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CATH Superfamily 2.60.40.10

Immunoglobulins

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:

"
Immunoglobulins
".

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 137585: Inactive tyrosine-protein kinase 7

There are 8 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
Receptor protein-tyrosine kinase. [EC: 2.7.10.1]
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
  • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
  • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
  • Formerly EC 2.7.1.112.
 286 A0A061IQG3 A0A061IQG3 A0A087QYQ0 A0A087QYQ0 A0A087RFH5 A0A087RFH5 A0A087RJP0 A0A087RJP0 A0A087V453 A0A087V453
(276 more...)
Protein-tyrosine-phosphatase. [EC: 3.1.3.48]
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
  • Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
 154 A0A060Y8W5 A0A060Y8W5 A0A061I2U3 A0A061I2U3 A0A0J9R470 A0A0J9R470 A0A0J9R4Q9 A0A0J9R4Q9 A0A0J9R500 A0A0J9R500
(144 more...)
Phospholipid-translocating ATPase. [EC: 3.6.3.1]
ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other.
  • Formerly EC 3.6.3.13.
 12 A0A0V1N3Q3 A0A0V1N3Q3 A0A0V1N3R8 A0A0V1N3R8 A0A0V1N3S4 A0A0V1N3S4 A0A0V1N470 A0A0V1N470 A0A0V1N475 A0A0V1N475
(2 more...)
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 6 A1KZ92 A1KZ92 A4IGL7 A4IGL7 Q3UQ28 Q3UQ28
    Rhodopsin kinase. [EC: 2.7.11.14]
    ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.
    • Acts on the bleached or activated form of rhodopsin.
    • Also phosphorylates the beta-adrenergic receptor, but more slowly.
    • Does not act on casein, histones or phosphovitin.
    • Inhibited by Zn(2+) and digitonin (cf. EC 2.7.11.15 and EC 2.7.11.16).
    • Formerly EC 2.7.1.97 and EC 2.7.1.125.
    		 4 B7Q2Q7 B7Q2Q7 E0V9F8 E0V9F8
    Iodide peroxidase. [EC: 1.11.1.8]
    (1) 2 iodide + H(2)O(2) + 2 H(+) = diiodine + 2 H(2)O. (2) [Thyroglobulin]-L-tyrosine + iodide + H(2)O(2) = [thyroglobulin]-3- iodo-L-tyrosine + 2 H(2)O. (3) [Thyroglobulin]-3-iodo-L-tyrosine + iodide + H(2)O(2) = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H(2)O. (4) 2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H(2)O(2) = [thyroglobulin]- L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H(2)O. (5) [Thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L- tyrosine + H(2)O(2) = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H(2)O.
    • Thyroid peroxidase catalyzes the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine.
    • It catalyzes both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.
    		 2 B7QCX2 B7QCX2
    Cellulose 1,4-beta-cellobiosidase (non-reducing end). [EC: 3.2.1.91]
    Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
      		 2 B7Q2Q7 B7Q2Q7
      IgA-specific serine endopeptidase. [EC: 3.4.21.72]
      Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa bonds in the hinge region. No small molecule substrates are known.
      • Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae.
      • Some other bacterial endopeptidases with similar specificity are of metallotype (see EC 3.4.24.13).
      • Belongs to peptidase family S6.
      		 2 E0VZZ8 E0VZZ8
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