SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_090273468.1 NCBI__GCF_900105005.1:WP_090273468.1 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 15 hits to proteins with known functional sites (download)

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
25% identity, 90% coverage: 18:423/451 of query aligns to 39:412/444 of Q8NLB7

query
sites
Q8NLB7

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D54 (≠ E30) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D33) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (≠ K86) mutation to A: Loss of transport activity.
W309 (≠ L316) mutation to V: Loss of transport activity.
D312 (= D322) mutation to A: Loss of transport activity.
R313 (= R323) mutation to A: Loss of transport activity.
I317 (vs. gap) mutation I->H,Y: Loss of transport activity.
R386 (≠ S398) mutation to A: Loss of transport activity.

P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 75% coverage: 67:405/451 of query aligns to 182:508/616 of P36035

query
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P36035

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K338 (= K239) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
9 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
26% identity, 79% coverage: 43:399/451 of query aligns to 30:382/446 of A0A0H2VG78

query
sites
A0A0H2VG78

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R102 (= R128) mutation to A: Loss of transport activity.
I105 (≠ Q131) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E148) mutation to A: Loss of transport activity.
Q137 (= Q163) mutation to A: Loss of transport activity.
Q250 (vs. gap) mutation to A: Loss of transport activity.
Q251 (vs. gap) mutation to A: Loss of transport activity.
N256 (≠ T263) mutation to A: Loss of transport activity.
W357 (≠ G374) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.

O15244 Solute carrier family 22 member 2; Organic cation transporter 2; hOCT2 from Homo sapiens (Human) (see 8 papers)
24% identity, 77% coverage: 75:423/451 of query aligns to 162:499/555 of O15244

query
sites
O15244

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F

L

A

V

I

S

G

K

G

A

E

G

W

W

S

L

G

I

A

G

A

Y

L

I

V

L

A

I

T

T

E

E

N

F

A

V

P

G

A

R

G

R

K

Y

R

R

A

R

L

T

F

V

G

G

T

I

F

F

P
x
Y

Q

Q

L

V

G

A

A

Y

P

T

L

V

G

G

F

L

I

L

I

V

A

L

N

A

G

G

L

-

F

-

L

-

I

-

V

V

A

A

A
x
Y

A

A

L

L

P

P

-

H

-

W

-

R

-

W

-

L

S

Q

D

F

D

T

P

V

S
|
S

R

L

P

P

S

N

E

F

A

F

F

F

L

L

D

L

W
x
Y

G
x
Y

W

W

R

C

I

I

P
|
P

-
x
E

-
x
S

-
x
P

-
x
R

F

W

L

L

F

I

S

S

A

Q

V

N

M

K

V

N

I

A

I

E

G

A

L

M

W

R

I

I

R

I

L

K

N

H

L

I

V

A

E

K

S

K

K

N

T

G

F

K

S

S

K

L

T

P

V

A

S

S

A

L

G

Q

K

R

V

L

-

R

V

L

K

E

L

E

P

E

L

T

G

G

E

K

V

K

M

L

R

N

K

P

N

S

W

F

R

L

E

D

L

L

I

V

L

R

G

T

T

P

F

Q

Y

I

M

R

L

K

A

H

T

T

Y

M

V

I

L

L

F

M

Y

Y

L

N

M

W

T

F

T

T

F

S

S

S

L

V

S

L

Y
|
Y

G

-

R

-

A

-

P

-

I

-

E

-

P

-

A

-

A

Q

G

G

Q

L

L

I

S

M

G

H

L

M

G

G

Y

L

S

A

Y

G

N

D

N

N

F

I

V
x
Y

L

L

M

D

L

F

I

F

V

Y

G

S

-

A

-

L

V

V

V

E

F

F

F

P

G

A

I

A

F

F

T

M

L

I

S

-

G

-

L

L

V

T

A

I

D

D

R
|
R

L

I

G

G

R

R

K

Y

T

P

L

W

I

A

L

A

V

S

T

N

L

M

-

V

-

A

G

G

I

A

G

C

F

L

S

A

L

S

L

V

W

F

V

I

P

P

L

-

N

-

M

-

G

-

F

-

V

-

G

G

V

D

M

L

A

Q

W

W

L

L

I
x
K

L

I

G

I

F

I

S

S

L

C

M

L

G

G

-

R

-

M

-

G

-

I

-

T

M

M

T

A

F

Y

G

E

P

I

M

V

G

C

A

L

L

V

L

N

P

A

E

E

L

L

F
x
Y

P

P

T

T

N

F

V

I

R

R

Y

N

T

L

G

G

S

V

G

H

I

I

S

C

Y

S

N

S

V

M

S

C

S

D

I

I

L

-

G

G

A

G

A

I

V

I

A

T

P

P

F

F

I

L

A

V

V

Y

W

R

L

L

W

T

S

N

V

I

G

W

D

L

G

E

S

L

P

P

F

L

L

M

V

V

M165 (≠ V78) to I: lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177507
Y169 (≠ H82) mutation to F: No change in TEA uptake.
T201 (≠ G117) to M: in dbSNP:rs145450955
Y241 (≠ P162) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-362 and F-377.
Y257 (≠ A182) mutation to F: No change in TEA uptake.
S270 (= S190) to A: decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs316019
Y279 (≠ W199) mutation to F: No change in TEA uptake.
Y280 (≠ G200) mutation to F: No change in TEA uptake.
P284 (= P204) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
PESPR 284:288 (≠ P---- 204) Proline-rich sequence
S286 (vs. gap) mutation to A: No change in TEA and metformin uptake. No change in tyrosine phosphorylation.
P287 (vs. gap) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
Y362 (= Y277) mutation to F: Decreased TEA uptake and YES1-mediated tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-241. Strong decrease in TEA uptake; when associated with F-377. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-377.
Y377 (≠ V300) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-362.
R400 (= R323) to C: lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol; dbSNP:rs8177516
K432 (≠ I360) to Q: lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177517
Y458 (≠ F381) mutation to F: No change in TEA uptake.

Sites not aligning to the query:

54 P → S: in dbSNP:rs8177504
73 Y→F: No change in TEA uptake.
92 Y→F: No change in TEA uptake.
128 Y→F: No change in TEA uptake.
544 Y→F: No change in TEA uptake.

8bvtA Cryo-em structure of rat slc22a6 bound to probenecid (see paper)
22% identity, 76% coverage: 70:410/451 of query aligns to 133:462/508 of 8bvtA

query
sites
8bvtA

M

M

I

V

A

G

R

V

P

L

L

L

G

G

A

A

V

M

F

V

F

F

G

G

H

Y

L

L

G

A

D

D

K

R

V

L

G

G

R

R

K

R

K

K

T

V

L

L

I

I

Y

L

A

N

L

Y

F

L

T

Q

M

T

G

A

V

V

A

S

T

G

F

T

L

C

I

A

G

A

L

Y

L

A

P

P

T

N

Y

Y

H

-

A

-

I

-

G

-

W

-

A

-

P

-

L

T

L

V

L

Y

V

C

I

V

M

F

R

R

L

L

A

L

Q

S

G

G

F

M

A

S

I

L

G

A

G

S

E

I

W

A

S

I

G

N

A

C

A
x
M

L

T

V

L

A

N

T

V

E

E

N

W

A

M

P

P

A

I

G

H

K

T

R

R

A

A

L

Y

F

V

G

G

T

T

F

L

P

-

Q

-

L

-

G

-

A

-

P

-

L
x
I

G

G

F

Y

I

V

I
x
Y

A

S

N

L

G

G

L

Q

F

F

L

L

I

L

-

A

-

G

V

I

A

A

A

Y

A

A

L

V

P

P

S

H

D

-

P

-

S

W

R

R

P

H

S

L

E

Q

A

L

F

V

L

V

D

S

W

V

G

P

W

F

R

F

I

I

P

A

F

F

L

I

F

Y

S

S

A

W

V

F

M

F

V

I

I

E

I

S

G

A

L

R

W

W

I

Y

-

S

-

G

R

R

L

L

N

D

L

L

V

T

E

L

S

R

K

A

T

L

F

Q

S

R

K

V

T

A

V

R

S

I

A

N

G

G

K

K

V

Q

-

E

-

G

V

A

K

K

L

L

P

S

L

I

G

-

E

E

V

V

M

L

R

R

K

T

N

S

W

L

R

Q

E

K

L

E

I

L

L

T

G

S

T

A

F

M

Y

E

M

L

L

L

A

R

T

C

Y

P

V

T

L

L

F

R

Y

H

L

L

M

F

T

L

T

C

F

L

S

S

L

M

S

L

Y

W

G

F

R

A

A

T

P

S

I

F

E

A

P

Y

A
x
Y

A

G

G

L

Q

V

L

M

S

D

G

L

L

Q

G

G

Y

F

S

G

Y

V

N

S

N

M

F

Y

V

L

L

I

M

Q

L

V

I

I

V

F

G

G

V

A

V

V

F

D

F

L

G

P

I

A

F

-

T

K

L

F

L

V

S

C

G

F

L

L

V

V

A

I

D

N

R

S

L

M

G

G

R

R

K

P

T

A

L

Q

I

-

L

M

V

A

T

S

L

L

G

L

I

L

I

A

G

G

F

I

S

C

L

I

L

L

W

V

V

N

P

G

L

I

N

P

M

K

G

S

F

H

V

T

G

I

V

I

M

R

A

T

W

S

L

L

-

A

I

V

L

L

G

G

F

K

S

G

L

C

M

L

G

A

M

S

T

S

F

F

G

N

P

C

M

I

G

F

A

L

L

Y

L

T

P

G

E

E

L

L

F

Y

P

P

T

T

N

V

V

I

R

R

Y

Q

T

T

G

G

S

L

G

G

I

M

S

G

Y

S

N

T

V

M

S

A

S

R

I

V

L

-

G

G

A

S

A

I

V

V

A

S

P

P

F

L

I

V

A

S

V

M

binding 4-(dipropylsulfamoyl)benzoic acid: M198 (≠ A143), I217 (≠ L168), Y221 (≠ I172), Y339 (≠ A285)

Sites not aligning to the query:

binding 4-(dipropylsulfamoyl)benzoic acid: 31, 35

8bvsA Cryo-em structure of rat slc22a6 bound to tenofovir (see paper)
22% identity, 76% coverage: 70:410/451 of query aligns to 124:453/502 of 8bvsA

query
sites
8bvsA

M

M

I

V

A

G

R

V

P

L

L

L

G

G

A

A

V

M

F

V

F

F

G

G

H

Y

L

L

G

A

D

D

K

R

V

L

G

G

R

R

K

R

K

K

T

V

L

L

I

I

Y

L

A

N

L

Y

F

L

T

Q

M

T

G

A

V

V

A

S

T

G

F

T

L

C

I

A

G

A

L

Y

L

A

P

P

T

N

Y

Y

H

-

A

-

I

-

G

-

W

-

A

-

P

-

L

T

L

V

L

Y

V

C

I

V

M

F

R

R

L

L

A

L

Q

S

G

G

F

M

A

S

I

L

G

A

G

S

E

I

W

A

S

I

G

N

A

C

A

M

L

T

V

L

A

N

T

V

E

E

N

W

A

M

P

P

A

I

G

H

K

T

R

R

A

A

L

Y

F

V

G

G

T

T

F

L

P

-

Q

-

L

-

G

-

A

-

P

-

L

I

G

G

F

Y

I

V

I
x
Y

A

S

N

L

G

G

L

Q

F

F

L

L

I

L

-

A

-

G

V

I

A

A

A

Y

A

A

L

V

P

P

S

H

D

-

P

-

S

W

R

R

P

H

S

L

E

Q

A

L

F

V

L

V

D

S

W

V

G

P

W

F

R

F

I

I

P

A

F

F

L

I

F

Y

S

S

A

W

V

F

M

F

V

I

I

E

I

S

G

A

L

R

W

W

I

Y

-

S

-

G

R

R

L

L

N

D

L

L

V

T

E

L

S

R

K

A

T

L

F

Q

S

R

K

V

T

A

V

R

S

I

A

N

G

G

K

K

V

Q

-

E

-

G

V

A

K

K

L

L

P

S

L

I

G

-

E

E

V

V

M

L

R

R

K

T

N

S

W

L

R

Q

E

K

L

E

I

L

L

T

G

S

T

A

F

M

Y

E

M

L

L

L

A

R

T

C

Y

P

V

T

L

L

F

R

Y

H

L

L

M

F

T

L

T

C

F

L

S

S

L

M

S

L

Y

W

G

F

R

A

A

T

P

S

I

F

E

A

P

Y

A
x
Y

A

G

G

L

Q

V

L

M

S

D

G

L

L

Q

G

G

Y

F

S

G

Y

V

N

S

N

M

F

Y

V

L

L

I

M

Q

L

V

I

I

V

F

G

G

V

A

V

V

F

D

F

L

G

P

I

A

F

-

T

K

L

F

L

V

S

C

G

F

L

L

V

V

A

I

D

N

R

S

L

M

G

G

R

R

K

P

T

A

L

Q

I

-

L

M

V

A

T

S

L

L

G

L

I

L

I

A

G

G

F

I

S

C

L

I

L

L

W

V

V

N

P

G

L

I

N

P

M

K

G

S

F

H

V

T

G

I

V

I

M

R

A

T

W

S

L

L

-

A

I

V

L

L

G

G

F

K

S

G

L

C

M

L

G

A

M

S

T

S

F

F

G

N

P

C

M

I

G

F

A

L

L

Y

L

T

P

G

E

E

L

L

F

Y

P

P

T

T

N

V

V

I

R

R

Y

Q

T

T

G

G

S

L

G

G

I

M

S

G

Y

S

N

T

V

M

S

A

S

R

I

V

L

-

G

G

A

S

A

I

V

V

A

S

P

P

F

L

I

V

A

S

V

M

binding [2-(6-amino-9h-purin-9-yl)-1-methylethoxy]methylphosphonic acid: Y212 (≠ I172), Y330 (≠ A285)

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
22% identity, 74% coverage: 75:408/451 of query aligns to 162:484/555 of Q9R0W2

query
sites
Q9R0W2

L

I

G

G

A

A

V

M

F

M

F

I

G

G

H

Y

L

L

G

A

D

D

K

R

V

F

G

G

R

R

K

K

K

F

T

C

L

L

I

L

Y

V

A

T

L

I

F

L

T

I

M

N

G

A

V

I

A

S

T

G

F

A

L

L

I

M

G

A

L

I

L

S

P

P

T

N

Y

Y

H

-

A

-

I

-

G

A

W

W

W

-

A

-

P

-

L

-

L

M

V

L

I

V

M

F

R

R

L

F

A

L

Q

Q

G

G

F

L

A

V

I

S

G

K

G

A

E

G

W

W

S

L

G

I

A

G

A

Y

L

I

V

L

A

I

T

T

E

E

N

F

A

V

P

G

A

L

G

G

K

Y

R

R

A

R

L

M

F

V

G

G

T

I

F

C

P

Y

Q

Q

L

I

G

A

A

F

P

T

L

V

G

G

-

L

-

I

-

L

-

A

-

G

-

V

-

A

F

Y

I

V

I

I

A

P

N

N

G

W

L

R

F

W

L

L

I

Q

V

F

A

A

A

V

A

T

L

L

P

-

S

-

D

-

P

-

S

-

R

-

P

P

S

N

E

F

A

C

F

F

L

L

D

L

W

Y

G

F

W

W

R

C

I

I

P

P

-

E

-

S

-

P

-

R

F

W

L

L

F

I

S

S

A

Q

V

N

M

K

V

I

I

V

I

K

G

A

L

M

W

K

I

I

R

I

L

K

N

H

L

I

V

A

E

K

S

K

K

N

T

G

F

K

S

S

K

V

T

P

V

V

S

S

A

L

G

Q

K

N

V

L

V

T

-

P

K

D

L

E

P

D

L

A

G

G

E

K

V

K

M

L

R

N

K

P

N

S

W

F

R

L

E

D

L

L

I

V

L

R

G

T

T

P

F

Q

Y

I

M

R

L

K

A

H

T

T

Y

L

V

I

L

L

F

M

Y

Y

L

N

M

W

T

F

T

T

F

S

S

S

L

V

S

L

Y

Y

G

-

R

-

A

-

P

-

I

-

E

-

P

-

A

-

A

Q

G

G

Q

L

L

I

S

M

G

H

L

M

G

G

Y

L

S

A

Y

G

N

D

N

N

F

I

V

Y

L

L

M

D

L

F

I

F

V

Y

G

S

-

A

-

L

V

V

V

E

F

F

F

P

G

A

I

A

F

F

T

I

L

I

S

-

G

-

L

L

V

T

A

I

D

D

R

R

L

V

G

G

R

R

K

Y

T

P

L

W

I

A

L

V

V

S

T

N

L

M

-

V

-

A

G

G

I

A

G

C

F

L

S

A

L

S

L

V

W

F

V

I

P

P

L

-

N

-

M

-

G

-

F

-

V

-

G

D

V

D

M

L

A

Q

W

W

L

L

I

K

L

I

G

T

F

I

S

A

L

C

M

L

G

G

-

R

-

M

-

G

-

I

-

T

M

M

T

A

F

Y

G

E

P

M

M

V

G
x
C

A

L

L

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

N

Y

V

I

R

R

Y

N

T

L

G

G

S

V

G

L

I

V

S

C

Y

S

N

S

V

M

S

C

S

D

I

I

L

-

G

G

A

G

A

I

V

I

A

T

P

P

F

F

I

L

C451 (≠ G374) Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; mutation to M: Transport activity strongly reduced.

Q7KWJ5 Hexose transporter 1; PfHT1 from Plasmodium falciparum (isolate 3D7) (see 5 papers)
22% identity, 87% coverage: 3:393/451 of query aligns to 6:431/504 of Q7KWJ5

query
sites
Q7KWJ5

E

K

N

D

I

I

V

C

S

S

S

E

Q

N

E

E

A

G

P

K

A

K

N

N

S

G

R

K

S

S

-

G

-

F

-

S

-

T

-

S

-

F

R

K

V

Y

M

V

L

L

A

S

S

A

L

C

V

I

G

A

T

S

T

F

I

I

E

F

F

G

Y

Y

D

Q

F

V

Y

S

V

V

Y

L

A
x
N

T

T

A

I

A
x
K

V

N

L

F

V

I

F

V

P

V

H

E

L

F

F

E

F

W

P
x
C

P

K

G

G

-

E

-

K

-

D

-

R

-

L

N

N

E
x
C

T

S

I

N

A

N

L

T

L

I

A

Q

S

S

F

S

A

F

I

L

F

L

G

A

A

S

A

V

M

F

I

I

A

G

R

A

P

V

L

L

G

G

A

C

V

G

F

F

F

S

G

G

H

Y

L

L

G

V

D

-

K

Q

V

F

G

G

R

R

K

R

K

L

T

S

L

L

-

L

-

I

I

I

Y

Y

A

N

L

F

F

F

T

F

M

L

G

-

V

-

A

V

T

S

F

I

L

L

I

T

G

S

L

I

L

T

P

H

T

H

Y

F

H

H

A

T

I

I

G

-

W

-

A

-

P

-

L

-

V

L

I

F

M

A

R

R

L

L

A

L

Q

S

G

G

F

F

A

G

I

I

G

G

G

L

E

V

W

T

S

V

G

S

A

V

A

P

L

M

V

Y

A

I

T

S

E

E

N

M

A

T

P

H

A

K

G

D

K

K

R

K

A

G

L

A

F

Y

G

G

T

V

F

M

P
x
H

Q
|
Q

L

L

G

F

A

I

P

T

L

F

G

G

F

I

I

F

I

V

A

A

N

V

G

M

L

L

F

G

L

L

I

A

V

M

A

G

A

E

A

G

L

-

P

P

S

K

D

A

D

D

P

S

S

T

R

E

P

P

S

L

E

T

A

S

F

F

L

A

D

K

W

L

G

W

W

W

R

R

I

L

P

M

F

F

L

L

F

F

S

P

A

S

V

V

M

I

V

S

I

L

I

I

G

G

-

I

-

L

-

A

-

L

-

V

-

F

-

K

-

E

-

T

-

P

-

Y

-

F

L

L

W

F

I

E

R

K

L

G

N

R

L

I

V

E

E

E

S

S

K

K

T

N

F

I

S

L

K

K

T

K

V

I

S

Y

A

E

G

T

K

D

V

N

V

V

K

D

L

E

P

P

L

L

G

N

-

A

-

I

-

K

E

E

V

A

M

V

R

E

K

Q

N

N

W

E

-

S

-

A

R

K

E

K

L

N

I

S

L

L

G

S

T

L

F

L

Y

S

M

A

L

L

A

K

T

I

Y

P

V

S

L

Y

F

R

Y

Y

L

V

M

I

T

I

T

L

F

G

S

C

L

L

S

L

Y
x
S

G
|
G

R
x
L

A
x
Q

P
x
Q

I

F

E

T

P

G

A
x
I

A
x
N

G

V

Q

L

L
x
V

S
|
S

G
x
N

L
x
S

G
x
N

Y
x
E

S

L

Y

Y

N

K

N

E

F

F

V

L

-

D

-

S

-

H

L

L

M

I

L

T

I

I

V

L

G

S

V

V

F

M

F

T

G

A

I

V

F
x
N

T

F

L

L

L

M

S

T

G

F

-

P

-

A

-

I

L

Y

V

I

A

V

D

E

R

K

L

L

G

G

R

-

R

R

K

K

T

T

L

L

I

L

L

L

V

-

T

-

L

W

G

G

I

C

I

V

G

G

F

V

S

L

L

V

L

A

W

Y

V

L

P

P

L

T

-

A

-

I

-

A

-

N

-

E

-

I

-

N

L

R

N

N

M

S

G

N

F

F

V

V

G

K

V

I

M

L

A

S

W

I

-

V

-

A

-

T

-

F

-

V

L

M

I

I

L

I

G

S

F
|
F

S
x
A

L

V

M

-

G

-

M

-

T

S

F

Y

G

G

P

P

-

V

M

L

G
x
W

A

I

L

Y

L

L

P

H

E

E

L

M

F

F

P

P

T

S

N

E

V

I

R

K

Y

D

T

S

G

A

S

A

G

S

I

L

S

A

N48 (≠ A38) mutation to A: Reduces D-glucose and D-fructose transport activity.
K51 (≠ A41) mutation to A: Reduces D-glucose and D-fructose transport activity. Reduces susceptibility to inhibition by compound HTI-1. Reduces susceptibility to inhibition by compound HTI-1; when associated with A-447.; mutation to Q: Reduces D-glucose and D-fructose transport activity.
C61 (≠ P51) modified: Disulfide link with 70
C70 (≠ E55) modified: Disulfide link with 61
H168 (≠ P162) mutation to N: Reduces D-glucose and D-fructose transport activity.
Q169 (= Q163) binding alpha-D-glucose; binding beta-D-glucose; mutation to A: Abolishes D-glucose and D-fructose transport activity.; mutation to N: In one study, shown to abolish D-glucose and D-fructose transport activity. In another study, shown to abolish D-fructose transport with no significant effects on D-glucose uptake and affinity. Reduces susceptibility to inhibition by compound 3361.
S302 (≠ Y277) mutation to A: No significant effects on affinity for D-glucose and D-fructose.
SGL 302:304 (≠ YGR 277:279) mutation to AGT: No significant effects on affinity for D-glucose and D-fructose.
L304 (≠ R279) mutation to T: No significant effects on affinity for D-glucose and D-fructose.
Q305 (≠ A280) binding alpha-D-glucose; binding beta-D-glucose; mutation to A: Reduces D-glucose and D-fructose transport activity.
Q306 (≠ P281) binding alpha-D-glucose; mutation to A: Reduces D-glucose and D-fructose transport activity.
I310 (≠ A285) mutation to A: Reduces D-glucose and D-fructose transport activity.
N311 (≠ A286) binding alpha-D-glucose; binding beta-D-glucose; mutation to A: Reduces D-glucose and D-fructose transport activity.
V314 (≠ L289) mutation to F: Reduces D-glucose and D-fructose transport activity.
S315 (= S290) mutation to A: No significant effects on D-glucose and D-fructose transport activities. Reduces turnover number for D-glucose.; mutation to Y: Reduces D-glucose and D-fructose transport activity.
N316 (≠ G291) mutation N->A,Y: Reduces D-glucose and D-fructose transport activity.
S317 (≠ L292) mutation to A: Reduces D-glucose and D-fructose transport activity.
N318 (≠ G293) mutation to A: Reduces D-glucose and D-fructose transport activity.
E319 (≠ Y294) mutation to A: No significant effects on D-glucose and D-fructose transport activities. Reduces turnover number for D-glucose.
N341 (≠ F313) binding beta-D-glucose; mutation to A: Abolishes D-glucose and D-fructose transport activity.
F403 (= F363) mutation to A: Reduces D-glucose and D-fructose transport activity.
A404 (≠ S364) mutation to E: Modestly reduces D-glucose and D-fructose transport activities and affinities for these substrates.
W412 (≠ G374) binding alpha-D-glucose; mutation to A: Reduces D-fructose transport with no significant effect on D-glucose uptake.

Sites not aligning to the query:

435 N→A: Reduces D-fructose transport with no significant effect on D-glucose uptake.
436 W→A: Reduces D-glucose and D-fructose transport activity.
439 A→N: Reduces D-glucose and D-fructose transport activity.
447 D→A: Reduces susceptibility to inhibition by compound HTI-1; when associated with A-51.

Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 36% coverage: 68:231/451 of query aligns to 91:254/583 of Q9Y7Q9

query
sites
Q9Y7Q9

A

A

A

T

M

N

I

I

A

G

R

N

P

I

L

M

G

G

A

Q

V

L

F

L

F

F

G

G

H

F

L

L

G

G

D

D

K

F

V

F

G

G

R

R

K

K

K

F

T

V

L

Y

I

G

Y

K

A

E

L

M

F

M

T

V

M

V

G

I

V

I

A

A

T

T

F

I

L

L

I

I

G

I

L

C

L

L

P

P

T

D

Y

R

H

I

A

P

I

T

G

P

W

T

W

A

A

K

P

M

L

M

L

W

L

L

V

F

I

A

M

F

R

R

L

V

A

M

Q

L

G

G

F

I

A

G

I

I

G

G

E

D

W

Y

S

P

G

M

A

S

A

A

L

S

V

I

A

T

T

S

E

E

N

Q

A

S

P

L

A

I

G

N

K

R

R

R

A

-

L

-

F

-

G

-

T

-

F

-

P

-

Q

-

L

-

G

G

A

A

P

L

L

L

G

A

F

W

I

I

I

F

A

S

N

N

G

Q

-

G

-

W

-

G

-

T

-

L

-

A

-

G

-

C

-

V

L

A

F

T

L

L

I

I

V

I

A

L

A

A

A

C

L

F

P

E

S

K

D

P

D

L

P

N

S

D

R

R

P

G

S

E

E

Y

A

T

F

K

L

L

D

N

W

G

G

V

W

W

R

R

I

I

P

Q

F

F

-

G

-

I

-

A

L

L

F

F

S

P

A

A

V

V

M

I

V

V

I

L

I

I

G

P

L

-

W

-

I

-

R

R

L

L

N

R

L

M

V

Q

E

E

S

S

K

E

T

Q

F

F

S

K

K

N

T

S

Sites not aligning to the query:

267 modified: Phosphoserine
269 modified: Phosphoserine
289 modified: Phosphoserine
290 modified: Phosphoserine
292 modified: Phosphoserine
330 modified: Phosphoserine

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
23% identity, 83% coverage: 75:447/451 of query aligns to 160:518/532 of 8et8A

query
sites
8et8A

L

L

G

G

A

S

V

L

F

G

F

V

G

G

H

Y

L

I

G

A

D

D

K

R

V

F

G

G

R

R

K

K

K

L

T

C

L

L

I

L

Y

A

A

T

L

T

F

L

T

I

M

S

G

A

V

V

A

S

T

G

F

V

L

L

I

M

G

A

L

V

L

A

P

P

T

D

Y

Y

H

T

A

S

I

-

G

-

W

-

A

-

P

-

L

-

L

M

V

L

I

L

M

F

R

R

L

L

A

L

Q

Q

G

G

F

L

A

V

I

S

G
x
K

G

G

E

S

W
|
W

S

M

G

S

A

G

A

Y

L

T

V

L

A

I

T

T

E

E

N

F

A

V

P

G

A

S

G

G

K

Y

R

R

A

R

L

T

F

V

G

A

T

I

F

L

P

Y

Q
|
Q

L

M

G

A

A

F

P

T

L

V

G

G

F

L

I

V

I

L

A

L

N

S

G

G

L

-

F

-

L

-

I

-

V

V

A

A

A

Y

A

A

L

I

P

P

-

H

-

W

-

R

-

W

-

L

S

Q

D

L

D

A

P

V

S

S

R

L

P

P

S

T

E

F

A

L

F

F

L

L

D

L

W

Y

G

Y

W

W

R

C

I

V

P

P

-

E

-

S

-

P

-

R

F

W

L

L

F

L

S

S

A

Q

V

K

M

R

V

N

I

T

I

Q

G

A

L

I

W

K

I

I

R

-

L

M

N

D

L

H

V

I

E

A

S

Q

K

K

T

N

F

G

S

K

K

L

T

P

V

P

S

A

A

D

G

L

K

K

V

M

V

L

K

S

L

L

P

K

L

E

G

D

-

S

-

T

E

E

V

K

M

L

R

S

K

P

N

S

W

F

R

A

E

D

L

L

I

F

L

R

G

T

T

P

F

Q

Y

L

M

R

L

K

A

H

T

T

Y

F

V

I

L

L

F

M

Y

Y

L

L

M
x
W

T

F

T

T

F

S

S

S

L

V

S

L

Y
|
Y

G

-

R

-

A

-

P

-

I

-

E

-

P

-

A

-

A

Q

G

G

Q

L

L

I

S

M

G

H

L

M

G

G

Y

A

S

T

Y

G

N

G

N

N

F

L

V

Y

L

L

M

D

L
x
F

I

F

V

Y

G
x
S

-

A

-

L

V

V

V
x
E

F

F

F

P

G

A

I

A

F

F

T

I

L

I

L

L

S

-

G

-

L

V

V

T

A

I

D

D

R

R

L

V

G

G

R

R

R

I

K

Y

T

P

L

L

I

A

L

V

V

S

T

N

L

L

G

-

I

V

I

A

G

G

F

A

S

A

L

C

L

L

W

I

V

M

P

I

L

F

L

I

N

S

M

Q

G

D

F

-

V

-

G

-

V

-

M

L

A

H

W

W

L

L

I

N

L

I

G

T

F

V

S

A

L

C

M

V

G

G

-

R

-

M

-

G

-

I

-

T

M

I

T

V

F

F

G

Q

P

M

M

V

G
x
C

A

L

L

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

N

F

V

I

R

R

Y

N

T

L

G

G

S

V

G

M

I

V

S

C

Y
x
S

N

S

V

L

S

C

S

D

I

-

L

L

G

G

A

G

A

I

V

I

A

T

P

P

F

F

I

L

A

V

V

F

W

R

L

L

W

M

S

E

V

V

G

W

D

Q

G

G

S

L

P

P

F

L

L

I

V

L

G

-

V

-

Y

-

L

-

A

-

S

-

M

-

A

-

F

-

I

F

T

T

L

V

I

V

A

G

L

L

V

V

V

A

G

G

-

G

-

M

-

T

-

L

K

P

E

E

T

T

K

K

N

G

V

V

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G136), W216 (= W139), Q240 (= Q163), W353 (≠ M270), Y360 (= Y277), F378 (≠ L303), S381 (≠ G306), E385 (≠ V308), C449 (≠ G374), S469 (≠ Y394)

Sites not aligning to the query:

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: 31, 35

8et7A Cryo-em structure of the organic cation transporter 1 in complex with diphenhydramine (see paper)
23% identity, 83% coverage: 75:447/451 of query aligns to 160:518/532 of 8et7A

query
sites
8et7A

L

L

G

G

A

S

V

L

F

G

F

V

G

G

H

Y

L

I

G

A

D

D

K

R

V

F

G

G

R

R

K

K

K

L

T

C

L

L

I

L

Y

A

A

T

L

T

F

L

T

I

M

S

G

A

V

V

A

S

T

G

F

V

L

L

I

M

G

A

L

V

L

A

P

P

T

D

Y

Y

H

T

A

S

I

-

G

-

W

-

A

-

P

-

L

-

L

M

V

L

I

L

M

F

R

R

L

L

A

L

Q

Q

G

G

F

L

A

V

I

S

G

K

G

G

E

S

W

W

S

M

G

S

A

G

A

Y

L

T

V

L

A

I

T

T

E

E

N

F

A

V

P

G

A

S

G

G

K

Y

R

R

A

R

L

T

F

V

G

A

T

I

F

L

P

Y

Q

Q

L

M

G

A

A

F

P

T

L

V

G

G

F

L

I

V

I

L

A

L

N

S

G

G

L

-

F

-

L

-

I

-

V

V

A

A

A

Y

A

A

L

I

P

P

-

H

-

W

-

R

-

W

-

L

S

Q

D

L

D

A

P

V

S

S

R

L

P

P

S

T

E

F

A

L

F

F

L

L

D

L

W

Y

G

Y

W

W

R

C

I

V

P

P

-

E

-

S

-

P

-

R

F

W

L

L

F

L

S

S

A

Q

V

K

M

R

V

N

I

T

I

Q

G

A

L

I

W

K

I

I

R

-

L

M

N

D

L

H

V

I

E

A

S

Q

K

K

T

N

F

G

S

K

K

L

T

P

V

P

S

A

A

D

G

L

K

K

V

M

V

L

K

S

L

L

P

K

L

E

G

D

-

S

-

T

E

E

V

K

M

L

R

S

K

P

N

S

W

F

R

A

E

D

L

L

I

F

L

R

G

T

T

P

F

Q

Y

L

M

R

L

K

A

H

T

T

Y

F

V

I

L

L

F

M

Y

Y

L

L

M

W

T

F

T

T

F

S

S

S

L

V

S

L

Y

Y

G

-

R

-

A

-

P

-

I

-

E

-

P

-

A

-

A

Q

G

G

Q

L

L

I

S

M

G

H

L

M

G

G

Y

A

S

T

Y

G

N

G

N

N

F

L

V

Y

L

L

M

D

L

F

I

F

V

Y

G

S

-

A

-

L

V

V

V
x
E

F

F

F

P

G

A

I

A

F

F

T

I

L

I

L

L

S

-

G

-

L

V

V

T

A

I

D

D

R

R

L

V

G

G

R

R

R

I

K

Y

T

P

L

L

I

A

L

V

V

S

T

N

L

L

G

-

I

V

I

A

G

G

F

A

S

A

L

C

L

L

W

I

V

M

P

I

L

F

L

I

N

S

M

Q

G

D

F

-

V

-

G

-

V

-

M

L

A

H

W

W

L

L

I

N

L

I

G

T

F

V

S

A

L

C

M

V

G

G

-

R

-

M

-

G

-

I

-

T

M

I

T

V

F
|
F

G

Q

P

M

M

V

G

C

A

L

L

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

N

F

V

I

R

R

Y

N

T

L

G

G

S

V

G

M

I

V

S

C

Y

S

N

S

V

L

S

C

S

D

I

-

L

L

G

G

A

G

A

I

V

I

A

T

P

P

F

F

I

L

A

V

V

F

W

R

L

L

W

M

S

E

V

V

G

W

D

Q

G

G

S

L

P

P

F

L

L

I

V

L

G

-

V

-

Y

-

L

-

A

-

S

-

M

-

A

-

F

-

I

F

T

T

L

V

I

V

A

G

L

L

V

V

V

A

G

G

-

G

-

M

-

T

-

L

K

P

E

E

T

T

K

K

N

G

V

V

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: E385 (≠ V308), F445 (= F370)

Sites not aligning to the query:

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: 35

6m20B Crystal structure of plasmodium falciparum hexose transporter pfht1 bound with glucose (see paper)
24% identity, 76% coverage: 53:393/451 of query aligns to 50:410/478 of 6m20B

query
sites
6m20B

G

S

N

N

E

N

T

T

I

I

A

Q

L

-

A

S

S

S

F

F

A

-

I

L

F

L

G

A

A

S

A

V

M

F

I

I

A

G

R

A

P

V

L

L

G

G

A

C

V

G

F

F

F

S

G

G

H

Y

L

L

G

V

D

-

K

Q

V

F

G

G

R

R

K

R

K

L

T

S

L

L

-

L

-

I

I

I

Y

Y

A

N

L

F

F

F

T

F

M

L

G

-

V

-

A

V

T

S

F

I

L

L

I

T

G

S

L

I

L

T

P

H

T

H

Y

F

H

H

A

T

I

I

G

-

W

-

A

-

P

-

L

-

V

L

I

F

M

A

R

R

L

L

A

L

Q

S

G

G

F

F

A

G

I

I

G

G

G

L

E

V

W

T

S

V

G

S

A

V

A

P

L

M

V

Y

A

I

T

S

E

E

N

M

A

T

P

H

A

K

G

D

K

K

R

K

A

G

L

A

F

Y

G

G

T

V

F

M

P

H

Q
|
Q

L

L

G

F

A

I

P

T

L

F

G

G

F

I

I

F

I

V

A

A

N

V

G

M

L

L

F

G

L

L

I

A

V

M

A

G

A

E

A

G

L

-

P

P

S

K

D

A

D

D

P

S

S

T

R

E

P

P

S

L

E

T

A

S

F

F

L

A

D

K

W

L

G

W

W

W

R

R

I

L

P

M

F

F

L

L

F

F

S

P

A

S

V

V

M

I

V

S

I

L

I

I

G

G

-

I

-

L

-

A

-

L

-

V

-

F

-

K

-

E

-

T

-

P

-

Y

-

F

L

L

W

F

I

E

R

K

L

G

N

R

L

I

V

E

E

E

S

S

K

K

T

N

F

I

S

L

K

K

T

K

V

I

S

Y

A

E

G

T

K

D

V

N

V

V

K

D

L

E

P

P

L

L

G

N

-

A

-

I

-

K

E

E

V

A

M

V

R

E

K

Q

N

N

W

E

-

S

-

A

R

K

E

K

L

N

I

S

L

L

G

S

T

L

F

L

Y

S

M

A

L

L

A

K

T

I

Y

P

V

S

L

Y

F

R

Y

Y

L

V

M

I

T

I

T

L

F

G

S

C

L

L

S

L

Y

S

G

G

R

L

A
x
Q

P

Q

I

F

E

T

P

G

A

I

A
x
N

G

V

Q

L

L

V

S

S

G

N

L

S

G

N

Y

E

S

L

Y

Y

N

K

N

E

F

F

V

L

-

D

-

S

-

H

L

L

M

I

L

T

I

I

V

L

G

S

V

V

F

M

F

T

G

A

I

V

F

N

T

F

L

L

L

M

S

T

G

F

-

P

-

A

-

I

L

Y

V

I

A

V

D

E

R

K

L

L

G

G

R

-

R

R

K

K

T

T

L

L

I

L

L

L

V

-

T

-

L

W

G

G

I

C

I

V

G

G

F

V

S

L

L

V

L

A

W

Y

V

L

P

P

L

T

-

A

-

I

-

A

-

N

-

E

-

I

-

N

L

R

N

N

M

S

G

N

F

F

V

V

G

K

V

I

M

L

A

S

W

I

-

V

-

A

-

T

-

F

-

V

L

M

I

I

L

I

G

S

F

F

S

A

L

V

M

-

G

-

M

-

T

S

F

Y

G
|
G

P

P

-

V

M

L

G
x
W

A

I

L

Y

L

L

P

H

E

E

L

M

F

F

P

P

T

S

N

E

V

I

R

K

Y

D

T

S

G

A

S

A

G

S

I

L

S

A

binding beta-D-glucopyranose: Q148 (= Q163), Q284 (≠ A280), N290 (≠ A286), G387 (= G371), W391 (≠ G374)

8jttA Hoct1 in complex with metformin in outward occluded conformation (see paper)
24% identity, 77% coverage: 76:423/451 of query aligns to 84:420/454 of 8jttA

query
sites
8jttA

G

G

A

S

V

L

F

G

F

V

G

G

H

Y

L

F

G

A

D

D

K

R

V

F

G

G

R

R

K

K

K

L

T

C

L

L

I

L

Y

G

A

T

L

V

F

L

T

V

M

N

G

A

V

V

A

S

T

G

F

V

L

L

I

M

G

A

L

F

L

S

P

P

T

N

Y

Y

H

M

A

S

I

-

G

-

W

-

A

-

P

-

L

-

L

M

V

L

I

L

M

F

R

R

L

L

A

L

Q

Q

G

G

F

L

A

V

I

S

G

K

G

G

E

N

W

W

S

M

G

A

A

G

A

Y

L

T

V

L

A

I

T

T

E

E

N

F

A

V

P

G

A

S

G

G

K

S

R

R

A

R

L

T

F

V

G

A

T

I

F

M

P

Y

Q

Q

L

M

G

A

A

F

P

T

L

V

G

G

F

L

I

V

I

A

A

L

N

T

G

G

L

L

F

-

L

-

I

-

V

-

A

A

A

Y

A

A

L

L

P

P

-

H

-

W

-

R

-

W

-

L

S

Q

D

L

D

A

P

V

S

S

R

L

P

P

S

T

E

F

A

L

F

F

L

L

D

L

W

Y

G

Y

W

W

R

C

I

V

P

P

-

E

-

S

-

P

-

R

F

W

L

L

F

L

S

S

A

Q

V

K

M

R

V

N

I

T

I

E

G

A

L

I

W

K

I

I

R

-

L

M

N

D

L

H

V

I

E

A

S

Q

K

K

T

N

F

G

S

K

K

L

T

P

V

P

S

A

A

D

G

L

K

K

V

M

V

L

K

S

L

L

P

E

-

E

-

D

L

V

G

T

E

E

V

K

M

L

R

S

K

P

N

S

W

F

R

A

E

D

L

L

I

F

L

R

G

T

T

P

F

R

Y

L

M

R

L

K

A

R

T

T

Y

F

V

I

L

L

F

M

Y

Y

L

L

M

W

T

F

T

T

F

D

S

S

L

V

S

L

Y
|
Y

G

Q

R

G

A

L

P

I

I

L

E

H

P

M

A

G

A

A

G

T

Q

S

L

-

S

-

G

-

L

-

G

G

Y

N

S

L

Y

Y

N

L

N

D

F

F

V

L

L

Y

M

S

L

A

I

L

V

V

G

E

V

I

-

P

-

G

V

A

F

F

F

I

G

A

I

L

F

I

T

T

L

I

L

-

S

-

G

-

L

-

V

-

A

-

D

D

R

R

L

V

G

G

R

R

R

I

K

Y

T

P

L

M

I

A

L

M

V

S

T

N

L

L

G

-

I

-

G

-

F

-

S

-

L

L

L

A

W

G

V

A

P

A

L

C

L

L

N

V

M

M

G

I

F

F

V

I

G

S

-

P

V

D

M

L

A

H

W

W

L

L

-

N

-

I