SCOP
[Home]
Summary of major changes in the classification that occurred in
SCOP 1.63
(Last modified 2003-06-09).
Membrane all-alpha fold [f.2; 56868], that was not a true fold, has been
dissolved with all its content having been reclassified from scratch to a
number of new and existing folds and superfamilies.
E-set domains family [b.1.1.5; 49208,
and b.1.1.6; 68902] of the immunoglobulin
superfamily have been transformed into a superfamily with its content having
been rearranged in several (new) families; one protein from the original family
[sp=69166] has been reassigned to a new fold.
In Nucleotidyltransferases fold/superfamily [e.9.1;
56699] of the multi-domain
class, the members of first three families have been split into domains. Their
common catalytic domains have been moved together (to a new fold/SF), whereas
other domains have been classified into different folds. The last, fourth
family remains in the multi-domain class in the fold of its own.
DNA repair protein MutM (Fpg) fold/SF/family [e.14.1;
56736] of the multi-domain
class has been split into three domains. Its middle domain has been classified
to the same SF as the ribosomal protein S13. This superfamily has been taken out
of the RuvA C-terminal domain-like fold [a.5;
46928] and classified to a new fold.
Superfamilies Catalytic domain of malonyl-CoA ACP transacylase [c.19.1;
52151]
and Cytosolic phospholipase A2 catalytic domain [c.75.1;
53644] have been merged
together.
Superfamilies Adenine nucleotide alpha hydrolases [c.26.2;
52402] and ETFP
adenine nucleotide-binding domain-like [c.29.1;
52431] have been merged together.
Superfamilies Muconalactone isomerase [d.58.4;
54909] and Lrp/AsnC-like
transcriptional regulator C-terminal domain [d.58.37;
69732] have been merged
together.
Superfamilies Synatpobrevin N-terminal domain [d.110.4;
64356] and Clathrin coat
assembly domain [d.110.6;
75520] have been merged together.
SAND domain fold/SF/family [b.99.1;
63763] has been moved (from all-beta) to the
alpha+beta class.
Trp repressor superfamily [a.107.1;
48295] has been moved from its own fold to
the DNA/RNA-binding 3-helical bundle fold [a.4].
Family Threonyl-tRNA synthetase (ThrRS), N-terminal 'additional' domain
[d.66.11;
55175]
has been taken out of the Alpha-L RNA-binding motif superfamily
[55174]
and put back to the ubiquitin-like fold (as a new SF).
C-terminal domain of ProRS superfamily [g.56.1;
64586] has been moved from
the Small proteins class (where it has its own fold) to the IF3-like fold [d.68]
In addition, the classifications below superfamily level have been refined for a
number of superfamilies without changing their overall contents. The pending
refinement of other superfamily classifications will be carried out gradually
through a number of future releases.
Copyright © 1994-2003
The scop authors / scop@mrc-lmb.cam.ac.uk
May 2003