SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011188633.1 NCBI__GCF_000025945.1:WP_011188633.1 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 9 hits to proteins with known functional sites (download)

P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
34% identity, 94% coverage: 26:533/538 of query aligns to 68:578/595 of P54582

query
sites
P54582

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W101 (= W59) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
E135 (= E93) mutation to A: Strongly decreased betaine transport.
G149 (= G107) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
M150 (≠ I108) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
G151 (= G109) mutation to A: Nearly abolishes betaine transport.
I152 (≠ V110) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
IG 152:153 (≠ VG 110:111) binding glycine betaine
G153 (= G111) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
F156 (≠ L114) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
W189 (= W150) mutation to C: Mildly decreased betaine transport.
W194 (= W155) mutation to L: Strongly decreased betaine transport.
Y197 (= Y158) mutation to L: Nearly abolishes betaine transport.
R210 (= R171) mutation to A: Nearly abolishes betaine transport.
S253 (≠ A214) binding glycine betaine
G301 (= G261) mutation to L: Strongly decreased betaine transport.
N309 (= N269) mutation to A: Decreases affinity for sodium ions.
T351 (= T311) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
W362 (= W320) mutation to C: Strongly decreased betaine transport.
W366 (= W324) mutation to C: No effect on betaine transport.
F369 (= F327) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
W371 (= W329) mutation to L: No effect on betaine transport.
W373 (≠ L331) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
WWISW 373:377 (≠ LTIAW 331:335) binding glycine betaine
W374 (≠ T332) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
W377 (= W335) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
F380 (= F338) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
F384 (= F342) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
R387 (= R345) mutation to A: Mildly decreased betaine transport.
R392 (= R350) mutation to K: Moderately decreased betaine transport.

4llhA Substrate bound outward-open state of the symporter betp (see paper)
33% identity, 95% coverage: 26:536/538 of query aligns to 12:522/524 of 4llhA

query
sites
4llhA

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binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I108), G95 (= G109), D97 (≠ G111), W314 (≠ L331), W315 (≠ T332), W318 (= W335)
binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (≠ S509), R499 (≠ K513)
binding sodium ion: A91 (≠ S105), M94 (≠ I108), G95 (= G109), F405 (= F425), T408 (= T428), S409 (= S429)

3p03C Crystal structure of betp-g153d with choline bound (see paper)
34% identity, 91% coverage: 26:515/538 of query aligns to 12:497/508 of 3p03C

query
sites
3p03C

L

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S

D

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V

A

A

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A

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F

F

H

H

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M

V

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L

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L

L

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K

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binding choline ion: A92 (≠ C106), M94 (≠ I108), D97 (≠ G111), F320 (= F338)

B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
27% identity, 86% coverage: 51:515/538 of query aligns to 45:511/514 of B4EY22

query
sites
B4EY22

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

Y

M

M

A

V

L

I

C

M

I

F

I

G

V

G

G

W

F

F

G

W

V

L

A

V

I

F

S

G

K

R

Y

Y

G

A

N

K

L

K

T

R

L

L

G

G

Q

D

A

-

G

-

D

E

E

K

P

P

E

E

F

F

S

S

T

T

T

A

T

S

W

W

I

I

A

F

M

M

L

M

F

F

S

A

C

S

G

C

I

T

G

S

V

A

G

A

Y

V

V

L

L

F

W

W

G

G

A

S

A

I

E
|
E

P

I

M

Y

F

Y

H

Y

F

I

M

S

N

S

T

P

P

P

Y

F

G

G

A

M

V

E

A

G

G

Y

S

S

P

A

E

P

A

A

L

K

P

E

V

I

A

G

I

L

R

A

I

Y

A

S

S

L

F

F

H

H

W

W

G

G

I

P

H

L

C

P

W

W

M

A

G

T

Y

Y

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S

I

F

V

L

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L

V

C

A

I

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A

A

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P

F

A

F

F

F

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K

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M

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V

M

I

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R

L

P

S

S

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S

A

T

L

L

H

T

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

V

T

N

S

G

V

L

W

F

G

G

R

T

L

V

D

D

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N

I

F

G

Y

A

L

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A

A

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L

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G

L

G

A

L

M

S

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L

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G

L

L

G

A

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T

I

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C

A

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D

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A

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I

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I

A

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I

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L

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G

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A

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S

N

D

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V

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x
R

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Y

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L

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L

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M

C

L

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|
W

T

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F

C

Y

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W

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A

L

W

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W

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M

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L

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V

L

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D

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V

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I

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I

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L

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L

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A

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L

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L

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K

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L

A

L

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I

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N

L

M

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L

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A

L

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L

A

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D

N

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A

A

C

S

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Y

F

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V

L

A

A

M

M

-

S

-

T

-

C

-

R

L

S

M

M

S

K

K

E

G

G

A

A

Y

-

E

E

P

P

K

P

T

L

L

L

M

V

K

R

V

I

V

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W

W

G

S

A

V

F

L

L

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G

G

T

I

L

I

A

G

V

I

L

L

V

A

S

L

G

G

L

L

G

K

A

P

L

I

K

Q

S

T

A

A

C

I

I

I

I

A

A

G

G

G

A

C

P

P

F

L

G

F

I

F

G

V

M

N

I

I

F

M

M

V

L

T

W

L

S

S

L

F

L

I

K

K

D

D

L

A

K

K

S

V

E

H

M

W

Q

K

H

D

S

C

E

S

M

P

E

Y

K

T

R

Q

Q

K

E111 (= E119) mutation to A: Abolishes transport activity.
R262 (≠ N269) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
W316 (= W324) mutation to A: 2.5-fold decrease in Vmax.
M331 (≠ V339) mutation to V: 10-fold decrease in Vmax.

P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
27% identity, 85% coverage: 51:508/538 of query aligns to 45:504/504 of P31553

query
sites
P31553

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

Y

M

M

A

V

L

V

C

M

I

L

I

F

V

G

G

W

F

F

G

W

V

L

A

V

I

F

S

G

K

P

Y

Y

G

A

N

K

L

K

T

R

L

L

G

G

Q

N

A

-

G

-

D

E

E

P

P

P

E

E

F

F

S

S

T

T

T

A

T

S

W

W

I

I

A

F

M

M

L

M

F

F

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A

C

S

G

C

I

T

G

S

V

A

G

A

Y

V

V

L

L

F

W

W

G

G

A

S

A

I

E

E

P

I

M

Y

F
x
Y

H

Y

F

I

M

S

N

T

T

P

P

P

Y

F

G

G

A

L

V

E

A

P

G

N

S

S

P

T

E

G

A

A

L

K

P

E

V

L

A

G

I

L

R

A

I

Y

A

S

S

L

F

F

H

H

W
|
W

G

G

I

P

H

L

C

P

W

W

M

A

G

T

Y

Y

S

S

I

F

V

L

G

S

L

V

C

A

I

F

A

A

F

Y

P

F

A

F

F

F

-

V

R

R

Q

K

N

M

R

E

P

V

M

I

T

R

L

P

S

S

V

S

A

T

L

L

H

V

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

A

T

K

S

G

V

L

W

F

G

G

R

T

L

I

L

V

D

D

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N

I

F

G

Y

A

L

I

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A

A

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L

V

I

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F

G

A

L

M

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A

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L

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L

L

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L

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A

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A

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N

D

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V

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L

L

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D

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V

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L

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x
M

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P
x
R

M

M

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L

F

F

Y

Y

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|
T

D

D

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P

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S

G

K

G

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F

F

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x
G

W
|
W

T

T

L

V

F

F

C

Y

W

W

L

A

L
x
W

T
x
W

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A

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x
Y

A
|
A

P
x
I

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x
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x
M

G

S

G

I

F

F

I

L

A

A

R

R

I

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S

R

R

G

G

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M

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H

D

Y114 (≠ F122) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
W142 (= W150) binding (R)-carnitine
D288 (≠ N295) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
M295 (≠ S302) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
R299 (≠ P306) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
T304 (= T311) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
GW 315:316 (≠ SW 323:324) binding 4-(trimethylamino)butanoate
W316 (= W324) mutation to L: Decrease in transport activity.
W323 (≠ L331) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
WW 323:324 (≠ LT 331:332) binding (R)-carnitine
W324 (≠ T332) mutation to L: Abolishes transport activity.
Y327 (≠ W335) mutation to L: Strong decrease in transport activity.
YAIQ 327:330 (≠ WAPF 335:338) binding (R)-carnitine
Q330 (≠ F338) mutation to L: Decrease in transport activity.
M331 (≠ V339) binding 4-(trimethylamino)butanoate

3hfxA Crystal structure of carnitine transporter (see paper)
27% identity, 85% coverage: 51:508/538 of query aligns to 34:493/493 of 3hfxA

query
sites
3hfxA

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

Y

M

M

A

V

L

V

C

M

I

L

I

F

V

G

G

W

F

F

G

W

V

L

A

V

I

F

S

G

K

P

Y

Y

G

A

N

K

L

K

T

R

L

L

G

G

Q

N

A

-

G

-

D

E

E

P

P

P

E

E

F

F

S

S

T

T

T

A

T

S

W

W

I

I

A

F

M

M

L

M

F

F

S

A

C

S

G

C

I

T

G

S

V

A

G

A

Y

V

V

L

L

F

W

W

G

G

A

S

A

I

E

E

P

I

M

Y

F
x
Y

H

Y

F

I

M

S

N

T

T

P

P

P

Y

F

G

G

A

L

V

E

A

P

G

N

S

S

P

T

E

G

A

A

L

K

P

E

V

L

A

G

I

L

R

A

I

Y

A

S

S

L

F

F

H

H

W
|
W

G

G

I

P

H

L

C

P

W

W

M

A

G

T

Y

Y

S

S

I

F

V

L

G

S

L

V

C

A

I

F

A

A

F

Y

P

F

A

F

F

F

-

V

R

R

Q

K

N

M

R

E

P

V

M

I

T

R

L

P

S

S

V

S

A

T

L

L

H

V

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

A

T

K

S

G

V

L

W

F

G

G

R

T

L

I

L

V

D

D

T

N

I

F

G

Y

A

L

I

V

A

A

T

L

V

I

G

F

G

A

L

M

S

G

T

T

A

S

L

L

G

G

L

L

G

A

I

T

I

P

S

L

L

V

S

T

Y

E

G

C

A

M

G

Q

L

W

I

L

F

F

G

G

I

I

E

P

V

H

G

T

V

L

G

Q

G

L

K

D

L

A

L

I

I

I

M

I

A

T

I

C

I

W

I

I

G

I

L

L

Y

N

V

A

I

I

S

C

A

V

I

A

T

C

G

G

L

L

H

Q

R

K

G

G

M

V

A

R

F

I

L

A

S

S

N

D

V

V

N

R

I

S

I

Y

L

L

A

S

I

F

S

L

W

M

C

L

L

G

F

W

I

V

L

F

I

I

F

V

G

S

E

G

T

A

N

S

T

F

L

I

L

M

R

N

L

Y

L

F

V

T

N

D

N

S

V

V

G

G

S

M

Y

L

V

L

S

M

E

Y

F

L

I

P

P

R

M

M

T

L

F

F

Y

Y

T

T

D

D

P

P

L

I

Q

A

Q

K

H

-

S

G

K

G

W

F

F

P

S

Q

S

G

W
|
W

T

T

L

V

F

F

C

Y

W

W

L

A

L
x
W

T
x
W

I

V

A

I

W
x
Y

A

A

P

I

F
x
Q

V

M

G

S

G

I

F
|
F

I

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

G

E

F

L

I

C

V

F

G

G

A

M

V

V

L

L

A

G

P

L

T

T

A

A

F

S

S

T

L

W

V

I

W

L

F

W

T

T

I

V

V

L

G

G

G

S

S

N

S

T

I

L

L

L

A

L

E

I

M

D

N

K

Q

N

T

I

A

I

P

N

M

I

W

P

T

N

S

L

I

I

S

E

A

Q

-

Y

D

G

V

V

G

A

S

R

G

A

I

I

Y

I

M

E

L

T

L

W

S

A

T

A

L

L

P

P

F

L

A

S

K

T

L

A

L

T

S

M

I

W

I

G

V

F

F

F

I

I

N

L

M

C

I

F

L

I

F

A

L

T

V

V

T

T

S

L

A

V

D

N

S

A

A

C

S

S

F

Y

F

T

V

L

A

A

M

M

L

S

M

T

S

C

-

R

-

E

-

V

K

R

G

D

A

G

Y

E

E

E

P

P

K

P

T

L

L

L

M

V

K

R

V

I

V

G

W

W

G

S

A

I

F

L

L

V

G

G

T

I

L

I

A

G

V

I

V

V

L

L

V

A

S

L

G

G

L

L

G

K

A

P

L

I

K

Q

S

T

A

A

C

I

I

I

I

A

A

G

G

G

A

C

P

P

F

L

G

F

I

F

G

V

M

N

I

I

F

M

M

V

L

T

W

L

S

S

L

F

L

I

K

K

D

D

L

A

K

K

S

Q

E

N

M

W

Q

K

H

D

binding carnitine: Y103 (≠ F122), W131 (= W150), W305 (= W324), W312 (≠ L331), W313 (≠ T332), Y316 (≠ W335), Y316 (≠ W335), Q319 (≠ F338), F323 (= F342)

2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 85% coverage: 51:507/538 of query aligns to 50:508/508 of 2wswA

query
sites
2wswA

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

Y

M

M

A

V

L

I

C

M

I

F

I

G

V

G

G

W

F
|
F

G

W

V

L

A

V

I
x
F

S

G

K
x
R

Y

Y

G

A

N

K

L

K

T

R

L

L

G

G

Q

D

A

-

G

-

D

E

E

K

P

P

E

E

F

F

S

S

T

T

T

A

T

S

W

W

I

I

A

F

M

M

L

M

F

F

S

A

C

S

G

C

I

T

G

S

V

A

G

A

Y

V

V

L

L

F

W

W

G

G

A

S

A

I

E

E

P

I

M

Y

F

Y

H

Y

F

I

M

S

N

S

T

P

P

P

Y

F

G

G

A

M

V

E

A

G

G

Y

S

S

P

A

E

P

A

A

L

K

P

E

V

I

A

G

I

L

R

A

I

Y

A

S

S

L

F

F

H

H

W

W

G

G

I

P

H

L

C

P

W

W

M

A

G

T

Y

Y

S

S

I

F

V

L

G

S

L

V

C

A

I

F

A

A

F

Y

P

F

A

F

F

F

-

V

R

R

Q

K

N

M

R

E

P

V

M

I

T

R

L

P

S

S

V

S

A

T

L

L

H

V

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

V

T

N

S

G

V

L

W

F

G

G

R

T

L

V

D

D

T

N

I

F

G

Y

A

L

I

V

A

A

T

L

V

I

G

L

G

A

L

M

S

G

T

T

A

S

L

L

G

G

L

L

G

A

I

T

I

P

S

L

L

V

S

T

Y

E

G

C

A

I

G

Q

L

Y

I

L

F

F

G

G

I

I

E

P

V

H

G

T

V

L

G

Q

G

L

K

D

L

A

L

I

I

I

M

I

A

S

I

C

I

W

I

I

G

L

L

L

Y

N

V

A

I

I

S

C

A

V

I

A

T

F

G

G

L

L

H

Q

R

K

G

G

M

V

A

K

F

I

L

A

S

S

N

D

V

V

N

R

I

T

I

Y

L

L

A

S

I

F

S

L

W

M

C

L

L

G

F

W

I

V

L

F

I

I

F

V

G

G

E

G

T

A

N

S

T

F

L

I

L

V

R

N

L

Y

L

F

V

T

N

D

N

S

V

V

G

G

S

T

Y

L

V

L

S

M

E

Y

F

M

I

P

P

R

M

M

T

L

F

F

Y

Y

T

T

D

D

P

P

L

I

Q

G

Q

K

H

-

S

G

K

G

W

F

F

P

S

Q

S

A

W

W

T

T

L

V

F

F

C

Y

W

W

L

A

L

W

T

W

I

V

A

I

W

Y

A

A

P

I

F

Q

V

M

G

S

G

I

F

F

I

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

G

E

F

L

I

C

V

L

G

G

A

M

V

V

L

S

A

G

P

L

T

T

A

A

F

G

S

T

L

W

V

L

W

I

F

W

T

T

I

I

V

L

G

G

S

N

S

T

I

L

-

Q

L

L

A

I

E

D

M

Q

N

N

Q

I

T

L

A

N

P

I

M

P

W

Q

T

L

S

I

I

D

S

Q

A

Y

D

G

V

V

G

P

S

R

G

A

I

I

Y

I

M

E

L

T

L

W

S

A

T

A

L

L

P

P

F

L

A

S

K

T

L

A

L

T

S

M

I

W

I

G

V

F

F

F

I

I

N

L

M

C

I

F

L

I

F

A

L

T

V

V

T

T

S

L

A

I

D

N

S

A

A

C

S

S

F

Y

F

T

V

L

A

A

M

M

-

S

-

T

-

C

-

R

L

S

M

M

S

K

K

E

G

G

A

A

Y

-

E

D

P

P

K

P

T

L

L

L

M

V

K

R

V

I

V

G

W

W

G

S

A

V

F

L

L

V

G

G

T

I

L

I

A

G

V

I

L

L

V

A

S

L

G

G

L

L

G

K

A

P

L

I

K

Q

S

T

A

A

C

I

I

I

I

A

A

G

G

G

A

C

P

P

F

L

G

F

I

F

G

V

M

N

I

I

F

M

M

V

L

T

W

L

S

S

L

F

L

I

K

K

D

D

L

A

K

K

S

V

E

H

M

W

Q

K

binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: F72 (= F73), F76 (≠ I77), R78 (≠ K79)

4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
27% identity, 85% coverage: 51:507/538 of query aligns to 37:495/495 of 4m8jA

query
sites
4m8jA

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

Y

M

M

A

V

L

I

C

M

I

F

I

G

V

G

G

W

F

F

G

W

V

L

A

V

I

F

S

G

K

R

Y

Y

G

A

N

K

L

K

T

R

L

L

G

G

Q

D

A

-

G

-

D

E

E

K

P

P

E

E

F

F

S

S

T

T

T

A

T

S

W

W

I

I

A

F

M

M

L

M

F

F

S

A

C

S

G

C

I

T

G

S

V

A

G

A

Y

V

V

L

L

F

W

W

G

G

A

S

A

I

E

E

P

I

M

Y

F

Y

H

Y

F

I

M

S

N

S

T

P

P

P

Y

F

G

G

A

M

V

E

A

G

G

Y

S

S

P

A

E

P

A

A

L

K

P

E

V

I

A

G

I

L

R

A

I

Y

A

S

S

L

F

F

H

H

W

W

G

G

I

P

H

L

C

P

W
|
W

M

A

G

T

Y

Y

S

S

I

F

V

L

G

S

L

V

C

A

I

F

A

A

F

Y

P

F

A

F

F

F

-

V

R

R

Q

K

N

M

R

E

P

V

M

I

T

R

L

P

S

S

V

S

A

T

L

L

H

V

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

V

T

N

S

G

V

L

W

F

G

G

R

T

L

V

D

D

T

N

I

F

G

Y

A

L

I

V

A

A

T

L

V

I

G

L

G

A

L

M

S

G

T

T

A

S

L

L

G

G

L

L

G

A

I

T

I

P

S

L

L

V

S

T

Y

E

G

C

A

I

G

Q

L

Y

I

L

F

F

G

G

I

I

E

P

V

H

G

T

V

L

G

Q

G

L

K

D

L

A

L

I

I

I

M

I

A

S

I

C

I

W

I

I

G

L

L

L

Y

N

V

A

I

I

S

C

A

V

I

A

T

F

G

G

L

L

H

Q

R

K

G

G

M

V

A

K

F

I

L

A

S

S

N

D

V

V

N

E

I

T

I

Y

L

L

A

S

I

F

S

L

W

M

C

L

L

G

F

W

I

V

L

F

I

I

F

V

G

G

E

G

T

A

N

S

T

F

L

I

L

V

R

N

L

Y

L

F

V

T

N

D

N

S

V

V

G

G

S

T

Y

L

V

L

S

M

E

Y

F

M

I

P

P

R

M

M

T

L

F

F

Y

Y

T

T

D

D

P

P

L

I

Q

G

Q

K

H

-

S

G

K

G

W

F

F

P

S

Q

S

A

W

W

T

T

L

V

F

F

C

Y

W

W

L

A

L
x
W

T
x
W

I

V

A

I

W

Y

A

A

P

I

F

Q

V

M

G

S

G

I

F

F

I

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

G

E

F

L

I

C

V

L

G

G

A

M

V

V

L

S

A

G

P

L

T

T

A

A

F

G

S

T

L

W

V

L

W

I

F

W

T

T

I

I

V

L

G

G

S

N

S

T

I

L

-

Q

L

L

A

I

E

D

M

Q

N

N

Q

I

T

L

A

N

P

I

M

P

W

Q

T

L

S

I

I

D

S

Q

A

Y

D

G

V

V

G

P

S

R

G

A

I

I

Y

I

M

E

L

T

L

W

S

A

T

A

L

L

P

P

F

L

A

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K

T

L

A

L

T

S

M

I

W

I

G

V

F

F

F

I

I

N

L

M

C

I

F

L

I

F

A

L

T

V

V

T

T

S

L

A

I

D

N

S

A

A

C

S

S

F

Y

F

T

V

L

A

A

M

M

-

S

-

T

-

C

-

R

L

S

M

M

S

K

K

E

G

G

A

A

Y

-

E

D

P

P

K

P

T

L

L

L

M

V

K

R

V

I

V

G

W

W

G

S

A

V

F

L

L

V

G

G

T

I

L

I

A

G

V

I

L

L

V

A

S

L

G

G

L

L

G

K

A

P

L

I

K

Q

S

T

A

A

C

I

I

I

I

A

A

G

G

G

A

C

P

P

F

L

G

F

I

F

G

V

M

N

I

I

F

M

M

V

L

T

W

L

S

S

L

F

L

I

K

K

D

D

L

A

K

K

S

V

E

H

M

W

Q

K

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W139 (= W155), W315 (≠ L331), W316 (≠ T332)

2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 85% coverage: 51:507/538 of query aligns to 38:496/496 of 2wsxA

query
sites
2wsxA

A

S

Y

Y

I

V

A

T

D

N

T

V

F

W

G

G

W

W

L

A

Y

F

V

E

S

W

I

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M

M

A

V

L

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M

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L

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G

K

P

Y

Y

G

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N

K

L

K

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L

L

G

G

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A

-

G

-

D

E

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P

P

P

E

E

F

F

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S

T

T

T

A

T

S

W

W

I

I

A

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M

M

L

M

F

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C

I

T

G

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A

G

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V

V

L

L

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W

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G

A

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A

I

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I

M

Y

F

Y

H

Y

F

I

M

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N

T

T

P

P

P

Y

F

G

G

A

L

V

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A

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G

N

S

S

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T

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G

A

A

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K

P

E

V

L

A

G

I

L

R

A

I

Y

A

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S

L

F

F

H

H

W
|
W

G

G

I

P

H

L

C

P

W

W

M

A

G

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Y

Y

S

S

I

F

V

L

G

S

L

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C

A

I

F

A

A

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Y

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F

A

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V

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R

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K

N

M

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P

V

M

I

T

R

L

P

S

S

V

S

A

T

L

L

H

V

G

P

L

L

L

V

G

G

D

E

K

K

A

H

S

A

T

K

S

G

V

L

W

F

G

G

R

T

L

I

L

V

D

D

T

N

I

F

G

Y

A

L

I

V

A

A

T

L

V

I

G

F

G

A

L

M

S

G

T

T

A

S

L

L

G

G

L

L

G

A

I

T

I

P

S

L

L

V

S

T

Y

E

G

C

A

M

G

Q

L

W

I

L

F

F

G

G

I

I

E

P

V

H

G

T

V

L

G

Q

G

L

K

D

L

A

L

I

I

I

M

I

A

T

I

C

I

W

I

I

G

I

L

L

Y

N

V

A

I

I

S

C

A

V

I

A

T

C

G

G

L

L

H

Q

R

K

G

A

M

V

A

R

F

I

L

A

S

S

N

D

V

V

N

R

I

S

I

Y

L

L

A

S

I

F

S

L

W

M

C

L

L

G

F

W

I

V

L

F

I

I

F

V

G

S

E

G

T

A

N

S

T

F

L

I

L

M

R

N

L

Y

L

F

V

T

N

D

N

S

V

V

G

G

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M

Y

L

V

L

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M

E

Y

F

L

I

P

P

R

M

M

T

L

F

F

Y

Y

T

T

D

D

P

P

L

I

Q

A

Q

K

H

-

S

G

K
x
G

W

F

F

P

S

Q

S
x
G

W

W

T

T

L

V

F

F

C

Y

W

W

L

A

L
x
W

T

W

I

V

A

I

W
x
Y

A

A

P

I

F

Q

V
x
M

G

S

G

I

F

F

I

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

G

E

F

L

I

C

V

F

G

G

A

M

V

V

L

L

A

G

P

L

T

T

A

A

F

S

S

T

L

W

V

I

W

L

F

W

T

T

I

V

V

L

G

G

G

S

S

N

S

T

I

L

L

L

A

L

E

I

M

D

N

K

Q

N

T

I

A

L

P

N

M

I

W

P

T

N

S

L

I

I

S

E

A

Q

-

Y

D

G

V

V

G

A

S

R

G

A

I

I

Y

I

M

E

L

T

L

W

S

A

T

A

L

L

P

P

F

L

A

S

K

T

L

A

L

T

S

M

I

W

I

G

V

F

F

F

I

I

N

L

M

C

I

F

L

I

F

A

L

T

V

V

T

T

S

L

A

V

D

N

S

A

A

C

S

S

F

Y

F

T

V

L

A

A

M

M

L

S

M

T

S

C

-

R

-

E

-

V

K

R

G

D

A

G

Y

E

E

D

P

P

K

P

T

L

L

L

M

V

K

R

V

I

V

G

W

W

G

S

A

I

F

L

L

V

G

G

T

I

L

I

A

G

V

I

V

V

L

L

V

A

S

L

G

G

L

L

G

K

A

P

L

I

K
x
Q

S

T

A

A

C

I

I

I

I

A

A

G

G

G

A

C

P

P

F

L

G

F

I

F

G

V

M

N

I

I

F

M

M

V

L

T

W

L

S

S

L

F

L

I

K

K

D

D

L

A

K

K

S

Q

E

N

M

W

Q

K

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W135 (= W150), G304 (≠ K319), G308 (≠ S323), W316 (≠ L331), Y320 (≠ W335), M324 (≠ V339), Q466 (≠ K477)

Query Sequence

>WP_011188633.1 NCBI__GCF_000025945.1:WP_011188633.1
MSKQKNNLMTRLLGQYDPFLFYTTALVTLAIVVFGAIYPEILGKYAMAGRAYIADTFGWL
YVSIMALCIIVGFGVAISKYGNLTLGQAGDEPEFSTTTWIAMLFSCGIGVGYVLWGAAEP
MFHFMNTPYGAVAGSPEALPVAIRIASFHWGIHCWMGYSIVGLCIAFPAFRQNRPMTLSV
ALHGLLGDKASTSVWGRLLDTIGAIATVGGLSTALGLGIISLSYGAGLIFGIEVGVGGKL
LIMAIIIGLYVISAITGLHRGMAFLSNVNIILAISWCLFILIFGETNTLLRLLVNNVGSY
VSEFIPMTFYTDPLQQHSKWFSSWTLFCWLLTIAWAPFVGGFIARISRGRTIRGFIVGAV
LAPTAFSLVWFTIVGGSSILAEMNQTAPMWTSISADVGSGIYMLLSTLPFAKLLSIIVFI
NMILFLVTSADSASFFVAMLMSKGAYEPKTLMKVVWGAFLGTLAVVLLVSGGLGALKSAC
IIAGAPFGIGMIFMLWSLLKDLKSEMQHSEMEKRQSEIEQIEMLKSEILKSQLQKEAL

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