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CATH Superfamily 2.40.50.140

Nucleic acid-binding proteins

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Nucleic acid-binding proteins
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 54616: 30S ribosomal protein S1

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Transferred entry: 1.17.7.4. [EC: 1.17.1.2]
    		64 A0A076JHN6 A0A076JM87 A0A080N2I7 A0A083X035 A0A086Z039 A0A086ZJY8 A0A086ZNZ8 A0A086ZUI9 A0A087A9T3 A0A087AEB2
    (54 more...)
    Polyribonucleotide nucleotidyltransferase. [EC: 2.7.7.8]
    RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.
    • ADP, IDP, GDP, UDP and CDP can act as donors.
    		 5 A0A0D6IFX6 A0A0K0X9A2 A0QYY6 L8FDD7 Q0RPU6
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase. [EC: 1.17.7.4]
    (1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+).
    • Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase.
    • This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis.
    • This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts.
    • The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate.
    • Formerly EC 1.17.1.2.
    		 2 A0A076JHN6 A0A087VUI3
    DNA ligase (NAD(+)). [EC: 6.5.1.2]
    NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
    • The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
    • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue.
    • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
    • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
    • RNA can also act as substrate, to some extent.
    • Cf. EC 6.5.1.1, EC 6.5.1.6, and EC 6.5.1.7.
    		 1 B4S4Y6
    Dephospho-CoA kinase. [EC: 2.7.1.24]
    ATP + 3'-dephospho-CoA = ADP + CoA.
      		 1 A0A1K7L0J1