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Proteins in SwissProt homologous to 1yt3A

25 proteins with E() < 0.001

Homologs in PDB


Acc   E.C. E() % id alen 151
&Y
155
&D
P09155
RND_ECOLI
Ribonuclease D; Short=RNase D3.1.13.55.7e-172100.0375 &Y&D
C9XUE4
RND_CROTZ
Ribonuclease D; Short=RNase D3.1.13.51.1e-13075.9369 &Y&D
C6C608
RND_DICDC
Ribonuclease D; Short=RNase D3.1.13.51.2e-11666.8373 &Y&D
A8GFH0
RND_SERP5
Ribonuclease D; Short=RNase D3.1.13.51.2e-11467.8373 &Y&D
P44442
RND_HAEIN
Ribonuclease D; Short=RNase D3.1.13.51e-6441.0371 &Y&D
A0KXU5
RND_SHESA
Ribonuclease D; Short=RNase D3.1.13.51.7e-5941.9372 &Y&D
A1SVE6
RND_PSYIN
Ribonuclease D; Short=RNase D3.1.13.52.3e-5439.7373 &Y&D
A6V8R6
RND_PSEA7
Ribonuclease D; Short=RNase D3.1.13.52.4e-5038.7377 &Y&D
A5G127
RND_ACICJ
Ribonuclease D; Short=RNase D3.1.13.58.9e-3633.2365 &Y&D
A9H9B7
RND_GLUDA
Ribonuclease D; Short=RNase D3.1.13.53.9e-3533.4368 &Y&D
A7HYE5
RND_PARL1
Ribonuclease D; Short=RNase D3.1.13.51e-3431.1370 &Y&D
Q0BVP4
RND_GRABC
Ribonuclease D; Short=RNase D3.1.13.54e-3331.3374 &Y&D
B8EN54
RND_METSB
Ribonuclease D; Short=RNase D3.1.13.51.1e-3131.2362 &Y&D
D4Z694
RND_SPHJU
Ribonuclease D; Short=RNase D3.1.13.53.4e-3132.1368 &Y&D
Q5NPM2
RND_ZYMMO
Ribonuclease D; Short=RNase D3.1.13.51.1e-3032.0378 &Y&D
Q6AJF4
RND_DESPS
Ribonuclease D; Short=RNase D3.1.13.52e-3030.2364 &Y&D
Q5GZ75
RND_XANOR
Ribonuclease D; Short=RNase D3.1.13.53.1e-3032.8372 &Y&D
Q6G329
RND_BARHE
Ribonuclease D; Short=RNase D3.1.13.55.9e-3028.8375 &Y&D
Q28RA7
RND_JANSC
Ribonuclease D; Short=RNase D3.1.13.56.6e-2931.7385 &Y&D
Q1QLI8
RND_NITHX
Ribonuclease D; Short=RNase D3.1.13.51.5e-2728.1366 &Y&D
Q12149
RRP6_YEAST
Exosome complex exonuclease RRP6; Riboso1.5e-1126.2309 &Y&D
P56960
EXOSX_MOUSE
Exosome component 10; Autoantigen PM/Scl1.9e-1023.4333 &Y&D
Q01780
EXOSX_HUMAN
Exosome component 10; Autoantigen PM/Scl2.7e-1025.3296 &Y&D
Q10146
RRP6_SCHPO
Exosome complex exonuclease rrp6; Riboso6.1e-1023.1299 &Y&D
O67779
DPO1_AQUAE
DNA polymerase I; Short=POL I2.7.7.72.6e-0628.3166 &Y&D

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.


Homologs in SwissProt for MACiE ID:


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