Structural Classification of Proteins
Fold: PIN domain-like
3 layers, a/b/a; core: parallel beta-sheet of 5 strands, order 32145
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a/b)
[51349]
Mainly parallel beta sheets (beta-alpha-beta units)
Fold:
PIN domain-like
[88722]
3 layers, a/b/a; core: parallel beta-sheet of 5 strands, order 32145
Superfamilies:
PIN domain-like
[88723] (2)
uperfamily
PIN domain
[89619] (7)
Pfam 01850
Hypothetical protein AF0591 [89620]
Archaeon Archaeoglobus fulgidus
[TaxId: 2234]
[89621] (1)
Hypothetical protein PAE2754 [102270]
Archaeon Pyrobaculum aerophilum
[TaxId: 13773]
[102271] (2)
Hypothetical protein AF1683 [117492]
Archaeoglobus fulgidus
[TaxId: 2234]
[117493] (1)
SQ
O28590
Trafficking protein B [142110]
Neisseria gonorrhoeae
[TaxId: 485]
[142111] (9)
SQ
Q5F882
1-138! SQ
Q9RF91
1-138
Hypothetical protein PH0500 [142112]
Pyrococcus horikoshii
[TaxId: 53953]
[142113] (4)
SQ
O58236
2-149
Conserved hypothetical protein PAE0151 [142114]
Pyrobaculum aerophilum
[TaxId: 13773]
[142115] (1)
SQ
Q8ZZP3
1-130
Hypothetical protein PF0355 [142116]
PH0500 ortholog
Pyrococcus furiosus
[TaxId: 2261]
[142117] (4)
SQ
Q8U3V0
2-148
5' to 3' exonuclease catalytic domain
[53045] (8)
contains an alpha-helical arch and additional strand 6 antiparallel to the rest; strand order 321456; similarity to the resolvase-like fold
T4 RNase H [53046]
Bacteriophage T4
[TaxId: 10665]
[53047] (2)
5' to 3' exonuclease domain of DNA polymerase Taq [53048]
Thermus aquaticus
[TaxId: 271]
[53049] (4)
T5 5'-exonuclease [53050]
Bacteriophage T5
[TaxId: 10726]
[53051] (4)
Flap endonuclease-1 (Fen-1 nuclease) [53052]
Archaeon Methanococcus jannaschii
[TaxId: 2190]
[53053] (2)
Archaeon Pyrococcus horikoshii
[TaxId: 53953]
[82436] (1)
Archaeon Pyrococcus furiosus
[TaxId: 2261]
[53055] (1)
Archaeon Archaeoglobus fulgidus
[TaxId: 2234]
[102272] (2)
Human (Homo sapiens)
[TaxId: 9606]
[142118] (3)
SQ
P39748
2-217
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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