SitesBLAST

R182 (= R15) to W: in MMDS1; patient's skin fibroblasts show deficiency of lipoic acid synthase and reduced lipoic acid content; dbSNP:rs1354126704
P183 (= P16) to R: in SPG93; likely pathogenic
G189 (= G22) to R: in MMDS1 and SPG93; pathogenic; alters protein structure; increases likelihood of existing as monomer; decreases ability to receive a Fe/S clusters from donor proteins; decreases delivery rates of [2Fe-2S] cluster to target proteins; dbSNP:rs2104735490; mutation to A: Alters protein structure. Increases likelihood of existing as monomer. Decreases ability to receive a Fe/S clusters from donor proteins. Decreases delivery rates of [2Fe-2S] cluster to target proteins.; mutation to K: Alters protein structure. Increases likelihood of existing as monomer. Decreases ability to receive a Fe/S clusters from donor proteins. Decreases delivery rates of [2Fe-2S] cluster to target proteins.
G190 (= G23) to R: in MMDS1; uncertain significance
G208 (= G42) to C: in MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes; increases homodimerization; unable to receive a Fe/S clusters from donor proteins; changes delivery rates of [2Fe-2S] cluster to target proteins; dbSNP:rs374514431
C210 (= C44) to F: in MMDS1 and SPG93; likely pathogenic

Sites not aligning to the query:

21 R → P: in MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes; dbSNP:rs776875884
25 M → K: in dbSNP:rs4453725
88 F → S: in SPG93; uncertain significance
99 L → V: in SPG93; uncertain significance
100 A → P: in SPG93; uncertain significance
101 R → G: in SPG93; uncertain significance
121 V → A: in SPG93; likely pathogenic
133 L → P: in SPG93; uncertain significance
241 V → L: in SPG93; uncertain significance

P63020 Fe/S biogenesis protein NfuA from Escherichia coli (strain K12) (see paper)
39% identity, 86% coverage: 3:72/81 of query aligns to 107:177/191 of P63020

query
sites
P63020

L

L

T

M

E

E

Q

R

V

V

E

E

Q

Y

A

M

L

L

E

Q

T

S

-

Q

I

I

R

N

P

P

Y

Q

L

L

K

A

A

G

D

H

G

G

D

R

V

V

S

S

V

L

E

M

E

E

I

I

T

T

S

E

E

D

G

G

T

Y

V

A

K

I

L

L

K

Q

L

F

L

G

G

G

N

G

C
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C

G

N

S

G

C
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C

P

S

M

M

S

V

F

D

M

V

T

T

M

L

K

K

S

E

G

G

I

I

E

E

Q

K

A

Q

I

L

M

L

K

N

A

E

V

F

P

P

Q

E

I

L

T

K

S

G

V

V

C149 (= C44) mutation to S: Loss of activity in vivo. Still able to bind a Fe/S cluster in vitro.
C152 (= C47) mutation to S: Loss of activity in vivo. Still able to bind a Fe/S cluster in vitro.

Sites not aligning to the query:

39 C→S: No effect on activity in vivo. Still able to bind a Fe/S cluster in vitro.
44 C→S: No effect on activity in vivo.

P32860 NifU-like protein, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 98% coverage: 3:81/81 of query aligns to 153:233/256 of P32860

query
sites
P32860

L

V

T

S

E

E

Q

L

V

I

E

E

Q

E

A

L

L

I

E

D

T

T

-

R

I

I

R

R

P

P

Y

A

L

I

K

L

A

E

D

D

G

G

D

D

V

I

S

D

V

Y

E

R

E

G

I

W

T

D

S

P

E

K

-

T

G

G

T

T

V

V

K

Y

L

L

K

R

L

L

L

Q

G
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G

N

A

C
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C

G
x
T

S
|
S

C
|
C

P

S

M

S

S

S

F

E

M

V

T

T

M

L

K

K

S

Y

G

G

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S

A

M

I

L

M

K

K

H

A

Y

V

V

P

D

Q

E

I

V

T

K

S

E

V

V

V

I

A

Q

V

I

N

M

M

D

A

P

E

E

Q

Q

E

E

G194 (= G42) mutation to C: Dominant negative mutant; cells show a severe synthetic sick phenotype on glycerol/lactate medium.
CTSC 196:199 (≠ CGSC 44:47) mutation to ATSA: Loss of function. Abolished homodimerization.

P05340 Nitrogen fixation protein NifU from Azotobacter vinelandii (see paper)
33% identity, 94% coverage: 5:80/81 of query aligns to 234:307/312 of P05340

query
sites
P05340

E

R

Q

R

V

I

E

E

Q

T

A

V

L

L

E

A

T

A

I

I

R

R

P

P

Y

T

L

L

K

Q

A

R

D

D

G

K

G

G

D

D

V

V

S

E

V

L

E

I

E

D

I

V

T

D

S

G

E

K

G

-

T

N

V

V

K

Y

L

V

K

K

L

L

L

T

G

G

N

A

C

C

G

T

S

G

C

C

P

Q

M

M

S

A

F

S

M

M

T

T

M

L

K

-

S

G

G

G

I

I

E

Q

Q

Q

A

R

I

L

M

I

K

E

A

E

V

L

P

G

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E

I

F

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S

K

V

V

V

I

A

P

V

V

N

S

M

A

A

A

E

A

Q

H

Sites not aligning to the query:

35 C→A: Slow diazotrophic growth, normal [2Fe-2S] EPR signal.
37 D→A: Increases stability of iron-bound protein.
62 C→A: Slow diazotrophic growth, normal [2Fe-2S] EPR signal.
106 C→A: Slow diazotrophic growth, normal [2Fe-2S] EPR signal.
137 binding [2Fe-2S] cluster; C→A: Slow diazotrophic growth, loss of [2Fe-2S] EPR signal.
139 binding [2Fe-2S] cluster; C→A: Slow diazotrophic growth, loss of [2Fe-2S] EPR signal.
172 binding [2Fe-2S] cluster; C→A: Slow diazotrophic growth, loss of [2Fe-2S] EPR signal.
175 binding [2Fe-2S] cluster; C→A: Slow diazotrophic growth, loss of [2Fe-2S] EPR signal.

Query Sequence

>CA265_RS20885
MNLTEQVEQALETIRPYLKADGGDVSVEEITSEGTVKLKLLGNCGSCPMSFMTMKSGIEQ
AIMKAVPQITSVVAVNMAEQE

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