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CATH Superfamily 3.10.28.10

Homing endonucleases

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:

"
Homing endonucleases
".

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 21878: Replicative DNA helicase Mcm

There are 6 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
DNA helicase. [EC: 3.6.4.12]
ATP + H(2)O = ADP + phosphate.
  • DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
  • Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15).
  • Some helicases unwind DNA as well as RNA (4,9).
  • May be identical with EC 3.6.4.13 (RNA helicase).
 19 A0A081N2H9 A0A101D3L2 A0A142B7P5 A0A170PG20 A0A1B7WWN5 A0A1C0VHV8 A0A1F8JNE1 A0A1J1K4Z6 A0A1J1KSL1 H1KWC7
(9 more...)
DNA topoisomerase (ATP-hydrolyzing). [EC: 5.99.1.3]
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
  • Can introduce negative superhelical turns into double-stranded circular DNA.
  • One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.99.1.2).
 10 A0A0G0KMV8 A0A0S4MSG7 A0A0S4PHF7 A0A0S4PRI2 A0A1G2FE56 A0A1G2FIE8 A0A1G2FPD7 A0A1J4WQP0 A0A1J5GT08 C0QRN3
H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
  • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
  • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
  • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
  • This movement is driven by the H(+) electrochemical potential gradient.
  • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
  • Formerly EC 3.6.1.34.
 3 F4HM98 I6TY35 Q8U4A6
Glutamine--fructose-6-phosphate transaminase (isomerizing). [EC: 2.6.1.16]
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.
  • Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
  • Formerly EC 5.3.1.19.
 3 A0A1G1JWE5 F6BAJ4 Q58815
Ribonucleoside-diphosphate reductase. [EC: 1.17.4.1]
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
  • This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair.
  • There are three types of this enzyme differing in their cofactors.
  • Class Ia enzymes contain a diferric-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin.
  • In all cases the cofactors are involved in generation of a transient thiyl radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl radical.
  • The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues.
  • A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position.
  • The disulfide bridge is reduced by the action of thioredoxin.
  • Cf. EC 1.1.98.6 and EC 1.17.4.2.
 1 A0A140L802
DNA-directed RNA polymerase. [EC: 2.7.7.6]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
  • Can initiate a chain de novo.
  • In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
  • See also EC 2.7.7.19 and EC 2.7.7.48.
 1 C9RDK7