SitesBLAST

M1 (= M1) modified: Initiator methionine, Removed
C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
H30 (≠ T27) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D31) mutation D->N,E: Little effect on the kinetic properties.
H81 (= H81) mutation to A: 5-fold decrease in glutamine affinity.
A105 (= A108) mutation to H: Little effect on the kinetic properties.
E349 (≠ D374) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
32% identity, 59% coverage: 3:383/648 of query aligns to 2:341/497 of 1ct9A

query
sites
1ct9A

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active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ P347), R308 (≠ D350), E332 (≠ D374)
binding adenosine monophosphate: L232 (≠ F272), L233 (= L273), S234 (= S274), S239 (= S279), A255 (≠ S298), V256 (≠ I299), D263 (≠ Y306), M316 (≠ V359), S330 (= S372), G331 (= G373), E332 (≠ D374)
binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (= V53), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D102)

Sites not aligning to the query:

active site: 1, 366
binding glutamine: 1

P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
31% identity, 59% coverage: 1:383/648 of query aligns to 1:374/561 of P08243

query
sites
P08243

M

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C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
A6 (≠ V5) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
V210 (≠ L229) to E: in dbSNP:rs1049674
F362 (≠ L371) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973

Sites not aligning to the query:

550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
31% identity, 59% coverage: 2:383/648 of query aligns to 1:361/509 of 6gq3A

query
sites
6gq3A

C
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Y

active site: W4 (vs. gap), L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ P347), R327 (≠ D350)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R49), V51 (≠ I52), V52 (= V53), Y73 (= Y74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S101), D96 (= D102)

P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 62% coverage: 1:399/648 of query aligns to 1:388/557 of P78753

query
sites
P78753

M

M

C

C

G

G

I

I

-

L

-

A

V

V

G

H

Y

H

W

V

S

A

R

E

N

D

S

I

R

E

S

A

V

F

D

K

-

P

V

K

A

A

S

L

R

H

M

L

A

S

H

K

R

Q

I

L

A

R

T

H

R

R

G

G

P

P

D

D

D

W

A

S

G

G

V

-

W

-

A

K

E

A

G

I

E

R

G

N

E

Q

P

T

V

I

L

L

A

C

H

H

R

E

R

R

L

L

S

A

I

I

V

V

D

G

L

V

S

E

P

-

A

S

G

G

H

A

Q

Q

P

P

M

L

V

V

S

S

P

D

C

D

G

G

R

K

Y

L

V

V

L

L

S

T

Y

V

N

N

G

G

E

E

I

I

Y

Y

N

N

H

H

T

L

E

K

L

L

R

R

Q

E

E

N

L

L

E

K

R

-

E

-

G

-

G

G

G

N

F

Y

D

K

W

F

R

K

G

T

H

Y

S

S

D

D

T

C

E

E

T

V

L

I

L

L

A

Y

A

L

L

Y

R

R

Y

E

W

H

G

G

V

P

H

A

G

C

A

A

L

-

E

N

R

M

L

L

N

D

G

G

M

M

F

F

A

S

F

W

A

V

L

L

W

Y

D

D

R

Q

T

D

E

K

R

D

T

K

L

V

F

V

L

A

A

A

R

R

D

D

R

P

M

I

G

G

E

I

K

T

P

T

L

L

Y

Y

Y

Q

G

G

R

F

S

S

G

S

-

D

-

S

-

P

D

D

T

T

F

A

L

Y

F

F

G

A

S

S

E

E

L

L

K

K

A

A

L

L

A

-

H

H

P

P

D

-

W

-

R

-

G

-

E

-

V

-

D

-

R

-

D

-

A

-

L

-

A

-

L

-

M

-

L

-

R

-

Y

-

N

-

V

-

P

-

A

-

P

-

W

-

S

-

I

V

Y

C

R

D

G

K

I

I

Y

I

K

A

L

F

P

P

A

G

H

H

Y

Y

L

Y

V

D

V

S

R

E

G

T

Q

K

G

Q

H

T

Q

V

V

R

G

Y

E

F

P

K

E

P

C

S

Y

W

W

W

D

D

L

E

P

N

E

K

V

I

A

P

S

S

E

N

G

P

A

V

R

D

E

Y

A

K

K

L

G

-

E

-

P

-

D

-

A

-

L

-

A

-

D

-

E

-

L

L

D

R

E

E

L

T

L

L

R

E

D

A

S

S

V

V

G

R

R

K

R

R

M

L

M

M

A

A

D

E

V

V

P

P

L

Y

G

G

A

V

F

L

L

L

S

S

G

G

F

L

D

D

S

S

T

S

M

L

V

I

V

A

-

S

-

I

-

A

-

R

-

E

-

T

-

E

-

K

-

L

-

A

-

N

A

S

Q

T

M

S

Q

Q

A

S

Q

E

S

E

A

A

R

R

P

T

V

I

K

T

-

A

-

W

-

P

-

K

-

L

-

H

T

S

F

F

S

A

I

I

G

G

N

L

A

P

D

G

A

S

E

P

Y

-

D

-

E

D

A

L

H

L

H

A

A

A

A

R

A

K

V

V

A

A

R

D

H

F

L

L

G

H

T

T

D

F

H

H

R

H

E

E

L

H

Y

T

V

F

T

T

P

I

E

D

D

E

A

G

-

L

-

D

-

A

-

L

Q

R

A

D

V

V

I

I

P

Y

R

H

L

L

P

-

E

E

I

T

F

Y

D

D

E

V

P

T

F

T

A

I

D

R

S

A

S

S

Q

-

I

T

P

P

T

M

Y

Y

L

L

V

L

S

S

-

R

E

K

L

I

A

K

R

A

R

Q

D

G

V

V

T

K

V

M

T

V

L

L

S

S

G

G

D

E

G

G

G

S

D

D

E

E

L

I

L

F

G

G

Y

Y

-

L

-

Y

-

F

-

G

-

N

-

A

-

P

N

S

R

R

H

E

V

A

V

F

G

H

P

S

G

E

V

C

W

V

R

R

V

V

N

K

R

N

L

L

Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 26% coverage: 2:168/648 of query aligns to 1:194/455 of 1ao0A

query
sites
1ao0A

C
|
C

G

G

I

V

V

F

G

G

Y

I

W

W

S

G

R

-

N

H

S

E

R

E

S

A

V

P

D

Q

V

I

A

T

S

Y

R

Y

M

G

A

L

H

H

R

S

I

L

A

Q

T
x
H

R

R

G
|
G

P

Q

D

E

D

G

A

A

G

G

V

I

W

V

A

A

E

T

G

-

E

D

G

G

E

E

P

K

V

L

L

T

A

A

H

H

R

K

R

G

L

Q

S

G

I

L

V

I

-

T

-

E

-

V

-

F

-

Q

-

N

-

G

D

E

L

L

S

S

P

K

A

V

-

K

-

G

-

K

-

G

-

A

-

I

G

G

H

H

-

V

-

R

-

Y

-

A

-

T

-

G

-

Y

-

E

-

N

-

V

Q

Q

P

P

M

L

V

L

-

F

-

R

-

S

S

Q

P

N

C

N

G

G

R

S

Y

L

V

A

L

L

S

A

Y

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

H

A

T

T

E

Q

L

L

R

K

Q

Q

E

Q

L

L

E

E

R

N

E

Q

G

G

G

S

G

I

F

F

D

Q

W

T

R

S

G

-

H

-

S

S

D

D

T

T

E

E

T

V

L

L

L

A

A

H

A

L

L

I

R

K

Y

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

V

I

H

K

G

N

A

S

L

L

E

S

R

M

L

L

N

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

T

T

E

E

R

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

E

L

K

R

P

P

L

L

Y

S

Y

I

G

G

R

M

S

M

G

G

D

D

T

A

F

Y

L

V

F

V

G

A

S

S

E

E

L

T

K

C

A

A

L

F

active site: C1 (= C2), G27 (= G29), N98 (= N75), G99 (= G76)
binding adenosine-5'-diphosphate: H25 (≠ T27)

Sites not aligning to the query:

active site: 238, 296, 301, 311, 419
binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
binding magnesium ion: 279, 341, 342
binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436

