTLAVVDAWSSLYGGAPVQSGDFDAGRGMAKTWLYFGGLRPAEDILTVPALPASVQARLKDFLALGLAHVRFAAVDWRHHSANVYFRGKGPLDTVQFARIHALSGSTPPAAHVVEEVLAYMPEDYCVAITLDLHSGDIERVCFYALKVPKNALPRIPTRIARFLEVAPSHDVEECNVIGWSFGRSGDYVKAERSYTGNMAEILAGWNCFFHGEEGRDHDLRALHQHTESTMGGAR | Function: Magnesium-independent aromatic prenyltransferase that catalyzes the irreversible transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the clorobiocin biosynthesis pathway. Clorobiocin is an aminocoumarin family antibiotic.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + dimethylallyl diphosphate = 3-dimethylallyl-4-hydroxyphenylpyruvate + diphosphate
Sequence Mass (Da): 35626
Sequence Length: 324
Pathway: Antibiotic biosynthesis.
EC: 2.5.1.111
|
P56772 | MPIGVPKVPFRSPGEGDTSWVDIYNRLYRERLFFLGQEVDTEISNQLISLMIYLSIEKDTKDLYLFINSPGGWVISGMAIYDTMQFVRPDVQTICMGLAASIASFILVGGAITKRIAFPHARVMIHQPASSFYEAQTGEFILEAEELLKLRETITRVYVQRTGKPIWVISEDMERDVFMSATEAQAYGIVDLVAVQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22124
Sequence Length: 196
Subcellular Location: Plastid
EC: 3.4.21.92
|
Q85FJ8 | MPIGVPKVPFRLPGEEDAVWVDVYNRLYRERLLFLGQQVDDEIANQLIGIMMYLNSEDQAKDMYLYVNSPGGAVLAGISVYDAMQFVVPDVHTICMGLAASMGSFILAGGEITRRIALPHARVMIHQPASSYYDGQAGECVMEAEEVLKLRDCITKVYAQRTGKPLWLISEDMERDVFLSAEEAQDYGVVDLVAVENVSR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22282
Sequence Length: 200
Subcellular Location: Plastid
EC: 3.4.21.92
|
A7M988 | MPIGVPRVRFQYRRDRSRVWIDIYNRLYRERCLFLAHVVESQIANQLVGLFIYLGVQDETKDIFLFINSPGGGIISGFAIYDTMQFVRPDIQTICVGLAASMGSFLLVGGAITKRLAFPHARVMIHQPMSAFFETQTVEAILEAEELLKLRESLAKVYVQRTGKPDWVIAEDMERDVFLSATEAQSYGIVDVVGVALASKG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22593
Sequence Length: 201
Subcellular Location: Plastid
EC: 3.4.21.92
|
Q3Z8J8 | MISPENVVPMVIESSARGERAFDIYSLLLKERIIFLGSQINDQVANLVIAQLLFLDREDPDKDISLYIHSPGGVISAGLAMYDTMQLIRPKVSTICVGVAASMATVLLCAGAKGKRYALPNATIHMHQAMGGAQGQASDIEIAAREIMRQQDILRNILVKHTGQPMEKIIHDSDRDYYLNAQQAVEYGLIDEILQKPENK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22091
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.4.21.92
|
Q9RSZ7 | MEVMSVIPYVIEQTGRGERSYDIYSRLLKDRIIFVGTPVESQMANSIVAQLLLLDSQNPEQEIQMYINCPGGEVYAGLAIYDTMRYIKAPVSTICVGMAMSMGSVLLMAGDKGKRMALPNSRIMIHQGSAGFRGNTPDLEVQAKEVLKLRDTLVDIYHKHTDLPQEKLLRDMERDYFMSPEEALKYGLIDQVIDQTRENRGGEE | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 23026
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 3.4.21.92
|
A4J7L9 | MSGLVPIVVEQTNRGERAYDIYSRLLKDRIIFIGGPIDDHIANLVIAQFLFLEAEDPEKDIHLYINSPGGVVTAGLAIYDTMQYIKPAVSTICLGQAASMGSFLLAAGAPGKRYALPMARIMIHQPLGGVQGQATDIDIHAKEILRMKDLLNDRLAHHTGQPLEQITRDTERDYFMSAEEAKKYGLIDEVMPYRK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21669
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.4.21.92
|
Q72CE8 | MPVPIVIESTGRAERAYDIYSRLLKDRIVLLGTPIDDQVASLICAQLLFLESENPEKEIHMYINSPGGSVTAGMAIYDTMQYINSPVSTLCMGQAASMGALLLAAGAPGLRFSLPHSRIMIHQPSGGFQGQATDIDIQAREVLRLKQSLNAIMSQHTGKPLEQVALDTERDYFMGPEEAQAYGLIDRVLTSRSEATDTISK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21912
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 3.4.21.92
|
Q06FP3 | MPVGVPKVPFLNPNPDPEPDSVEEELDSMEEKATWVDLYNRLYRQRWLFLGKDLEEEVANNIVGLMIHLNIEDPFWTQTLYINCLGGLIIPGLALYDTIGFVEPDVKTICLGIAASMASVVLVGGTVTERCAFPNARVMIHQPRAKEFDDRFSDLNLEGHLFLQLRNCVTQIYIHRTNKPAWVIIADLERDTFMSATEARTYGIIDGVYAFEEEYEEWS | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 24988
Sequence Length: 219
Subcellular Location: Plastid
EC: 3.4.21.92
|
Q3BAL3 | MPIGVPKVPFRNPGEEDAVWVDVYNRLHRERLLFLGQEVDSEISNQIVGLMVYLSIEDDTRDLYLFINSPGGWVIPGIAIYDTMQFVLPDVHTICMGLAASMGSFILVGGEITKRLAFPHARVMIHQPASSFYEAQARDFILEAEELLKLRETLTKVYVQRTGNPLWVISEDMERDVFMSATEAQAHGIVDLVAIENENTGNSI | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22925
Sequence Length: 204
Subcellular Location: Plastid
EC: 3.4.21.92
|
Q6YXM7 | MPIGVPKVPFRLPGEEDAVWIDVYNNRLYRERLLFLGQHVDDEIANQLIGIMMYLNGEDENKDMYLYINSPGGAVLAGISVYDAMQFVVPDVHTICMGLAASMGSFILAGGEITKRIALPHARVMIHQPASSYYDGQAGECIMEAEEVLKLRDYITRVYVQRIGKPLWVISEDMERDVFMSAQEAKTYGIVDLVAIENT | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22337
Sequence Length: 199
Subcellular Location: Plastid
EC: 3.4.21.92
|
P84723 | APTEADATWVDLYNRVMIHQPASSYYAAEMHNEAKTDNPEEVLDLDRDVFMSAAYGIVDTVWYVQAELVNGRGGAVVAGL | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 8790
Sequence Length: 80
Subcellular Location: Plastid
EC: 3.4.21.92
|
A4GYT6 | MPIGVPKVPFRNPGEDSSNWIDVYNRLYRERLLFLGQDIDSEISNQLIGLMVYLSTESEIKDLYLFINSPGGWVIPGIAIYDTMQFVRPDVQTVCMGLAASMGSFILVGGKITKRLAFPHARVMIHQPFAAFYEAQIGEFVLEAEELLKLREILTRVYAQRTGKPLWVVSEDMERDVFMSAAEAQVHGIVDLVAVA | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22041
Sequence Length: 196
Subcellular Location: Plastid
EC: 3.4.21.92
|
B5YI38 | MSIVPIVIEQTGRTERVYDIYSRLLKDRIIFIGTEINDHVANVVIAQLLFLQTEDPEKDIHIYINSPGGMVSSGLAIYDTMQYVKPDIATYCIGQASSMACVLLAAGTKGKRFALPHSRVMIHQPIGGFYGQATDVEIHAKEILKMKDLLNNILAKHTGQPIEKIQKDTERDFFMSAEEAKLYGIVDEVISSIKK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21783
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.4.21.92
|
Q0ZIZ4 | MPIGVPKVPFRNPGEDDISWIDVYNRLYRERLLFLGQEVESEISNQLIGLMIYLSIEDENKDLYFFINSPGGWVLPGIAIYDTMQFVPPEVHTICLGLAASMGSFILVGGTITKRLAFPHARVMIHQPAAAFYEAQAGEFVMEAEELLKLREIITKVYVQRTGKPLWVVSEDLERDVFMSATEAQTHGIVDLVAVQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22075
Sequence Length: 196
Subcellular Location: Plastid
EC: 3.4.21.92
|
P45865 | MKVFIVIMIIVVIFFALILLDIFMGRAGYRKKAYEPVFSKKKSDIELIHCGADLVERMMNDIRQAASSVHMMFFIMKNDEVSHNMYTLLKTKAQAGVSVYLLLDWAGCRAIKKTALQTMKNAGVHVHVMNRPRFPFFFFHMQKRNHRKITVIDGKIGYIGGFNIAEEYLGKKAKFGNWEDYHLRMIGEGVHDLQTLFASDLKRNTGIELGSDVWPKLQQGTISHKIYATDGYSLENIYLANIAQAKNRLTVCTPYYIPSKPLQEALINARKNGVSVRIIVPMKSDHPLVREAAFTYYSELLDAGCLIYRYYQGFYHVKALIIDDHLSIIGTANFDKRSLFLNEEVNVEIDDEAFTSEVYATIEEDMKKSELLTMEDFSKRTFRQRPAEWLGRALSYFL | Function: Involved in the biosynthesis of cardiolipin.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45842
