SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_009154436.1 NCBI__GCF_000244955.1:WP_009154436.1 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 11 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, 63% coverage: 28:306/446 of query aligns to 56:318/444 of Q8NLB7

query
sites
Q8NLB7

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D57 (= D29) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R82) mutation to A: Loss of transport activity.
W309 (≠ I297) mutation to V: Loss of transport activity.
D312 (= D300) mutation to A: Loss of transport activity.
R313 (= R301) mutation to A: Loss of transport activity.
I317 (≠ K305) mutation I->H,Y: Loss of transport activity.

Sites not aligning to the query:

54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
386 R→A: Loss of transport activity.

Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 41% coverage: 67:251/446 of query aligns to 94:291/583 of Q9Y7Q9

query
sites
Q9Y7Q9

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S267 (≠ K227) modified: Phosphoserine
S269 (≠ P229) modified: Phosphoserine
S289 (≠ I249) modified: Phosphoserine
S290 (≠ A250) modified: Phosphoserine

Sites not aligning to the query:

292 modified: Phosphoserine
330 modified: Phosphoserine

O15244 Solute carrier family 22 member 2; Organic cation transporter 2; hOCT2 from Homo sapiens (Human) (see 8 papers)
29% identity, 34% coverage: 42:192/446 of query aligns to 132:284/555 of O15244

query
sites
O15244

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M165 (≠ A74) 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 (≠ H78) mutation to F: No change in TEA uptake.
T201 (≠ A110) to M: in dbSNP:rs145450955
Y241 (≠ A158) 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 (vs. gap) mutation to F: No change in TEA uptake.
S270 (≠ G178) 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 (= Y187) mutation to F: No change in TEA uptake.
Y280 (≠ G188) mutation to F: No change in TEA uptake.
P284 (= P192) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.

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.
284:288 Proline-rich sequence
286 S→A: No change in TEA and metformin uptake. No change in tyrosine phosphorylation.
287 P→A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
362 Y→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.
377 Y→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.
400 R → 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
432 K → 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
458 Y→F: No change in TEA uptake.
544 Y→F: No change in TEA uptake.

6rw3A The molecular basis for sugar import in malaria parasites. (see paper)
22% identity, 53% coverage: 48:285/446 of query aligns to 36:276/437 of 6rw3A

query
sites
6rw3A

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binding beta-D-glucopyranose: Q138 (= Q159), Q264 (≠ D273), N270 (≠ T279)
binding alpha-D-glucopyranose: Q138 (= Q159), Q264 (≠ D273), I269 (≠ L278), N270 (≠ T279)

Sites not aligning to the query:

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
29% identity, 34% coverage: 42:192/446 of query aligns to 132:284/555 of Q9R0W2

query
sites
Q9R0W2

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Sites not aligning to the query:

451 Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; C→M: Transport activity strongly reduced.

Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
29% identity, 28% coverage: 42:167/446 of query aligns to 132:250/556 of Q63089

query
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Q63089

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A

C

G

G

T

D

L

A

A

W

A

K

F

V

S

D

A

L

F

F

A

Q

-

S

-
x
C

-

V

-

N

V

L

G

G

F

F

I

F

A

-

R

-

P

-

L

L

G

G

A

S

A

L

V

V

I

V

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

M
x
C

L

L

V

L

L

V

T

T

L

T

L

L

L

V

T

T

G

S

G

V

T

S

T

G

F

V

L

L

I

T

G

A

V

V

L

A

P

P

T

D

Y

Y

A

T

A

S

I

-

G

-

L

-

A

-

P

-

V

-

L

-

L

M

T

L

L

L

L

F

R

R

V

L

L

L

Q

Q

G

G

F
x
M

G
x
V

V
x
S

G
x
K

G
|
G

E
x
S

W
|
W

G
x
V

G
x
S

A
x
G

V
x
Y

L
x
T

I
x
L

A
x
I

T
|
T

E
|
E

H
x
F

A
x
V

S

G

P

S

R

G

R

Y

R

R

A

R

V

T

Y

T

G

A

S

I

F

L

A

Y

Q

Q

F

M

G

A

V

F

P

T

V

V

G

G

V

L

L

V

C155 (vs. gap) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
C179 (≠ M88) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474.
M212 (≠ F129) mutation to L: No change in TEA and MPP(+) uptake.
V213 (≠ G130) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
S214 (≠ V131) mutation to G: Decreased TEA and MPP(+) uptake.
K215 (≠ G132) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
G216 (= G133) mutation to A: Decreased TEA and MPP(+) uptake.
S217 (≠ E134) mutation to G: No change in TEA and MPP(+) uptake.
W218 (= W135) mutation to F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax.; mutation to Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
V219 (≠ G136) mutation to L: No change in TEA and MPP(+) uptake.
S220 (≠ G137) mutation to I: Decreased TEA and MPP(+) uptake.
G221 (≠ A138) mutation to A: Decreased TEA and MPP(+) uptake.
Y222 (≠ V139) mutation to F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
T223 (≠ L140) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
L224 (≠ I141) mutation to V: Decreased TEA and MPP(+) uptake.
I225 (≠ A142) mutation to G: No change in TEA and MPP(+) uptake.
T226 (= T143) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
E227 (= E144) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
F228 (≠ H145) mutation to I: No change in TEA and MPP(+) uptake.
V229 (≠ A146) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.

Sites not aligning to the query:

26 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
286 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550.
292 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550.
296 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550.
322 C→S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451.
328 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550.
358 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474.
418 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474.
437 C→S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474.
451 C→M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322.
470 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474.
474 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470.
475 D→E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; D→N: Decreased MPP(+) uptake.; D→R: Decreased MPP(+) uptake.
550 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328.

Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 65% coverage: 82:372/446 of query aligns to 108:429/514 of Q9LT15

query
sites
Q9LT15

R

K

I

H

G

G

R

R

K

K

-

V

S

S

M

M

L

F

V

I

L

-

T

-

L

-

T

-

G

G

T

L

T

A

F

F

L

L

I

I

G

G

V

A

L

L

P

F

T

N

Y

A

A

F

A

A

I

V

G

N

L

V

A

S

A

-

P

-

V

-

L

M

L

L

T

I

L

I

L

G

R

R

V

L

L

L

Q

L

G

G

F

V

G

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V

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G

G

F

E

A

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N

G

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A

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E
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E

H

M

A

A

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P

P

A

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K

R

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R

R

A

G

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A

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G

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F

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Q

F

M

G

A

V

I

P

T

V

I

G

G

V
x
I

L

L

T

V

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A

N

N

L

L

A

I

F

N

L

Y

S

G

V

T

S

S

G

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M

M

S

A

D

-

E

-

A

-

F

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L

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D

Q

Y

H

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G

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W

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L

G

F

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A

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I

V

G

R

S

S

F

R

I

L

L

R

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D

D

A

T

P

P

-

N

-

S

-

M

-

L

-

E

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R

-

G

E

K

F

N

E

E

K

E

A

A

K

K

Q

Q

-

M

-

L

-

K

-

I

-

R

-

G

-

A

-

D

-

N

-

V

-

D

-

H

-

E

H

F

K

Q

D

D

L

L

-

I

-

D

-

A

-

V

-

E

-

A

-

K

A

V

K

E

V

N

P

P

I

W

A

K

E

N

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M

R

E

Q

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Q

K

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Y

R

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-

P

N

A

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V

I

L

F

A

C

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S

L

A

A

I

S

P

I

F

A

F

P
x
Q

A

I

V

T

G

G

Y

I

T
x
N

V

V

I

I

V

M

Y

F

M

Y

L

A

T

P

Y

V

G

L

T

F

T

K

V

T

A

L

G

G

F

F

-

G

D

D

R

D

T

A

L

L

L

M

T

S

L

A

I

V

L

I

T

T

S

G

T

V

A

V

L
x
N

W

M

I

L

A

S

T

T

I

F

V

-

V

V

S

S

A

I

I

Y

L

A

S

V

D
|
D

R

R

F

Y

G

G

A

R

K

R

R

L

V

L

F

F

T

L

I

E

G

G

A

G

L

I

T

Q

A

M

V

F

L

I

W

C

P

Q

L

L

P

L

L

V

-

G

-

S

-

F

-

I

-

G

-

A

-

R

F

F

A

G

L

T

V

S

N

G

T

T

G

G

E

T

T

L

M

T

P

P

A

A

L

T

L

A

A

D

F

W

V

I

V

L

A

A

A

F

I

I

V

C

Q

V

G

Y

I

V

M

A

A

G

-

F

-

A

-

W

-

S

-

W

G

G

A

P

Q

L

G

G

G
x
W

L

L

F

V

-

P

S

S

E

E

I

I

F

C

P

P

M

L

R

E

V

I

R

R

Y

P

S

A

G

G

I

Q

S

A

I

I

G

N

E162 (= E144) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
Q177 (= Q159) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
I184 (≠ V166) mutation to A: Reduces affinity for glucose 3-fold.
Q295 (≠ P251) binding beta-D-glucose
Q296 (≠ P252) binding beta-D-glucose
N301 (≠ T257) binding beta-D-glucose
N332 (≠ L287) binding beta-D-glucose
D344 (= D300) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
W410 (≠ G354) binding beta-D-glucose

Sites not aligning to the query:

39 F→A: Reduces affinity for glucose 8-fold.
43 L→A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
77 modified: Disulfide link with 449; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
449 modified: Disulfide link with 77; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).

7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
25% identity, 65% coverage: 82:372/446 of query aligns to 88:409/487 of 7aaqA

query
sites
7aaqA

R

K

I

H

G

G

R

R

K

K

-

V

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S

M

M

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F

V

I

L

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T

-

L

-

T

-

G

G

T

L

T

A

F

F

L

L

I

I

G

G

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A

L

L

P

F

T

N

Y

A

A

F

A

A

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A

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P

-

V

-

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M

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L

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L

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L

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G

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A

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E

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A

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P

A

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F

G

A

F

Q
|
Q

F

M

G

A

V

I

P

T

V

I

G

G

V
x
I

L

L

T

V

S

A

N

N

L

L

A

I

F

N

L

Y

S

G

V

T

S

S

G

K

M

M

S

A

D

-

E

-

A

-

F

-

L

-

D

Q

Y

H

G

G

W

W

R

R

I

V

P

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F

L

L

G

F

L

S

A

I

A

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V

L

P

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A

V

V

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M

I

V

L

I

V

G

R

S

S

F

R

I

L

L

R

P

D

D

A

T

P

P

-

N

-

S

-

M

-

L

-

E

-

R

-

G

E

K

F

N

E

E

K

E

A

A

K

K

Q

Q

-

M

-

L

-

K

-

I

-

R

-

G

-

A

-

D

-

N

-

V

-

D

-

H

-

E

H

F

K

Q

D

D

L

L

-

I

-

D

-

A

-

V

-

E

-

A

-

K

A

V

K

E

V

N

P

P

I

W

A

K

E

N

L

I

F

M

R

E

Q

S

Q

K

P

Y

R

R

-

P

N

A

L

L

V

I

L

F

A

C

S

S

L

A

A

I

S

P

I

F

A

F

P
x
Q

P

Q

A

I

V

T

G

G

Y

I

T
x
N

V

V

I

I

V

M

Y

F

M

Y

L

A

T

P

Y

V

G

L

T

F

T

K

V

T

A

L

G

G

F

F

-

G

D

D

R

D

T

A

L

L

L

M

T

S

L

A

I

V

L

I

T

T

S

G

T

V

A

V

L
x
N

W

M

I

L

A

S

T

T

I

F

V

-

V

V

S

S

A

I

I

Y

L

A

S

V

D

D

R

R

F

Y

G

G

A

R

K

R

R

L

V

L

F

F

T

L

I

E

G

G

A

G

L

I

T

Q

A

M

V

F

L

I

W

C

P

Q

L

L

P

L

L

V

-

G

-

S

-

F

-

I

-

G

-

A

-

R

F

F

A

G

L

T

V

S

N

G

T

T

G

G

E

T

T

L

M

T

P

P

A

A

L

T

L

A

A

D

F

W

V

I

V

L

A

A

A

F

I

I

V

C

Q

V

G

Y

I

V

M

A

A

G

-

F

-

A

-

W

-

S

-

W

G
|
G

A

P

Q

L

G

G

G
x
W

L

L

F

V

-

P

S

S

E

E

I

I

F

C

P

P

M

L

R

E

V

I

R

R

Y

P

S

A

G

G

I

Q

S

A

I

I

G

N

binding beta-D-glucopyranose: Q157 (= Q159), I164 (≠ V166), Q275 (≠ P251), N281 (≠ T257), N312 (≠ L287), G386 (= G350), W390 (≠ G354)

O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
29% identity, 28% coverage: 42:167/446 of query aligns to 132:250/556 of O08966

query
sites
O08966

G

G

S

S

L

S

F

I

F

V

P

T

E

E

F

F

S

N

A

L

T

V

A

C

G

G

T

D

L

A

A

W

A

K

F

V

S

D

A

L

F

F

A

Q

-

S

-

C

-

V

-

N

V

L

G

G

F

F

I

F

A

-

R

-

P

-

L

L

G

G

A

S

A

L

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V

I

V

G

G

H

Y

F

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G

A

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D

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G

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R

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C

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L

L

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L

L

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T

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A

V

V

L

A

P

P

T

D

Y

Y

A

T

A

S

I

-

G

-

L

-

A

-

P

-

V

-

L

-

L

M

T

L

L

L

L

F

R

R

V

L

L

L

Q

Q

G

G

F

M

G

V

V

S

G

K

G

G

E

S

W

W

G

V

G

S

A

G

V

Y

L

T

I

L

A

I

T

T

E

E

H

F

A

V

S

G

P

S

R

G

R

Y

R

R

A

R

V

T

Y

T

G

A

S

I

F

L

A

Y

Q

Q

F

V

G

A

V

F

P

T

V

V

G

G

V

L

L

V

Sites not aligning to the query:

