SCOPe 2.08: Domain d1rlla2: 1rll A:141-461

Lineage for d1rlla2 (1rll A:141-461)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 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 d1rlla2: 1rll A:141-461 [303011]
   Other proteins in same PDB: d1rlla1, d1rlla3, d1rlla4, d1rllb1, d1rllb3, d1rllb4
   automated match to d1l9ma4
   complexed with ca, gsp, mg

Details for d1rlla2

PDB Entry: 1rll, 1.9 Å

PDB Description: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium

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

SCOPe Domain Sequences for d1rlla2:

Sequence; same for both SEQRES and ATOM records:

>d1rlla2 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 d1rlla2:

• d1rlla2 first appeared in SCOPe 2.06
  
• d1rlla2 appears in SCOPe 2.07