SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CCNA_03582 FitnessBrowser__Caulo:CCNA_03582 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 20 (the maximum) hits to proteins with known functional sites (download)

Q9M8S8 Inositol-phosphate phosphatase; L-galactose 1-phosphate phosphatase; Myo-inositol monophosphatase; EC 3.1.3.25; EC 3.1.3.93 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 79% coverage: 32:241/265 of query aligns to 29:241/271 of Q9M8S8

query
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Q9M8S8

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P92 (= P96) mutation to L: In vtc4-1; low levels of ascorbate.

Q9K4B1 Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see paper)
31% identity, 78% coverage: 36:243/265 of query aligns to 30:240/266 of Q9K4B1

query
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Q9K4B1

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G118 (= G125) mutation to R: Requires histidine to grow.

5zonA Histidinol phosphate phosphatase from mycobacterium tuberculosis (see paper)
33% identity, 79% coverage: 32:241/265 of query aligns to 22:231/256 of 5zonA

query
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binding phosphate ion: E65 (= E75), I83 (≠ V97), D84 (= D98), G85 (= G99), T86 (= T100)
binding zinc ion: D42 (= D52), E65 (= E75), E65 (= E75), E66 (= E76), D81 (= D95), D81 (= D95), D211 (= D221)

5yhtA Crystal structure of a phosphatase from mycobacterium tuberculosis in complex with its substrate (see paper)
33% identity, 79% coverage: 32:241/265 of query aligns to 21:230/255 of 5yhtA

query
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5yhtA

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binding phosphoric acid mono-[2-amino-3-(3h-imidazol-4-yl)-propyl]ester: E64 (= E75), I82 (≠ V97), D83 (= D98), G84 (= G99), T85 (= T100), D186 (= D195), D210 (= D221)
binding phosphate ion: R180 (≠ D189), R182 (= R191)
binding zinc ion: D41 (= D52), E64 (= E75), D80 (= D95), D80 (= D95), D210 (= D221)

P95189 Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 79% coverage: 32:241/265 of query aligns to 24:233/260 of P95189

query
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P95189

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D86 (= D98) mutation to N: Causes a probable loss of enzymatic activity.

Q19420 Inositol monophosphatase ttx-7; IMP; IMPase; Abnormal thermotaxis protein 7; D-galactose 1-phosphate phosphatase; Inositol-1(or 4)-monophosphatase; EC 3.1.3.25; EC 3.1.3.94 from Caenorhabditis elegans (see paper)
28% identity, 77% coverage: 41:244/265 of query aligns to 42:253/285 of Q19420

query
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Q19420

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Q

Q

A

S

L

L

G

G

L

L

I

H

S

N

H

R

T

V

M

Q

R

F

E

G

E

D

K

R

A

W

T

L

E

D

L

I

A

A

A

Q

E

S

Y

-

G

-

F

-

D

N

L

M

R

R

T

N

P

Q

M

V

-

M

-

A

-

G

-

V

-

R

-

G

-

H

-

R

-

S

-

F

-

G

D

S

S

A

I

I

K

N

M

M

C

V

R

M

I

V

A

A

E

Q

G
|
G

S

S

A

C

D

D

I

G

Y

Y

P

V

R

E

H

Y

G

G

P

-

T

I

S

H

E

A

W

W

D

D

T

V

A

A

G

P

H

S

A

I

V

I

L

V

V

T

A

E

A

A

G

G

A

V

F

V

T

T

Q

D

P

P

D

T

G

G

S

S

P

P

F

F

G216 (= G206) mutation to E: In nj40; induces defects in thermotaxis.

2p3nA Thermotoga maritima impase tm1415 (see paper)
25% identity, 89% coverage: 20:256/265 of query aligns to 9:236/256 of 2p3nA

query
sites
2p3nA

K

K

I

L

T

L

E

R

E

K

A

V

A

G

V

H

V

L

I

L

L

M

P

I

F

H

W

W

-

G

R

R

T

V

E

D

L

N

A

V

V

E

A

K

Q

K

K

T

A

G

D

F

E

K

S

D

P

I

V

V

T

T

E

E

A

I

D

D

R

R

A

E

G

A

E

Q

R

R

L

M

I

I

L

V

E

D

R

E

L

I

A

R

A

K

L

F

Y

F

P

P

A

D

I

E

P

N

V

I

I

M

S

A

E
|
E

E

E

D

G

A

I

S

F

E

E

F

-

G

-

T

-

P

-

E

-

S

-

V

K

G

G

P

D

R

R

F

L

F

W

L

I

V

I

D
|
D

P

P

V
x
I

D
|
D

G

G

T
|
T

K

I

A

N

F

F

V

V

R

H

G

G

D

L

P

P

N

N

F

F

T

S

V

I

N

S

I

L

G

A

L

Y

I

V

E

E

H

N

G

G

V

E

P

V

V

K

A

L

G

G

A

V

V

V

C

H

A

A

P

P

A

A

T

L

G

N

E

E

V

T

W

L

F

Y

T

A

T

E

A

E

D

G

G

S

A

G

A

A

K

F

R

F

A

N

G

G

P

E

D

R

-

I

-

R

-

V

A

S

A

E

E

N

A

A

P

S

I

L

R

E

V

E

R

C

P

V

W

G

P

S

T

T

G

G

Q

S

A

Y

L

V

G

D

L

F

I

T

S

G

H

K

T

F

M

I

-

E

R

R

E

M

E

E

K

K

A

R

T

T

E

R

L

-

A

-

E

-

Y

-

G

-

F

-

D

R

L

I

R

R

T

I

P

L

M

G

D

S

S

A

I

L

K

N

M

A

C

A

R

Y

I

V

A

G

E

A

G

G

S

R

A

V

D

D

I

F

Y

F

P

V

-

T

-

W

R

R

H

I

G

N

P

P

T

-

S

-

E

-

W

W

D
|
D

T

I

A

A

G

G

H

L

A

I

V

I

L

V

V

K

A

E

A

A

G

G

A

M

F

V

T

T

Q

D

P

F

D

S

G

G

S

K

P

E

F

A

L

N

Y

A

G

F

K

S

A

K

D

N

Q

F

S

I

F

F

R

S

N

N

G

G

active site: D79 (= D95), I81 (≠ V97), D82 (= D98), T84 (= T100), D201 (= D221)
binding magnesium ion: E65 (= E75), D79 (= D95), I81 (≠ V97), D82 (= D98)

O33832 Fructose-1,6-bisphosphatase/inositol-1-monophosphatase; FBPase/IMPase; Inositol-1-phosphatase; I-1-Pase; EC 3.1.3.11; EC 3.1.3.25 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
25% identity, 89% coverage: 20:256/265 of query aligns to 9:236/256 of O33832

query
sites
O33832

K

K

I

L

T

L

E

R

E

K

A

V

A

G

V

H

V

L

I

L

L

M

P

I

F

H

W

W

-

G

R

R

T

V

E

D

L

N

A

V

V

E

A

K

Q

K

K

T

A

G

D

F

E

K

S

D

P

I

V

V

T

T

E

E

A

I

D

D

R

R

A

E

G

A

E

Q

R

R

L

M

I

I

L

V

E

D

R

E

L

I

A

R

A

K

L

F

Y

F

P

P

A

D

I

E

P

N

V

I

I

M

S

A

E
|
E

E

E

D

G

A

I

S

F

E

E

F

-

G

-

T

-

P

-

E

-

S

-

V

K

G

G

P

D

R

R

F

L

F

W

L

I

V

I

D
|
D

P

P

V
x
I

D

D

G

G

T

T

K

I

A

N

F

F

V

V

R

H

G

G

D

L

P

P

N

N

F

F

T

S

V

I

N

S

I

L

G

A

L

Y

I

V

E

E

H

N

G

G

V

E

P

V

V

K

A

L

G

G

A

V

V

V

C

H

A

A

P

P

A

A

T

L

G

N

E

E

V

T

W

L

F

Y

T

A

T

E

A

E

D

G

G

S

A

G

A

A

K

F

R

F

A

N

G

G

P

E

D

R

-

I

-

R

-

V

A

S

A

E

E

N

A

A

P

S

I

L

R

E

V

E

R

C

P

V

W

G

P

S

T

T

G

G

Q

S

A

Y

L

V

G

D

L

F

I

T

S

G

H

K

T

F

M

I

-

E

R

R

E

M

E

E

K

K

A

R

T

T

E

R

L

-

A

-

E

-

Y

-

G

-

F

-

D

R

L

I

R

R

T

I

P

L

M

G

D

S

S

A

I

L

K

N

M

A

C

A

R

Y

I

V

A

G

E

A

G

G

S

R

A

V

D

D

I

F

Y

F

P

V

-

T

-

W

R

R

H

I

G

N

P

P

T

-

S

-

E

-

W

W

D

D

T

I

A

A

G

G

H

L

A

I

V

I

L

V

V

K

A

E

A

A

G

G

A

M

F

V

T

T

Q

D

P

F

D

S

G

G

S

K

P

E

F

A

L

N

Y

A

G

F

K

S

A

K

D

N

Q

F

S

I

F

F

R

S

N

N

G

G

E65 (= E75) binding Mg(2+)
D79 (= D95) binding Mg(2+)
I81 (≠ V97) binding Mg(2+)

Q6NPM8 Bifunctional phosphatase IMPL2, chloroplastic; Histidinol-phosphatase; Histidinol-phosphate phosphatase; HPP; Inositol-phosphate phosphatase; L-galactose 1-phosphate phosphatase; Protein HISTIDINE BIOSYNTHESIS 7; Protein MYO-INOSITOL MONOPHOSPHATASE-LIKE 2; EC 3.1.3.15; EC 3.1.3.25; EC 3.1.3.93 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 89% coverage: 28:263/265 of query aligns to 100:331/346 of Q6NPM8

query
sites
Q6NPM8

V

V

I

I

L

R

P

K

F

Y

W

F

R

R

T

K

E

K

L

F

A

D

V

I

A

V

Q

D

K

K

A

D

D

D

E

M

S

S

P

P

V

V

T

T

E

I

A

A

D

D

R

Q

A

M

G

A

E

E

R

E

L

A

I

M

L

V

E

S

R

I

L

I

A

F

A

Q

L

N

Y

L

P

P

A

S

I

H

P

A

V

I

I

Y

S

G

E

E

D

K

A

G

S

-

E

-

F

W

G

R

T

C

P

K

E

E

S

E

V

S

G

A

P

D

R

Y

F

V

F

W

L

V

V

L

D

D

P

P

V

I

D

D

G

G

T

T

K

K

A

S

F

F

V

I

R

T

G

G

D

K

P

P

N

V

F

F

T

G

V

T

N

L

I

I

G

A

L

L

I

L

E

Y

H

K

G

G

V

K

P

P

V

I

A

L

G
|
G

A

L

V

I

C

D

A

Q

P

P

A

I

T

L

G

K

E

E

V

R

W

W

F

I

T

G

T

M

A

N

D

G

G

R

A

R

A

T

K

K

R

L

A

N

G

G

P

E

D

D

A

I

A

S

E

-

A

-

P

-

I

T

R

R

V

S

R

C

P

P

W

K

P

L

T

S

G

Q

Q

A

A

Y

L

L

G

Y

L

T

I

T

S

S

H

P

T

H

M

L

R

F

E

S

E

E

K

E

A

A

T

E

E

K

L

A

A

Y

A

S

E

R

Y

V

G

R

F

D

D

K

L

V

R

K

T

V

P

P

M

L

D

Y

-

G

-

C

S

D

S

C

I

Y

K

A

M

Y

C

A

R

L

I

L

A

A

E

S

G

G

S

F

A

V

D

D

I

L

Y

V

P

I

R

E

H

S

G

G

P

-

T

L

S

K

E

P

W

Y

D

D

T

F

A

L

A

A

G

L

H

V

A

P

V

V

L

I

V

E

A

G

A

A

G

G

A

T

F

I

T

T

Q

D

P

W

D

T

G

G

S

K

P

R

F

F

L

L

Y

W

G

E

K

A

A

S

D

S

Q

S

S

A

F

V

R

A

N

T

G

S

W

F

F

N

V

V

A

V

R

A

G

A

G

G

G195 (= G125) mutation to R: Loss of histidinol-phosphatase activity.

5djkA Structure of m. Tuberculosis cysq, a pap phosphatase with po4 and 2ca bound (see paper)
31% identity, 75% coverage: 52:250/265 of query aligns to 39:225/251 of 5djkA

query
sites
5djkA

D

D

R

R

A

Q

G

A

E

N

R

S

L

L

I

L

L

L

E

R

R

R

L

L

A

Q

A

A

L

E

Y

R

P

P

A

G

I

D

P

A

V

V

I

L

S

S

E
|
E

E

E

D

A

A

H

S

D

E

D

F

L

G

A

T

R

P

L

E

K

S

S

V

-

G

-

P

D

R

R

F

V

F

W

L

I

V

I

D
|
D

P

P

V
x
L

D
|
D

G

G

T

T

K

R

A

E

F

F

V

S

R

T

-

P

G

G

D

R

P

D

N

D

F

W

T

A

V

V

N

H

I

I

G

A

L

L

I

W

E

R

H

R

G

P

V

E

P

I

V

T

A

D

G

A

A

A

V

V

C

A

A

L

P

P

A

A

T

R

G

G

E

N

V

V

W

V

F

Y

T

R

T

T

A

-

D

D

G

T

A

V

A

T

K

S

R

G

A

A

G

A

P

P

D

A

A

G

A

V

E

P

A

G

P

T

I

L

R

R

V

I

R

A

P

V

W

S

P

A

T

T

G

R

Q

P

A

P

L

A

G

V

L

L

I

-

S

-

H

H

T

R

M

I

R

R

E

Q

E

T

K

L

A

A

T

I

E

Q

L

-

A

P

A

V

E

S

Y

I

G

G

F

-

D

-

L

-

R

-

T

-

P

-

M

-

D

S

S

A

S

G

I

A

K

K

M

A

C

M

R

A

I

V

A

I

E

D

G

G

S

Y

A

V

D

D

I

A

Y

Y

P

L

R

H

H

A

G

G

P

G

T

Q

S

W

E

E

W

W

D
|
D

T

S

A

A

G

P

H

A

A

G

V

V

L

M

V

L

A

A

G

G

G

M

A

H

F

A

T

S

Q

R

P

L

D

D

G

G

S

S

P

P

F

L

L

R

Y

Y

G

N

K

Q

A

L

D

D

binding calcium ion: E62 (= E75), D80 (= D95), D80 (= D95), L82 (≠ V97), D83 (= D98), D196 (= D221)

5djjA Structure of m. Tuberculosis cysq, a pap phosphatase with po4 and 2mg bound (see paper)
31% identity, 75% coverage: 52:250/265 of query aligns to 45:231/257 of 5djjA

query
sites
5djjA

D

D

R

R

A

Q

G

A

E

N

R

S

L

L

I

L

L

L

E

R

R

R

L

L

A

Q

A

A

L

E

Y

R

P

P

A

G

I

D

P

A

V

V

I

L

S

S

E
|
E

E

E

D

A

A

H

S

D

E

D

F

L

G

A

T

R

P

L

E

K

S

S

V

-

G

-

P

D

R

R

F

V

F

W

L

I

V

I

D
|
D

P

P

V
x
L

D
|
D

G
|
G

T
|
T

K

R

A

E

F

F

V

S

R

T

-

P

G

G

D

R

P

D

N

D

F

W

T

A

V

V

N

H

I

I

G

A

L

L

I

W

E

R

H

R

G

P

V

E

P

I

V

T

A

D

G

A

A

A

V

V

C

A

A

L

P

P

A

A

T

R

G

G

E

N

V

V

W

V

F

Y

T

R

T

T

A

-

D

D

G

T

A

V

A

T

K

S

R

G

A

A

G

A

P

P

D

A

A

G

A

V

E

P

A

G

P

T

I

L

R

R

V

I

R

A

P

V

W

S

P

A

T

T

G

R

Q

P

A

P

L

A

G

V

L

L

I

-

S

-

H

H

T

R

M

I

R

R

E

Q

E

T

K

L

A

A

T

I

E

Q

L

-

A

P

A

V

E

S

Y

I

G

G

F

-

D

-

L

-

R

-

T

-

P

-

M

-

D

S

S

A

S

G

I

A

K

K

M

A

C

M

R

A

I

V

A

I

E

D

G

G

S

Y

A

V

D

D

I

A

Y

Y

P

L

R

H

H

A

G

G

P

G

T

Q

S

W

E

E

W

W

D
|
D

T

S

A

A

G

P

H

A

A

G

V

V

L

M

V

L

A

A

G

G

G

M

A

H

F

A

T

S

Q

R

P

L

D

D

G

G

S

S

P

P

F

L

L

R

Y

Y

G

N

K

Q

A

L

D

D

binding magnesium ion: E68 (= E75), D86 (= D95), D86 (= D95), L88 (≠ V97), D89 (= D98), D202 (= D221)
binding phosphate ion: E68 (= E75), D86 (= D95), L88 (≠ V97), D89 (= D98), G90 (= G99), T91 (= T100)

C4M633 Inositol polyphosphate 1-phosphatase; EhIPPase; 3'(2'),5'-bisphosphate nucleotidase; EC 3.1.3.57; EC 3.1.3.7 from Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) (see paper)
24% identity, 89% coverage: 11:246/265 of query aligns to 5:248/285 of C4M633

query
sites
C4M633

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E68 (= E75) binding Mg(2+); binding Mg(2+)
D106 (= D95) binding Mg(2+); binding Mg(2+)
L108 (≠ V97) binding Mg(2+)
D109 (= D98) binding Mg(2+)
D223 (= D221) binding Mg(2+)

4qxdB Crystal structure of inositol polyphosphate 1-phosphatase from entamoeba histolytica (see paper)
24% identity, 89% coverage: 11:246/265 of query aligns to 5:248/289 of 4qxdB

query
sites
4qxdB

L

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active site: E68 (= E75)
binding magnesium ion: E68 (= E75), D106 (= D95), D106 (= D95), L108 (≠ V97), D109 (= D98), D109 (= D98), D223 (= D221)
binding phosphate ion: E68 (= E75), L108 (≠ V97), D109 (= D98), G110 (= G99), T111 (= T100)

P9WKJ1 3'-phosphoadenosine 5'-phosphate phosphatase; PAP phosphatase; 3'(2'),5'-bisphosphate nucleotidase; 3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase; D-fructose-1,6-bisphosphate 1-phosphohydrolase; DPNPase; Fructose-1,6-bisphosphatase; FBPase; Inositol-1-monophosphatase; I-1-Pase; IMPase; Inositol-1-phosphatase; EC 3.1.3.7; EC 3.1.3.11; EC 3.1.3.25 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 75% coverage: 52:250/265 of query aligns to 50:241/267 of P9WKJ1

query
sites
P9WKJ1

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L71 (≠ I73) mutation to A: No effect on IMPase and FBPase activities. Much less sensitive to inhibition by Li(+).
D94 (= D98) mutation to N: Less than 3% of wild-type IMPase and FBPase activities.

Sites not aligning to the query:

40 D→N: Less than 2% of wild-type IMPase and FBPase activities.

5djgA Structure of m. Tuberculosis cysq, a pap phosphatase with pap, mg, and li bound (see paper)
29% identity, 75% coverage: 52:250/265 of query aligns to 45:228/254 of 5djgA

query
sites
5djgA

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D

binding adenosine-3'-5'-diphosphate: E68 (= E75), D86 (= D95), D89 (= D98), G90 (= G99), S149 (≠ R157), R152 (≠ P160), G172 (= G187), S173 (≠ D195), K177 (= K199), H191 (≠ R213), G193 (= G215), G194 (≠ P216), Q195 (≠ T217), D199 (= D221)
binding lithium ion: D86 (= D95), D89 (= D98), D199 (= D221)
binding magnesium ion: E68 (= E75), D86 (= D95), L88 (≠ V97)

1jp4A Crystal structure of an enzyme displaying both inositol-polyphosphate 1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities (see paper)
25% identity, 85% coverage: 36:260/265 of query aligns to 30:280/302 of 1jp4A

query
sites
1jp4A

E

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N

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x
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x
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A

A

active site: D47 (= D52), E70 (= E75), D111 (= D95), V113 (= V97), D114 (= D98), T116 (= T100), D241 (= D221)
binding adenosine monophosphate: D114 (= D98), T189 (≠ S171), H192 (≠ M174), G213 (≠ P193), G214 (≠ D195), K218 (= K199), F232 (≠ R213), G236 (vs. gap), C237 (≠ T217), D241 (= D221)
binding magnesium ion: E70 (= E75), D111 (= D95), D111 (= D95), V113 (= V97), D114 (= D98), D241 (= D221)
binding phosphate ion: E70 (= E75), D111 (= D95), V113 (= V97), D114 (= D98), G115 (= G99), T116 (= T100)

5djhA Structure of m. Tuberculosis cysq, a pap phosphatase with amp, po4, and 3mg bound (see paper)
28% identity, 75% coverage: 52:250/265 of query aligns to 45:226/252 of 5djhA

query
sites
5djhA

D

D

R

R

A

Q

G

A

E

N

R

S

L

L

I

L

L

L

E

R

R

R

L

L

A

Q

A

A

L

E

Y

R

P

P

A

G

I

D

P

A

V

V

I

L

S

S

E
|
E

E

E

D

A

A

H

S

D

E

D

F

L

G

A

T

R

P

L

E

K

S

S

V

-

G

-

P

D

R

R

F

V

F

W

L

I

V

I

D
|
D

P

P

V
x
L

D
|
D

G
|
G

T
|
T

K

R

A

E

F

F

V

S

R

T

-

P

G

G

D

R

P

D

N

D

F

W

T

A

V

V

N

H

I

I

G

A

L

L

I

W

E

R

H

R

G

S

V

P

P

E

V

I

A

T

-

D

G

A

A

A

V

V

C

A

A

L

P

P

A

A

T

R

G

G

E

N

V

V

W

V

F

Y

T

R

T

T

A

-

D

-

G

-

A

-

K

-

R

-

A

-

G

-

P

D

D

T

A

V

A

T

E

S

A

V

P

P

I

G

R

T

V

L

R

R

P

I

W

A

P

V

T
x
S

G

A

Q

T

A
x
R

L

P

G

P

L

A

I

V

S

L

H

H

T

R

M

I

R

R

E

Q

E

T

K

L

A

A

T

I

E

Q

L

-

A

P

A

V

E

S

Y

I

G
|
G

F

-

D

-

L

-

R

-

T

-

P

-

M

-

D
x
S

S

A

S

G

I

A

K
|
K

M

A

C

M

R

A

I

V

A

I

E

D

G

G

S

Y

A

V

D

D

I

A

Y

Y

P

L

R
x
H

H

A

G
|
G

P
x
G

T
x
Q

S

W

E

E

W

W

D
|
D

T

S

A

A

G

P

H

A

A

G

V

V

L

M

V

L

A

A

G

G

G

M

A

H

F

A

T

S

Q

R

P

L

D

D

G

G

S

S

P

P

F

L

L

R

Y

Y

G

N

K

Q

A

L

D

D

binding adenosine monophosphate: D89 (= D98), S147 (≠ T163), R150 (≠ A166), G170 (= G187), S171 (≠ D195), K175 (= K199), H189 (≠ R213), G191 (= G215), G192 (≠ P216), Q193 (≠ T217), D197 (= D221)
binding magnesium ion: E68 (= E75), D86 (= D95), D86 (= D95), L88 (≠ V97), D89 (= D98), D197 (= D221)
binding phosphate ion: E68 (= E75), D86 (= D95), L88 (≠ V97), D89 (= D98), G90 (= G99), T91 (= T100)

P0ADG4 Nus factor SuhB; Inositol-1-monophosphatase; I-1-Pase; IMPase; Inositol-1-phosphatase; EC 3.1.3.25 from Escherichia coli (strain K12) (see 5 papers)
27% identity, 76% coverage: 40:241/265 of query aligns to 32:232/267 of P0ADG4

query
sites
P0ADG4

A

S

Q

Q

K

K

A

G

D

S

E

N

S

D

P

F

V

V

T

T

E

N

A

V

D

D

R

K

A

A

G

A

E

E

R

A

L

V

I

I

L

I

E

D

R

T

L

I

A

R

A

K

L

S

Y

Y

P

P

A

Q

I

H

P

T

V

I

I

I

S

T

E
|
E

E

E

D

S

A

G

S

E

E

L

F

E

G

G

T

T

P

D

E

Q

S

D

V

V

G

Q

P

-

R

-

F

-

F

W

L

V

V

I

D
|
D

P

P

V
x
L

D
|
D

G

G

T

T

K

T

A

N

F

F

V

I

R

K

G

R

D

L

P

P

N

H

F

F

T

A

V

V

N

S

I

I

G

A

L

V

I

R

E

I

H

K

G

G

V

R

P

T

V

E

A

V

G

A

A

V

V

V

C

Y

A

D

P

P

A

M

T

R

G

N

E

E

V

L

W

F

F

T

T

A

T

T

A

R

D

G

G

Q

A

G

A

A

K

Q

R

L

A

N

G

G

P

-

D

-

A

-

E

-

A

-

P

-

I

Y

R
|
R

V

L

R

R

P

G

W

S

P

T

T

A

G

R

Q

D

A

L

L

D

G

G

L

T

I

I

S

L

H

A

T

T

M

G

R

F

E

P

E

F

K

K

A

A

T

K

E

Q

L

Y

A

A

A

T

E

T

Y

Y

-

I

-

N

-

I

-

V

-
x
G

-

K

-

L

-

F

-

N

-

E

G

C

F

A

D

D

L

F

R
|
R

T
x
R

P

T

M

G

D

S

S

A

I

L

K

D

M

L

C

A

R

Y

I

V

A

A

E

A

G

G

S

R

A

V

D

D

I

G

Y

F

P

F

R

E

H

I

G

G

P

-

T

L

S

R

E

P

W

W

D

D

T

F

A

A

G

G

H

E

A

L

V

L

L

V

V

R

A

E

A

A

G

G

A

I

F

V

T

S

Q

D

P

F

D

T

G

G

E67 (= E75) binding Mg(2+)
D84 (= D95) binding Mg(2+)
L86 (≠ V97) binding Mg(2+)
D87 (= D98) mutation to N: Loss of IMPase activity, still complements dnaB121 helicase mutation.
R139 (= R157) mutation to C: In suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with A-250.
G173 (vs. gap) mutation to V: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNA polymerase (RNAP).
R183 (= R191) mutation to A: Some growth at 30 degrees Celsius, greater IMPase activity, partially inhibited by RNAP.
R184 (≠ T192) mutation to A: Grows at 30 degrees Celsius, makes more dimer, partially inhibited by RNAP, crystallizes.; mutation to I: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNAP.

Sites not aligning to the query:

250 V→A: In suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with C-139.
251:254 KAML→AAMA: 3-fold decreased affinity for NusA, less efficient in delaying or suppressing Rho-dependent transcription termination.

2qflA Structure of suhb: inositol monophosphatase and extragenic suppressor from e. Coli (see paper)
27% identity, 76% coverage: 40:241/265 of query aligns to 32:232/262 of 2qflA

query
sites
2qflA

A

S

Q

Q

K

K

A

G

D

S

E

N

S

D

P

F

V

V

T

T

E

N

A

V

D
|
D

R

K

A

A

G

A

E

E

R

A

L

V

I

I

L

I

E

D

R

T

L

I

A

R

A

K

L

S

Y

Y

P

P

A

Q

I

H

P

T

V

I

I

I

S

T

E
|
E

E

E

D

S

A

G

S

E

E

L

F

E

G

G

T

T

P

D

E

Q

S

D

V

V

G

Q

P

-

R

-

F

-

F

W

L

V

V

I

D
|
D

P

P

V
x
L

D
|
D

G

G

T
|
T

K

T

A

N

F

F

V

I

R

K

G

R

D

L

P

P

N

H

F

F

T

A

V

V

N

S

I

I

G

A

L

V

I

R

E

I

H

K

G

G

V

R

P

T

V

E

A

V

G

A

A

V

V

V

C

Y

A

D

P

P

A

M

T

R

G

N

E

E

V

L

W

F

F

T

T

A

T

T

A

R

D

G

G

Q

A

G

A

A

K

Q

R

L

A

N

G

G

P

-

D

-

A

-

E

-

A

-

P

-

I

Y

R

R

V

L

R

R

P

G

W

S

P

T

T

A

G

R

Q

D

A

L

L

D

G

G

L

T

I

I

S

L

H

A

T

T

M

G

R

F

E

P

E

F

K

K

A

A

T

K

E

Q

L

Y

A

A

A

T

E

T

Y

Y

-

I

-

N

-

I

-

V

-

G

-

K

-

L

-

F

-

N

-

E

G

C

F

A

D

D

L

F

R

R

T

A

P

T

M
x
G

D
x
S

S
x
A

S

A

I

L

K

D

M

L

C

A

R

Y

I

V

A

A

E

A

G

G

S

R

A

V

D

D

I

G

Y

F

P

F

R

E

H

I

G

G

P

-

T

L

S

R

E

P

W

W

D
|
D

T

F

A

A

G

G

H

E

A

L

V

L

L

V

V

R

A

E

A

A

G

G

A

I

F

V

T

S

Q

D

P

F

D

T

G

G

active site: D44 (= D52), E67 (= E75), D84 (= D95), L86 (≠ V97), D87 (= D98), T89 (= T100), D212 (= D221)
binding ethyl acetate: D87 (= D98), G186 (≠ M194), S187 (≠ D195), A188 (≠ S196)

6zk0AAA human impase with ebselen (see paper)
25% identity, 89% coverage: 9:244/265 of query aligns to 3:240/274 of 6zk0AAA

query
sites
6zk0AAA

Q

Q

D

E

L

C

A

M

D

D

W

Y

G

A

R

V

T

T

L

L

A

A

K

R

I

-

T

-

E

-

E

Q

A

A

A

G

V

E

V

V

I

V

L

C

P

E

F

A

W

I

R

K

T

N

E

E

L

M

A

N

V

V

A

M

Q

L

K

K

A

S

D

-

E

-

S

S

P

P

V

V

-

D

-

L

-

V

T

T

E

A

A

T

D

D

R

Q

A

K

G

V

E

E

R

K

L

M

I

L

L

I

E

S

R

S

L

I

A

K

A

E

L

K

Y

Y

P

P

A

S

I

H

P

S

V

F

I

I

S

G

E
|
E

E

E

D

S

A

V

S

A

E

A

F

G

G

E

T

K

P

S

E

I

S

L

V

T

G

D

P

N

R

P

F

T

F

W

L

I

V

I

D
|
D

P

P

V
x
I

D
|
D

G

G

T

T

K

T

A

N

F

F

V

V

R

H

G

R

D

F

P

P

N

F

F

V

T

A

V

V

N

S

I

I

G

G

L

F

-

A

-

V

-

N

-

K

I

I

E

E

H

F

G

G

V

V

-

V

-

Y

-

S

P

C

V

V

A

E

G

G

A
x
K

V

M

C

Y

A

T

P

A

A

R

T

K

G

G

E

K

V

G

W

A

F

F

T
x
C

T
x
N

A

G

D
x
Q

G

K

A

L

A

Q

K

V

R

S

A

Q

G

Q

P

E

D

D

A

I

A

T

E

K

A

S

P

-

I

L

R

L

V

V

R

T

P

E

W

L

P

G

T

S

G

S

Q

R

A

T

L

P

G

E

L

T

I

V

S

R

H

M

T

V

M

L

R

S

E

N

E

M

K

E

A

K

T

L

E

F

L

C

A

I

A

P

E

V

Y

H

G

G

F

-

D

-

L

I

R

R

T

S

P

V

M

G

D

T

S

A

I

V

K

N

M

M

C

C

R

L

I

V

A

A

E

T

G

G

S

G

A

A

D

D

I

A

Y

Y

P

Y

R

E

H

M

G

G

P

I

T

H

S

C

E

-

W

W

D

D

T

V

A

A

A

G

G

A

H

G

A

I

V

I

L

V

V

T

A

E

A

A

G

G

A

V

F

L

T

M

Q

D

P

V

D

T

G

G

S

G

P

P

F

F

binding N-phenyl-2-selanylbenzamide: K126 (≠ A126), C138 (≠ T138), N139 (≠ T139), Q141 (≠ D141)
binding manganese (ii) ion: E67 (= E75), D87 (= D95), I89 (≠ V97), D90 (= D98)

Query Sequence

>CCNA_03582 FitnessBrowser__Caulo:CCNA_03582
MSDDKRTVQDLADWGRTLAKITEEAAVVILPFWRTELAVAQKADESPVTEADRAGERLIL
ERLAALYPAIPVISEEDASEFGTPESVGPRFFLVDPVDGTKAFVRGDPNFTVNIGLIEHG
VPVAGAVCAPATGEVWFTTADGAAKRAGPDAAEAPIRVRPWPTGQALGLISHTMREEKAT
ELAAEYGFDLRTPMDSSIKMCRIAEGSADIYPRHGPTSEWDTAAGHAVLVAAGGAFTQPD
GSPFLYGKADQSFRNGWFVARGGRP

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