SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 202575 FitnessBrowser__MR1:202575 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

A0A0H2VFI8 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
80% identity, 100% coverage: 1:555/555 of query aligns to 1:555/555 of A0A0H2VFI8

query
sites
A0A0H2VFI8

M

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E188 (= E188) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-456 (called EQ2).
E470 (= E470) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-188 (EQ2).

P0A9W3 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Escherichia coli (strain K12) (see 4 papers)
80% identity, 100% coverage: 1:555/555 of query aligns to 1:555/555 of P0A9W3

query
sites
P0A9W3

M
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M1 (= M1) modified: Initiator methionine, Removed
95:139 (vs. 95:139, 78% identical) Arm
E188 (= E188) mutation to Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity, 47-fold decrease in translation; when associated with Q-470 (called EQ2).
242:322 (vs. 242:322, 83% identical) PtIM
E470 (= E470) mutation to Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity, 47-fold decrease in translation; when associated with Q-188 (EQ2).

3j5sD Etta binds to ribosome exit site and regulates translation by restricting ribosome and tRNA dynamics (see paper)
80% identity, 100% coverage: 2:555/555 of query aligns to 1:554/554 of 3j5sD

query
sites
3j5sD

A

A

Q

Q

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V

Y

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L
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H

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P

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A

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N

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E

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N

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A

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L

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K

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R

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D

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E

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Y

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Y

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N

L

L

D
x
N

N
x
V

I
x
Q

L

L

E

E

R
|
R

A
|
A

A

A

N

D

A
|
A

L

L

R

R

L

L

P

P

D

D

W

W

D

D

E

A

K

K

I

I

E

A

V

N

L

L

S

S

G

G

E

E

R

R

V

V

A

A

I

L

C

C

R

R

L

L

E

E

K

K

P

P

E

D

M

M

L

L

D

D

E

E

P

P

T

T

N

N

H

H

L

L

D

D

A

A

E

E

S

S

V

V

A

A

W

W

L

L

E

E

H
x
R

F
|
F

L

L

Q

H

E

D

Y

F

A
x
E

G

G

T

T

V

V

A

A

I

I

T

T

H

H

D

D

R

R

Y

Y

F

F

L

L

D

D

N

N

A

V

A

A

G

G

W

W

I

I

L

L

E

E

L

L

D

D

R

R

G

G

E

E

G

G

I

I

P

P

W
|
W

E

E

G

G

N

N

Y

Y

S

S

W

W

L

L

E

E

Q

Q

K

K

D

D

A

Q

R

R

L

L

K

A

Q
|
Q

E

E

S

A

A

S

A
x
Q

E

E

S

A

A

A

R

R

Q

R

K

K

T

S

I

I

A

E

K

K

E

E

L

L

E

E

W

W

V

V

R
|
R

Q
|
Q

G

G

A

T

K

K

G

G

R

R

Q

Q

S

S

K

K

G

G

K

K

A

A

R

R

M

L

A

A

R

R

F

F

E

E

L

L

N

N

T

S

N

T

D

E

Y

Y

Q

Q

K

K

R

R

N

N

E

E

T

T

N

N

E

E

L

L

F

F

I

I

P

P

G

G

P

P

R

R

L

L

G
|
G

D
|
D

K

K

V

V

I

L

E

E

V

V

N

S

N

N

L

L

T

R

K

K

S

S

Y

Y

G

G

D

D

R

R

V

L

L

L

I

I

D

D

N

D

L

L

S

S

F

F

S

S

V

I

P

P

K

K

G

G

A

A

I

I

V

V

G

G

I

I

G

G

A

P

N

N

G

G

A

A

G

G

K

K

S

S

T

T

L

L

F

F

R

R

M

M

L

I

S

S

G

G

S

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E

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Q

Q

P

P

D

D

S

S

G

G

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I

I

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L

L

G

G

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E

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T

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V

Q

K

L

L

A

A

S

S

V

V

E

D

Q

Q

F

F

R

R

D

D

S

S

M

M

N

D

D

N

K

S

N

K

T

T

I

V

W

W

Q

E

E

E

I

V

S

S

G

G

Q

L

D

D

I

I

M

M

R

K

I

I

N

G

N

N

M

T

E

E

I

M

P

P

S

S

R

R

A

A

Y

Y

V

V

G

G

R

R

F

F

N

N

F

F

R

K

G

G

G

V

D

D

Q

Q

Q

G

K

K

I

R

I

V

G

G

T

E

L

L

S

S

G

G

E

E

R

R

N

G

R

R

V

L

H

H

L

L

A

A

K

K

L

L

Q

Q

A

V

G

G

N

N

V

M

L

L

D

D

E

E

P

P

T

T

N

N

D

D

L

L

D

D

V

I

E

E

T

T

L

L

R

R

A

A

L

L

E

E

E

N

A

A

I

L

L

L

E

E

F

F

P

P

G

G

C

C

A

A

M

M

V

V

I

I

S

S

H

H

D

D

R

R

W

W

F

F

L

L

D

D

R

R

I

I

A

A

T

T

H

H

I

I

L

L

D

D

Y

Y

R

Q

D

D

E

E

G

G

Q

K

V

V

N

E

F

F

Y

F

E

E

G

G

N

N

Y

F

T

T

E

E

Y

Y

S

E

A

E

W

Y

L

K

K

K

N

R

T

T

Y

L

G

G

A

A

D

D

V

A

V

L

E

E

P

P

H

K

R

R

L

I

K

K

Y

Y

K

K

R

R

M

I

T

A

K

K

binding : F3 (= F4), H8 (≠ L9), S27 (= S28), R63 (= R64), N140 (≠ D141), V141 (≠ N142), Q142 (≠ I143), R145 (= R146), A146 (= A147), A149 (= A150), R202 (≠ H203), F203 (= F204), E208 (≠ A209), W239 (= W240), Q256 (= Q257), Q260 (≠ A261), R276 (= R277), Q277 (= Q278), G319 (= G320), D320 (= D321)

P9WQK3 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
52% identity, 100% coverage: 1:555/555 of query aligns to 1:557/558 of P9WQK3

query
sites
P9WQK3

M

M

A

A

Q

E

F

F

V

I

Y

Y

S

T

M

M

L

K

R

K

V

V

G

R

K

K

V

A

V

-

P

H

P

G

K

D

K

K

Q

V

I

I

L

L

K

D

D

D

I

V

S

T

L

L

S

S

F

F

F

Y

P

P

G

G

A

A

K

K

I

I

G

G

V

V

L

V

G

G

L

P

N

N

G

G

S

A

G

G

K

K

S

S

T

S

L

V

L

L

R

R

I

I

M

M

A

A

G

G

I

L

D

D

T

K

E

P

I

N

E

N

G

G

E

D

A

A

R

F

P

L

M

A

P

T

G

G

L

A

K

T

I

V

G

G

Y

I

L

L

P

Q

Q

Q

E

E

P

P

K

P

L

L

D

N

P

E

N

D

Q

K

T

T

V

V

R

R

E

G

A

N

I

V

E

E

A

G

V

M

S

G

E

D

A

I

K

K

N

I

A

K

L

L

K

D

R

R

L

F

D

N

E

E

V

V

Y

A

A

E

A

L

Y

M

A

A

E

-

P

-

D

-

A

T

D

D

F

Y

-

T

D

D

A

E

L

L

A

M

K

E

E

E

Q

M

G

G

E

R

L

L

E

Q

A

E

I

E

I

L

Q

D

A

H

Q

A

D

D

A

A

H

W

N

D

L

L

D

D

N

A

I

Q

L

L

E

E

R

Q

A

A

A

M

N

D

A

A

L

L

R

R

L

C

P

P

D

P

W

A

D

D

E

E

K

P

I

V

E

T

V

N

L

L

S

S

G

G

E

E

R

R

V

V

A

A

I

L

C

C

R

K

L

L

E

S

K

K

P

P

E

D

M

L

L

L

D

D

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E

P

P

T

T

N

N

H

H

L

L

D

D

A

A

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E

S

S

V

V

A

Q

W

W

L

L

E

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H

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F

H

L

L

Q

A

E

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Y

Y

A

P

G

G

T

A

V

I

V

L

A

A

I

V

T

T

H

H

D

D

R

R

Y

Y

F

F

L

L

D

D

N

N

A

V

A

A

G

E

W

W

I

I

L

L

E

E

L

L

D

D

R

R

G

G

E

R

G

A

I

Y

P

P

W

Y

E

E

G

G

N

N

Y

Y

S

S

S

T

W

Y

L

L

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E

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K

K

K

D

A

A

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R

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L

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V

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G

A

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D

S

A

A

K

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L

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Q

K

K

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I

L

A

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K

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L

L

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W

W

V

V

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G

G

A

A

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K

G

A

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R

Q

Q

S

A

K

K

G

S

K

K

A

A

R

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M

L

A

Q

R

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F

Y

E

E

L

M

N

A

T

A

N

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D

A

Y

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K

K

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R

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-

L

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D

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F

N

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F

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I

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L

L

G

G

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N

K

V

V

V

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V

V

N

D

N

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L

L

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D

K

K

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G

Y

Y

G

D

D

G

R

R

V

A

L

L

I

I

D
x
K

N

D

L

L

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S

F

F

S

S

V

L

P

P

K

R

G

N

A

G

I

I

V

V

G

G

I

V

I

I

G

G

A

P

N

N

G

G

A

V

G

G

K

K

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T

T

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L

L

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F

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K

M

T

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V

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K

L

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Y

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V

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Q

F

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A

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M

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N

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D

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W

W

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E

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S

G

D

G

G

Q

L

D

D

I

Y

M

I

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N

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N

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M

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P

P

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R

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A

A

Y

Y

V

V

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S

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A

F

F

N

G

F

F

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K

G

G

G

P

D

D

Q

Q

K

K

I

P

I

A

G

G

T

V

L

L

S

S

G

G

E

E

R

R

N

N

R

R

V

L

H

N

L

L

A

A

K

L

L

T

L

L

Q

K

A

Q

G

G

N

N

V

L

L

I

L

L

D

D

E

E

P

P

T

T

N

N

D

D

L

L

D

D

V

V

E

E

T

T

L

L

R

G

A

S

L

L

E

E

E

N

A

A

I

L

L

L

E

N

F

F

P

P

G

G

C

C

A

A

M

V

V

V

I

I

S

S

H

H

D

D

R

R

W

W

F

F

L

L

D

D

R

R

I

T

A

C

T

T

H

H

I

I

L

L

-

A

-

W

-

E

-

G

D

D

Y

D

R

D

D

N

E

E

G

A

Q

K

V

W

N

F

F

W

Y

F

E

E

G

G

N

N

Y

F

T

G

E

A

Y

Y

S

E

A

E

W

N

L

K

K

V

N

E

T

R

Y

L

G

G

A

V

D

D

V

A

E

R

P

P

H

H

R

R

L

V

K

T

Y

H

K

R

R

K

M

L

T

T

K

R

K338 (≠ D340) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

7mscx 70SIC in complex with MtbEttA at Pre_R0 state (see paper)
53% identity, 95% coverage: 2:530/555 of query aligns to 1:531/547 of 7mscx

query
sites
7mscx

A

A

Q
x
E

F
|
F

V

I

Y

Y

S

T

M

M

L

K

R

K

V

V

G

R

K

K

V

A

V

-

P
x
H

P

G

K

D

K

K

Q

V

I

I

L

L

K

D

D

D

I

V

S

T

L

L

S

S

F

F

F
x
Y

P

P

G

G

A

A

K

K

I

I

G

G

V

V

L

V

G

G

L

P

N
|
N

G

G

S

A

G
|
G

K
|
K

S
|
S

T
x
S

L

V

L

L

R

R

I

I

M

M

A

A

G

G

I

L

D

D

T

K

E

P

I

N

E

N

G

G

E

D

A

A

R

F

P

L

M

A

P

T

G

G

L

A

K

T

I

V

G

G

Y

I

L

L

P

Q

Q
|
Q

E

E

P

P

K

P

L

L

D

N

P

E

N

D

Q

K

T

T

V

V

R

R

E

G

A

N

I

V

E

E

A

G

V

M

S

G

E

D

A

I

K

K

N

I

A

K

L

L

K

D

R

R

L

F

D

N

E

E

V

V

Y

A

A

E

A

L

Y

M

A

A

E

-

P

-

D

-

A

T

D

D

F

Y

-

T

D

D

A

E

L

L

A

M

K

E

E

E

Q

M

G

G

E

R

L

L

E

Q

A

E

I

E

I

L

Q

D

A

H

Q

A

D

D

A

A

H

W

N

D

L

L

D

D

N

A

I

Q

L

L

E

E

R
x
Q

A

A

A

M

N

D

A

A

L

L

R

R

L

C

P

P

D

P

W

A

D

D

E

E

K

P

I

V

E

T

V
x
N

L

L

S
|
S

G
|
G

E

E

R

R

V

V

A

A

I

L

C

C

R

K

L

L

E

S

K

K

P

P

E

D

M

L

L

L

D
|
D

E

E

P

P

T

T

N

N

H

H

L

L

D

D

A

A

E

E

S

S

V

V

A

Q

W

W

L

L

E

E

H

Q

F

H

L

L

Q

A

E

S

Y

Y

A

P

G

G

T

A

V

I

V

L

A

A

I

V

T

T

H
|
H

D

D

R

R

Y

Y

F

F

L

L

D

D

N

N

A

V

A

A

G

E

W

W

I

I

L

L

E

E

L

L

D

D

R

R

G

G

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R

G

A

I

Y

P

P

W

Y

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E

G

G

N

N

Y

Y

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S

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W

Y

L

L

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Q

K

K

K

D

A

A

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R

R

L

L

K

A

Q

V

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Q

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G

A
x
R

A
x
K

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D

S

A

A
x
K

R

L

Q

Q

K

K

T

R

I

L

A

T

K

E

E

E

L

L

E

A

W

W

V

V

R
|
R

Q
x
S

G

G

A

A

K
|
K

G
x
A

R
|
R

Q
|
Q

S

A

K

K

G
x
S

K
|
K

A
|
A

R
|
R

M

L

A

Q

R
|
R

F

Y

E

E

L

M

N

A

T

A

N

E

D

A

Y

E

Q

K

K

T

R
|
R

N

K

-

L

E

D

T

F

N

E

E

E

L

I

F

Q

I

I

P

P

P

V

G

G

P

P

R
|
R

L

L

G
|
G

D
x
N

K

V

V

V

I

V

E

E

V

V

N

D

N

H

L

L

T

D

K

K

S

G

Y
|
Y

G

D

D

G

R
|
R

V

A

L

L

I

I

D

K

N

D

L

L

S

S

F

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binding phosphoaminophosphonic acid-adenylate ester: H14 (≠ P16), N39 (= N41), G42 (= G44), K43 (= K45), S44 (= S46), S45 (≠ T47), Q74 (= Q76), N158 (≠ V162), S160 (= S164), G161 (= G165), G162 (= G166), H213 (= H217), Y330 (= Y333), R333 (= R336), N355 (= N358), G356 (= G359), G358 (= G361), K359 (= K362), T360 (≠ S363), T361 (= T364), K437 (= K440), S443 (= S446), G445 (= G448), E446 (= E449), H496 (= H499)
binding magnesium ion: S44 (= S46), Q74 (= Q76), D183 (= D187)
binding : E2 (≠ Q3), F3 (= F4), Y28 (≠ F30), Q142 (≠ R146), R256 (≠ A260), K257 (≠ A261), K260 (≠ A264), R273 (= R277), S274 (≠ Q278), K277 (= K281), K277 (= K281), A278 (≠ G282), R279 (= R283), Q280 (= Q284), S283 (≠ G287), K284 (= K288), A285 (= A289), R286 (= R290), R289 (= R293), R301 (= R305), R315 (= R318), G317 (= G320), N318 (≠ D321), T382 (= T385), D410 (= D413), Y411 (≠ I414), R422 (= R425), A423 (= A426)

Sites not aligning to the query:

binding : 543, 544, 547

P43672 ATP-binding protein Uup; EC 3.6.1.- from Escherichia coli (strain K12) (see 3 papers)
32% identity, 91% coverage: 21:527/555 of query aligns to 18:523/635 of P43672

query
sites
P43672

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D181 (= D187) mutation to N: No longer hydrolyzes ATP, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, not required to suppress bipA deletion.
E182 (= E188) mutation to Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-464 (called EQ2).
294:300 (vs. 300:306, 14% identical) mutation Missing: Decreases growth at 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.
D465 (= D469) mutation to N: No longer hydrolyzes ATP, has a high level of transposon excision. Inhibits growth at 37 and 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.
E466 (= E470) mutation to Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-181 (EQ2).

Sites not aligning to the query:

551:635 C-terminal domain (CTD), binds DNA, required to complement a deletion mutant; mutation Missing: Reduces DNA binding 2-fold, no change in ATP hydrolysis, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.

A0A0H2VBH0 Probable ATP-binding protein YheS from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
32% identity, 96% coverage: 4:537/555 of query aligns to 2:522/637 of A0A0H2VBH0

query
sites
A0A0H2VBH0

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T

T

T

H

D

I

D

L

L

D

Y

Y

L

R

V

D

H

E

D

G

R

Q

K

V

V

N

E

F

P

Y

F

E

D

G

G

N

D

Y

L

T

E

E

D

Y

Y

S

Q

A

Q

W

W

L

L

K

S

N

D

T

V

E175 (= E188) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-456 (called EQ2).
E456 (= E470) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-175 (EQ2).

P63389 Probable ATP-binding protein YheS from Escherichia coli (strain K12) (see paper)
32% identity, 96% coverage: 4:537/555 of query aligns to 2:522/637 of P63389

query
sites
P63389

F

I

V

V

Y

F

S

S

M

S

L

L

R

Q

V

I

G

R

K

R

V

G

V

V

P

-

K

-

K

R

Q

V

I

L

L

L

K

D

D

N

I

A

S

T

L

A

S

T

F

I

F

N

P

P

G

G

A

Q

K

K

I

V

G

G

V

L

L

V

G

G

L

K

N

N

G

G

S

C

G

G

K

K

S

S

T

T

L

L

R

A

I

L

M

L

A

K

G

N

I

-

D

E

T

I

E

S

I

A

E

D

G

G

E

G

A

S

R

Y

P

T

M

F

P

P

G

G

-

S

L

W

K

Q

I

L

G

A

Y

W

L

V

P

N

Q

Q

E

E

P

T

K

P

L

A

D

L

P

P

N

-

Q

-

T

-

V

-

R

-

E

Q

A

A

I

A

E

L

E

E

A

Y

V

V

S

I

E

D

A

G

K

D

N

R

A

E

L

Y

K

R

R

Q

L

L

D

-

E

E

V

A

Y

Q

A

L

A

H

Y

D

A

A

E

N

P

E

D

R

A

N

D

D

F

G

D

H

A

A

L

I

A

A

K

T

E

I

Q

H

G

G

E

K

L

L

E

D

A

A

I

I

I

-

Q

-

A

-

Q

-

D

D

A

A

H

W

N

S

L

-

D

-

N

-

I

I

L

R

E

S

R

R

A

A

N

S

A

L

L

L

R

H

-

G

L

L

P

G

D

F

W

S

D

N

E

E

K

Q

I

L

E

E

V

R

-

P

-

V

-

S

-

D

L

F

S

S

G

G

E

W

R

R

R

M

R

R

V

L

A

N

I

L

C

A

R

Q

L

A

L

L

L

I

E

C

K

R

P

S

E

D

M

L

L

L

D

D

E
|
E

P

P

T

T

N

N

H

H

L

L

D

D

A

L

E

D

S

A

V

V

A

I

W

W

L

L

E

E

H

K

F

W

L

L

Q

K

E

S

Y

Y

A

Q

G

G

T

T

V

L

V

I

A

L

I

I

T

S

H

H

D

D

R

R

Y

D

F

F

L

L

D

D

N

P

A

I

A

V

G

D

W

K

I

I

L

I

E

H

L

I

D

E

R

Q

G

Q

E

S

G

M

I

F

P

E

W

Y

E

T

G

G

N

N

Y

Y

S

S

W

F

L

E

E

V

Q

Q

K

R

D

A

A

T

R

R

L

L

K

A

Q

Q

E

Q

S

Q

A

A

A

M

E

Y

S

E

A

S

R

Q

Q

Q

K

E

T

R

I

V

A

A

K

H

E

L

L

Q

E

S

W

Y

V

I

-

D

-

R

-

F

-

R

R

A

Q

K

G

A

A

T

K

K

G

A

R

K

Q

Q

S

A

K

Q

G

S

K

R

A

I

R

K

M

M

A

L

R

E

F

R

E

M

E

E

L

L

N

I

T

A

N

P

D

A

Y

H

Q

V

K

D

R

-

N

N

E

P

T

F

N

R

E

F

L

S

F

F

I

R

P

A

P

P

G

-

P

E

R

S

L

L

G

P

D

N

K

P

V

L

I

L

E

K

V

M

N

E

N

K

L

V

T

S

K

A

S

G

Y

Y

G

G

D

D

R

R

V

I

L

I

I

L

D

D

N

S

L

I

S

K

F

L

S

N

V

L

P

V

K

P

G

G

A

S

I

R

V

I

G

G

I

L

G

G

A

R

N

N

G

G

A

A

G

G

K

K

S

S

T

T

L

L

F

I

R

K

M

L

L

L

S

A

G

G

S

E

E

L

Q

A

P

P

D

V

S

S

G

G

S

E

I

I

E

G

L

L

G

A

E

K

T

G

V

I

Q

K

L

L

A

G

S

Y

V

F

E

A

Q

Q

F

-

R

-

D

-

S

-

M

-

N

H

D

Q

K

L

N

E

T

Y

I

L

W

R

Q

A

E

D

I

E

S

S

G

P

G

I

Q

Q

D

H

I

L

M

A

R

R

I

L

N

A

N

P

M

Q

E

E

I

L

P

E

S

Q

-

K

-

L

R

R

A

D

Y

Y

V

L

G

G

R

G

F

F

N

G

F

F

R

Q

G

G

G

D

D

K

Q

V

Q

T

K

E

I

E

I

T

G

R

T

R

L

F

S

S

G

G

E

E

R

K

N

A

R

R

V

L

H

V

L

L

A

A

K

L

L

I

L

V

Q

W

A

Q

G

R

G

P

N

N

V

L

L

L

D

D

E
|
E

P

P

T

T

N

N

D

H

L

L

D

D

V

L

E

D

T

M

L

R

R

Q

A

A

L

L

E

T

E

E

A

A

I

L

L

I

E

E

F

F

P

E

G

G

C

A

A

L

M

V

V

V

I

V

S

S

H

H

D

D

R

R

W

H

F

L

L

L

D

-

R

R

I

S

A

T

T

T

H

D

I

D

L

L

D

Y

Y

L

R

V

D

H

E

D

G

R

Q

K

V

V

N

E

F

P

Y

F

E

D

G

G

N

D

Y

L

T

E

E

D

Y

Y

S

Q

A

Q

W

W

L

L

K

S

N

D

T

V

E175 (= E188) mutation to Q: Causes growth defect at 37 degrees Celsius, 7-fold decrease in translation; when associated with Q-456 (called EQ2).
E456 (= E470) mutation to Q: Causes growth defect at 37 degrees Celsius, 7-fold decrease in translation; when associated with Q-175 (EQ2).

8buu9 50S ribosomal protein L13 (see paper)
29% identity, 92% coverage: 19:530/555 of query aligns to 19:516/573 of 8buu9

