SitesBLAST

R257 (= R285) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ T313) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
C344 (≠ G375) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
C349 (≠ G380) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
R376 (≠ K408) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.

B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
22% identity, 50% coverage: 55:329/551 of query aligns to 29:304/496 of B4EZY7

query
sites
B4EZY7

A

S

K

K

R

R

N

Q

T

K

S

T

T

A

A

D

D

D

Y

Y

Y

F

T

R

A

G

G

G

S

R

I

V

T

P

G

G

F

W

Q

A

N

A

G

G

L

V

A

S

I

V

A

F

G
x
A

D

T

F
x
T

M
x
L

S
|
S

A

S

A

I

S
x
T

F

F

L

M

G

S

I

I

S

P

A

A

L

K

V

A

Y

Y

T

T

S

S

G

D

Y

W

D

T

G

F

L

I

I

I

Y

G

S
x
Q

I

Y

G

L

F

A

L

I

V

A

G

I

W

L

P

P

I

L

I

V

L

F

F

Y

L

F

M

Y

A

I

E

P

R

F

L

F

R

R

N

K

L

L

G

-

K

K

F

I

T

T

F

-

S

-

D

-

V

-

A

S

S

A

Y

Y

R

E

L

Y

G

L

Q

E

T

A

Q

R

I

F

R

D

L

V

L

R

S

S

A

R

-

L

F

F

G

A

S

S

L

L

I

S

V

F

V

M

A

L

F

F

Y

H

L

I

-

G

-
x
R

I

V

A

A

Q

I

M

I

V

T

G

Y

A

L

G

T

K

V

L

L

-

A

I

L

Q

R

L

P

L

F

F

M

G

G

L

I

D

D

Y

P

Y

V

V

V

A

L

V

I

V

V

L

L

V

I

G

S

V

L

L

L

M

C

V

I

M

I

Y

Y

V

T

L

W

F

M

G

G

M

I

L

E

A

G

T

V

T

I

W

W

V

T

Q
x
D

I

V

I

I

K

Q

A

G

V

L

L

L

L

S

S

G

G

G

A

A

S

V

F

L

M

I

A

F

I

I

M

M

V

I

M

C

K

F

S

K

V

V

G

D

F

G

D

G

F

I

G

S

S

E

L

I

F

F

A

T

E

T

A

T

V

A

K

Q

I

A

H

D

E

K

-

F

K

P

G

T

A

T

Q

Q

I

W

M

R

S

W

P

S

G

W

G

T

L

D

V

S

S

T

D

I

P

P

I

V

S

L

A

M

I

I

S

G

L

F

G

L

L

F

A

A

L

N

M

I

F

Q

G

Q

T

F

A

T

G

A

L

S

P

Q

H

D

I

V

L

V

M

Q

R

R

F

Y

F

I

T

V

V

T

S

D

D

S

A

I

K

K

E

E

A

T

R

K

K

R

S

T

V

L

F

I

Y

T

A

N

T

A

G

K

F

L

I

V

G

A

Y

I

F

I

Y

P

I

I

L

F

T

F

F

F

I

A

I

I

G

G

F

S

G

A

A

L

I

F

L

V

L

Y

V

Y

S

Q

T

Q

N

N

P

P

E

S

A56 (≠ G82) binding Na(+)
T58 (≠ F84) mutation to A: 2-fold increase in Neu5Ac transport.
L59 (≠ M85) binding Na(+)
S60 (= S86) mutation to A: Abolishes Neu5Ac transport.
T63 (≠ S89) mutation to A: Abolishes Neu5Ac transport.
Q82 (≠ S108) mutation to D: Abolishes Neu5Ac transport.
R135 (vs. gap) mutation to E: Abolishes Neu5Ac transport.
D182 (≠ Q209) binding Na(+); mutation to A: Abolishes Neu5Ac transport.

Sites not aligning to the query:

339 binding Na(+)
342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
343 binding Na(+); S→A: Abolishes Neu5Ac transport.
345 binding Na(+); S→A: Reduces Neu5Ac transport.
346 binding Na(+); S→A: Slightly increases Neu5Ac transport.