Sequence Length: 398
Subcellular Location: Cell membrane
|
P59715 | MKCSWREGNKIQLLENGEQYYPAVFKAIGEAQERIILETFIWFEDNVGKQLHAALLAAAQRGVKAEVLLDGYGSPDLSDEFVNELTAAGVVFRYYDPRPRLFGMRTNVFRRMHRKIVVIDARIAFIGGLNYSSEHMSSYGPEAKQDYAVRLEGPIVEDILQFELENLPGQSAARRWWRRHHKAEENRQPGEAQVLLVWRDNEEHRDDIERHYLKMLTQAQREVIIANAYFFPGYRFLHALRKAARRGVRIKLIIQGEPDMPIVRVGARLLYNYLVKGGVQVFEYRRRPLHGKVALMDDHWATVGSSNLDPLSLSLNLEANVIIHDRHFNQTLRDNLNGIIAADCQQVDETMLPKRTWWNLTKSVLAFHFLRHFPALVGWLPAHTPRLTQVDPPAQPTMETQDRVETENTGVNP | Function: Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47636
Sequence Length: 413
Subcellular Location: Cell membrane
EC: 2.7.8.-
|
P75919 | MPRLASAVLPLCSQHPGQCGLFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARYWYCKSVSPLQQVLDVPEGEMADRIELPASWHNDAMTHRYLRKMESSPFINHLVDGTLPLIWAKTRLLSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKKLLRYGVELYELKPTREQSSTLHDRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPVEWLL | Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a cardiolipin + ethanolamine
Sequence Mass (Da): 53666
Sequence Length: 473
EC: 2.7.8.-
|
O66043 | MKNRLNVLAFFALLFAALYISRGFLQSWMVGTLSVVFTLSVIFIGIIIFFENRHPTKTLTWLLVLAAFPVVGFFFYLMFGQNHRKSKRFSKKAIEDERAFQKIEGQRQLNEEQLKKMGGHQQLLFRLAHKLGKNPISFSSETKVLTDGKETYAHILQALKMAEHHIHLEYYIVRHDDLGNQIKDILISKAKEGVHVRFLYDGVGSWKLSKSYVEELRDAGVEMVSFSPVKLPFLTHTINYRNHRKIIVIDGVVGFVGGLNIGDEYLGKDAYFGYWRDTHLYVRGEAVRTLQLIFLQDWHYQTGETILNQTYLSPSLSMTKGDGGVQMIASGPDTRWEVNKKLFFSMITSAKKSIWIASPYFIPDDDILSALKIAALSGIDVRILVPNRPDKRIVFHASRSYFPELLEAGVKVYEYNRGFMHSKIIIVDHEIASIGTSNMDMRSFHLNFEVNAYLYRTSSVTKLVSDYVYDLEHSNQINFSLFKNRPFFHRLIESTSRLLSPLL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57907
Sequence Length: 503
Subcellular Location: Cell membrane
EC: 2.7.8.-
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Q93YW7 | MAIYRSLRKLVEINHRKTRPFFTAATASGGTVSLTPPQFSPLFPHFSHRLSPLSKWFVPLNGPLFLSSPPWKLLQSATPLHWRGNGSVLKKVEALNLRLDRIRSRTRFPRQLGLQSVVPNILTVDRNDSKEEDGGKLVKSFVNVPNMISMARLVSGPVLWWMISNEMYSSAFLGLAVSGASDWLDGYVARRMKINSVVGSYLDPLADKVLIGCVAVAMVQKDLLHPGLVGIVLLRDVALVGGAVYLRALNLDWKWKTWSDFFNLDGSSPQKVEPLFISKVNTVFQLTLVAGAILQPEFGNPDTQTWITYLSWLVASTTMASTAAYGVQYWKKRPISMIKRS | Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL. Possesses high activity with PG species carrying dioleoyl groups and low activity with species carrying one or two palmitoyl groups. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. In mitochondrial fission, CL stabilizes the protein complex of the major mitochondrial fission factors, DRP3A and DRP3B.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-diacyl-sn-glycerol = a cardiolipin + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38042
Sequence Length: 341
Subcellular Location: Mitochondrion inner membrane
EC: 2.7.8.41
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Q54MZ9 | MKGELIDITMKSGLKCDAYVSRPKDSQKELKPVIFVMDAFGLRDWLYEMADKIAEEGYFVVQPNFYYRIGKNIITNLEKLKSADTKDEVICQIRTQMAKINREETVSDVSEMFDFIDKQEGVRKSKEGVAIVGYCFGGGVAMRSAIAFPDIVKVVASFHAGRLAIPDDENSIHKHLKGVKAECYFGHADNDQSMPLDQIHLFEKSLTEAGIKYTSEIYNNPSCAHGWVMGDTLMYNPIGSDKHYDELFKLLKRAL | Function: Cysteine hydrolase.
Sequence Mass (Da): 28841
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q96DG6 | MANEAYPCPCDIGHRLEYGGLGREVQVEHIKAYVTKSPVDAGKAVIVIQDIFGWQLPNTRYIADMISGNGYTTIVPDFFVGQEPWDPSGDWSIFPEWLKTRNAQKIDREISAILKYLKQQCHAQKIGIVGFCWGGTAVHHLMMKYSEFRAGVSVYGIVKDSEDIYNLKNPTLFIFAENDVVIPLKDVSLLTQKLKEHCKVEYQIKTFSGQTHGFVHRKREDCSPADKPYIDEARRNLIEWLNKYM | Function: Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin.
Sequence Mass (Da): 28048
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q8R1G2 | MANEANPCPCDIGHKLEYGGMGHEVQVEHIKAYVTRSPVDAGKAVIVVQDIFGWQLPNTRYMADMIARNGYTTIVPDFFVGQEPWDPAGDWSTFPAWLKSRNARKVNREVDAVLRYLRQQCHAQKIGIVGFCWGGVVVHQVMTAYPDIRAGVSVYGIIRDSEDVYNLKNPTLFIFAENDTVIPLEQVSTLTQKLKEHCIVNYQVKTFSGQTHGFVHRKREDCSPADKPYIEEARRNLIEWLNKYV | Function: Cysteine hydrolase.
Sequence Mass (Da): 27902
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q6P7K0 | MANEACPCPCDIGDKIEYGAKGQEVQIEHIKAYVSKPHSSTDKAVIVVQDIFGWQLPNTRFMADLLTAHGYITICPDFFVGQEPWKPSNDRSTFTEWLQTRQATKVEKEINVVLKYLKEQCHVKKIGVIGFCWGGVVTHHLMLKYPELKAGVSFYGIIRDVEDRYNLLNPTLFIFAEMDHVIPLEQVSLLEEKLKVHSKVDFQVKVFPKQTHGFVHRKNEDINPEDKPFIEEARKNMLEWLHKYIN | Function: Cysteine hydrolase.
Sequence Mass (Da): 28471
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q21153 | MSFDHLLTSSKRRELLQNLGIGHGSDVFSTGLFRKAECNAETAISQRSIPRANPDHLRPIFDRFATKEIKGKKLMTPEDFIRGYLGLYTEENYNKETVRLLASAADTTKDGDISFEEFCAFEALLCSPDALYLTAFELFDRNASDTISCDEFEAVIRHTQPLHDQDFDFSSEFIKRYFGADKQRNVNYHSFCQLLHDFYEEQGIQAFKRYDKNGNGTISSLDFQQIMTTVKGHLLTDFVRHNLIAVSGGGASGHKFSDTRGGFVTFPYYAAFNSLLAKMELIKRVYVSTTRGNLDIEMTKEEFLHAIQSYTQVTPYEVEILFHLSELNHPGRKTLCLKDIQAIDPERLKRVSQMDRLINIKAVHHKDDRGVGTAFLESAYRFLLGSVAGACGATAVYPIDLVKTRMQNQRTSGSFVGEVMYKNSLDCFKKVVKFEGLLGLYRGLLPQIVGVAPEKAIKLTMNDYMRDKFTKDGKIPLYGEIIAGGTGGMCQVVFTNPLEIVKIRLQTAGEVQQAGKKIGVFTVLKELGFLGLYKGSRACFLRDIPFSAIYFPAYAHAKLASADEDGMNSPGTLFASAFIAGVPAAGLVTPADVIKTRLQVAARAGQTTYNGVIDCARKLIKEEGPMSLWKGTAARVCRSSPQFAVTLLTYEVLQRLFYVDFAGSRPTGSELATTKTIQDESSTNPDHVGGYKLAAATFSGIEHKFGLFLPKFETSK | Function: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79595
Sequence Length: 716
Domain: Upon calcium binding, the EF-hand-containing regulatory N-terminal domain binds to the C-terminal domain, opening a vestibule which allows the substrates to be translocated through the carrier domain. In the absence of calcium, the linker loop domain may close the vestibule, which may prevent substrates from entering the carrier domain.
Subcellular Location: Mitochondrion inner membrane
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D6W196 | MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKVNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESSIKFGSFEVTKKIMTKLEGCRDTKDLSKFSTYIAGGLAGMAAQFSVYPIDTLKFRVQCAPLDTKLKGNNLLFQTAKDMFREGGGQIILQRCHSRYSGHISLCCIRFGDFFCLKKMVYCQTGKDPEPTTRSGHSKQPGCTSNGCIQWNCRSFCCLSNQSFKNKTTSPRNICTSLCV | Function: Calcium-dependent mitochondrial solute carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55715
Sequence Length: 494
Subcellular Location: Mitochondrion inner membrane
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P0CI40 | MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKMNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESSIKFGSFEVTKKIMTKLEGCRDTKDLSKFSTYIAGGLAGMAAQFSVYPIDTLKFRVQCAPLDTKLKGNNLLFQTAKDMFREGGLRLFYRGVTVGIVGIFPYAALDLGTFSALKKWYIAKQAKTLNLPQDQVTLSNLVVLPMGAFSGTVGASVVYPINLLRTRLQAQGTYAHPYVYNGFKDVLLKTLEREGYQGLFKGLVPTLAKVCPAVSISYLCYENLKKFMNLE | Function: Calcium-dependent mitochondrial solute carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61270
Sequence Length: 545
Subcellular Location: Mitochondrion inner membrane
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Q20799 | MINKNEQTESTSGAAEQKEDDEEQYVQLSSLGEYKDEVTPLLSPKHVPLVLGKVTKEAAIATHSALHGGMSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSPDDEGRVDFYSFSSYVLENEQKLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMMLYPSSDLKDIVDFWRHNLIIDIGEDSQIPEDFSQQEMQEGIWWRHLVAGGAAGAVSRTCTAPFDRIKVYLQVNSSKTNRLGVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFMCYDQLKRLIQKKKGNEEISTFERLCAGSAAGAISQSTIYPMEVMKTRLALRKTGQLDRGIIHFAHKMYTKEGIRCFYKGYLPNLIGIIPYAGIDLAIYETLKRTYVRYYETNSSEPGVLALLACGTCSSTCGQLSSYPFALVRTRLQALSITRYSPQPDTMFGQFKYILQNEGVTGFYRGITPNFLKVIPAVSISYVVYEKVRTGLGVPVCSRGGLEDIHQFLPCSIHSIIQFFFFPRTFLLTISGRSLRVKPVWRSHFSKFNK | Function: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66337
Sequence Length: 588
Subcellular Location: Mitochondrion inner membrane
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F2RB81 | MVELPDLLTDLFRRHRGRTALRTAGRTWTYEELDRVTSALARRIDAECPAGRRVLVAGEHTAEAVVWALAAMRSHAVHTPMNPGLPADRFEEFARVADAALLVCFEREALVRGEKAGLRALYAGDVGWPTDPAPAPADGTADEPARSRVAYSIFTSGSTGDPKLVDVGHGGLLNLCRSLRRLLDITPDDQVLHFASLSFDASVSEILGTLYAGATLVVPVRDQASWLGSVSRHLAAHGCDLAMLSPSVYARLDEAARSRIRKVEFCGEALGEGEYDKAARYSRVFNAYGPTEATVCFSLAELTSYTPSIGTPVDGFRAYVRDPDSGDHATAGTGELVIVGDGVALGYAGGSPAENEVFGTVDGSPAYATGDVVSLSDDGELTYLGRIDEQIKRLGHRVNLAHVGSTLSRHLGREVALVRQDATILLVTAADGEATEESLMARIRDLVPVWEAPDRLVLVDALPLTSGGKVDRSALRELLASPAGAPHGGTDGEDAAELRRVLDVVTAVLGQEIGPETSIFDAGGSSLAMIQIQVKLSDAYGEEAVEAAFAAMDYDFAPAAFLRHLRGEAVAPAESAVDTLLRRVETERDALRAELPLLRRDTRHEPVPGAADGDREVLLTGASGFIGGHVLDRLLAAGRPVLVVSTGDPDGVLTGHATRFGRQAADYARVRAISYAELERWVDRRRGPVVDAVVHCGYQVNHLLPLDSHLSGSVRNTALVVRAAAALGARSFAFLSAASAGADFLPLSAATLTAVGDPYSRSKLISEEYVNTLAVLGCAVSHYRPGLVYGHRPEDRHHLKDDWFTALLETARRVGAMPRLSGHVPVCDVGTLADTLLGRPDANPGTADGASRTPDSRSAVVVHRTYALDELLRHTGLTEADVLAPAAWFERVRDGGEVPAPLLAAMQAALSGPGWPSAHREVDHDILGRLLGTPPDTPAGDRPERTGTTAEAQNGAAHAPTPR | Cofactor: Binds 1 phosphopantetheine covalently.
Function: Involved in chloramphenicol biosynthesis . Activates 4-amino-L-phenylalanine by adenylation and loads it onto its peptidyl carrier domain, via a thioester linkage to the phosphopanthetheine moiety . Can also adenylate tyrosine and phenylalanine at low rates, but not L-p-nitrophenylalanine or threo-phenylserine .
Catalytic Activity: 4-amino-L-phenylalanine + ATP + holo-[peptidyl-carrier protein] = 4-amino-L-phenylalanyl-[peptidyl-carrier protein] + AMP + diphosphate
Sequence Mass (Da): 102318
Sequence Length: 963
Domain: Contains an N-terminal adenylation domain, an internal peptidyl carrier domain and a C-terminal domain that is homologous to nicotinamide-dependent dehydrogenases.
Pathway: Antibiotic biosynthesis.
EC: 6.2.1.-
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B2K217 | MNIDKIFENPSNLRSFEFNNDVCKVFDDMVSRSVPGYHNIQDIISLTYDEFSQNRVFIDVGCSTGTTIAKILSENQVNYCYGIDISESMLAIAQEKCGEHESLVTFKNCNLLNGTDNVINSEKVPDFIILNLVLQFIRPPERKKFITNIKSLCSSSTLMLVFEKIIFNDAEINMKYIDSYLKWKGKNGYSESEVSNKRKALENKLIPYLHEENIELFKSSGFNSVEICFSFLNFRGYLCRC | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27715
Sequence Length: 241
EC: 2.1.3.-
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A8EVV4 | MIDKVFNKSITKQFEFDEEVASVFDDMLNRSVPFYKEMQRLSINFACNFLSENDKVYDLGCSTASTLIELSKHCKHNLKLIGIDNSDAMLKRASNKAKAFGVEIELINADLHDVTYNDAKLILSNYTLQFIRPLQREKLVKKIYDSLDEKGIFIFSEKVISTNSNLNKQCIDEYYEFKKTQGYSEFEISQKREALENVLIPYTEDENKKMIKDAGFSHCETIFKWVNFATFIAIK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27291
Sequence Length: 235
EC: 2.1.3.-
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Q4FQB1 | MSHPMSQSQPATVKHDTLFTTPLDKAARFSFDEQVVACFPDMIRRSVPGYGQVLAMLPIFARRHCKYRQQGDNGQRVSRIYDLGCSLGAASMTLAGEFESQDLQIKAIDISPAMTTEATTLLSDNYPEHDIEVITADIRDIEFEPCDMVILNLTLQFLPAADRVAVLEKIYAALSEGGILVLTEKTHAFDEQYDAWLVERYYDFKRANGYTEMEISGKRNALENVLITDTLDEHHTRLAQVGFQRHLTWFQFLNFVSIVAFK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 29723
Sequence Length: 262
EC: 2.1.3.-
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A5WC55 | MTNHTITTAERELYLALIQRAQYRPIATQWLANLPQWLSDVKDKRRYAHAPAYLSAVENLPQIKVKNVDLNSDILTIDADLTDGQSKQITALMKQLMPWRKGPFQIGSGDNKVFIDTEWHSDWKWNRIKPHLGTLQGRYVLDVGGGSGYHGWRMAGAGAKQVVIIDPSCLFYHQFMAIRHFVAGFDTDMDSDRTGVGYRTHYIPVGLEQLPSSSDQGNQLFDTVFCMGVLYHRQSPFEHLIQLKNQLINGGQLVLETLVIEGDANTVLVPHNRYAKMNNVYFIPSVAALTGWLEKVGFSEVKCVDIDITSIKEQRATDWMSYQSLKDFLDPNDPTKTVEGYPAPMRATLIATK | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39917
Sequence Length: 353
EC: 2.5.1.-
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A1AVT4 | MLSDFYKYATSTQLDLICTQLINLSTHVFNTNNGNIPKWEQAIKQIKTQNTGSLDFITPYLNISAHHINNFTLEKSLKQLIPWRKGPYQIGDLQLDSEWRGDMKWHRLIPHIKPLKDKVVLDVGSGNGYFTYLMAISGAKIALGIEPFLLFNYQFQAIRTLINNLPNVFVLPLSLDKIPKKPLFDTVFSMGVLYHQKDYELHLNQLKDVMKPSGELILETLIIDLEKVKKIIPKGRYAKMRNVYCLPSKNTLRTWLEDAEFKNIKLLDVTKTTSKEQRATHWIGNNTQSLKNFLDPNNRDLTIEGFPAPKRAIFICQK | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36706
Sequence Length: 318
EC: 2.5.1.-
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Q21JL7 | MIDYTSFLEQEKEGPLARWVEILPDQISEGLSTKRYGDLEQWLTAMQNLPQVDNVQVSYQSAVTLKSTAPLAQETHTLIEQQFRALIPWRKGPYNIFDIEIDTEWHSDWKWDRVLPHLAPLKHRKILDVGCGNGYHCWRMYGEGASQVIGIDPSPRFVVQFYMLKHFIGSNAPVDLLPVPMEAVPANLQAFDTTFSMGVLYHRRSPMDHLRELKATLRPGGQLVLETLVIEGKLGEVLVPEGRYAMMNNVWFLPSVPTLISWLTKCGFKNARCVDVNQTSTDEQRSTEWMTFQSLSDFLDPNDPTLTAEGHPAPLRAVILAEAPE | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36933
Sequence Length: 325
EC: 2.5.1.-
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Q8ZNV1 | MIEFGNFYQLIAKNHLSHWLETLPAQIASWQREQQHGLFKQWSNAVEFLPEMTPWRLDLLHSVTAESETPLSEGQLKRIDTLLRNLMPWRKGPFSLYGVDIDTEWRSDWKWDRVLPHLSDLTGRTILDVGCGSGYHLWRMIGAGAHLAVGIDPTQLFLCQFEAVRKLLGNDQRAHLLPLGIEQLPALKAFDTVFSMGVLYHRRSPLEHLWQLKDQLVNEGELVLETLVIDGDENTVLVPGDRYAQMRNVYFIPSAPALKKWLEKCGFIDVRIADVCVTTTEEQRRTEWMVTESLADFLDPNDRSKTVEGYPAPQRAVLIARKP | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37111
Sequence Length: 323
EC: 2.5.1.-
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G7IBJ4 | MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRINLWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELIIDSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEKAWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHFFQFGIFDDAVTLEITSSNFLTKYYYCLWWGLRNLSSSGENLLTSTHVAEINFAVIVAILGLVLFALLIGNMQTYLQSTTIRLEEWRIRRTDTERWMHHRQLPHYLKENVRRHDQFRWVATRGVDEEAILRDLPVDLRRDIKRHLCLNLVRQVPLFDQMDDRMLDAICERLKPTLCTPGTCIVREGDPVDEMLFIVRGRLDSCTTNGGRTGFFNTCRIGSGDFCGEELLPWALDPRPTAVLPSSTRTVRAITEVEAFALIAEDLKFVAAQFRRLHSKQLRQTFRFYSHQWRTWAACFIQAAWFRYKRMKETNEVKEKENLMMMSNVKYYGNDDSQYFSAPLQVPKGSSYSMYSGKLVGSLRRGRSMRYGSELDMLGTLRKPIEPDFNDDGD | Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations . Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors . Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations . May function during fertilization in both female and male gametophytic Ca(2+) signaling .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81946