query
sites
8buu9

K

R

Q

K

I

V

L

L

K

Q

D

N

I

L

S

H

L

F

S
x
E

F

I

F
x
K

P

N

G

G

A

D

K

R

I

I

G

G

V

L

L

V

G

G

L

Y

N
|
N

G
|
G

S

T

G
|
G

K
|
K

S
x
T

T
|
T

L

L

L

A

R

N

I

I

M

I

A

F

G

G

I

K

D

I

T

T

E

P

I

D

E

N

G

G

E

L

A

I

R

E

P

K

M

S

P

R

G

D

L

L

K

R

I

M

G

G

Y

Y

L

L

P

S

Q

Q

E

-

P

-

K

-

L

-

D

-

P

-

N

-

Q

-

T

-

V

-

R

-

E

-

A

S

I

I

E

D

E

Y

A

E

V

V

S

S

E

H

A

F

K

Q

N

Q

A

S

L

I

K

A

R

E

L

V

D

E

E

E

V

-

Y

-

A

-

Y

-

A

-

E

-

P

-

D

-

A

-

D

-

F

-

D

-

A

-

L

-

A

-

K

-

E

-

Q

-

G

-

E

-

L

-

E
x
H

A

E

I

L

I

F

Q
|
Q

A

H

Q

A

D
x
S

A

S

H

L

N

G

L

L

D

N

N

K

I

V

L

F

E

-

R

-

A

-

N

-

A

-

L

-

R

-

L

-

P

-

D

D

W

W

D

S

E

E

-

D

K
x
R

I

L

E

T

V
x
H

L

L

S
|
S

G

G

E
|
E

R

K

R

L

R

K

V

L

A

A

I

L

C

S

R

M

L

V

L

W

L

A

E

T

K

K

P

P

E

D

M

F

L

L

L

I

L

L

D

D

E

Q

P

P

T

T

N

N

H

H

L

L

D

D

A

F

E

T

S

G

V

I

A

N

W

W

L

L

E

V

H

S

F

E

L

L

Q

E

E

K

Y

F

A

H

G

G

T

P

V

V

V

L

A

I

I

I

T

S

H

H

D

D

R

R

Y

H

F

F

L

L

D

D

N

K

A

T

A

V

G

N

W

R

I

I

L

F

E

E

L

L

D

E

R

E

G

S

E

R

G

I

I

Q

P

F

W

F

E

N

G

G

N

N

Y

Y

S

S

S

D

W

Y

L

R

E

I

Q

E

K

K

D

E

A

Q

R

R

L

I

K

A

Q
x
N

E

Q

S

R

A
x
H

A
x
Q

E

Y

S

Q

A

V

R

Q

Q

Q

K

R

T

Q

I

I

A

E

K

K

-

I

-

E

-

T

-
x
Q

-

M

-

V

E
x
Q

L

L

-

K

-

S

-
x
W

-

S

-

E

-
x
K

-
x
A

-
x
H

-
x
R

-

D

-

S

-

T

-

K

-

Q

-

G

-

S

-

A

-
x
S

-
x
E

-

R

-
x
R

-
x
Q

-
x
I

-
x
G

-

F

-
x
K

E
|
E

W
x
Y

V

H

R
|
R

Q

V

G
x
K

A

A

K
|
K

G
x
K

R

L

Q
x
D

S
x
N

K

Q

G

V

K
|
K

A
x
S

R
x
K

M

M

A

K

R
|
R

F

L

E

Q

-

N

E

E

L

L

N

N

T

K

N

H

D

K

Y

L

Q

E

K

K

R

P

N

N

E

E

T

E

N

A

E

A

L

V

-
x
R

-

F

-

Q

F

F

I

D

P

S

P

H

G

G

P
x
K

R
|
R

L

-

G

G

D

K

K
x
R

V

I

I

I

E

E

V

A

N

K

L

L

T

T

K

K

S

M

Y
x
F

G

D

D

D

R
|
R

V

I

L

L

I

F

D

Q

N

D

L

S

S

P

F

F

S

Y

V

I

P

N

K

H

G

G

A

D

I

R

V

I

G

G

I

L

G

G

A

E

N

N

G
|
G

A

C

G
|
G

K
|
K

S
x
T

T
|
T

L

L

F

I

R

K

M

M

L

I

S

L

G

G

S

D

E

D

Q

L

P

S

D

F

S

V

G

G

S

E

I

L

E
x
W

L

K

G
x
S

E

D

T
x
S

V

V

Q

K

L

I

A

A

S

Y

V

L

E

S

Q
|
Q

-

D

F

V

R

A

D

D

S

L

M

S

N

A

D

D

K

K

N

T

T

A

I

I

W

-

Q

-

E

E

I

A

S

L

G

G

G

F

Q

T

D

D

I

R

M

E

R

S

I

I

N

-

M

-

E

-

I
x
L

P

K

S

A

R
|
R

A
x
T

Y

L

V

L

G
x
A

R
x
N

F

L

N

G

F

L

R
x
K

G

E

G

Q

D

L

Q

I

Q

T

K

K

I

P

I

I

G

G

T
|
T

L

L

S
|
S

G
x
L

G
|
G

E
|
E

R

R

N

T

R

R

V

V

H

K

L

L

A

V

K

D

L

M

L

L

Q

M

A

K

G

E

G

Y

N

D

V

V

L

L

L

I

L

L

D

D

E

Q

P

P

T

T

N

N

D

H

L

L

D

D

V

L

E

P

T

S

L

R

R

E

A

Q

L

L

E

E

E

Q

A

T

I

L

L

S

E

E

F

F

P

T

G

G

C

T

A

I

M

I

V

T

I

V

S

S

H

H

D

D

R

H

W

Y

F

F

L

L

D

N

R

K

I

L

A

C

T

D

H

R

I

L

L

L

D

V

Y

F

R

E

D

N

E

Q

G

-

Q

Q

V

I

N

K

F

R

Y

F

E

E

G

M

N

K

Y

P

T

Q

E

E

Y

Y

binding adenosine-5'-triphosphate: N41 (= N41), G42 (= G42), G44 (= G44), K45 (= K45), T46 (≠ S46), T47 (= T47), R116 (≠ K159), H119 (≠ V162), S121 (= S164), E124 (= E167), F325 (≠ Y333), R328 (= R336), G351 (= G359), G353 (= G361), K354 (= K362), T355 (≠ S363), T356 (= T364), Q385 (= Q393), T431 (= T444), S433 (= S446), L434 (≠ G447), G435 (= G448), E436 (= E449)
binding magnesium ion: T46 (≠ S46), T355 (≠ S363), Q385 (= Q393), L434 (≠ G447)
binding : E28 (≠ S28), K30 (≠ F30), H95 (≠ E129), Q99 (= Q133), S102 (≠ D136), N214 (≠ Q257), H217 (≠ A260), Q218 (≠ A261), Q232 (vs. gap), Q235 (≠ E272), W239 (vs. gap), K242 (vs. gap), A243 (vs. gap), H244 (vs. gap), R245 (vs. gap), S254 (vs. gap), E255 (vs. gap), R257 (vs. gap), Q258 (vs. gap), I259 (vs. gap), G260 (vs. gap), K262 (vs. gap), E263 (= E274), Y264 (≠ W275), R266 (= R277), K268 (≠ G279), K270 (= K281), K271 (≠ G282), D273 (≠ Q284), N274 (≠ S285), K277 (= K288), S278 (≠ A289), K279 (≠ R290), R282 (= R293), R302 (vs. gap), K310 (≠ P317), R311 (= R318), R314 (≠ K322), W373 (≠ E381), S375 (≠ G383), S377 (≠ T385), L409 (≠ I422), R412 (= R425), T413 (≠ A426), A416 (≠ G429), N417 (≠ R430), K421 (≠ R434)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 16
binding : 8

P0A9U3 Probable ATP-binding protein YbiT from Escherichia coli (strain K12) (see paper)
29% identity, 92% coverage: 19:530/555 of query aligns to 14:523/530 of P0A9U3

query
sites
P0A9U3

K

K

Q

P

I

L

L

F

K

E

D

N

I

I

S

S

L

V

S

K

F

F

F

G

P

G

G

G

A

N

K

R

I

Y

G

G

V

L

L

I

G

G

L

A

N

N

G

G

S

S

G

G

K

K

S

S

T

T

L

F

L

M

R

K

I

I

M

L

A

G

G

G

I

D

D

L

T

E

E

P

I

T

E

L

G

G

E

N

A

V

R

S

P

L

M

D

P

P

G

N

L

E

K

R

I

I

G

G

Y

K

L

L

P

R

Q

Q

E

D

P

Q

K

F

L

A

D

F

P

E

N

E

Q

F

T

T

V

V

R

L

E

D

A

T

I

V

E

I

E

M

A

G

V

H

S

K

E

E

A

L

K

W

N

E

A

V

L

K

K

Q

R

E

L

R

D

D

E

R

V

I

Y

Y

A

A

A

L

Y

P

A

E

E

M

P

S

D

E

A

E

D

D

F

G

D

Y

A

K

L

V

A

A

K

-

E

-

Q

-

G

-

E

D

L

L

E

E

A

V

I

K

I

Y

Q

G

A

E

Q

M

D

D

A

G

H

Y

N

S

L

A

D

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N

A

I

R

L

A

E

G

R

E

A

L

N

L

A

G

L

V

R

G

L

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P

P

-

V

-

E

-

Q

D

H

W

Y

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K

M

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K

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V

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A

L

L

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F

E

A

K

D

P

P

E

D

M

I

L

L

D

D

E
|
E

P

P

T

T

N

N

H

N

L

L

D

D

A

I

E

D

S

T

V

I

A

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W

W

L

L

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Q

F

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L

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N

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Y

R

A

D

G

S

T

T

V

M

V

I

A

I

I

I

T

S

H

H

D

D

R

R

Y

H

F

F

L

L

D

N

N

M

A

V

A

C

G

T

W

H

I

M

L

A

E

D

L

L

D

D

R

Y

G

G

E

E

G

L

I

R

P

V

W

Y

E

P

G

G

N

N

Y

Y

S

D

S

E

W

Y

L

M

E

T

Q

A

K

A

D

-

A

T

R

Q

L

A

K

R

Q

E

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S

L

A

L

A

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N

A

A

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K

Q

K

K

K

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A

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Q

A

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L

L

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S

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F

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-

A

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F

I

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K

L

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N

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D

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K

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S

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N

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L

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F

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-

R

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K

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K

L

L

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A

I

L

E

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V

V

N

E

N

G

L

L

T

T

K

K

S

G

Y

F

G

D

D

N

R

G

V

P

L

L

I

F

D

K

N

N

L

L

S

N

F

L

S

L

V

L

P

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K

V

G

G

A

E

I

K

V

L

G

A

I

V

I

L

G

G

A

T

N

N

G

G

A

V

G

G

K

K

S

S

T

T

L

L

F

L

R

K

M

T

L

L

S

V

G

G

S

D

E

L

Q

Q

P

P

D

D

S

S

G

G

S

T

I

V

E

K

L

W

G

S

E

E

T

N

V

A

Q

R

L

I

A

G

S

Y

V

Y

E

A

Q

Q

-

D

-

H

-

E

-

Y

-

E

F

F

R

E

D

N

S

D

M

L

N

T

D

V

K

F

N

E

T

W

I

M

W

S

Q

Q

E

W

I

K

S

Q

G

E

G

G

Q

D

D

D

I

-

M

-

R

-

I

-

N

-

M

-

E

E

I

Q

P

A

S

V

R

R

A

S

Y

I

V

L

G

G

R

R

F

L

N

L

F

F

R

S

G

Q

G

D

D

D

Q

I

Q

K

K

K

I

P

I

A

G

K

T

V

L

L

S

S

G

G

E

E

R

K

N

G

R

R

V

M

H

L

L

F

A

G

K

K

L

L

L

M

Q

M

A

Q

G

K

G

P

N

N

V

I

L

L

L

I

L

M

D

D

E
|
E

P

P

T

T

N

N

D

H

L

L

D

D

V

M

E

E

T

S

L

I

R

E

A

S

L

L

E

N

E

M

A

A

I

L

L

E

E

L

F

Y

P

Q

G

G

C

T

A

L

M

I

V

F

I

V

S

S

H

H

D

D

R

R

W

E

F

F

L

V

D

S

R

S

I

L

A

A

T

T

H

R

I

I

L

L

D

E

Y

I

R

T

D

P

E

E

G

R

Q

V

V

I

N

D

F

F

Y

-

E

S

G

G

N

N

Y

Y

T

E

E

D

Y

Y

E181 (= E188) mutation to Q: Causes growth defect at 37 degrees Celsius, 15-fold decrease in translation; when associated with Q-464 (called EQ2).
E464 (= E470) mutation to Q: Causes growth defect at 37 degrees Celsius, 15-fold decrease in translation; when associated with Q-181 (EQ2).

