Structural Classification of Proteins
Superfamily: Zinc beta-ribbon
uperfamily
Lineage:
Root:
scop
Class:
Small proteins
[56992]
Usually dominated by metal ligand, heme, and/or disulfide bridges
Fold:
Rubredoxin-like
[57769]
metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2
Superfamily:
Zinc beta-ribbon
[57783]
uperfamily
Families:
Transcriptional factor domain
[57784] (6)
Transcriptional factor SII, C-terminal domain [57785]
Human (Homo sapiens)
[TaxId: 9606]
[57786] (1)
Transcription initiation factor TFIIB, N-terminal domain [57789]
Archaeon Pyrococcus furiosus
[TaxId: 2261]
[57790] (1)
Human (Homo sapiens)
[TaxId: 9606]
[57791] (3)
SQ
Q00403
2-59
RBP9 subunit of RNA polymerase II [57787]
contains two differently decorated domains of this fold
Archaeon Thermococcus celer
[TaxId: 2264]
[57788] (1)
Baker's yeast (Saccharomyces cerevisiae)
[TaxId: 4932]
[64575] (41)
SQ
P27999
; part of multichain biological unit
Transcription initiation factor TFIIE-alpha [118283]
Human (Homo sapiens)
[TaxId: 9606]
[118284] (1)
SQ
P29083
113-174
DNA primase zinc finger
[57792] (2)
contains alpha-helices in the N- and C-terminal extensions (linkers?)
Zinc-binding domain of DNA primase [57793]
Bacillus stearothermophilus
[TaxId: 1422]
[57794] (1)
Zinc-binding domain of primase-helicase [90207]
Bacteriophage T7
[TaxId: 10760]
[90208] (1)
Prokaryotic DNA topoisomerase I, a C-terminal fragment
[57795] (1)
Duplication: contains tandem repeats of several domains with zinc-binding sites being lost in some of them
Prokaryotic DNA topoisomerase I, a C-terminal fragment [57796]
Escherichia coli
[TaxId: 562]
[57797] (1)
Putative zinc binding domain
[118285] (1)
Pfam 05129
; DUF701
Hypothetical UPF0222 protein MGC4549 [118286]
Mouse (Mus musculus)
[TaxId: 10090]
[118287] (1)
SQ
P60003
PhnA zinc-binding domain
[144191] (1)
Pfam 08274
Hypothetical protein PA0128, N-terminal domain [144192]
Pseudomonas aeruginosa
[TaxId: 287]
[144193] (1)
SQ
Q9I704
2-39
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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