SitesBLAST

R102 (= R129) mutation to A: Loss of transport activity.
I105 (≠ Q132) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E149) mutation to A: Loss of transport activity.
Q137 (≠ S164) mutation to A: Loss of transport activity.
Q250 (vs. gap) mutation to A: Loss of transport activity.
Q251 (≠ Y260) mutation to A: Loss of transport activity.
N256 (≠ Y265) mutation to A: Loss of transport activity.
W357 (vs. gap) mutation to A: Loss of transport activity.

Sites not aligning to the query:

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

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
32% identity, 30% coverage: 76:205/439 of query aligns to 203:328/727 of Q9Z2I6

query
sites
Q9Z2I6

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Sites not aligning to the query:

1:57 Interaction with SYT1
529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
31% identity, 30% coverage: 76:205/439 of query aligns to 203:328/727 of Q496J9

query
sites
Q496J9

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Sites not aligning to the query:

519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
563 F→A: No longer interacts with BoNT/A HC.
565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.

A1Z8N1 Facilitated trehalose transporter Tret1-1; DmTret1-1 from Drosophila melanogaster (Fruit fly) (see paper)
26% identity, 76% coverage: 85:416/439 of query aligns to 461:811/857 of A1Z8N1

query
sites
A1Z8N1

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Sites not aligning to the query:

248 modified: Phosphoserine
249 modified: Phosphoserine
250 modified: Phosphoserine
320 modified: Phosphoserine
322 modified: Phosphoserine
845 modified: Phosphoserine
846 modified: Phosphoserine

4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
23% identity, 58% coverage: 129:381/439 of query aligns to 129:409/475 of 4gc0A

query
sites
4gc0A

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x
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W

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A

binding 6-bromo-6-deoxy-beta-D-glucopyranose: Q164 (= Q168), Q284 (≠ M254), N290 (≠ Y260), L293 (≠ T263), W388 (≠ V358)

4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
23% identity, 58% coverage: 129:381/439 of query aligns to 129:409/475 of 4gbzA

query
sites
4gbzA

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x
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F

V

S

A

F

A

F

F

F

A

G

M

M

S

Y

W

N

G

G

P

A

V

M

C

V
x
W

A

V

A

L

L

L

T

S

E

E

V

I

M

F

P

P

A

N

E

A

V

I

R

R

V

-

A

-

G

G

F

K

S

A

L

L

A

A

F

I

S

A

L

V

A

A

binding beta-D-glucopyranose: Q164 (= Q168), Q284 (≠ M254), N290 (≠ Y260), W388 (≠ V358)

4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
23% identity, 58% coverage: 129:381/439 of query aligns to 129:409/475 of 4gbyA

query
sites
4gbyA

R

R

L

I

Q

G

G

G

F

I

S

G

A

V

G

G

A

L

E

A

L

S

G

M

G

L

V

S

S

P

V

M

Y

Y

L

I

A

A

E

E

M

L

A

A

T

P

P

A

G

H

N

I

R

R

G

G

F

K

Y

L

T

V

S

S

W

F

Q

N

S

-

A

-

S

-

Q

-

Q
|
Q

V

F

A

A

I

I

V

I

M

F

A

G

A

Q

A

L

I

L

G

V

Y

Y

G

C

L

V

N

N

E

Y

W

F

L

I

S

A

A

R

Q

S

Q

G

I

D

G

A

A

S

W

W

-

L

-

N

-

T

-

D

G

G

W

W

R

R

V

Y

P

M

F

F

L

A

I

S

G

E

C

C

A

I

I

P

V

A

P

L

F

L

L

F

F

L

M

M

L

L

R

L

R

Y

S

T

L

V

Q

P

E

E

T

S

A

P

A

R

F

W

-

L

E

M

A

S

R

R

Q

G

H

K

H

Q

P

E

Q

Q

A

A

R

E

E

G

I

I

F

L

S

R

M

K

L

I

L

M

A

G

N

N

W

T

R

L

-

A

-

T

-

Q

-

A

-

V

-

Q

-

E

-

I

-

K

-

H

-

S

-

L

-

D

-

H

-

G

-

R

-

K

-

T

-

G

-

R

-

L

-

M

-

F

-

G

-

V

-

G

-

V

I

I

V

V

I

I

G

G

G

V

M

M

L

L

L

S

T

I

A

F

M
x
Q

T

Q

T

F

T

V

T

G

F

I

Y
x
N

L

V

I

V

T

L

V

Y

Y

Y

T

A

P

P

T

E

F

V

G

F

R

K

S

T

V

-

L

L

K

G

L

A

S

S

T

T

A

D

D

I

S

A

L

L

M

L

V

Q

T

T

L

I

V

V

A

G

V

V

S

I

N

N

F

L

V

T

W

F

L

T

P

V

I

L

G

A

G

I

A

M

V

T

S

V

D

D

R

K

I

F

G

G

R

R

K

K

P

P

L

L

L

Q

-

I

-

G

-

A

-

L

-

G

L

M

A

A

V

I

S

G

V

M

L

F

A

S

I

L

F

G

T

T

A

A

Y

F

P

-

A

-

L

-

S

-

W

-

L

Y

A

T

D

Q

A

A

P

P

S

G

F

I

A

V

R

A

M

L

L

L

I

S

V

M

L

L

L

F

W

Y

F

V

S

A

F

A

F

F

F

A

G

M

M

S

Y

W

N

G

G

P

A

V

M

C

V
x
W

A

V

A

L

L

L

T

S

E

E

V

I

M

F

P

P

A

N

E

A

V

I

R

R

V

-

A

-

G

G

F

K

S

A

L

L

A

A

F

I

S

A

L

V

A

A

binding beta-D-xylopyranose: Q164 (= Q168), Q284 (≠ M254), N290 (≠ Y260), W388 (≠ V358)

P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
23% identity, 58% coverage: 129:381/439 of query aligns to 133:413/491 of P0AGF4

query
sites
P0AGF4

R
|
R

L

I

Q

G

G

G

F

I

S

G

A

V

G

G

A

L

E

A

L

S

G

M

G

L

V

S

S

P

V

M

Y

Y

L

I

A

A

E
|
E

M

L

A

A

T

P

P

A

G

H

N

I

R
|
R

G

G

F

K

Y

L

T

V

S

S

W

F

Q

N

S

-

A

-

S

-

Q

-

Q
|
Q

V

F

A

A

I

I

V

I

M

F

A

G

A

Q

A

L

I

L

G

V

Y

Y

G

C

L

V

N

N

E

Y

W

F

L

I

S

A

A

R

Q

S

Q

G

I

D

G

A

A

S

W

W

-

L

-

N

-

T

-

D

G

G

W

W

R

R

V

Y

P

M

F

F

L

A

I

S

G

E

C

C

A

I

I

P

V

A

P

L

F

L

L

F

F

L

M

M

L

L

R

L

R

Y

S

T

L

V

Q

P

E

E

T

S

A

P

A

R

F

W

-

L

E

M

A

S

R

R

Q

G

H

K

H

Q

P

E

Q

Q

A

A

R

E

E

G

I

I

F

L

S

R

M

K

L

I

L

M

A

G

N

N

W

T

R

L

-

A

-

T

-

Q

-

A

-

V

-

Q

-

E

-

I

-

K

-

H

-

S

-

L

-

D

-

H

-

G

-

R

-

K

-

T

-

G

-

R

-

L

-

M

-

F

-

G

-

V

-

G

-

V

I

I

V

V

I

I

G

G

G

V

M

M

L

L

L

S

T

I

A

F

M
x
Q

T
x
Q

T

F

T

V

T

G

F

I

Y
x
N

L

V

I

V

T

L

V
x
Y

Y

Y

T

A

P

P

T

E

F

V

G

F

R

K

S

T

V

-

L

L

K

G

L

A

S

S

T

T

A

D

D

I

S

A

L

L

M

L

V

Q

T

T

L

I

V

V

A

G

V

V

S

I

N
|
N

F

L

V

T

W

F

L

T

P

V

I

L

G

A

G

I

A

M

V

T

S

V

D

D

R

K

I

F

G
|
G

R
|
R

K

K

P

P

L

L

L

Q

-

I

-

G

-

A

-

L

-

G

L

M

A

A

V

I

S

G

V

M

L

F

A

S

I

L

F

G

T

T

A

A

Y

F

P

-

A

-

L

-

S

-

W

-

L

Y

A

T

D

Q

A

A

P

P

S

G

F

I

A

V

R

A

M

L

L

L

I

S

V

M

L

L

L

F

W

Y

F

V

S

A

F

A

F

F

F

A

G

M

M

S

Y

W

N

G

G

P

A

V

M

C

V
x
W

A

V

A

L

L

L

T

S

E
|
E

V

I

M

F

P

P

A

N

E

A

V

I

R
|
R

V

-

A

-

G

G

F

K

S

A

L

L

A

A

F

I

S

A

L

V

A

A

R133 (= R129) mutation R->C,H,L: Abolishes xylose transport.
E153 (= E149) mutation to A: Abolishes xylose transport.
R160 (= R156) mutation to A: Abolishes xylose transport.
Q168 (= Q168) binding ; mutation to A: Abolishes xylose transport.
Q288 (≠ M254) mutation to A: Abolishes xylose transport.
QQ 288:289 (≠ MT 254:255) binding
Q289 (≠ T255) mutation to A: Strongly decreases xylose transport.
N294 (≠ Y260) binding ; mutation to A: Abolishes xylose transport.
Y298 (≠ V264) mutation to A: Abolishes xylose transport.
N325 (= N292) mutation to A: No effect on xylose transport.
G340 (= G307) mutation to A: Abolishes xylose transport.
R341 (= R308) mutation R->A,W: Abolishes xylose transport.
W392 (≠ V358) binding ; mutation to A: Abolishes xylose transport.
E397 (= E363) mutation to A: Abolishes xylose transport.
R404 (= R370) mutation to A: Strongly decreases xylose transport.

Sites not aligning to the query:

24 F→A: Decreases xylose transport.
83 G→A: Abolishes xylose transport.
415 binding
416 W→A: Strongly decreases xylose transport.

Query Sequence

>BPHYT_RS27915 FitnessBrowser__BFirm:BPHYT_RS27915
MNPTEPIAATSSVSRSTRAAAVLRVTSGNFLEQFDFFLFGFYATFISKIFFPSTSEFASL
MLTFAVFGAGFLMRPLGAIFLGAYIDKVGRRMGLIVTLSIMASGTVLIACVPGYASIGLL
APALVLLGRLLQGFSAGAELGGVSVYLAEMATPGNRGFYTSWQSASQQVAIVMAAAIGYG
LNEWLSAQQIGAWGWRVPFLIGCAIVPFLFMLRRSLQETAAFEARQHHPQAREIFSMLLA
NWRIVIGGMLLTAMTTTTFYLITVYTPTFGRSVLKLSTADSLMVTLLVAVSNFVWLPIGG
AVSDRIGRKPLLLAVSVLAIFTAYPALSWLADAPSFARMLIVLLWFSFFFGMYNGAMVAA
LTEVMPAEVRVAGFSLAFSLATAVFGGFTPAVSTYLIQVTHDKAAPGYWLSFAALCGLCA
TLGLYRRRASSSASAASSA

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