SCOP 1.75: Domain d1efza_: 1efz A:

Lineage for d1efza_ (1efz A:)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.20: tRNA-guanine transglycosylase [51713] (1 family)

5. Family c.1.20.1: tRNA-guanine transglycosylase [51714] (2 proteins)

6. Protein Queosine tRNA-guanine transglycosylase [51715] (1 species)
   contains zinc-binding subdomain

7. Species Zymomonas mobilis [TaxId:542] [51716] (33 PDB entries)
   Uniprot P28720

8. Domain d1efza_: 1efz A: [29659]
   complexed with prf, zn; mutant

Details for d1efza_

PDB Entry: 1efz, 2 Å

PDB Description: mutagenesis and crystallographic studies of zymomonas mobilis trna- guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity

PDB Compounds: (A:) tRNA-guanine transglycosylase

SCOP Domain Sequences for d1efza_:

Sequence; same for both SEQRES and ATOM records:

>d1efza_ c.1.20.1 (A:) Queosine tRNA-guanine transglycosylase {Zymomonas mobilis [TaxId: 542]}
rprfsfsiaaregkartgtiemkrgvirtpafmpvgtaatvkalkpetvratgadiilgn
tyhlmlrpgaeriaklgglhsfmgwdrpiltdaggyqvmslssltkqseegvtfkshldg
srhmlspersieiqhllgsdivmafdectpypatpsraassmersmrwakrsrdafdsrk
eqaenaalfgiqqgsvfenlrqqsadalaeigfdgyavgglavgegqdemfrvldfsvpm
lpddkphylmgvgkpddivgavergidmfdcvlptrsgrngqaftwdgpinirnarfsed
lkpldsechcavcqkwsrayihhlirageilgamlmtehniafyqqlmqkirdsisegrf
sqfaqdfraryf

Timeline for d1efza_:

• d1efza_ first appeared (with stable ids) in SCOP 1.55
  
• d1efza_ appears in SCOP 1.73
  
• d1efza_ appears in SCOPe 2.01
  
• d1efza_ appears in the current release, SCOPe 2.08