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CATH Superfamily 2.40.70.10

Acid Proteases

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:

"
Acid Proteases
".

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 23189: Putative gag-pol polyprotein

There are 10 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
RNA-directed DNA polymerase. [EC: 2.7.7.49]
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
  • Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time.
  • Cannot initiate a chain de novo.
  • Requires a RNA or DNA primer.
  • DNA can also serve as template.
  • See also EC 2.7.7.7.
 48 A1Z651 D0UFA3 P03355 P03356 P03370 P03371 P04584 P05895 P05896 P05897
(38 more...)
Retroviral ribonuclease H. [EC: 3.1.26.13]
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
  • Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication.
  • To perform this task the enzyme combines two distinct activities.
  • The polymerase domain (EC 2.7.7.49) occupies the N-terminal two- thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third.
  • The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.
 34 P03370 P03371 P04584 P05895 P05896 P05897 P05962 P11204 P12451 P12502
(24 more...)
Exoribonuclease H. [EC: 3.1.13.2]
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
  • This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.
 34 P03370 P03371 P04584 P05895 P05896 P05897 P05962 P11204 P12451 P12502
(24 more...)
DNA-directed DNA polymerase. [EC: 2.7.7.7]
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
  • Cannot initiate a chain de novo.
  • Requires a primer which may be DNA or RNA.
  • See also EC 2.7.7.49.
 30 A1Z651 D0UFA3 P03355 P04584 P05895 P05896 P05897 P05962 P12451 P12502
(20 more...)
Ribonuclease H. [EC: 3.1.26.4]
Endonucleolytic cleavage to 5'-phosphomonoester.
  • Acts on RNA-DNA hybrids.
 14 A1Z651 D0UFA3 P03355 P03356 P10272 P10273 P11227 P21414 P26808 P26809
(4 more...)
Human endogenous retrovirus K endopeptidase. [EC: 3.4.23.50]
Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ- cleavage site.
  • Belongs to peptidase family A2.
 13 P10265 P63119 P63120 P63121 P63122 P63123 P63124 P63125 P63127 P63128
(3 more...)
HIV-2 retropepsin. [EC: 3.4.23.47]
Endopeptidase for which the P1 residue is preferably hydrophobic.
  • Responsible for the post-translational processing of the human immunodeficiency virus polyprotein.
  • Belongs to peptidase family A2.
 12 P04584 P05962 P12451 P15833 P17757 P18042 P18096 P20876 P24107 Q74120
(2 more...)
HIV-1 retropepsin. [EC: 3.4.23.16]
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
  • Present in human immunodeficiency virus type 1.
  • Contributes to the maturation of the viral particle, and is a target of antiviral drugs.
  • Active enzyme is a dimer of identical 11-kDa subunits.
  • Similar enzymes occur in other retroviruses.
  • Belongs to peptidase family A2.
 11 M1KP19 P05895 P05896 P05897 P12502 P19505 P22382 P27973 P27980 Q02836
(1 more...)
DUTP diphosphatase. [EC: 3.6.1.23]
dUTP + H(2)O = dUMP + diphosphate.
    		 8 A0A061HYU0 P03370 P16901 P23426 P23427 P31625 P35956 Q1W0S4
    Acireductone dioxygenase (Fe(2+)-requiring). [EC: 1.13.11.54]
    1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 4-(methylthio)-2- oxobutanoate + formate.
    • If Ni(2+) is bound instead of Fe(2+), the reaction catalyzed by EC 1.13.11.53 occurs instead.
    • The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway.
    		 1 A0A061I5E9