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Q27490 | MARTKHTARKSFGGKAPRKSLATKAARKVFPVDGQVKKRYRPSSNALKEIRKYQKSTELLVRKLPFQRLVREVAQEIMPNVRFQSAAIQALHEAAEAYLIGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERG | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
PTM: Acetylation is generally linked to gene activation.
Sequence Mass (Da): 15286
Sequence Length: 134
Subcellular Location: Nucleus
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Q27532 | MARTKQTARKSTGGKAPRKALATKAARKSAIVTGSVKKVHRFRPGTVALREIRRYQKSTELLLRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERS | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
PTM: Acetylation is generally linked to gene activation.
Sequence Mass (Da): 15349
Sequence Length: 136
Subcellular Location: Nucleus
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Q27489 | MCPGGKAPRKQLATKAARKNAIVVGAVKKPHRFRPGTVALREIRRYQKSTDLLLRKLPFQRLVREIAQDVKQDLRFQSAAIQALQEASEYFLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERN | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
PTM: Acetylation is generally linked to gene activation.
Sequence Mass (Da): 14523
Sequence Length: 127
Subcellular Location: Nucleus
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P59169 | MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9acK14ac molecules are 30-fold less abundant than H3K9ac or H3K14ac. Very low level of H3K9meK14ac. H3K14 is specifically acetylated by HAG1 and deacetylated by HDA6. H3K9ac is deacetylated by HDT1. H3K9ac is restricted to euchromatin. H3K18ac, but not H3K9ac, is cell-cycle dependent and linked to replication. Reduced H4R3me2s increases H3K14ac in the FLC chromatin and activates or maintains its transcription. Vernalization decreases H3K9/14ac in the promoter region of FLC.
Sequence Mass (Da): 15406
Sequence Length: 136
Subcellular Location: Nucleus
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Q8J1L3 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALIYEETRSVLKTFLESVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Sequence Mass (Da): 11398
Sequence Length: 103
Subcellular Location: Nucleus
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P84040 | MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylated on Lys-6 and Lys-13 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H4 Lys-6 acetylation but not for H4 Lys-13 acetylation.
Sequence Mass (Da): 11381
Sequence Length: 103
Subcellular Location: Nucleus
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Q89443 | MGKPTLLEPGHLYNVPAEHKNDVPIHYIITWIKQRLPEFGGAIPTSLADRVLIIKSRTGSGKSTALPVHVFRILRNENTHSFQKYLGRSVICTQPRVLTAVTLAKDIGASTHYPDMILGQTVGYHTKPLTEKPNRGLIYATAGVLLAQLHTMTDDEIASRYAFMIIDEAHERALGIDLMLMYIKSMLQRMLQRGSIGALRIPFVILTSATIDTHKYSTYFGIGKENIILVEGRQYGVETHWPLYNTNNYIKTACETALTIHKENIHDRPTEADILIFMPGMAEIRFLSMLLNNANMDLAKEKLPLMLILPIDSEAIAQENEAYLGLKAEIKNLWVKNPLTAKVEKPLRRVIVSTVVAETGLTIETLKYVIDPGWNRSIETYYPEWAGGLITRPAAQSRIEQRKGRVGRVFPGHFYPLYTKHVFEQIPAQQYPEIITEGPGAIFLSIVVETIKKNKEGVFKAEEIDMLDPPPTDALASAIERAIVAGLLTRGEKGLQLTQLGDIASRFSFLSIEEARMCFSGYFWQAAISDIATILAVVSVADKKLTNLLDSKQRNGAMLAEAVLAGIPPFLQNIDNAYTNIHLLLADDLLEGLFIFEGFQHAIVYFINNKVNNVAKHLREWCEKKMLKYSSMVQILARREDILNELAIVGLNPFHQWQNRLASANAETFLKRVCTLKQCMYEAYRLNCFCYDKHRLLYTGRNGIHFSYHDAVIKNPSCIVTPRIMLSPVSKQYMEWRLEPSFVSVLDGFVNVDINFLSPRQEIPNILGGVEDEEEEPPLPIQVFLHKYVKTHFHFSGKSFKELKMKPSQMIKFPETTLINMIPDIPKNVVQTYLEINVCHQYSFKRLIYCETFYTDMDDVQHENSVELIGLPMAAHHLTINDFNKLYHLLKPDGFLIVYDLHKGQEAFWLHSLQDALGHHTIRRDMDFHTIPEWETIFKECGFTPIFSKQPSEHELFIVFKK | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 109630
Sequence Length: 962
Subcellular Location: Host membrane
EC: 3.6.4.13
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P83716 | MKEDNNTSEESGRINRRNVLKTVGAAGLFAAGSTGMAAAADSLSQAEEPKLLTGTEKRTLARELAKTPAFRELAQRARADGAQIRSDADSIVAGYARGEDFAREVVQYDLENLTDAAEASIVIGRNPETGEIEVANLDYYYETDDGVLDEVHRFEPTNASETDGVQSAATSDGATVIAVDTDAIREAQNSEIDVDESSPSNAAPTPADIDITGCSACKYAAGQVCTIGCSAAGGFICGLLGITIPVAGLSCLGFVEIVCTVADEYSGCGDAVAKEACNRAGLC | Function: Has antibacterial activity against a wide variety of haloarchaeons. Causes cell lysis and death, possibly by disrupting the cell wall .
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 29379
Sequence Length: 283
Domain: The helix-loop-helix (HLH) region is essential for immunity function of Immunity protein HalI and interaction with Halocin-C8.
Subcellular Location: Secreted
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Q8TLF1 | MLFDYRKGGLFLGTISEKIFSRAAGTEAKANDFVLADVDYAMAHDGTSVLAVNAFKEMEMEKVWDPSRIVVPFDHIAPANNETSATLQREIREWVKEQGIPNFYEVGEGICHQVLPENGFALPGKLVVGADSHSCTYGAFGAFATGVGATDMAEIFATGKLWFKVPESFRMTVEGSLRKGVYAKDLTLYLIGKTGIAGATYKAVEFYGQAIRELTVAGRMTLCNMAIEMGAKTGIVPPDEKTFEFLKNRAAATYEPVYADPDAVYLEEFTYDADDIEPQVACPHQVDNVKPVGEVEGTHVDQVFIGTCTNGRLEDLEVAAAVLKGKQVAVRTIVIPASRTTLLAAIENGTMETLLKAGVTLATPGCGPCLGAHQGVLGEGEVCVSTANRNFKGRMGKGGFIYLASPATAAASALTGEITDPRTV | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate. These reactions are part of the biosynthesis pathway of coenzyme B.
Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate
Sequence Mass (Da): 45377
Sequence Length: 424
Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
EC: 4.2.1.114
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Q58409 | MTLVEKILSKKVGYEVCAGDSIEVEVDLAMTHDGTTPLAYKALKEMSDSVWNPDKIVVAFDHNVPPNTVKAAEMQKLALEFVKRFGIKNFHKGGEGICHQILAENYVLPNMFVAGGDSHTCTHGAFGAFATGFGATDMAYIYATGETWIKVPKTIRVDIVGKNENVSAKDIVLRVCKEIGRRGATYMAIEYGGEVVKNMDMDGRLTLCNMAIEMGGKTGVIEADEITYDYLKKERGLSDEDIAKLKKERITVNRDEANYYKEIEIDITDMEEQVAVPHHPDNVKPISDVEGTEINQVFIGSCTNGRLSDLREAAKYLKGREVHKDVKLIVIPASKKVFLQALKEGIIDIFVKAGAMICTPGCGPCLGAHQGVLAEGEICLSTTNRNFKGRMGHINSYIYLASPKIAAISAVKGYITNKLD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Cannot catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.
Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate
Sequence Mass (Da): 46063
Sequence Length: 420
Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
EC: 4.2.1.114
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Q9ZNE0 | MGQTLAEKILSHKVGRPVRAGELVVVEVDQVMVVDSIAGSFFKRLEYLEATPRYPERVSIVIDHVAPAANLEVAKAQKEIREWGKRHGIRVFDVGRGVCHQVLIEEGLAQPGWVVVGSDSHSTTYGAVGAFGTGMGATDIALAAASGRTWLRVPESVKVVFRGRLPKGVTAKDAALEMVRLLTAEGATYMAVEIHLLDGAEALTRGERMTLANLTVEAGAKAGLVVPSGEILEMYRVPDWLYPDPDARYAKEVEIDLSALTPRVSVPFYVDNVHEVAQVKGKRVDQVFIGTCTNGRIEDLRAAAEVLRGRKVAPWVRLLVVPASSQVLEEAARDGTLLTLLEAGATIGTPGCGPCMGRHMGVLAPGEVCVSTSNRNFRGRMGAPDAEIYLASPRVAAASAVAGYLTTPEELEEEEVHA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the reversible hydration of cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate) to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Can catalyze neither the dehydration of (R)-homocitrate ((2R)-2-hydroxybutane-1,2,4-tricarboxylate) into cis-homoaconitate in vitro, nor the reverse reaction. Is not active toward (S)-homocitrate, cis-aconitate or citrate as substrate.
Catalytic Activity: (2R,3S)-homoisocitrate = cis-homoaconitate + H2O
Sequence Mass (Da): 44819
Sequence Length: 418
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
EC: 4.2.1.36
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Q8TRF7 | MANPIVGRVWKFGDDINTDAIIPGKYLRTRDMQIFGTHAMEGIDPEFTKKAKPGDIIVAGTNFGCGSSREQAPLALKHSGIACIVAKSFARIFFRNAINIGLPLMEADVECQEGDEIKVDLFKGEVLVPEKGIFKGNKLPDFLLDILNDGGLVAHRKKVKGEHK | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate. These reactions are part of the biosynthesis pathway of coenzyme B.
Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate
Sequence Mass (Da): 17963
Sequence Length: 164
Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
EC: 4.2.1.114
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Q58667 | MIIKGRAHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDENFPKKVKEGDVIVAGENFGCGSSREQAVIAIKYCGIKAVIAKSFARIFYRNAINVGLIPIIANTDEIKDGDIVEIDLDKEEIVITNKNKTIKCETPKGLEREILAAGGLVNYLKKRKLIQSKKGVKT | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Cannot catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.
Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate
Sequence Mass (Da): 18665
Sequence Length: 170
Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
EC: 4.2.1.114
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O26917 | MEGIIRGRVWRFGDNVDTDMIIPGRYLRTFSLDELASHVMEGARPEFASQVRKGDIIVAGRNFGCGSSREQAPVALKHAGVVAIIAESFARIFYRNAINIGLPVIMAKVDADDGDEVSIDLRSGQIRNLTAGSEYRMKPFNDYMLSILEDGGLVNHYLKTIDTGISGDEG | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate. These reactions are part of the biosynthesis pathway of coenzyme B.
Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate
Sequence Mass (Da): 18651
Sequence Length: 170
Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
EC: 4.2.1.114
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Q9ZND9 | MPRVWKFGDQINTDDILPGKYAPFMVGEDRFHLYAFAHLRPEFAKEVRPGDILVFGRNAGLGSSREYAPEALKRLGVRAIIAKSYARIFFRNLVNLGIVPFESEEVVDALEDGDEVELDLESGVLTRGEERFALRPPPPFLLEALKEGSLLDYYKKHGRFPGE | Function: Catalyzes the reversible hydration of cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate) to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Can catalyze neither the dehydration of (R)-homocitrate ((2R)-2-hydroxybutane-1,2,4-tricarboxylate) into cis-homoaconitate in vitro, nor the reverse reaction. Is not active toward (S)-homocitrate, cis-aconitate or citrate as substrate.
Catalytic Activity: (2R,3S)-homoisocitrate = cis-homoaconitate + H2O
Sequence Mass (Da): 18468
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
EC: 4.2.1.36
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Q4W1W1 | MASSEEDGTNGGASEAGEEKEAPGRRRRLGLLATVWLTFYNIAMTAGWLVLAIAMVRFYMEKGTHKGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVAGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVVGELLTIYAALPYVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 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 in 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
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28731
Sequence Length: 249
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.2.1.134
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B0YJ81 | MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 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 in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 32388
Sequence Length: 288
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.2.1.134
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Q8TF76 | MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPKGRIVPRGIDRLERTRSSRKSKHQEATETSLLHSHRFKKGQKLGKDSFPTQDLTPLQNVCFWTKTRASFSFHKKKIVTDVSEVCSIYTTATSLSGSLLSECSNRPVMNRTSGAPSSWHSSSMYLLSPLNTLSISNKKASDAEKVYGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK | Function: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle.