5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 50% coverage: 55:329/551 of query aligns to 25:300/480 of 5nv9A

query
sites
5nv9A

A

S

K

K

R

R

N

Q

T

K

S

T

T

A

A

D

D

D

Y

Y

Y

F

T

R

A

G

G

G

S

R

I

V

T

P

G

G

F

W

Q

A

N

A

G

G

L

V

A

S

I

V

A

F

G
x
A

D
x
T

F
x
T

M
x
L

S
|
S

A

S

A
x
I

S
x
T

F

F

L

M

G

S

I

I

S

P

A

A

L

K

V

A

Y

Y

T

T

S

S

G

D

Y

W

D

T

G

F

L

I

I

I

Y
x
G

S
x
Q

I

Y

G

L

F

A

L

I

V

A

G

I

W

L

P

P

I

L

I

V

L

F

F

Y

L

F

M

Y

A

I

E

P

R

F

L

F

R

R

N

K

L

L

G

-

K

K

F

I

T

T

F

-

S

-

D

-

V

-

A

S

S

A

Y

Y

R

E

L

Y

G

L

Q

E

T

A

Q

R

I

F

R

D

L

V

L

R

S

S

A

R

-

L

F

F

G

A

S

S

L

L

I

S

V

F

V

M

A

L

F

F

Y

H

L

I

-

G

-
x
R

I

V

A

A

Q

I

M

I

V

T

G

Y

A

L

G

T

K

V

L

L

-

A

I

L

Q

R

L

P

L

F

F

M

G

G

L

I

D

D

Y

P

Y

V

V

V

A

L

V

I

V

V

L

L

V

I

G

S

V

L

L

L

M

C

V

I

M

I

Y

Y

V

T

L

W

F

M

G

G

M

I

L

E

A

G

T
x
V

T

I

W

W

V

T

Q
x
D

I

V

I

I

K

Q

A

G

V

L

L

L

L

S

S

G

G

G

A

A

S

V

F

L

M

I

A

F

I

I

M

M

V

I

M

C

K

F

S

K

V

V

G

D

F

G

D

G

F

I

G

S

S

E

L

I

F

F

A

T

E

T

A

T

V

A

K

Q

I

A

H

D

E

K

-

F

K

P

G

T

A

T

Q

Q

I

W

M

R

S

W

P

S

G

W

G

T

L

D

V

S

S

T

D

I

P

P

I

V

S

L

A

M

I

I

S

G

L
x
F

G

L

L

F

A

A

L

N

M

I

F

Q

G

Q

T

F

A

T

G

A

L

S

P

Q

H

D

I

V

L

V

M

Q

R

R

F

Y

F

I

T

V

V

T

S

D

D

S

A

I

K

K

E

E

A

T

R

K

K

R

S

T

V

L

F

I

Y

T

A

N

T

A

G

K

F

L

I

V

G

A

Y

I

F

I

Y

P

I

I

L

F

T

F

F

F

I

A

I

I

G

G

F

S

G

A

A

L

I

F

L

V

L

Y

V

Y

S

Q

T

Q

N

N

P

P

E

S

binding sodium ion: A52 (≠ G82), T53 (≠ D83), L55 (≠ M85), S56 (= S86), V174 (≠ T205), D178 (≠ Q209)
binding N-acetyl-beta-neuraminic acid: T54 (≠ F84), S56 (= S86), I58 (≠ A88), T59 (≠ S89), G77 (≠ Y107), Q78 (≠ S108), R131 (vs. gap), F239 (≠ L268)

Sites not aligning to the query:

binding sodium ion: 335, 338, 338, 339, 341, 342

Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
23% identity, 33% coverage: 39:219/551 of query aligns to 19:201/643 of Q92911

query
sites
Q92911

M

V

F

F

V

A

V

L

F

M

I

L

A

L

F

V

T

S

M

T

G

G

I

I

T

G

K

L

W

W

-

V

-

G

-

L

A

A

A

R

K

G

R

G

N

Q

T

R

S

S

T

A

A

E

D

D

Y

F

T

T

A

G

G

G

G

R

S

R

I

L

T

A

G

A

F

L

Q

P

N

V

G

G

L

L

A

S

I

L

A

S

G

A

D

S

F

F

M

M

S

S

A

A

A

V

S

Q

F

V

L

L

G

G

I

V

S

P

A

S

L

E

V

A

Y

Y

T

R

S

Y

G

G

Y

L

D

K

G

F

L

L

I

W

Y

M

S

C

I

L

G

G

F

Q

L

L

V

L

G

N

W

S

P

V

I

L

I

T

L
x
A

F

L

L

L

M

F

A

M

E

P

R

V

L

F

R

Y

N

R

L

L

G

G

K

L

F

T

T

S

F

T

S

Y

D

E

V

Y

A

L

S

E

Y

M

R

R

L

F

G

S

Q

R

T

A

Q

-

I

V

R

R

L

L

L

C

S

G

A

T

F

L

G

Q

S

Y

L

I

I

V

V

A

V

T

A

M

F

L

Y

Y

L

T

I

G

A

I

Q

V

M

I

V

Y

G

A

A

P

G

A

K

L

L

I

I

L

Q

N

L

Q

L

V

F

T

G

G

L

L

D

D

Y

I

Y

W

V

A

A

S

V

L

L

S

V

T

G

G

V

I

L

I

M

C

V

T

M

F

Y

Y

V

T

L

A

F

V

G

G

M

M

L

K

A

A

T

V

W

W

V

T

Q

D

I

V

I

F

K

Q

A

V

V

V

L

V

L

M

L

L

S

S

G

G

A102 (≠ L119) natural variant: A -> P

Sites not aligning to the query:

226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
536 T → Q: requires 2 nucleotide substitutions
556 S → Q: requires 2 nucleotide substitutions

P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
21% identity, 83% coverage: 14:470/551 of query aligns to 6:492/662 of P11170

query
sites
P11170

V

L

S

S

P

P

A

L

L

T

A

S

D

T

A

A

I

A

T

P

G

L

E

E

V

S

E

Y

K

E

Q

R

A

I

T

R

N

N

Y

A

T

A

A

D

I

I

I

S

M

V

F

I

V

V

V

I

F

Y

I

F

A

L

F

V

T

V

M

M

G

A

I

V

T

G

K

L

W

W

A

A

-

M

-

F

A

S

K

T

R

N

N

R

T

G

S

T

T

V

A

G

D

G

Y

F

T

L

A

A

G

G

G

R

S

S

I

M

T

V

G

W

F

W

Q

P

N

I

G

G

L

A

A

S

I

L

A

F

G

A

D

S

F

N

M

I

S

G

A

S

A

G

S

H

F

F

L

V

G

G

I

L

S

A

A

G

L

T

V

G

Y

A

T

A

S

S

G

G

-

I

-

A

-

T

-

G

-

F

-

E

Y

W

D

N

G

A

L

L

I

I

Y

M

S

V

I

V

G

-

F

-

L

V

V

L

G

G

W

W

-

V

-

F

-

V

P

P

I

I

I

Y

L

I

F

-

L

-

M

-

A

-

E

-

R

-

L

-

R

-

N

R

L

A

G

G

K

V

F

V

T

T

F

M

S

P

D

E

V

Y

A

L

S

Q

Y

K

R

R

L

F

G

G

Q

G

T

K

Q

R

I

I

R

Q

L

I

L

Y

S

L

A

S

F

I

G

L

S

S

L

L

I

L

V

L

V

Y

A

I

F

F

Y

T

L

K

I

I

A

S

Q

A

M

D

V

I

G

F

A

S

G

G

K

A

L

I

-

F

I

I

Q

Q

L

L

L

T

F

L

G

G

L

L

D

D

Y

I

Y

Y

V

V

A

A

V

I

L

I

V

L

G

L

V

V

L

I

M

T

V

G

M

L

Y

Y

V

T

L

I

F

T

G

G

M

L

L

A

A

A

T

V

T

I

W

Y

V

T

Q

D

I

T

I

L

K

Q

A

T

V

A

L

I

L

M

S

V

G

G

A

S

S

V

F

I

M

L

A

T

I

G

M

F

V

A

M

F

K

H

S

E

V

V

G

G

-

G

-

Y

F

E

D

A

F

F

G

T

S

E

L

K

F

Y

A

M

E

R

A

A

V

I

K

P

I

S

H

Q

E

I

K

S

G

Y

A

G

Q

N

I

T

M

S

S

I

P

P

G

Q

G

K

L
x
C

V

Y

S

T

D

P

P

R

I

E

S

D

A

A

I

F

S

H

L

I

G

F

L

R

A

D

L

A

M

I

F

T

G

G

T

D

A

I

G

P

L

W

P

P

-

G

-

L

-

V

-

F

-

G

-

M

H

S

I

I

L

L

M

T

R

L

F

W

F

Y

T

W

V

C

S

T

D

D

-

Q

-

V

-

I

-

V

-

Q

-

R

A

C

K

L

E

S

A

A

R

K

K

N

S

L

V

S

F

H

Y

V

A

K

T

A

G

G

F

C

I

I

-

L

-

C

G

G

Y

Y

F

L

Y

K

I

V

-

M

-

P

-

M

-

F

L

L

T

I

F

V

I

M

G

G

F

M

G

V

A

S

I

R

L

I

L

L

V

Y

S

T

T

D

N

K

-

V

-

A

-

C

-

V

-

P

P

S

E

E

F

C

K

E

D

R

V

Y

T

C

G

G

A

T

I

R

V

V

G

G

G

C

T

T

N

N

M

I

V

A

A

F

I

P

H

T

L

L

A

V

S

V

A

E

V

L

G

M

G

P

N

N

L

G

F

L

L

R

G

G

F

L

I

M

S

L

A

S

V

V

A

M

F

M

A

A

T

S

I

L

L

M

A

S

V

S

V

L

A

T

G

S

L

I

T

F

L

N

A

S

G

A

A

S

S

T

A

L

V

F

S

T

H

M

D

D

L

I

Y

Y

A

T

C

K

V

I

I

R

K

K

Q

-

G

-

K

K

A

A

R

S

E

E

E

K

D

E

E

L

M

M

R

I

V

A

T

G

K

R

L

L

T

F

T

M

L

L

T

F

L

L

G

I

V

G

V

I

A

S

I

I

L

A

L

W

G

V

I

P

I

I

F

V

E

Q

K

S

Q

A

N

Q

I

S

A

G

F

Q

M

L

V

F

G

D

L

Y

A

I

F
x
Q

S

S

I

I

A
x
T

A

S

S

Y

C

L

N

G

F

P

P

P

-

I

-

A

V

V

L

F

F

L

L

L

S

A

M

I

Y

F

W

W

K

K

G

R

L

V

S

N

T

E

R

P

G

G

A

A

L

F

F

W

G

G

G

L

S

V

L

L

G

G

C255 (≠ L258) modified: Disulfide link with 608
Q457 (≠ F438) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
T460 (≠ A441) mutation to W: Decreased affinity for glucose and phlorizin.

Sites not aligning to the query:

608 modified: Disulfide link with 255

Query Sequence

>GFF2882 FitnessBrowser__psRCH2:GFF2882
MILRFLMTALLLAVSPALLADAITGEVEKQATNYTAIIMFVVFIAFTMGITKWAAKRNTS
TADYYTAGGSITGFQNGLAIAGDFMSAASFLGISALVYTSGYDGLIYSIGFLVGWPIILF
LMAERLRNLGKFTFSDVASYRLGQTQIRLLSAFGSLIVVAFYLIAQMVGAGKLIQLLFGL
DYYVAVVLVGVLMVMYVLFGGMLATTWVQIIKAVLLLSGASFMAIMVMKSVGFDFGSLFA
EAVKIHEKGAQIMSPGGLVSDPISAISLGLALMFGTAGLPHILMRFFTVSDAKEARKSVF
YATGFIGYFYILTFIIGFGAILLVSTNPEFKDVTGAIVGGTNMVAIHLASAVGGNLFLGF
ISAVAFATILAVVAGLTLAGASAVSHDLYACVIKQGKAREEDEMRVTKLTTLTLGVVAIL
LGIIFEKQNIAFMVGLAFSIAASCNFPVLFLSMYWKGLSTRGALFGGSLGLFTALLLTII
SPTVWVDVFGFAEAIFPYKYPALFSMAAAFAGIWFFSVTDKSKRAGEERERFFAQFVRSQ
TGLGATGAVAH

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