Sequence Length: 710
Subcellular Location: Nucleus membrane
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G7JND3 | MVTPKFMSDLFEGDHLELAKLTSPNGDNGIKFNEKHVAPRVLSRVFSEDYKRVKRRRRIFDPRGQTIHQWNKIFLVACLISLFVDPLFFYLPIVQDEVCIDIGIAVEVFLIIIRSIADVFYVIHIFMRFHTAYVAPSSRVFGRGELVIDSSKIASRYLHKGFFLDFIAALPLPQVLIWIVIPNLGGSTIANTKNVLRFIIIIQYLPRLFLIFPLSSQIVKATGVVTETAWAGAAYNLMLYMLASHVLGACWYLLSIERQEACWKSVCKLEESSCQFDFFDCNMVKDSLRVSWFVTSNVTNLCSPNSLFYQFGIYGDAVTSKVTTSAFFNKYFFCLWWGLRNLSSLGQGLLTSTFVGEIMFAIVIATLGLVLFALLIGNMQTYLQSTTVRLEEWRVKRTDTEQWMHHRQLPQELRQSVRKYDQYKWIATRGVDEESLLRGLPLDLRRDIKRHLCLELVRRVPLFDAMDERMLDAICERLKPALCTENTYLVREGDPVNEMLFIIRGNLDSYTTDGGRTGFFNSCRIGPGDFCGEELLTWALDPRPTMVIPSSTRTVKAISEVEAFALIAEDLKFVASQFRRLHSKQLRNKLRFHSHQWRTWAACFIQVAWRRTIQEKKGSC | Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations . Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors . Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations . May function during fertilization in both female and male gametophytic Ca(2+) signaling .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71425
Sequence Length: 620
Subcellular Location: Nucleus membrane
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Q00195 | MMTEKSNGVKSSPANNHNHHPPPSIKANGKDDHRAGSRPQSVAADDDTSPELQRLAEMDTPRRGRGGFQRIVRLVGVIRDWANKNFREEEPRPDSFLERFRGPELQTVTTHQGDDKGGKDGEGKGTKKKFELFVLDPAGDWYYRWLFVIAMPVLYNWCLLVARACFSDLQRNYFVVWLVLDYFSDTVYIADLIIRLRTGFLEQGLLVKDPKKLRDNYIHTLQFKLDVASIIPTDLIYFAVGIHSPEVRFNRLLHFARMFEFFDRTETRTSYPNIFRISNLVLYILVIIHWNACIYYVISKSIGFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKDMEAKVIKWFDYLWTNKKTVDEREVLKNLPAKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVAASMEVDVQEKLEQLETNMDTLYTRFARLLAEYTGAQQKLKQRITVLETKMKQNHEDDYLSDGINTPEPTAAE | Function: Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76177
Sequence Length: 664
Domain: The C-terminal coiled-coil domain mediates trimerization of CNGA subunits.
Subcellular Location: Membrane
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Q16281 | MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADSGQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQANVGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVFYNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLWQHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNMFRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSIKQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEEKGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQRLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78838
Sequence Length: 694
Domain: The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits.
Subcellular Location: Membrane
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Q9JJZ8 | MAKVNTQCSQPSPTQLSIKNADRDLDHVENGLGRVSRLIISIRAWASRHLHDEDQTPDSFLDRFHGSELKEVSTRESNAQPNPGEQKPPDGGEGRKEEPIVVDPSSNIYYRWLTAIALPVFYNWCLLVCRACFDELQSEHLTLWLVLDYSADVLYVLDMLVRARTGFLEQGLMVRDTKRLWKHYTKTLHFKLDILSLIPTDLAYLKLGVNYPELRFNRLLKFSRLFEFFDRTETRTNYPNVFRIGNLVLYTLIIIHWNACIYFAISKFIGFGTDSWVYPNTSKPEYARLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVIDFLVGILIFATIVGNVGSMISNMNAPRVEFQAKIDSVKQYMQFRKVTKDLETRVIRWFDYLWANRKTVDEKEVLKNLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRALEEKGRQILMKDNLIDEDLVAARVDTRDVEEKVEYLESSLDILQTRFARLLAEYSASQMKLKQRLTRLESQMNRRCCGFSPDRENSEDASKTD | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones (By similarity). Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72702
Sequence Length: 631
Domain: The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits.
Subcellular Location: Membrane
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Q3UW12 | MSQDSKVKTTESTPPAPTKARKWLPVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFPDLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQGILVVDKSMIASRYVRTWSFLLDLASLVPTDAAYVQLGPHIPTLRLNRFLRVPRLFEAFDRTETRTAYPNAFRIAKLMIYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPLPAREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRRLERRVIDWYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQYAVLGAGLYFGEISIINIKGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEKGREILLKMNKLDVNAEAAEIALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEWQTREWPMPDDMGEADDEAEPGEGTSKDGEEKAGQEGPSGLE | Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65835
Sequence Length: 575
Domain: The C-terminal coiled-coil domain mediates trimerization of CNGA subunits.
Subcellular Location: Membrane
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Q64359 | MSQDGKVKTTESTPPAPTKARKWLPVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFPDLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQGILVVDKGMIASRYVRTWSFLLDLASLVPTDAAYVQLGPHIPTLRLNRFLRVPRLFEAFDRTETRTAYPNAFRIAKLMLYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPLPDREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNKRLERRVIDWYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQYAVLGAGLYFGEISIINIKGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEKGREILLKMNKLDVNAEAAEIALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEWQTREWPMPEDMGEADDEAEPGEGTSKDGEGKAGQAGPSGIE | Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65675
Sequence Length: 575
Domain: The C-terminal coiled-coil domain mediates trimerization of CNGA subunits.
Subcellular Location: Membrane
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Q24278 | MRHFKVKAMVQSLDISAITGQQTDAEPSKRSKPSALRRTLQALRQRLTKRNRPKPPDWFLEKFSNTTNTDKIGKGCPAMEDAALSSEIRGSSVLCNRLSVDPTLQSHYRWLAIVSLAVLYNIIFVVGRAVFWEINKSAPAFWYTLDYLCDFIYLLDTLVHMHEGFLDQGLLVRDAFRLRRHYFHTKGWYLDVLSMLPTDLAYIWWPPETCSSLYLPCPVIVRLNRLLRINRLWEWFDRTETATGYPNAFRICKVVLAILVLIHWNACMYFAISYEIGFSSDSWVYNLNGTRNNTLQRQYIYSFYWSTLTLTTIGETPTPENDVEYLFVVADFLAGVLIFATIVGNIGSMISNMNVARVEFQNRMDGVKQYMAFRRVGHELEARVIRWFAYTWSQSGALDEERVLAALPDKLKAEIAIQVHMDTLKQVRIFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVVGDDGITVLATLGAGSVFGEVSVLEIAGNRTGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEARSTLTQRGCQLLRKDGLLDEQIFADSQRVHDSIEGGIEKLELSVENLNMRLARLLAEYTASQAKIKQRLAKLEMNGGPGTWRLECEPQSRARSGRLYSLQPKRRPRSRPDATAKSSDAAKQNTL | Function: Approximately 50-fold more sensitive to cGMP than to cAMP. May be involved in transduction cascades of both invertebrate photoreceptors and olfactory sensillae.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75823
Sequence Length: 665
Subcellular Location: Membrane
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Q9NQW8 | MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPVTSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPAAPVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKPTEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCCFIPLRLVFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKFQLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYLLFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVRTWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRKDLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQKENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTSRQSLIISMAPSAEGGEEVLTIEVKEKAKQ | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92167
Sequence Length: 809
Subcellular Location: Membrane