PTM: Autophosphorylated on both serine and threonine residues (By similarity). Strongly phosphorylated during mitosis but this does not appear to significantly affect its intrinsic kinase activity. Phosphorylation by AURKB is required for full activity toward histone H3 at 'Ser-3' in mitosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 88495
Sequence Length: 798
Subcellular Location: Nucleus
EC: 2.7.11.1
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O13924 | MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY | Function: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 56521
Sequence Length: 488
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9Z4Z7 | MKTESDVQTGAPTAADGALIALAREVCPGFAPGEVVYRSRTSLVVGGELDGVEALAKVRTPDWRRQCLREIDTYDLFDAVPPPVPVPRRFASDRERAVLVMERLTGEVLAPDRFPVTPVSREDLAGVLEAVERLRHWRPAAAGAWAVDYRGMLEGVHAQGVFDDGHWADLLRLLELSGAPREFGHGDLVLANVVRSRGRQVLIDWASSALYLPGLDLAQLWMLLGDVPGARARIEVEVADRADDRDGMMPFLVNLTLLLYRERRAHRRFTDDASRARAVGLDAAWELTRHRVRQCLATAG | Function: Phosphotransferase that is responsible for the production of the 3-phosphohydroxyasparaginyl residues found at position 9 in the non-ribosomally synthesized calcium-dependent antibiotic (CDA) derivatives CDA1b and CDA2a/b. It is not known whether the phosphorylation reaction takes place before, during or after peptide assembly.
Sequence Mass (Da): 33186
Sequence Length: 300
Pathway: Antibiotic biosynthesis; calcium-dependent antibiotic biosynthesis.
EC: 2.7.1.-
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Q7BLV3 | MNTLSQAIKAYNSNDYQLALKLFEKSAEIYGRKIVEFQITKCKEKLSAHPSVNSAHLSVNKEEKVNVCDSPLDIATQLLLSNVKKLVLSDSEKNTLKNKWKLLTEKKSENAEVRAVALVPKDFPKDLVLAPLPDHVNDFTWYKKRKKRLGIKPEHQHVGLSIIVTTFNRPAILSITLACLVNQKTHYPFEVIVTDDGSQEDLSPIIRQYENKLDIRYVRQKDNGFQASAARNMGLRLAKYDFIGLLDCDMAPNPLWVHSYVAELLEDDDLTIIGPRKYIDTQHIDPKDFLNNASLLESLPEVKTNNSVAAKGEGTVSLDWRLEQFEKTENLRLSDSPFRFFAAGNVAFAKKWLNKSGFFDEEFNHWGGEDVEFGYRLFRYGSFFKTIDGIMAYHQEPPGKENETDREAGKNITLDIMREKVPYIYRKLLPIEDSHINRVPLVSIYIPAYNCANYIQRCVDSALNQTVVDLEVCICNDGSTDNTLEVINKLYGNNPRVRIMSKPNGGIASASNAAVSFAKGYYIGQLDSDDYLEPDAVELCLKEFLKDKTLACVYTTNRNVNPDGSLIANGYNWPEFSREKLTTAMIAHHFRMFTIRAWHLTDGFNEKIENAVDYDMFLKLSEVGKFKHLNKICYNRVLHGDNTSIKKLGIQKKNHFVVVNQSLNRQGITYYNYDEFDDLDESRKYIFNKTAEYQEEIDILKDIKIIQNKDAKIAVSIFYPNTLNGLVKKLNNIIEYNKNIFVIVLHVDKNHLTPDIKKEILAFYHKHQVNILLNNDISYYTSNRLIKTEAHLSNINKLSQLNLNCEYIIFDNHDSLFVKNDSYAYMKKYDVGMNFSALTHDWIEKINAHPPFKKLIKTYFNDNDLKSMNVKGASQGMFMTYALAHELLTIIKEVITSCQSIDSVPEYNTEDIWFQFALLILEKKTGHVFNKTSTLTYMPWERKLQWTNEQIESAKRGENIPVNKFIINSITL | Function: Catalyzes the polymerization of hyaluronan, a polysaccharide composed of a repeating disaccharide of N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcUA) units. Each unit has the composition in beta-(1->4)-GlcUA-beta-(1->3)-GlcNAc.
Catalytic Activity: [hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 111839
Sequence Length: 972
Subcellular Location: Cell membrane
EC: 2.4.1.212
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Q4X0W8 | MALILERLYLLSSPRNAIIRNTRSEAGRELIFSFGLPSLSLPSCIASQYGKRRRLYFTTQLHVNSFLHWTCDANDAVNITLVQPDEQKLKTVSSFHPQFTYPIFGDDERIFGYKGLIIRLRFAAHDLRPQLHISYDEKFKPVEDIAAVDIPKTLKPWIPEDAFVTLPDYEKAVLEDKAAKDFKPPGKLVHCYVSRNRNFEIWAGSLADPEVRRLLDRAQIFVSLFIEAGTPLATDDPEWTLQRWTVYFVYEIVKPPTPTASKYSIVGYATTYRWWHYRRDRTQVPVVKNDPFPSGPEIHPSQLPSRLRIAQFLILPPHQNSGHGRHLYTAIHSACVQDPSVVELTVEDPNEAFDVLRDSADYHILRPEFIKHEVNINPDPYEAHSRNQRPRRVPTAALIPVKLLHDIRTSYKIDSTQFAHILEMFLLSQIPLKNRHAGGANMSRLLIKKHRAEDPNERRYYWWRMLTKQRLYKRSKDILIQLDLDERIQKLEETVSNVEEGYEVLLKEFSEREEKLKARGVVESPAATVSDDASAGPSGTSRDQRVKRKFTVEDDEDKVEEEDTAKRTKV | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 65962
Sequence Length: 570
Subcellular Location: Cytoplasm
EC: 2.3.1.48
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Q2UEX1 | MASEGDWTCDANDAVQITLVQPGEQKPKTLSSFHPQFTYPIFGDDETIFGYKGLIIRLRFAAHDLRPHIHISYDEKFKTVGDTSAVDLIKTLSPFIPEEAFSTLPDYENAVQEDKDAKDFVPPGKLVHNYVTRGRTYEIWAASLADPQVRRLLDRAQVFVSLFIEAGTPLETEDPEWTLERWTVYFVYEKVKPPTPTASQYSIVGYATTYRWWFYQRDSPEKGTVTNDPFPGPEIRPAQLPARLRIAQFLILPPHQGSGHGTHLYTTIHTACFNDSTIVELTVEDPNEAFDALRDTADFHILRPEFLKHNVNINPDPYAELSKKQRPRRVPTSALIPTKLLHDIRSTYKIASTQFAHVLEMFLLGEIPTKNRHAGGANMSRLLVKKYNATDPNERRYYWWRMLVKQRLFKRSRDILIQLEMSDRIEKLEETVTNVEEGYEALIKVFTAREEALMAKQEESGESPETAVLEDSVASSSDSSTRDQRTKRKFTVEDEDEEEEGESEVSKRPKV | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 58620
Sequence Length: 511
Subcellular Location: Cytoplasm
EC: 2.3.1.48
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Q59VF4 | MSSAKEQSSVTAALQPEQWTTSSNEALKLFVTNPEAALNFQPTFTYPIFGDAETIYGYKDLDIFLCFDHYTFKPFLNIKYSAKLTDDPEIIDIKKTIDEFLPKSTIFKDEVKWVDSIKEEKDNGYKIPGKLIDSFSENDKEYDIYKIDLKSDNGYELHQRLQILVLLFIEAGSFIDAKDELWNLYVLYEKDNKSTSNNEPSIVGFTTAYNYWKYPGAKKFDSTEQESRIKISQFIILPIYQGQGLGQLFYSHLFDKWLAQDDIIEVVVEDPNESFDDLRDRADLKRLNTSEQFDFKAVTPKVDKEWVEKTRRALKLEKRQFARLLEIILLYKLKHGYPGITKRDVRLFIKKRLYDKNKEGLATLDDNTKKDKLQTAYQALEDDYYRILGDLKLNIKRENDEEETDTVSKKQKV | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-14' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 48355
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 2.3.1.48
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Q6FKS5 | MSIDDFKPEKWTISSNEALKLSLVSEDNAIQFSPTFTYPIFGTEEQIFGYKDLVIHLAFDAITFKPFLNVKFSSKFEGSEEELVNIKEKLLEYLPIDDTIYKDEEKWIDSFKKEQESIEAYKNDQNIDEYKIDNADFEIYKVNLQDPKMKRFHRRIQIFSLLFIEAASYIDEDDPKWEIFIVQTKKDKKFVGYATAYNYWYYPGANNFDSESKYRYRGKISQFLILPPYQGRGHGSHLYNSIVKNWRNDSSILEIVVEDPNESFDDLRDVNDLEMLYKDGFFNKLPQERPIPNAWIESTRLKYKIEKRQFSRLLEMILLSTGSNNFEYQVKQRLLIKNKDGLEGMEVSDIKDALNKSFESLREDYDRILGKCQFSNDADGPSKKKIKT | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 45819
Sequence Length: 388
Subcellular Location: Cytoplasm
EC: 2.3.1.48
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P0CO07 | MAETLEEWISDSNQVLNLQMVRTPEDASLLQYEEQQNIDVFNPAFTYPIFGDNEKIFGYKGLDIKLHFASGSLRQYLDISYDAKLASSTTPPDEIEGALYKFIPPDYTKSEVEFQKRVAGDAETFKPLGEKIGSYAHPSAGRKGKGQGDSGMAAGKAIEDNEDVVEYEMYKATWSTPGFREYHRRMQIFVLLFIEGGSYVHEDEDAWEFIVLYERRTRPDSGIFTYHFVGYVSVYPFWCYPDRVRLRLSQFVILPPYQHQGHGSKLYNMLFRHMLDRSEVAELTIEDPAEAFEDLRDRNDLRFLVKEGIVKDPMLYVDVGKGKRGSRVEWELAIRRKYKIAQRQFDRLLEMLLFRQLDKGNPDKVKAYRLHVKARLYRFNYEMLSQMTVEERKEALAKTYESVVEDYKRILGMTFG | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 48537
Sequence Length: 416
Subcellular Location: Cytoplasm
EC: 2.3.1.48
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Q81105 | MQLFHLCLIISCTCPTFQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLXDTASALYREALESPEHCSPHHTALRQAILCWGKLMTLATWVGNNLEDPASRDLVVNYVNTNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | Function: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury during adult infections.
PTM: Phosphorylated.
Sequence Mass (Da): 24689
Sequence Length: 214
Subcellular Location: Secreted
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P0C6G7 | MQLFHLCLIISCSCPTVQASKLCLGWLWGMDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | Function: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury during adult infections.
PTM: Phosphorylated.
