SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 209090 MicrobesOnline__882:209090 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 19 hits to proteins with known functional sites (download)

2nv4A Crystal structure of upf0066 protein af0241 in complex with s-adenosylmethionine. Northeast structural genomics consortium target gr27 (see paper)
41% identity, 39% coverage: 4:131/332 of query aligns to 2:122/133 of 2nv4A

query
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2nv4A

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binding s-adenosylmethionine: Q16 (≠ L18), A19 (≠ C21), P20 (= P22), R21 (≠ K23), Q22 (≠ N24), Y55 (≠ T57), M57 (≠ L59), D58 (≠ H60), K59 (≠ L61), R82 (= R86), G91 (= G95), L92 (= L96), D111 (≠ E120), L113 (= L122)

O29998 S-adenosyl-L-methionine-binding protein AF_0241 from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) (see paper)
41% identity, 39% coverage: 4:131/332 of query aligns to 2:122/139 of O29998

query
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O29998

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Q16 (≠ L18) binding
PRQ 20:22 (≠ PKN 22:24) binding
DK 58:59 (≠ HL 60:61) binding
R82 (= R86) binding
L92 (= L96) binding
LDGS 113:116 (≠ LHGT 122:125) binding

Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
28% identity, 52% coverage: 156:329/332 of query aligns to 8:174/181 of Q58813

query
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Q58813

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N25 (= N173) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
30% identity, 54% coverage: 149:328/332 of query aligns to 5:183/207 of 6btgA

query
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6btgA

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active site: E76 (= E218), H95 (= H237), H97 (= H239), Y116 (≠ M265), H157 (= H302)
binding manganese (ii) ion: E76 (= E218), H95 (= H237), H97 (= H239), H157 (= H302)

P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
30% identity, 54% coverage: 149:328/332 of query aligns to 5:183/213 of P0DTQ0

query
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P0DTQ0

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E76 (= E218) binding
H95 (= H237) binding
H97 (= H239) binding
H157 (= H302) binding

7x78A L-fuculose 1-phosphate aldolase (see paper)
31% identity, 54% coverage: 155:332/332 of query aligns to 8:182/203 of 7x78A

query
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7x78A

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binding magnesium ion: E70 (= E218), H89 (= H237), H91 (= H239), H152 (= H302)
binding sulfate ion: R8 (= R155), N26 (= N173), T40 (= T187), H61 (≠ R209), Q63 (≠ A211), S68 (= S216), S69 (= S217)

Sites not aligning to the query:

binding sulfate ion: 5

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
31% identity, 53% coverage: 158:332/332 of query aligns to 14:185/210 of 2fuaA

query
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2fuaA

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Q

K

A

A

L

L

A

W

L

L

G

A

E

H

E

E

L

V

E

E

H

V

L

L

A

A

G

Q

I

L

H

Y

L

L

S

T

V

T

L

L

active site: E73 (= E218), H92 (= H237), H94 (= H239), Y113 (≠ I258), A117 (≠ E262), H155 (= H302)
binding cobalt (ii) ion: E73 (= E218), H92 (= H237), H94 (= H239), H155 (= H302)

Sites not aligning to the query:

active site: 209

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
31% identity, 53% coverage: 158:332/332 of query aligns to 14:185/206 of 4fuaA

query
sites
4fuaA

C

C

H

L

T

E

A

M

W

T

Q

R

R

L

G

G

L

L

L

N

S

Q

G

G

F

T

N

A

G
|
G

N
|
N

V

V

S

S

L

V

R

R

L

Y

G

Q

A

D

T

G

C

M

L

L

V

I

T

T

C

P

T
|
T

G

G

A

I

A

P

K

Y

G

E

D

K

L

L

S

T

P

E

G

S

D

H

L

I

A

V

V

F

V

I

D

D

I

-

A

G

S

N

G

G

K

K

R

H

I

E

A

E

G

G

G

K

K

L

P

P

S
|
S

E
|
E

L

W

A

R

M

F

H

H

L

M

E

A

V

A

Y

Y

R

Q

R

S

Q

R

P

P

R

D

A

A

Q

N

A

A

I

V

V

V

H
|
H

T

N

H
|
H

P

A

P

V

R

H

L

C

L

T

A

A

L

V

G

S

L

I

R

L

V

N

A

R

P

S

Q

I

Q

P

M

A

L

I

H

H

I
x
Y

D

M

V

I

Y

A

E
x
A

A

A

Q

G

M

G

L

-

V

-

S

N

R

S

L

I

G

P

S

C

A

A

P

P

A

Y

H

A

A

T

P

F

G

G

T

T

Q

R

A

E

L

L

A

S

D

E

A

H

V

V

G

A

E

L

A

A

A

L

V

K

T

N

R

R

E

K

A

A

V

T

W

L

M

L

E

Q

R

H

H
|
H

G

G

L

L

V

I

C

A

W

C

G

E

E

V

T

N

P

L

M

E

Q

K

A

A

L

L

A

W

L

L

G

A

E

H

E

E

L

V

E

E

H

V

L

L

A

A

G

Q

I

L

H

Y

L

L

S

T

V

T

L

L

active site: E73 (= E218), H92 (= H237), H94 (= H239), Y113 (≠ I258), A117 (≠ E262), H155 (= H302)
binding phosphoglycolohydroxamic acid: G28 (= G172), N29 (= N173), T43 (= T187), S71 (= S216), S72 (= S217), E73 (= E218), H92 (= H237), H94 (= H239), H155 (= H302)
binding zinc ion: H92 (= H237), H94 (= H239), H155 (= H302)

P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 53% coverage: 158:332/332 of query aligns to 14:185/215 of P0AB87

query
sites
P0AB87

C

C

H

L

T

E

A

M

W

T

Q

R

R

L

G

G

L

L

L

N

S

Q

G

G

F
x
T

N
x
A

G
|
G

N
|
N

V

V

S

S

L

V

R

R

L

Y

G

Q

A

D

T

G

C

M

L

L

V

I

T

T

C

P

T
|
T

G
|
G

A

I

A

P

K

Y

G

E

D

K

L

L

S

T

P

E

G

S

D

H

L

I

A

V

V

F

V

I

D

D

I

-

A

G

S

N

G

G

K

K

R

H

I

E

A

E

G

G

G

K

K

L

P

P

S
|
S

E
|
E

L

W

A

R

M

F

H

H

L

M

E

A

V

A

Y

Y

R

Q

R

S

Q

R

P

P

R

D

A

A

Q

N

A

A

I

V

V

V

H
|
H

T

N

H
|
H

P

A

P

V

R

H

L

C

L

T

A

A

L

V

G

S

L

I

R

L

V

N

A

R

P

S

Q

I

Q

P

M

A

L

I

H

H

I
x
Y

D

M

V

I

Y

A

E

A

A

A

Q

G

M

G

L

-

V

-

S

N

R

S

L

I

G

P

S

C

A

A

P

P

A

Y

H

A

A

T

P
x
F

G

G

T

T

Q

R

A

E

L

L

A

S

D

E

A

H

V

V

G

A

E

L

A

A

A

L

V

K

T

N

R

R

E

K

A

A

V

T

W

L

M

L

E

Q

R

H

H
|
H

G

G

L

L

V

I

C

A

W

C

G

E

E

V

T

N

P

L

M

E

Q

K

A

A

L

L

A

W

L

L

G

A

E

H

E

E

L

V

E

E

H

V

L

L

A

A

G

Q

I

L

H

Y

L

L

S

T

V

T

L

L

T26 (≠ F170) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ N171) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 172:173) binding
N29 (= N173) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
TG 43:44 (= TG 187:188) binding
S71 (= S216) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 216:217) binding
E73 (= E218) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
H92 (= H237) binding
H94 (= H239) binding
Y113 (≠ I258) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
F131 (≠ P278) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
H155 (= H302) binding

Sites not aligning to the query:

206 F→W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
32% identity, 51% coverage: 165:332/332 of query aligns to 21:185/209 of 1dzuP

query
sites
1dzuP

G

G

L

L

L

N

S

Q

G

G

F

A

N

A

G

G

N

N

V

V

S

S

L

V

R

R

L

Y

G

Q

A

D

T

G

C

M

L

L

V

I

T

T

C

P

T

T

G

G

A

I

A

P

K

Y

G

E

D

K

L

L

S

T

P

E

G

S

D

H

L

I

A

V

V

F

V

I

D

D

I

-

A

G

S

N

G

G

K

K

R

H

I

E

A

E

G

G

G

K

K

L

P

P

S

S

E
|
E

L

W

A

R

M

F

H

H

L

M

E

A

V

A

Y

Y

R

Q

R

S

Q

R

P

P

R

D

A

A

Q

N

A

A

I

V

V

V

H
|
H

T

N

H
|
H

P

A

P

V

R

H

L

C

L

T

A

A

L

V

G

S

L

I

R

L

V

N

A

R

P

S

Q

I

Q

P

M

A

L

I

H

H

I

Y

D

M

V

I

Y

A

E

A

A

A

Q

G

M

G

L

-

V

-

S

N

R

S

L

I

G

P

S

C

A

A

P

P

A

Y

H

A

A

T

P

F

G

G

T

T

Q

R

A

E

L

L

A

S

D

E

A

H

V

V

G

A

E

L

A

A

A

L

V

K

T

N

R

R

E

K

A

A

V

T

W

L

M

L

E

Q

R

H

H
|
H

G

G

L

L

V

I

C

A

W

C

G

E

E

V

T

N

P

L

M

E

Q

K

A

A

L

L

A

W

L

L

G

A

E

H

E

E

L

V

E

E

H

V

L

L

A

A

G

Q

I

L

H

Y

L

L

S

T

V

T

L

L

binding zinc ion: E73 (= E218), H92 (= H237), H94 (= H239), H155 (= H302)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
34% identity, 49% coverage: 162:325/332 of query aligns to 19:184/207 of 6voqA

query
sites
6voqA

W

F

Q

S

R

R

G

G

L

Y

L

A

S

T

G

G

F

S

N

A

G

G

N

N

V

L

S

S

L

L

R

L

L

L

-

P

G

D

A

G

T

N

C

L

L

L

V

A

T

T

C

P

T

T

G

G

A

A

A

C

K

L

G

G

D

E

L

L

S

Q

P

A

G

Q

D

R

L

L

A

S

V

V

D

T

I

L

A

-

S

Q

G

G

K

E

R

W

I

I

A

S

G

G

G

D

K

K

P

P

S

S

S

K

E
|
E

L

V

A

T

M

F

H

H

L

R

E

A

V

V

Y

Y

R

L

R

H

Q

N

P

P

R

A

A

C

Q

K

A

A

I

I

V

V

H
|
H

T

L

H
|
H

P

S

P

H

R

Y

L

L

L

T

A

A

L

L

G

S

L

C

R

L

-

Q

-

G

V

L

A

D

P

P

Q

H

Q

N

M

C

L

I

H

R

I

P

D

F

V

T

Y

P

E
x
Y

A

V

Q

V

M

M

L

R

V

V

S

G

R

D

L

V

G

P

S

V

A

V

P

P

A

Y

H

Y

A

R

P

P

G

G

T

D

Q

D

A

R

L

I

A

A

D

Q

A

A

V

L

G

A

E

G

A

L

A

A

V

P

T

R

R

Y

E

N

A

A

V

F

W

L

M

L

E

A

R

N

H
|
H

G

G

L

P

V

V

C

V

W

T

G

G

E

S

T

S

P

L

M

R

Q

E

A

A

L

T

A

N

L

N

G

T

E

E

L

L

E

E

H

E

L

T

A

A

active site: E75 (= E218), H94 (= H237), H96 (= H239), Y121 (≠ E262), H161 (= H302)
binding zinc ion: E75 (= E218), H94 (= H237), H96 (= H239), H161 (= H302)

Q6NDF6 S-adenosyl-L-methionine-binding protein RPA0152 from Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
34% identity, 39% coverage: 8:136/332 of query aligns to 27:148/167 of Q6NDF6

query
sites
Q6NDF6

I

I

G

G

T

R

V

I

R

H

S

T

R

P

L

W

T

N

R

R

L

L

D

K

D

E

C

C

P
|
P

K
x
R

N
x
H

G

G

D

R

E

A

G

D

A

G

P

P

E

V

A

C

W

R

I

I

D

E

I

V

L

F

P

E

E

T

F

W

A

L

A

P

G

A

L

L

D

A

T

G

L

I

E

D

A

D

G

G

Q

T

E

L

L

L

T

E

L

V

V

F

T

Y

W

W

L

L

H
|
H

L
x
R

A

S

D

R

R

R

D

D

T

L

L

L

A

L

V

Q

H

C

P

P

R

R

G

N

D

D

T

G

S

D

R

-

P

-

M

A

R

R

G

G

V

T

F

F

N

S

T

I

R
|
R

S

S

P

P

A

L

R

R

P

P

N

N

P

P

L

I

G

G

L
x
T

H

S

D

I

V

A

R

R

L

V

L

D

G

R

T

R

A

-

P

-

G

-

P

-

D

D

G

G

M

-

V

A

R

N

L

L

L

F

V

I

A

R

P

G

L

L

E
x
D

A
x
C

L
|
L

H
x
D

G
|
G

T
|
T

P

P

V

L

V

V

D

D

I

L

K

K

T

P

S

D

L

R

S

A

Q

E

PRH 41:43 (≠ PKN 22:24) binding
HR 79:80 (≠ HL 60:61) binding
R103 (= R86) binding
T113 (≠ L96) binding
DCLDGT 132:137 (≠ EALHGT 120:125) binding

3okxA Crystal structure of yaeb-like protein from rhodopseudomonas palustris
34% identity, 39% coverage: 8:136/332 of query aligns to 22:140/156 of 3okxA

query
sites
3okxA

I

I

G

G

T

R

V

I

R

H

S

T

R

P

L

W

T

N

R

R

L
|
L

D

K

D

E

C
|
C

P
|
P

K
x
R

N
x
H

G

G

D

R

E

A

G

D

A

G

P

P

E

V

A

C

W

R

I

I

D

E

I

V

L

F

P

E

E

T

F

W

A

L

A

P

G

A

L

L

D

A

T

G

L

I

E

D

A

D

G

G

Q

T

E

L

L

L

T

E

L

V

V

F

T
x
Y

W

W

L
|
L

H
|
H

L
x
R

A
x
S

D

R

R

R

D

D

T

L

L

L

A

L

V

Q

H

C

P

P

R

-

G

G

D

D

T

A

S

-

R

-

P

-

M

-

R

R

G

G

V

T

F

F

N

S

T

I

R
|
R

S

S

P
|
P

A

L

R

R

P

P

N

N

P

P

L

I

G

G

L
x
T

H

S

D

I

V

A

R

R

L

V

L

D

G

R

T

R

A

-

P

-

G

-

P

-

D

D

G

G

M

-

V

A

R

N

L

L

L

F

V

I

A

R

P

G

L

L

E
x
D

A
x
C

L
|
L

H

D

G

G

T

T

P

P

V

L

V

V

D

D

I

L

K

K

T

P

S

D

L

R

S

A

Q

E

binding s-adenosylmethionine: L32 (= L18), C35 (= C21), P36 (= P22), R37 (≠ K23), H38 (≠ N24), Y71 (≠ T57), L73 (= L59), H74 (= H60), R75 (≠ L61), S76 (≠ A62), R95 (= R86), P97 (= P88), T105 (≠ L96), D124 (≠ E120), C125 (≠ A121), L126 (= L122)

4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
26% identity, 54% coverage: 154:331/332 of query aligns to 10:206/224 of 4m6rA

query
sites
4m6rA

V

I

R

P

R

E

L

L

C

C

H

K

T

Q

A

F

W

Y

Q

H

R

L

G

G

L

W

L

V

S

T

G

G

F

T

N

G

G

G

N

G

V

I

S

S

L

L

R

K

L

H

G

G

A

D

T

E

C

I

L

Y

V

I

T

A

C

P

T

S

G

G

A

V

A

Q

K

K

G

E

D

R

L

I

S

Q

P

P

G

E

D

D

L

M

A

F

V

V

V

C

D

D

I

I

A

-

S

N

G

E

K

K

R

D

I

I

A

S

G

G

G

P

K

S

P

P

S

S

S

K

E

K

L

L

A

K

-

K

-

S

-

Q

-

C

-

T

-

P

M

L

H

F

L

M

E

N

V

A

Y

Y

R

T

R

M

Q

R

P

-

R

G

A

A

Q

G

A

A

I

V

V

I

H
|
H

T

T

H
|
H

P

S

P

K

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binding zinc ion: H97 (= H237), H99 (= H239), H177 (= H302)