P0A9U4 Probable ATP-binding protein YbiT from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
29% identity, 92% coverage: 19:530/555 of query aligns to 14:523/530 of P0A9U4

query
sites
P0A9U4

K

K

Q

P

I

L

L

F

K

E

D

N

I

I

S

S

L

V

S

K

F

F

F

G

P

G

G

G

A

N

K

R

I

Y

G

G

V

L

L

I

G

G

L

A

N

N

G

G

S

S

G

G

K

K

S

S

T

T

L

F

L

M

R

K

I

I

M

L

A

G

G

G

I

D

D

L

T

E

E

P

I

T

E

L

G

G

E

N

A

V

R

S

P

L

M

D

P

P

G

N

L

E

K

R

I

I

G

G

Y

K

L

L

P

R

Q

Q

E

D

P

Q

K

F

L

A

D

F

P

E

N

E

Q

F

T

T

V

V

R

L

E

D

A

T

I

V

E

I

E

M

A

G

V

H

S

K

E

E

A

L

K

W

N

E

A

V

L

K

K

Q

R

E

L

R

D

D

E

R

V

I

Y

Y

A

A

A

L

Y

P

A

E

E

M

P

S

D

E

A

E

D

D

F

G

D

Y

A

K

L

V

A

A

K

-

E

-

Q

-

G

-

E

D

L

L

E

E

A

V

I

K

I

Y

Q

G

A

E

Q

M

D

D

A

G

H

Y

N

S

L

A

D

E

N

A

I

R

L

A

E

G

R

E

A

L

N

L

A

G

L

V

R

G

L

I

P

P

-

V

-

E

-

Q

D

H

W

Y

D

G

E

P

K

M

I

S

E

E

V

V

L

-

S

A

G

P

G

G

E

W

R

K

R

L

R

R

V

V

A

L

I

L

C

A

R

Q

L

A

L

L

L

F

E

A

K

D

P

P

E

D

M

I

L

L

D

D

E
|
E

P

P

T

T

N

N

H

N

L

L

D

D

A

I

E

D

S

T

V

I

A

R

W

W

L

L

E

E

H

Q

F

V

L

L

Q

N

E

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Y

R

A

D

G

S

T

T

V

M

V

I

A

I

I

I

T

S

H

H

D

D

R

R

Y

H

F

F

L

L

D

N

N

M

A

V

A

C

G

T

W

H

I

M

L

A

E

D

L

L

D

D

R

Y

G

G

E

E

G

L

I

R

P

V

W

Y

E

P

G

G

N

N

Y

Y

S

D

S

E

W

Y

L

M

E

T

Q

A

K

A

D

-

A

T

R

Q

L

A

K

R

Q

E

E

R

S

L

A

L

A

A

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D

S

N

A

A

R

K

Q

K

K

K

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A

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Q

A

I

K

A

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E

L

L

E

Q

-

S

-

F

-

V

-

S

-

R

W

F

V

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A

Q

N

G

A

A

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K

K

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Q

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A

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G

S

K

R

A

A

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R

M

-

A

-

R

Q

F

I

E

D

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K

L

I

N

K

T

L

N

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D

E

Y

V

Q

K

K

A

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N

S

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Q

N

N

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L

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F

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-

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D

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K

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K

L

L

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D

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N

V

A

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L

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E

V

V

N

E

N

G

L

L

T

T

K

K

S

G

Y

F

G

D

D

N

R

G

V

P

L

L

I

F

D

K

N

N

L

L

S

N

F

L

S

L

V

L

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K

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G

G

A

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I

K

V

L

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A

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V

I

L

G

G

A

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N

N

G

G

A

V

G

G

K

K

S

S

T

T

L

L

F

L

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K

M

T

L

L

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G

G

S

D

E

L

Q

Q

P

P

D

D

S

S

G

G

S

T

I

V

E

K

L

W

G

S

E

E

T

N

V

A

Q

R

L

I

A

G

S

Y

V

Y

E

A

Q

Q

-

D

-

H

-

E

-

Y

-

E

F

F

R

E

D

N

S

D

M

L

N

T

D

V

K

F

N

E

T

W

I

M

W

S

Q

Q

E

W

I

K

S

Q

G

E

G

G

Q

D

D

D

I

-

M

-

R

-

I

-

N

-

M

-

E

E

I

Q

P

A

S

V

R

R

A

S

Y

I

V

L

G

G

R

R

F

L

N

L

F

F

R

S

G

Q

G

D

D

D

Q

I

Q

K

K

K

I

P

I

A

G

K

T

V

L

L

S

S

G

G

E

E

R

K

N

G

R

R

V

M

H

L

L

F

A

G

K

K

L

L

L

M

Q

M

A

Q

G

K

G

P

N

N

V

I

L

L

L

I

L

M

D

D

E
|
E

P

P

T

T

N

N

D

H

L

L

D

D

V

M

E

E

T

S

L

I

R

E

A

S

L

L

E

N

E

M

A

A

I

L

L

E

E

L

F

Y

P

Q

G

G

C

T

A

L

M

I

V

F

I

V

S

S

H

H

D

D

R

R

W

E

F

F

L

V

D

S

R

S

I

L

A

A

T

T

H

R

I

I

L

L

D

E

Y

I

R

T

D

P

E

E

G

R

Q

V

V

I

N

D

F

F

Y

-

E

S

G

G

N

N

Y

Y

T

E

E

D

Y

Y

E181 (= E188) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-464 (called EQ2).
E464 (= E470) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-181 (EQ2).

7p7q0 30S ribosomal protein S19 (see paper)
29% identity, 90% coverage: 34:532/555 of query aligns to 28:533/534 of 7p7q0

query
sites
7p7q0

K

K

I

V

G

G

V

I

L

V

G

G

L

V

N
|
N

G
|
G

S

A

G
|
G

K
|
K

S
x
T

T
|
T

L

L

L

F

R

R

I

L

M

L

A

L

G

R

I

-

D

E

T

L

E

K

I

L

E

D

G

K

E

G

A

K

R

I

P

T

M

I

P

G

G

N

L

S

K

R

I

I

G

G

Y

Y

L

L

P

P

Q
|
Q

E

E

P

I

K

I

-

I

L

M

D

D

P

E

N

K

Q

M

T

T

V

V

R

L

E

E

A

F

I

L

E

A

E

E

A

G

V

-

S

R

E

P

A

I

K

K

N

K

A

M

L

E

K

T

R

E

L

L

D

N

E

Y

V

I

Y

Y

A

E

A

K

Y

L

A

T

E

V

P

V

D

D

A

D

D

D

F

K

-

Q

D

D

A
x
R

L

L

A

L

K

K

E

R

Q

M

G

G

E

W

L

L

E

Q

A

E

I

Q

I

L

Q

E

A

Y

Q

F

D

D

A

C

H
x
Y

N

E

L

A

D

E

N

S

I

I

L

L

E
x
L

R

D

A

L

A

V

N

D

A

S

L

M

R

Q

L

I

P

D

D

F

-

D

-

L

W

F

D

D

E
x
Q

K

P

I

I

E

S

V
x
E

L

L

S
|
S

G
|
G

E
x
Q

R

K

R

S

R

K

V

I

A

S

I

F

C

A

R

K

L

V

L

L

L

Y

E

S

K

K

P

P

E

E

M

I

L

L

D

D

E

Q

P

P

T

T

N

N

H

H

L

L

D

D

A

S

E

S

S

T

V

K

A

E

W

F

L

V

E

T

H

K

F

Y

L

L

Q

K

E

S

Y

Y

A

R

G

G

T

S

V

V

V

L

A

I

I

I

T

S

H

H

D

D

R

I

Y

D

F

F

L

L

D

N

N

Q

A

I

G

D

W

K

I

I

L

M

E

Y

L

I

D

D

R

K

-

V

-

T

G

H

E

K

G

I

I

S

P

I

W

Y

E

E

G

G

N

D

Y

Y

S

Y

S

T

W

Y

L

-

E

-

Q

-

K

-

D

-

A

-

R

-

L

K

K

K

Q
x
K

E

Y

S

S

A

E

A

N

E

Q

S

L

A

L

R

R

Q

E

K
|
K

T

M

I

I

-

I

-

Q

-

E

-

K

-

E

A

V

K

K

E

E

L

L

-

A

E

T

W
x
F

V

V

R
x
Q

Q
x
K

G

A

A
x
K

K
x
Q

G

A

R
x
S

Q
|
Q

S
x
T

K
x
N

G
x
H

K

A

A

L

R
x
K

M
x
R

A
x
M

R

G

F
x
L

E
|
E

E
x
R

L

A

N

I

T
x
R

N

L

D

D

Y
x
K

Q

K

K

K

R

K

N

N

E

L

T

T

N

K

-

R

-

D

-
x
K

-

V

-

Y

-

K

-

R

-

V

E

K

L

M

F

D

I

I

P

K

P

P

G

N

P

R

R

E

L

V

G

A

D

R

K

T

V

P

I

L

E

K

V

V

N

E

N

N

L

V

T

T

K

F

S

H

Y
|
Y

-

P

G

G

D

H

R

P

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L

L

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Y

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N

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N
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G

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K

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S

T
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T

L

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M

G

G

S

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N

Q

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G

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E

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V

L

L

A

C

K

K

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S

binding adenosine-5'-triphosphate: N35 (= N41), G36 (= G42), G38 (= G44), K39 (= K45), T40 (≠ S46), T41 (= T47), Q69 (= Q76), Q154 (≠ E158), E158 (≠ V162), S160 (= S164), G161 (= G165), G162 (= G166), Q163 (≠ E167), Y339 (= Y333), N365 (= N358), G366 (= G359), G368 (= G361), K369 (= K362), S370 (= S363), T371 (= T364), Q400 (= Q393), K441 (= K440), V445 (≠ T444), S447 (= S446), G449 (= G448), E450 (= E449)
binding magnesium ion: T40 (≠ S46), Q69 (= Q76), S370 (= S363), Q400 (= Q393)
binding : R114 (≠ A120), Y132 (≠ H138), L139 (≠ E145), K248 (≠ Q257), K258 (= K267), F273 (≠ W275), Q275 (≠ R277), K276 (≠ Q278), K278 (≠ A280), Q279 (≠ K281), S281 (≠ R283), Q282 (= Q284), Q282 (= Q284), T283 (≠ S285), T283 (≠ S285), N284 (≠ K286), H285 (≠ G287), H285 (≠ G287), K288 (≠ R290), R289 (≠ M291), M290 (≠ A292), L292 (≠ F294), E293 (= E295), R294 (≠ E296), R297 (≠ T299), K300 (≠ Y302), K310 (vs. gap), R426 (= R425), S430 (≠ G429), D436 (≠ G435)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 10
binding : 2, 22

P40024 ABC transporter ATP-binding protein ARB1; ATP-binding cassette protein involved in ribosome biogenesis 1; EC 3.6.5.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 97% coverage: 7:543/555 of query aligns to 88:609/610 of P40024

query
sites
P40024

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N

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N

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A

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A

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N

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GG 229:230 (= GG 165:166) mutation to DE: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity; when associated with D-519.
Y346 (vs. gap) mutation to A: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity.
G519 (= G448) mutation to D: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity; when associated with 229-D-E-230.

P39115 Ribosome protection protein VmlR; Multidrug resistance system ATP-binding protein VmlR from Bacillus subtilis (strain 168) (see 2 papers)
29% identity, 90% coverage: 21:518/555 of query aligns to 19:480/547 of P39115

query
sites
P39115

I

V

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K

D

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E

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V

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Q

D

N

I

L

M

M

R

R

I

-

N

-

M

-

E

-

I

-

P

-

S

-

R

-

A

-

Y

-

V

-

G

-

R

H

F

L

N

G

F

F

R

T

G

A

D

Q

Q

W

Q

T

K

E

I

P

I

I

G

K

T

H

L

M

S

S

G

M

G

G

E

E

R

R

N

V

R

K

V

I

H

K

L

L

A

M

K

A

L

Y

L

I

Q

L

A

E

G

E

G

K

N

D

V

V

L

L

L

I

L

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D

D

E
|
E

P

P

T

T

N

N

D

H

L

L

D

D

V

L

E

P

T

S

L

R

R

E

A

Q

L

L

E

E

A

T

I

L

L

S

E

Q

F

Y

P

S

G

G

C

T

A

L

M

L

V

A

I

V

S

S

H

H

D

D

R

R

W

Y

F

F

L

L

D

E

R

K

I

T

A

T

T

N

H

S

I

K

L

L

D

V

Y

I

R

S

D

N

E

N

G

G

E129 (= E188) mutation to Q: Probably has no ATPase activity, does not confer lincomycin resistance, cells enter stationary phase at lower cell density, almost all protein is bound to ribosomes; when associated with Q-432 (called EQ2). Used for electron microscopy.
183:289 (vs. 242:321, 22% identical) Antibiotic resistance domain (ARD)
F237 (vs. gap) mutation to A: No longer confers resistance to virginiamycin M, still confers resistance to lincomycin and tiamycin.; mutation to V: Still confers resistance to virginiamycin M, lincomycin and tiamycin.
E432 (= E470) mutation to Q: Probably has no ATPase activity, does not confer lincomycin resistance, cells enter stationary phase at lower cell density, almost all protein is bound to ribosomes; when associated with Q-129 (called EQ2). Used for electron microscopy.

Sites not aligning to the query:

483:547 C-terminal extension (CTE)
492:547 mutation Missing: No longer confers resistance to virginiamycin M.

O42943 Uncharacterized ABC transporter ATP-binding protein C16H5.08c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 90% coverage: 21:522/555 of query aligns to 90:590/618 of O42943

query
sites
O42943

I

L

L

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D

N

I

A

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T

L

I

S

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L

F

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G

A

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G

G

V

L

L

L

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G

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N

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G

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K

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S

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A

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A

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D

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E

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Y

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P

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I

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-

Y

-

L

I

L

E

N

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A

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A

A

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P

P

M

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P

D

G

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L

N

K

A

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Y

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Q

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A

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K

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Q

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R

E

E

A

A

E

I

I

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A

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T

A

A

K

D

N

D

A

V

L

D

K

D

R

V

L

L

D

L

E

E

V

-

Y

-

A

S

A

K

Y

Y

A

E

E

E

P

L

D

D

A

-

D

D

F

M

D

D

A

P

L

S

A

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K

F

E

E

Q

A

G

K

E

-

L

-

E

-

A

-

I

-

Q

A

A

A

Q

M

D

I

A

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H

H

N

G

L

L

D

G

N

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I

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M

A

M

A

A

N

K

A

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L

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D

D

E

-

K

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I

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A

A

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A

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F

E

I

K

K

P

P

E

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M

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D

E

E

P

P

T

T

N

N

H

H

L

L

D

D

A

L

E

E

S

A

V

V

A

V

W

W

L

L

E

E

H

N

F

Y

L

L

Q

A

E

K

Y

Y

A

D

G

K

T

I

V

L

V

V

A

V

I

T

T

S

H

H

D

S

R

Q

Y

D

F

F

L

L

D

N

N

N

A

V

A

C

G

T

W

N

I

I

L

I

E

D

L

L

-

T

D

S

R

K

G

K

E

Q

G

L

I

V

P

Y

W

Y

E

G

G

G

N

N

Y

F

S

D

S

I

W

Y

L

M

E

R

Q

T

K

K

D

E

A

E

R

N

L

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Q

N

E

Q

S

M

A

K

A

A

E

Y

S

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A

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R

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Q

Q

K

E

T

E

I

I

A

A

K

H

E

I

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K

E

K

W

F

V

I

R

A

Q

S

G

A

A

G

K

T

G

Y

-

A

-

N

-

L

-

V

R

R

Q

Q

S

A

K

K

G

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K

K

A

Q

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I

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-

K

-

M

-

E

-

A

A

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F

E

E

T

F

N

D

E

E

L

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F

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P

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P

P

P

R

-

L

-

G

-

D

-

K

-

V

I

I

I

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A

V

F

N

N

N

D

L

V

T

A

K

F

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Y

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G

-

N

-

L

D

D

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A

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I

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G

G

A

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N

N

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A

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S

T

T

L

L

F

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N

M

L

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I

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I

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I

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A

A

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Q

Q

F

-

R

-

D

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S

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M

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A

N

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Y

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Y

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E

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R

-

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Q

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G

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F

F

N

G

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I

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G

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L

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S

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R

V

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V

L

F

A

A

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A

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L

L

A

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L

A

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Q

G

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H

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I

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D

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E

P

P

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N

D

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L

I

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D

A

A

L

L

E

A

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K

A

A

I

I

L

N

E

V

F

W

P

T

G

G

C

G

A

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V

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H

D

D

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R

F

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K

F

L

Sites not aligning to the query:

50 modified: Phosphoserine
53 modified: Phosphoserine
54 modified: Phosphothreonine
55 modified: Phosphoserine
64 modified: Phosphoserine

6ha8V 50S ribosomal protein L1 (see paper)
29% identity, 90% coverage: 21:518/555 of query aligns to 18:479/541 of 6ha8V

query
sites
6ha8V

I

V

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G

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N
|
N

G
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G

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x
A

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G

K
|
K

S
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S

T
|
T

L

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M

-

A

-

G

-

I

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D

-

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-

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-

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I

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N

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A

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P

M

A

P

Q

G

G

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-

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A

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I

I

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A

A

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E

A

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T

A

A

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-

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-

E

-

V

-

Y

-

A

-

A

A

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A

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P

A

D

D

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-

D

-

F

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D

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-

A

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-

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-

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Q

G

T

E
x
P

L

A

E

E

A

-

I

-

Q

-

A

-

Q

-

D

-

A

-

H

-

N

-

L

-

D

K

N
x
K

I

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L

L

E
|
E

R
x
K

A

W

A

H

N

V

A

P

L

L

R

R

L

-

P

-

D

D

W

F

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x
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S

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|
G

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x
H

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G

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N

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A

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L

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E

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D

G

Q

E

T

G

L

I

I

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E

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F

E
x
K

G

G

N

N

Y

Y

S

S

S

G

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Y

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-

F

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D
x
K

A

K

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x
T

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-
x
R

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Y

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E

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A

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x
Q

-

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A
x
W

A

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E

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x
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A

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x
H

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A

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S

I
x
T

A

K

K

K

E

E

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x
G

-
x
F

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x
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E
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E

