SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 7024907 FitnessBrowser__ANA3:7024907 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)

P30878 Melibiose permease; Melibiose carrier; Melibiose transporter; Melibiose/cation symporter; Na+ (Li+)/melibiose symporter; Thiomethylgalactoside permease II from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
28% identity, 95% coverage: 5:463/481 of query aligns to 2:473/476 of P30878

query
sites
P30878

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K18 (≠ V21) mutation to C: Loss of transporter activity.
KD 18:19 (≠ VN 21:22) binding
D19 (≠ N22) mutation to C: Loss of transporter activity.
R52 (= R55) mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
D55 (= D58) mutation to C: Alters cation selectivity. Retains a low level of H(+)-coupled melibiose transport, but retains only a weak activity with Na(+) or Li(+).
N58 (≠ T61) mutation to C: Alters cation selectivity. Decreases H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
D59 (= D62) mutation to C: Alters cation selectivity. Retains only a low level of H(+)-coupled melibiose binding and active transport, but Na(+) or Li(+) does not stimulate either binding or transport.
Y120 (≠ F123) mutation to C: Loss of transporter activity.
T121 (= T124) mutation to C: Alters cation selectivity. Inhibits H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
M123 (≠ V126) mutation to C: Does not affect transporter activity.
D124 (≠ T127) binding ; mutation to C: Alters cation selectivity. Loss of transporter activity.
W128 (≠ I131) binding ; mutation to C: Loss of transporter activity.
R149 (≠ L152) binding ; mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
K377 (= K373) mutation to C: Inhibits Na(+)- and Li(+)-coupled activity, with little effect on H(+)-coupled melibiose transport.

7l17A Crystal structure of sugar-bound melibiose permease melb (see paper)
28% identity, 92% coverage: 5:445/481 of query aligns to 1:449/453 of 7l17A

query
sites
7l17A

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binding 4-nitrophenyl alpha-D-galactopyranoside: K17 (≠ V21), D18 (≠ N22), I21 (= I25), Y25 (≠ M29), Y119 (≠ F123), D123 (≠ T127), W127 (≠ I131), R148 (≠ L152), W341 (= W342), T372 (≠ S369), V375 (≠ Q372)

7l16A Crystal structure of sugar-bound melibiose permease melb (see paper)
28% identity, 92% coverage: 5:445/481 of query aligns to 1:449/453 of 7l16A

query
sites
7l16A

K

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K

binding dodecyl 6-O-alpha-D-galactopyranosyl-beta-D-glucopyranoside: K17 (≠ V21), D18 (≠ N22), I21 (= I25), Y25 (≠ M29), Y119 (≠ F123), D123 (≠ T127), W127 (≠ I131), R148 (≠ L152), F156 (= F160), S246 (≠ Y244), N250 (≠ G248), L271 (= L270), W341 (= W342), V375 (≠ Q372)

P02921 Melibiose permease; Melibiose carrier; Melibiose transporter; Melibiose/cation symporter; Na+ (Li+)/melibiose symporter; Thiomethylgalactoside permease II from Escherichia coli (strain K12) (see 5 papers)
24% identity, 92% coverage: 5:447/481 of query aligns to 2:460/473 of P02921

query
sites
P02921

K

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H

K18 (≠ V21) mutation to C: Abolishes transporter activity.
D19 (≠ N22) mutation to C: Abolishes transporter activity. Can bind Na(+). Large decrease in the affinity for melibiose in the presence of H(+).
D35 (= D38) mutation to C: Abolishes transporter activity.
R52 (= R55) mutation to C: Abolishes transporter activity.
D55 (= D58) mutation to C: Abolishes transporter activity. Chemical restoration of the charge via the oxidation of the thiol to the sulfinic and/or sulfonic acid results in partial recovery of transporter activity. Does not bind Na(+). Binds melibiose in the presence of H(+).
D59 (= D62) mutation to C: Loses ability to catalyze Na(+) or H(+)-coupled melibiose transport against a concentration gradient. Does not bind Na(+). Binds melibiose in the presence of H(+).
D124 (≠ T127) mutation to C: Abolishes transporter activity. Chemical restoration of the charge via the oxidation of the thiol to the sulfinic and/or sulfonic acid results in partial recovery of transporter activity. Can bind Na(+), but structural changes induced by Na(+) are less complete and of smaller amplitude. Large decrease in the affinity for melibiose in the presence of H(+).
K138 (≠ P141) mutation to C: Can transport melibiose.
R139 (≠ K142) mutation to C: Can transport melibiose.
R141 (= R144) mutation R->C,Q: Abolishes melibiose transport. Decreases affinity for melibiose.; mutation to K: Retains ion-coupled melibiose transport.
R149 (≠ L152) mutation to C: Abolishes melibiose transport.; mutation R->K,Q: Retains ion-coupled melibiose transport.
R199 (≠ L196) mutation to C: Does not affect transporter activity.
E203 (≠ C200) mutation to C: Does not affect transporter activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

Q9DA75 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; Mfsd2a from Mus musculus (Mouse) (see 2 papers)
22% identity, 97% coverage: 4:468/481 of query aligns to 38:529/534 of Q9DA75

query
sites
Q9DA75

H

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P

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E

Y55 (≠ V21) mutation to A: Significant reduction in LPC transport.
Q56 (≠ N22) mutation to A: Slightly reduced LPC transport.
F64 (≠ L30) mutation to A: Slightly increased LPC transport.
Q67 (≠ T33) mutation to H: Abolishes LPC transport.
S82 (≠ G48) mutation to A: No effect on LPC transport.
F86 (≠ L52) mutation to A: Slightly reduced LPC transport.
R89 (= R55) mutation to A: No effect on LPC transport.
D92 (= D58) mutation to A: Significant reduction in LPC transport. Abolishes LPC transport; when associated with A-96.
T95 (= T61) mutation to A: Significant reduction in LPC transport.
D96 (= D62) mutation to A: Abolishes LPC transport. Abolishes LPC transport; when associated with A-92.
E159 (≠ T120) mutation to A: Slightly reduced LPC transport.
T163 (= T124) mutation to A: Slightly reduced LPC transport.; mutation to M: Abolishes LPC transport.
H166 (≠ T127) mutation to A: Abolishes LPC transport.
P168 (= P129) mutation to T: Significant reduction in LPC transport.
S170 (≠ I131) mutation to L: Significant reduction in LPC transport.
R190 (= R151) mutation to A: Abolishes LPC transport.
E194 (≠ A155) mutation to A: Significant reduction in LPC transport.
T202 (= T163) mutation to A: Slightly increased LPC transport.; mutation to F: Significant reduction in LPC transport.; mutation to M: Significant reduction in LPC transport.
Q207 (vs. gap) mutation to A: Slightly reduced LPC transport.
C216 (≠ I168) modified: Disulfide link with 464; mutation to A: Significant reduction in LPC transport.
A254 (= A190) mutation to F: Abolishes LPC transport.
F305 (≠ C237) mutation to A: Significant reduction in LPC transport.
S309 (≠ T241) mutation to A: Significant reduction in LPC transport.
R330 (≠ D262) mutation to H: No effect on LPC transport.
Q334 (≠ L266) mutation to A: Slightly reduced LPC transport.
N335 (≠ S267) mutation to A: Significant reduction in LPC transport.
S343 (≠ A276) mutation to L: Significant reduction in LPC transport.
F403 (≠ A338) mutation to A: Significant reduction in LPC transport.
P406 (≠ F341) mutation to H: Significant reduction in LPC transport.
W407 (= W342) mutation to A: Significant reduction in LPC transport.
T439 (≠ Q372) mutation to A: No effect on LPC transport.
K440 (= K373) mutation to A: Abolishes LPC transport.
T451 (≠ G384) mutation to A: Slightly reduced LPC transport.
D455 (≠ T388) mutation to A: Slightly reduced LPC transport.
R461 (vs. gap) mutation to A: Slightly reduced LPC transport.
C464 (≠ E396) modified: Disulfide link with 216; mutation to A: Significant reduction in LPC transport.
P497 (≠ K429) mutation to L: Abolishes LPC transport.

F1NCD6 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; GgMFSD2A from Gallus gallus (Chicken) (see paper)
23% identity, 91% coverage: 6:444/481 of query aligns to 36:508/528 of F1NCD6

query
sites
F1NCD6

L

L

S

S

V

V

I

C

E

S

K

K

I

L

G

C

Y

Y

G

A

S

V

G

G

D

G

M

A

A

P

V

Y

N

Q

V

T

I

G

S

C

S

A

M

L

M

G

L

F

I

F

I

L

T

Q

F

I

F

Y

Y

L

T

L

D

D

I

V

F

A

G

Q

L

L

K

D

P

P

A

F

D

Y

V

A

G

S

I

I

L

I

F

L

L

F

L

V

V

G

R

R

L

A

I

W

D

D

A

A

I

I

T

T

D

D

P

P

L

M

M

V

G

G

I

F

N

I

D

S

K

K

V

T

T

P

-

W

T

T

R

R

W

F

G

G

R

R

Y

L

R

M

P

P

Y

W

F

I

L

I

F

F

M

-

A

S

I

T

P

P

F

F

G

A

-

V

I

I

S

S

V

Y

F

F

L

L

T

I

F

W

S

F

T

V

P

P

D

D

W

I

D

S

Y

-

N

T

A

G

K

Q

L

V

I

M

W

W

A

Y

Y

L

S

I

T

F

Y

Y

I

C

L

I

V

F

T

Q

I

T

I

L

F

V

T

T

T

C

V

F

T

H

I

V

P

P

Y

Y

I

S

S

A

I

L

I

T

S

M

V

F

I

I

T

S

D

R

D

E

P

Q

K

S

E

E

R

R

L

D

S

S

A

A

N

T

G

A

Y

Y

R

R

L

M

F

T

F

V

A

E

K

V

I

L

A

G

A

T

F

V

L

L

V

G

T

T

I

A

I

I

V

Q

-

G

-

Q

-

I

-

V

-

G

-

K

-

A

-

V

-

T

-

P

-
x
C

-

I

-

E

-

N

-

P

P

P

I

F

L

L

A

S

S

E

-

T

-
x
N

-

F

-

S

-

V

A

A

W

I

G

R

G

N

E

V

N
|
N

I

M

A

T

-

H

-

Y

-

T

-

G

-

S

-

L

A

A

G

D

Y

T

Q

R

K

N

A

A

M

Y

G

M

V

V

M

A

A

A

L

G

M

V

A

I

T

G

L

G

L

L

F

Y

L

I

F

L

C

C

F

A

F

V

T

I

T

L

T

S

E

V

R

G

V

V

A

R

Y

E

K

K

V

R

E

E

T

S

-

S

-

E

-

L

-

Q

-

S

-

D

K

E

P

P

V

V

G

S

M

F

-

F

-

R

Q

G

L

L

R

K

L

L

L

V

F

M

K

N

N

H

D

G

Q

A

W

Y

L

I

V

K

L

L

V

I

A

T

I

G

C

F

V

L

I

F

G

T

T

S

I

L

G

A

Y

F

V

M

I

L

R

L

G

E

S

G

V

N

A

F

A

A

Y

L

Y

F

A

C

T

T

Y

Y

Y

T

L

L

G

G

G

F

D

R

A

N

K

E

M

F

L

Q

S

N

A

I

F

L

L

L

S

A

T

I

G

M

V

L

G

-

A

S

A

A

I

T

L

L

A

T

M

I

V

P

A

F

S

W

T

Q

W

W

I

F

T

L

K

T

R

R

Y

F

C

G

K

K

L

-

K

-

L

-

F

-

R

-

Y

K

S

T

Q

A

I

V

V

Y

V

V

G

G

I

I

L

S

S

S

A

A

I

V

M

P

F

F

F

L

-

I

-

T

-

V

A

V

V

V

Q

L

P

D

G

S

D

N

I

L

V

V

L

V

A

T

F

Y

V

I

L

V

Y

A

F

V

A

A

I

A

S

G

F

I

V

S

V

V

D

A

L

A

H

A

A

F

P

L

V

L

F

P

W

W

S

S

V

M

I

L

S

P

E

D

S

V

V

I

D

D

Y

D

G

F

T

K

V

L

K

Q

-

H

-

P

-

E

-

S

T

R

G

G

H

H

R

E

V

-

S

-

G

A

L

I

A

F

F

F

G

S

G

F

I

Y

S

V

F

F

A

F

Q

T

K

K

A

F

G

T

M

S

G

G

A

V

A

S

G

L

F

G

V

I

V

S

G

T

M

L

L

S

L

L

T

D

Y

F

F

A

N

G

Y

Y

Q

Q

P

T

-

R

G

G

E
x
C

T

S

Q

Q

S

P

E

S

F

E

A

V

L

N

T

I

G

T

I

L

S

K

L

L

M

L

L

V

T

S

V

A

I

V

P

P

G

V

A

G

F

L

H

I

A

L

L

L

M

G

G

L

L

L

M

F

F

K

K

L

Y

Y

K

P

I

I

S

D

D

E

R

E

V

K

Y

R

E

R

E

E

I

N

K

K

Q

K

A

A

L

L

P

Q

E

D

C207 (vs. gap) modified: Disulfide link with 460
N218 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
N227 (= N177) modified: carbohydrate, N-linked (GlcNAc...) asparagine
C460 (≠ E396) modified: Disulfide link with 207