Sequence Mass (Da): 24329
Sequence Length: 212
Subcellular Location: Secreted
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Q62I60 | MTAIRGGSRRAPGLALALLGGVLLGACHGDENAQVNALPGFVSGSVRKTAYDGASDDLLTAGLGKTGLGSDTRPGFANPAQPSAAELRRLAIYSNYRALVDITPNGGYGRFWGPNVDLAGNDTLGEGKIAGTEYLAYSDDGSGRKNVTLLVQVPASFDPANPCIVTATASGSRGVYGAIAAAGEWGLKRGCAVAYNDKGGGNGAHEIGTGVVTLIDGTLATASSAGSSSLFTASESSSTLAAFNSAFPNRYAYKHAHSQQNPEQDWGRVTLQAVEFAYWALNEQFGPVVDGTRHGIRYRPGDITTIAASVSNGGGSALAAAEQDTRGWITAVVVGEPQINVRMTPGVTVEQGGAPVPSFGRPLADYATLANLLQPCAAAAVAATGAPYLSALPMGVTQSIRTQRCATLAAAGLVSGADTASQASDALAQLYAAGYLADSDLLQAPMWDSQAMPAIAVTYANAYTRSRVTDNLCNFSFATTNPVTGAVAAPAVSPMTNLFGAGNGVPPTNGINLVFNGASGGVDHRLATPDASFAGAFCLRQLWTANQLGIGTNVDAVRVAANLQHKPAIIVHGRSDALVPVNHASRAYVAQNSATEGRASQLSFYEVTNGQHFDAFLSVPGFDTRFVPVHYYDEQALNLMWNHLKSGAPLPPSQVIRTVPRGGVPGAAPALSTANLPPIVQSPGANAIAVNAGVIDVPL | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+)
Sequence Mass (Da): 71704
Sequence Length: 699
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Secreted
EC: 3.1.1.22
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Q0K9H3 | MHSTQIPPQQKQKRRLRLTVLAAAASMLAAACVSGDDNNNGNGSNPNTKPANIGTVTINSYNGTTDDLLTAGLGKDGLASATAPLPANPTAPTAAELRRYAIHTNYRAIVDTTASGGYGSLYGPNVDAQGNVTGSDGKVAGVEYLAFSDDGSGQQNVTMLVQIPASFNTSKPCMITATSSGSRGVYGAIATGEWGLKRGCAVAYTDKGTGAAPHDLDTDTVPLIDGTRATRAAAGKNAQFAAPAGATSLADFTAANPHRLAFKHAHSQRNPEKDWGKFTLQAVEFAIWAINDRFGAVSANGTRQRTLDKDRIVVIASSVSNGGGAAVAAAEQDAGGLIDGVAVGEPNLNMPPNTGIVVQRGATPVAASGRTLYDYTTTANLLQHCAARATALTQAPFYTNPATATFFANRCQTLAEKGLVSGANTDEQSASALQALHDAGWEAESDDLHPSLAVFDVAAAISVNYANAYAQASVTDRLCGYSFASTLTDLKPAAIAPAALASMFATGNGVPPQPPVQLINDLDPQHGPYLNLASVSPSTLREDLNYDGANCLRSLLAGSDAAARALQAGQALTLRNGNLRGKPAVIVHGRSDGLLPVNHTSRPYLGLNRQQEGVTSKLSYVEVENAQHFDAFIGLVPGYSNRYVPLHVYLNRALDAVYDNLTAGKALPPSQVLRTTPRGGTLNTPAPALLPSNVPPFAASPAAGNAITVNANAVQVPD | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers. Seems to have also poly(3-hydroxybutyrate) depolymerase activity since it is able to release 3HB-monomers from artificial amorphous PHB.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+)
Sequence Mass (Da): 74286
Sequence Length: 718
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Cytoplasm
EC: 3.1.1.22
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A1TWS1 | MKRMMLCTLIGAATVTLTACKKDEVFNSLPDFLVSDVRQFDYDGNTDDLLTAGLGPEGLASATPPAFVDALNPTPAELRRLAIYNNYRALVDTAPGGGYGSLFGPAVGNASGRIPGQEFIAMMQVPGATVPVTVMAQVPDSFDPDFPCMVTAPSSGSRGIYGAIGTAGEWGLKKGCAVVYTDKGTGTGAHNLATNTAQSVNGTLTMEPEEALFRADLDAQSRDDFNSQWPDRFAWKHAHSKQNPEADWGRHVLQSIEFGFYMLNTLHGRELGNGETLRTINPRNTLVIASSVSNGGGASVRAAEQDEKGLIDGVAVSEPNVNPAVDRSFSIRQGNGPALTEHSRSLLDYTTALAVYQGCANQAPGIRDLAPLNGMFNPPATGQNICHSLFNKGLVSGATKDDWALDAQRILNEDFGVQPEQNLLAPVHFGLAVAQSIAMTYANAYGRAGVEDRVCGLSLAATGSAGAVVPLAPAAEASLFAASNGIPPSAGVNLVYDNAEGQPTSLAVSASPSSSQVDYGLDALLCLRSLAEGRDVVTGEPLEGAQAELHEAISRGISAVRASGDLQRKPTVFVTGRADAILPINHTSRPYVGLNQAVEGRHSNLRYYEILNAHHLDVLNGFPGIGDRYVPLHHYYFQALDLMWARLTDKQPLPPSQVVRTVPRGSLTTPLTLANLPPIQSEPAEADRIVFTGNQLQIPD | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+)
Sequence Mass (Da): 74222
Sequence Length: 700
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Secreted
EC: 3.1.1.22
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A1VUF3 | MTIIIAGKNTLTLTSLAAAVLALGACGGNSDPFESKNTKPAYLGAVAIASYDGASDDLLTAGLGKTGLGGTAPAVADPLKPTPAELRRLAIFNNYRAILDISTNGGYGTLYGPNVDAKGVITTGEGKIAGTEYIAYSDDGTGRQNITMMVQVPASFNPANACIVTGTSSGSRGVYGAIGSAGEWGLKNGCAVAYTDKGTGTGIHDLQNNTVNVQNGVRTDAAAAGKNSIFTAELSASERAAFNAATPNRFAVKHAHSQQNPEKDWGKWTLQSVEFAYFVLNEKYGDLARDGATHLKKLTPSNTIVIASSVSNGAGAALAAAEQDTQGLISGVAVAEPEVQLAPDARLSVKRGASVLVGTGKPLYDYFTLANLLQPCAALVSPATNAFNTVNAATATNRCSALKANGLVTGTTTAEQAASALAALVAAGWQPESNVLQASHYSFATLSVGLTYANTYGRFSVKDNLCGFSFAATGAAASATPNAPVPASASALATSFGASNGVPPTIGINIVNNLSAGGPLLDAASLSAGGVQDYNIAGALCMRELATGSSANAVRVRQGMSEVVRSANLRGKPALIVQGRADTLLPVAFTGRPYYGMNKIVEGTASRLSYIEVTNAQHFDAFLAFPGYPERMVPLHRYFIQAMDMMYANLKTGAALPASQVVRTVPRGLTGAVANPIAASNVPPIKTTPAAADQITFANNVVTIAD | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+)
Sequence Mass (Da): 72290
Sequence Length: 706
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Secreted
EC: 3.1.1.22
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Q7N4V5 | MRNQTFIIVGAGQAGAMAAATLRQQQFDGDIILIGKEYHAPYERPILSKDYLINPEEAPKYLFSEDFYLEKQIDLRIGQLVSQIMPSKHCVVLENGGKLRYDKLLLTMGARARRFPLLDQLGENIYTLRTLDDAQRLRQAVKKDKRILIVGGGVIGLELAATSCELGANVTVIEQADNIMGRCAPPLLQDYLLNRHQEKGVQFFLDTNIVSAQKQGSELVLILNTGEKVIGDIIIYGIGAEFRDQLAADAGLVTDGGIVIDSRCQTSEPDIFAAGDVCLQREPLTGDLQRRETWENANRQATIAAHAMMGLAPPQPGAPWFWTDQWGINIQMVGNMQAEEWHIQGDLQSDKAILFGTENEVLVGAVAINQGREMRNLRKLLANPAQVVSGVEWA | Function: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 43579
Sequence Length: 394
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.18.1.3
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P0ABR6 | MTTPSDLNIYQLIDTQNGRVTPRIYTDPDIYQLELERIFGRCWLFLAHESQIPKPGDFFNTYMGEDAVVVVRQKDGSIKAFLNQCRHRAMRVSYADCGNTRAFTCPYHGWSYGINGELIDVPLEPRAYPQGLCKSHWGLNEVPCVESYKGLIFGNWDTSAPGLRDYLGDIAWYLDGMLDRREGGTEIVGGVQKWVINCNWKFPAEQFASDQYHALFSHASAVQVLGAKDDGSDKRLGDGQTARPVWETAKDALQFGQDGHGSGFFFTEKPDANVWVDGAVSSYYRETYAEAEQRLGEVRALRLAGHNNIFPTLSWLNGTATLRVWHPRGPDQVEVWAFCITDKAASDEVKAAFENSATRAFGPAGFLEQDDSENWCEIQKLLKGHRARNSKLCLEMGLGQEKRRDDGIPGITNYIFSETAARGMYQRWADLLSSESWQEVLDKTAAYQQEVMK | Cofactor: Binds 1 Fe cation.
Function: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively (By similarity).
Catalytic Activity: 3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+)
Sequence Mass (Da): 51109
Sequence Length: 453
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.14.12.19
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Q01770 | MSNAMFCYQCQETVGNKGCTQVGVCGKKPETAALQDALIYVTKGLGQIATRLRAEGKAVDHRIDRLVTGNLFATITNANFDDDILAERVRMTCAAKKELAASLTDKSGLSDAALWEASEKSAMLAKAGTVGVMATTDDDVRSLRWLITFGLKGMAAYAKHADVLGKHENSLDAFMQEALAKTLDDSLSVADLVALTLETGKFGVSAMALLDAANTGTYGHPEITKVNIGVGSNPGILISGHDLRDLEMLLKQTEGTGVDVYTHSEMLPAHYYPAFKKYAHFKGNYGNAWWKQKEEFESFNGPVLLTTNCLVPPKDSYKDRVYTTGIVGFTGCKHIPGEIGEHKDFSAIIAHAKTCPAPTEIESGEIIGGFAHNQVLALADKVIDAVKSGAIKKFVVMAGCDGRAKSRSYYTDFAEGLPKDTVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLEDVNDLPIVYNIAWYEQKAVIVLLALLSLGVKNIHLGPTLPAFLSPNVAKVLVEQFNIGGITSPQDDLKAFFG | Cofactor: Binds 1 spin-admixed [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 58659
Sequence Length: 545
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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P31101 | MFCFQCQETAKNTGCTVKGMCGKPEETANLQDLLIFVLRGIAIYGEKLKELGQPDRSNDDFVLQGLFATITNANWDDARFEAMISEGLARRDKLRNAFLAVYKAKNGKDFSEPLPEAATWTGDSTAFAEKAKSVGILATENEDVRSLRELLIIGLKGVAAYAEHAAVLGFRKTEIDEFMLEALASTTKDLSVDEMVALVMKAGGMAVTTMALLDEANTTTYGNPEITQVNIGVGKNPGILISGHDLKDMAELLKQTEGTGVDVYTHGEMLPANYYPAFKKYPHFVGNYGGSWWQQNPEFESFNGPILLTTNCLVPLKKENTYLDRLYTTGVVGYEGAKHIADRPAGGAKDFSALIAQAKKCPPPVEIETGSIVGGFAHHQVLALADKVVEAVKSGAIKRFVVMAGCDGRQKSRSYYTEVAENLPKDTVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLDDINDLPVSYDIAWYEQKAVAVLLALLFLGVKGIRLGPTLPAFLSPNVAKVLVENFNIKPIGTVQDDIAAMMAGK | Cofactor: Binds 1 spin-admixed [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 59979
Sequence Length: 553
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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A0A2H5AIZ1 | MIINIKETTMVRPSQPTPSQRLWNSNLDLVVPRFHTPSVYFYRRPGNASDFFDARVLKEALGRALVPFYPMAGRLARDEDGRVEIDCNGEGVRFVVAETDSAIDEFGDFAPTMELKKLIPKVEYGDDISAFPLLVLQITHFKCGGTSLGVGMQHHVADGASGLHFINSWSDIARGLDIAVPPFIDRSLLRARDPPSPSFPHIEYQPAPSMNTSPAPIQDPTVKSDPTATAVSIFKLTKQQLDLLKSRVSAKYSSYALVAGHVWRCTSIARGLPDDQRTKLYCATDGRARLQPPLPSGYFGNVIFTATPVADAGEITGEDSGLEAAAGRIQRALMRMDDEYLRSALDYLELQPDLSKLVRGAHTFRCPNIGLTSWTRLPIHDADFGWGRPIFMGPGGIAYEGLAFMLPSSEGDGSLSIAISLQAEHMIKFQKLLYEI | Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to various acyl acceptors. Can use feruloyl-CoA and caffeoyl-CoA as acyl donors.
Sequence Mass (Da): 47985
Sequence Length: 436
Pathway: Phenylpropanoid metabolism.
EC: 2.3.1.-
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P45579 | MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLAAESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESFKA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NADPH-dependent reduction of 2-oxoglutarate and 2-oxobutanoate, leading to the respective 2-hydroxycarboxylate. Cannot use NADH instead of NADPH as a redox partner. Do not catalyze the reverse reactions.
Catalytic Activity: 2-hydroxybutanoate + NADP(+) = 2-oxobutanoate + H(+) + NADPH
Sequence Mass (Da): 39092
Sequence Length: 362
EC: 1.1.1.-
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P30178 | MESGHRFDAQTLHSFIQAVFRQMGSEEQEAKLVADHLIAANLAGHDSHGIGMIPSYVRSWSQGHLQINHHAKTVKEAGAAVTLDGDRAFGQVAAHEAMALGIEKAHQHGIAAVALHNSHHIGRIGYWAEQCAAAGFVSIHFVSVVGIPMVAPFHGRDSRFGTNPFCVVFPRKDNFPLLLDYATSAIAFGKTRVAWHKGVPVPPGCLIDVNGVPTTNPAVMQESPLGSLLTFAEHKGYALAAMCEILGGALSGGKTTHQETLQTSPDAILNCMTTIIINPELFGAPDCNAQTEAFAEWVKASPHDDDKPILLPGEWEVNTRRERQKQGIPLDAGSWQAICDAARQIGMPEETLQAFCQQLAS | Function: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions.
Catalytic Activity: 2-hydroxyglutarate + NADP(+) = 2-oxoglutarate + H(+) + NADPH
Sequence Mass (Da): 38897
Sequence Length: 361
EC: 1.1.1.-
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P80960 | SLLRKNVDSLTEEEILTLQSVMRELQNDSSEHGFQSIASFHGSPPLCPSPEANKKVACCVHGMASFPQWHRIFTKQMEAALMGHGAKVGMPYWDWTTSFTKLPRFIPYDDEQLNPFVRITDLEDHFTTRDPQPELFKDPEGGDESFFFRQVLIALEQRDYCDFEVQFEVIHNSIHYWIGGHQKYGMSTLEYTAYDPLFFIHHSNVDRLWAIWQELQKYRGLPYDESDCGVELMREPLQPFAQTSATNPNNVTRAHSTPKSLFNYRQLAGYTYDTLTLNGMTISQLESSLLRLQKEEDRVFAGFLLRGIGSSADVTFDLCDKDEHCDFAGTFAVLGGPLEMPWSFDRLFKMDVTKVFKQMRLRPDDSEYHFELEVTARAGTDLSPELLKPGSVSFLPGRKIQNTPDVR | Cofactor: Binds 2 copper ions per heterodimer.
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Sequence Mass (Da): 46756
Sequence Length: 407
Subcellular Location: Secreted
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P83040 | DDQGHTHRNLVRKSVRNLSPAERRSLVHALKSLQEDSSADGFQSLASFHAQPPLCPYPEANKRFACCVHGMATFPEWHRLYTVQFEDALRRHGSVVGIPYWDTVVPQEDLPAFFNDEIWDDPLFHANFTNPFNGADIDFNHQKIARDINVDKLFKEGPKGYDTWSFKQYIYALEQEDYCDFEVQFEIAHNAIHAWVGGTEEYSMGHLHYASYDPVFILHHSNTDRLFALWQELQKFRGHDPNEVNCALEMMREPLKPFSFGAPYNLNPTTKEHSKPEDTFDYKGHFHYEYDHLELQGMNVQRLHDYINQQKERDRVFAGFLLEGIGTSAHLDFSICKIDGECTHAGYFDVLGGSLETPWQFDRLYKYEITDVLESKGLDVHDVFDIKITQTSWDNEDISTDRFPPPSVIYVPK | Cofactor: Binds 2 copper ions per heterodimer.
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Sequence Mass (Da): 47963
Sequence Length: 413
Subcellular Location: Secreted
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Q9HXM1 | MTRRTAFFFDELCLWHAAGPHALTLPVGGWVQPPAAAGHAESPETKRRLKSLLDVSGLTARLQLRSAPPASDEDLLRVHPAHYLERFKALSDAGGGSLGQDAPIGPGSYEIARLSAGLAIAALDAVLAGEADNAYSLSRPPGHHCLPDQAMGFCFFANIAVAIEAAKARHGVERVAVLDWDVHHGNGTQAIYYRRDDVLSISLHQDGCFPPGYSGAEDIGEDRGRGFNLNVPLLPGGGHDAYMQAMQRIVLPALERFRPQLIVVASGFDANAVDPLARMQLHSDSFRAMTAMVRDAAERHAGGRLVVVHEGGYSEAYVPFCGLAVIEELSGVRSAVRDPLRDFIELQQPNAAFRDFQRQRLEELAAQFGLCPAQPLQAAR | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines.
Sequence Mass (Da): 41049
Sequence Length: 380
EC: 3.5.1.-
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Q9XSK7 | MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEATEGDGDKKGNAEGSSDEEGKLVIDEPTKEKNEKGALKRRAGDLLEDSPKRPKEAEDLEGEEKEGATLEGERPLPVEAEKNSTPSEPGSGRGPPQEEEEEEEEEEAAKEDAEAPGLRDHESL | Function: Acts as a transcriptional repressor (By similarity). Has mitogenic activity for fibroblasts (By similarity). Heparin-binding protein (By similarity).
PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
Sequence Mass (Da): 26604
Sequence Length: 239
Domain: The PWWP domain harbors the heparin-binding sites and is responsible for DNA-binding, while the C-terminal region is essentially unstructured.
Subcellular Location: Nucleus
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P51858 | MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL | Function: Acts as a transcriptional repressor . Has mitogenic activity for fibroblasts . Heparin-binding protein .
PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
Sequence Mass (Da): 26788
Sequence Length: 240
Domain: The PWWP domain harbors the heparin-binding sites and is responsible for DNA-binding, while the C-terminal region is essentially unstructured.
Subcellular Location: Nucleus
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P52357 | MSLSSLFNGKYDTKFLLNMSSAAKVELIVEKVAALADACLETPLPTDWFRNILDPELEFNSNFEEIHSIGDEEFAQPLPFLPFRVLLITGTAGAGKTSSIQTLAANSDCLITATTSIAAQNLSGLLNRTKSAQVKTIFKTFGFNSSHVSMNERISCSVTTLDSIADQQKHDLSTYWNVIADIAERALNAANGKTKVIPDLCESSVIVIDEAGVILRHILHTVVFFYWFYNGLHKTQLYKNRVIPCIVCVGSPTQSGALISSFNPLTQNKDVKKGFDILSALICDDILSNYCKISENWVIFVNNKRCTDVEFGEFLKHIEFGLPLKPELIEYVDRFVRPATYIRNPTNEIGMTRLFLSHYEVKSYFKVLHEQVELTNKDNLFTFPVYFIIQNKAFEDYKNEISNFTLEIEPWFKTNLHRLNTYSQFADQDLSKTIQIEEIVLDDGSVEETLITCHLKHIKHSSIGVTSRTKSSTVGFSGTYEKFVELLQSDLFIEKTACEYSVHAYSFLTGLMYGGMYSFCLSEFTTSEVMTEIRKIKLPNIDFLQTMTAEVSLQTFDESDEYYDLHIAPTDEEMLASDPCPDPFFLKYKQLPLTNVLTFEEISYLYTVFKEIFISRFAILQRHSKEMFGKSNLITYNRNNVSSKRCGEICSHVKSFYGMLTYAVPANNYTLEGYTYDNVIFLGTDKMLPPIIYKRGLPKIVIKDEMGFISILDNNVSKLTDTVNGNSFHICTTIDYAIVSKVAMTVTKSQGLSIQRVALDFGNDPKNLKLSSIYVGMSRVVDPNNLIMNLNPLRLNYENDNIIASHIVKALKNKDTMLIF | Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Possesses helicase-like motifs and therefore may act as the helicase subunit of the complex.
Sequence Mass (Da): 92914
Sequence Length: 820
Subcellular Location: Host nucleus
EC: 3.6.4.-
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Q6UDG9 | MAEDRGTRLWQFPDHVYLNFTAMHGIQHVVDRISSLAEESVTPAERPPLSWFEAVARADSPDEVPPRELPFRVYLITGNAGSGKSTCIQALTEMLNCVTTGSTRVAALNVFTKLSSAYTSPAIQTIFHDFGFKGSHVQAVLGKFKYPKQPDPKSLVDAQMSDLYYYWDVLKDIANKVVEGGLPETMRVLLSLELKSGKPFTDAAPFLSAATPALIRSNVVLIDEAGVLGKHILTAVVFSWWLHNALWQTRRYAEGKVPVIVCIGSPTQTDAMESVFEHSTLRHLVSNKTNILSHLIRSSEMAERMNLNRNWTIFINNKRCTEQDFGNVLKAFEFGLPMNEGHARFLDQFVVSESYIKDPSKLPGWTRLFASHDDVKVYMSRLHANLRARRSDKFKVFVLPIYTVVSLEAFDKYKELTGQTSLTMEKWLTANASRLGNYSQSRDLDVTTPRFEYGTADGKKFALITTDASHVLNSQISVTKRVKKLVFGFEGSFGDFAAVLSEDTFFKKHGEDHVEFAYRFIAALLFSGMIAFYDFLRTEGLPQDKVDAAYSRLQAVTADLLAATHEQLGIAAAAGAQTGSGARRSRNADAFAFDDDASEEVTDAELDDLFGAMTDNSMDAFYLNYEKLPADAHGQEIFFHFDMLKRLFSERYDALSGLFGKTFTSAPFRTFVGQASFNGSNAFVSSFSGGILSFTSQTDAYTLRGVTRAPVPCFVDELFRGRDWAAAILRETDMPRVVVSDSMGFVSVINHNMSTFVDNVSGEELQMAATVDHGISSNLAMTITRSQGLGLDRVAICFATSQLKLNTAYVAMSRVTSCRYLRMNVNPLRTHYEDTRRVSAHILAALRCKDVKLVY | Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Possesses helicase-like motifs and therefore may act as the helicase subunit of the complex.
Sequence Mass (Da): 95258
Sequence Length: 855
Subcellular Location: Host nucleus
EC: 3.6.4.-
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Q01014 | MAELSPEFILNMTSDAKVRIIVEKIRKLSNITTRPPEMTLYNDQFDPEQCPGTLLPFTCYVITGTAGAGKSTSISALYQNLNCLITGATTVASQNLSRCLKTYCPTIFNAFGFKSKHINILPRSVPRRTLDTIEQIQNFELCKYWPILTSIIQEFSKKKNLGQYSSISLAAFNMLAKMTTTLWTTNVIVIDEAGTLSSHILTAVVFCYWFYNSWLNTPLYRSGAVPCIVCVGSPTQTDAFNSTYNHIQQKYNIMECDNILSFIIGNKVVSEYISLTNNWALFINNKRCTDPEFGHLLKTLEYSLKISPKTMEYIDRFVVPKAQILNPLEFLGWTRLFLSHAEVKSYLSSLHTALVTGTNVSGAKLFTCPIVCEVFTKAFNEYKSHVNLPSLTATEWLSKNLHRLSNYSQFIDQDMTAIHTETTDTSTKVTYLTKYVKNTYISLNGKTKKCVCGYVGTYKNFKKILESESFIDSHANDQPEFVYSFLCTILYNSLYNFHNYGVTEKNESYLNDLANLKLPENLTHLYTQTDLDIEREALMLEDDVFYHMVSPPPTASSASLPCLISWYTALKDIFISRLKLATTWFSNKFLDREFTSFTINMLVRDNIEFTSTNGRLHGLLEYASTVESYKLQGYTFLPVNFGRSQTTVISKDLQDKMPSIVVQDSSGFIACLEKNVNKMLETLDDGKSFHLCSAGDYGISSKLAMTIVKAQGTSLDKVAICFSNHKKIKVSHIYVAISRATNPNHIVMDCNPLKLLVNDTQSISSQHIIKALNNPNTLLVY | Function: This protein may be a helicase and is required for replication of viral DNA.
Sequence Mass (Da): 88254
Sequence Length: 781
Subcellular Location: Host nucleus
EC: 3.6.4.-
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Q9NRZ9 | MPAERPAGSGGSEAPAMVEQLDTAVITPAMLEEEEQLEAAGLERERKMLEKARMSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLERKKESLKVKKGKNSIDASEEKPVMRKKRGREDESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSNSIIKDRLSETVRQNTKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMFGSSEKETIELSPTGRPKRRTRKSINYSKIDDFPNELEKLISQIQPEVDRERAVVEVNIPVESEVNLKLQNIMMLLRKCCNHPYLIEYPIDPVTQEFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLNLSKNFLDPKELMELLKSRDYEREIKGSREKVISDKDLELLLDRSDLIDQMNASGPIKEKMGIFKILENSEDSSPECLF | Function: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis (By similarity).
Sequence Mass (Da): 97074
Sequence Length: 838
Subcellular Location: Nucleus
EC: 3.6.4.-
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Q60848 | MAEQTEPAVITPAMLEEEEQLEAAGLEKERKMLEEAQKSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLEKKKRSLKLTEGKSLVDGNGEKPVMKKKRGREDESYNISEVMSKEEILSVAKKHKDNEDESSSTTSLCVEDIQKNKDSNSMIKDRLSQTVRQNSKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVALEVPPKREVVVYAPLCNKQEIFYTAIVNRTIANMFGSCEKETVELSPTGRPKRRSRKSINYSELDQFPSELEKLISQIQPEVNRERTVVEGNIPIESEVNLKLRNIMMLLRKCCNHPYMIEYPIDPVTQEFKIDEELVTNSGKFLILDRMLPELKKRGHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLSQSKNFLDAKELMELLKSRDYEREVKGSREKVISDEDLELLLDRSDLIDQMKASRPIKGKTGIFKILENSEDSSAECLF | Function: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis.
Sequence Mass (Da): 95126
Sequence Length: 821
Subcellular Location: Nucleus
EC: 3.6.4.-
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H2KY86 | MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKSTDPDGICQLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERMDAVLKQCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPMVGRERLGKAQYLQMAGRAGRAGFDTKGDCITIIKAGEEERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHYFITIEPLEQDVASEPSAQASSIPRVPGKISPSDLGNAVFNAGFDPDEATRLHADLVSSLNQGVIFASHFHLLFIITPYEQVCNINWDLFLLMYNALPSSERKLLAECGLEEKFILEAIITRVDLTAGTPRMRLYIALMLQKIWNHEPMYTVAERFGVEKGWLQATLQSSISQAASIAKFSEKITTMWPLRKLLPELVQRLSEAAQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARANPLKLVQELGTIRMAQANSIIASARMVLRDQVDEKMEELDVWGVATDSFNYF | Function: Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair . Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA) .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 102969
Sequence Length: 923
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q9YFQ8 | MSKGLYDIPSWATTETRTLAKLAGVERLFEPQYMALQAGVEKGENLVVAAPTGSGKTFIALVAIVNSLARAGGRAFYLVPLKSVAYEKYTSFSILSRMGLKLKISVGDFREGPPEAPVVIATYEKFDSLLRVSPSLARNVSVLIVDEIHSVSDPKRGPILESIVSRMLASAGEAQLVGLSATVPNAGEIAEWIGGKIVESSWRPVPLREYVFKEYKLYSPTGGLREVPRVYGLYDLDLAAEAIEDGGQALVFTYSRRRAVTLAKRAAKRLGRRLSSREARVYSAEASRAEGAPRSVAEELASLIAAGIAYHHAGLPPSLRKTVEEAFRAGAVKVVYSTPTLAAGVNLPARRVVIDSYYRYEAGFREPIRVAEYKQMAGRAGRPGLDEFGEAIIVAERLDRPEDLISGYIRAPPERVESRLAGLRGLRHFILGIVAPEGEVSIGSIEKVSGLTLYSLQRGLPRETIARAVEDLSAWGLVEVKGWRIAATSLGREVAAVYLDPESVPVFREEVKHLSFDNEFDILYLISTMPDMVRLPATRREEERLLEAILDASPRMLSSVDWLGPEEMAAVKTAVVLKLWIDEASEDTIYGEWGVHTGDLLNMVSTAEWIASGLSRIAPYLGLNSKVSHILSVIARRIKHGVKPELLQLVEIPGVGRVRARILFEAGYRSIEDLATARAEDLMRLPLIGPSTARQILEFLGRVDEAREAEAREMLARKGLLSYLEGDAVAGEEGE | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80474
Sequence Length: 735
EC: 3.6.4.12
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P0DMI1 | MKVEELAESISSYAVGILKEEGIEELFPPQAEAVEKVFSGKNLLLAMPTAAGKTLLAEMAMVREAIKGGKSLYVVPLRALAGEKYESFKKWEKIGLRIGISTGDYESRDEHLGDCDIIVTTSEKADSLIRNRASWIKAVSCLVVDEIHLLDSEKRGATLEILVTKMRRMNKALRVIGLSATAPNVTEIAEWLDADYYVSDWRPVPLVEGVLCEGTLELFDGAFSTSRRVKFEELVEECVAENGGVLVFESTRRGAEKTAVKLSAITAKYVENEGLEKAILEENEGEMSRKLAECVRKGAAFHHAGLLNGQRRVVEDAFRRGNIKVVVATPTLAAGVNLPARRVIVRSLYRFDGYSKRIKVSEYKQMAGRAGRPGMDERGEAIIIVGKRDREIAVKRYIFGEPERITSKLGVETHLRFHSLSIICDGYAKTLEELEDFFADTFFFKQNEISLSYELERVVRQLENWGMVVEDHHLAPTKLGSLVSRLYIDPLTGFIFHDVLSRMELSDIGALHLICRTPDMERLTVRKTDSWVEEEAFRLRKELSYYPSDFSVEYDWFLSEVKTALCLKDWIEEKDEDEICAKYGIAPGDLRRIVETAEWLSNAMNRIAEEVGNTSVSGLTERIKHGVKEELLELVRIRHIGRVRARKLYNAGIRNAEDIVRHREKVASLIGRGIAERVVEGISVKSLNPES | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 77835
Sequence Length: 691
Domain: The N-terminal region (1-400) has DNA-dependent ATPase activity but no helicase activity.
EC: 3.6.4.12
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A8MB76 | MNIEELPLPSLLRDFLISKRGIRTLYPPQEEAIRAGLLNGENILMVSATASGKTLLAEVAAVNNVLVNDKKSLVAVPLKALAFEKLNDFNTYSELGIRVAASTGDYNSEDKWLGSYDVIITTYEKLDSLLRLKPSWIWNVGQLIIDEIHFINDDERGPIIESIVAKLRMLNLNPQIIGLSATIGNPEELANWLNAKLVKSDWRPVSLREGVYHKGVVTYVNDGEKRISGQGDSLINLTVDTLNDGGQVLVFSSSRQGAVRIARKLAEYICSSPVRYIDPGEAGKLAEEVRETSSSRILAEELTGLIKCGVSFHHAGLELEVRRVIEEGFRRGVLRVLASTTTLAAGVNLPARRVIVNEYRRYEPGYGFIEIPVMEYKQMAGRAGRPGLDPYGEAIIIVSSKDEVDYVIDKYIKSPPEYVKSNFMNPTSLKFHTLSAVASQYAETIDELVKFTSNTFAGFQGKLSAMIQANSVRRMISRIIDELVDYGFIIRNGDKLEATEVGAVVNRMYLDPDTAHVFIMGLRNLNSDADLNAYSLMLVVKSPKIPKVKVRRNELDELAQQAASMWSSIPLKPSDVDELVNYPEDYEDFLSEFKTAMALLEWINESNEDQIMKTYDVQPGDLRVLSDQAEWLIGALQELARTLGLSGNVVNGLRALRYRVKYGVNDELLELVVNLEGVGRVRARALYAAGYRSIEDLAKANVSDLTRIRGIGDKIAGSIIEQAHQLVKDGRVIKFNESTVKGKTRRGGGGLLDHMY | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84006
Sequence Length: 756
EC: 3.6.4.12
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Q5UYM9 | MDVADLPGVPEWLPDHLRDDGIEELYPPQAEAVEAGVTEGENLVASIPTASGKTLIAELAMLSSVARGGKALYIVPLRALASEKQADFEEFEQYGLDIGVSTGNYESEGGWLADKDIVVATSEKVDSLVRNDAPWIEDLTCVVTDEVHLVDDGERGPTLEVTLAKLRRLNPDLQTVALSATIGNAEALATWLDAGLVDSDWRPIDLQKGVHYGQALHLEDGSQQRLSVQNNEKQTAAIVRDTLEDDGSTLVFVNSRRNAEAAAGRLANTVRPHLSTEERDQLADIAEEIRDVSDTETSDDLADAVADGAAFHHAGLSRGHRELVEDAFRDRLVKVVCATPTLAAGVNTPSRRVVVRDWRRYDGSAGGMAPLSVLEVHQMMGRAGRPGLDPYGEAVLIASSHDEVDELFERYVWADPEPVRSKLAAEPALRTHILATVASGFARSRKGLLEFLEQTLYASQTDDSGQLERVVDDVLTYLQRNDFLEIEAGELDATSLGHTVSRLYLDPMSAAEIVDGLRDWERGASDSTSASGSPADAQAEPPANSGFTTASELAEDADESDADRDPDDISALGLYHLVSRTPDMYQLYLRSGDREEYEMELFEREEELLGPTPSEFEEGRFEDWLSALKTARLLEDWATEVDEATITDRYGVGPGDIRGKVETAQWLLGAAESLASEVDLDAARAISEARIRVEHGVREELVDLAGVRGVGRKRARRLFQAGITDRAQLRDADKAVVLAALRGRRKTAENVLENAGHRDPSMEGVEPAPDVSVDLNDGADGDASAESTANDDQASLGDF | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86768
Sequence Length: 799
EC: 3.6.4.12
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B9MRJ1 | MLWVIGINHKVEVDIRQKFSLIKTKLQEKLISLKKLANEVIILSTCNRTEIYFFSEEYVDIEKIFTELDWDKRYMHLFYIYKDKDCIKHLFEVVCGFDSLLIGEDQIVAQVKEAKEISKLVGGKNPVLERLFEVALKCSKEFRTKARLNEHPITIASVVGKVLKESNIRKIAIIGLGNIGILFCNYFKNSDVDKVFLIGRKNEKIDQFVKLNPEKFRYYDKKKTILEAQCLICSTSAPHSVVHKDDIPEGKNLLIFDLAVPRDVDVEVYELPNVKVIDIDQVHKIDTINREFRISKMQENYHIIDKYVDEFIDWLEFRQYRNLIMEMKRHAEQLCKAQVKYIKNVDSRERKEVERLLIRMANLYIDRAIEVLREAHKEGSGEICSNLIKRIFLK | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46380
Sequence Length: 394
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A8MAH6 | MGIDDYLSKIRALTLNHKRVSTITLSETYFNRDEVYGKLMNYYDEVFLLQTCNRVEVYVYGDDDSVAEDMYKVKGTINHVDKLVGMNAVRHIFRVAAGLESAAVGESEILGQVEDAFNDARKRGALGGLLGFTIERAIRTGKEIRSRFPEISIGLASIGSLVAEYVHRVRGLNSRIAVIGAGSIGSDIVRRLAEKGFRNVIIVNRTLDKAKAAALRYGFNYAPIDSLRSVIRDSDVVIFATSATNPLLRRRDAEELSGKPIIIDVGVPRNVDPEIPGVVSIDELKNIENEIREGKRKALDEASRLIELRLIEYRRLFARRVIEGMIGELTKWGLSIGESEVKRAVKAGLIKNEEDGAALAVKSTVKKIMLPLLTYLKELAEEDKFDEALIIISGIKAKLNGDGKQS | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 45009
Sequence Length: 406
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A5VM68 | MYLMCVSLNYHQLPLDLREKFSFTKEEVPKADKLLNDEKSILENLLISTCNRTEVYAVVDQIHTGRYYIRRFLAEWFHYTIDDFTKFVTVTTKDAVAEHLFKVITGLDSLIKGEPQILGQMKDAFQIATKEGTTGAILNHLFRQAITFSKRMHTKYRVSELAQSSGQAGLHQIKMQFGSLEGKTLAVVGLGQIGKHTAYNASNMGFSKVLLLNRTDSKAEQIATELQGVVEARPFNQLATVVHNVDAAIFAATVKQPLFKADEQISTMIVDLGVPRNVAVNSTKLKYYDVDHVHMILNSNDEKRRLMIQKIANEIPQEVNDFYIWEKQLHIVPVIRGLREHSLRIEGEAYDSLLRKLPELDSHERKVISKHMKSIVNQMIKGPIKEIKELSVTPGATADIDFFCKIFGMDNLKVENQNNDK | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47865
Sequence Length: 421
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q8Y6X4 | MFILTMGLNHHTAPIDIREKLVFKETEEEMALVTLQQEKSILENVIISTCNRTEIVAVVDQIHTGRYYLKRFMANWFQMDMEKIEPYLFFHEETEAVNHLYKVTAGLDSLVLGETQILGQVKHAFEIAKQTETTGTLLNKLFREVVTFAKKVHHHTKINENAVSVSYAAVEVAKKLYGSLDNKKIVLVGAGEMSELALQNLAGSGIADITIINRTKSNAELLANQFQAKVGAYENMNEHLMLADIVLVSTSATEPIIKQAAMQDLMEQKASSMLVIDIGLPRNVEHDCSYIPNFHLYDIDDLAGVVSANSLERQRIVLELENTIEVEVRNFFEWEKQLGVVPVIRALREKALDMQEVAMTSLENKLPGLTEREYIQIGKHMKSIINQMLKQPISELKEMSVEEDATTSIEHFKRIFGLSETDVTVIEKEQAETRS | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 49250
Sequence Length: 435
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A0LDT6 | MKLVVVGLNHKSAPVSLREKVAYSSDTLPRSLQALTRLDAVHEGTILSTCNRVEIYMASRDPDAAAAQTSQWIARDHALDPADVTPHLYTKAESEAVRHGFCVASSLDSMVLGEAQILGQMKQAYQDALSAGSTGVVLNRFFQHAFLTAKRVRTETSIAENSVSVASAAVDLAKRIFGDLSGHSCLLIGAGEMCELAARHLVTHGVKEVLVTNRTFSRAVDLAQQFDGHAFPIEALAENLHRADIVISSTGSTVYMVGPDMVKQALKSRRQRPIFLIDIAVPRDLDPEIGQVDSAFLYDMDDLNKIVNDNRQDRAEAAQAAMQIIEGETPLFIQWLDTLDVVPTIKQMRRKAEAAKDQLLQKHLAGWDLSDTDRQRVENLARQLVNKLMHDPTERLRSLTNEHDGDRYIDAARKLYKLDDD | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46617
Sequence Length: 421
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q0W5T5 | MAQVCSISVNHRHAGIEGIERARFRDPDVAMLRLLSLPGVSEAVVLQTCNRVEIYAVAESVEDIVGFARAEGMPLEIAEVRAGDDCLKGLLRLACGLESMIVGEDQILGQLKTALLQARRLGTIGPVLSTAIQKSIHVGARARIETEINKGSVSIGSAAVELAESLLGDLRGRTILVVGAGEMGTLVANAMAEKSLRAIYVANRTFEQAEKLASSLQGVAIRLERLCDYMGSADVVICATGAPHLIITKKMVEQCKGEKPLIFIDITNPRNIEETVGEVPGVTLHNIDSLRQINEASMRRRQGEARKVEAIIEEELVLLQRDIRRLHADRVIGDLYQRTDHIRATELRRAVARLSTAGSLTEQQISILHDFSMALTNKILAAPTRQLRRAAERCDEDCLRTAEELFDLWVEESNGIPGNKTKASKTD | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46694
Sequence Length: 427
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A9FDP5 | MIFVGLSHKTAPIEVRERLAIGRDRLPEVLARLTAHPAIGEALVLSTCNRVEIYASPRQQAPAPPRPGSAPPPSDEELSRNNEALRAAVATLVGLGGDAVRGHLAGRVGSDAVLHLFRVAASLDSMVVGEPQILGQMKEAIEVARGAKTLGVRLGRAAHRAIKVGKRVRTETAIGAGQVSVSSVAIDLARQIFADLAGHTALLIGAGDMAEAASKLLVRAGARLIVVNRSPDRAAALAREVGGEPRPWADLERSVIDADIVISSTSSPNYVVTPDLVRRARKARKGRSLFLIDIAVPRDIDPAVNKLDSVYLYDVDDLSQIVAESVEGRAAEAARAEAIVADEAQAFEAWTLERALTPTIVGLRARTRSILVAEVERSLSGKLRHLGVAERQALAMMIDAATNKLLHVPTTRLRAMASDPRVAEHVDSLRELFDIDGAPPENAAASALAEGELRGAVDGPPTPRSARGAAPPASGARGGGSPRHADPRPQAAEDNGVYARQPGGRPAEAGVMAVANPAAAVSAAGLKGA | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 55293
Sequence Length: 529
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A6TJD5 | MRTIKIGSRASQLALVQAEIIINMLKEKFPQYTYEIIKITTLGDRILDKTLDKIGGKGLFVKEIQKALAEEKIDLAIHSMKDMPGETPEELVLGAITKREDPRDVLITRENKSLEELPKGAVIGSSSLRRQAQVMALRGDIKVVPIRGNVGTRLGKIETESLDGVILAAAGLNRLGLKEKISSYLEIEDFTPAVGQGALGCEARRKDIEMLEMLLAINHEETYRCVMAERAFLKLLEGGCHVPIGAYGQQQGQELHMTGMVASSDGRRVIKEQVMGDIADFQALGIQLGETLIEKGAKEILETVNTDNRIVNTEGS | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34706
Sequence Length: 316
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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A8MGE4 | MKIRVGSRESKLAVKQSEIVIEAIRKYDPNIEIELVTMKTTGDIKLDQTLDKIGGKGLFIKELDQALYDDRVDITVHSFKDMPMAIDEYLPIVAVSKREDPRDVLVLPKTVKEPDFSKPIGCSSFRRKIQLQEIYPHCSVEPIRGNVLTRLEKLDRGEFSAITLALAGLKRLGLEERISRIFEVTEILPAACQGVIVVQARKGFDVSFLSDFHDKEAWDISMAERSFVRTLNGGCSSPVAAYGEIKDNYLTLTGLYVDSSNSVHKKTITGARKQGEEMGFNLALQMKGEDEVHGKD | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33149
Sequence Length: 296
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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O66621 | MKIRIGTRKSKLALWQANYVKDFLEKHWGVEVELVKITTTGDKITDVPLAKIGGKGLFVKEIEKALLEGSIDLAVHSLKDVPMVIPKGLKLGAITKRENPYDVLISRSGKKLYELPSGSVIGTSSLRRQVQIKKRRRDLKVEVLRGNVDTRMRKLKEGLYDAVILAYAGVKRMGYESEITEVLEDFIPAVGQGSLAIEIREGDKRIEELIKPLNNEESFLCAIAERTFLRRLEGGCQVPVGAFAKIENGTLKMKAFISDIEAERYIEGYREGNPEEAEKLGLSLAEELLKKGGEEILKEIYSSQ | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34031
Sequence Length: 304
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q43316 | MDIASSSLSQAHKVVLTRQPSSRVNTCSLGSVSAIGFSLPQISSPALGKCRRKQSSSGFVKACVAVEQKTRTAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDKILSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCNLPREDVRDAFICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEENFRGNVQTRLSKLQGGKVQATLLALAGLKRLSMTENVASILSLDEMLPAVAQGAIGIACRTDDDKMATYLASLNHEETRLAISCERAFLETLDGSCRTPIAGYASKDEEGNCIFRGLVASPDGTKVLETSRKGPYVYEDMVKMGKDAGQELLSRAGPGFFGN | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 41043
Sequence Length: 382
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
Subcellular Location: Plastid
EC: 2.5.1.61
|
O29026 | MKLIVGTRGSKLALAQTNKVAERLKERYEVEIRIVKTAGDIMKDKPLYEFKGMGAFVRALDTALAEGKVDVAVHSFKDVPSQRVEGTVVAAVIERDSPCDVLISRDGSTLEELDEGAVVGTSSLRRRAQLSRLRGDLRFENLRGNLDTRLRKLREGNYDAIVVAEAGLKRLGLDREVEYQPFPPEVIVPPANQGIIAIATRKGEEDLVAFLNDEKTWLEAMVERAVIKELGVGCAVPVGVYAEAQSRVRLICEILDKKYLRVEEKLSKDTAVEEAAEIGKDLRKEIYGG | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32006
Sequence Length: 289
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
|
Q75DY0 | MGEETLRIAGRRSKLAVIQSESVKEIVQREFPNYTCTVLAKQTLGDQVQSKPLYAFGGKALWTKELEDLLYEEDLDQRIDMIVHSLKDMPTQLPEGFELGAITKRVDPSDCLVMAAGSPYKTLGDLPNGSVVGTSSIRRSAQLRRRYPHLVFASVRGNIQTRLKKLDDPENECKCIILATAGLVRLGLESRITQRFDSTIMLHAVGQGALGIETRTGDERLQAILAKVADRNSTICCLAERSLMRTLEGGCSVPIGVYSTFDEETSMLTLDGLVVSVDGADAAEATVSYKIKSDKEDAIACGQLLAAKLLEAGAKKILDAIHLPEA | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 35526
Sequence Length: 326
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q6CT60 | MESKETVRIGGRRSKLAVVQSEQVKVMIESKFSHIECPLLSVHTLGDQVQSKPLYSFGGKAVWTKELEDLLYKDDESRIDLIVHSLKDMPTLLPDGFELGGITKRVDPTDALVMPIGSPYSSLSELPDGSVVGTSSVRRSAQLKRKFPNLKFESIRGNIQTRLAKLDDPETPYKCIVLASAGLMRSGLDSRITQRFNADTMCYAVGQGALGIEIRKDDEKMKKILKEICDPSTTICCLAERSLLRTLEGGCSVPIGVVSNYDESTKVLTLKGIVINVEGTEWVEIEHKVTISNEREDSINCGKELAAKLTQNGAKEILDSINLDKIT | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 36045
Sequence Length: 327
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q1INI6 | MATLRIGSRGSQLALWQANHISALLRERGHEVELEIIKTTGDKILDVALAKVGTKGMFTKEIEEALAAGKVDVAVHSLKDLPTELPQGFELAAVTKRENPRDVFLSVKYDSISGLPQGAKVGTSSLRRQAQIKAIRPDLEIFPLRGNVDTRVRKLEQGEYDAIILAFAGLNRLGKTQLVKEIISEDVMCPAAGQGALGIEIRLGDTRMREILSFLNDYDARATTTAERALLNQLGGGCQVPIGAFAEVKDGQVHLTAICARPDGSEILRESKSGADPAHLGEEVGKTLLARGATKILEDVYSQNIAAPAQP | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33492
Sequence Length: 311
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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C4Z552 | MHYRIGTRGSKLALVQSEYVKRRMEEAYPEDTFELVIIKTTGDKVTDKPLAAIGTKGFFVKEIEEALLSGSIDMAVHSMKDMPAECAAGLTFAKAWKREDCRDVLILKTAGSFSELPSGAVIGTGSLRRACQLAMLRPDIQFTAIRGNVDTRINKLMDDSYGLDGIVLAAAGLNRLGRSSEITEYLDPEVVIPAPAQGVLAIETAEVNTELLDKINALSDDNSDREAVAERTFLRLTGGGCHAPVGAHCVTKDNGDLRMVVLFGNDDCSRILRIEVTGTDSEAVGHEAARMLGLE | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 31916
Sequence Length: 295
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
|
Q1MPL2 | MKKITIATRGSKLAFWQANYIKDQLQKMYSYLEVDLMVIKTKGDHILDVPLAKVGGKGLFVKEIEEALLSGEADCAVHSMKDVPMELPFELCLAAITEREDPTDMFLSIKYSGVKSLPENALVGTSSLRRQAQLLALRPDLQIIPLRGNIDTRLRKLMAEEFDAIIMATAGIKRLGLIAPYMSSLPCSVMLPAVGQGALGIEVQKERQDVLELFSFLNHKETYHCIQAERDFLAGLDGGCQVPIAGYATICKQETICLEGLVAKSDGSVMIRNRLERSVSDAYDIGMTLSKILLAEGADDILASMHTIL | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33993
Sequence Length: 309
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
|
Q5ZRY6 | MSAKIIRIATRQSPLALWQANHVREMLVKQWPNLSIELLPMITSGDRFLKDKLLSAGGKGLFVKELEEALLDKRADLAVHSTKDMPAQLPDGLLLTAICKRDNPFDALISPQFKSLAALPKNAIIGTSSLRRQSQLLAYNPNLQIKTLRGNIHTRLSKLESGEYQAIILAAAGLERMGLAHHITQLIPDDIMLPTCAQGALCIECRTDDLEIQELVHGLNDPISALCVHTERRVNAKLGGNCHIPFAVYCTITEEKLLLLRAKVLNMDGSQMIDDEQQGKIAEAEVIADRCTESLMTKGAMSLLSTIPS | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33987
Sequence Length: 309
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q6AHF1 | MIVSDGPAERRQGALRVGTRGSPLAVAQTQAVSAAVARATGFDIELVTVTTHGDTSRESLSELGGTGVFATALRDALRNGECDLVVHSLKDLPTAPAPGLVLGAVPKRADARDTLCARDGLRFGELPEGASVGTGSPRRAAQLRAQRPGLDIVDIRGNVDTRLSRVSAGDLDAVVLAAAGLGRLGRLDAATDFFSLSTMPTAPGQGALALEVREGDERGRGPIARALAAVDHATTCAATTAERAVLAGLEAGCAAPVGATAMIDDGLLFLTATVYRPDGAAQLTASHAATPDSFGAAHLDEAARDVGERVVAELLASGAADLAPLKGLR | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33375
Sequence Length: 329
EC: 2.5.1.61
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A5VM67 | MTNKVIVGSRKSKLAMAQTELVIASLEKIFPDIKFEIKNVITEGDRNRHVSLAKIGGKGVFVKEIEDELKDGTIDFAVHSLKDVMPILPEELVLGAFPKRVSPYDCLVSRKNLSSLNDLPKGARIGTNSLRRQGQLLSIRPDLKIIPIRGNIDTRLRKIDTEALDGIILAEAGLTRLNIDLSSYHVLDLQNYIMPAVGQGCLAIECRKNDTRIRKMLDQINDEESAYCVQVEREFMRELGGSCNFPIGGHAYAKNGQILFDGLIASPNGEHVIKETKIPANNSGVGKKVADQLLAKDKFGIIEGE | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33658
Sequence Length: 305
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
|
Q8Y6X5 | MKRKIIVGSRRSKLALTQSNWVINKLKENYPEFDFEIKEIVTKGDRILDVTLSKVGGKGLFVSEVEQALSDEAIDFAVHSMKDVPSSLKEGLIIGAIPKRESPLDCFVFNQVNSLDELPQGSVIGTSSLRRAAQLLKHRPDFVIKPIRGNIDTRLQKLHAENFDAIILAKAGLARMGWLENTTLKLEDIPPEVCLPAVGQGALAIECRESDQQIRDMLTSIHHEETGICVEAERVFLKKLNGGCEIPIAGFATRANEFVQFKGLVGNADGSIILESEQVGANPSEIGNKVAEDLLSEGADTIIKELRNV | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33937
Sequence Length: 309
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
|
Q4L709 | MRKLVVGSRRSKLALTQSQQFIDKLKAVDPTLEIEIKEIVTKGDRIVNKQLSKVGGKGLFVKEIQQELFDKEIDMAIHSLKDVPSIIPEGLTLGCIPDREVPFDAYISKNHIPLNELPDGSIIGTSSLRRGAQILSKYPNLEIKWIRGNIDTRLKKLEIEDYDAIILAAAGLRRMGWSDDIVTTYLDKDILLPAIGQGALGIECRSDDVELLELLSKVHNQAVANCVTAERTFLSAMDGSCQVPIGGYATNKENGEIEFTGLIMTPDGTKRYEHTEVGKNPVDLGEAVSRVLKEQGAYEIIKKLNEEQAH | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34349