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O65717 | MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNESCPIQTPNTTLFDFGIFLDALQSGVVESQDFPQKFFYCFWWGLQNLSSLGQNLKTSTYIWEICFAVFISIAGLVLFSFLIGNMQTYLQSTTTRLEEMRVKRRDAEQWMSHRLLPENLRKRIRRYEQYKWQETRGVDEENLLSNLPKDLRRDIKRHLCLALLMRVPMFEKMDEQLLDALCDRLQPVLYTEESYIVREGDPVDEMLFIMRGKLLTITTNGGRTGFLNSEYLGAGDFCGEELLTWALDPHSSSNLPISTRTVRALMEVEAFALKADDLKFVASQFRRLHSKQLRHTFRYYSQQWKTWAACFIQAAWRRYIKKKLEESLKEEENRLQDALAKEACGSSPSLGATIYASRFAANILRTIRRSGSVRKPRMPERMPPMLLQKPAEPDFNSDD | Function: Acts as cyclic nucleotide-gated ion channel. Can be activated by cyclic AMP which leads to an opening of the cation channel. May be responsible for cAMP-induced calcium entry in cells and thus should be involved in the calcium signal transduction. Could transport K(+), Na(+) and Pb(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83097
Sequence Length: 716
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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O65718 | MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVASCIRQQCMRTGNCNLSLACKEEVCYQFVSPTSTVGYPCLSGNLTSVVNKPMCLDSNGPFRYGIYRWALPVISSNSLAVKILYPIFWGLMTLSTFANDLEPTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLHAVMAKKRKMQIRCRDMEWWMKRRQLPSRLRQRVRRFERQRWNALGGEDELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELLSWCLRRPFLDRLPPSSATFVCLENIEAFSLGSEDLRYITDHFRYKFANERLKRTARYYSSNWRTWAAVNIQMAWRRRRKRTRGENIGGSMSPVSENSIEGNSERRLLQYAAMFMSIRPHDHLE | Function: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Could also transport lithium, cesium and rubium and displays a strong selectivity against sodium. Seems to directly participate in pathogen-induced calcium influx. May function in homeostasis, re-establishing ionic balance after defense action and/or other stimuli. Could mediate the initiation of the developmentally regulated cell death programs.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83241
Sequence Length: 726
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q9SKD7 | MMNPQRNKFVRFNGNDDEFSTKTTRPSVSSVMKTVRRSFEKGSEKIRTFKRPLSVHSNKNKENNKKKKILRVMNPNDSYLQSWNKIFLLLSVVALAFDPLFFYIPYVKPERFCLNLDKKLQTIACVFRTFIDAFYVVHMLFQFHTGFITPSSSGFGRGELNEKHKDIALRYLGSYFLIDLLSILPIPQVVVLAIVPRMRRPASLVAKELLKWVIFCQYVPRIARIYPLFKEVTRTSGLVTETAWAGAALNLFLYMLASHVFGSFWYLISIERKDRCWREACAKIQNCTHAYLYCSPTGEDNRLFLNGSCPLIDPEEITNSTVFNFGIFADALQSGVVESRDFPKKFFYCFWWGLRNLSALGQNLKTSAFEGEIIFAIVICISGLVLFALLIGNMQKYLQSTTVRVEEMRVKRRDAEQWMSHRMLPDDLRKRIRKYEQYKWQETKGVEEEALLSSLPKDLRKDIKRHLCLKLLKKVPWFQAMDDRLLDALCARLKTVLYTEKSYIVREGEPVEDMLFIMRGNLISTTTYGGRTGFFNSVDLVAGDFCGDLLTWALDPLSSQFPISSRTVQALTEVEGFLLSADDLKFVATQYRRLHSKQLRHMFRFYSVQWQTWAACFIQAAWKRHCRRKLSKALREEEGKLHNTLQNDDSGGNKLNLGAAIYASRFASHALRNLRANAAARNSRFPHMLTLLPQKPADPEFPMDET | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81669
Sequence Length: 706
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q94AS9 | MATEQEFTRASRFSRDSSSVGYYSEEDNTEEEDEEEEEMEEIEEEEEEEEEEDPRIGLTCGGRRNGSSNNNKWMMLGRILDPRSKWVREWNKVFLLVCATGLFVDPLFLYTLSVSDTCMCLLVDGWLALTVTALRSMTDLLHLWNIWIQFKIARRWPYPGGDSDGDTNKGGGTRGSTRVAPPYVKKNGFFFDLFVILPLPQVVLWVVIPSLLKRGSVTLVVSVLLVTFLFQYLPKIYHSIRHLRRNATLSGYIFGTVWWGIALNMIAYFVAAHAAGACWYLLGVQRSAKCLKEQCENTIGCDLRMLSCKEPVYYGTTVMVLDRARLAWAQNHQARSVCLDINTNYTYGAYQWTIQLVSSESRLEKILFPIFWGLMTLSTFGNLESTTEWSEVVFNIIVLTSGLLLVTMLIGNIKVFLHATTSKKQAMHLKMRNIEWWMKKRHLPIGFRQRVRNYERQRWAAMRGVDECEMVQNLPEGLRRDIKYHLCLDLVRQVPLFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGVKSCCMLGPGNFSGDELLSWCLRRPFVERLPPSSSTLVTLETTEAFGLDAEDVKYVTQHFRYTFVNEKVKRSARYYSPGWRTWAAVAVQLAWRRYKHRLTLTSLSFIRPRRPLSRCASLGEDKLRLYAAILTSPKPNPDDFDDY | Function: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and sodium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Might constitute a common downstream component of the signaling pathways leading to hypersensitive response (HR).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80081
Sequence Length: 694
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q8RWS9 | MAGKRENFVRVDDLDSRLPSSSVAFQQNYASNFSGQLHPIHASNETSRSFKKGIQKGSKGLKSIGRSLGFGVYRAVFPEDLKVSEKKIFDPQDKFLLYCNKLFVASCILSVFVDPFFFYLPVINAESKCLGIDRKLAITASTLRTFIDVFYLAHMALQLRTAYIAPSSRVFGRGELVIDPAQIAKRYLQRWFIIDFLSVLPLPQIVVWRFLQSSNGSDVLATKQALLFIVLVQYIPRFLRVLPLTSELKRTAGVFAETAWAGAAYYLLLYMLASHIVGAFWYLLALERNDACWQEACIDAGNCSTDFLYCGNQNMDGYAVWNRAKESVLKSKCRADLDDNNPPFDFGIYTQALSSGIVSSQNFIVKYCYCLWWGLQNLSTLGQGLETSTYPMEIIFSISLAISGLILFALLIGNMQTYLQSLTIRLEEMRVKRRDSEQWMHHRMLPQDLRERVRRYDQYKWLETRGVDEEYLVQNLPKDLRRDIKRHLCLALVRRVPLFKSMDDKLLDAICMRLKPCLFTESTYLVREGDPVDEMLFIIRGRLESVTTDGGRSGFFNRSLLKEGEFCGEELLTWALDPKSGVNLPSSTRTVKALTEVEAFALTSEELKFVASQFRRLHSRQVQHTFRFYSHQWRTWAACFIQAAWRRYCKRKKMEEAEAEAAAVSSSTAGPSYSIGAAFLATKFAANALRTIHRNRNTKIRDLVKLQKPPEPDFTAD | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81969
Sequence Length: 717
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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O82226 | MFDTCGPKGVKSQVISGQRENFVRLDSMDSRYSQSSETGLNKCTLNIQGGPKRFAQGSKASSGSFKKGFRKGSEGLWSIGRSIGLGVSRAVFPEDLEVSEKKIFDPQDKFLLLCNKLFVASCILAVSVDPLFLYLPFINDKAKCVGIDRKLAIIVTTIRTVIDSFYLFHMALRFRTAYVAPSSRVFGRGELVIDPAQIAKRYLQQYFIIDLLSVLPVPQIIVWRFLYTSRGANVLATKQALRYIVLVQYIPRFLRMYPLSSELKRTAGVFAETAWAGAAYYLLLYMLASHIVGALWYLLALERNNDCWSKACHNNQNCTRNFLFCGNQNMKGYAAWDNIKVSYLQLKCPVNVPEDEEPPFDFGIYLRALSSGIVSSKNFVSKYFFCLWWGLQNLSTLGQGLETSTYPGEVIFSITLAIAGLLLFALLIGNMQTYLQSLTIRLEEMRVKRRDSEQWMHHRMLPPELRERVRRYDQYKWLETRGVDEENLVQNLPKDLRRDIKRHLCLALVRRVPLFENMDERLLDAICERLKPCLFTEKSYLVREGDPVNEMLFIIRGRLESVTTDGGRSGFYNRSLLKEGDFCGDELLTWALDPKSGSNLPSSTRTVKALTEVEAFALIADELKFVASQFRRLHSRQVQHTFRFYSQQWRTWAACFMQAAWRRYIKRKKLEQLRKEEEEEEAAAASVIAGGSPYSIRATFLASKFAANALRSVHKNRTAKSTLLLSSTKELVKFQKPPEPDFSAEDH | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85441
Sequence Length: 747
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q9S9N5 | MYKSQYISGQREKFVRLDDIDSSSSPATGMMMQRNCFGFNLKNRGGEKKKASKSFREGVKKIRSEGLITIGKSVTRAVFPEDLRITEKKIFDPQDKTLLVWNRLFVISCILAVSVDPLFFYLPIVDNSGSSCIGIDTKLAVTTTTLRTIVDVFYLTRMALQFRTAYIAPSSRVFGRGELVIDPAKIAERYLTRYFVVDFLAVLPLPQIAVWKFLHGSKGSDVLPTKTALLNIVIVQYIPRFVRFIPLTSELKKTAGAFAEGAWAGAAYYLLWYMLASHITGAFWYMLSVERNDTCWRFACKVQPDPRLCVQILYCGTKFVSSGETEWIKTVPELLKSNCSAKADDSKFNYGIYGQAISSGIVSSTTFFSKFCYCLWWGLQNLSTLGQGLQTSTFPGEVLFSIAIAIAGLLLFALLIGNMQTYLQSLTVRLEEMRIKRRDSEQWMHHRSLPQNLRERVRRYDQYKWLETRGVDEENIVQSLPKDLRRDIKRHLCLNLVRRVPLFANMDERLLDAICERLKPSLFTESTYIVREGDPVNEMMFIIRGRLESVTTDGGRSGFFNRGLLKEGDFCGEELLTWALDPKAGSNLPSSTRTVKALTEVEAFALEAEELKFVASQFRRLHSRQVQQTFRFYSQQWRTWASCFIQAAWRRYSRRKNAELRRIEEKEEELGYEDEYDDESDKRPMVITRSESSSRLRSTIFASRFAANALKGHRLRSSESSKTLINLQKPPEPDFDAE | Function: Putative cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84634
Sequence Length: 738
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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A9ZSY0 | MNLQDELDELKIYMTIDKTTIQELNRCMAEKREEQLFRHHEDAGVKKSTPEKNEKAISEQTLEKVIELENRLKSFEKNSRKLKEESKKLKKENDFLKSHLQHYQEDSESRGKELEKLLRVSSSVEQDKSELQTKVTALEREVTTLRRQVAKAKALRDENEEVVNPEEKEHCPTDKAKSEMATTDVRAQHCDCKTTTTKVKFKAAKKKCSVGRHHTVLNHSIKVMSHVENLSKDGWEDMSEGSSDSETQTFQNLGTVIVETSQNIRPIENDGNQKETDQTEDSRAQQEVQTYSCEDLKAPQNTKKMTFQNKSGSLQKNLHSALPARVNREKCKTKPAQKSSSNTILLRERIVSLQQQNSLLQNARKAAESSAKEFKEANEKLLHQQQISDHRFQTSRQTIKLTLDLAELRKEKEDLLKKVESSSDITSLAEEVSRIMAPQIQVTTLGPSRSTDLEIKQLQCKLKNATNELTKQSSSVKSLKLELLAKDDHMKAMQEKMSRMERDITMKRHLIEDLKFRQKINSESNESFNEMLGTLEKKDLKMNLLISKLNDTETAMAQIKSAASEQLQGLALQSEQVLEGTQKKLLLANEKIEEFTVFVQALVNELQSDAHRTRQQVRELRQTQKSRHACKTSTHKAQTLAASILNISRSDLEEILHTGDEMEIEKTKIDAENDKDWMLYIQKLLQGQLPFASYLLEAVLGKIKENKKLTEGYFTVMKDIK | Function: Required for centrosome cohesion and recruitment of CEP68 to centrosomes.