Q8NA29 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; HsMFSD2A; MFSD2a from Homo sapiens (Human) (see 6 papers)
22% identity, 94% coverage: 4:455/481 of query aligns to 39:538/543 of Q8NA29

query
sites
Q8NA29

H

Q

K

Q

L

L

S

S

V

V

I

C

E

N

K

K

I

L

G

C

Y

Y

G

A

S

L

G

G

D

G

M

A

A

P

V

Y

N
x
Q

V

V

V

T

I

G

S

C

S

A

M

L

M

G

L
x
F

I
x
F

I

L

T

Q

F

I

F

Y

Y

L

T

L

D
|
D

I

V

-

A

-

Q

-

K

-

D

-

E

-
x
V

-

V

-

F

-

C

-

F

-

S

F

F

G

Q

L

V

K

G

P

P

A

F

D

S

V

A

G

S

I

I

L

I

F

L

L

F

L

V

V

G

R
|
R

L

A

I

W

D
|
D

A

A

I

I

T

T

D
|
D

P

P

L

L

M

V

G

G

I

L

-

C

I

I

N

S

D

K

K

S

V

P

T

W

T

T

R

C

W

L

G

G

R

R

Y

L

R

M

P

P

Y

W

F

I

L

I

F

F

M

S

A

T

I

P

P

L

F

A

G

V

I

I

S

A

V

Y

F

F

L

L

T

I

F

W

S

F

T

V

P

P

D

D

W

F

D

P

Y

H

N

G

A

-

K

Q

L

T

I

Y

W

W

A

Y

Y

L

S

L

T

F

Y

Y

I

C

L

L

V

F

T

E

I

T

I

M

F

V

T
|
T

T

C

V

F

T

H

I

V

P
|
P

Y

Y

I
x
S

S

A

I

L

I

T

S

M

V

F

I

I

T

S

D

T

D

E

P

Q

K

T

E

E

R

R

L

D

S

S

A

A

N

T

G

A

Y

Y

R

R

L
x
M

F

T

F

V

A

E

K

V

I

L

A

G

A

T

F

V

L

L

V

G

T
|
T

I

A

I

I

-

Q

-

G

-

Q

-

I

-

V

-

G

-

Q

-

A

-

D

V

T

P

P

I
x
C

L

F

-

Q

-

D

-

L

-
x
N

-

S

-

T

-

V

-

A

-

S

-

Q

-

S

A

A

S
x
N

A

H

W

T

G

H

G

G

E

T

N

T

I

S

A

H

A

R

G

E

Y

T

Q

Q

K

K

A

A

M

Y

G

L

V

L

M

A

A

A

L

G

M

V

A

I

T
x
V

L

C

L

I

F

Y

L

I

F

I

C

C

-

A

-

V

-

I

-

L

-

I

F

L

F

G

T

V

T

R

T

E

E

Q

R

R

V

E

A

P

Y

Y

K

E

V

A

-

Q

E

Q

T

S

K

E

P

P

V

I

G

A

-

Y

-

F

M

R

Q

G

L

L

R

R

L

L

L

V

F

M

K

S

N

H

D

G

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Y

L

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L

L

V

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A

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I

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C

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F

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T

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L

G

A

Y

F

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M

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G
x
E

S

G

V

N

A
x
F

A

V

Y

L

Y

F

A

C

T

T

Y
|
Y

Y

T

L

L

G

G

G

F

D
x
R

A

N

K

E

M
x
F

L

Q

S

N

A

L

F
x
L

L

L

S

A

T
x
I

G
x
M

V

L

G

-

A
x
S

A

A

I

T

L

L

A

T

M
x
I

V

P

A

I

S

W

T
x
Q

W

W

I

F

T

L

K

T

R

R

Y

F

C

G

K

K

L

-

K

-

L

-

F

-

R

-

Y

K

S

T

Q

A

I

V

V

Y

V

V

G

G

I

I

L

S

S

S

A

A

I

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M

P

F

F

F

L

-

I

-

L

-

V

A

A

V

L

Q

M

P

E

G

S

D

N

I

L

V

I

L

I

A

T

F

Y

V

A

L

V

Y

A

F

V

A

A

I
x
A

S

G

F

I

V

S

V

V

D

A

L

A

H

A

A
x
F

P

L

V

L

F

P

W
|
W

S

S

V

M

I

L

S

P

E

D

S

V

V

I

D

D

Y

D

G

F

T

H

V

L

K

K

T

Q

G

P

-

H

-

F

H

H

R

G

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T

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E

G

P

L

I

A

F

F

F

G

S

G

F

I

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S

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F

F

A

F

Q

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K
|
K

A

F

G

A

M

S

G

G

A

V

A

S

G

L

F

G

V

I

V

S

G

T

M

L

L

S

L

L

T

D

