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CATH Superfamily 3.40.50.410

von Willebrand factor, type A domain

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:

"
von Willebrand factor, type A 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 19681: Copine III, isoform CRA_a

There are 4 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: 2.3.2.23, 2.3.2.27 and 6.2.1.45. [EC: 6.3.2.19]
    		13 A0A0B2NSH4 A0A0B2PB96 A0A0B2R5V1 A0A0B2RCR6 A0A0B2RLM6 A0A0B2RQK4 A0A0B2SES2 A0A0B2SG11 A0A0B2SJ90 A0A0B2SMZ5
    (3 more...)
    RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
    S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
    • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
    • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
    • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
    • Formerly EC 6.3.2.19 and EC 6.3.2.21.
    		 7 A0A178U7R6 A0A178VGS3 Q8LB88 Q8RX26 Q9LY87 Q9SAL0 Q9SS90
    Alcohol sulfotransferase. [EC: 2.8.2.2]
    3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate.
    • Primary and secondary alcohols, including aliphatic alcohols, ascorbate, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15).
    		 1 B0ESD5
    CTP synthase (glutamine hydrolyzing). [EC: 6.3.4.2]
    ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.
    • The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place.
    • The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP.
    • Ammonia then reacts with this intermediate generating CTP and a phosphate.
    • The enzyme can also use ammonia from the surrounding solution.
    		 1 A0A1J7H9M2
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