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x
Y

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R

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G
x
K

A

A

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|
K

G
x
R

R

T

Q
x
D

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A

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Q

G

I

K

K

A
x
S

R
x
K

M

Q

A
x
K

R
|
R

F

L

E

E

-
x
K

-

E

-

L

-

E

-

K

-

A

-

K

-

A

E

E

L

P

N

V

T

T

N

P

D

E

Y

Y

Q

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K

V

R

R

N

-

E

-

T

-

N

-

E

-

L

F

F

S

I

I

P

D

P

T

G

T

P

H

R
x
K

L

T

G
|
G

D

K

K
x
R

V

F

I

L

E

E

V

V

N

Q

N

N

L

V

T

T

K

K

S

A

Y
x
F

G

G

D

E

R
|
R

V

T

L

L

I

F

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K

N

N

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A

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F

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Q

K

H

G

G

A

E

I

K

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G

A

I

I

G

G

A

P

N
|
N

G
|
G

A
x
S

G
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G

K
|
K

S
x
T

T
|
T

L

L

F

L

R

N

M

I

L

I

S

L

G

G

S

Q

E

E

Q

T

P

A

D

E

-

G

-

S

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V

-
x
W

-

V

S
|
S

G

P

S
|
S

I

A

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N

L

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G

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Q
|
Q

L

E

A

V

-

F

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L

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P

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L

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E

Q

Q

F

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D

E

S

E

M

L

N

F

D

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-

N

N

T

E

I

T

W

F

Q

K

E

A

I
x
R

S

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G
x
H

G

V

Q

Q

D
x
N

I
x
L

M

M

R

R

I

-

N

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M

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E

-

I

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P

-

S

-

R

-

A

-

Y

-

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x
H

F

L

N

G

F

F

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T

G

A

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x
Q

Q

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Q

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K
x
E

I

P

I

I

G

K

T

H

L
x
M

S
|
S

G

M

G
|
G

E

E

R

R

N

V

R

K

V

I

H

K

L

L

A

M

K

A

L

Y

L

I

Q

L

A

E

G

E

G

K

N

D

V

V

L

L

L

I

L

L

D

D

E

Q

P

P

T

T

N

N

D

H

L

L

D

D

V

L

E

P

T

S

L

R

R

E

A

Q

L

L

E

E

A

T

I

L

L

S

E

Q

F

Y

P

S

G

G

C

T

A

L

M

L

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A

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S

H
|
H

D

D

R

R

W

Y

F

F

L

L

D

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K

I

T

A

T

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N

H

S

I

K

L

L

D

V

Y

I

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D

N

E

N

G

G

binding adenosine-5'-triphosphate: N38 (= N41), G39 (= G42), A40 (≠ S43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (= T47), Q102 (≠ E158), S104 (= S164), G105 (= G165), G106 (= G166), F300 (≠ Y333), R303 (= R336), N325 (= N358), G326 (= G359), S327 (≠ A360), G328 (= G361), K329 (= K362), T330 (≠ S363), T331 (= T364), Q359 (= Q387), Q398 (≠ D437), E401 (≠ K440), M406 (≠ L445), S407 (= S446), G409 (= G448), H460 (= H499)
binding : P84 (≠ E127), K88 (≠ N142), E91 (= E145), K92 (≠ R146), H147 (≠ E207), K181 (≠ E241), K193 (≠ D252), T197 (≠ K256), R200 (vs. gap), Q215 (vs. gap), W222 (≠ A260), K225 (≠ S263), A226 (= A264), H227 (≠ R265), T231 (≠ I269), G235 (vs. gap), F236 (vs. gap), K237 (≠ L273), E238 (= E274), Y239 (≠ W275), R241 (= R277), K243 (≠ G279), K245 (= K281), R246 (≠ G282), D248 (≠ Q284), S253 (≠ A289), K254 (≠ R290), K256 (≠ A292), R257 (= R293), K260 (vs. gap), K285 (≠ R318), G287 (= G320), R289 (≠ K322), W347 (vs. gap), S349 (= S377), S351 (= S379), R382 (≠ I408), H384 (≠ G410), N387 (≠ D413), L388 (≠ I414), H391 (≠ R430)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 13
binding : 1, 2

Q9USH9 Uncharacterized ABC transporter ATP-binding protein C825.01 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 93% coverage: 19:535/555 of query aligns to 288:802/822 of Q9USH9

query
sites
Q9USH9

K

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N

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G

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K

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K

Sites not aligning to the query:

27 modified: Phosphoserine
47 modified: Phosphoserine
51 modified: Phosphoserine
55 modified: Phosphoserine
57 modified: Phosphotyrosine
97 modified: Phosphoserine
137 modified: Phosphoserine
163 modified: Phosphoserine

6r84A Protein VMS1,Vms1,Protein VMS1,Vms1 (see paper)
31% identity, 64% coverage: 158:512/555 of query aligns to 76:426/446 of 6r84A

query
sites
6r84A

E

K

K

K

I

T

E

K

V

D

L

M

S

S

G

G

E

W

R

K

R

M

R

R

V

V

A

A

I

L

C

A

R

K

L

A

L

L

L

F

E

V

K

K

P

P

E

T

M

L

L

L

D

D

E

D

P

P

T

T

N

A

H

H

L

L

D

D

A

L

E

E

S

A

V

C

A

V

W

W

L

L

E

E

H

E

F

Y

L

L

Q

K

E

R

Y

F

A

D

G

R

T

T

V

L

V

V

A

L

I

V

T

S

H

H

D

S

R

Q

Y

D

F

F

L

L

D

N

N

G

A

V

A

C

G

T

W

N

I

M

L

I

E

D

L

M

D

R

R

A

G

Q

E

K

G

L

I

T

P

A

W

Y

E

G

G

G

N

N

Y

Y

S

D

S

S

W

Y

L

H

E

-

Q

-

K

-

D

-

A

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R

-

L

-

K

K

Q

T

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R

S

S

A

E

A

L

E

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S

T

A

N

R

Q

Q

M

K
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K

T

Q

I

Y

A

N

K

K

E

Q

L

Q

E
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E

W
x
E

V

I

R

Q

Q

H

G

I

A

K

K

K

G
x
F

R

I

Q

A

S

S

K

A

G

G

K
x
T

-
x
Y

A
|
A

R
x
N

M

L

A
x
V

R
x
K

F
x
Q

E

A

E

K

L
x
S

N
x
R

T

Q

N

K

D

I

Y

L

Q

D

K
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K

R

M

N

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E

A

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G

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L

F

F

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P

P

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D

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K

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K

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A

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L

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G

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N

N

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G

A

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G

G

K

K

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L

F

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K

M

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L

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P

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G

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I

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V

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K

L

L

A

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V

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Q

F

H

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D

Q

S

D

M

Q

N

L

D

D

K

L

N

T

T

-

I

-

W

-

Q

-

E

-

I

-

S

K

G

S

G

A

Q

L

D

E

I

F

M

V

R

R

I

D

N

K

N

Y

M

S

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N

I

I

P

S

S

Q

-

D

-

F

-

Q

-

F

-

W

R

R

A

G

Y

Q

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L

G

G

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F

Y

N

G

F

L

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T

G

G

G

E

D

G

Q

Q

Q

T

K

V

I

Q

I

M

G

A

T

T

L

L

S

S

G

E

G

G

E

Q

R

R

N

S

R

R

V

V

H

V

L

F

A

A

K

L

L

L

L

A

Q

L

A

E

G

Q

G

P

N

N

V

V

L

L

D

D

E

E

P

P

T

T

N

N

D

G

L

L

D

D

V

I

E

P

T

T

L

I

R

D

A

S

L

L

E

A

E

D

A

A

I

I

L

N

E

E

F

F

P

N

G

G

C

G

A

V

M

V

V

V

I

V

S

S

H

H

D

D

R

F

W

R

F

L

L

L

D

D

R

K

I

I

A

A

T

Q

H

D

I

I

L

F

binding : K178 (= K267), E185 (= E274), E186 (≠ W275), F193 (≠ G282), T199 (≠ K288), Y200 (vs. gap), A201 (= A289), N202 (≠ R290), V204 (≠ A292), K205 (≠ R293), Q206 (≠ F294), S209 (≠ L297), R210 (≠ N298), K216 (= K304)

7p486 ABC-F type ribosomal protection protein (see paper)
25% identity, 88% coverage: 19:507/555 of query aligns to 15:463/510 of 7p486

