Structural Classification of Proteins
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Family: HMA, heavy metal-associated domain

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Ferredoxin-like [54861]
    alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2
  4. Superfamily: HMA, heavy metal-associated domain [55008]
    link to SUPERFAMILY database - Superfamily
  5. Family: HMA, heavy metal-associated domain [55009]

Protein Domains:

  1. Mercuric ion binding protein MerP [55010]
    1. Shigella flexneri [TaxId: 623] [55011] (3) picpic
    2. Ralstonia metallidurans CH34 [TaxId: 266264] [110979] (1) picpic
      SQ O66016 Q58AI1 Q5NUU9 Q6UP70 Q7BRH5 Q7BRH6 Q7X3A5 # 100% identity
  2. Potential copper-translocating P-type ATPase CopA (YvgX) [75441]
    duplication: contains tandem repeat of two HMA domains in the N-terminal region
    1. Bacillus subtilis [TaxId: 1423] [75442] (6) picpic
  3. Metal ion-transporting ATPase ZntA, N-terminal domain [82683]
    1. Escherichia coli [TaxId: 562] [82684] (2) picpic
  4. Copper transporter domain ccc2a [64279]
    1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [64280] (3) picpic
  5. Menkes copper-transporting ATPase [55012]
    1. Human (Homo sapiens) [TaxId: 9606] [55013] (7) picpic
  6. ATX1 metallochaperone protein (ATOX1) [55014]
    1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [55015] (5) picpic
    2. Human (Homo sapiens), HAH1 [TaxId: 9606] [55016] (5) picpic
      SQ O00244
  7. Copper chaperone [55017]
    1. Enterococcus hirae [TaxId: 1354] [55018] (1) picpic
    2. Bacillus subtilis, CopZ [TaxId: 1423] [69736] (4) picpic
    3. Synechocystis sp. pcc 6803, Scatx1 [TaxId: 1148] [102998] (1) picpic
  8. Copper chaperone for superoxide dismutase, N-terminal domain [55019]
    1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [55020] (2) picpic
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MRC 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