PTM: Phosphorylated directly or indirectly by NEK2.
Sequence Mass (Da): 82721
Sequence Length: 721
Subcellular Location: Cytoplasm
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Q12860 | MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENTYGAIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITDPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKENIHYQRNFMLDSNGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMEAARAVDLIPWMEYEFRVVATNTLGRGEPSIPSNRIKTDGAAPNVAPSDVGGGGGRNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMSPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWEHVLEKIVESYQIRYWAAHDKEEAANRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPPSDMIEAFTKKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKVLYRPDGQHDGKLYSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGAPTLSPSLLGLLLPAFGILVYLEF | Function: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 113320
Sequence Length: 1018
Subcellular Location: Cell membrane
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P0DM15 | RDCQEKWEYCIVPILGFVYCCPGLICGPFVCV | Function: MuO-conotoxins are gating-modifier toxins that inhibit sodium current by trapping the domain II voltage sensor in the closed position to prevent opening of the sodium channel. This toxin shows high activity on Nav1.4/SCN4A (IC(50)=81 nM) and Nav1.8/SCN10A (IC(50)=96-529 nM). It also shows low activity on other sodium channels (Nav1.5/SCN5A, IC(50)=431-3900 nM > Nav1.1/SCN1A, IC(50)=3.3 uM; Nav1.2/SCN2A, IC(50)=5.1-6.3 uM; Nav1.3/SCN3A, IC(50)=2.2 uM; Nav1.6/SCN8A, IC(50)=1.2-4.6 uM; Nav1.7/SCN9A, IC(50)=2.3-5.5 uM) . On Nav1.8/SCN10A, it causes a small left shift in the voltage dependence of activation and the voltage dependence of inactivation . In addition, it has been shown to interact with lipid membranes .
Sequence Mass (Da): 3654
Sequence Length: 32
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P13671 | MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIETKKRVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRSEYGAALAWEKGSSGLEEKTFSEWLESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEYAAKFDPCQCAPCPNNGRPTLSGTECLCVCQSGTYGENCEKQSPDYKSNAVDGQWGCWSSWSTCDATYKRSRTRECNNPAPQRGGKRCEGEKRQEEDCTFSIMENNGQPCINDDEEMKEVDLPEIEADSGCPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQRTECIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNSWTPPISNSLTCEKDTLTKLKGHCQLGQKQSGSECICMSPEEDCSHHSEDLCVFDTDSNDYFTSPACKFLAEKCLNNQQLHFLHIGSCQDGRQLEWGLERTRLSSNSTKKESCGYDTCYDWEKCSASTSKCVCLLPPQCFKGGNQLYCVKMGSSTSEKTLNICEVGTIRCANRKMEILHPGKCLA | Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
PTM: All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cysteine residues are supposed to have disulfide linkages only within the same module.
Sequence Mass (Da): 104786
Sequence Length: 934
Subcellular Location: Secreted
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P10643 | MKVISLFILVGFIGEFQSFSSASSPVNCQWDFYAPWSECNGCTKTQTRRRSVAVYGQYGGQPCVGNAFETQSCEPTRGCPTEEGCGERFRCFSGQCISKSLVCNGDSDCDEDSADEDRCEDSERRPSCDIDKPPPNIELTGNGYNELTGQFRNRVINTKSFGGQCRKVFSGDGKDFYRLSGNVLSYTFQVKINNDFNYEFYNSTWSYVKHTSTEHTSSSRKRSFFRSSSSSSRSYTSHTNEIHKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDSEKLKQNDFNSVEEKKCKSSGWHFVVKFSSHGCKELENALKAASGTQNNVLRGEPFIRGGGAGFISGLSYLELDNPAGNKRRYSAWAESVTNLPQVIKQKLTPLYELVKEVPCASVKKLYLKWALEEYLDEFDPCHCRPCQNGGLATVEGTHCLCHCKPYTFGAACEQGVLVGNQAGGVDGGWSCWSSWSPCVQGKKTRSRECNNPPPSGGGRSCVGETTESTQCEDEELEHLRLLEPHCFPLSLVPTEFCPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDGIQSHPQKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEMKNARCVQKENPLTQAVPKCQRWEKLQNSRCVCKMPYECGPSLDVCAQDERSKRILPLTVCKMHVLHCQGRNYTLTGRDSCTLPASAEKACGACPLWGKCDAESSKCVCREASECEEEGFSICVEVNGKEQTMSECEAGALRCRGQSISVTSIRPCAAETQ | Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C7 serves as a membrane anchor.
PTM: C7 has 28 disulfide bridges.
Sequence Mass (Da): 93518
Sequence Length: 843
Subcellular Location: Secreted
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P27658 | MAVLPGPLQLLGVLLTISLSSIRLIQAGAYYGIKPLPPQIPPQMPPQIPQYQPLGQQVPHMPLAKDGLAMGKEMPHLQYGKEYPHLPQYMKEIQPAPRMGKEAVPKKGKEIPLASLRGEQGPRGEPGPRGPPGPPGLPGHGIPGIKGKPGPQGYPGVGKPGMPGMPGKPGAMGMPGAKGEIGQKGEIGPMGIPGPQGPPGPHGLPGIGKPGGPGLPGQPGPKGDRGPKGLPGPQGLRGPKGDKGFGMPGAPGVKGPPGMHGPPGPVGLPGVGKPGVTGFPGPQGPLGKPGAPGEPGPQGPIGVPGVQGPPGIPGIGKPGQDGIPGQPGFPGGKGEQGLPGLPGPPGLPGIGKPGFPGPKGDRGMGGVPGALGPRGEKGPIGAPGIGGPPGEPGLPGIPGPMGPPGAIGFPGPKGEGGIVGPQGPPGPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGQKGVPGLPGVPGLLGPKGEPGIPGDQGLQGPPGIPGIGGPSGPIGPPGIPGPKGEPGLPGPPGFPGIGKPGVAGLHGPPGKPGALGPQGQPGLPGPPGPPGPPGPPAVMPPTPPPQGEYLPDMGLGIDGVKPPHAYGAKKGKNGGPAYEMPAFTAELTAPFPPVGAPVKFNKLLYNGRQNYNPQTGIFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPVMYTYDEYKKGFLDQASGSAVLLLRPGDRVFLQMPSEQAAGLYAGQYVHSSFSGYLLYPM | Function: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis.