query
sites
7p486

K

K

Q

Q

I

L

L

I

K

K

D

R

I

L

S

S

L

F

S
x
H

F

I

F

E

P

D

G

H

A

E

K

H

I

L

G

A

V

L

L

I

G

G

L

V

N
|
N

G
|
G

S

I

G
|
G

K
|
K

S
|
S

T

T

L

L

R

H

I

-

M

-

A

-

G

-

I

-

D

-

T

-

E

-

I

-

E

-

G

-

E

-

A

-

R

-

P

-

M

-

P

-

G

-

L

-

K

-

I

-

G

-

Y

-

L

-

P

-

Q

-

E

-

P

-

K

H

L

I

D

H

P

K

N

N

Q

E

T

L

V

I

R

D

E

T

A

A

I

M

E

M

E

E

A
x
Q

V

D

S

L

E

S

A

K

K

H

N

D

A

D

L

I

K

D

R

V

L

M

D

D

E

Y

V

V

Y

M

A

S

A

A

Y

Y

A

I

E

-

P

-

D

-

A

-

D

-

F

-

D

-

A

-

L

-

A

-

K

-

E

-

Q

-

G

-

E

-

L

-

E

-

A

-

I

-

Q

-

A

-

Q

-

D

-

A

-

H

-

N

-

L

-

D

-

N

-

I

I

L

I

E

E

R

G

A

N

A

K

N

L

A

G

L

L

R

S

L

S

P

T

D

H

W

F

D

E

E

Q

K

K

I

I

E

G

V
x
T

L

L

S
|
S

G

G

G
|
G

E
|
E

R

Q

R

T

R

K

V

V

A

S

I

F

C

L

R

K

L

V

L

I

L

L

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S

K

D

P

A

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M

L

L

L

L

I

D

D

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Q

P

P

T

T

N

N

H

H

L

M

D

D

A

K

E

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M

V

K

A

V

W

W

L

L

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K

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A

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F

Q

K

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Y

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A

Q

G

R

T

A

V

I

V

L

A

F

I

V

T

S

H

H

D

D

R

R

Y

E

F

F

L

L

D

N

N

E

A

T

A

P

G

D

W

A

I

I

L

L

E

E

L

L

D

T

R

K

G

D

E

G

G

A

I

T

P

R

W

Y

E

S

G

G

N

H

Y

Y

S

D

W

Y

L

K

E

N

Q
|
Q

K

K

D

D

A

I

-

E

-

I

-

E

-
x
T

-

E

-

K

-

L

R

K

L

Y

K

E

Q
x
K

E

E

S

Q

A

K

A

E

E

Q

S

K

A

A

R

I

Q

E

K

E

T

S

I

I

A
x
K

K

K

E
x
Y

L

K

E

E

W
|
W

V
x
Y

R

Q

-

R

-

A

Q

Q

G

K

A

A

K
x
S

G

V

R
|
R

Q

S

S
x
P

K
x
Y

G

A

K
x
Q

A
x
K

R
x
Q

M

L

A
x
S

R
x
K

F

L

-

A

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x
K

-
x
R

-

F

-

K

-

S

-

K

-

E

E
x
H

E

Q

L

L

N

N

T
x
R

N

K

D

L

Y

E

Q

E

K

S

R

K

N

S

-

D

-

N

-

P

-

L

E

E

T

E

N

N

E

K

L

S

F
|
F

-
x
S

I

I

P

E

P

N

G

N

P

E

R

F

L

K

G

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D
x
H

K

Y

V

L

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V

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F

N

E

N

N

L

V

T

S

K

F

S

S

Y
|
Y

G

K

D

S

R

R

V

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L

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F

D

K

N

D

L

T

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Y

F

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P

K

K

R

G

N

A

Q

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T

V

V

G

I

I

I

I

E

G

G

A

K

N
|
N

G
|
G

A

S

G
|
G

K
|
K

S
|
S

T
|
T

L

L

F

I

R

Q

M

L

L

I

S

L

G

G

S

N

E

L

Q

L

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x
K

L

K

G

H

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T

D

V

L

Q

D

L

I

A

G

S

Y

V

F

E

S

Q
|
Q

F

D

R

F

D

Q

S

N

M

L

N

N

D

P

K

N

N

N

T

S

I

V

W

L

Q

E

E

E

I

-

S

-

G

-

Q

-

D

-

I

V

M

M

R

D

I

I

N

E

N

N

M

M

E

M

I

I

P
x
T

-

D

S

A

R
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R

A
x
T

Y

I

V

L

G
x
A

R
x
S

F

F

N

Y

F

F

R

D

G

K

G

S

D

R

Q

M

Q

N

K

D

I

K

I

V

G

R

T
x
Q

L

L

S
|
S

G
x
M

G
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G

E

E

R

K

N

C

R

R

V

L

H

Q

L

F

A

V

K

K

L

L

L

Y

Q

F

A

S

G

N

G

P

N

H

V

I

L

L

L

I

L

L

D

D

E

Q

P

P

T

T

N

N

D

Y

L

F

D

D

V

I

E

S

T

M

L

Q

R

E

A

K

L

I

E

I

E

Q

A

L

I

I

L

Q

E

S

F

F

P

N

G

G

C

A

A

V

M

I

V

I

I

V

S

S

H

H

D

D

R

E

W

I

F

F

L

K

D

D

R

E

I

I

binding adenosine-5'-triphosphate: N37 (= N41), G38 (= G42), G40 (= G44), K41 (= K45), S42 (= S46), T100 (≠ V162), S102 (= S164), G104 (= G166), E105 (= E167), Y294 (= Y333), N319 (= N358), G320 (= G359), G322 (= G361), K323 (= K362), S324 (= S363), T325 (= T364), Q354 (= Q393), Q400 (≠ T444), S402 (= S446), M403 (≠ G447), G404 (= G448)
binding magnesium ion: S42 (= S46), Q61 (≠ A93), S324 (= S363), Q354 (= Q393)
binding : H24 (≠ S28), Q188 (= Q250), T195 (vs. gap), K202 (≠ Q257), K215 (≠ A270), Y217 (≠ E272), W220 (= W275), Y221 (≠ V276), S229 (≠ K281), R231 (= R283), P233 (≠ S285), Y234 (≠ K286), Q236 (≠ K288), K237 (≠ A289), Q238 (≠ R290), S240 (≠ A292), K241 (≠ R293), K244 (vs. gap), R245 (vs. gap), H251 (≠ E295), R255 (≠ T299), F272 (= F312), S273 (vs. gap), H282 (≠ D321), K342 (≠ E381), T378 (≠ P423), R381 (= R425), T382 (≠ A426), A385 (≠ G429), S386 (≠ R430)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 12, 13

7nhl0 50S ribosomal protein L32 (see paper)
30% identity, 66% coverage: 164:527/555 of query aligns to 80:465/465 of 7nhl0

query
sites
7nhl0

S
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S

G
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G

G

G

E
|
E

R

V

R

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R

R

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N

A

Y

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A

L

L

L

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N

P

P

E

E

M

L

L

L

L

A

D

D

E

Q

P

P

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N

T

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N

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A

N

E
x
N

S

Y

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I

A

E

W
x
K

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L

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D

L

L

Q

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E
x
N

Y

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x
H

G

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V

I

A

I

I

V

T

S

H

H

D

D

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A

F

F

L

L

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D

N

N

A

L

A

C

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I

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E

L

I

D

D

R

E

G

G

E

R

G

I

I

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W

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E

K

G

G

N

N

Y

Y

S

S

S

N

W

Y

L

V

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E

Q

Q

K

K

D

E

A

L

R

E

L

R

K

H

-
x
R

-

E

-

L

-

E

-

Y

-

E

-
x
K

-

Y

-

E

-

K

-

E

-

K

-
x
R

-

L

-

E

-

K

-

A

-

I

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N

-

I

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K

A

A

E

Q

S
x
R

A
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A

R

T

Q
x
K

K

K

-

P

-
x
K

-

N

-

L

-
x
S

-

S

-
x
S

-
x
E

-

G

T
x
K

I

I

A
x
K

K
x
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x
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x
F

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x
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x
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x
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K

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Q
x
R

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x
K

K

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A
x
S

R

L

M

E

A
x
T

R
|
R

F

L

E

E

E

K

L

L

N

E

T

R

N

-

D

-

Y

V

Q

E

K

K

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N
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N

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-

N

-

E

-

L

-

F

-

I

L

P

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L

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L
x
D

G

L

D

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K

N

V

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N

L
x
R

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T

K

I

S

I

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G

G

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E

-

D

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S

-

G

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T

-
x
I

-

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-

G

R
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R

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L

I

W

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K

N

A

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K

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F

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K

G

G

G

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D

I

K

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G

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N

G
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G

A
x
T

G
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G

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K

S
x
T

T

T

L

F

F

I

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K

M

K

L

I

S

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H

S

G

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S

N

G

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S

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Q

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I

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Q

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M

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-

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-

N

Q

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x
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R

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x
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x
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x
V

L

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S

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G

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E

R

R

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V

R

K

V

V

H

A

L

L

A

T

K

K

L

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F

Q

L

A

S

G

E

G

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N

N

V

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L

L

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Q

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P

T

T

N

N

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F

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A

L

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R

E

A

A

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N

G

G

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S

H

H

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D

R

R

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F

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Y

binding adenosine-5'-triphosphate: S80 (= S164), G81 (= G165), E83 (= E167), I281 (vs. gap), R284 (= R336), L286 (= L338), N306 (= N358), G307 (= G359), T308 (≠ A360), G309 (= G361), K310 (= K362), T311 (≠ S363), K379 (= K440), V383 (≠ T444), S385 (= S446), G387 (= G448), E388 (= E449)
binding magnesium ion: T311 (≠ S363), Q337 (= Q393)
binding : N112 (≠ E196), K116 (≠ W200), N123 (≠ E207), H125 (≠ A209), R173 (vs. gap), K180 (vs. gap), R187 (vs. gap), R201 (≠ S263), A202 (= A264), K204 (≠ Q266), K207 (vs. gap), S210 (vs. gap), S212 (vs. gap), E213 (vs. gap), K215 (≠ T268), K217 (≠ A270), V218 (≠ K271), T219 (≠ E272), Y222 (≠ W275), F223 (≠ V276), A224 (≠ R277), S225 (≠ Q278), K226 (≠ G279), K228 (= K281), R231 (≠ Q284), K232 (≠ S285), S236 (≠ A289), T239 (≠ A292), R240 (= R293), N251 (= N306), D259 (≠ L319), N268 (= N328), R269 (≠ L329), E360 (= E421), T361 (≠ I422), L362 (≠ P423), R364 (= R425), T365 (≠ A426), A368 (≠ G429), R369 (= R430), R374 (≠ G435)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 13, 16, 38, 39, 41, 42, 43, 44, 78
binding magnesium ion: 43, 71
binding : 2, 23, 25, 27

Query Sequence

>202575 FitnessBrowser__MR1:202575
MAQFVYSMLRVGKVVPPKKQILKDISLSFFPGAKIGVLGLNGSGKSTLLRIMAGIDTEIE
GEARPMPGLKIGYLPQEPKLDPNQTVREAIEEAVSEAKNALKRLDEVYAAYAEPDADFDA
LAKEQGELEAIIQAQDAHNLDNILERAANALRLPDWDEKIEVLSGGERRRVAICRLLLEK
PEMLLLDEPTNHLDAESVAWLEHFLQEYAGTVVAITHDRYFLDNAAGWILELDRGEGIPW
EGNYSSWLEQKDARLKQESAAESARQKTIAKELEWVRQGAKGRQSKGKARMARFEELNTN
DYQKRNETNELFIPPGPRLGDKVIEVNNLTKSYGDRVLIDNLSFSVPKGAIVGIIGANGA
GKSTLFRMLSGSEQPDSGSIELGETVQLASVEQFRDSMNDKNTIWQEISGGQDIMRINNM
EIPSRAYVGRFNFRGGDQQKIIGTLSGGERNRVHLAKLLQAGGNVLLLDEPTNDLDVETL
RALEEAILEFPGCAMVISHDRWFLDRIATHILDYRDEGQVNFYEGNYTEYSAWLKNTYGA
DVVEPHRLKYKRMTK

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