SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf6N2E2_1718 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1718 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)

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
48% identity, 96% coverage: 3:188/194 of query aligns to 2:185/187 of P00903

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P00903

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C79 (= C80) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H171) mutation to Q: Loss of activity.
E170 (= E173) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
40% identity, 96% coverage: 3:189/194 of query aligns to 75:265/276 of Q42565

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G150 (= G78) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G103) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
36% identity, 99% coverage: 3:194/194 of query aligns to 4:193/193 of P00900

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C84 (= C80) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1i7qB Anthranilate synthase from s. Marcescens (see paper)
36% identity, 99% coverage: 3:194/194 of query aligns to 3:192/192 of 1i7qB

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active site: G58 (= G56), C83 (= C80), L84 (= L81), H169 (= H171), E171 (= E173)
binding glutamic acid: P55 (= P53), G56 (= G54), P57 (= P55), G58 (= G56), C83 (= C80), L84 (= L81), Q87 (= Q84), Y131 (= Y129), H132 (= H130), S133 (= S131), L134 (= L132), H169 (= H171)

Q9LVW7 Carbamoyl-phosphate synthase small chain, chloroplastic; Carbamoyl-phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 96% coverage: 2:188/194 of query aligns to 240:420/430 of Q9LVW7

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Q9LVW7

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H410 (≠ N179) mutation to Y: In ven6-1; reticulate leaf phenotype.

7yc6A GMP synthase [glutamine-hydrolyzing] subunit A
27% identity, 96% coverage: 3:189/194 of query aligns to 2:176/183 of 7yc6A

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binding zinc ion: C76 (= C80), D101 (= D111), E123 (≠ M133), E123 (≠ M133), H136 (≠ R148), C140 (≠ G153), C140 (≠ G153), H158 (= H171)

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
32% identity, 68% coverage: 44:174/194 of query aligns to 230:355/379 of 1ce8B

query
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1ce8B

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P

P

G

G

H

D

P

P

A

A

D

P

V

C

G

D

Y

Y

-

A

I

I

E

T

V

A

I

I

R

Q

H

K

F

F

-

L

Q

E

G

T

R

D

L

I

P

P

L

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

L

L

A

A

F

S

G

G

A

A

Q

K

V

T

C

V

R

K

A

M

P

K

H

F

V

G

M

H

H

H

G

G

K

G

V

N

S

H

T

P

I

V

E

K

N

D

D

V

G

E

K

K

G

N

V

V

Y

-

D

-

H

-

T

-

Q

-

A

-

Q

-

A

V

I

M

R

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

M

A

I

V

S

D

E

E

Q

A

P

T

L

L

P

P

D

A

C

N

L

L

E

R

I

V

T

T

S

H

R

K

S

S

T

L

D

F

D

D

G

G

Y

T

V

L

M

Q

G

G

V

I

R

H

H

R

R

T

H

D

L

K

P

P

V

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C80), H352 (= H171), E354 (= E173)

Sites not aligning to the query:

binding L-ornithine: 119, 122

1jdbF Carbamoyl phosphate synthetase from escherichia coli (see paper)
32% identity, 68% coverage: 44:174/194 of query aligns to 230:355/380 of 1jdbF

query
sites
1jdbF

F

M

S

N

P

P

D

D

F

G

C

I

V

F

L

L

G

S

P

N

G

G

P

P

G

G

H

D

P

P

A

A

D

P

V

C

G

D

Y

Y

-

A

I

I

E

T

V

A

I

I

R

Q

H

K

F

F

-

L

Q

E

G

T

R

D

L

I

P

P

L

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

L

L

A

A

F

S

G

G

A

A

Q

K

V

T

C

V

R

K

A

M

P

K

H

F

V

G

M

H

H

H

G

G

K

G

V

N

S

H

T

P

I

V

E

K

N

D

D

V

G

E

K

K

G

N

V

V

Y

-

D

-

H

-

T

-

Q

-

A

-

Q

-

A

V

I

M

R

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

M

A

I

V

S

D

E

E

Q

A

P

T

L

L

P

P

D

A

C

N

L

L

E

R

I

V

T

T

S

H

R

K

S

S

T

L

D

F

D

D

G

G

Y

T

V

L

M

Q

G

G

V

I

R

H

H

R

R

T

H

D

L

K

P

P

V

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C80), H352 (= H171), E354 (= E173)

Sites not aligning to the query:

binding glutamine: 119, 122

3r75B Crystal structure of 2-amino-2-desoxyisochorismate synthase (adic) synthase phze from burkholderia lata 383 in complex with benzoate, pyruvate, glutamine and contaminating zn2+ (see paper)
30% identity, 92% coverage: 2:180/194 of query aligns to 432:606/622 of 3r75B

query
sites
3r75B

K

R

V

A

F

L

L

I

I

V

D

D

A

A

Y

E

D

D

S

H

F

F

V

T

F

A

I

M

I

I

S

A

Q

Q

Y

Q

L

L

E

S

Q

S

L

L

G

G

L

L

E

A

T

T

H

E

V

V

-

C

E

G

R

V

H

H

D

D

V

A

P

V

D

D

L

L

I

A

Q

R

R

Y

I

-

E

-

A

-

F

-

S

-

P

-

D

D

F

V

C

V

V

V

L

M

G

G

P

P

G

G

P

P

G

G

H

D

P

P

A

S

D

D

V

A

G

G

Y

D

I

P

E

R

V

I

I

A

R

R

H

L

F

Y

-

A

-

W

-

L

-

R

-

H

-

L

-

I

-

D

Q

E

G

G

R

K

L

-

P

P

L

F

L

M

G

A

V

V

C
|
C

L

L

G

S

H

H

Q

Q

A

I

I

L

G

N

L

A

A

I

F

L

G

G

A

I

Q

P

V

L

C

V

R

R

A

R

P

E

H

V

V

P

M

N

H

Q

G

G

K

I

V

Q

S

V

T

E

I

I

E

D

N

L

D

F

G

G

K

Q

-

R

-

E

-

R

-

V

G

G

V

F

Y
|
Y

D

N

H

T

T

Y

Q

V

A

A

Q

Q

A

T

I

V

R

R

A

-

T

-

R

-

Y

-

H

-

S

-

L

-

M

-

I

-

S

D

E

E

Q

M

P

D

L

V

P

D

D

G

C

V

L

G

E

T

I

V

T

A

-

I

S

S

R

R

S

D

T

P

D

R

D

T

G

G

Y

E

V

V

M

H

G

A

V

L

R

R

H

G

R

P

H

T

L

F

P

-

V

-

E

S

G

S

V

M

Q

Q

F

F

H
|
H

P

A

E

E

S

S

I

V

L

L

T

T

E

V

N

D

G

G

binding zinc ion: C512 (= C80), Y552 (= Y116), H597 (= H171)

Sites not aligning to the query:

active site: 143, 195, 238, 273, 298, 322, 346, 363, 376, 380
binding magnesium ion: 238, 376
binding pyruvic acid: 322, 345, 346, 360, 361, 380

P05990 CAD protein; Protein rudimentary; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
28% identity, 69% coverage: 40:173/194 of query aligns to 226:355/2224 of P05990

query
sites
P05990

R

R

I

L

E

E

A

D

F

E

S

Q

P

F

D

D

F

A

C

L

V

F

L

L

G

S

P

N

G

G

P

P

G

G

H

N

P

P

A

E

D

S

V

C

G

D

Y

Q

I

I

-

V

E

Q

V

Q

I

V

R

R

H

K

F

V

-

I

-

E

Q

E

G

G

R

Q

L

K

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

L

K

A

A

F

I

G

G

A

-

Q

-

V

-

C

C

R

S

A

T

P

Y

H

K

V

M

M

K

H

Y

G

G

K

-

V

-

S

-

T

-

I

-

E

-

N

N

D

R

G

G

K

H

G

N

V

L

-

P

-

C

Y

L

D

H

H

R

T

A

Q

T

A

G

Q

R

A

C

I

L

R

M

A

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

M

A

I

V

S

D

E

L

Q

E

P

Q

L

L

P

P

D

D

C

G

L

W

E

S

I

E

T

L

S

F

R

V

S

N

T

A

D

N

D

D

G

G

Y

T

V

N

M

E

G

G

V

I

R

V

H

H

R

A

H

S

L

K

P

P

V

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
1883 modified: Phosphoserine
1885 modified: Phosphoserine
1892 modified: Phosphoserine
1894 modified: Phosphoserine

P27708 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
29% identity, 63% coverage: 51:173/194 of query aligns to 219:338/2225 of P27708

query
sites
P27708

L

L

G

S

P

N

G

G

P

P

G

G

H

D

P

P

A

A

D

S

V

-

G

-

Y

Y

I

P

E

S

V

V

I

V

R

S

H

T

F

L

Q

S

G

R

R

V

L

L

-

S

-

E

-

P

-

N

-

P

-

R

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

L

L

A

A

F

I

G

G

A

A

Q

K

V

T

C

Y

R

K

A

M

P

R

H

Y

V

G

M

N

H

R

G

G

K

H

V

N

S

Q

T

P

I

C

E

L

N

L

D

V

G

G

K

S

G

G

V

-

Y

-

D

-

H

-

T

-

Q

-

A

-

Q

R

A

C

I

F

R

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

M

A

I

V

S

E

E

T

Q

D

P

S

L

L

P

P

D

A

C

D

L

W

E

A

I

P

T

L

S

F

R

T

S

N

T

A

D

N

D

D

G

G

Y

S

V

N

M

E

G

G

V

I

R

V

H

H

R

N

H

S

L

L

P

P

V

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; unknown pathological significance; dbSNP:rs751610198
177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
456 modified: Phosphothreonine; by MAPK1
735 Y → C: in a colorectal cancer sample; somatic mutation
1406 modified: Phosphoserine; by PKA
1471 binding ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding ; H→A: No zinc-binding and no catalytic activity.
1475 binding
1505 binding
1512 D→N: No change in catalytic activity.
1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
1562 T→A: Abolishes dihydroorotase activity.
1563 F→A: Abolishes dihydroorotase activity.
1590 binding ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding ; C→S: Reduces dihydroorotase activity.
1614 binding ; H→A: Abolishes dihydroorotase activity.
1637 binding ; E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding
1686 binding ; binding ; D→N: Abolishes dihydroorotase activity.
1690 binding ; H→N: 3% of wild-type catalytic activity.
1789:2225 natural variant: Missing (in DEE50; unknown pathological significance)
1859 modified: Phosphoserine; by RPS6KB1 and PKA
1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
1900 modified: Phosphoserine

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
21% identity, 97% coverage: 2:189/194 of query aligns to 7:197/501 of 1gpmA

query
sites
1gpmA

K

R

V

I

F

L

L

I

I

L

D

D

A

F

Y

G

D

S

S

Q

F

Y

V

T

F

Q

I

L

I

V

S

A

Q

R

Y

R

L

V

E

R

Q

E

L

L

G

G

L

V

E

Y

T

C

H

E

V

L

E

W

R

A

H

W

D

D

V

V

P

T

D

E

L

-

I

-

Q

A

R

Q

I

I

E

R

A

D

F

F

S

N

P

P

D

S

F

G

C

I

V

I

L

L

G

S

P

G

G
|
G

P

P

G

E

H

S

P

T

A

T

D

E

V

E

G

N

Y

S

I

P

E

R

V

A

I

P

R

Q

H

Y

-

V

F

F

Q

E

G

A

R

G

L

V

P

P

L

V

L

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

T

I

M

G

A

L

M

A

Q

F

L

G

G

A

G

Q

H

V

V

C

E

R

A

A

S

P

N

H

E

V

R

M

E

H

F

G

G

K

Y

V

A

S

Q

T

V

-

E

I

V

E

V

N

N

D

D

G

S

-

A

-

L

-

V

K

R

G

G

V

I

Y

E

D

D

H

A

T

L

Q

T

A

A

Q

D

A

G

-

K

-

P

-

L

I

L

R

D

A

V

T

W

R

M

Y

S

H

H

S

G

L

D

M

K

I

V

S

T

E

A

Q

I

P

P

L

-

P

S

D

D

C

F

L

I

E

T

I

V

T

A

S

S

R

T

S

E

T

S

D

C

D

P

G

F

Y

A

V

I

M

M

G

A

V

N

R

E

H

E

R

K

H

R

L

F

P

-

V

-

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

E

R

N

Q

G

G

L

M

D

R

L

M

F

L

R

E

S

R

F

F

I

V

R

R

active site: G57 (= G54), C84 (= C80), Y85 (≠ L81), H179 (= H171), E181 (= E173)

Sites not aligning to the query:

active site: 237, 357
binding adenosine monophosphate: 231, 232, 233, 238, 256, 257, 258, 313
binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
22% identity, 96% coverage: 3:188/194 of query aligns to 28:207/693 of P49915

query
sites
P49915

V

V

F

V

L

I

I

L

D

D

A

A

Y

G

D

A

S

Q

F

Y

V

G

F

K

I

V

I

I

S

D

Q

R

Y

R

L

V

E

R

Q

E

L

L

G

F

L

V

E

Q

T

S

H

E

V

I

E

F

R

P

H

L

D

E

V

T

P

P

D

A

L

F

I

A

Q

I

R

K

I

E

E

Q

A

G

F

F

S

R

P

A

D

I

F

I

C

I

V

S

L

G

G

G

P

P

G

N

P

S

G

V

H

Y

P

A

A

E

D

D

V

A

G

P

Y

W

I

F

E

D

V

P

I

A

R

I

H

F

F

T

Q

I

G

G

R

K

L

-

P

P

L

V

L

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

A

M

I

M

G

N

L

K

A

V

F

F

G

G

A

G

Q

T

V

V

C

H

R

K

A

K

P

S

H

V

V

R

M

E

H

D

G

G

K

V

V

F

S

N

T

I

I

S

E

V

N

D

D

N

G

T

K

C

G

S

V

L

Y

F

D

R

H

G

T

L

Q

Q

A

K

Q

E

A

E

I

V

R

V

A

L

T

L

R

T

Y

H

H

G

S

D

L

-

M

-

I

-

S

S

E

V

Q

D

P

K

L

V

P

A

D

D

C

G

L

F

E

K

I

V

T

V

S

A

R

R

S

S

T

G

D

N

D

-

G

-

Y

I

V

V

M

A

G

G

V

I

R

A

H

N

R

E

H

S

L

K

P

K

V

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

E

E

N

N

G

G

L

K

D

V

L

I

F

L

R

K

S

N

F

F

I

L

C104 (= C80) active site, For GATase activity
H190 (= H171) active site, For GATase activity
E192 (= E173) active site, For GATase activity

Sites not aligning to the query:

337 binding
522 binding
610 binding
685 binding
691 binding

P08955 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
27% identity, 65% coverage: 47:173/194 of query aligns to 215:338/2225 of P08955

query
sites
P08955

D

D

F

G

C

L

V

F

L

L

G

S

P

N

G

G

P

P

G

G

H

D

P

P

A

A

D

S

-

Y

-

P

-

G

-

V

V

V

G

A

Y

T

I

L

E

N

V

R

I

V

R

L

H

S

F

E

Q

P

G

N

R

P

L

R

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

L

L

A

A

F

I

G

G

A

A

Q

K

V

T

C

Y

R

K

A

M

P

R

H

Y

V

G

M

N

H

R

G

G

K

H

V

N

S

Q

T

P

I

C

E

L

N

L

D

V

G

G

K

T

G

G

V

-

Y

-

D

-

H

-

T

-

Q

-

A

-

Q

R

A

C

I

F

R

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

M

A

I

V

S

D

E

A

Q

D

P

S

L

L

P

P

D

A

C

G

L

W

E

T

I

P

T

L

S

F

R

T

S

N

T

A

D

N

D

D

G

C

Y

S

V

N

M

E

G

G

V

I

R

V

H

H

R

D

H

S

L

L

P

P

V

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.

2vxoB Human gmp synthetase in complex with xmp (see paper)
23% identity, 96% coverage: 3:188/194 of query aligns to 6:182/658 of 2vxoB

query
sites
2vxoB

V

V

F

V

L

I

I

L

D

D

A

A

Y

G

D

A

S

Q

F

Y

V

G

F

K

I

V

I

I

S

D

Q

R

Y

R

L

V

E

R

Q

E

L

L

G

F

L

V

E

Q

T

S

H

E

V

I

E

F

R

P

H

L

D

E

V

T

P

P

D

A

L

F

I

A

Q

I

R

K

I

E

E

Q

A

G

F

F

S

R

P

A

D

I

F

I

C

I

V

S

L

G

G
|
G

P

P

G

N

P

S

G

V

H

Y

P

A

A

E

D

D

V

A

G

P

Y

W

I

F

E

D

V

P

I

A

R

I

H

F

F

T

Q

I

G

G

R

K

L

-

P

P

L

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

M

I

M

G

N

L

K

A

V

F

F

G

G

A

G

Q

T

V

V

C

-

R

-

A

-

P

-

H

H

V

K

M

K

H

S

G

D

K

G

V

V

S

F

T

N

I

I

E

S

N

V

D

D

G

N

K

T

-

C

G

S

V

L

Y

F

D

R

H

G

T

L

Q

Q

A

K

Q

E

A

E

I

V

R

V

A

L

T

L

R

T

Y

H

H

G

S

D

L

-

M

-

I

-

S

S

E

V

Q

D

P

K

L

V

P

A

D

D

C

G

L

F

E

K

I

V

T

V

S

A

R

R

S

S

T

G

D

N

D

-

G

-

Y

I

V

V

M

A

G

G

V

I

R

A

H

N

R

E

H

S

L

K

P

K

V

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

E

E

N

N

G

G

L

K

D

V

L

I

F

L

R

K

S

N

F

F

I

L

active site: G55 (= G52), C82 (= C80), Y83 (≠ L81), H165 (= H171), E167 (= E173)

Sites not aligning to the query:

active site: 223, 381
binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
24% identity, 96% coverage: 3:188/194 of query aligns to 2:181/475 of 2ywcA

query
sites
2ywcA

V

V

F

L

L

V

I

L

D

D

A

F

Y

G

D

S

S

Q

F

Y

V

T

F

R

I

L

I

I

S

A

Q

R

Y

R

L

L

E

R

Q

E

L

L

G

R

L

A

E

F

T

S

H

L

V

I

E

L

R

P

H

G

D

D

V

A

P

P

D

-

L

-

I

L

Q

E

R

E

I

V

E

L

A

K

F

H

S

R

P

P

D

Q

F

A

C

L

V

I

L

L

G

S

P

G

G
|
G

P

P

G
x
R

H

S

P

V

A

F

D

D

V

P

G

D

Y

A

I

P

E

R

V

P

-

D

I

P

R

R

H

L

F

F

Q

S

G

S

R

G

L

L

P

P

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

L

I

L

G

A

L

Q

A

E

F

L

G

G

A

G

Q

R

V

V

C

E

R

R

A

A

P

G

H

R

V

A

M

E

H

Y

G

G

K

K

V

A

S

L

T

L

I

T

E

R

N

H

D

E

G

G

-

P

-

L

-

F

K

R

G

G

V

L

Y

E

D

G

H

E

T

V

Q

Q

A

V

Q

W

A

M

I

-

R

-

A

-

T

-

R

-

Y

S

H

H

S

Q

L

D

M

A

I

V

S

T

E

A

Q

P

P

P

L

-

P

P

D

G

C

W

L

R

E

V

I

V

T

A

S

-

R

-

S

E

T

T

D

E

G

N

Y

P

V

V

M

A

G

A

V

I

R

A

H

S

R

P

H

D

L

G

P

R

V

A

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

E

P

N

K

G

G

L

M

D

Q

L

I

F

L

R

E

S

N

F

F

I

L

active site: G51 (= G54), R53 (≠ G56), C78 (= C80), Y79 (≠ L81), H164 (= H171), E166 (= E173)

Sites not aligning to the query:

active site: 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 430, 467, 471, 472, 473

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
23% identity, 96% coverage: 2:188/194 of query aligns to 5:188/490 of 5tw7F

query
sites
5tw7F

K

K

V

I

F

L

L

I

I

L

D

D

A

F

Y

G

D

S

S

Q

F

V

V

T

F

R

I

L

I

I

S

A

Q

R

Y

R

L

V

E

R

Q

E

L

A

G

H

L

V

E

Y

T

C

H

E

V

L

E

H

R

S

H

F

D

D

V

M

P

P

D

-

L

-

I

L

Q

D

R

E

I

I

E

K

A

A

F

F

S

N

P

P

D

K

F

G

C

I

V

I

L

L

G

S

P

G

G
|
G

P

P

G

N

H

S

P

V

A

Y

D

E

V

S

G

D

Y

Y

I

Q

E

A

V

D

I

T

R

G

H

I

F

F

Q

D

G

L

R

G

L

I

P

P

L

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

F

I

M

G

A

L

H

A

H

F

L

G

G

A

G

Q

E

V

V

C

Q

R

P

A

G

P

N

H

Q

V

R

M

E

H

F

G

G

-

Y

-

A

K

Q

V

V

S

K

T

T

I

I

E

D

N

S

D

G

-

L

G

T

K

R

G

G

V

I

Y

Q

D

D

H

D

T

A

Q

-

A

P

Q

N

A

T

I

L

R

D

A

V

T

W

R

M

Y

S

H

H

S

G

L

D

M

K

I

V

S

S

E

K

Q

-

P

-

L

L

P

P

D

D

C

G

L

F

E

A

I

V

T

I

S

G

R

D

S

T

T

P

D

S

D

C

G

P

Y

I

V

A

M

M

G

-

V

M

R

E

H

N

R

T

H

E

L

K

P

Q

V

F

E

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

E

K

N

Q

G

G

L

R

D

A

L

L

F

L

R

N

S

R

F

F

I

V

active site: G55 (= G54), C81 (= C80), Y82 (≠ L81), H171 (= H171), E173 (= E173)

Sites not aligning to the query:

active site: 229, 345
binding magnesium ion: 466, 469, 472

P20054 Protein PYR1-3; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
30% identity, 73% coverage: 47:188/194 of query aligns to 238:379/2225 of P20054

query
sites
P20054

D

D

F

G

C

V

V

F

L

I

G

S

P

N

G

G

P

P

G

G

H

D

P

P

A

S

D

L

V

C

G

G

-

K

Y

A

I

I

E

E

V

N

I

I

R

R

H

K

F

V

Q

L

G

A

R

-

L

L

P

P

L

V

-

A

-

K

-

A

-

V

L

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

A

L

I

L

G

G

L

L

A

A

F

A

G

G

A

A

Q

Q

V

T

C

-

R

-

A

-

P

-

H

H

V

K

M

M

H

-

G

-

K

-

V

-

S

-

T

A

I

F

E

G

N

N

D

R

G

G

-

L

-

N

K

Q

G

P

V

C

Y

V

D

D

H

Q

T

I

Q

S

A

G

Q

R

A

C

I

H

R

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

M

V

I

I

S

D

E

S

Q

N

P

S

L

L

P

P

-

A

-

G

D

S

C

G

L

W

E

K

I

T

T

Y

S

F

R

I

S

N

T

A

D

N

D

D

G

A

Y

S

V

N

M

E

G

G

V

I

R

Y

H

H

R

E

H

S

L

K

P

P

V

W

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

L

A

T

G

E

P

N

T

G

D

L

T

D

E

-

Y

L

L

F

F

R

D

S

N

F

F

I

V

Sites not aligning to the query:

1 modified: N-acetylmethionine

6w2jB Cps1 bound to allosteric inhibitor h3b-374 (see paper)
27% identity, 74% coverage: 47:189/194 of query aligns to 215:357/1364 of 6w2jB

query
sites
6w2jB

D

D

F

G

C

I

V

L

L

I

G

A

P

G

G

G

P

P

G

G

H

N

P

P

A

A

D

L

-

A

-

E

-

P

-

L

V

I

G

Q

Y

N

I

V

E

R

V

K

I

I

R

L

H

E

F

S

Q

D

G

R

R

K

L

E

P

P

L

L

L

F

G

G

V

I

C

S

L

T

G

G

H

N

Q

L

A

I

I

T

G

G

L

L

A

A

F

A

G

G

A

A

Q

K

V

T

C

Y

R

K

A

M

P

S

H

M

V

A

M
x
N

H

R

G

G

K

Q

V

-

S

-

T

-

I

-

E

-

N

-

D

-

G

N

K

Q

G

P

V

V

Y

L

D

N

H

I

T

T

Q

N

A

K

Q

Q

A

A

I

F

R

I

A

T

T

A

R
x
Q

Y

N

H
|
H

S

G

L

Y

M

A

I

L

S

-

E

D

Q

N

P

T

L

L

P

P

D

A

C

G

L

W

E

K

I

P

T

L

S

F

R

V

S

N

T

V

D

N

D

D

G

Q

Y

T

V

N

M
x
E

G

G

V

I

R

M

H

H

R

E

H

S

L

K

P

P

V

F

E

F

G

A

V

V

Q

Q

F

F

H

H

P

P

E

E

-

V

-

T

-

P

-

G

S

P

I

I

L

D

T

T

E

E

N

Y

G

L

L

F

D

D

L

S

F

F

R

F

S

S

F

L

I

I

R

K

binding zinc ion: N273 (≠ M101), Q293 (≠ R128), H295 (= H130), E320 (≠ M156)

Sites not aligning to the query:

active site: 593, 607, 609, 615, 811, 937, 1055, 1191
binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 547, 549, 557, 666, 667, 668, 669, 671, 672, 673, 674, 698, 702, 705, 706, 737, 739, 740

6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
27% identity, 74% coverage: 47:189/194 of query aligns to 215:357/1422 of 6w2jA

query
sites
6w2jA

D

D

F

G

C

I

V

L

L

I

G

A

P

G

G

G

P

P

G

G

H

N

P

P

A

A

D

L

-

A

-

E

-

P

-

L

V

I

G

Q

Y

N

I

V

E

R

V

K

I

I

R

L

H

E

F

S

Q

D

G

R

R

K

L

E

P

P

L

L

L

F

G

G

V

I

C

S

L

T

G

G

H

N

Q

L

A

I

I

T

G

G

L

L

A

A

F

A

G

G

A

A

Q

K

V

T

C

Y

R

K

A

M

P

S

H

M

V

A

M
x
N

H

R

G

G

K

Q

V

-

S

-

T

-

I

-

E

-

N

-

D

-

G

N

K

Q

G

P

V

V

Y

L

D

N

H

I

T

T

Q

N

A

K

Q

Q

A

A

I

F

R

I

A

T

T

A

R
x
Q

Y

N

H
|
H

S

G

L

Y

M

A

I

L

S

-

E

D

Q

N

P

T

L

L

P

P

D

A

C

G

L

W

E

K

I

P

T

L

S

F

R

V

S

N

T

V

D

N

D

D

G

Q

Y

T

V

N

M
x
E

G

G

V

I

R

M

H

H

R

E

H

S

L

K

P

P

V

F

E

F

G

A

V

V

Q

Q

F

F

H

H

P

P

E

E

-

V

-

T

-

P

-

G

S

P

I

I

L

D

T

T

E

E

N

Y

G

L

L

F

D

D

L

S

F

F

R

F

S

S

F

L

I

I

R

K

binding zinc ion: N273 (≠ M101), Q293 (≠ R128), H295 (= H130), E320 (≠ M156)

Sites not aligning to the query:

active site: 651, 665, 667, 673, 869, 995, 1113, 1249
binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 605, 607, 615, 724, 725, 726, 727, 729, 730, 731, 732, 756, 760, 763, 764, 794, 795, 797, 798

Query Sequence

>Pf6N2E2_1718 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1718
VKVFLIDAYDSFVFIISQYLEQLGLETHVERHDVPDLIQRIEAFSPDFCVLGPGPGHPAD
VGYIEVIRHFQGRLPLLGVCLGHQAIGLAFGAQVCRAPHVMHGKVSTIENDGKGVYDHTQ
AQAIRATRYHSLMISEQPLPDCLEITSRSTDDGYVMGVRHRHLPVEGVQFHPESILTENG
LDLFRSFIRCHVHK

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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