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GO_0033676
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GO_0033676 |
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obsolete N-terminal peptidyl-serine deamination
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GO_0018059 |
[OBSOLETE. The oxidative deamination of N-terminal peptidyl-serine to form pyruvic acid with an amide bond between its 1-carboxyl group and the N-terminal residue.] |
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N-terminal protein amino acid deamination, from amino carbon
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GO_0018058 |
[The oxidative deamination of the alpha carbon of an encoded N-terminal amino acid, to form pyruvic acid retaining an amide bond between its 1-carboxyl group and the adjacent residue. The pyruvate 2-oxo group may become an enzyme active site, or it may be reduced to an alcohol.] |
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peptidyl-lysine oxidation
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GO_0018057 |
[The oxidation of the terminal amino-methylene groups of peptidyl-L-lysine or peptidyl-5-hydroxy-L-lysine to aldehyde groups to form allysine or hydroxyallysine residues, respectively; these are intermediates in the formation of covalent cross-links between adjacent polypeptide chains in proteins such as collagens.] |
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GO_0018056
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GO_0018056 |
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GO_0018055
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GO_0018055 |
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obsolete peptidyl-lysine biotinylation
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GO_0018054 |
[OBSOLETE. The covalent modification of peptidyl-lysine by biotin to form peptidyl-N6-biotinyl-L-lysine.] |
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obsolete C-terminal peptidyl-valine amidation
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GO_0018053 |
[OBSOLETE. The formation of a C-terminal peptidyl-valine amide by hydrolysis and oxidation of an interior Val-Gly peptide in a secreted protein.] |
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cytochrome c-heme linkage
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GO_0018063 |
[The linkage of cytochromes and other heme proteins to heme.] |
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obsolete peptidyl-tryptophan succinylation
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GO_0018062 |
[OBSOLETE. The modification of an N-terminal peptidyl-tryptophan residue to form peptidyl-N2-succinyl-L-tryptophan.] |
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peptidyl-L-3-phenyllactic acid biosynthetic process from peptidyl-phenylalanine
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GO_0018061 |
[The modification of a N-terminal peptidyl-phenylalanine residue by either oxidative deamination or by transamination and subsequent reduction to form peptidyl-L-3-phenyllactic acid.] |
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obsolete N-terminal peptidyl-cysteine deamination
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GO_0018060 |
[OBSOLETE. The oxidative deamination of N-terminal peptidyl-cysteine to form pyruvic acid with an amide bond between its 1-carboxyl group and the N-terminal residue.] |
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3'-5' DNA/RNA helicase activity
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GO_0033679 |
[Unwinding of a DNA/RNA duplex in the 3' to 5' direction, driven by ATP hydrolysis.] |
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5'-3' DNA/RNA helicase activity
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GO_0033678 |
[Unwinding of a DNA/RNA duplex in the 5' to 3' direction, driven by ATP hydrolysis.] |
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obsolete peptide cross-linking via 4'-(L-tryptophan)-L-tryptophyl quinone
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GO_0018069 |
[OBSOLETE. The cross-linking of a tryptophan residue to tryptophyl quinone to form 4'-(L-tryptophan)-L-tryptophyl quinone, a cofactor found at the active site of methylamine dehydrogenase.] |
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obsolete peptidyl-L-2',4',5'-topaquinone biosynthetic process from peptidyl-tyrosine
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GO_0018068 |
[OBSOLETE. The modification of protein tyrosine to L-2',4',5'-topaquinone, characteristic of the active site of copper amine oxidases.] |
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obsolete peptidyl-L-3',4'-dihydroxyphenylalanine biosynthetic process from peptidyl-tyrosine
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GO_0018067 |
[OBSOLETE. The modification of protein tyrosine to peptidyl-L-3',4'-dihydroxyphenylalanine (DOPA).] |
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obsolete protein-cofactor linkage
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GO_0018065 |
[OBSOLETE. The covalent attachment of a cofactor to a protein.] |
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protein-L-histidine N-tele-methyltransferase activity
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GO_0018064 |
[Catalysis of the reaction: L-histidyl-[protein] + S-adenosyl-L-methionine = N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine.] |
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obsolete peptidyl-histidine bromination
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GO_0018074 |
[OBSOLETE. The bromination of peptidyl-histidine to form peptidyl-L-bromohistidine; the position of the bromine substitution is unknown.] |