Y

F

F

A

N

G

Y
|
Y

Q

Q

P

T

-

R

G

G

E
x
C

T

S

Q

Q

S

P

E

E

F

R

A

V

L

K

T

F

G

T

I

L

S

N

L

M

M

L

L

V

T

T

V

M

I

A

P

P

G

I

A

V

F

L

H

I

A

L

L

L

M

G

G

L

L

L

M

F

F

K

K

M

Y

Y

K
x
P

I

I

S

D

D

E

R

E

V

R

Y

R

E

R

E

Q

I

N

K

K

-

K

-

A

-

L

Q

Q

A

A

L

L

P

R

E

D

Q

E

A

A

H

S

-

S

-

G

V

C

S

S

Q

E

T

T

D

D

A

S

K

T

Q

E

Q57 (≠ N22) mutation to E: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to L: Abolished lysophosphatidylcholine (LPC) transport.
F65 (≠ L30) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
F66 (≠ I31) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
D73 (= D38) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
V81 (vs. gap) natural variant: Missing (in NEDMISBA; unknown pathological significance; dbSNP:rs1570238098)
R103 (= R55) mutation R->A,K,E: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: No effect on cell sensitivity toward tunicamycin.
D106 (= D58) mutation to A: No effect on cell sensitivity toward tunicamycin.
D110 (= D62) mutation to A: Drastic loss of cell sensitivity toward tunicamycin. Abolished lysophosphatidylcholine (LPC) transport.
T172 (= T124) to M: in NEDMISBA; no effect on cell membrane localization; loss of LPC transport activity; dbSNP:rs1057517688
P177 (= P129) mutation to T: Reduced expression; no effect on cell membrane localization; decreased LPC transport activity.
S179 (≠ I131) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057517689
M200 (≠ L152) mutation to F: Reduced lysophosphatidylcholine (LPC) transport.
T211 (= T163) to M: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs756467073
C225 (≠ I168) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
N230 (vs. gap) mutation to Q: Loss of glycosylation; when associated with Q-240.
N240 (≠ S171) mutation to Q: Loss of glycosylation; when associated with Q-230.
V263 (≠ T194) to F: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity
E325 (≠ G248) mutation E->A,D,Q,R: Abolished lysophosphatidylcholine (LPC) transport.
F328 (≠ A251) mutation F->A,Y: Reduced lysophosphatidylcholine (LPC) transport.
Y334 (= Y257) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.
R339 (≠ D262) to H: in NEDMISBA; reduced expression; no effect on cell membrane localization; no effect on LPC transport activity; dbSNP:rs776741331; mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
F342 (≠ M265) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
L346 (≠ F269) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
I349 (≠ T272) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
M350 (≠ G273) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
S352 (≠ A276) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057519087
I357 (≠ M281) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
Q361 (≠ T285) mutation to W: Reduced lysophosphatidylcholine (LPC) transport.
A404 (≠ I330) mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
F412 (≠ A338) mutation F->I,W: Reduced lysophosphatidylcholine (LPC) transport.
W416 (= W342) mutation W->A,F: Reduced lysophosphatidylcholine (LPC) transport.
K449 (= K373) mutation K->A,R,Q: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: Loss of plasma membrane localization. Loss of cell sensitivity toward tunicamycin.
Y468 (= Y392) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
C473 (≠ E396) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
P506 (≠ K429) to L: in NEDMISBA; reduced expression; no effect on cell membrane localization; loss of LPC transport activity

