![]() | Class d: Alpha and beta proteins (a+b) [53931] (380 folds) |
![]() | Fold d.142: ATP-grasp [56058] (2 superfamilies) Consists of two subdomains with different alpha+beta folds shares functional and structural similarities with the PIPK and protein kinase superfamilies |
![]() | Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (6 families) ![]() has a circularly permuted topology |
![]() | Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (2 proteins) automatically mapped to Pfam PF01653 |
![]() | Protein Adenylation domain of NAD+-dependent DNA ligase [56097] (4 species) contains additional, N-terminal all-alpha subdomain |
![]() | Species Enterococcus faecalis [TaxId:1351] [118124] (9 PDB entries) Uniprot Q837V6 5-317 |
![]() | Domain d1taea_: 1tae A: [112376] complexed with na, nad, so4 |
PDB Entry: 1tae (more details), 2.7 Å
SCOPe Domain Sequences for d1taea_:
Sequence; same for both SEQRES and ATOM records: (download)
>d1taea_ d.142.2.2 (A:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]} qpltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlitpd sptqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelkidg laislryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkqsf valneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqfea leelsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdelgf tvkaprwaiaykfppeeaetv
Timeline for d1taea_: