SitesBLAST

Q9NRK6 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein; Mitochondrial ATP-binding cassette 2; M-ABC2; EC 7.6.2.- from Homo sapiens (Human) (see 7 papers)
37% identity, 94% coverage: 31:586/592 of query aligns to 170:733/738 of Q9NRK6

query
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Q9NRK6

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C215 (≠ L76) mutation to S: Does not affect ATPase activity; when associated with L-224 and G-582. Activated by Zn (II) mesoporphyrin; when associated with L-224 and G-582.
C224 (≠ V81) mutation to L: Does not affect ATPase activity; when associated with S-215 and G-582. Activated by Zn (II) mesoporphyrin; when associated with S-215 and G-582.
N229 (≠ T86) mutation to A: Does not affect ATPase activity in the absence or presence of biliverdin. No increased ATPase activity in the presence of biliverdin; when associated with A-398. Increased ATPase activity in the absence of biliverdin compared to WT; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-398 and A-407.
F398 (≠ M255) mutation to A: No increased ATPase activity in the presence of biliverdin. No increased ATPase activity in the presence of biliverdin; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-229 and A-407.
T402 (= T256) binding biliverdin IXalpha
N407 (≠ G261) mutation to A: Increased ATPase activity in the absence of biliverdin compared to WT. No increased ATPase activity in the presence of biliverdin. Increased ATPase activity in the absence of biliverdin compared to WT; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-398. No increased ATPase activity in the presence of biliverdin; when associated with A-229 and A-398.
R471 (≠ A328) to T: in a breast cancer sample; somatic mutation
K533 (= K390) mutation to E: Increases hemoglobin biosynthetic process.
S534 (= S391) binding Mg(2+)
D545 (= D402) to N: in dbSNP:rs35698797
C582 (≠ A439) mutation to G: Does not affect ATPase activity; when associated with S-215 and L-224. Activated by Zn (II) mesoporphyrin; when associated with S-215 and L-224.
S635 (= S489) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
Q638 (= Q492) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
D658 (= D512) binding Mg(2+); mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
E659 (= E513) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.

Sites not aligning to the query:

150 A → S: in dbSNP:rs4148756

4ayxA Structure of the human mitochondrial abc transporter, abcb10 (rod form b) (see paper)
37% identity, 92% coverage: 28:572/592 of query aligns to 12:565/571 of 4ayxA

query
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4ayxA

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binding phosphomethylphosphonic acid adenylate ester: Y348 (= Y358), S376 (= S386), G377 (= G387), G379 (= G389), K380 (= K390), S381 (= S391), T382 (= T392)
binding glycine: R17 (vs. gap), Y81 (= Y91)
binding magnesium ion: S381 (= S391), Q422 (= Q432)

Q9NUT2 Mitochondrial potassium channel ATP-binding subunit; ATP-binding cassette sub-family B member 8, mitochondrial; ABCB8; Mitochondrial ATP-binding cassette 1; M-ABC1; Mitochondrial sulfonylurea-receptor; MITOSUR from Homo sapiens (Human) (see 4 papers)
38% identity, 87% coverage: 74:589/592 of query aligns to 197:713/735 of Q9NUT2

query
sites
Q9NUT2

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V

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M

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K

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|
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x
Q

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|
G

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x
G

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|
G

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|
K

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x
T

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D

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A

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Y

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A

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N

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F

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G

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L

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G

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E

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G

G

A

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L

L

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S

G

G

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Q

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K

Q

Q

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I

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A

A

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I

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R

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V

V

V

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Q

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A

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D

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A

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A

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I

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V

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L

L

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V

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A

G

A

A

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I

I

I

V

V

V

M

M

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A

Q

D

G

G

R

R

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V

W

E

E

Q
x
A

G

G

D

T

H

H

A

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T

E

L

L

S

L

A

K

Q

K

G

G

L

L

Y

Y

A

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E

L

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R

L

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Q

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D

507:514 (vs. 384:391, 63% identical) binding ATP
GK 512:513 (= GK 389:390) mutation to AR: Renders the protein unstable.
K513 (= K390) mutation to A: Abolish binding to ATP.
A690 (≠ Q566) to G: in a breast cancer sample; somatic mutation

Sites not aligning to the query:

152 V → I: in dbSNP:rs4148844
165 I → T: in a breast cancer sample; somatic mutation

Q9JI39 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein; EC 7.6.2.- from Mus musculus (Mouse) (see 2 papers)
35% identity, 96% coverage: 21:586/592 of query aligns to 122:698/715 of Q9JI39

query
sites
Q9JI39

I

V

W

W

R

K

F

L

-

L

-

G

-

L

A

V

R

R

R

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Y

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G

G

R

R

I

L

A

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A

A

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A

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L

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Y

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V

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A

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|
G

K
|
K

S

S

T

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V

L

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L

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C

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N

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Y

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W

-

D

-

A

A

D

D

D

N

-

L

-

S

-

V

-

T

-

A

D

Q

A

Q

I

V

W

E

A

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A

A

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E

A

V

A

A

N

N

A

A

S

E

F

F

L

I

R

R

A

S

L

F

P

P

D

Q

G

G

L

F

D

D

S

T

F

V

L

V

G

G

E

E

A

K

G

G

A

I

R

L

L

L

S

S

G

G

G
|
G

Q

Q

R

K

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

L

L

L

R

K

D

N

A

P

P

K

L

I

L

L

D

D

E
|
E

A

A

T

T

S

S

A

A

L

L

D

D

A

A

E

E

S

N

E

E

R

H

L

L

V

V

Q

Q

D

E

A

A

L

L

D

D

R

R

L

L

M

M

K

E

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G

R

R

T

T

T

V

I

L

V

I

I

I

A

A

H

H

R

R

L

L

A

S

T

T

V

I

R

K

A

N

A

A

D

N

R

F

I

V

I

A

V

V

M

L

D

D

Q

H

G

G

R

K

I

I

V
x
C

E

E

Q

H

G

G

D

T

H

H

A

E

T

E

L

L

S

L

A

L

Q

K

-

P

G

N

G

G

L

L

Y

Y

A

R

R

K

L

L

A

M

R

N

L

K

Q

Q

G497 (= G389) mutation to A: Decreases ATP binding about 50%.
K498 (= K390) mutation to R: Decreases ATP binding about 50%.
C547 (≠ A439) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
G602 (= G491) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
E624 (= E513) mutation to Q: Affects ATP hydrolysis but not binding.
C675 (≠ V564) mutation to A: Prevents ABCB10 glutathionylation.

Sites not aligning to the query:

1:82 modified: transit peptide, Mitochondrion

7y48B Cryo-em structure of biliverdin-bound mitochondrial abc transporter abcb10 from biortus (see paper)
36% identity, 92% coverage: 28:572/592 of query aligns to 11:561/567 of 7y48B

query
sites
7y48B

Y

Y

P

P

G

E

R

R

-

R

I

L

A

A

L

V

A

G

A

F

L

L

V

T

V

M

A

S

C

V

A

I

T

S

L

M

A

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A

P

P

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F

F

L

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G

L

K

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I

I

I

D

D

K

V

G

I

F

Y

I

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A

N

S

P

G

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G

V

D

D

V

Y

G

S

P

D

Y

N

F

L

H

T

Y

R

L

L

L

C

L

L

-

G

-

L

-

S

-

A

I

V

V

F

L

L

V

C

L

G

S

A

L

A

A

A

T

N

A

A

T

I

R

R

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V

Y

Y

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M

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W

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G

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V

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S

L

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L

L

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L

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F

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D

E

K

N

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G

E

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L

A

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A

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D

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A

A

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L

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T

N

V

L

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S

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D

A

G

L

L

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R

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A

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G

V

A

L

Q

A

A

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G

V

G

G

I

I

I

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Y

M

L

M

F

F

A

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P

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L

L

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A

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M

F

L

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I

V

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P

V

P

V
|
V

M

S

L

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I

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L

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Y

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G

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R

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Y

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M

F

-

F

-

G

-

A

T
|
T

A

G

I

L

I

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I
x
G

G

N

L

L

I
|
I

F

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G

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-

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V

T

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V

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W

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V

G

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L

binding Biliverdine IX Alpha: V171 (= V182), T248 (= T256), G252 (≠ I260), I255 (= I263)

4aywA Structure of the human mitochondrial abc transporter, abcb10 (plate form) (see paper)
36% identity, 92% coverage: 28:569/592 of query aligns to 12:558/560 of 4aywA

query
sites
4aywA

Y

Y

P

P

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E

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R

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x
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I

L

A

A

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H

H

binding phosphoaminophosphonic acid-adenylate ester: Y348 (= Y358), S376 (= S386), G377 (= G387), G379 (= G389), K380 (= K390), S381 (= S391), T382 (= T392)
binding cholesterol hemisuccinate: R17 (vs. gap), A77 (= A87), Y81 (= Y91)

7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
35% identity, 94% coverage: 32:586/592 of query aligns to 17:570/572 of 7v5cA

query
sites
7v5cA

I

L

A

V

A

A

L

S

A

F

L

L

V

I

V

V

A

A

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E

A

A

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S

A

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D

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A

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binding adenosine-5'-diphosphate: Y342 (= Y358), T344 (= T360), S372 (≠ A388), K374 (= K390), S375 (= S391), S376 (≠ T392), S473 (= S489), Q476 (= Q492)
binding beryllium trifluoride ion: S370 (= S386), K374 (= K390), Q416 (= Q432), H528 (= H544)
binding magnesium ion: S375 (= S391), Q416 (= Q432)

7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
35% identity, 94% coverage: 32:586/592 of query aligns to 16:569/570 of 7vfiA

query
sites
7vfiA

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binding cholesterol hemisuccinate: E30 (≠ T46), I41 (= I57), R137 (= R152), I274 (≠ A289), F281 (≠ G296)
binding : Q130 (≠ T145), Y237 (≠ I259)

Q9NP78 ABC-type oligopeptide transporter ABCB9; ATP-binding cassette sub-family B member 9; ATP-binding cassette transporter 9; ABC transporter 9 protein; hABCB9; TAP-like protein; TAPL; EC 7.4.2.6 from Homo sapiens (Human) (see 4 papers)
36% identity, 82% coverage: 104:586/592 of query aligns to 261:741/766 of Q9NP78

query
sites
Q9NP78

I

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K545 (= K390) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
H699 (= H544) mutation to A: Loss of peptide transport activity; whena ssociated with A-545.

Sites not aligning to the query:

17 Intramolecular salt bridge with Arg-57. Essential for the release from the ER; D→N: Loss of lysosomal localization. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect dimerization. Does not affect peptide transport activity. Decreases interaction with YIF1B.; D→R: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-100.
45 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-49. Loss of lysosomal localization; when assosiated with K-49 and D-100. Does not affect peptide transport activity; when assosiated with K-49 and D-100.; D→N: Decreases lysosomal localization; when associated with N-49.
49 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-45. Loss of lysosomal localization; when assosiated with K-45 and D-100. Does not affect peptide transport activity; when assosiated with K-45 and D-100.; D→N: Decreases lysosomal localization; when associated with N-45.
57 Intramolecular salt bridge with Asp-17. Essential for the release from the ER; R→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-100.; R→D: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with R-17. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
100 K→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-57.; K→D: Decreases lysosomal localization. Loss of lysosomal localization; when assosiated with R-17. Loss of lysosomal localization; when assosiated with K-45 and K-49. Does not affect peptide transport activity; when assosiated with K-45 and K-49. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
121 V → M: in dbSNP:rs3803002
136:137 LL→AA: No effect on lysosomal localization.

7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
38% identity, 87% coverage: 74:586/592 of query aligns to 61:562/563 of 7ehlA

query
sites
7ehlA

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Q

binding phosphoaminophosphonic acid-adenylate ester: Y334 (= Y358), G365 (= G389), K366 (= K390), T367 (≠ S391), T368 (= T392)
binding cholesterol: R139 (= R152), L157 (= L171), L168 (≠ V182), G172 (≠ V186), G260 (= G274), L273 (≠ I288), F276 (= F291), Q284 (≠ A299), R285 (≠ G300)

Q0WML0 ABC transporter B family member 27; ABC transporter ABCB.27; AtABCB27; Aluminum tolerance-related ATP-binding cassette transporter; Antigen peptide transporter-like 2; Transporter associated with antigen processing-like protein 2; AtTAP2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 86% coverage: 83:592/592 of query aligns to 131:640/644 of Q0WML0

query
sites
Q0WML0

S

S

L

I

A

C

T

T

A

A

T

L

R

R

F

A

Y

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E261 (= E213) mutation to K: In als1-1; loss of aluminum tolerance.

5ochC The crystal structure of human abcb8 in an outward-facing state
37% identity, 88% coverage: 74:591/592 of query aligns to 51:534/537 of 5ochC

query
sites
5ochC

Y

H

L

L

L

I

I

L

V

Y

L

G

V

V

L

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S

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|
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R

A

G

R

Q

I

V

-

V

A

G

V

F

V

I

P

S

Q

Q

E

E

T

P

V

V

L

L

F

F

G

G

A

T

S

T

A

I

R

M

D

E

N

N

L

I

R

R

Y

F

G

G

R

K

W

L

D

E

A

A

D

S

D

D

D

E

A

E

I

V

W

Y

A

T

A

A

E

R

A

E

A

A

N

N

A

A

A

H

S

E

F

F

L

I

R

T

A

S

L

F

P

P

D

E

G

G

L

Y

D

N

S

T

F

V

L

V

G

G

E

E

A

R

G

G

A

T

R

T

L

L

S

S

G

G

Q

Q

R

K

Q

Q

R

R

I

L

A

A

I

I

A

A

R

R

A

A

I

L

L

I

R

K

D

Q

A

P

P

T

L

V

L

L

L

I

L

L

D

D

E

E

A

A

T

T

S

S

A

A

L

L

D

D

A

A

E

E

S

S

E

E

R

R

L

V

V

V

Q

Q

D

E

A

A

L

L

D

D

R

R

L

A

M

S

K

A

E

G

R

R

T

T

T

V

I

L

V

V

I

I

A

A

H

H

R

R

L

L

A

S

T

T

V

V

R

R

A

G

A

A

D

H

R

C

I

I

I

V

V

V

M

M

D

A

Q

D

G

G

R

R

I

V

V

W

E

E

Q

A

G

G

D

T

H

H

A

E

T

E

L

L

S

L

A

K

Q

K

G

G

L

L

Y

Y

A

A

R

E

L

L

A

I

R

R

L

R

Q

Q

F

A

N

L

D

D

V

A

A

A

binding adenosine-5'-diphosphate: Y300 (= Y358), C302 (≠ T360), G329 (= G387), G331 (= G389), K332 (= K390), T333 (≠ S391), T334 (= T392)

3wmgA Crystal structure of an inward-facing eukaryotic abc multidrug transporter g277v/a278v/a279v mutant in complex with an cyclic peptide inhibitor, acap (see paper)
38% identity, 83% coverage: 98:586/592 of query aligns to 89:586/589 of 3wmgA

query
sites
3wmgA

E

E

R

R

V

L

V

A

A

R

D

D

I

L

R

R

I

V

A

A

V

A

Q

F

A

S

N

N

L

L

L

V

R

E

L

Q

A

D

P

V

R

T

F

Y

F

F

E

D

E

R

N

R

R

K

P

A

S

G

E

E

I

L

A

G

S

G

R

K

L

L

T

N

A

N

D

D

T

V

A

Q

I

V

I

I

E

-

Q

Q

V

Y

V

S

G

F

T

S

T

K

V

L

S

G

V

A

A

V

L

L

R

F

N

N

I

L

V

A

L

Q

A

C

I

V

G

V

G

G

I

I

Y

V

L

A

F

F

A

I

I

F

A

A

P

P

K

A

L

L

A

T

A

G

M

V

L

L

L

I

L

A

G

L

I

S

P

P

V

L

V

V

M

V

L

L

P

A

V

V

I

V

L

V

M

Q

G

M

R

I

R

E

L

M

R

S

N

G

L

N

S

T

R

K

S

R

T

S

Q

S

D

E

R

A

I

Y

A

A

D

S

V

A

G

G

A

S

T

V

V

A

S

A

E

E

T

V

L

F

R

S

A

N

M

I

K

R

I

T

V

T

Q

K

G

A

F

F

N

E

Q

A

E

E

S

R

R

Y

E

E

A

T

E

Q

R

R

F

Y

G

G

A

S

V

K

V

L

G

D

S

P

S

L

F

Y

D

R

T

L

A

G

R

R

I

Y

R

I

T

S

R

D

A

G

V

L

M

F

T

F

A

G

I

L

I

S

I

M

G

L

L

V

I

I

F

F

G

C

S

V

I

Y

T

A

M

L

V

A

M

L

W

W

Q

W

G

G

A

G

I

Q

D

L

V

I

A

A

N

R

G

G

R

S

L

L

S

N

G

L

G

G

S
x
N

I

L

A

L

A

T

F

A

I

F

L

F

T

S

G

A

G

I

L

L

V

G

A

F

G

M

A

G

F

V

G

G

A

Q

L

A

A

A

E

Q

V

V

Y

W

G

P

D

D

I

V

V

T

R

R

A

G

A

L

G

G

A

A

A

G

R

E

L

L

S

F

E

A

L

M

L

I

T

D

A

R

E

V

A

P

E

Q

I

Y

K

R

A

R

P

P

-

D

P

P

K

G

P

A

I

E

A

V

L

V

P

T

Q

Q

P

P

P

L

-

V

-

L

R

K

G

Q

R

G

L

I

S

V

F

F

D

E

H

N

V

V

G

H

F

F

R

R

Y

Y

P

P

T

T

R

R

P

M

E

N

M

V

L

E

A

V

L

L

D

R

D

G

V

I

S

S

F

L

T

T

V

I

E

P

P

N

G

G

E

K

M

T

V

V

A

A

V

I

V

V

G

G

P

G

S

S

G

G

A

A

G

G

K

K

S

S

T

T

I

I

L

I

Q

Q

L

L

A

L

Q

M

R

R

F

F

Y

Y

D

D

-

I

-

E

P

P

E

Q

S

G

G

G

A

G

I

L

R

L

L

L

-

F

D

D

G

G

I

T

A

P

L

A

P

W

D

N

A

Y

D

D

P

F

A

H

D

A

I

L

R

R

A

S

R

Q

I

I

A

G

V

L

V

V

P

S

Q

Q

E

E

T

P

V

V

L

L

F

F

G

S

A

G

S

T

A

I

R

R

D

D

N

N

L

I

R

L

Y

Y

G

G

R

K

W

R

D

D

A

A

D

T

D

D

D

E

A

E

I

V

W

I

A

Q

A

A

A

L

E

R

A

E

A

A

N

N

A

A

A

Y

S

S

F

F

L

V

R

M

A

A

L

L

P

P

D

D

G

G

L

L

D

D

S

T

F

E

L

V

G

G

E

E

A

R

G

G

A

L

R

A

L

L

S

S

G

G

Q

Q

R

K

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

I

L

L

R

K

D

H

A

P

P

T

L

L

L

C

L

L

D

D

E

E

A

S

T

T

S

S

A

A

L

L

D

D

A

A

E

E

S

S

E

E

R

A

L

L

V

V

Q

Q

D

E

A

A

L

L

D

D

R

R

L

M

M

M

K

A

E

S

R

D

-

G

-

V

T

T

T

S

I

V

V

V

I

I

A

A

H

H

R

R

L

L

A

S

T

T

V

V

R

A

A

R

A

A

D

D

R

L

I

I

I

L

V

V

M

M

D

Q

Q

D

G

G

R

V

I

V

V

V

E

E

Q

Q

G

G

D

N

H

H

A

S

T

E

L

L

S

M

A

A

Q

L

G

G

-

P

-

S

G

G

L

F

Y

Y

A

Y

R

Q

L

L

A

V

R

E

L

K

Q

Q

binding : N277 (≠ S287)

Sites not aligning to the query:

binding decyl-beta-d-maltopyranoside: 6, 13, 13, 18
binding : 43, 61, 62

6a6mA Crystal structure of an outward-open nucleotide-bound state of the eukaryotic abc multidrug transporter cmabcb1 (see paper)
38% identity, 83% coverage: 98:586/592 of query aligns to 90:587/589 of 6a6mA

query
sites
6a6mA

E

E

R

R

V

L

V

A

A

R

D

D

I

L

R

R

I

V

A

A

V

A

Q

F

A

S

N

N

L

L

L

V

R

E

L

Q

A

D

P

V

R

T

F

Y

F

F

E

D

E

R

N

R

R

K

P

A

S

G

E

E

I

L

A

G

S

G

R

K

L

L

T

N

A

N

D

D

T

V

A

Q

I

V

I

I

E

-

Q

Q

V

Y

V

S

G

F

T

S

T

K

V

L

S

G

V

A

A

V

L

L

R

F

N

N

I

L

V

A

L

Q

A

C

I

V

G

V

G

G

I

I

Y

V

L

A

F

F

A

I

I

F

A

A

P

P

K

A

L

L

A

T

A

G

M

V

L

L

L

I

L

A

G

L

I

S

P

P

V

L

V

V

M

V

L

L

P

A

V

G

I

A

L

A

M

Q

G

M

R

I

R

E

L

M

R

S

N

G

L

N

S

T

R

K

S

R

T

S

Q

S

D

E

R

A

I

Y

A

A

D

S

V

A

G

G

A

S

T

V

V

A

S

A

E

E

T

V

L

F

R

S

A

N

M

I

K

R

I

T

V

T

Q

K

G

A

F

F

N

E

Q

A

E

E

S

R

R

Y

E

E

A

T

E

Q

R

R

F

Y

G

G

A

S

V

K

V

L

G

D

S

P

S

L

F

Y

D

R

T

L

A

G

R

R

I

Y

R

I

T

S

R

D

A

G

V

L

M

F

T

F

A

G

I

L

I

S

I

M

G

L

L

V

I

I

F

F

G

C

S

V

I

Y

T

A

M

L

V

A

M

L

W

W

Q

W

G

G

A

G

I

Q

D

L

V

I

A

A

N

R

G

G

R

S

L

L

S

N

G

L

G

G

S

N

I

L

A

L

A

A

F

A

I

F

L

F

T

S

G

A

G

I

L

L

V

G

A

F

G

M

A

G

F

V

G

G

A

Q

L

A

A

A

E

Q

V

V

Y

W

G

P

D

D

I

V

V

T

R

R

A

G

A

L

G

G

A

A

A

G

R

E

L

L

S

F

E

A

L

M

L

I

T

D

A

R

E

V

A

P

E

Q

I

Y

K

R

A

R

P

P

-

D

P

P

K

G

P

A

I

E

A

V

L

V

P

T

Q

Q

P

P

P

L

-

V

-

L

R

K

G

Q

R

G

L

I

S

V

F

F

D

E

H

N

V

V

G

H

F

F

R

R

Y
|
Y

P

P

T

T

R
|
R

P

M

E

N

M

V

L

E

A

V

L

L

D

R

D

G

V

I

S

S

F

L

T

T

V

I

E

P

P

N

G

G

E

K

M

T

V

V

A

A

V

I

V

V

G
|
G

P
x
G

S
|
S

G
|
G

A

A

G
|
G

K
|
K

S
|
S

T
|
T

I

I

L

I

Q

Q

L

L

A

L

Q

M

R

R

F

F

Y

Y

D

D

-

I

-

E

P

P

E

Q

S

G

G

G

A

G

I

L

R

L

L

L

-

F

D

D

G

G

I

T

A

P

L

A

P

W

D

N

A

Y

D

D

P

F

A

H

D

A

I

L

R

R

A

S

R

Q

I

I

A

G

V

L

V

V

P

S

Q
|
Q

E

E

T

P

V

V

L

L

F

F

G

S

A

G

S

T

A

I

R

R

D

D

N

N

L

I

R

L

Y

Y

G

G

R

K

W

R

D

D

A

A

D

T

D

D

D

E

A

E

I

V

W

I

A

Q

A

A

A

L

E

R

A

E

A

A

N

N

A

A

A

Y

S

S

F

F

L

V

R

M

A

A

L

L

P

P

D

D

G

G

L

L

D

D

S

T

F

E

L

V

G

G

E

E

A

R

G

G

A

L

R

A

L

L

S

S

G

G

Q

Q

R

K

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

I

L

L

R

K

D

H

A

P

P

T

L

L

L

C

L

L

D

D

E

E

A

S

T

T

S

S

A

A

L

L

D

D

A

A

E

E

S

S

E

E

R

A

L

L

V

V

Q

Q

D

E

A

A

L

L

D

D

R

R

L

M

M

M

K

A

E

S

R

D

-

G

-

V

T

T

T

S

I

V

V

V

I

I

A

A

H

H

R

R

L
|
L

A

S

T

T

V

V

R

A

A

R

A

A

D

D

R

L

I

I

I

L

V

V

M

M

D
x
Q

Q
x
D

G

G

R

V

I

V

V

V

E

E

Q

Q

G

G

D

N

H

H

A

S

T

E

L

L

S

M

A

A

Q

L

G

G

-

P

-

S

G

G

L
x
F

Y

Y

A

Y

R

Q

L
|
L

A

V

R

E

L

K

Q

Q

binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y358), R355 (= R361), S380 (= S386), G383 (= G389), K384 (= K390), S385 (= S391), T386 (= T392), Q429 (= Q432)
binding decyl-beta-d-maltopyranoside: G378 (= G384), G379 (≠ P385), G381 (= G387), L545 (= L546), Q558 (≠ D559), D559 (≠ Q560), F579 (≠ L578), L583 (= L582)
binding magnesium ion: S385 (= S391), Q429 (= Q432)

7fc9A Crystal structure of cmabcb1 in lipidic mesophase revealed by lcp-sfx (see paper)
38% identity, 82% coverage: 98:582/592 of query aligns to 90:583/584 of 7fc9A

query
sites
7fc9A

E

E

R

R

V

L

V

A

A

R

D

D

I

L

R

R

I

V

A

A

V

A

Q

F

A

S

N

N

L

L

L

V

R

E

L

Q

A

D

P

V

R

T

F

Y

F

F

E

D

E

R

N

R

R

K

P

A

S

G

E
|
E

I

L

A

G

S

G

R

K

L

L

T

N

A

N

D
|
D

T

V

A

Q

I

V

I

I

E

-

Q

Q

V

Y

V

S

G

F

T

S

T

K

V

L

S

G

V

A

A

V

L

L

R

F

N

N

I

L

V

A

L

Q

A

C

I

V

G

V

G

G

I

I

Y

V

L

A

F

F

A

I

I

F

A

A

P

P

K

A

L

L

A

T

A

G

M

V

L

L

L

I

L

A

G

L

I

S

P

P

V

L

V

V

M

V

L

L

P

A

V

G

I

A

L

A

M

Q

G

M

R

I

R

E

L

M

R

S

N

G

L

N

S
x
T

R

K

S

R

T

S

Q
x
S

D
x
E

R

A

I

Y

A

A

D

S

V

A

G

G

A

S

T

V

V

A

S

A

E

E

T

V

L

F

R

S

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binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y358), R355 (= R361), S380 (= S386), G383 (= G389), K384 (= K390), S385 (= S391), T386 (= T392), Q429 (= Q432), H543 (= H544)
binding magnesium ion: D127 (= D135), T188 (≠ S197), S192 (≠ Q201), E312 (≠ R321), S385 (= S391), Q429 (= Q432)
binding zinc ion: E119 (= E127), D127 (= D135), S192 (≠ Q201), E193 (≠ D202), N347 (≠ H353), H349 (≠ G355), H349 (≠ G355), E359 (≠ L365), D451 (= D454), E452 (≠ D455), E510 (= E513), H543 (= H544)

Sites not aligning to the query:

binding zinc ion: 31, 74

O06967 Multidrug resistance ABC transporter ATP-binding/permease protein BmrA; EC 7.6.2.- from Bacillus subtilis (strain 168) (see 2 papers)
35% identity, 94% coverage: 30:588/592 of query aligns to 27:579/589 of O06967

query
sites
O06967

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K380 (= K390) mutation to A: Complete loss of ATPase activity.; mutation to R: Retains 2% ATPase activity; unable to transport Hoechst 33342. Traps ADP in a beryllium fluoride-dependent manner, confirming ATPase activity. Probably unable to undergo NBD dimerization.
E504 (= E513) mutation E->A,C,D,Q,S: Complete loss of ATPase activity; mutant proteins trap ATP in a vanadate-independent manner whereas the wild-type protein traps ADP.

8rgnA Bmra e504-r6g-70umatpmg
34% identity, 94% coverage: 30:588/592 of query aligns to 19:571/578 of 8rgnA

query
sites
8rgnA

G

G

R

K

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A

A

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V

G

G

P

P

S
|
S

G

G

A

G

G
|
G

K
|
K

S
x
T

T
|
T

I

L

L

F

Q

K

L

L

A

L

Q

E

R

R

F

F

Y

Y

D

S

P

P

E

T

S

A

G

G

A

T

I

I

R

R

L

L

D

G

G

D

I

E

A

P

L

V

P

D

D

T

A

Y

D

S

P

L

A

E

D

S

I

W

R

R

A

E

R

H

I

I

A

G

V

Y

V

V

P

S

Q
|
Q

E

E

T

S

V

P

L

L

F

M

G

S

A

G

S

T

A

I

R

R

D

E

N

N

L

I

R

C

Y

Y

G

G

-

L

R

E

W

R

D

D

A

V

D

T

D

D

D

A

A

E

I

I

W

E

A

K

A

A

E

E

A

M

A

A

N

Y

A

A

A

L

S

N

F

F

L

I

R

K

A

E

L

L

P

P

D

N

G

Q

L

F

D

D

S

T

F

E

L

V

G

G

E

E

A

R

G

G

A
x
I

R

M

L

L

S
|
S

G

G

G
|
G

Q

Q

R

R

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

L

L

L

R

R

D

N

A

P

P

S

L

I

L

L

L

M

L

L

D

D

E

A

A

A

T

T

S

S

A

S

L

L

D

D

A

S

E

Q

S

S

E

E

R

K

L

S

V

V

Q

Q

D

Q

A

A

L

L

D

E

R

V

L

L

M

M

K

E

E

G

R

R

T

T

I

I

V

V

I

I

A

A

H
|
H

R

R

L

L

A

S

T

T

V

V

R

V

A

D

A

A

D

D

R

Q

I

L

V

F

M

V

D

E

Q

K

G

G

R

E

I

I

V

T

E

G

Q

R

G

G

D

T

H

H

A

H

T

E

L

L

S

M

A

A

Q

S

G

H

G

G

L

L

Y

Y

A

R

R

D

L

F

A

A

R

E

L

Q

Q

Q

F

L

N

K

binding adenosine-5'-triphosphate: D108 (≠ E121), Y342 (= Y358), I348 (≠ A366), S368 (= S386), G371 (= G389), K372 (= K390), T373 (≠ S391), T374 (= T392), Q414 (= Q432), I469 (≠ A486), S472 (= S489), G474 (= G491), H527 (= H544)

8gk7A Msba bound to cerastecin c (see paper)
34% identity, 95% coverage: 24:584/592 of query aligns to 9:564/564 of 8gk7A

query
sites
8gk7A

F

Y

A

L

R

K

R

P

Y

Y

P

W

G

G

R

V

I

A

A

L

A

V

L

L

A

I

A

G

L

F

V

G

V

M

A

N

A

S

C

A

A

T

T

E

L

V

A

S

I
x
V

P

A

G

K

G

L

F

I

R

K

L

F

V

I

I

I

D

D

K

A

G

I

F

Q

I

N

A

A

S

S

G

R

G

A

D

D

V

L

G

D

P

W

Y

F

F

P

H

L

Y

L

L
x
I

L

I

L

L

I

L

V

V

L

F

V

F

L
x
R

S

G

L

L

A

G

T

L

A

F

T

M

R

G

F

G

Y

Y

F

Y

V

T

S

A

W

V

M

I

G

S

E

R

R

S

V

L

V

V

A

F

D

S

I

I

R

R

I

Q

A

E

V

V

Q

Y

A

A

N

K

L

L

R

R

L

L

A

P

P

A

R

Q

F

Y

E

L

E

D

N

N

R

S

P

S

S

G

E

H

I

I

A

T

S

A

R

K

L

I

T

M

A

Y

D

N

T

V

A

E

I

Q

I

L

E

T

Q

A

V

A

V

S

G

S

T

E

T

S

V

L

S

K

V

T

A

I

L

V

R

R

N

D

I

G

V

M

L

I

A

T

I

L

G

G

G

L

I

L

I

G

Y

Y

L

L

F

F

A

Y

I

T

A

N

P

W

K

R

L

L

A

T

A

I

M

C

L

I

L

M

L

V

G

F

I

L

P

P

V

V

V

I

M

G

L

I

P

L

V

V

I

R

L

K

M

A

G

S

R

K

R

R

L

M

R

R

N

K

L

L

S

S

R

M

S

Q

T

V

Q

Q

D

D

R

T

I

M

A

G

D

D

V

V

G

N

A

H

T

V

V

V

S

Q

E

E

T

S

L

I

R

N

A

G

M

N

K

A

I

V

V

V

Q

K

G

S

F

F

N

A

Q

G

E

E

S

E

R

S

E

E

A

Q

E

E

R

R

F

F

G

Y

A

K

V

S

G

E

S

E

S

N

F

L

D

K

T

R

A

G

R

L

R

K

R

M

I

V

R

I

T

V

R

Q

A

N

V

L

M

N

T

S

A

P

I

V

I

Q

G

V

L

V

I
x
M

F

A

G

C

S

A

I
x
M

T

A

M

L

V

I

M

V

W

W

Q

L

G

A

A

L

I

R

D

P

V

Q

A

I

N

L

G

G

R

N

L

T

S

T

G

A

G

G

S

E

I

F

A

V

A

A

F

Y

I
|
I

L
x
T

T

A

G
x
A

G
|
G

L

L

V

L

A
x
S

G

K

A

P

F

V

G

K

A

N

L

L

A

T

E

D

V

V

Y

N

G

E

D

K

I

L

V

Q

R

R

A

G

A

L

G

A

A

A

A

H

R

S

L

V

S

F

E

E

L

L

T

D

A

L

-

P

E

E

A

E

E

Q

I

N

K

S

A

G

P

E

P

L

K

K

P

P

I

-

A

-

L

-

P

-

Q

-

P

Q

P

L

R

Q

G

G

R

A

L

I

S

R

F

F

D

D

H

H

V

V

G

V

F

L

R

N

Y
|
Y

P

A

T

D

R

G

P
x
T

E

Q

M

-

L

-

A

A

L

I

D

K

D

D

V

F

S

S

F

L

T

D

V

I

E

R

P

P

G

G

E

E

M

T

V

V

A

A

V

L

V

V

G

G

P

R

S
|
S

G
|
G

A

A

G
|
G

K
|
K

S
x
T

T

S

I

L

L

V

Q

N

L

M

A

L

Q

V

R

R

F

F

Y

Q

D

E

P

V

E

S

S

S

G

G

A

Q

I

I

R

Y

L

L

D

D

G

D

I

L

A

P

L

I

P

R

D

D

A

I

D

E

P

L

A

S

D

S

I

L

R

R

A

T

R

Q

I

I

A

A

V

M

V

V

P

N

Q

Q

E

Q

T

V

V

V

L

L

F

F

G

N

A

R

S

T

A

V

R

R

D

E

N

N

L

I

R

A

Y

Y

G

G

R

Q

-

L

W

H

D

N

A

A

D

S

D

D

D

E

A

D

I

V

W

I

A

A

E

K

A

A

N

Y

A

A

A

H

S

D

F

F

L

I

R

M

A

N

L

L

P

P

D

N

G

G

L

Y

D

D

S

T

F

V

L

L

G

G

E

A

A

Q

G

G

A

L

R
x
N

L
|
L

S
|
S

G
|
G

Q

Q

R

R

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

I

L

L

R

K

D

N

A

A

P

P

L

I

L

L

L

I

L

L

D

D

E

E

A

A

T

T

S

S

A

A

L

L

D

D

A

N

E

E

S

S

E

E

R

H

L

F

V

I

Q

Q

D

Q

A

A

L

F

D

D

R

E

L

A

M

M

K

Q

E

D

R

R

T

T

I

I

V

V

I

I

A

A

H

H

R

R

L

L

A

S

T

T

V

I

R

E

A

N

A

A

D

D

R

R

I

I

I

V

V

V

M

M

D

D

Q

R

G

G

R

Q

I

I

V

V

E

E

Q

Q

G

G

D

T

H

H

A

Q

T

E

L

L

S

L

A

A

Q

K

G

H

G

G

L

A

Y

Y

A

Y

R

Q

L

L

A

H

R

Q

binding phosphoaminophosphonic acid-adenylate ester: Y339 (= Y358), T343 (≠ P362), S365 (= S386), G366 (= G387), G368 (= G389), K369 (= K390), T370 (≠ S391), N467 (≠ R487), L468 (= L488), S469 (= S489), G470 (= G490), G471 (= G491)
binding 2-[(4-butylbenzene-1-sulfonyl)amino]-5-[(3-{4-[(4-butylbenzene-1-sulfonyl)amino]-3-carboxyanilino}-3-oxopropyl)carbamoyl]benzoic acid: V34 (≠ I49), I60 (≠ L75), R67 (≠ L82), M248 (≠ I263), M252 (≠ I267), I277 (= I292), T278 (≠ L293), A280 (≠ G295), G281 (= G296), S284 (≠ A299)

9csiA Lipid A export ATP-binding/permease protein MsbA (see paper)
34% identity, 95% coverage: 24:584/592 of query aligns to 14:569/569 of 9csiA

query
sites
9csiA

F

Y

A

L

R

K

R

P

Y

Y

P

W

G

G

R

V

I

A

A

L

A

V

L

L

A

I

A

G

L

F

V

G

V

M

A

N

A

S

C

A

A

T

T

E

L

V

A

S

I
x
V

P

A

G

K

G

L

F

I

R

K

L

F

V

I

I

I

D

D

K

A

G

I

F

Q

I

N

A

A

S

S

G

R

G

A

D

D

V

L

G

D

P

W

Y

F

F

P

H

L

Y

L

L
x
I

L

I

L

L

I

L

V

V

L

F

V

F

L
x
R

S

G

L

L

A

G

T

L

A

F

T

M

R

G

F

G

Y

Y

F

Y

V

T

S

A

W

V

M

I

G

S

E

R

R

S

V

L

V

V

A

F

D

S

I

I

R

R

I

Q

A

E

V

V

Q

Y

A

A

N

K

L

L

R

R

L

L

A

P

P

A

R

Q

F

Y

E

L

E

D

N

N

R

S

P

S

S

G

E

H

I

I

A

T

S

A

R

K

L

I

T

M

A

Y

D

N

T

V

A

E

I

Q

I

L

E

T

Q

A

V

A

V

S

G

S

T

E

T

S

V

L

S

K

V

T

A

I

L

V

R

R

N

D

I

G

V

M

L

I

A

T

I

L

G

G

G

L

I

L

I

G

Y

Y

L

L

F

F

A

Y

I

T

A

N

P

W

K

R

L

L

A

T

A

I

M

C

L

I

L

M

L

V

G

F

I

L

P

P

V

V

V

I

M

G

L

I

P

L

V

V

I

R

L

K

M

A

G

S

R

K

R

R

L

M

R

R

N

K

L

L

S

S

R

M

S

Q

T

V

Q

Q

D

D

R

T

I

M

A

G

D

D

V

V

G

N

A

H

T

V

V

V

S

Q

E

E

T

S

L

I

R

N

A

G

M

N

K

A

I

V

V

V

Q

K

G

S

F

F

N

A

Q

G

E

E

S

E

R

S

E

E

A

Q

E

E

R

R

F

F

G

Y

A

K

V

S

G

E

S

E

S

N

F

L

D

K

T

R

A

G

R

L

R

K

R

M

I

V

R

I

T

V

R

Q

A

N

V

L

M

N

T

S

A

P

I

V

I

Q

G

V

L

V

I
x
M

F

A

G

C

S

A

I
x
M

T

A

M

L

V

I

M

V

W

W

Q

L

G

A

A

L

I

R

D

P

V

Q

A

I

N

L

G

G

R

N

L

T

S

T

G

A

G

G

S

E

I

F

A

V

A

A

F

Y

I

I

L
x
T

T

A

G
x
A

G
|
G

L

L

V

L

A

S

G

K

A

P

F

V

G

K

A

N

L

L

A

T

E

D

V

V

Y

N

G

E

D

K

I

L

V

Q

R

R

A

G

A

L

G

A

A

A

A

H

R

S

L

V

S

F

E

E

L

L

T

D

A

L

-

P

E

E

A

E

E

Q

I

N

K

S

A

G

P

E

P

L

K

K

P

P

I

-

A

-

L

-

P

-

Q

-

P

Q

P

L

R

Q

G

G

R

A

L

I

S

R

F

F

D

D

H

H

V

V

G

V

F

L

R

N

Y
|
Y

P

A

T
x
D

R

G

P
x
T

E

Q

M

-

L

-

A

A

L

I

D

K

D

D

V

F

S

S

F

L

T

D

V

I

E

R

P

P

G

G

E

E

M

T

V

V

A

A

V

L

V

V

G

G

P

R

S
|
S

G
|
G

A

A

G
|
G

K
|
K

S
x
T

T
x
S

I

L

L

V

Q

N

L

M

A

L

Q

V

R

R

F

F

Y

Q

D

E

P

V

E

S

S

S

G

G

A

Q

I

I

R

Y

L

L

D

D

G

D

I

L

A

P

L

I

P

R

D

D

A

I

D

E

P

L

A

S

D

S

I

L

R

R

A

T

R

Q

I

I

A

A

V

M

V

V

P

N

Q
|
Q

E

Q

T

V

V

V

L

L

F

F

G

N

A

R

S

T

A

V

R

R

D

E

N

N

L

I

R

A

Y

Y

G

G

R

Q

-

L

W

H

D

N

A

A

D

S

D

D

D

E

A

D

I

V

W

I

A

A

E

K

A

A

N

Y

A

A

A

H

S

D

F

F

L

I

R

M

A

N

L

L

P

P

D

N

G

G

L

Y

D

D

S

T

F

V

L

L

G

G

E

A

A

Q

G

G

A

L

R

N

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

I

I

A

A

I

I

A

A

R

R

A

A

I

I

L

L

R

K

D

N

A

A

P

P

L

I

L

L

L

I

L

L

D

D

E

E

A

A

T

T

S

S

A

A

L

L

D

D

A

N

E

E

S

S

E

E

R

H

L

F

V

I

Q

Q

D

Q

A

A

L

F

D

D

R

E

L

A

M

M

K

Q

E

D

R

R

T

T

I

I

V

V

I

I

A

A

H

H

R

R

L

L

A

S

T

T

V

I

R

E

A

N

A

A

D

D

R

R

I

I

I

V

V

V

M

M

D

D

Q

R

G

G

R

Q

I

I

V

V

E

E

Q

Q

G

G

D

T

H

H

A

Q

T

E

L

L

S

L

A

A

Q

K

G

H

G

G

L

A

Y

Y

A

Y

R

Q

L

L

A

H

R

Q

binding 3,3'-[(1,4-dioxobutane-1,4-diyl)bis(azanediyl)]bis[(4-butylbenzene-1-sulfonamido)benzoic acid]: V39 (≠ I49), I65 (≠ L75), R72 (≠ L82), M253 (≠ I263), M257 (≠ I267), T283 (≠ L293), A285 (≠ G295), G286 (= G296)
binding phosphoaminophosphonic acid-adenylate ester: Y344 (= Y358), D346 (≠ T360), T348 (≠ P362), S370 (= S386), G371 (= G387), G373 (= G389), K374 (= K390), T375 (≠ S391), S376 (≠ T392), Q416 (= Q432)
binding magnesium ion: T375 (≠ S391), Q416 (= Q432)

Query Sequence

>WP_011951494.1 NCBI__GCF_000016765.1:WP_011951494.1
MARRDPNPETSERKLGELTMIWRFARRYPGRIAAALAALVVAACATLAIPGGFRLVIDKG
FIASGGDVGPYFHYLLLIVLVLSLATATRFYFVSWMGERVVADIRIAVQANLLRLAPRFF
EENRPSEIASRLTADTAIIEQVVGTTVSVALRNIVLAIGGIIYLFAIAPKLAAMLLLGIP
VVMLPVILMGRRLRNLSRSTQDRIADVGATVSETLRAMKIVQGFNQESREAERFGAVVGS
SFDTARRRIRTRAVMTAIIIGLIFGSITMVMWQGAIDVANGRLSGGSIAAFILTGGLVAG
AFGALAEVYGDIVRAAGAAARLSELLTAEAEIKAPPKPIALPQPPRGRLSFDHVGFRYPT
RPEMLALDDVSFTVEPGEMVAVVGPSGAGKSTILQLAQRFYDPESGAIRLDGIALPDADP
ADIRARIAVVPQETVLFGASARDNLRYGRWDADDDAIWAAAEAANAASFLRALPDGLDSF
LGEAGARLSGGQRQRIAIARAILRDAPLLLLDEATSALDAESERLVQDALDRLMKERTTI
VIAHRLATVRAADRIIVMDQGRIVEQGDHATLSAQGGLYARLARLQFNDVAA

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