7mjsX Single-particle cryo-em structure of major facilitator superfamily domain containing 2a in complex with lpc-18:3 (see paper)
30% identity, 31% coverage: 6:152/481 of query aligns to 1:147/458 of 7mjsX

query
sites
7mjsX

L

L

S

S

V

V

I

C

E

S

K

K

I

L

G

C

Y

Y

G

A

S

V

G

G

D

G

M

A

A

P

V

Y

N

Q

V

T

I

G

S

C

S

A

M

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binding [(2~{R})-2-oxidanyl-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propyl] (9~{Z},12~{Z},15~{Z})-octadeca-9,12,15-trienoate: F25 (≠ L30), M147 (≠ L152)

Sites not aligning to the query:

binding [(2~{R})-2-oxidanyl-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propyl] (9~{Z},12~{Z},15~{Z})-octadeca-9,12,15-trienoate: 148, 265, 290, 297, 301, 348, 352, 353, 356

8d2sA Zebrafish mfsd2a isoform b in inward open ligand bound conformation (see paper)
28% identity, 31% coverage: 5:152/481 of query aligns to 2:149/475 of 8d2sA

query
sites
8d2sA

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binding [(2~{R})-2-oxidanyl-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propyl] (9~{Z},12~{Z},15~{Z})-octadeca-9,12,15-trienoate: F27 (≠ L30), R52 (= R55), D55 (= D58), S128 (≠ I131), D142 (≠ L145), R148 (= R151), M149 (≠ L152)

Sites not aligning to the query:

binding [(2~{R})-2-oxidanyl-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propyl] (9~{Z},12~{Z},15~{Z})-octadeca-9,12,15-trienoate: 150, 152, 152, 153, 153, 156, 157, 273, 274, 277, 280, 301, 302, 303, 305, 306, 306, 307, 309, 309, 313, 336, 352, 356, 360, 360, 361, 364, 364, 365, 368, 368, 389, 389, 393, 393, 400, 401, 404

Q3T9M1 Sphingosine-1-phosphate transporter MFSD2B; Major facilitator superfamily domain-containing protein 2B; mMfsd2b from Mus musculus (Mouse) (see 2 papers)
28% identity, 31% coverage: 5:152/481 of query aligns to 28:175/494 of Q3T9M1

query
sites
Q3T9M1

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D85 (= D62) mutation to A: Decreased sphingosine-1-phosphate transport.
T147 (= T124) mutation to A: Decreased export of sphingosine-1-phosphate.

Sites not aligning to the query:

413 K→A: Decreased sphingosine-1-phosphate transport.

A6NFX1 Sphingosine-1-phosphate transporter MFSD2B; Major facilitator superfamily domain-containing protein 2B; hMfsd2b from Homo sapiens (Human) (see paper)
26% identity, 31% coverage: 5:152/481 of query aligns to 38:185/504 of A6NFX1

query
sites
A6NFX1

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D95 (= D62) mutation to A: Abolishes export of sphingosine-1-phosphate.
T157 (= T124) mutation to A: Abolishes export of sphingosine-1-phosphate.

Sites not aligning to the query:

423 K→A: Does not affect export of sphingosine-1-phosphate.

Query Sequence

>7024907 FitnessBrowser__ANA3:7024907
MSYHKLSVIEKIGYGSGDMAVNVVISSMMLIITFFYTDIFGLKPADVGILFLLVRLIDAI
TDPLMGIINDKVTTRWGRYRPYFLFMAIPFGISVFLTFSTPDWDYNAKLIWAYSTYILVT
IIFTTVTIPYISIISVITDDPKERLSANGYRLFFAKIAAFLVTIIVPILASAWGGENIAA
GYQKAMGVMALMATLLFLFCFFTTTERVAYKVETKPVGMQLRLLFKNDQWLVLVAICVIG
TIGYVIRGSVAAYYATYYLGGDAKMLSAFLSTGVGAAILAMVASTWITKRYCKLKLFRYS
QIVVGILSAIMFFAVQPGDIVLAFVLYFAISFVVDLHAPVFWSVISESVDYGTVKTGHRV
SGLAFGGISFAQKAGMGAAGFVVGMLLTYFNYQPGETQSEFALTGISLMLTVIPGAFHAL
MGLLMFKYKISDRVYEEIKQALPEQAHVSQTDAKQTSKAIASDTVTAETVTPKTAAPQVS
A

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