I-AniI

Type

Wild-Type

Target Sequence

-11	-10	-9	-8	-7	-6	-5	-4	-3	-2	-1	1	2	3	4	5	6	7	8	9	10	11
C	T	G	A	G	G	A	G	G	T	T	T	C	T	C	T	G	T	A	A	A	G

FASTA Sequence

Simple FASTA Numbered FASTA

Crystal Structure

PDB File

PyMOL File

Position Weight Matrix

pos A C G T -11 0.25 0.25 0.25 0.25 -10 0.16 0.40 0.13 1.00 -9 0.10 0.01 1.00 0.02 -8 1.00 0.19 0.13 0.45 -7 0.02 0.00 1.00 0.01 -6 0.00 0.02 0.65 1.00 -5 1.00 0.80 1.00 1.00 -4 0.00 0.00 1.00 0.08 -3 0.02 0.00 1.00 0.02 -2 0.00 1.00 0.61 0.46 -1 0.23 0.00 0.05 1.00 1 0.23 0.00 0.05 1.00 2 0.23 1.00 0.02 0.55 3 0.02 0.02 0.05 1.00 4 0.03 1.00 0.02 0.04 5 0.62 0.35 0.57 1.00 6 0.01 0.24 1.00 0.01 7 0.36 0.40 0.20 1.00 8 0.72 0.89 0.56 1.00 9 1.00 0.35 0.85 1.00 10 1.00 0.75 0.65 0.75 11 0.25 0.25 0.25 0.25

Amino Acid Contact Modules

Module	Amino Acid Contact Modules (?)
-11 → -9:	Tyr 27
-8 → -6:	Ser 20, Thr 22, Gly 25*, Thr 29, Glu 31, Ile 55, Ser 57, Arg 70, Arg 72
-6 → -4:	Tyr 18, Ser 20, Gly 33, Glu 35, Ser 57, Arg 59*, Ala 68, Arg 70
-5 → -3:	Tyr 18, Gly 33, Glu 35, Arg 59*, Glu 65*, Met 66, Ala 68, Arg 70
+3 → +5:	Cys 150, Ser 152, Asp 168, Ala 170*, Asp 194*, Cys 198*, Lys 200
+4 → +6:	Ser 152, Tyr 154, Ser 166, Asp 168, Lys 190*, Tyr 192, Asp 194*, Lys 202
+6 → +8:	Tyr 154, Leu 156, Tyr 162, Ile 164*, Ser 166, Lys 190*, Thr 204
+9 → +11:	Leu 156, Asp 159*, Asp 160*, Tyr 162

Key

	Experiment
	Crystal Structure
	Sequence Alignment
*	Uncertain

Specificity Changing Mutations

Amino Acid Mutations (?)	Specificity Changes	Reference
K24N, T29K	-8A to -8G	1
L156Q, I164R, T204S	+8A to +8C	1
Y18W, E35K, R61Q	-3G to -3C	1
K24N, G25R, T29I	-9G to -9C	1
T29S, E31R, R70L	-6G to -6C	1
D168E	+5T to +5C	1

1	Thyme SB, Jarjour J, Takeuchi R, Havranek JJ, Ashworth J, Scharenberg AM, Stoddard BL, Baker D. (2009) Exploitation of binding energy for catalysis and design. Nature, 461, 1300-1304.

Additional Information

Author: Barry Stoddard

Notes:
1.) Source organism: Aspergillus nidulans 2.) Host gene: mitochondrial cytochrome oxidase (COX) B gene 3.) Intron-encoded 4.) Cleavage activity verified via many in vitro experiments. 5.) Additional mutations added for solubilization: F80K and L233K Mutation added to knockout RNA binding/maturase activity: R239E Mutation added to create nickase: K227M 6.) Structures: 1P8K, 2QOJ, 3EH8

Date Added: 2012-01-29