P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
27% identity, 26% coverage: 2:168/648 of query aligns to 12:209/476 of P00497

query
sites
P00497

C
|
C

G

G

I

V

V

F

G

G

Y

I

W

W

S

G

R

-

N

H

S

E

R

E

S

A

V

P

D

Q

V

I

A

T

S

Y

R

Y

M

G

A

L

H

H

R

S

I

L

A

Q

T

H

R

R

G

G

P

Q

D

E

D

G

A

A

G

G

V

I

W

V

A

A

E

T

G

-

E

D

G

G

E

E

P

K

V

L

L

T

A

A

H

H

R

K

R

G

L

Q

S

G

I

L

V

I

-

T

-

E

-

V

-

F

-

Q

-

N

-

G

D

E

L

L

S

S

P

K

A

V

-

K

-

G

-

K

-

G

-

A

-

I

G

G

H

H

-

V

-

R

-

Y

-

A

-

T

-

A

-

G

-

Y

-

E

-

N

-

V

Q

Q

P

P

M

L

V

L

-

F

-

R

-

S

S

Q

P

N

C

N

G

G

R

S

Y

L

V

A

L

L

S

A

Y

H

N

N

G

G

E

N

I

L

Y

V

N

N

H

A

T

T

E

Q

L

L

R

K

Q

Q

E

Q

L

L

E

E

R

N

E

Q

G

G

G

S

G

I

F

F

D

Q

W

T

R

S

G

-

H

-

S

S

D

D

T

T

E

E

T

V

L

L

L

A

A

H

A

L

L

I

R

K

Y

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

V

I

H

K

G

N

A

S

L

L

E

S

R

M

L

L

N

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

T

T

E

E

R

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

E

L

K

R

P

P

L

L

Y

S

Y

I

G

G

R

M

S

M

G

G

D

D

T

A

F

Y

L

V

F

V

G

A

S

S

E

E

L

T

K

C

A

A

L

F

C12 (= C2) active site, Nucleophile; mutation to F: Loss of enzyme activity and N-terminal processing.

Sites not aligning to the query:

1:11 modified: propeptide
247 binding [4Fe-4S] cluster
294 binding Mg(2+)
356 binding Mg(2+)
357 binding Mg(2+)
393 binding [4Fe-4S] cluster
394 F→V: Partial loss of activity.
442 D→S: Partial loss of activity.
448 binding [4Fe-4S] cluster; C→S: Loss of activity.
451 binding [4Fe-4S] cluster; C→S: Loss of activity.
452 F→C: Lethal.

1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
27% identity, 26% coverage: 2:168/648 of query aligns to 1:198/465 of 1gph1

query
sites
1gph1

C

C

G

G

I

V

V

F

G

G

Y

I

W

W

S

G

R

-

N

H

S

E

R

E

S

A

V

P

D

Q

V

I

A

T

S

Y

R

Y

M

G

A

L

H

H

R

S

I

L

A

Q

T

H

R

R

G

G

P

Q

D

E

D

G

A

A

G

G

V

I

W

V

A

A

E

T

G

-

E

D

G

G

E

E

P

K

V

L

L

T

A

A

H

H

R

K

R

G

L

Q

S

G

I

L

V

I

-

T

-

E

-

V

-

F

-

Q

-

N

-

G

D

E

L

L

S

S

P

K

A

V

-

K

-

G

-

K

-

G

-

A

-

I

G

G

H

H

-

V

-

R

-

Y

-

A

-

T

-

A

-

G

-

Y

-

E

-

N

-

V

Q

Q

P

P

M

L

V

L

-

F

-

R

-

S

S

Q

P

N

C

N

G

G

R

S

Y

L

V

A

L

L

S

A

Y

H

N

N

G

G

E

N

I

L

Y

V

N

N

H

A

T

T

E

Q

L

L

R

K

Q

Q

E

Q

L

L

E

E

R

N

E

Q

G

G

G

S

G

I

F

F

D

Q

W

T

R

S

G

-

H

-

S

S

D

D

T

T

E

E

T

V

L

L

L

A

A

H

A

L

L

I

R

K

Y

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

V

I

H

K

G

N

A

S

L

L

E

S

R

M

L

L

N

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

T

T

E

E

R

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

E

L

K

R

P

P

L

L

Y

S

Y

I

G

G

R

M

S

M

G

G

D

D

T

A

F

Y

L

V

F

V

G

A

S

S

E

E

L

T

K

C

A

A

L

F

Sites not aligning to the query:

active site: 300, 305, 315, 423
binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440

1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 41% coverage: 76:338/648 of query aligns to 74:307/500 of 1jgtB

query
sites
1jgtB

G
|
G

E

E

I

I

Y

Y

N

N

H

R

T

D

E

E

L

L

R

L

Q

S

E

V

L

L

E

P

R

-

E

-

G

-

G

A

G

G

F

P

D

A

W

P

R

E

G

G

H

-

S

-

D

D

T

A

E

E

T

L

L

V

L

L

A

R

A

L

L

L

R

E

Y

R

W

Y

G

D

V

L

H

H

G

-

A

A

L

F

E

R

R

L

L

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

-

D

-

R

R

T

T

E

G

R

D

T

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

M

A

G

G

E

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

R

V

S

A

G

P

D

G

T

E

F

V

L

R

F

A

G

S

S

T

E

E

L

A

K

K

A

A

L

L

A

A

H

H

P

R

D

D

W

P

R

K

G

G

E

F

V

P

D

L

R

A

D

D

A

A

L

R

A

R

L

V

M

-

L

-

R

-

Y

-

N

-

V

-

P

-

A

-

P

-

W

-

S

A

I

G

Y

L

R

T

G

G

I

V

Y

Y

K

Q

L

V

P

P

P

A

A

G

H

A

Y

V

L

M

V

D

V

I

R

D

-

L

G

G

Q

S

G

G

H

T

Q

A

V

V

G

T

E

H

P

R

E

T

C

W

Y

T

W

P

D

G

L

L

P

-

E

-

V

-

A

-

S

-

E

-

G

-

A

S

R

R

E

R

A

I

K

L

G

P

E

E

P

G

D

E

A

A

L

V

A

A

D

A

E

V

L

R

D

A

E

A

L

L

L

E

R

K

D

A

S

V

V

A

G

Q

R

R

R

V

M

T

M

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

F
x
I

D
|
D

S
|
S

T

S

M

G

V

V

V

A

A

A

Q

C

M

A

Q

H

A

-

Q

R

S

A

A

A

R

G

P

E

V

L

K

D

T

T

F

V

S
|
S

I
x
M

G

G

N

T

A

D

D

T

A

S

E

-

Y

-

D

N

E

E

A

F

H

R

H

E

A

A

A

R

A

A

V

V

A

V

R

D

H

H

L

L

G

R

T

T

D

R

H

H

R

R

E

E

L

I

Y

T

V

I

T

P

P

T

E

T

D

E

A

L

Q

L

A

A

V

Q

I

L

P

P

active site: G74 (= G76)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F272), L245 (= L273), S246 (= S274), G248 (= G276), I249 (≠ F277), D250 (= D278), S251 (= S279), S269 (= S298), M270 (≠ I299)
binding magnesium ion: D250 (= D278)

Sites not aligning to the query:

active site: 73, 319, 345, 379, 440
binding diphosphomethylphosphonic acid adenosyl ester: 327, 344, 345, 348, 420, 440
binding n2-(carboxyethyl)-l-arginine: 323, 345, 346, 348, 349, 354, 370, 379
binding magnesium ion: 348

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
28% identity, 26% coverage: 2:168/648 of query aligns to 1:199/460 of 6lbpA

query
sites
6lbpA

C
|
C

G

G

I

V

V

V

G

G

Y

I

W

Y

S

G

R

D

N

S

S

E

R

-

S

-

V

-

D

-

V

-

A

A

S

S

R

R

M

L

A

C

-

Y

-

L

-

A

-

L

H

H

R

A

I

L

A

Q

T

H

R

R

G
|
G

P

Q

D

E

D

G

A

A

G

G

-

I

-

V

-

T

-

V

-

S

-

K

-

D

-

K

-

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

-

G

-

L

-

V

-

S

-

E

V

V

W

F

A

S

E

E

G

S

E

K

-

L

-

D

-

Q

-

L

-

P

G

G

E

D

P

I

V

A

L

I

A

G

H

H

R

V

R

R

L

Y

S

S

I

T

V

A

D

G

L

S

S

S

P

M

A

L

G

K

H

N

-

V

Q

Q

P

P

M

F

V

V

S

A

P

G

-

Y

-

R

C

F

G

G

R

S

Y

V

V

G

L

V

S

A

Y

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

H

Y

T

T

E

K

L

L

R

R

Q

A

E

D

L

L

E

E

R

E

E

N

G

G

G

S

G

I

F

F

D

N

W

T

R

S

G

-

H

-

S

S

D

D

T

T

E

E

T

V

L

V

L

L

A

H

A

L

L

I

R

A

-

I

-

S

-

K

-

A

-

R

-

P

-

F

Y

F

W

M

G

R

V

I

H

V

G

D

A

A

L

C

E

E

R

K

L

L

N

Q

G

G

M

-

F

-

A

A

F

Y

A

S

L

M

W

V

D

F

R

V

T

T

E

E

R

D

T

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

M

H

G

G

E

F

K

R

P

P

L

L

Y

V

Y

M

G

G

-

R

R

R

S

S

G

N

D

G

T

A

F

V

L

V

F

F

G

A

S

S

E

E

L

T

K

C

A

A

L

L

active site: C1 (= C2), G27 (= G29), N102 (= N75), G103 (= G76)