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Sequence Mass (Da): 73364
Sequence Length: 744
Subcellular Location: Secreted
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Q83PC5 | MSIKEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHVVEEVRLRK | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 36388
Sequence Length: 316
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
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Q38WQ7 | MTERIALFPGSFDPFTKGHLDTVERASRLFDRVIIAVMTNAAKKPLFDGPTKVALIETVIADLDNVSVVAQPKTLTANFAQAVGARYLIRGIRNANDFEYERDIAALNQTQDAQLETVLLLAKQEFSFISSSMVKEIAAFGGQVDQLVPPAVAVALQEKLKHGRD | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18059
Sequence Length: 165
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
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Q5ZY26 | MQMVINEMKQKAIYPGTFDPVTNGHIDIITRASTIFPELIVAVASNKNKRPYLSWESRISLLEESVGHLTGVRVVGFDNLLIDFVLEQNAGIILRGLRAVSDFEYEFQLAGMNRKLSKKVETLFLTPAEHLMYISSTLVREIAALNGDISQFVPPNVVRELKKRQNERSL | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 19231
Sequence Length: 170
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
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B1MXS2 | MSIALFPGSFDPLTNGHLDIIERASLMFDKVVVGVGYNTGKKALFTPEEKLALISEVVSDLPNVEVAIMHGLTVQFMAEIGARFIVRGLRNSKDFEYERDIAGVNSALADVETILLLAKPENQNISSSMVKEIGSMGADNMAKFVPKVVVDALKERLN | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17211
Sequence Length: 158
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
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Q8ZL48 | MQKRAIYPGTFDPITNGHLDIVTRATQMFDHVILAIAASPSKKPMFTLDERVALAQKATAHLGNVEVVGFSDLMANFARDRQANILIRGLRAVADFEYEMQLAHMNRHLMPQLESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPDNVHQALMDKLK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17956
Sequence Length: 159
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
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O34932 | MTLVIGLTGGIASGKSTVANMLIEKGITVIDADIIAKQAVEKGMPAYRQIIDEFGEDILLSNGDIDRKKLGALVFTNEQKRLALNAIVHPAVRQEMLNRRDEAVANREAFVVLDIPLLFESKLESLVDKIIVVSVTKELQLERLMKRNQLTEEEAVSRIRSQMPLEEKTARADQVIDNSGTLEETKRQLDEIMNSWA | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22013
Sequence Length: 197
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q89YY6 | MAIKIGITGGIGSGKSVVSRLLEIMGIPVYISDIEAKRITHTNDVIRRELCALVGQDVFLNGELNRPLLASYIFGSPEHAKKVNAVIHPQVKEDFRRWVKGKGDIAMVGMESAILLEAGFKQEVDFVVMVYAPLEVRVERAIRRDYSSRELIMKRIEAQMSDEVKRNHADFVIVNDDETPLIPQVLKFISLLSKNNHYLCSAKK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22948
Sequence Length: 204
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q6G1B3 | MKIIGLTGSIAMGKSTAADFFKQAGISVFSADETVHQLYKSKPILSLIEHTFPGVVENGKVNRLKLSKILINDSEKLQTLEEIIHPLVQEKEKEFIDTARQQGKKIVVLDIPLLFEKKGEKRVDSIIVVSAPLAIQKERTMTRPDMNEKKFSFINAKQMPDEKKRERADFIINTGKDLENTHQQVFSIIENLLKN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22131
Sequence Length: 195
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q6MIK8 | MKWIGLTGGIACGKSTVSRMLRTHDIPVVDADEIAKEVVKPGSAGLKSVIQEFGPEFLTADGALDRRKLGQKVFGHPELLHKLEAITHPLIREETRRRRRLYEDMGHKLAIYDIPLLFETRAKDQFDGVIVVACTKEQQKERLRRQNWSEDEIEMRIASQIPIQFKEQQADFVLHNNRDEQHLLREVDRVLKWLEELKNQN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23343
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q8G5L8 | MGTMMRIGLTGGIAAGKSTVAARLKQLGALHIDYDALAHQIVEPGGVALPQIVAEFGPDALLADGTMNRPWIADHVFGANAAPGARERLDAIEHPLIYAEAARLEHEHPEAAIIIHDIPLLAEVIDDIPFAFDHIVTVEAPVCMRLDRMVEERGMSLEQAEARIRHQSSEEERRAIADIVIDSTHPLPEMLAQVGEIYAGWCAGR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22256
Sequence Length: 205
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q493P4 | MSYIVALTGGICSGKSVVAKKFSNLSKKVSVIDADVISKNITQPGSIALRMITKHFGPHILFSNGSLNRSMLKKIIFFNPKDKEWLEQLLHPLIRKETQKTINILSNRSSYILWVVPLLIENNLQKYADHILMIDVHVDIQLNRIISRDKIHKQYAENILLSQVSRQHRLNYADNVIENNKSIDGMTQHIHNLHRDYLKAEKTTTKKTIFSK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24382
Sequence Length: 212
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q2KUM5 | MLRIGLTGGIGSGKTRVADKLGEWGAAVIDTDAIAHALTQADGLAMPAIIQAFGPEAVRADGAMDRAWVRNRVFREPQARACLEAILHPLIGQETQAAAERAVGSYLVFVVPLLVESGRWRGQLDRICVVDCDPETQIKRVQNRSGLTESDIRRIMDAQAARATRLKAADDVIVNDGSTTAEVLLARARSLHQSYLALADKHDRHGSTEAGPP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22923
Sequence Length: 213
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q7WF46 | MYKIGLTGGIGSGKSRVADMLAEWGASVIDADEISHALTAPGGAAMPAIAREFGPQAVAADGALDRAWMRDLVFREPAARGRLEALLHPLIGLHTEQAAAQARGLYLVFVVPLLVESGRWRGRVDRICVVDCDPATQIARVQKRSGLTEPAIRRIMAAQAARATRLEAADDVIVNDGATSPDTLRARARTLHDRWLALAGAASQPGGKAAGTPE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22588
Sequence Length: 214
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
O51497 | MGRNPLIIGVTGRIASGKDTVSKIISNKYGFYEINADKLGHSVLHEKKEEIVKIFGQKILNTKNEIDKLLLRNLVFNDNKELKKLESVSHPVILSKIKKILIQNQSTKIIINAALLFKMNLEKLCDYIIVLKAKNSIIKNRLSYSIPNIDSNMINKILKIQKDIFFEKNIINLKIINIINNKNYAYLEKEIEKKMQGIINYERFE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23729
Sequence Length: 205
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
P57299 | MTYIVALTGGISSGKTTISNGFKKIGINVIDTDIIAKNIIEKNLQVSFSIKRKFGKKILNIDNSINRLLLRQYVFNNHHHRLWLENLLHPKIYQESKHQIKMTQSNWCLWVVPLLVEKKLEKKAHRILLIDTPVKEQIKRTVRRDKISFLEAKKIIALQSSRKTRISLSDDIIFNKKNFKKINLYIYYFNLLYSHLSRIYNKNKTINIKKNFLTKFY | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25718
Sequence Length: 217
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q9X1A7 | MVIGVTGKIGTGKSTVCEILKNKYGAHVVNVDRIGHEVLEEVKEKLVELFGGSVLEDGKVNRKKLAGIVFESRENLKKLELLVHPLMKKRVQEIINKTSGLIVIEAALLKRMGLDQLCDHVITVVASRETILKRNREADRRLKFQEDIVPQGIVVANNSTLEDLEKKVEEVMKLVWEKRE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 20331
Sequence Length: 180
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q72K90 | MGHEAKHPIIIGITGNIGSGKSTVAALLRSWGYPVLDLDALAARARENKEEELKRLFPEAVVGGRLDRRALARLVFSDPERLKALEAVVHPEVRRLLMEELSRLEAPLVFLEIPLLFEKGWEGRLHGTLLVAAPLEERVRRVMARSGLSREEVLARERAQMPEEEKRKRATWVLENTGSLEDLERALKAVLAELTGGAKGGRG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22590
Sequence Length: 203
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q8DKG1 | MSRLLRLGITGGIACGKSVVAGYLQRQYGVPIVDADVLARQVVAVGTPIYQAIVDRYGDGICRRDGTLDRSRLGEIVFAQPQERQWLEAQIHPAVVAEMEQAMATCDQPLMALVIPLLFEAHLEGLVDHIWVVATPPEQQLARLQQRDRLSAHAAGQRLASQLPLEEKIRRADTVLWNTGSLEELYRQVDQAFSLLGRGGKGG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22346
Sequence Length: 203
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q3SGD0 | MFTIGLTGGIGSGKSAAAERFAELGVPVIDTDVIAHELTRPGSRALDVIRASFGEAVIAADGSLDRPVLRRRVFVDPAARRQLEAILHPLILHEVKARLASLSGPYAVAVIPLLVETGAYDAPVDRIAVVDCPEELQIARTIARSGLTPDEVGAILAAQAARPARLAVADDVIVNTGSLAALRDQVDALHQRYLTLAANRLP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21303
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q73M71 | MDSVLNGRQSRQSLDAPSEPILIGLSGPSCSGKNTASTILQDYGFYCIDADAVSRKVFTEHEKEILNLFQAEAEKRGINLKNENGIDKKAFALLVFSDEELLKKHEAFILPIIEEKIWEEIKRAFTEKPERPILLNAPTLHKTSFIKKCLFILYIDAPFILRLIRAKKRDRLPLKNIWLRFSKQKKFFSQYFFLNADTIVVKNFWSSASLKRKLLQEVKKRGF | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25840
Sequence Length: 223
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
O83319 | MREFCPLIGVIGRSGAGKNVVSRLLAERGCYCIDADARTRELLESYGDSIVERFQVAAAARGLSLRRKDGGLHSAHLGVLLFSEPKLLQQHEEFLLPKVTRLLCEDIARAQAARPKAIVLNAPTLHKTELLQACSFVLYIWAPSILRMWRCKKRERVSFTHLLRRFSAQKGFYAQSIAQNADTYTVANCGRVASLARKVDCILTRRGVLGE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23584
Sequence Length: 211
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q9KPE3 | MSFVVALTGGIASGKTTVANLFHDQFGIDLVDADVIARDVVKPETEGLKAIAAHFGQAILHPDGSLNRAALRERIFAAPNEKAWLNQLLHPMIRQGMRNALTQTTSPYALLIVPLLVENQLQTMADRVLVVDVDEKIQIERTMARDKVSREQAEAILAAQASRAQRLAIADDVLKNDAENQKLLPQITLLHQKYLAMSRQNL | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22307