Q96GX9 Methylthioribulose-1-phosphate dehydratase; MTRu-1-P dehydratase; APAF1-interacting protein; hAPIP; EC 4.2.1.109 from Homo sapiens (Human) (see 5 papers)
26% identity, 53% coverage: 156:331/332 of query aligns to 30:224/242 of Q96GX9

query
sites
Q96GX9

R

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C76 (≠ V202) to Y: in dbSNP:rs1977420
S84 (≠ A211) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.
S87 (≠ K214) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.
S89 (= S216) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.
Q96 (vs. gap) mutation to A: Mildly reduced enzyme activity.
C97 (vs. gap) mutation to A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
H115 (= H237) mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.; mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.
H117 (= H239) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.
E139 (≠ Q254) active site, Proton donor/acceptor; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
M181 (≠ V287) to V: in dbSNP:rs17850327
H195 (= H302) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.

Sites not aligning to the query:

7 R → W: in dbSNP:rs2956114
23 H → R: in dbSNP:rs17850326

4c25A L-fuculose 1-phosphate aldolase (see paper)
27% identity, 52% coverage: 155:328/332 of query aligns to 18:186/212 of 4c25A

query
sites
4c25A

R

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active site: E79 (= E218), H98 (= H237), H100 (= H239), Y119 (= Y261), H160 (= H302)
binding zinc ion: G30 (= G169), H98 (= H237), H100 (= H239), H160 (= H302)

7bu1A Crystal structure of trmo from pseudomonas aeruginosa
29% identity, 48% coverage: 7:164/332 of query aligns to 7:152/205 of 7bu1A

query
sites
7bu1A

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binding s-adenosylmethionine: K18 (≠ L18), I21 (≠ C21), F62 (≠ A62), H63 (≠ D63), R73 (= R86), T75 (≠ P88), Q83 (≠ L96), S84 (≠ H97), D102 (≠ E120), L103 (≠ A121), L104 (= L122), T107 (= T125)

7btzA Crystal structure of trmo
30% identity, 48% coverage: 7:164/332 of query aligns to 10:161/212 of 7btzA

query
sites
7btzA

P

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binding s-adenosyl-l-homocysteine: I24 (≠ C21), F65 (≠ L59), H66 (= H60), Q67 (≠ L61), R79 (= R86), T81 (≠ P88), Q89 (≠ L96), S90 (≠ H97), D108 (≠ E120), L109 (≠ A121), L110 (= L122), T113 (= T125)

P28634 tRNA (adenine(37)-N6)-methyltransferase; tRNA (m6t6A37) methyltransferase; tRNA methyltransferase O; EC 2.1.1.- from Escherichia coli (strain K12) (see paper)
46% identity, 16% coverage: 81:134/332 of query aligns to 87:139/235 of P28634

query
sites
P28634

G

G

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V

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L

R92 (= R86) mutation to A: Inhibits tRNA m(6)t(6)A37 formation.
K136 (= K131) mutation to A: Inhibits tRNA m(6)t(6)A37 formation.

Sites not aligning to the query:

194 D→A: Inhibits tRNA m(6)t(6)A37 formation; when associated with A-196.
196 R→A: Inhibits tRNA m(6)t(6)A37 formation; when associated with A-194.

Query Sequence

>209090 MicrobesOnline__882:209090
MQPVLRPIGTVRSRLTRLDDCPKNGDEGAPEAWIDILPEFAAGLDTLEAGQELTLVTWLH
LADRDTLAVHPRGDTSRPMRGVFNTRSPARPNPLGLHDVRLLGTAPGPDGMVRLLVAPLE
ALHGTPVVDIKTSLSQRRDTGWGDGVPLREAETVRRLCHTAWQRGLLSGFNGNVSLRLGA
TCLVTCTGAAKGDLSPGDLAVVDIASGKRIAGGKPSSELAMHLEVYRRQPRAQAIVHTHP
PRLLALGLRVAPQQMLHIDVYEAQMLVSRLGSAPAHAPGTQALADAVGEAAVTREAVWME
RHGLVCWGETPMQALALGEELEHLAGIHLSVL

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