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:

"
Phosphatidylinositol 3-/4-kinase, catalytic domain
".

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 1687: Phosphatidylinositol 3-kinase gamma isoform

There are 12 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
Phosphatidylinositol 3-kinase. [EC: 2.7.1.137]
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo- inositol 3-phosphate.
    433 A0A016WFY8 A0A023F599 A0A024GV66 A0A026WWV9 A0A044RGA8 A0A060RTZ4 A0A060WR34 A0A061AQ32 A0A061BA46 A0A061H6Q6
    (423 more...)
    1-phosphatidylinositol 4-kinase. [EC: 2.7.1.67]
    ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo- inositol 4-phosphate.
      180 A0A023BAL1 A0A060RP41 A0A074STD5 A0A074TZE0 A0A077TKI2 A0A077TP82 A0A077X856 A0A077XB77 A0A077XCU5 A0A077Y2M5
      (170 more...)
      Phosphatidylinositol-4,5-bisphosphate 3-kinase. [EC: 2.7.1.153]
      ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
      • This enzyme also catalyzes the phosphorylation of PtdIns4P to PtdIns(3,4)P(2), and of PtdIns to PtdIns3P.
      43 A0A024R720 A0A061I7L5 A0A096MY63 A0A0A1TX84 A0A0A1U299 A0A0A1U2Z4 A0A0A1UEI9 A0A0A1UEJ1 A0A0D9RKI4 A0A0G2K344
      (33 more...)
      Histone-lysine N-methyltransferase. [EC: 2.1.1.43]
      S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
        31 A0A0V0RW82 A0A0V0TJ41 A0A0V0TJ63 A0A0V0VE62 A0A0V0VE66 A0A0V0VEG2 A0A0V0X582 A0A0V0X5B5 A0A0V0ZSE1 A0A0V0ZSE8
        (21 more...)
        Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
        ATP + a protein = ADP + a phosphoprotein.
        • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
        • Formerly EC 2.7.1.37 and EC 2.7.1.70.
        19 A0A024R720 A0A061HZ27 A0A061IHE6 A0A096MY63 A0A0D9RKI4 A0A0G2K344 D2GUC9 F1Q3M8 G7NZ32 H2QNS1
        (9 more...)
        Phosphatidylinositol-4-phosphate 3-kinase. [EC: 2.7.1.154]
        ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl- 1D-myo-inositol 3,4-bisphosphate.
        • This enzyme also phosphorylates PtdIns to PtdIns3P.
        16 A0A061IAB7 A2RUF7 B7PIF4 B7QET6 E0VBF9 G4VAN8 L7RRS0 O00443 O00750 O70167
        (6 more...)
        Glycylpeptide N-tetradecanoyltransferase. [EC: 2.3.1.97]
        Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
        • The enzyme from Saccharomyces cerevisiae is highly specific for tetradecanoyl-CoA, and for N-terminal glycine in oligopeptides containing serine in the 5-position.
        • The enzyme from mammalian heart transfers acyl groups to a specific acceptor protein of 51 kDa.
        2 G0R493 G0R500
        Ribonuclease P. [EC: 3.1.26.5]
        Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
        • Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
        1 B0EJW7
        Aminopeptidase Y. [EC: 3.4.11.15]
        Preferentially, release of N-terminal lysine.
        • Inhibited by Zn(2+) and Mn(2+).
        • Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4- nitroanilide.
        • Belongs to peptidase family M28B.
        1 G0R0I5
        Type I site-specific deoxyribonuclease. [EC: 3.1.21.3]
        Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.
        • Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine.
        • They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence.
        • Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.
        • Formerly EC 3.1.24.1 and EC 3.1.24.2.
        • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
        1 G0QKS1
        Exodeoxyribonuclease VII. [EC: 3.1.11.6]
        Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
        • Preference for single-stranded DNA.
        • Similar enzyme: Micrococcus luteus exonuclease.
        1 G0R0I5
        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.
        1 G0R2G9