Structural Classification of Proteins
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Superfamily: Alpha-L RNA-binding motif

common motif in otherwise different folds
link to SUPERFAMILY database - Superfamily

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Alpha-L RNA-binding motif [55173]
    alpha(2)-beta(2)-loop-beta; 2 layers: alpha/beta
  4. Superfamily: Alpha-L RNA-binding motif [55174]
    common motif in otherwise different folds
    link to SUPERFAMILY database - Superfamily

Families:

  1. Ribosomal protein S4 [55178] (3)
    has a RRF/tRNA synthetase additional domain-like fold
    1. Ribosomal protein S4 [55179]
      also contains a Zn-binding N-terminal subdomain
      1. Thermus thermophilus [TaxId: 274] [55180] (45) picpic
      2. Bacillus stearothermophilus [TaxId: 1422] [55181] (2) picpic
      3. Escherichia coli [TaxId: 562] [160439] (26) picpic
        SQ P0A7V8 1-205
  2. Heat shock protein 15 kD [55182] (1)
    there are additional C-terminal structures
    1. Heat shock protein 15 kD [55183]
      ribosome-binding protein
      1. Escherichia coli [TaxId: 562] [55184] (2) picpic
  3. Tyrosyl-tRNA synthetase (TyrRS), C-terminal domain [75465] (2)
    there are additional N-terminal structures
    1. Tyrosyl-tRNA synthetase (TyrRS), C-terminal domain [75466]
      1. Thermus thermophilus [TaxId: 274] [82701] (2) picpic
      2. Bacillus stearothermophilus [TaxId: 1422] [75467] (1) picpic
  4. YbcJ-like [103046] (1)
    overall topological similarity to the TyrRS C-domain
    1. Hypothetical protein YbcJ [103047]
      1. Escherichia coli [TaxId: 562] [103048] (1) picpic
  5. Pseudouridine synthase RsuA N-terminal domain [75468] (2)
    1. Pseudouridine synthase RsuA N-terminal domain [75469]
      1. Escherichia coli [TaxId: 562] [75470] (3) picpic
      2. Haemophilus influenzae [TaxId: 727] [103049] (1) picpic

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site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk