SCOPe 2.07: Domain d1l9ma4: 1l9m A:141-461

Lineage for d1l9ma4 (1l9m A:141-461)

1. Root: SCOPe 2.07

2. Class d: Alpha and beta proteins (a+b) [53931] (388 folds)

3. Fold d.3: Cysteine proteinases [54000] (1 superfamily)
   consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn

4. Superfamily d.3.1: Cysteine proteinases [54001] (24 families)
   the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta-sheet

5. Family d.3.1.4: Transglutaminase core [54044] (3 proteins)

6. Protein Transglutaminase catalytic domain [54045] (4 species)

7. Species Human (Homo sapiens), TGase E3 [TaxId:9606] [75334] (9 PDB entries)

8. Domain d1l9ma4: 1l9m A:141-461 [73735]
   Other proteins in same PDB: d1l9ma1, d1l9ma2, d1l9ma3, d1l9mb1, d1l9mb2, d1l9mb3
   complexed with br, ca, cl

Details for d1l9ma4

PDB Entry: 1l9m, 2.1 Å

PDB Description: three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

PDB Compounds: (A:) Protein-glutamine glutamyltransferase E3

SCOPe Domain Sequences for d1l9ma4:

Sequence; same for both SEQRES and ATOM records:

>d1l9ma4 d.3.1.4 (A:141-461) Transglutaminase catalytic domain {Human (Homo sapiens), TGase E3 [TaxId: 9606]}
dsvfmgnhaereeyvqedagiifvgstnrigmigwnfgqfeedilsiclsildrslnfrr
daatdvasrndpkyvgrvlsaminsnddngvlagnwsgtytggrdprswdgsveilknwk
ksglspvrygqcwvfagtlntalrslgipsrvitnfnsahdtdrnlsvdvyydpmgnpld
kgsdsvwnfhvwnegwfvrsdlgpsyggwqvldatpqersqgvfqcgpasvigvregdvq
lnfdmpfifaevnadritwlydnttgkqwknsvnshtigryistkavgsnarmdvtdkyk
ypegsdqerqvfqkalgklkp

Timeline for d1l9ma4:

• d1l9ma4 first appeared in SCOP 1.61
  
• d1l9ma4 appears in SCOPe 2.06
  
• d1l9ma4 appears in the current release, SCOPe 2.08