Structural Classification of Proteins
Fold: Ribonuclease PH domain 2-like
beta(2)-alpha-beta(2)-alpha; 3 layers: alpha/beta/alpha; antiparallel sheet: order 2134
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a+b)
[53931]
Mainly antiparallel beta sheets (segregated alpha and beta regions)
Fold:
Ribonuclease PH domain 2-like
[55665]
beta(2)-alpha-beta(2)-alpha; 3 layers: alpha/beta/alpha; antiparallel sheet: order 2134
Superfamilies:
Ribonuclease PH domain 2-like
[55666] (1)
uperfamily
Ribonuclease PH domain 2-like
[55667] (14)
Ribonuclease PH, domain 2 [103150]
Aquifex aeolicus
[TaxId: 63363]
[103151] (4)
Pseudomonas aeruginosa
[TaxId: 287]
[103152] (2)
Bacillus subtilis
[TaxId: 1423]
[103153] (3)
Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domains 2 and 5 [55668]
duplication of two-domain units formed by domains 1-2 and 4-5
Streptomyces antibioticus
[TaxId: 1890]
[55669] (2)
Exosome complex exonuclease RRP45 [160586]
Human (Homo sapiens)
[TaxId: 9606]
[160587] (1)
SQ
Q86Y41
185-302
Exosome complex exonuclease RRP42 [160588]
Human (Homo sapiens)
[TaxId: 9606]
[160589] (1)
SQ
Q15024
192-285
Exosome complex exonuclease 1, ECX1 [160590]
Sulfolobus solfataricus
[TaxId: 2287]
[160591] (50)
SQ
Q9UXC2
156-241! SQ
Q9UXC2
156-248
Archaeoglobus fulgidus
[TaxId: 2234]
[160592] (6)
SQ
O29757
154-252
Exosome complex exonuclease RRP41 [160593]
Human (Homo sapiens)
[TaxId: 9606]
[160594] (1)
SQ
Q9NPD3
152-241
Exosome complex exonuclease RRP46 [160595]
Human (Homo sapiens)
[TaxId: 9606]
[160596] (1)
SQ
Q9NQT4
147-235
Exosome complex exonuclease 2, ECX2 [160597]
Archaeoglobus fulgidus
[TaxId: 2234]
[160598] (6)
SQ
O29756
179-257
Sulfolobus solfataricus
[TaxId: 2287]
[160599] (51)
SQ
Q9UXC0
192-275
Exosome complex exonuclease MTR3 [160600]
Human (Homo sapiens)
[TaxId: 9606]
[160601] (1)
SQ
Q5RKV6
176-270
Exosome complex exonuclease RRP43 [160602]
Human (Homo sapiens)
[TaxId: 9606]
[160603] (1)
SQ
Q96B26
188-276
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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