![]() | Class d: Alpha and beta proteins (a+b) [53931] (376 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] (4 families) ![]() has a circularly permuted topology |
![]() | Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (1 protein) |
![]() | Protein Adenylation domain of NAD+-dependent DNA ligase [56097] (4 species) contains additional, N-terminal all-alpha subdomain |
![]() | Species Thermus filiformis [TaxId:276] [56099] (2 PDB entries) |
![]() | Domain d1v9pa3: 1v9p A:1-317 [100546] Other proteins in same PDB: d1v9pa1, d1v9pa2, d1v9pb1, d1v9pb2 complexed with amp, zn |
PDB Entry: 1v9p (more details), 2.9 Å
SCOPe Domain Sequences for d1v9pa3:
Sequence; same for both SEQRES and ATOM records: (download)
>d1v9pa3 d.142.2.2 (A:1-317) Adenylation domain of NAD+-dependent DNA ligase {Thermus filiformis [TaxId: 276]} mtreearrrinelrdliryhnyryyvladpeisdaeydrllrelkeleerfpefkspdsp teqvgarpleptfrpvrhptrmysldnaftyeevlafeerleralgrkrpflytvehkvd glsvnlyyeegvlvfgatrgdgevgeevtqnlltiptiprrlkgvpdrlevrgevympie aflrlneeleergekvfknprnaaagslrqkdprvtakrglratfyalglgleesglksq yelllwlkekgfpvehgyekalgaegveevyrrflaqrhalpfeadgvvvklddlalwre lgytaraprfalaykfp
Timeline for d1v9pa3: