SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_106712578.1 NCBI__GCF_003010955.1:WP_106712578.1 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 11 hits to proteins with known functional sites (download)

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
24% identity, 49% coverage: 14:228/440 of query aligns to 43:239/444 of Q8NLB7

query
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Q8NLB7

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D54 (≠ E25) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D28) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (≠ K81) mutation to A: Loss of transport activity.

Sites not aligning to the query:

309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 37% coverage: 66:226/440 of query aligns to 94:262/583 of Q9Y7Q9

query
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Q9Y7Q9

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Sites not aligning to the query:

267 modified: Phosphoserine
269 modified: Phosphoserine
289 modified: Phosphoserine
290 modified: Phosphoserine
292 modified: Phosphoserine
330 modified: Phosphoserine

O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 37% coverage: 64:226/440 of query aligns to 102:271/572 of O42885

query
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O42885

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Sites not aligning to the query:

12 modified: Phosphoserine
14 modified: Phosphoserine
292 modified: Phosphoserine
296 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, 65% coverage: 31:315/440 of query aligns to 27:350/475 of 4gc0A

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4gc0A

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binding 6-bromo-6-deoxy-beta-D-glucopyranose: Q164 (≠ L158), Q284 (≠ T260), N290 (= N266), L293 (vs. gap)

Sites not aligning to the query:

binding 6-bromo-6-deoxy-beta-D-glucopyranose: 388

4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
23% identity, 65% coverage: 31:315/440 of query aligns to 27:350/475 of 4gbzA

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V

I

binding beta-D-glucopyranose: Q164 (≠ L158), Q284 (≠ T260), N290 (= N266)

Sites not aligning to the query:

binding beta-D-glucopyranose: 388

4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
23% identity, 65% coverage: 31:315/440 of query aligns to 27:350/475 of 4gbyA

query
sites
4gbyA

I

I

Y

S

G

G

T

T

A

V

A

E

A

S

L

L

I

-

F

-

P

N

E

T

I

V

F

F

F

V

S

A

A

P

E

Q

N

N

P

L

Q

S

A

E

A

S

A

A

I

A

A

N

S

S

F

L

A

L

T

G

F

F

G

C

V

V

A

A

-

S

-

A

Y

L

I

I

A

G

R

C

P

I

F

I

G

G

A

G

V

A

I

L

L

G

G

G

H

Y

I

C

G

S

D

N

K

R

F

F

G

G

R

R

K

R

K

D

V

S

L

L

T

K

F

I

T

A

L

A

L

V

L

L

M

F

G

-

F

-

S

-

T

-

F

F

I

I

I

S

G

G

C

V

L

G

P

S

T

A

Y

W

D

P

H

E

V

L

G

G

I

F

L

T

A

S

-

I

-

N

-

P

-

D

-

N

-

T

-

V

P

P

I

V

L

Y

L

L

-

A

-

G

-

Y

-

V

-

P

-

E

-

F

V

V

V

I

A

Y

R

R

L

I

Q

G

G

G

V

I

S

G

A

V

A

G

G

L

E

A

Q

S

A

M

G

L

A

S

N

P

S

M

M

Y

T

I

L

A

E

E

H

L

A

A

P

P

P

A

N

H

R

I

R

R

A

G

F

K

F

L

T

V

S

S

F

F

T

N

L
x
Q

S

F

G

A

T

I

Q

I

A

F

G

G

L

Q

I

L

L

L

A

V

T

Y

L

C

V

V

F

N

I

Y

P

F

I

I

S

A

K

R

L

S

P

G

E

D

A

A

D

S

L

W

L

L

S

N

W

T

-

D

A

G

W

W

R

R

I

Y

P

M

F

F

F

A

L

S

S

E

L

C

V

I

V

P

V

A

V

L

G

F

F

L

W

M

V

L

R

L

R

Y

T

T

L

V

P

P

E

E

T

S

P

P

V

R

F

W

L

L

E

M

E

S

T

R

K

G

K

K

H

Q

E

E

T

Q

A

A

E

E

V

G

P

I

F

L

V

R

M

K

L

I

F

M

S

G

N

N

-

T

-

L

-

A

-

T

-

Q

-

A

-

V

-

Q

-

E

-

I

-

K

H

H

W

S

A

L

D

D

V

H

L

G

R

R

-

K

-

T

-

G

-

R

-

L

I

L

I

M

F

F

A

G

A

V

L

G

I

V

S

I

V

V

V

I

S

G

T

V

I

M

F

L

S

S

V

I

F

F

T
x
Q

L

Q

S

F

Y

V

A

G

V

I

N
|
N

-

V

-

L

-

Y

-

A

-

P

-

E

-

V

-

F

-

K

T

T

M

L

Q

G

I

A

D

S

R

T

S

D

T

I

M

A

L

L

T

L

V

Q

L

T

V

I

L

I

A

V

N

G

L

V

V

I

A

N

L

L

G

T

A

F

I

T

P

V

L

L

W

A

A

I

S

M

L

T

A

V

D

D

R

K

V

F

G

G

R

R

K

K

P

P

I

L

F

Q

I

I

L

I

G

G

A

A

L

L

G

G

C

M

A

A

V

I

binding beta-D-xylopyranose: Q164 (≠ L158), Q284 (≠ T260), N290 (= N266)

Sites not aligning to the query:

binding beta-D-xylopyranose: 388

P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
23% identity, 65% coverage: 31:315/440 of query aligns to 31:354/491 of P0AGF4

query
sites
P0AGF4

I

I

Y

S

G

G

T

T

A

V

A

E

A

S

L

L

I

-

F

-

P

N

E

T

I

V

F

F

F

V

S

A

A

P

E

Q

N

N

P

L

Q

S

A

E

A

S

A

A

I

A

A

N

S

S

F

L

A

L

T

G

F

F

G

C

V

V

A

A

-

S

-

A

Y

L

I

I

A

G

R

C

P

I

F

I

G

G

A

G

V

A

I

L

L

G

G

G

H

Y

I

C

G

S

D

N

K

R

F

F

G
|
G

R

R

K

R

K

D

V

S

L

L

T

K

F

I

T

A

L

A

L

V

L

L

M

F

G

-

F

-

S

-

T

-

F

F

I

I

I

S

G

G

C

V

L

G

P

S

T

A

Y

W

D

P

H

E

V

L

G

G

I

F

L

T

A

S

-

I

-

N

-

P

-

D

-

N

-

T

-

V

P

P

I

V

L

Y

L

L

-

A

-

G

-

Y

-

V

-

P

-

E

-

F

V

V

V

I

A

Y

R
|
R

L

I

Q

G

G

G

V

I

S

G

A

V

A

G

G

L

E

A

Q

S

A

M

G

L

A

S

N

P

S

M

M

Y

T

I

L

A

E
|
E

H

L

A

A

P

P

P

A

N

H

R

I

R
|
R

A

G

F

K

F

L

T

V

S

S

F

F

T

N

L
x
Q

S

F

G

A

T

I

Q

I

A

F

G

G

L

Q

I

L

L

L

A

V

T

Y

L

C

V

V

F

N

I

Y

P

F

I

I

S

A

K

R

L

S

P

G

E

D

A

A

D

S

L

W

L

L

S

N

W

T

-

D

A

G

W

W

R

R

I

Y

P

M

F

F

F

A

L

S

S

E

L

C

V

I

V

P

V

A

V

L

G

F

F

L

W

M

V

L

R

L

R

Y

T

T

L

V

P

P

E

E

T

S

P

P

V

R

F

W

L

L

E

M

E

S

T

R

K

G

K

K

H

Q

E

E

T

Q

A

A

E

E

V

G

P

I

F

L

V

R

M

K

L

I

F

M

S

G

N

N

-

T

-

L

-

A

-

T

-

Q

-

A

-

V

-

Q

-

E

-

I

-

K

H

H

W

S

A

L

D

D

V

H

L

G

R

R

-

K

-

T

-

G

-

R

-

L

I

L

I

M

F

F

A

G

A

V

L

G

I

V

S

I

V

V

V

I

S

G

T

V

I

M

F

L

S

S

V

I

F

F

T
x
Q

L
x
Q

S

F

Y

V

A

G

V

I

N
|
N

-

V

-

L

-
x
Y

-

Y

-

A

-

P

-

E

-

V

-

F

-

K

T

T

M

L

Q

G

I

A

D

S

R

T

S

D

T

I

M

A

L

L

T

L

V

Q

L

T

V

I

L

I

A

V

N

G

L

V

V

I

A
x
N

L

L

G

T

A

F

I

T

P

V

L

L

W

A

A

I

S

M

L

T

A

V

D

D

R

K

V

F

G
|
G

R
|
R

K

K

P

P

I

L

F

Q

I

I

L

I

G

G

A

A

L

L

G

G

C

M

A

A

V

I

G83 (= G83) mutation to A: Abolishes xylose transport.
R133 (= R123) mutation R->C,H,L: Abolishes xylose transport.
E153 (= E143) mutation to A: Abolishes xylose transport.
R160 (= R150) mutation to A: Abolishes xylose transport.
Q168 (≠ L158) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
Q288 (≠ T260) mutation to A: Abolishes xylose transport.
QQ 288:289 (≠ TL 260:261) binding beta-D-xylose
Q289 (≠ L261) mutation to A: Strongly decreases xylose transport.
N294 (= N266) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
Y298 (vs. gap) mutation to A: Abolishes xylose transport.
N325 (≠ A286) mutation to A: No effect on xylose transport.
G340 (= G301) mutation to A: Abolishes xylose transport.
R341 (= R302) mutation R->A,W: Abolishes xylose transport.

Sites not aligning to the query:

24 F→A: Decreases xylose transport.
392 binding beta-D-xylose; W→A: Abolishes xylose transport.
397 E→A: Abolishes xylose transport.
404 R→A: Strongly decreases xylose transport.
415 binding beta-D-xylose
416 W→A: Strongly decreases xylose transport.

8fvzA Pipt y150a
25% identity, 96% coverage: 13:435/440 of query aligns to 4:433/433 of 8fvzA

query
sites
8fvzA

K

K

A

L

A

V

L

L

A

L

S

A

W

G

I

V

G

G

S

F

A

F

V

L

E

D

Y

A

Y

Y

D

D

F

L

F

F

I

I

Y

I

G

N

T

Q

A

V

A

A

A

P

L

M

I

L

-

A

-

Q

-

V

-

Y

F

F

P

P

E

K

I

T

F

G

F

L

S

P

A

A

E

Q

N

R

P

Q

Q

D

A

L

A

M

A

K

I

A

A

A

S

-

F

-

A

-

T

-

F

-

G

-

V

-

A

A

Y

N

I

I

A

G

R

C

P

V

F

V

G

G

A

Q

V

V

I

M

L

F

G

G

H

V

I

L

G

G

D

D

K

S

F

F

G

G

R

R

K

K

K

F

V

V

L

Y

T

G

F

K

T

E

L

L

L

I

L

L

M

I

G

I

F

V

S

A

T

T

F

I

I

F

I

Q

G

M

C

S

L

A

P

P

T

S

Y

H

-

W

D

D

H

G

V

N

G

R

I

V

L

L

A

T

P

W

I

I

L

-

V

T

V

I

A

C

R

R

L

V

L

F

Q

L

G

G

V

I

S

G

A

I

A

G

G

G

E

D

Q

A

A

P

G

M

A

S

N

A

S

T

M

V

T

V

L

S

E

D

H

R

A

A

P

N

P

I

N

H

R

R

A

G

F

T

F

L

T

L

S

C

F

F

T

I

L
x
F

S

A

G

N

T

Q

Q

G

A

W

G

G

L

S

I

F

L

V

A

G

T

S

L

L

V

V

-

T

F

I

I

V

P

T

I

I

S

S

-

G

-

F

-

K

-

H

-

R

-

L

K

K

L

S

P

G

E

H

A

T

D

H

L

D

L

V

S

D

W

K

A

A

W

W

R

R

I

I

P

L

F

I

F

G

L

L

S

S

L

L

V

I

V

P

V

A

V

F

V

-

G

-

F

-

W

-

V

-

R

-

R

G

T

T

L

L

P

Y

E

Q

T

R

P

L

V

T

F

G

L

V

E

I

E

A

T

S

K

K

H

A

E

H

T

W

A

Q

E

E

V

-

P

-

F

F

V

V

M

A

L

Y

F

F

S

S

-

T

-

W

N

N

H

H

W

F

A

R

D

N

V

L

L

L

R

G

I

S

I

M

F

L

A

G

A
x
W

L

F

I

L

S

-

V

-

V

V

S
x
D

T

I

I

A

F

F

S
x
Y

V

G

F

I

T

N

L

L

S

N

Y

Q

A

S

V

V

N

V

T

L

M

A

Q

Q

I

I

-

G

-

F

-

A

-

G

-

K

-

T

-

G

D

D

R

V

S

Y

T

D

M

K

L

L

T

F

V

Q

L

L

V

A

L

T

A

G

N

N

L

I

V

I

-

V

-

T

A

A

L

L

G

G

A

F

I

L

P

P

L

G

W

Y

A

Y

-

F

-

T

-

L

S

F

L

L

A

I

D

D

R

I

V

V

G

G

R

R

K

K

P

K

I

L

-

Q

-

F

-

M

-

G

F

F

I

I

L

M

G

S

A

G

L

L

G

F

C

L

A

A

V

I

L

L

I

A

W

G

P

E

Y

-

I

I

W

D

A

H

I

I

S

G

Q

K

G

G

N

-

L

-

P

P

L

L

I

L

F

A

V

C

V

F

G

T

I

F

L

M

L

Q

S

F

G

F

I

F

V

N

Y

F

S

G

A

A

S
x
N

N

T

G

T

V

T

W

F

P

-

A

I

L

V

Y

A

G

A

E

E

M

L

F

F

D

P

T

T

R

R

V

I

R

R

L

A

S

S

G

A

M

H

A

G

I

I

G

S

T

A

-

A

-

G

Q

K

I

C

G

G

F

A

A

I

L

L

G

S

F

L

A

V

P

F

T

N

I

Q

S

L

A

K

A

A

L

K

L

I

G

G

T

T

G

S

P

A

N

V

G

L

W

W

V

I

P

F

V

F

A

S

A

-

F

-

T

-

S

-

V

-

T

T

A

C

I

I

I

L

A

G

A

F

V

I

S

S

A

T

A

F

T

L

A

I

S

D

E

E

T

T

Y

M

R

G

T

V

-

D

-

P

P

D

M

E

Q

K

D

D

L

L

G

E

K

E

R

R

P

R

V

A

R

R

binding phosphate ion: F145 (≠ L158), W235 (≠ A247), D239 (≠ S253), Y243 (≠ S257), N346 (≠ S347)

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
22% identity, 55% coverage: 76:318/440 of query aligns to 63:326/446 of A0A0H2VG78

query
sites
A0A0H2VG78

G

G

H

P

I

L

G

A

D

D

K

K

F

L

G

G

R

R

K

R

V

L

L

V

T

M

F

L

T

I

L

A

L

I

L

V

M

-

G

-

F

-

S

-

T

-

F

F

I

I

G

G

C

A

L

L

P

I

T

L

Y

A

D

A

H

S

V

T

G

N

I

L

L

A

A

-

P

-

I

-

L

L

V

I

A

G

R
|
R

L

L

L

I

Q
x
I

G

G

V

L

S

A

A

V

A

G

G

G

E

S

Q

M

A

S

G

T

A

V

N

P

S

V

M

Y

T

L

L

S

E
|
E

H

M

A

A

P

P

P

T

N

E

R

Y

R

R

A

G

F

S

F

L

T

G

S

S

F

L

T

N

L
x
Q

S

L

G

M

T

I

Q

T

A

I

G

G

L

I

I

L

L

A

A

A

T

Y

L

L

V

V

F

-

I

-

P

-

I

-

S

-

K

N

L

Y

P

A

E

F

A

A

D

D

L

I

L

E

S

G

W

W

A

R

W

W

R

M

I

L

P

G

F

L

-

A

F

V

L

V

S

P

L

S

V

V

V

I

V

L

V

V

G

G

F

I

W

Y

V

F

R

-

T

-

L

M

P

P

E

E

T

S

P

P

V

R

F

W

L

L

E

L

E

E

T

N

K

R

K

N

H

E

E

E

T

A

A

A

E

R

V

Q

P

V

F

M

V

K

M

I

L

T

F

Y

S

D

N

D

H

S

W

E

A

I

D

D

-

K

-

E

-

L

-

K

-

E

-

M

-

K

-

E

-

I

-

N

-

A

-

I

-

S

-

E

-

S

-

T

-

W

-

T

V

V

L

I

R

K

I

S

I

P

F

W

A

L

A

G

L

R

I

I

S

L

V

I

V

V

S

G

T

C

I

I

F

F

S

A

V

I

F

F

T
x
Q

L
x
Q

S

F

Y

I

A

G

V

I

N
|
N

T

A

M

V

Q

I

I

F

D

Y

R

S

S

S

T

S

M

I

L

F

T

A

V

K

L

A

V

G

L

L

A

G

N

E

L

A

-

A

-

S

-

I

-

L

-

G

-

S

V

V

A

G

L

I

G

G

A

T

I

I

P

N

L

V

W

L

A

V

S

T

L

I

-

V

-

A

-

I

-

F

-

V

A

V

D

D

R

K

V

I

G

D

R

R

K

K

P

K

I

L

F

L

I

V

L

G

G

G

A

N

L

I

G

G

-

M

-

I

-

A

-

S

-

L

-

I

C

M

A

A

V

I

L

L

I

I

W

W

R102 (= R123) mutation to A: Loss of transport activity.
I105 (≠ Q126) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E143) mutation to A: Loss of transport activity.
Q137 (≠ L158) mutation to A: Loss of transport activity.
Q250 (≠ T260) mutation to A: Loss of transport activity.
Q251 (≠ L261) mutation to A: Loss of transport activity.
N256 (= N266) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.
357 W→A: Loss of transport activity.

Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
31% identity, 22% coverage: 76:171/440 of query aligns to 78:170/452 of Q5EXK5

query
sites
Q5EXK5

G

G

H

P

I

L

G

S

D
|
D

K

R

F

F

G

G

R

R

K

K

K

R

V

V

L

I

T

E

F

F

T

C

L

V

L

A

L

L

M

F

G

G

F

L

S

F

T

S

F

L

I

L

I

S

G

A

C

F

L

A

P

P

T

D

Y

L

D

Q

H

-

V

-

G

-

I

-

L

-

A

-

P

-

I

-

L

M

L

L

V

V

V

F

A

L

R

R

L

F

L

L

Q

T

G

G

V

L

S

G

A

L

A

G

G

G

E

A

Q

M

A

P

G

N

A

T

N

I

S

T

M

M

T

T

L

S

E

E

H

Y

A

L

P

P

P

A

N

R

R

R

A

G

-

A

-

L

-

V

-

T

-

L

F

M

F

F

T

C

S

G

F

F

T

T

L

L

S

G

G

S

T

A

Q

F

A

G

G

G

L

V

I

V

L

S

A

A

T

Q

L

L

V

V

D82 (= D80) mutation to A: Loss of activity.

Sites not aligning to the query:

311 V→W: Loss of activity.
314 D→A: Loss of activity.

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
30% identity, 34% coverage: 71:221/440 of query aligns to 163:295/555 of Q9R0W2

query
sites
Q9R0W2

G

G

A

A

V

M

I

M

L

I

G

G

H

Y

I

L

G

A

D

D

K

R

F

F

G

G

R

R

K

K

K

F

V

C

L

L

T

L

F

V

T

T

L

I

L

L

L

I

M

N

G

A

F

I

S

S

T

G

F

A

I

L

I

M

G

A

C

I

L

S

P

P

T

N

Y

Y

D

-

H

-

V

-

G

-

I

-

L

-

A

-

P

-

I

A

L

W

L

M

V

L

V

V

A

F

R

R

L

F

L

L

Q

Q

G

G

-

L

V

V

S

S

A

K

A

A

G

G

E

W

Q

L

A

I

G

G

A

Y

N

I

S

L

M

I

T

T

L

E

E

F

H

V

A

G

P

L

P

G

N

Y

R

R

A

M

F

V

F

G

T

I

S

C

F

Y

T

Q

L

I

S

A

G

F

T

T

Q

V

A

G

G

L

L

L

I

I

L

L

A

A

T

G

L

V

V

A

F

Y

I

V

P

-

I

-

S

-

K

-

L

I

P

P

E

N

A

W

D

R

L

W

L

L

S

Q

W

F

A

A

W

V

R

T

I

L

P

P

F

N

F

F

L

C

S

F

L

L

V

L

V

Y

V

-

G

-

F

F

W

W

V

-

R

-

T

C

L

I

P

P

E

E

T

S

P

P

V

R

F

W

L

L

E

I

E

S

T

Q

K

N

K

K

Sites not aligning to the query:

451 Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; C→M: Transport activity strongly reduced.

Query Sequence

>WP_106712578.1 NCBI__GCF_003010955.1:WP_106712578.1
MHQPVTGVKAPGKAALASWIGSAVEYYDFFIYGTAAALIFPEIFFSAENPQAAAIASFAT
FGVAYIARPFGAVILGHIGDKFGRKKVLTFTLLLMGFSTFIIGCLPTYDHVGILAPILLV
VARLLQGVSAAGEQAGANSMTLEHAPPNRRAFFTSFTLSGTQAGLILATLVFIPISKLPE
ADLLSWAWRIPFFLSLVVVVVGFWVRRTLPETPVFLEETKKHETAEVPFVMLFSNHWADV
LRIIFAALISVVSTIFSVFTLSYAVNTMQIDRSTMLTVLVLANLVALGAIPLWASLADRV
GRKPIFILGALGCAVLIWPYIWAISQGNLPLIFVVGILLSGIVYSASNGVWPALYGEMFD
TRVRLSGMAIGTQIGFALGGFAPTISAALLGTGPNGWVPVAAFTSVTAIIAAVSAATASE
TYRTPMQDLGKRPVRISVTA

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