SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing H281DRAFT_04927 H281DRAFT_04927 iron complex transport system ATP-binding protein 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)

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 paper)
63% identity, 95% coverage: 14:272/272 of query aligns to 7:265/265 of P07821

query
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P07821

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K50 (= K57) mutation to Q: Lack of activity.
D172 (= D179) mutation to E: Lack of activity.

1l7vC Bacterial abc transporter involved in b12 uptake (see paper)
35% identity, 83% coverage: 28:254/272 of query aligns to 9:231/231 of 1l7vC

query
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1l7vC

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binding cyclo-tetrametavanadate: N34 (= N53), G35 (= G54), A36 (≠ S55), G37 (= G56), K38 (= K57), S39 (= S58), T40 (= T59)

4fi3C Structure of vitamin b12 transporter btucd-f in a nucleotide-bound state (see paper)
35% identity, 83% coverage: 28:254/272 of query aligns to 9:231/248 of 4fi3C

query
sites
4fi3C

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binding phosphoaminophosphonic acid-adenylate ester: R14 (≠ L33), P33 (≠ H52), N34 (= N53), G35 (= G54), A36 (≠ S55), G37 (= G56), K38 (= K57), S39 (= S58), T40 (= T59), R121 (= R150), Q125 (≠ S154), L126 (= L155), S127 (= S156), G128 (= G157), G129 (= G158), E130 (= E159), Q158 (≠ E180), H190 (= H213)
binding magnesium ion: S39 (= S58), Q79 (= Q99)

7kypI Psabc from streptococcus pneumoniae in complex with fab (see paper)
29% identity, 87% coverage: 18:253/272 of query aligns to 1:230/234 of 7kypI

query
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7kypI

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binding cyclohexyl-hexyl-beta-d-maltoside: Q56 (≠ R80), E63 (= E86)

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 83% coverage: 18:243/272 of query aligns to 1:229/343 of P30750

query
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P30750

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40:46 (vs. 53:59, 71% identical) binding
E166 (= E180) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

278:283 binding
295 N→A: Reduces the binding of L-methionine to undetectable levels.
295:296 binding

A0R6H8 Mycobactin import ATP-binding/permease protein IrtA; EC 7.2.2.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 85% coverage: 15:244/272 of query aligns to 605:831/860 of A0R6H8

query
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A0R6H8

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G

R

E

P

R

D

V

I

-

P

L

V

L

L

H

H

P

D

L

I

A

S

L

L

T

Q

L

L

P

T

R

P

G

G

R

T

V

V

C

T

G

A

L

L

I

V

G

G

H

P

N

S

G

G

S

S

G

G

K

K

S

S

T

T

L

L

L

A

K

A

L

L

A

A

R

R

Q

F

Q

H

S

D

P

V

K

D

A

A

G

G

T

A

L

I

R

R

F

L

A

G

G

G

R

R

P

D

L

I

R

R

E

T

W

L

E

T

N

A

R

D

E

E

F

L

A

Y

R

R

Q

Q

V

V

A

G

Y

F

L

V

P

L

Q

Q

Q

D

Q

T

P

Q

A

L

A

V

S

G

G

G

M

-

T

T

V

V

R

A

E

E

L

N

V

I

A

A

L

L

G

A

R

D

Y

P

P

-

W

-

H

D

G

A

A

S

L

I

G

E

R

R

F

I

T

Q

G

D

V

A

-

A

-

R

D

D

A

A

E

Q

K

I

V

H

H

D

E

R

A

I

M

M

E

R

L

L

T

P

D

N

I

G

T

Y

R

D

F

T

G

P

D

L

R

G

A

A

V

A

D

S

S

S

L

L

S

S

G

G

E

E

R

K

Q

Q

R

R

A

L

W

T

I

I

A

A

M

R

L

A

V

I

A

L

Q

A

D

D

S

T

Q

P

C

V

L

L

L

I

L

L

D

D

E

E

P

A

I

T

S

A

A

F

L

A

D

D

I

P

A

E

H

S

Q

E

I

Y

E

L

V

V

L

Q

D

Q

L

A

V

L

R

N

T

R

L

L

S

T

Q

R

Q

D

R

R

G

-

L

-

G

T

V

V

V

L

V

V

V

I

L

A

H

H

D

R

I

L

N

H

M

T

A

I

A

T

R

H

F

-

C

A

D

D

D

Q

L

I

I

V

A

V

L

L

K

E

N

G

G

G

R

R

L

I

L

V

A

E

S

T

G

G

T

T

A

H

P

E

E

R

L

L

I

L

E

D

Sites not aligning to the query:

55 R→E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT; when associated with E-234 and E-241.
234 Q→E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT; when associated with E-55 and E-241.
241 R→E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT; when associated with E-55 and E-234.

3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
29% identity, 83% coverage: 18:243/272 of query aligns to 2:230/344 of 3tuzC

query
sites
3tuzC

M

M

Y

I

E

K

L

L

D

S

D

N

V

I

S

T

-

K

-

V

F
|
F

R

H

I
x
Q

G

G

E

T

R

R

V

T

L

I

-

Q

-
x
A

L

L

H

N

P

N

L

V

A

S

L

L

T

H

L

V

P

P

R

A

G

G

R

Q

V

I

C

Y

G

G

L

V

I

I

G

G

H

A

N

S

G
|
G

S
x
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

L

I

K

R

L

C

L

V

A

N

R

L

Q

L

Q

E

S

R

P

P

K

T

A

E

G

G

T

S

L

V

R

L

F

V

A

D

G

G

R

Q

P

E

L

L

R

T

E

T

W

L

E

S

N

E

R

S

E

E

F

L

A

T

-

K

-

A

-

R

R

R

Q

Q

V

I

A

G

Y

M

L

I

P

F

Q

Q

Q

H

Q

F

P

N

A

L

S

S

G

S

M

R

T

T

V

V

R

F

E

G

L

N

V

V

A

A

L

L

-

P

-

L

-

E

-

L

G

D

R

N

Y

T

P

P

W

K

H

D

G

E

A

V

L

K

G

R

R

R

F

V

T

T

G

-

V

-

D

-

A

-

E

-

K

-

V

-

H

-

E

E

A

L

M

L

E

S

L

L

T

V

D

G

I

L

T

G

R

D

F

K

G

H

D

D

R

S

A

Y

V

P

D

S

S

N

L

L

S

S

G

G

E

Q

R

K

Q

Q

R

R

A

V

W

A

I

I

A

A

M

R

L

A

V

L

A

A

Q

S

D

N

S

P

Q

K

C

V

L

L

L

C

D

D

E

Q

P

A

I

T

S

S

A

A

L

L

D

D

I

P

A

A

H

T

Q

T

I

R

E

S

V

I

L

L

D

E

L

L

V

L

R

K

T

D

L

I

S

N

Q

R

R

L

G

G

L

L

G

T

V

I

V

L

V

I

L

T

H

H

D

E

I

M

N

D

M

V

A

V

A

K

R

R

F

I

C

C

D

D

D

C

L

V

I

A

A

V

L

I

K

S

N

N

G

G

R

E

L

L

L

I

A

E

S

Q

G

D

T

T

A

V

P

S

E

E

L

V

I

F

binding adenosine-5'-diphosphate: F12 (= F26), Q14 (≠ I28), A21 (vs. gap), G42 (= G54), A43 (≠ S55), G44 (= G56), K45 (= K57), S46 (= S58), T47 (= T59)

Sites not aligning to the query:

binding selenomethionine: 274, 279, 281, 282, 283, 284, 311, 312, 313

3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
29% identity, 83% coverage: 18:243/272 of query aligns to 2:230/344 of 3tuiC

query
sites
3tuiC

M

M

Y

I

E

K

L

L

D

S

D

N

V

I

S

T

-

K

-

V

F
|
F

R

H

I
x
Q

G

G

E

T

R

R

V

T

L

I

-

Q

-

A

L

L

H

N

P

N

L

V

A

S

L

L

T

H

L

V

P

P

R

A

G

G

R

Q

V

I

C

Y

G

G

L

V

I

I

G

G

H

A

N
x
S

G
|
G

S
x
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

L

I

K

R

L

C

L

V

A

N

R

L

Q

L

Q

E

S

R

P

P

K

T

A

E

G

G

T

S

L

V

R

L

F

V

A

D

G

G

R

Q

P

E

L

L

R

T

E

T

W

L

E

S

N

E

R

S

E

E

F

L

A

T

-

K

-

A

-

R

R

R

Q

Q

V

I

A

G

Y

M

L

I

P

F

Q

Q

Q

H

Q

F

P

N

A

L

S

S

G

S

M

R

T

T

V

V

R

F

E

G

L

N

V

V

A

A

L

L

-

P

-

L

-

E

-

L

G

D

R

N

Y

T

P

P

W

K

H

D

G

E

A

V

L

K

G

R

R

R

F

V

T

T

G

-

V

-

D

-

A

-

E

-

K

-

V

-

H

-

E

E

A

L

M

L

E

S

L

L

T

V

D

G

I

L

T

G

R

D

F

K

G

H

D

D

R

S

A

Y

V

P

D

S

S

N

L

L

S

S

G

G

E

Q

R

K

Q

Q

R

R

A

V

W

A

I

I

A

A

M

R

L

A

V

L

A

A

Q

S

D

N

S

P

Q

K

C

V

L

L

L

C

D

D

E

Q

P

A

I

T

S

S

A

A

L

L

D

D

I

P

A

A

H

T

Q

T

I

R

E

S

V

I

L

L

D

E

L

L

V

L

R

K

T

D

L

I

S

N

Q

R

R

L

G

G

L

L

G

T

V

I

V

L

V

I

L

T

H

H

D

E

I

M

N

D

M

V

A

V

A

K

R

R

F

I

C

C

D

D

D

C

L

V

I

A

A

V

L

I

K

S

N

N

G

G

R

E

L

L

L

I

A

E

S

Q

G

D

T

T

A

V

P

S

E

E

L

V

I

F

binding adenosine-5'-diphosphate: F12 (= F26), Q14 (≠ I28), S41 (≠ N53), G42 (= G54), A43 (≠ S55), G44 (= G56), K45 (= K57), S46 (= S58), T47 (= T59)

6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
29% identity, 83% coverage: 18:243/272 of query aligns to 2:230/344 of 6cvlD

query
sites
6cvlD

M

M

Y

I

E

K

L

L

D

S

D

N

V

I

S

T

-

K

-

V

F
|
F

R

H

I
x
Q

G

G

E

T

R

R

V

T

L
x
I

-

Q

-

A

L

L

H

N

P

N

L

V

A

S

L

L

T

H

L

V

P

P

R

A

G

G

R

Q

V

I

C

Y

G

G

L

V

I

I

G

G

H

A

N
x
S

G
|
G

S
x
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

L

I

K

R

L

C

L

V

A

N

R

L

Q

L

Q

E

S

R

P

P

K

T

A

E

G

G

T

S

L

V

R

L

F

V

A

D

G

G

R

Q

P

E

L

L

R

T

E

T

W

L

E

S

N

E

R

S

E

E

F

L

A

T

-

K

-

A

-

R

R

R

Q

Q

V

I

A

G

Y

M

L

I

P

F

Q

Q

Q

H

Q

F

P

N

A

L

S

S

G

S

M

R

T

T

V

V

R

F

E

G

L

N

V

V

A

A

L

L

-

P

-

L

-

E

-

L

G

D

R

N

Y

T

P

P

W

K

H

D

G

E

A

V

L

K

G

R

R

R

F

V

T

T

G

-

V

-

D

-

A

-

E

-

K

-

V

-

H

-

E

E

A

L

M

L

E

S

L

L

T

V

D

G

I

L

T

G

R

D

F

K

G

H

D

D

R

S

A

Y

V

P

D

S

S
x
N

L
|
L

S
|
S

G
|
G

E
x
Q

R

K

Q

Q

R

R

A

V

W

A

I

I

A

A

M

R

L

A

V

L

A

A

Q

S

D

N

S

P

Q

K

C

V

L

L

L

C

D

D

E

Q

P

A

I

T

S

S

A

A

L

L

D

D

I

P

A

A

H

T

Q

T

I

R

E

S

V

I

L

L

D

E

L

L

V

L

R

K

T

D

L

I

S

N

Q

R

R

L

G

G

L

L

G

T

V

I

V

L

V

I

L

T

H
|
H

D

E

I

M

N

D

M

V

A

V

A

K

R

R

F

I

C

C

D

D

D

C

L

V

I

A

A

V

L

I

K

S

N

N

G

G

R

E

L

L

L

I

A

E

S

Q

G

D

T

T

A

V

P

S

E

E

L

V

I

F

binding phosphothiophosphoric acid-adenylate ester: F12 (= F26), Q14 (≠ I28), I19 (≠ L33), S41 (≠ N53), G42 (= G54), A43 (≠ S55), G44 (= G56), K45 (= K57), S46 (= S58), T47 (= T59), N141 (≠ S154), L142 (= L155), S143 (= S156), G144 (= G157), G145 (= G158), Q146 (≠ E159), H200 (= H213)

P59852 Lactococcin-G-processing and transport ATP-binding protein LagD; EC 3.4.22.-; EC 7.-.-.- from Lactococcus lactis subsp. lactis (Streptococcus lactis) (see paper)
27% identity, 89% coverage: 4:246/272 of query aligns to 455:694/703 of P59852

query
sites
P59852

N

N

L

T

T

N

V

I

D

N

S

I

A

S

R

K

A

N

V

I

H

F

G

N

E

K

P

D

M

I

Y

-

E

K

L

L

D

D

D

K

V

V

S

S

F

F

R

S

I

Y

G

N

E

M

R

K

V

L

-

P

L

V

L

L

H

R

P

D

L

V

A

S

L

L

T

E

L

I

P

Y

R

S

G

K

R

S

V

K

C

V

G

A

L

L

I

V

G

G

H

V

N

S

G

G

S

S

G

G

K

K

S

S

T

T

L

L

L

A

K

K

L

L

A

V

R

K

Q

F

Q

Y

S

D

P

P

K

S

A

E

G

G

T

N

L

I

R

T

F

Y

A

G

G

D

R

I

P

N

L

C

R

Q

E

D

W

I

E

E

N

N

R

H

E

K

F

L

A

R

R

N

Q

H

V

V

A

T

Y

Y

L

V

P

P

Q

Q

Q

E

Q

S

P

F

A

F

S

N

G

G

M

T

T

I

V

I

R

D

E

N

L

L

V

T

-

F

A

G

L

L

G

S

R

H

Y

Q

P

P

W

-

H

-

G

-

A

-

L

-

G

-

R

-

F

-

T

-

G

-

V

-

D

E

A

F

E

E

K

K

V

I

H

F

E

R

A

A

M

C

E

K

-

A

-

C

L

L

T

V

D

D

I

F

T

I

-

N

-

Q

-

P

-

L

R

R

F

F

G

D

-

S

-

V

-

L

D

E

R

E

A

G

V

G

D

N

S

N

L

L

S

S

G

G

E

Q

R

K

Q

Q

R

R

A

L

W

A

I

I

A

A

M

R

L

A

V

I

A

L

Q

N

D

D

S

S

Q

E

C

I

L

I

L

F

D

D

E

E

P

A

I

T

S

S

A

G

L

L

D

D

I

T

A

L

H

L

Q

E

I

K

E

E

V

I

L

L

D

E

L

Y

V

L

R

I

T

K

L

L

S

Q

Q

D

Q

K

R

T

G

-

L

-

G

-

V

I

V

F

V

I

L

A

H

H

D

H

I

L

N

S

M

I

A

-

A

A

R

K

F

A

C

C

D

D

D

E

L

I

I

I

A

V

L

L

K

D

N

Q

G

G

R

I

L

L

L

V

A

G

S

R

G

G

T

T

A

H

P

E

E

E

L

L

I

S

E

E

E

K

K

E

Sites not aligning to the query:

13 C→A: Complete loss of precursor processing.
95 V→M: 5-fold reduction of precursor processing.

1jj7A Crystal structure of thE C-terminal atpase domain of human tap1 (see paper)
30% identity, 86% coverage: 13:246/272 of query aligns to 6:242/251 of 1jj7A

query
sites
1jj7A

V

L

H

H

G

L

E

E

P

G

M

L

Y

V

E

Q

L

F

D

Q

D

D

V

V

S

S

F

F

R

A

I
x
Y

G

P

E

N

R

R

-

P

-

D

-

V

V

L

L
x
V

L

L

H

Q

P

G

L

L

A

T

L

F

T

T

L

L

P

R

R

P

G

G

R

E

V

V

C

T

G

A

L

L

I

V

G

G

H

P

N
|
N

G
|
G

S
|
S

G
|
G

K
|
K

S
|
S

T
|
T

L

V

L

A

K

A

L

L

A

Q

R

N

Q

L

Q

Y

S

Q

P

P

K

T

A

G

G

G

T

Q

L

L

R

L

F

L

A

D

G

G

R

K

P

P

L

L

R

P

E

Q

W

Y

E

E

N

H

R

R

E

Y

F

L

A

H

R

R

Q

Q

V

V

A

A

Y

A

L

V

P

G

Q

-

Q

Q

Q

E

P

P

A

Q

A

V

S

F

G

G

M

R

T

S

V

L

R

Q

E

E

L

N

V

I

A

A

L

Y

G

G

R

-

Y

L

P

T

W

Q

H

K

G

P

A

T

L

M

G

E

R

E

F

I

T

T

G

A

V

A

D

A

A

V

E

K

K

S

V

G

H

A

E

H

A

S

M

F

E

-

L

I

T

S

D

G

I

L

T

P

R

Q

F

G

G

Y

D

D

R

T

A

E

V

V

D

D

-

E

-

A

-

G

-

S

S

Q

L

L

S

S

G

G

E

Q

R

R

Q

Q

R

A

A

V

W

A

I

L

A

A

M

R

L

A

V

L

A

I

Q

R

D

K

S

P

Q

C

C

V

L

L

L

I

L

L

D

D

E

D

P

A

I

T

S

S

A

A

L

L

D

D

I

A

A

N

H

S

Q

Q

I

L

E

Q

V

V

L

E

D

Q

L

L

V

L

R

Y

T

E

L

S

S

P

Q

E

Q

R

R

Y

G

S

L

R

G

S

V

V

V

L

V

I

L

T

H

Q

D

H

I

L

N

S

M

L

A

V

A

E

R

Q

F

-

C

A

D

D

D

H

L

I

I

L

A

F

L

L

K

E

N

G

G

G

R

A

L

I

L

R

A

E

S

G

G

G

T

T

A

H

P

Q

E

Q

L

L

I

M

E

E

E

K

K

K

binding adenosine-5'-diphosphate: Y21 (≠ I28), V29 (≠ L33), N49 (= N53), G50 (= G54), S51 (= S55), G52 (= G56), K53 (= K57), S54 (= S58), T55 (= T59)

O06967 Multidrug resistance ABC transporter ATP-binding/permease protein BmrA; EC 7.6.2.- from Bacillus subtilis (strain 168) (see 2 papers)
31% identity, 82% coverage: 20:243/272 of query aligns to 342:564/589 of O06967

query
sites
O06967

E

Q

L

L

D

D

D

R

V

V

S

S

F

F

R

G

I

Y

G

K

-

P

E

D

R

Q

V

L

L

I

L

L

H

K

P

E

L

V

A

S

L

A

T

V

L

I

P

E

R

A

G

G

R

K

V

V

C

T

G

A

L

I

I

V

G

G

H

P

N

S

G

G

S

G

G

G

K
|
K

S

T

T

T

L

L

L

F

K

K

L

L

A

E

R

R

Q

F

Q

Y

S

S

P

P

K

T

A

A

G

G

T

T

L

I

R

R

F

L

A

G

G

D

R

E

P

P

L

V

R

D

E

T

W

Y

E

S

N

L

R

E

E

S

F

W

A

R

R

E

Q

H

V

I

A

G

Y

Y

L

V

P

S

Q

Q

Q

E

Q

S

P

P

A

L

A

M

S

S

G

G

M

-

T

T

V

I

R

R

E

E

L

N

V

I

A

C

L

Y

G

G

R

-

Y

-

P

-

W

-

H

-

G

-

A

-

L

L

G

E

R

R

-

D

F

V

T

T

G

D

V

A

D

E

A

I

E

E

K

K

V

A

H

A

E

E

-

M

A

A

M

Y

E

A

L

L

T

N

D

F

I

I

-

K

-

E

-

L

-

P

-

N

-

Q

-

F

-

D

T

T

R

E

F

V

G

G

D

E

R

R

A

G

V

I

D

-

S

M

L

L

S

S

G

G

E

Q

R

R

Q

Q

R

R

A

I

W

A

I

I

A

A

M

R

L

A

V

L

A

L

Q

R

D

N

S

P

Q

S

C

I

L

L

L

M

L

L

D

D

E
|
E

P

A

I

T

S

S

A

S

L

L

D

D

I

S

A

Q

H

S

Q

E

I

K

E

S

V

V

L

Q

D

Q

L

A

V

L

R

E

T

V

L

L

S

M

Q

E

Q

G

R

R

G

-

L

-

G

T

V

T

V

I

V

V

V

I

L

A

H

H

D

R

I

L

N

S

M

T

A

V

R

D

F

-

C

A

D

D

D

Q

L

L

I

L

A

F

L

V

K

E

N

K

G

G

R

E

L

I

L

T

A

G

S

R

G

G

T

T

A

H

P

H

E

E

L

L

I

M

K380 (= K57) 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 (= E180) 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.

7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp (see paper)
30% identity, 88% coverage: 20:259/272 of query aligns to 5:247/262 of 7chaI

query
sites
7chaI

E

E

L

L

D

K

D

G

V

L

S

T

F

F

R

K

I
x
R

G

G

E

S

R
|
R

V

A

L
x
I

L

F

H

D

P

N

L

I

A

D

L

V

T

R

L

I

P

P

R

R

G

G

R

K

V

V

C

T

G

G

L

I

I

M

G

G

H
x
P

N
x
S

G
|
G

S
x
C

G
|
G

K
|
K

S
x
T

T
|
T

L

L

K

R

L

L

L

I

A

A

R

S

Q

Q

Q

L

S

R

P

P

K

S

A

K

G

G

T

E

L

V

R

W

F

V

A

N

G

G

R

Q

P

N

L

L

R

P

E

Q

W

L

E

S

N

R

R

G

E

D

F

L

A

F

-

D

-

M

-

R

R

K

Q

Q

V

F

A

G

Y

V

L

L

P

F

Q

Q

Q

S

Q

G

P

A

A

L

A

F

S

T

G

D

M

L

T

D

V

V

R

F

E

E

L

N

V

V

A

A

L

-

G

-

R

-

Y

F

P

P

W

-

H

-

G

-

A

-

L

L

G

R

R

V

F

H

T

T

G

Q

V

L

D

P

A

E

E

E

K

M

V

I

H

R

E

D

A

I

M

V

E

-

L

L

T

M

D

K

I

L

T

Q

R

A

F

V

G

G

D

L

R

R

A

G

V

A

-

V

-

E

-

L

-

M

-

P

D

D

S

E

L

L

S

S

G

G

E

M

R

K

Q

R

R

R

A

V

W

A

I

L

A

A

M

R

L

A

V

I

A

A

Q

L

D

D

S

P

Q

Q

C

I

L

L

L

Y

D

D

E

E

P

P

I

F

S

V

A

G

L

Q

D

D

I

P

A

I

H

A

Q

M

I

G

E

V

V

L

L

V

D

R

L

L

V

I

R

R

T

L

L

L

S

N

Q

D

Q

A

R

L

G

G

L

I

G

T

V

S

V

I

V

V

L

S

H
|
H

D

D

I

L

N

A

M

E

A

T

A

A

R

S

F

I

C

A

D

D

D

Y

L

I

I

Y

A

I

L

V

K

G

N

D

G

G

R

R

L

V

L

L

A

G

S

H

G

G

T

T

A

-

P

P

E

D

L

V

I

L

E

K

E

E

-

T

-

D

-

P

K

R

M

I

L

R

G

Q

A

F

I

V

Y

K

G

G

V

I

P

P

M

D

G

G

T

P

V

V

binding phosphoaminophosphonic acid-adenylate ester: R13 (≠ I28), R16 (= R31), I18 (≠ L33), P37 (≠ H52), S38 (≠ N53), G39 (= G54), C40 (≠ S55), G41 (= G56), K42 (= K57), T43 (≠ S58), T44 (= T59), H198 (= H213)

7t55A Cryo-em structure of pcat1 in the inward-facing wide conformation under atp turnover condition (see paper)
28% identity, 83% coverage: 20:246/272 of query aligns to 480:704/715 of 7t55A

query
sites
7t55A

E

E

L

F

D

R

D

N

V

V

S

D

F

F

R

R

I
x
Y

G

G

E

L

R

R

V

K

-

P

L

V

L

L

H

K

P

N

L

I

A

N

L

L

T

T

L

I

P

P

R

K

G

G

R

K

V

T

C

V

G

A

L

I

I

V

G

G

H

E

N

S

G
|
G

S
|
S

G
|
G

K
|
K

S
x
T

T
|
T

L

L

L

A

K

K

L

L

A

M

R

N

Q

F

Q

Y

S

S

P

P

K

E

A

K

G

G

T

D

L

I

R

L

F

I

A

N

G

G

R

H

P

S

L

I

R

K

E

N

W

I

E

S

N

L

R

E

E

L

F

I

A

R

R

K

Q

K

V

I

A

A

Y

F

L

V

P

S

Q
|
Q

Q

D

Q

V

P

F

A

I

A

F

S

S

G

G

M

-

T

T

V

V

R

K

E

E

L

N

V

L

A

C

L

L

G

G

R

N

Y

-

P

-

W

-

H

-

G

-

A

-

L

-

G

-

R

-

F

-

T

E

G

N

V

V

D

D

A

M

E

D

K

E

V

I

H

I

E

K

A

A

M

A

E

K

L

M

T

A

D

N

-

A

-

H

-

D

-

F

-

I

-

E

-

K

-

L

-

P

-

L

-

K

I

Y

T

D

R

T

F

F

G

L

D

N

R

E

A

S

V

G

D

A

S

N

L

L

S

S

G

E

G

G

E

Q

R

K

Q

Q

R

R

A

L

W

A

I

I

A

A

M

R

L

A

V

L

A

L

Q

K

D

K

S

P

Q

D

C

I

L

L

L

I

L

L

D

D

E

E

P

A

I

T

S

S

A

N

L

L

D

D

I

S

A

I

H

T

Q

E

I

N

E

H

V

I

L

K

D

D

L

A

V

I

R

Y

T

G

L

L

S

-

Q

-

Q

E

R

D

G

D

L

V

G

T

V

V

V

I

L

A

H

H

D

R

I

L

N

S

M

T

A

I

A

V

R

N

F

-

C

C

D

D

D

K

L

I

I

Y

A

L

L

L

K

K

N

D

G

G

R

E

L

I

L

V

A

E

S

S

G

G

T

S

A

H

P

T

E

E

L

L

I

I

E

A

E

L

K

K

binding adenosine-5'-triphosphate: Y488 (≠ I28), G515 (= G54), S516 (= S55), G517 (= G56), K518 (= K57), T519 (≠ S58), T520 (= T59), Q560 (= Q99)
binding magnesium ion: K518 (= K57), T519 (≠ S58)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 252
binding : 11, 14, 45, 46, 47, 48, 49, 52, 63, 64, 65, 66, 75, 83, 91, 92, 93

3vx4D Crystal structure of the nucleotide-binding domain of s. Mutans coma, a bifunctional atp-binding cassette transporter involved in the quorum-sensing pathway (see paper)
27% identity, 83% coverage: 21:246/272 of query aligns to 10:232/240 of 3vx4D

query
sites
3vx4D

L

F

D

E

D

N

V

L

S

S

F

Y

R

K

I
x
Y

G

G

-

F

E

G

R

R

V

D

L
x
T

L

L

H

S

P

D

L

I

A

N

L

L

T

S

L

I

P

K

R

K

G

G

R

S

V

K

C

V

G

S

L

L

I

V

G

G

H
x
A

N
x
S

G
|
G

S
|
S

G
|
G

K
|
K

S
x
T

T
|
T

L

L

L

A

K

K

L

L

L

I

A

V

R

N

Q

F

Q

Y

S

E

P

P

K

N

A

K

G

G

T

I

L

V

R

R

F

I

A

N

G

G

R

N

P

D

L

L

R

K

E

V

W

I

E

D

N

K

R

T

E

A

F

L

A

R

R

R

Q

H

V

I

A

S

Y

Y

L

L

P

P

Q
|
Q

Q

Q

Q

A

P

Y

A

V

A

F

S

S

G

G

M

S

T

I

V

M

R

D

E

N

L

L

V

V

A

-

L

-

G

-

R

-

Y

-

P

-

W

-

H

-

G

-

A

-

L

L

G

G

R

A

F

K

T

E

G

G

V

T

D

S

A

Q

E

E

K

D

V

I

H

I

E

R

A

A

M

C

E

E

L

I

T

A

D

E

I

I

-

R

-

S

-

D

-

I

-

E

-

Q

-

M

-

P

-

Q

-

G

-

Y

-

Q

T

T

R

E

F

L

G

S

D

D

R

G

A

A

V

-

D

-

S
x
G

L
x
I

S
|
S

G
|
G

E
x
Q

R

K

Q

Q

R

R

A

I

W

A

I

L

A

A

M

R

L

A

V

L

A

L

Q

T

D

Q

S

A

Q

P

C

V

L

L

L

I

L

L

D

D

E

A

P

A

I

T

S

S

A
x
S

L

L

D

D

I

I

A

L

H

T

Q

E

I

K

E

K

V

I

L

I

D

S

L

N

V

L

R

L

T

Q

L

M

S

T

Q

E

Q

K

R

T

G

-

L

-

G

-

V

I

V

F

V

V

L

A

H
|
H

D

R

I

L

N

S

M

I

A

S

A

Q

R

R

F

-

C

T

D

D

D

E

L

V

I

I

A

V

L

M

K

D

N

Q

G

G

R

K

L

I

L

V

A

E

S

Q

G

G

T

T

A

H

P

K

E

E

L

L

I

L

E

A

E

K

K

Q

binding adenosine-5'-triphosphate: Y17 (≠ I28), T23 (≠ L33), A42 (≠ H52), S43 (≠ N53), G44 (= G54), S45 (= S55), G46 (= G56), K47 (= K57), T48 (≠ S58), T49 (= T59), Q89 (= Q99), G144 (≠ S154), I145 (≠ L155), S146 (= S156), G147 (= G157), G148 (= G158), Q149 (≠ E159), S174 (≠ A184), H200 (= H213)
binding magnesium ion: T48 (≠ S58), Q89 (= Q99)

P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 76% coverage: 37:244/272 of query aligns to 23:224/393 of P9WQI3

query
sites
P9WQI3

L

L

A

N

L

L

T

T

L

I

P

A

R

D

G

G

R

E

V

F

C

L

G

I

L

L

I

V

G

G

H

P

N

S

G

G

S

C

G

G

K

K

S

T

T

T

L

T

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H193 (= H213) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.

Q96J66 ATP-binding cassette sub-family C member 11; Multidrug resistance-associated protein 8; EC 7.6.2.2; EC 7.6.2.3 from Homo sapiens (Human) (see 5 papers)
31% identity, 78% coverage: 34:246/272 of query aligns to 527:723/1382 of Q96J66

query
sites
Q96J66

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T546 (≠ N53) to M: significantly decreased transport activity of DHEAS and estrone 3-sulfate; no effect on glycosylation; reduced ATP-dependent 5-FdUMP transport; no effect on plasma membrane localization; dbSNP:rs17822471
R630 (= R150) to W: no effect on glycosylation; dbSNP:rs41282045
V648 (= V169) to I: no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization; dbSNP:rs16945930
V687 (= V209) to I: no effect on glycosylation; dbSNP:rs16945928

Sites not aligning to the query:

19 R → H: no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization; dbSNP:rs16945988
180 G → R: in dry earwax and lack of axillary odor phenotype; loss of N-glycosylation; strongly reduced plasma membrane localization; no DHEAS transport and largely reduced estrone 3-sulfate transport; decreased protein concentration in axillary sweat; dbSNP:rs17822931; mutation G->A,P: Does not affect N-glycosylation.; mutation G->L,H,D,E: Loss of N-glycosylation.
317 A → E: no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization; dbSNP:rs11863236
735 K → R: no effect on glycosylation; dbSNP:rs16945926
838 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation.
844 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation.
970 M → V: no effect on glycosylation; dbSNP:rs41280943
1344 H → R: no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization; dbSNP:rs16945916

Q03518 Antigen peptide transporter 1; APT1; ATP-binding cassette sub-family B member 2; Peptide supply factor 1; Peptide transporter PSF1; PSF-1; Peptide transporter TAP1; Peptide transporter involved in antigen processing 1; Really interesting new gene 4 protein; RING4; EC 7.4.2.14 from Homo sapiens (Human) (see 10 papers)
30% identity, 86% coverage: 13:246/272 of query aligns to 497:733/748 of Q03518

query
sites
Q03518

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V518 (vs. gap) to I: in allele TAP1*x; dbSNP:rs41561219
S545 (= S58) binding
D637 (= D153) to G: in allele TAP1*02:01, allele TAP1*04:01 and allele TAP1*x; dbSNP:rs1135216
R648 (= R160) to Q: in allele TAP1*04:01; dbSNP:rs1057149
R659 (≠ Q171) to Q: in a lung cancer cell line deficient in MHC class I presentation; dbSNP:rs121917702
D674 (= D186) mutation to A: Impairs allosteric coupling of peptide transport to ATP hydrolysis, converting the unidirectional active pump into a passive bidirectional nucleotide-gated facilitator. Inactive in peptide transport when associated with 'A-638' of TAP2.

Sites not aligning to the query:

7 P → S: in dbSNP:rs375389015
17 G → R: in dbSNP:rs57640466
32 Inter-subunit salt bridge with TAPBP; D→K: Complete loss of interaction with TAPBP, resulting in impaired PLC assembly and antigen presentation.
333 I → V: in allele TAP1*02:01, allele TAP1*03:01, allele TAP1*04:01 and allele TAP1*x; dbSNP:rs1057141
370 A → V: in allele TAP1*x; dbSNP:rs2127679
375:420 Part of the peptide-binding site
419 G → C: in dbSNP:rs2228110
453:487 Part of the peptide-binding site
458 V → L: in allele TAP1*04:01; dbSNP:rs41550019

5d3mA Folate ecf transporter: amppnp bound state (see paper)
32% identity, 83% coverage: 18:243/272 of query aligns to 5:231/280 of 5d3mA

query
sites
5d3mA

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