32 L→F: Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.
36 Y→C: Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
31% identity, 30% coverage: 60:192/446 of query aligns to 152:282/532 of 8et8A

query
sites
8et8A

S

S

A

C

F

V

A

N

V

V

G

G

F

F

I

F

A

-

R

-

P

-

L

L

G

G

A

S

A

L

V

G

I

V

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

M

C

L

L

V

L

L

A

T

T

L

T

L

L

L

I

T

S

G

A

G

V

T

S

T

G

F

V

L

L

I

M

G

A

V

V

L

A

P

P

T

D

Y

Y

A

T

A

S

I

-

G

-

L

-

A

-

P

-

V

-

L

-

L

M

T

L

L

L

L

F

R

R

V

L

L

L

Q

Q

G

G

F

L

G

V

V

S

G
x
K

G

G

E

S

W
|
W

G

M

G

S

A

G

V

Y

L

T

I

L

A

I

T

T

E

E

H

F

A

V

S

G

P

S

R

G

R

Y

R

R

A

R

V

T

Y

V

G

A

S

I

F

L

A

Y

Q
|
Q

F

M

G

A

V

F

P

T

V

V

G

G

-

L

V

V

L

L

T

L

S

S

N

G

L

V

A

A

F

Y

-

A

-

I

-

P

-

H

-

W

-

R

-

W

-

L

-

Q

L

L

S

A

V

V

S

S

G

-

M

L

S

P

D

T

E

F

A

L

F

F

L

L

D

L

Y

Y

G

Y

W

W

R

C

I

V

P

P

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G132), W216 (= W135), Q240 (= Q159)

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, 353, 360, 378, 381, 385, 449, 469

8et7A Cryo-em structure of the organic cation transporter 1 in complex with diphenhydramine (see paper)
31% identity, 30% coverage: 60:192/446 of query aligns to 152:282/532 of 8et7A

query
sites
8et7A

S

S

A

C

F

V

A

N

V

V

G

G

F

F

I

F

A

-

R

-

P

-

L

L

G

G

A

S

A

L

V

G

I

V

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

M

C

L

L

V

L

L

A

T

T

L

T

L

L

L

I

T

S

G

A

G

V

T

S

T

G

F

V

L

L

I

M

G

A

V

V

L

A

P

P

T

D

Y

Y

A

T

A

S

I

-

G

-

L

-

A

-

P

-

V

-

L

-

L

M

T

L

L

L

L

F

R

R

V

L

L

L

Q

Q

G

G

F

L

G

V

V

S

G

K

G

G

E

S

W

W

G

M

G

S

A

G

V

Y

L

T

I

L

A

I

T

T

E

E

H

F

A

V

S

G

P

S

R

G

R

Y

R

R

A

R

V

T

Y

V

G

A

S

I

F

L

A

Y

Q

Q

F

M

G

A

V

F

P

T

V

V

G

G

-

L

V

V

L

L

T

L

S

S

N

G

L

V

A

A

F

Y

-

A

-

I

-

P

-

H

-

W

-

R

-

W

-

L

-

Q

L

L

S

A

V

V

S

S

G

-

M

L

S

P

D

T

E

F

A

L

F

F

L

L

D

L

Y

Y

G

Y

W

W

R

C

I

V

P

P

Sites not aligning to the query:

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: 35, 385, 445

Query Sequence

>WP_009154436.1 NCBI__GCF_000244955.1:WP_009154436.1
MAVSQPGTTPSKRGIFAASFIGTSIEWYDYYIFGTAAALVFGSLFFPEFSATAGTLAAFS
AFAVGFIARPLGAAVIGHFGDRIGRKSMLVLTLLLTGGTTFLIGVLPTYAAIGLAAPVLL
TLLRVLQGFGVGGEWGGAVLIATEHASPRRRAVYGSFAQFGVPVGVLTSNLAFLSVSGMS
DEAFLDYGWRIPFLFSIVLVVVGILVRSRLRDAPEFEKAKQHKDLAKVPIAELFRQQPRN
LVLASLASIAPPAVGYTVIVYMLTYGTTVAGFDRTTLLTLILTSTALWIATIVVSAILSD
RFGAKRVFTIGALTAVLWPLPLFALVNTGETMPALLAFVVAAIVQGIMAGAQGGLFSEIF
PMRVRYSGISIGYQMGGMLGGALTPIVATALYGAYNSSTPIALYVAGMSLLSFLAVLGLR
TGHDNDTGESSRPATAEAGRRAELAE

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