Sites not aligning to the query:

active site: 243, 301, 306, 316, 424
binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437

Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 26% coverage: 2:168/648 of query aligns to 87:285/561 of Q9STG9

query
sites
Q9STG9

C

C

G

G

I

V

V

V

G

G

Y

I

W

Y

S

G

R

-

N

D

S

S

R

E

S

A

V

S

D

R

V

L

A

C

S

Y

R

L

M

A

A

L

H

H

R

A

I

L

A

Q

T

H

R

R

G

G

P

Q

D

E

D

G

A

A

G

G

-

I

-

V

-

T

-

V

-

S

-

K

-

D

-

K

-

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

-

G

-

L

-

V

-

S

-

E

V

V

W

F

A

S

E

E

G

S

E

K

-

L

-

D

-

Q

-

L

-

P

G

G

E

D

P

I

V

A

L

I

A

G

H

H

R

V

R

R

L

Y

S

S

I

T

V

A

D

G

L

S

S

S

P

M

A

L

G

K

H

N

-

V

Q

Q

P

P

M

F

V

V

S

A

P

G

-

Y

-

R

C

F

G

G

R

S

Y

V

V

G

L

V

S

A

Y
x
H

N

N

G

G

E

N

I

L

Y

V

N

N

H

Y

T

T

E

K

L

L

R

R

Q

A

E

D

L

L

E

E

R

E

E

N

G

G

G

S

G

I

F

F

D

N

W

T

R

S

G

-

H

-

S

S

D

D

T

T

E

E

T

V

L

V

L

L

A

H

A

L

L

I

R

A

-

I

-

S

-

K

-

A

-

R

-

P

-

F

Y

F

W

M

G

R

V

I

H

V

G

D

A

A

L

C

E

E

R

K

L

L

N

Q

G

G

M

-

F

-

A

A

F

Y

A

S

L

M

W

V

D

F

R

V

T

T

E

E

R

D

T

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

M

H

G

G

E

F

K
x
R

P
|
P

L

L

Y

V

Y

M

G

G

-

R

R

R

S

S

G

N

D

G

T

A

F

V

L

V

F

F

G

A

S

S

E

E

L

T

K

C

A

A

L

L

H187 (≠ Y74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K148) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P149) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.

Sites not aligning to the query:

371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.

Query Sequence

>WP_077244558.1 NCBI__GCF_001995255.1:WP_077244558.1
MCGIVGYWSRNSRSVDVASRMAHRIATRGPDDAGVWAEGEGEPVLAHRRLSIVDLSPAGH
QPMVSPCGRYVLSYNGEIYNHTELRQELEREGGGFDWRGHSDTETLLAALRYWGVHGALE
RLNGMFAFALWDRTERTLFLARDRMGEKPLYYGRSGDTFLFGSELKALAAHPDWRGEVDR
DALALMLRYNNVPAPWSIYRGIYKLPPAHYLVVRGQGHQVGEPECYWDLPEVASEGAREA
KGEPDALADELDELLRDSVGRRMMADVPLGAFLSGGFDSTMVVAQMQAQSARPVKTFSIG
NADAEYDEAHHAAAVARHLGTDHRELYVTPEDAQAVIPRLPEIFDEPFADSSQIPTYLVS
ELARRDVTVTLSGDGGDELLGGYNRHVVGPGVWRRVNRLPGWLRGFLGGAVGNLSQRDLR
QWRRRLPARMQVPNLELKLEKLAKALGASDGPGFYRALRSRWKAPEGMVLGASEQQEQEG
PVDWLSDLPGLREQMMLLDMLTYLPDDILTKVDRASMAVSLEARVPLLDHRLVEFAWQVP
TEYKVRDGQGKWLLRKVLDRYVPSSLMERPKQGFGIPIEHWLRGPLRDWAESLLDEQRLC
EEGFFDPAPIRRVWTEHLAGRGRSQHRLWCVLMFQAWLDEQRKQFAVG

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory