SitesBLAST

P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
29% identity, 93% coverage: 8:248/258 of query aligns to 16:258/265 of P07821

query
sites
P07821

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K50 (= K42) mutation to Q: Lack of activity.
D172 (= D164) mutation to E: Lack of activity.
E173 (= E165) mutation to A: Lack of activity.

4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
33% identity, 86% coverage: 4:226/258 of query aligns to 2:224/240 of 4ymuJ

query
sites
4ymuJ

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binding adenosine-5'-triphosphate: F11 (≠ Y13), V16 (= V18), S36 (≠ N38), G37 (= G39), S38 (= S40), G39 (= G41), K40 (= K42), S41 (≠ T43), T42 (= T44), E162 (= E165), H194 (= H197)
binding magnesium ion: S41 (≠ T43), E162 (= E165)

8bmpA Cryo-em structure of the folate-specific ecf transporter complex in msp2n2 lipid nanodiscs bound to atp and adp (see paper)
33% identity, 91% coverage: 9:242/258 of query aligns to 11:244/278 of 8bmpA

query
sites
8bmpA

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binding adenosine-5'-triphosphate: F13 (= F11), N39 (= N38), G42 (= G41), K43 (= K42), S44 (≠ T43), T45 (= T44)

5x40A Structure of a cbio dimer bound with amppcp (see paper)
31% identity, 93% coverage: 4:242/258 of query aligns to 5:244/280 of 5x40A

query
sites
5x40A

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binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y13), V18 (≠ T17), A20 (≠ V18), N40 (= N38), G41 (= G39), G43 (= G41), K44 (= K42), S45 (≠ T43), T46 (= T44), Q88 (= Q82), H139 (≠ N138), M140 (≠ E139), L141 (= L140), S142 (= S141), G144 (= G143), Q145 (= Q144), Q166 (≠ E165), H198 (= H197)
binding magnesium ion: S45 (≠ T43), Q88 (= Q82)

6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
33% identity, 91% coverage: 4:238/258 of query aligns to 3:236/238 of 6s8nB

query
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6s8nB

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binding 2-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione: R90 (≠ S88), M133 (≠ R136), G134 (≠ F137), Q135 (≠ N138)

6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
33% identity, 91% coverage: 4:238/258 of query aligns to 3:236/238 of 6s8gA

query
sites
6s8gA

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T

G

K
x
R

T

R

V

V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N
|
N

G

G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-

L

R

H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P

P

Q
|
Q

K

E

E

A

H

S

I

I

S

F

S

R

N

R

F

-

P

-

L

L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G

V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N

Q

E
x
S

L

L

S
|
S

G

G

Q
x
E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R

R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E

E

P

P

F

F

N

A

G

G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H

H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

G

L

A

G

E

E

binding phosphoaminophosphonic acid-adenylate ester: Y12 (= Y13), R15 (≠ K16), N37 (= N38), G40 (= G41), K41 (= K42), T42 (= T43), T43 (= T44), Q84 (= Q82), S136 (≠ E139), S138 (= S141), E141 (≠ Q144)

6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
33% identity, 90% coverage: 4:235/258 of query aligns to 3:233/235 of 6mhzA

query
sites
6mhzA

I

L

V

T

A

A

E

K

D

N

V

L

T

A

F

K

A

A

Y
|
Y

D

K

T

G

K

R

T

R

V

V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N
|
N

G
|
G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-

L

R

H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P

P

Q
|
Q

K

E

E

A

H

S

I

I

S

F

S

R

N

R

F

-

P

-

L

L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G

V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N

Q

E
x
S

L

L

S
|
S

G
|
G

Q

E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R

R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E
|
E

P

P

F

F

N

A

G
|
G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H
|
H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

binding adp orthovanadate: Y12 (= Y13), N37 (= N38), G38 (= G39), G40 (= G41), K41 (= K42), T42 (= T43), T43 (= T44), Q84 (= Q82), S136 (≠ E139), S138 (= S141), G139 (= G142), G140 (= G143), E162 (= E165), G166 (= G169), H194 (= H197)

6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
33% identity, 90% coverage: 4:235/258 of query aligns to 3:233/233 of 6b8bA

query
sites
6b8bA

I

L

V

T

A

A

E

K

D

N

V

L

T

A

F

K

A

A

Y
|
Y

D

K

T

G

K
x
R

T

R

V
|
V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N

N

G
|
G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-

L

R

H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P

P

Q

Q

K

E

E

A

H

S

I

I

S
x
F

S
x
R

N
x
R

F

-

P

-

L

L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G

V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N

Q

E

S

L

L

S

S

G

G

Q

E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R

R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E

E

P

P

F

F

N

A

G

G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H

H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

binding adenosine-5'-diphosphate: Y12 (= Y13), R15 (≠ K16), V17 (= V18), G38 (= G39), G40 (= G41), K41 (= K42), T42 (= T43), T43 (= T44)
binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (≠ S87), R90 (≠ S88), R91 (≠ N89)

6b89A E. Coli lptb in complex with adp and novobiocin (see paper)
33% identity, 90% coverage: 4:235/258 of query aligns to 3:233/234 of 6b89A

query
sites
6b89A

I

L

V

T

A

A

E

K

D

N

V

L

T

A

F

K

A

A

Y
|
Y

D

K

T

G

K
x
R

T

R

V
|
V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N
|
N

G
|
G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-
x
L

R
x
H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P
|
P

Q
|
Q

K

E

E
x
A

H
x
S

I

I

S
x
F

S
x
R

N
x
R

F

-

P

-

L
|
L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G
x
V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N
x
Q

E

S

L

L

S

S

G

G

Q

E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R
|
R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E

E

P

P

F

F

N

A

G

G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H

H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

binding adenosine-5'-diphosphate: Y12 (= Y13), R15 (≠ K16), V17 (= V18), N37 (= N38), G38 (= G39), G40 (= G41), K41 (= K42), T42 (= T43), T43 (= T44)
binding magnesium ion: T42 (= T43), Q84 (= Q82)
binding novobiocin: L71 (vs. gap), H72 (≠ R70), P83 (= P81), A86 (≠ E84), S87 (≠ H85), F89 (≠ S87), R90 (≠ S88), R91 (≠ N89), L92 (= L92), V101 (≠ G101), Q135 (≠ N138), R149 (= R152)

4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium (see paper)
33% identity, 90% coverage: 4:235/258 of query aligns to 3:233/234 of 4p31A

query
sites
4p31A

I

L

V

T

A

A

E

K

D

N

V

L

T

A

F

K

A

A

Y
|
Y

D

K

T

G

K
x
R

T

R

V
|
V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N

N

G
|
G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-

L

R

H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P

P

Q
|
Q

K

E

E

A

H

S

I

I

S

F

S

R

N

R

F

-

P

-

L

L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G

V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N

Q

E

S

L

L

S

S

G

G

Q

E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R

R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E

E

P

P

F

F

N

A

G

G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H

H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

binding adenosine-5'-diphosphate: Y12 (= Y13), R15 (≠ K16), V17 (= V18), G38 (= G39), G40 (= G41), K41 (= K42), T42 (= T43), T43 (= T44)
binding magnesium ion: T42 (= T43), Q84 (= Q82)

6mbnA Lptb e163q in complex with atp (see paper)
33% identity, 91% coverage: 4:238/258 of query aligns to 4:237/241 of 6mbnA

query
sites
6mbnA

I

L

V

T

A

A

E

K

D

N

V

L

T

A

F

K

A

A

Y
|
Y

D

K

T

G

K
x
R

T

R

V
|
V

L

V

S

E

D

D

V

V

N

S

F

L

E

T

I

V

E

N

K

S

G

G

E

E

F

I

V

V

A

G

I

L

T

L

G

G

A

P

N
|
N

G
|
G

S

A

G
|
G

K
|
K

T
|
T

L

T

L

F

R

Y

L

M

I

V

T

V

G

G

I

I

L

V

K

P

P

R

I

D

K

A

G

G

K

N

I

I

L

I

V

I

F

D

G

D

V

D

D

D

T

I

N

S

D

L

-

L

-

P

-

L

R

H

E

A

R

R

V

A

Q

R

K

R

Y

G

I

I

G

G

L

Y

M

L

P

P

Q

Q

K

E

E

A

H

S

I

I

S

F

S

R

N

R

F

-

P

-

L

L

S

S

V

V

K

Y

D

D

V

N

V

L

L

M

M

A

G

V

L

L

S

Q

A

I

R

R

K

D

G

D

V

L

E

S

R

A

K

E

L

-

S

Q

R

R

E

E

D

D

I

-

E

-

L

R

A

A

K

N

E

E

N

L

L

M

R

E

L

E

V

F

G

H

L

I

E

E

S

H

L

L

W

R

D

D

R

S

R

M

F

G

N

Q

E

S

L

L

S

S

G

G

Q

E

R

R

Q

R

R

R

V

V

L

E

L

I

A

A

R

R

A

A

L

L

A

A

V

A

K

N

P

P

E

K

I

F

L

I

L

L

D

D

E

Q

P

P

F

F

N

A

G

G

V

V

D

D

V

P

P

I

S

S

Q

V

N

I

R

D

I

I

I

K

D

R

L

I

I

I

Y

E

E

H

L

L

T

R

R

D

D

S

G

G

L

L

T

G

A

V

I

L

M

I

V

T

V

D

H
|
H

N

N

I

V

N

R

P

E

L

T

L

L

H

A

K

V

I

C

D

E

K

R

A

A

M

Y

L

I

L

V

-

S

R

Q

N

G

R

H

M

L

I

I

A

A

F

H

G

G

K

T

P

P

E

T

E

E

V

I

F

L

T

Q

S

D

K

E

Y

H

L

V

F

K

E

R

A

V

Y

Y

G

L

A

G

E

E

binding adenosine-5'-triphosphate: Y13 (= Y13), R16 (≠ K16), V18 (= V18), N38 (= N38), G39 (= G39), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44), H195 (= H197)

1g291 Malk (see paper)
32% identity, 88% coverage: 1:226/258 of query aligns to 1:228/372 of 1g291

query
sites
1g291

M

M

K

A

A

G

I

V

V

R

A

L

E

V

D

D

V

V

T

W

F

K

A

V

Y

F

D

G

T

E

K

V

T

T

V

A

L

V

S

R

D

E

V

M

N

S

F

L

E

E

I

V

E

K

K

D

G

G

E

E

F

F

V

M

A

I

I

L

T

L

G

G

A

P

N
x
S

G
|
G

S
x
C

G
|
G

K
|
K

T
|
T

L

T

L

L

R

R

L

M

I

I

T

A

G

G

I

L

L

E

K

E

P

P

I

S

K

R

G

G

K

Q

I

I

L

Y

V

I

F

G

G

D

V

K

D

L

T

V

N

A

D
|
D

R

P

E
|
E

R

-

V

-

Q

-

K
|
K

Y

G

I

I

G

F

L

V

M

P

P

P

Q
x
K

K
x
D

E

R

H

D

I

I

S

A

S

M

N

V

F

F

P

Q

-

S

-

Y

-

A

-

L

-

Y

-

P

-

H

L

M

S

T

V

V

K

Y

D

D

V

N

V

I

L

A

M

F

G

P

L

L

S

K

A

L

R

R

K

K

G

-

V

-

E

-

R

-

K

-

L

V

S

P

R

R

E

Q

D

E

I

I

-

D

E

Q

L

R

A

V

K

R

E

E

N

V

L

A

R

E

L

L

V

L

G

G

L

L

E

T

S

E

L

L

W

L

D

N

R

R

R

K

F

P

N

R

E

E

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

L

A

L

L

A

G

R

R

A

A

L

I

A

V

V

R

K

K

P

P

E

Q

I

V

L

F

L

L

L

M

D

D

E

E

P

P

F

L

N

S

G

N

V

L

D

D

V

A

P

K

S

L

Q

R

N

V

R

R

I

M

I

R

D

A

L

E

I

L

Y

K

E

K

L

L

T

Q

R

R

D

Q

-

L

G

G

L

V

T

T

A

T

I

I

M

Y

V

V

V

T

H

H

N

D

I

Q

N

V

P

E

L

A

L

M

H

T

K

M

I

G

D

D

K

R

-

I

A

A

M

V

L

M

L

N

R

R

N

G

R

V

M

L

I

Q

A

Q

F

V

G

G

K

S

P

P

E

D

E

E

V

V

F

Y

binding magnesium ion: D69 (= D69), E71 (= E71), K72 (= K75), K79 (≠ Q82), D80 (≠ K83)
binding pyrophosphate 2-: S38 (≠ N38), G39 (= G39), C40 (≠ S40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)

Sites not aligning to the query:

binding magnesium ion: 292, 293, 359

Q99758 Phospholipid-transporting ATPase ABCA3; ABC-C transporter; ATP-binding cassette sub-family A member 3; ATP-binding cassette transporter 3; ATP-binding cassette 3; Xenobiotic-transporting ATPase ABCA3; EC 7.6.2.1; EC 7.6.2.2 from Homo sapiens (Human) (see 15 papers)
30% identity, 86% coverage: 16:237/258 of query aligns to 546:756/1704 of Q99758

query
sites
Q99758

K

R

T

A

V

A

L

V

S

R

D

D

V

L

N

N

F

L

E

N

I

L

E

Y

K

E

G

G

E

Q

F

I

V

T

A

V

I

L

T

L

G

G

A

H

N
|
N

G

G

S

A

G

G

K

K

T

T

L

T

L

L

R

S

L

M

I
x
L

T

T

G

G

I

L

L

F

K

P

P

P

I

T

K

S

G

G

K

R

I

A

L

Y

V

I

F

S

G

G

V

Y

D

E

-

I

T

S

N

Q

D

D

R

M

E

V

R

Q

V

I

Q
x
R

K

K

Y

S

I

L

G

G

L

L

M

C

P

P

Q

Q

K

H

E

D

H

I

I

L

S

F

S

D

N

N

F

L

P

T

L

V

S

A

V

E

K

H

D

-

V

-

L

L

M

Y

G

F

L

Y

S

A

A

Q

R

L

K

K

G

G

V

L

E

S

R

R

K

Q

L

K

S

C

R

P

E

E

D

E

I

V

E

-

L

-

A

-

K

K

E

Q

N

M

L

L

R

H

L

I

V

I

G

G

L

L

E

E

S

D

L

K

W

W

D

N

R

S

R

R

F

S

N

R

E

F

L

L

S

S

G

G

Q

M

R

R

Q

R

R

K

V

L

L

S

L

I

A

G

R

I

A

A

L

L

A

I

V

A

K

G

P

S

E

K

I

V

L

L

L

I

L

L

D

D

E

E

P

P

F

T

N
x
S

G

G

V

M

D

D

V

A

P

I

S

S

Q

R

N

R

R

A

I

I

I

W

D

D

L

L

I

L

Y

Q

E

R

L

Q

T

K

R

S

D

D

G

R

L

T

T

I

A

V

I

L

M

T

V

T

V

-

H

-

N

-

I

-

N

-

P

-

L

-

H

H

K

F

I

M

D

D

K

E

A

A

M

D

L

L

R

G

N

D

R

R

-

I

-

A

M

I

I

M

A

A

F

K

G

G

K

E

P

L

E

Q

E

C

V

C

F

G

T

S

S

S

K

L

Y

F

L

L

F

K

E

Q

A

K

Y

Y

G

G

A

A

N568 (= N38) to D: in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport; dbSNP:rs121909184
L579 (≠ I49) to P: in SMDP3; uncertain significance
R605 (≠ Q74) to Q: in SMDP3; uncertain significance; dbSNP:rs760006956
S693 (≠ N168) mutation to L: Does not affect protein oligomerization.

Sites not aligning to the query:

43 R → L: in SMDP3; uncertain significance
53 N→Q: Does not affect N-glycosylation. Does not affect protein expression. Does not affect lamellar body membrane location.
101 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; dbSNP:rs121909182
124 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-140. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.
140 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N → H: in dbSNP:rs45447801; N→Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-124. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.
173:174 LK→AA: Loss of proteolytic processing.
174:175 Cleavage; by CTSL
215 Q → K: in SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization; dbSNP:rs879159551
280 R → C: in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs201299260
288 R → K: in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs117603931
290 L → M: in a breast cancer sample; somatic mutation
292 E → V: in SMDP3; uncertain significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death; dbSNP:rs149989682
766 P → S: in dbSNP:rs45592239
801 E → D: in a breast cancer sample; somatic mutation
945 N→Q: Does not affect lamellar body membrane location. Does not affect protein expression. Does not affect proteolytic processing.
982 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs1402761450
1069 H → Q: in a breast cancer sample; somatic mutation
1076 N → K: in SMDP3; uncertain significance; dbSNP:rs2093663770
1221 G → S: in SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; G→A: Decreases ATP hydrolysis activity of 15% compared to the wild-type.; G→T: Decreases ATP hydrolysis activity of 36% compared to the wild-type.; G→V: Decreases ATP hydrolysis activity of 18% compared to the wild-type.
1302 G → E: in SMDP3; uncertain significance; dbSNP:rs2093657978
1388 K → N: in SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport
1553 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs121909183
1580 L → P: in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport; L→A: Decreases ATP hydrolysis activity of 13% compared to the wild-type.; L→F: Decreases ATP hydrolysis activity of 13% compared to the wild-type.; L→V: Decreases ATP hydrolysis activity of 56% compared to the wild-type.
1591 Q → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs28936691

Q0P9C4 Protein glycosylation K; EC 7.5.2.5 from Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (see 2 papers)
33% identity, 76% coverage: 8:202/258 of query aligns to 353:546/564 of Q0P9C4

query
sites
Q0P9C4

D

N

V

L

T

S

F

F

A

G

Y

Y

D

E

T

G

K

K

T

K

V

Y

L

L

-

F

S

K

D

N

V

L

N

N

F

L

E

N

I

I

E

K

K

K

G

G

E

E

F

K

V

I

A

A

I

F

T

I

G

G

A

E

N

S

G

G

S

C

G

G

K
|
K

T
x
S

T

T

L

L

L

V

R

D

L

L

I

I

T

I

G

G

I

L

L

L

K

K

P

P

I

K

K

E

G

G

K

Q

I

I

L

L

V

I

-

D

-

E

F

Q

G

E

V

L

D

N

T

A

N

N

D

N

R

T

E

K

R

N

V

Y

Q

R

K

Q

Y

K

I

I

G

G

L

Y

M

I

P

P

Q

Q

K

N

E

I

H

Y

I

L

S

-

N

-

F

F

P

N

L

D

S

S

V

I

K

A

D

K

V

N

V

I

L

T

M

F

G

G

L

D

S

A

A

V

-

D

R

E

K

E

G

K

V

L

E

N

R

R

K

V

L

I

S

K

R

Q

E

A

D

N

I

L

E

E

L

H

A

F

K

I

E

K

N

N

L

L

R

P

L

-

V

Q

G

G

L

V

E

Q

S

T

L

K

W

V

D

G

R

D

R

G

F

G

N

S

E

N

L

L

S

S

G

G

G
|
G

Q

Q

R

K

Q

Q

R
|
R

V

I

L

A

L

I

A

A

R

R

A

A

L

L

A

Y

V

L

K

E

P

P

E

E

I

M

L
|
L

L

V

L

L

D

D

E
|
E

P

A

F

T

N

S

G

A

V

L

D

D

V

T

P

Q

S

S

Q

E

N

A

R

K

I

I

I

M

D

D

L

E

I

I

Y

Y

E

K

L

I

T

S

R

K

D

D

G

K

L

-

T

T

A

M

I

I

M

I

V

I

V

A

H

H

N

R

I

L

N

S

P

T

L

I

K388 (= K42) mutation to A: Reduced efficiency of the N-linked protein glycosylation pathway.
S389 (≠ T43) mutation to A: Impaired N-linked protein glycosylation pathway.
G488 (= G143) mutation to D: Impaired N-linked protein glycosylation pathway.
R492 (= R147) mutation to C: No effect on the N-linked protein glycosylation pathway.
L506 (= L161) mutation to A: Reduced efficiency of the N-linked protein glycosylation pathway.
E510 (= E165) mutation to Q: Abolishes ATPase activity and strongly reduces translocation of lipid-linked oligosaccharide.

Sites not aligning to the query:

46:67 Important for stimulation of ATPase activity by lipid-linked oligosaccharides and subsequent translocation of lipid-linked oligosaccharides; SDFSYFDRNKYLISLKEYLNIP→GSSGSSGS: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding. Abolishes translocation of lipid-linked oligosaccharide.
50 Y→A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-56 and A-63.
53:55 RNK→ANA: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding. Strongly decreases translocation of lipid-linked oligosaccharide.
56 Y→A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-50 and A-63.
63 Y→A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-50 and A-56.
86 R→A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-260; A-302 and A-309.
260 R→A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-302 and A-309.
302 R→A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-260 and A-309.
309 R→A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-260 and A-302.

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
32% identity, 86% coverage: 12:234/258 of query aligns to 26:245/378 of P69874

query
sites
P69874

A
x
C

Y
x
F

D

D

T

G

K

K

T

E

V

V

L

I

S

P

D

Q

V

L

N

D

F

L

E

T

I

I

E

N

K

N

G

G

E

E

F
|
F

V

L

A

T

I

L

T

L

G

G

A

P

N

S

G

G

S
x
C

G

G

K

K

T

T

L

V

L
|
L

R

R

L

L

I

I

T

A

G

G

I

L

L

E

K

T

P

V

I

D

K

S

G

G

K

R

I

I

L

M

V
x
L

F

D

G

N

V

E

D

D

T

I

N

T

D

H

R

V

E

P

R

A

V

E

Q

N

K

R

Y

Y

I

V

G

N

L

T

M

V

P

F

Q

Q

K

S

E

Y

H

A

I

L

S

-

N

-

F

F

P

P

-

H

L

M

S

T

V

V

K

F

D

E

V

N

V

V

L

A

M

F

G

G

L

L

S

R

A

M

R

Q

K

K

G

T

V

P

E

A

R

A

K

E

L

I

S

T

R

P

E

R

D

-

I

-

E

-

L

-

A

V

K

M

E

E

N

A

L

L

R

R

L

M

V
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V

G

Q

L

L

E

E

S

T

L

F

W

A

D

Q

R

R

R

K

F

P

N

H

E

Q

L

L

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S

G

G

Q

Q

R

Q

Q

Q

R

R

V

V

L

A

L

I

A

A

R

R

A

A

L

V

A

V

V

N

K

K

P

P

E

R

I

L

L

L

D
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D

E

E

P

S

F

L

N

S

G

A

V

L

D

D

V

Y

P

K

S

L

Q

R

N

K

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M

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D

N

L

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A

L

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Q

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R

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K

-

L

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G

L

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A

F

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H

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E

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A

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L

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D

K

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L

M

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D

-

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-

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L

F

F

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A

A

C26 (≠ A12) mutation to A: Lower ATPase activity and transport efficiency.
F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
C54 (≠ S40) mutation to T: Loss of ATPase activity and transport.
L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
L76 (≠ V62) mutation to P: Lower ATPase activity and transport efficiency.
V135 (= V127) mutation to M: Loss of ATPase activity and transport.
D172 (= D164) mutation to N: Loss of ATPase activity and transport.

Sites not aligning to the query:

276 C→A: Lower ATPase activity and transport efficiency.
297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 88% coverage: 1:226/258 of query aligns to 1:222/371 of P68187

query
sites
P68187

M

M

K

A

A

S

I

V

V

Q

A

L

E

Q

D

N

V

V

T

T

F

K

A

A

Y

W

D

G

T

E

K

V

T

V

V

V

L

S

S

K

D

D

V

I

N

N

F

L

E

D

I

I

E

H

K

E

G

G

E

E

F

F

V

V

A

V

I

F

T

V

G

G

A

P

N

S

G

G

S

C

G

G

K

K

T

S

T

T

L

L

R

R

L

M

I

I

T

A

G

G

I

L

L

E

K

T

P

I

I

T

K

S

G

G

K

D

I

L

L

F

V

I

F

G

G

E

V

K

D

R

T

M

N

N

D

D

R

T

E

P

R

P

V

A

Q

E

K

R

Y

G

I

V

G

G

L

M

M

V

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F

Q

Q

K

S

E

Y

H
x
A

I

L

S

Y

S

P

N

H

F

-

P

-

L

L

S

S

V

V

K

A

D

E

V

N

V

M

L

S

M

F

G

G

L

L

S

K

A

L

R

-

K

A

G

G

V

A

E
x
K

R

K

K

E

L

V

S

I

R

N

E

Q

D

R

I
x
V

E

N

L

Q

A
x
V

K

A

E
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E

N

V

L

L

R

Q

L

L

V
x
A

G

-

L

-

E

-

S

H

L

L

W

L

D

D

R

R

R

K

F

P

N

K