Sequence Length: 310
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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A3CL78 | MKVIKVGTRKSKLAMTQTQQLVDQLKALHPERDFVLVPYTTKGDRLTHVSLQEIGGKGVFVKEIERALLAGEINMAVHSLKDMPAKLAEGCALGAISQREDVRDCLIFRQAGQTLADLPKGSLIGTSSIRRQVQLQAQRPDLAFKPLRGNIDTRIKKLEEGEYDAIVLAMAGLKRLGWLDQSRLHIQPLETSLCLPAISQGALAVECREEDEELLSLLAAVQDEKTAAEVAVERAVLAQMNADCTFPIAAFAQKNGQGYQLEAMLAKEDGQCIFVSLQGQDGQQLAEQAVRQLADKGAVGMPWLKK | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33494
Sequence Length: 306
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q30S90 | MKKLVIATRGSQLALWQSNHIKAILQEQNPGLEVELNVIVTTGDRIQDKALSKIGGKGLFLKELEEAMLQGEAQIAVHSLKDVPTVMPDGLILAAITEREDSRDALLSEKYANIDALPKNAVVGTSSLRRRMQIQKLRPDLIIKDLRGNVDTRIRKLKEGEFDAIILAAAGINRLSLLDAVKHVYPISLEEMVPSMGQGALGIEAVNDAEVLRIVAGLEDEYSRIETTIERSFVDELEGGCQVPIGVNASVLDDGTISIRAVLGLPNGEEMLSDSKITSKKDYENIGREIAAEFIEKGAKELLSRAEAMMENK | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34233
Sequence Length: 313
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q4KKQ4 | MTTRTEAVKAYLLDLQDRICAALETEDGGARFIEDAWTRPAGGGGRTRVIGDGAVIEKGGVNFSHVFGSGLPPSASAHRPELAGRGFEALGVSLVIHPHNPHVPTSHANVRFFIAEKEGEEPVWWFGGGFDLTPYYGNIDDCVHWHRVAERACAPFGADVYPRYKAWCDSYFHIKHRNEPRGIGGLFFDDLNEWDFDTSFAFMRAIGDAYIEAYLPIVQRRKAAAYTAQQREFQEFRRGRYVEFNLVYDRGTLFGLQSGGRTESILMSLPPQVRWGYDWKAEPGSEEARLTEYFLQDRDWLAASN | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 34437
Sequence Length: 305
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.3
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Q8XXC3 | MDTQAVRAYLLDLQDRITTAVGTLDGGTFVTDTWDKPPTERLRGSGRTCILENGAVLERGGVGFSHVMGDTLPPSATANRPELAGRGFEAMGVSLVFHPRNPYAPTVHMNVRCFVAQRPDAEPVWWFGGGMDLTPYYGFAEDAAHFHRTCKQALEPFGEELYPRFKQWCDDYFYLKHRKEARGVGGIFFDDFAELGFERSFEMMRAVGDALLPAWLPIAEQRHATPYGERERAFQAYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSMPPVANWRYDWQPEPGSPEAALYTDFLPARDWV | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 34212
Sequence Length: 302
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.3
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Q3B7D0 | MALRLGQLGSGPWWRAVRGDYAQLRAPSPRSASACVCRLPGTAGTQPRRGLGHGSSAGGGSRLGTGLAAALAGMAGLAAAVLGHVQRAEMVPKSSGARSPSPGRLEEDGDELARRCSTFMSSPVTELRELGRRPDDMKTKMELMIMETQAQVCRALAQVDGVADFSVDRWERKEGGGGITCVLQDGRVFEKAGVNISVVHGNLSEEAANQMRSRGKALKKKDGKLPFTAMGISSVIHPKNPYAPTMHFNYRYFEVEEADGKMHWWFGGGCDLTPTYLNREDAVHFHRTLKEACDQHGPDIYPKFKKWCDDYFFIAHRGERRGIGGIFFDDLDSPSKEEAFRFVKTCAEAVVPSYVPIVKKHCDDSYTPQDKLWQQLRRGRYVEFNLVYDRGTKFGLFTPGSRIESILMSLPLTARWEYMHSPPENSKEAEILEVLRHPKDWVH | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity).
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 49278
Sequence Length: 443
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Mitochondrion intermembrane space
EC: 1.3.3.3
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P13103 | MALNVIATLTLISVCVHADRICVGYLSTNSSERVDTLLENGVPVTSSIDLIETNHTGTYCSLNGVSPVHLGDCSFEGWIVGNPACTSNFGIREWSYLIEDPAAPHGLCYPGELNNNGELRHLFSGIRSFSRTELIPPTSWGEVLDGTTSACRDNTGTNSFYRNLVWFIKKNNRYPVISKTYNNTTGRDVLVLWGIHHPVSVDETKTLYVNSDPYTLVSTKSWSEKYKLETGVRPGYNGQRSWMKIYWSLIHPGEMITFESNGGFLAPRYGYIIEEYGKGRIFQSRIRMSRCNTKCQTSVGGINTNRTFQNIDKNALGDCPKYIKSGQLKLATGLRNVPAISNRGLFGAIAGFIEGGWPGLINGWYGFQHQNEQGTGIAADKESTQKAIDQITTKINNIIDKMNGNYDSIRGEFNQVEKRINMLADRIDDAVTDIWSYNAKLLVLLENDKTLDMHDANVKNLHEQVRRELKDNAIDEGNGCFELLHKCNDSCMETIRNGTYDHTEYAEESKLKRQEIDGIKLKSEDNVYKALSIYSCIASSVVLVGLILSFIMWACSSGNCRFNVCI | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
PTM: Palmitoylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63308
Sequence Length: 566
Subcellular Location: Virion membrane
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A6X6W2 | MSEMDKVQEKPSQTTKTEVQAKLPKVGVLLVNLGTPDGTSYGPMRRYLAEFLSDRRVIEWPRLIWYPILYGIVLNTRPKRSGKLYDRIWNREKNESPLRTYTRAQGEKLATALADYPNVVVDWAMRYGQPSIESVTDRLLQQGCERIVMFPLYPQYSATTTATVNDKFFEALMKKRFQPAVRIVPSYETEPVYIEALARSIEKHLETLSFKPEVVLASYHGIPKSYSDKGDPYRQQCLETSRLLQARLGLDDSQFRSTFQSRFGPEEWLQPYTDETVEELAKHGVKSMAVLNPGFVADCLETVDEIGNEAAEEFLENGGESFSHIPCLNDSEDGMKVIETLVRRELQGWV | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 40051
Sequence Length: 350
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q92FV4 | MKKRIAIVLFNLGGPKNLKSVKPFLFNLFYDKAIINLPNPLRYIIAKIISITREKKSQKIYSLIGGKSSLLQETEEQKLALTEKLKQLIKEDFAIFINMRYSAPFAKEVIGQIKKYNPSEIILLPLYSQFSSTTTGSSVKNFLQNLDIDIPIKTICCYPLEKDFIKAHVSLIKEKLYDKNFRILFSAHGLPEKIIKAGDPYSFQIKETVQAIVKELNIKDLDYKITYQSRVGPIEWLKPNTEDEIELAGKLKKDIIIVPISFVSEHVETLVELDIEYKLIADKYEIQYIRIPTLGTNKIFINSLTNILLRFINKVDTNLVMSSSSTRICPNEFTKCLCKLTS | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39238
Sequence Length: 342
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q9ZC84 | MNKRIAIVLFNLGGPEDIEYVKPFLFNLFYDKAIINLPNPLRYIIAKIISITREKKSQKIYSLIGSKSYLIQETEKQKLAITEKLKEFIKEDFIIFINMRYSTPFAKEVIGQIKEYNPSEIILLPLYPQFSSTTTGSSVKNFLQNIDIDIPIKTICCYPIEEDFIKAHVSIIKEKLYDKNFRILFSAHGLPKRIIKAGDPYSFQIKETVNKIVKELNIKDLDYKITYQSRVGPIEWLKPNTEDEIELAGKLKKDIIIVPISFVSEHVETLVELDIEYKLIADKYKIQYTRIPTLGTNKIFINSLTNILLRFINNTNTNLVMSSSSKRICPNKFTKCLCNLTN | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39611
Sequence Length: 342
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q5T8I9 | MEENNLQCSSVVDGNFEEVPRETAIQFKPPLYRQRYQFVKNLVDQHEPKKVADLGCGDTSLLRLLKVNPCIELLVGVDINEDKLRWRGDSLAPFLGDFLKPRDLNLTITLYHGSVVERDSRLLGFDLITCIELIEHLDSGDLARFPEVVFGYLSPSMIVISTPNSEFNPLFPSVTLRDSDHKFEWTRMEFQTWALYVANRYDYSVEFTGVGEPPAGAENVGYCTQIGIFRKNGGKATESCLSEQHDQHVYKAVFTTSYPSLQQERFFKLVLVNEVSQQVESLRVSHLPRRKEQAGERGDKPKDIGGSKAPVPCFGPVFTEVEKAKIENSPTPFCVGDKFFVPLQRLLAYPKLNRLCANEEMMRSVIADSIPLSSDGSAVVADLRNYFDEQFEF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis.
Catalytic Activity: S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide
Sequence Mass (Da): 44525
Sequence Length: 393
Subcellular Location: Cytoplasm
EC: 2.1.1.386
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Q9UST9 | MGVSSFYPPLHVQRRRKLFKILQGGFPVRSLLDIGCGDARFLSYLVPCNDQVPIEFLAGIDINEQSIERATEALQVRTEDFLQLRWRPLHIELLLGNIKDFTHYKHVDAVVASEFIEHCQVAEILAFEKLVFGNLKPNVCVVSTPNFEFNTIFEKLSTLTSSISSRTSTNFRHPEHVFEWDRKEFAKWAYKICKRYPEYTVEFTGCGLLNDLIDGDDLLHFRPSSTYGFCTQIAVFHQSKNNAASHCFLKDQNSSILLYKKITYPFMEQLFPPTVQQFMNLLKKAFFDHLFGRHCLLLFQVIAGKCALSVKLPFLFIWESSPLIRHAFHYDDSIYLSYCPELKKSKHKGIALANSFSFRIAKVLKKSRIFIITFHHYV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of small RNAs.
Catalytic Activity: S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide
Sequence Mass (Da): 43827
Sequence Length: 378
Subcellular Location: Cytoplasm
EC: 2.1.1.386
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Q230X8 | MIEAYETDVFMDPIGMKVWEKRHQYVATKLSALNCKRVLDMGTNTCKLIQRLSRSLQFTQIDGLDIDGQLLETQGIQNAKPDLIQNQYASMRDHQLVVNLYQGSALNKIQHLKDQQYDAVILVELIEHLQVEDVFLIEQNLFGFLRPQFVIVTTPNSDFNVYFNFKEQGVLFRDKDHKFEWSQNQFQIWAQKVCQNYGYKVIELTGVGEHKTEGTKNGFCTQIVVFEKDTQQEKYLNFAFFNLQEGEIRQVCQILYPFESKEQHFQREVVDSIRYILHITDKQNQFEDGSYQNYTTLSRIMQNHSISSNWQIQGDYFKLKTYIQNISEFLVHENQFNFQESFVTLNYQAQMEDEENEDQLESDSENVKMQQQQYYFSNDNCFSTKDTTYSSFSTADNLFSQKIQLGQQQMALEEIELEDTIDY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Required for programmed DNA elimination.
Catalytic Activity: S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide
Sequence Mass (Da): 49946
Sequence Length: 423
Subcellular Location: Nucleus
EC: 2.1.1.386
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C0IN03 | MELEFFKPPLYQQRYQFVKSYVDTYKPKKVADLGCSTCSLLHTLRFWDCIKVLVGLDIDEDVLSRKKFTLTPLPAHYLEPRNTSLTINLYQGSVTQKDPALLGFDLITCIELIEHLEAEELENFREVLFGFMAPITVIISTPNAEFNILFPKCTGFRHPDHKFEWNRREFQSWATEVAKCFNYTVEITGVGEPPRDSKNVGFCSQIAVFTRNYTESEESLQRKMECKSVYKTVLHIVYPSLQEEKYLRRAVQKVALFHAYQIKANFLQQFIHREEEEEPHNTDTEHRPCMDLKLTSRWPTLPQTEQDESMEPFLQEDTLYVPLKKIFSVPKVKELCGNMDNLRTMITGEATLSNDGNAILYHIDLENSC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis.