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q8D308 | MLINSPYIVAMTGGIGSGKSTIAKIFSELKVPIIESDIISKKIMFSEKSILNSIKNKLGINFSLNNNKYSKLVLRECIFESKSSVLFINKILHPVVKKKIKKIISNVNFPYIIWVTSLLIEENLYKYVNRILVIDVDPEIQIKRSILRDNVSKNQILNIINFQISREKRLTFAHDIINNYDYSCIRRKVFELHKYYLFKSKKYFKYDM | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24396
Sequence Length: 208
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q7M7Q5 | MESLHYAIALSGGIGTGKSTVASLLRLYGFEVIDADSIAHRLLKEKQKEVVDLFGEGILKEGEIDRKSLGARVFGDPKERARLEALLHPPIRQEILQKAQKLEAKAFPYFIDIPLFFEKRDDYPMVNQTLLIYAPRKLQVERIKKRDSLSMEEIEARLGAQMDIKEKVPMAHYILSNEGNLNDLTQEVERLIETIKKDFHV | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22989
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q5GT26 | MIIGLTGGIGVGKSFIANCFKEFGAAVFDADFIVHQLYRVDKNIISYAEKNFPGAIANGEIDKTVLSKYFLDYDENWKQFQSLVHSAVQNELEIFIAQDKEINRKLLVLDVPLLLETRFHLYCDFIIFIYADSAAQAQRLSERNIDKEKLDLISSIQLPVKEKRQMSDFTIDTSTSKEHVLSQVKDIVDSLSLSS | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22132
Sequence Length: 195
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q8PHK7 | MSDFIVGLTGGIASGKSALAAEFEKLGVPVIDADVIARQVAEPGPILDAIAAYFGDSVLLPDGTLNRQALRYRVFADTAQRQALEAITHPAIRRELQRAALAAQGPYAIVAIPLLAEAGGRATYPWLDRILVVDVPVALQHERLMQRDGATAELADRMITAQATREKRLAIADEVVCNHGVLKQLSQAARRLDADYRARANP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21757
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
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Q7P0S9 | MKLLIDAGNSRVKWALYQGEDCVRQGAAEHGELAGLAAVWRDLPLTGAWMSSVARREVADALAAAVPCPLHRVHAERRFGDVRNHYRNTAEQGADRWLAVLAARELCRGDVIVACAGTALTVEALTAEGDYLGGLILPGHGLMLQSLAQGTANLNRPAGEVVDFPQGTQDALASGAIAALAGAIAEQRRRLAERTGRAPATVILTGGDAARIAPWLAAPMQIVDNLVLMGLLKVANT | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 24952
Sequence Length: 237
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q97EB4 | MILVLDVGNTNIVLGIYNDTKLTAEWRLSTDVLRSADEYGIQVMNLFQQDKLDPTLVEGVIISSVVPNIMYSLEHMIRKYFKINPLVVGPGIKTGINIKYDNPKEVGADRIVNAVAAHEIYKRSLIIIDFGTATTFCAVRENGDYLGGAICPGIKVSSEALFEKAAKLPRVELIKPAYAICKNTISSIQSGIVYGYIGQVRYIVERMKEELQEEGEKEPLVVATGGLAKLISEEAKNVDVINPFLTLEGLRIIYEKNRVKVI | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 29049
Sequence Length: 262
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q181F7 | MLLVFDVGNTNMVLGIYKGDKLVNYWRIKTDREKTSDEYGILISNLFDYDNVNISDIDDVIISSVVPNVMHSLENFCIKYCKKQPLIVGPGIKTGLNIKYDNPKQVGADRIVNAVAGIEKYGAPSILVDFGTATTFCAISEKGEYLGGTIAPGIKISSEALFQSASKLPRVELAKPGMTICKSTVSAMQSGIIYGYVGLVDKIISIMKKELNCDDVKVIATGGLAKLIASETKSIDYVDGFLTLEGLRIIYEKNQE | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27939
Sequence Length: 256
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
C5BPP8 | MKLLVDAGNSRIKWWVPECQAHGVVDRLALDDLAGEIAAVIDISKLSSVRVSCVAGKSIETQLRGELGFARDLDVKFARVSSPLPILTVAYREIHRLGVDRWLAMLAVREKFPDRFCAVLDAGSAVTVDFVTEAGVHEGGMIVPGVQTMARALWSNTSDVAVERLELVPRWCPGVDTYDCVRQGVSALYTGLVNEVHSYIDGSAERHLSPAIVVTGGDRHWFTQAFSSPVVVDPHLVLKGLLVLDELEK | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27199
Sequence Length: 249
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q9WZY5 | MYLLVDVGNTHSVFSITEDGKTFRRWRLSTGVFQTEDELFSHLHPLLGDAMREIKGIGVASVVPTQNTVIERFSQKYFHISPIWVKAKNGCVKWNVKNPSEVGADRVANVVAFVKEYGKNGIIIDMGTATTVDLVVNGSYEGGAILPGFFMMVHSLFRGTAKLPLVEVKPADFVVGKDTEENIRLGVVNGSVYALEGIIGRIKEVYGDLPVVLTGGQSKIVKDMIKHEIFDEDLTIKGVYHFCFGD | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27154
Sequence Length: 246
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
B9L0J2 | MLMVIDIGNTNVVVGLFAGHELRARWRLATARDRMPDEWWVQLNVLSQSAGFSLGEVVGIAISSVVPSLTATFQELAQRYLLVEPLIVNGAQDYGLPVRVEHPAEVGADRICNAIAAVERYGAPVIVVDFGTGTTFDVIDADGAYIGGAIAPGITIAFEALTQRAARLYTVALQAPPRAIGRNTRESLQSGTVLGYAELVRGLIRRIRSELGHEAPAIATGGLATLIAPLVPEFSAVEADLTLYGLRSAYERMHRSLGA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27691
Sequence Length: 259
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q5SIJ5 | MLLAVDIGNTSTALGLFSGEELIAHFRIHTDRMRMESEYRVILKNLFALEDLPPPKAALLASVVPPVEREMKRAIERLFGVEARVVEAADTGLEVLIDNPREAGADRLVNAVGALAYPSPTGRYIVVDFGTATTFDLVEAPNRYLGGAIAIGPQTAADALAQRTAKLPRIDLTPPKAAVGKNTLEALRSGLVLGYAALVEGMVRRFKEEAGEALVIATGGFAETLRPLCPCFDVVDEDLTLKGLLRIHLGRG | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27055
Sequence Length: 252
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q8DJS3 | MVPPETNQWFALMIGNTRQHWALFRGEHLSRTWHLTPEELACNPAQDYPNLPCWGASVGSVPLHQVYPRAIALTLEDIPLPQMYPTLGLDRALALWGALQVYGAPVCVVDAGTALTLTLANDRREFAGGVILPGVGLMARALADYTAALPYVPLPTEPPRRWGTTTTTAIASGLYYGTAAILQAYLDAFLQEFPQGTVIVTGGDRPFVSELLRTFLDSDRWCEDDHLVFWGIRALRNPAAKIEMHPMERIDEFH | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28166
Sequence Length: 254
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q3SLJ6 | MSGCRILLDAGNSSLKWAVVEDGTWLARGRSDYSDLSAVEAELDAGSECFIASVASRVYEEKLAALLTAAGCSAVWLKSEAAFDDVTNDYRDPTQLGVDRWMGLVAARARRRAPTLVVSAGTAMTVDALSGDGSFLGGLIVPGVALMQRSLQQGTAGGAAAGGAWQAFPRCTADAAYSGIIAALCGAVEGQHVRLAAHEGISPACLITGGGAETLLPHLGVDAEHVPTLVLEGIERVARAGGRG | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 25010
Sequence Length: 244
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
O83446 | MLLIDVGNSHVVFGIQGENGGRVCVRELFRLAPDARKTQDEYSLLIHALCERAGVGRASLRDAFISSVVPVLTKTIADAVAQISGVQPVVFGPWAYEHLPVRIPEPVRAEIGTDLVANAVAAYVHFRSACVVVDCGTALTFTAVDGTGLIQGVAIAPGLRTAVQSLHTGTAQLPLVPLALPDSVLGKDTTHAVQAGVVRGTLFVIRAMIAQCQKELGCRCAAVITGGLSRLFSSEVDFPPIDAQLTLSGLAHIARLVPTSLLPPATVSGSSGN | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28472
Sequence Length: 273
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q3MC63 | MISQQFPKHVENQWLALEIGNSRLHWALFMGESLKFTWDTEYLPESVIQQLGNGETNWELGTGEKGISSSTFPPLPPAPCPSGSQSLMGETPKTELSHPLPLFIASVVPKQTALWQSYPNVRVITLDQIPLNNTYPTLGIDRALALWGAGMSWGFPMLVIDAGTALTFTAADGERNLVGGAILPGVGLQFASLGQKTEQLPQVEMAEIKSLPPHFALNTAEAIQSGVIYTLIAGIRDFTEEWLSLFPDGKVAIKGGDRILLLNYLQALYPELAGRLIVEPNMIFWGMQTIVAGVA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 32142
Sequence Length: 295
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
A1WJV9 | MTFLAIDVGNTRLKWALYDAPRAGAALRAHGVEFLDHIDRLAEGSWARLPPPGHMLGCVVAGDAVKRRVQEQMEIWDVTPSWVVASAQEAGLSNGYDHPSRLGADRWVAMIGARQHVLARGPARPLVLVMVGTAVTVECVDAQGRFIGGLILPGHGIMLRALESGTAGLHVPTGEVRLFPTNTSDALTSGGTYAIAGAVERMVQHVIAHCGTEPICLMTGGAGWKVAPSMTRPFELLENLIFDGLLEIAMRRLAAA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27312
Sequence Length: 256
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q7MS38 | MLLCDIGNTYLHFYQEGKVWKELPRRLKAGMEVQEVYYISVNPPSARRLLEVYPHAIDLAPHMVLDTAYKGLGVDRMAACKGIEDGVVVDAGSAITVDVMQNQVHLGGFIMPGIASFSSMLKSISPALEKELNLSVELSALPQNTRDALSYGAIKAIVMMIQNSCKNKRLFFTGGDGKYLARFFENAIHDNSIVFKGMLKTLEEMKEGKR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 23319
Sequence Length: 210
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
O68098 | MTRLLVLGGTTEASRLAKTLADQGFEAVFSYAGRTGAPVAQPLPTRIGGFGGVAGLVDYLTREGVSHVIDATHPFAAQMSANAVAACAQTGVALCAFERAPWTAQAGDRWTHVPDLAAAVAALPQAPARVFLAIGKQHLRDFSAAPQHHYLLRLVDPPEGPLPLPDARAVIARGPFTVQGDTELLRSETITHVVAKNAGGAGAEAKLIAARSLGLPVILIDRPAVPARDICATLEGVMGWLADHGATPRGV | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 26048
Sequence Length: 251
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 6/10.
EC: 1.3.1.54
|
Q53139 | MTRILILGGTGEARALAAALADVPGVEAVSSLAGRVRDPRLPVGDVRIGGFGGADGLAECVRAHPVDAIVDATHPFAAQITRNAADAAHRRGIPLVVLRRPEWSPRPGEHWHGAADLADAAELLPDLGTRIFLTIGRQGVDAFADLQALWFLIRAIDPPDVAMPPHSTLLLARGPFAVADETALMREHRIDVLVTKNSGGGQTDAKLDAARALGIPVLMIRRPPLPPATETVDDVAGAIAWVGTLTRR | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 26142
Sequence Length: 248
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 6/10.
EC: 1.3.1.54
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Subsets and Splits