SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing AO353_26710 FitnessBrowser__pseudo3_N2E3:AO353_26710 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 6 hits to proteins with known functional sites (download)

P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
25% identity, 59% coverage: 117:374/434 of query aligns to 125:411/491 of P0AGF4

query
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P0AGF4

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R133 (= R126) mutation R->C,H,L: Abolishes xylose transport.
E153 (= E146) mutation to A: Abolishes xylose transport.
R160 (≠ K153) mutation to A: Abolishes xylose transport.
Q168 (= Q165) binding ; mutation to A: Abolishes xylose transport.
Q288 (≠ L251) mutation to A: Abolishes xylose transport.
QQ 288:289 (≠ LT 251:252) binding
Q289 (≠ T252) mutation to A: Strongly decreases xylose transport.
N294 (≠ Y257) binding ; mutation to A: Abolishes xylose transport.
Y298 (≠ V261) mutation to A: Abolishes xylose transport.
N325 (= N289) mutation to A: No effect on xylose transport.
G340 (= G304) mutation to A: Abolishes xylose transport.
R341 (= R305) mutation R->A,W: Abolishes xylose transport.
W392 (≠ V355) binding ; mutation to A: Abolishes xylose transport.
E397 (= E360) mutation to A: Abolishes xylose transport.
R404 (= R367) 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.

4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
25% identity, 59% coverage: 117:374/434 of query aligns to 121:407/475 of 4gc0A

query
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4gc0A

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binding 6-bromo-6-deoxy-beta-D-glucopyranose: Q164 (= Q165), Q284 (≠ L251), Q285 (≠ T252), N290 (≠ Y257), L293 (≠ T260), W388 (≠ V355)

Sites not aligning to the query:

binding 6-bromo-6-deoxy-beta-D-glucopyranose: 20, 411

4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
25% identity, 59% coverage: 117:374/434 of query aligns to 121:407/475 of 4gbzA

query
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4gbzA

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binding beta-D-glucopyranose: Q164 (= Q165), Q171 (≠ A172), Q284 (≠ L251), Q285 (≠ T252), N290 (≠ Y257), L293 (≠ T260), F379 (≠ I346), G384 (≠ N351), W388 (≠ V355)

Sites not aligning to the query:

binding beta-D-glucopyranose: 20, 411

4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
25% identity, 59% coverage: 117:374/434 of query aligns to 121:407/475 of 4gbyA

query
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4gbyA

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I

I

M

F

P

P

V

N

E

A

V

I

R

R

V

G

A

K

G

A

F

L

S

A

L

I

A

A

binding beta-D-xylopyranose: Q164 (= Q165), Q284 (≠ L251), Q285 (≠ T252), N290 (≠ Y257), F379 (≠ I346), G384 (≠ N351), W388 (≠ V355)

Sites not aligning to the query:

binding beta-D-xylopyranose: 20, 411

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
28% identity, 28% coverage: 73:192/434 of query aligns to 203:306/727 of Q9Z2I6

query
sites
Q9Z2I6

L

V

G

G

A

A

V

F

I

F

L

W

G

G

A

G

Y

L

I

A

D

D

D

K

V

V

G

G

R

R

R

K

K

Q

G

S

L

L

I

L

V

I

T

C

L

M

S

S

I

V

M

N

A

G

S

F

G

F

T

A

I

F

L

L

I

S

V

S

L

F

V

V

P

Q

G

G

Y

Y

E

-

T

-

I

-

G

G

L

F

F

F

A

-

P

-

A

-

L

-

V

-

L

L

I

L

G

C

R

R

L

L

L

L

Q

S

G

G

F

F

S

G

A

I

G

G

A

G

E

A

L

I

G

P

G

T

V

V

S

F

V

S

Y

Y

L

F

A

A

E

E

I

V

A

L

T

A

P

R

G

E

R

K

K

R

G

G

F

E

F

H

T

L

S

S

W

W

Q

L

S

C

A

M

S

F

Q

W

Q

M

V

I

A

G

I

G

V

I

V

Y

A

A

A

S

A

A

L

M

G

A

Y

W

A

A

L

-

N

-

Q

-

W

-

M

-

P

-

A

-

T

-

V

I

V

I

A

P

D

H

W

Y

G

G

W

W

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)
28% identity, 28% coverage: 73:192/434 of query aligns to 203:306/727 of Q496J9

query
sites
Q496J9

L

V

G

G

A

A

V

F

I

F

L

W

G

G

A

G

Y

L

I

A

D

D

D

K

V

V

G

G

R

R

R

K

K

Q

G

S

L

L

I

L

V

I

T

C

L

M

S

S

I

V

M

N

A

G

S

F

G

F

T

A

I

F

L

L

I

S

V

S

L

F

V

V

P

Q

G

G

Y

Y

E

-

T

-

I

-

G

G

L

F

F

F

A

-

P

-

A

-

L

-

V

-

L

L

I

F

G

C

R

R

L

L

L

L

Q

S

G

G

F

F

S

G

A

I

G

G

A

G

E

A

L

I

G

P

G

T

V

V

S

F

V

S

Y

Y

L

F

A

A

E

E

I

V

A

L

T

A

P

R

G

E

R

K

K

R

G

G

F

E

F

H

T

L

S

S

W

W

Q

L

S

C

A

M

S

F

Q

W

Q

M

V

I

A

G

I

G

V

I

V

Y

A

A

A

S

A

A

L

M

G

A

Y

W

A

A

L

-

N

-

Q

-

W

-

M

-

P

-

A

-

T

-

V

I

V

I

A

P

D

H

W

Y

G

G

W

W

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.

Query Sequence

>AO353_26710 FitnessBrowser__pseudo3_N2E3:AO353_26710
MQATTHPPATSARSKVSAIFRVTSGNFLEQFDFFLFGFYATYIAAAFFPASSEFASLMMT
FAVFGAGFLMRPLGAVILGAYIDDVGRRKGLIVTLSIMASGTILIVLVPGYETIGLFAPA
LVLIGRLLQGFSAGAELGGVSVYLAEIATPGRKGFFTSWQSASQQVAIVVAAALGYALNQ
WMPATVVADWGWRIPFFVGCMIVPFIFLLRRSLEETAEFTARRHRPSMRQVFGTLLQNWQ
IVIAGMLMVALTTTAFYLITVYAPTFGKTVLHLSTSDALLVTLLVGVSNFCWLPLGGALS
DRIGRRPVLVAMTLLTLATAYPALTYLVQAPSFINMLLVLLWLSFIYGLYNGAMVAALTE
IMPVEVRVAGFSLAYSLATAVFGGFTPAISTFLIQYSGDKAAPGYWMSFAALCALCATLY
LYRRSTGRLQVAVQ

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