Catalytic Activity: S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide
Sequence Mass (Da): 42977
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 2.1.1.386
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Q05819 | MKKQILYLIVLQQLFLCSAYAQQKKSGNIPYRVNVQADSAKQKAIIDNKWVAVGINKPYALQYDDKLRFNGKPSYRFELKAEDNSLEGYAAGETKGRTELSYSYATTNDFKKFPPSVYQNAQKLKTVYHYGKGICEQGSSRSYTFSVYIPSSFPDNATTIFAQWHGAPSRTLVATPEGEIKTLSIEEFLALYDRMIFKKNIAHDKVEKKDKDGKITYVAGKPNGWKVEQGGYPTLAFGFSKGYFYIKANSDRQWLTDKADRNNANPENSEVMKPYSSEYKTSTIAYKMPFAQFPKDCWITFDVAIDWTKYGKEANTILKPGKLDVMMTYTKNKKPQKAHIVNQQEILIGRNDDDGYYFKFGIYRVGNSTVPVTYNLSGYSETAR | Function: Degrades heparin and heparan sulfate. Also implicated in the release of heparin-bound growth factors from the extracellular matrix.
PTM: The N-terminus is blocked.
Catalytic Activity: Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 43807
Sequence Length: 384
Subcellular Location: Periplasm
EC: 4.2.2.7
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P05546 | MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS | Function: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.
PTM: Phosphorylated by FAM20C in the extracellular medium.
Sequence Mass (Da): 57071
Sequence Length: 499
Domain: The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition.
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P49182 | MKHPLCTLLSLITFMCIGSKGLAEQLTNENLTTSFLPANFHKENTVTNDWIPEGEEDEDYLDLEKLLGEDDDYIYIIDAVSPTDSESSAGNILQLFQGKSRIQRLNILNAKFAFNLYRVLKDQATTSDNLFIAPVGISTAMGMISLGLRGETHEEVHSVLHFRDFVNASSKYEVTTIHNLFRKLTHRLFRRNFGYTLRSVNGLYIQKQFPIREDFKAAMREFYFAEAQEANFPDPAFISKANNHILKLTKGLIKEALENIDPATQMLILNCIYFKGTWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPRKLSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVEVLKSMGITKLFNKNGNMSGISDQRIAIDLFKHQSTITVNEEGTQAAAVTTVGFMPLSTQVRFTVDRPFLFLVYEHRTSCLLFMGKVTNPAKS | Function: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.
PTM: N-glycosylated; different glycan composition appears to lead to two forms of this protein (68 and 72 kDa).
Sequence Mass (Da): 54497
Sequence Length: 478
Domain: The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition.
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Q2U0K2 | MWWPRATADRLQTCTFWFLWLFTWDDEIDQSTSDLFIHIHKANDFRKESLEYVKFCLGVGDDETAKWDFQNNPPNRPLIRSLDVIGAHLQKVYNHDQIMTFVNEIDYYMGCQQREQKRKLTGRLPIVAEYLETRMGTSAVTSMLALNEYGGALILGLKRR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing.
Sequence Mass (Da): 18825
Sequence Length: 160
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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P49008 | MKRLTFGACICCLLSLMACSQKAKQVQIPEYDKGINIIPLPMQLTESDDSFEVDDKTTICVSAEELKPIAKLLADKLRASADLSLQIEIGEEPSGNAIYIGVDTALPLKEEGYMLRSDKRGVSIIGKSAHGAFYGMQTLLQLLPAEVESSNEVLLPMTVPGVEIKDEPAFGYRGFMLDVCRHFLSVEDIKKHIDIMAMFKINRFHWHLTEDQAWRIEIKKYPRLTEVGSTRTEGDGTQYSGFYTQEQVRDIVQYASDRFITVIPEIEMPGHAMAALAAYPQLACFPREFKPRIIWGVEQDVYCAGKDSVFRFISDVIDEVAPLFPGTYFHIGGDECPKDRWKACSLCQKRMRDNGLKDEHELQSYFIKQAEKVLQKHGKRLIGWDEILEGGLAPSATVMSWRGEDGGIAAANMNHDVIMTPGSGGLYLDHYQGDPTVEPVAIGGYAPLEQVYAYNPLPKELPADKHRYVLGAQANLWAEYLYTSERYDYQAYPRLLAVAELTWTPLAKKDFADFCRRLDNACVRLDMHGINYHIPLPEQPGGSSDFIAFTDKAKLTFTTSRPMKMVYTLDETEPTLTSTPYTVPLEFAQTGLLKIRTVTAGGKMSPVRRIRVEKQPFNMSMEVPAPKPGLTIRTAYGDLYDVPDLQQVASWEVGTVSSLEEIMHGKEKITSPEVLERRVVEATGYVLIPEDGVYEFSTENNEFWIDNVKLIDNVGEVKKFSRRNSSRALQKGYHPIKTIWVGAIQGGWPTYWNYSRVMIRLKGEEKFKPISSDMLFQ | Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 87661
Sequence Length: 777
Subcellular Location: Cell outer membrane
EC: 3.2.1.52
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P48823 | MSFITSAHATAAQVPLTTSQMLGQKLMLDFRYYCGESKKPSGDCRAAMTTLPPELSELISRYDIGGAILFAENVQNTAQIISLTNALQSAAQQSKSQLPLFIAIDQEGGRVARINREQATSFTGNMSIGATYPKQGDIYATKVASAIGKELNSLGINVNFAPTVDVNSNPNNPVINVRSFSENPTVVTKLGLAQVKAFEAAGVLSALKHFPGHGDTHVDSHTGLPRVDHDRDKINQQDLLPFAEIIKASPPGMIMTAHIQYPALDNSKVVNSQGESMIRPATMSYQIMTQLLRHELGYQGVTVTDALDMAGISDFFNPVDATIETFNAGVDIALMPIAIRNRADIKRFEQYMAQLADALETNKLNQEQLSSSMARIAKLKTKLPQSSASLAIANSTLGNPSHRRLEAELALAAITEVKNDGVLPLRDNAQVVHLIMPDRQKCFALEQALQTYSKNSLTLSCTSLQAYDPDIAHDAIKQADMIIAAHASPPQSAVEIGGMDDVKKLREHGVARNVQPAALKALLQYGQQQGKKQLFISLRAPYEISTFGPLSNAVLASYAYNVDVNHDKKVAGPAYTALAKVILGIAKAEGSLPVTVNH | Function: Most active towards p-nitrophenyl-N-acetyl-beta-D-glucosaminide(PNP-beta-GlcNAc) and diacetylchitobiose.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64539
Sequence Length: 598
EC: 3.2.1.52
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Q54K55 | MIILKRNIVFLLIIIIVLGIFIATSIEIKNYKLSLNQNKNEISKNPPIWPAPFYGQFGNNSILISKEFNFTIISDSTLLLNKTLSKYYNLIFTQDNLINSSSNTLNKLNINLKSKNEILKFGFDESYKLIIKNNENSKLEGNTVYGIMRGLETFYQLIKYNFSDNSYFIENCLPLIINDKPRFPHRGVMLDTSRHFYSVDTILKVIESLSYNKFNTLHWHIIDSQSFPLSSKSYPNLINGAWSKSEIYSYHDIKRIIKYGKENGIRIQLEIDMPGHAKSWSVGYPDLLPHGWNDSTTTIKCPDYDVPLDPSSPLSLPISFGLLSEFSGTDYGYNPNYDDKSNNLFNLTVDDLFHVGGDEIEYQCWNNSKRIKDWMNENNLKTFQDVAKQFQLKIIKQLLKIGKIPVLWEDTFQLFYKDLPKDVIVEIYHDQSTAINATNNGYKIISSIARYWYLEYSYSNWIRAYNFEPTLNISKSNIHLVLGGEGAIWSESIDSSNLFQKLYPTSSAIAERLWSPIYYTNLLNAKSRLQSFRCSLLKRGINSAPLNNSSPLSAFSCYNS | Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64555
Sequence Length: 560
Subcellular Location: Lysosome
EC: 3.2.1.52
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Q54K56 | MKLKFIFLILFFIIGNSIGIKISKEINKIKLNDISIDGEILLNKSSDSSSSQSSKIINIWPMPKKVLNGDITVYISPHFQFTTNLTKSTTLKKAMDRYYKLIFTEDSKSHSGISILNEIKILVKSEDETLQIGFDESYEIYIDDSGDDGGKIIAETVYGAIRGLETLYQMIGFDYQREYYQIKHCPWIIQDSPRYPHRGVMLDTSRHFYSVDVLKEFIEALAYNKFNVFHWHAVDSQSFPLTSTTFPKITKGSWSSQEIYSTRDIKEIIQHAKEYGIRVELEIDMPGHAYSWGIGYPSVLPANFSHSIQCQQPCPTECNIPLDVSSKESYVIAMGLLEEFNGASMFNESFFHIGGDEVAYSCWNNSLRIVDWMKRENISSFQDAAIFFEIKAIEQLIQLGKTPVMWEDAYLLFGSSGITEKLPEEVVVQIYHDPLLALNTTRDGYKTLQSPYWPYYLDNPSVDWEKVYEFEPSNGIHEKRLRLLLGGETCMWSELVDASNLFAKVFPRAFATAERLWFSIENSNSTTFAKPRLERFRCFLLERGIGAAPLNSTSPDDPNSCYSS | Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64566
Sequence Length: 564
Subcellular Location: Lysosome
EC: 3.2.1.52
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Q86M34 | MIVLLLLISYCFAGNGVNVKNQLLLMPYPTTVNAQFGSNDCVEATSNIKMVLSNNCQNDPNCLSFMTFNFNHTITYPLQRQRNLEDFRVSIFAPIDIEEMKGNVVYSANTVNIELTGNNIEEIYPPLKIGIDESYSLDVTKEGIKISATTVYGARLGLETLIQMLRPYQGKYIIKHIPIMIEDKPRLQWRGLMIDVARNSFSRSAFVKIINAMAAIKANVLHIHLSDAQTFMFESKEYPELSKKGAFFQNKVLTQSFIKQLVQYGAKRGVIVYPEIDTPAHTASWNAGYPGVVADIWDYIVSSSMRYGENVLALNPANEKTFSIIDALMKEMGEVFGNDYVHFGGDEVWTGAWSKAKEYPAILEWMNKKGINTLKELEAYFNKYAQEQIIKNGKTPVCWEEVYQKGSADKKTIIQVWNNVNLLKEAATAGYKVILSAGYYLDMQMPLCSDYVADSCTNPNHMWVWTNRDMYRNDPIKELDYATKQNVLGGEACSWDESVDEQNFFDRVFQRFSAVAERFWSSEDITDPESHEVRANYVRCLGLRRNFLKGTGPLYHSYCQLPEDI | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates . May contribute to amoebic pathogenicity and may be involved in the destruction of extracellular matrix components (Probable).
PTM: Glycosylated.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64372
Sequence Length: 565
Subcellular Location: Cytoplasmic granule
EC: 3.2.1.52
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P49614 | MRHRGLGLAALLALLAAVAPRSSAAAGAALWPMPLSVKTSPRLLHLSRDNFSIGYGPSSTAGPTCSLLQEAFRRYHEYIFGFDKRQRRPAKPNSAIELQQLLVTVVLDSECDLFPNITSDESYTLLVKEPVAFLKANRVWGVLRGLETFSQLIYQDSYGTFTVNESDIIDSPRFPHRGILIDTARHFLPVKSILKTLDAMAFNKFNVLHWHIVDDQSFPYQSVTFPELSNKGSYSLSHVYTPNDVHTVIEYARLRGIRVIPEFDSPGHTQSWGKGQKDLLTPCYNEHKQSGTFGPINPILNSTYNFLSQFFKEVSMVFPDHFVHLGGDEVEFQCWESNPEIQGFMKQKGFGKDFRRLESFYLQKLLGIVSTVKKGSIVWQEVFDDHVKLLPGTIVQVWKNQVYTEELREVTAAGFPVILSAPWYLDWISYGQDWRNYYKVDPLHFDGSQEQKKLVIGGEACLWGEFVDATNLTPRLWPRASAVGERLWSPEDITSVGNAYNRLTVHRCRMVRRGISAEPLFTGYCDYEYKT | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (By similarity). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity).
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 60427
Sequence Length: 531
Subcellular Location: Lysosome
EC: 3.2.1.52
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P07686 | MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides . The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide . Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A . During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity).
PTM: N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc(2) and Man(5 to 7)-GlcNAc(2), respectively.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 63137
Sequence Length: 556
Subcellular Location: Lysosome
EC: 3.2.1.52
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