SCOPe 2.06: Domain d1vjja6: 1vjj A:141-461

Lineage for d1vjja6 (1vjj A:141-461)

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 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 d1vjja6: 1vjj A:141-461 [303236]
   Other proteins in same PDB: d1vjja5, d1vjja7, d1vjja8, d1vjjb5, d1vjjb7, d1vjjb8
   automated match to d1l9ma4
   complexed with ca, cl, gdp, mg

Details for d1vjja6

PDB Entry: 1vjj, 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 d1vjja6:

Sequence; same for both SEQRES and ATOM records:

>d1vjja6 d.3.1.4 (A:141-461) Transglutaminase catalytic domain {Human (Homo sapiens), TGase E3 [TaxId: 9606]}
dsvfmgnhaereeyvqedagiifvgstnrigmigwnfgqfeedilsiclsildrslnfrr
daatdvasrndpkyvgrvlsaminsnddngvlagnwsgtytggrdprswngsveilknwk
ksglspvrygqcwvfagtlntalrslgipsrvitnfnsahdtdrnlsvdvyydpmgnpld
kgsdsvwnfhvwnegwfvrsdlgpsyggwqvldatpqersqgvfqcgpasvigvregdvq
lnfdmpfifaevnadritwlydnttgkqwknsvnshtigryistkavgsnarmdvtdkyk
ypegsdqerqvfqkalgklkp

Timeline for d1vjja6:

• d1vjja6 is new in SCOPe 2.06-stable
  
• d1vjja6 appears in SCOPe 2.07
  
• d1vjja6 appears in the current release, SCOPe 2.08