SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_024772127.1 NCBI__GCF_000520995.1:WP_024772127.1 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 3 hits to proteins with known functional sites (download)

Q6LX42 Sodium/alanine symporter AgcS; Alanine permease; Alanine/glycine:cation symporter from Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL) (see paper)
38% identity, 90% coverage: 47:508/515 of query aligns to 19:444/453 of Q6LX42

query
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Q6LX42

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T75 (= T127) binding D-alanine; binding L-alanine
G79 (= G131) binding L-alanine
N80 (= N132) binding D-alanine; mutation to A: Markedly reduces L-alanine uptake; when associated with A-274 and A-308.
I165 (≠ G220) mutation to A: Shows poor substrate selectivity, allowing additional amino acids such as L-valine and L-leucine to be efficiently transported. Decreases L-alanine uptake.
Q170 (= Q225) binding D-alanine; binding L-alanine
F273 (= F334) mutation to A: Shows poor substrate selectivity, allowing additional amino acids such as L-valine and L-leucine to be efficiently transported. Decreases L-alanine uptake.
FS 273:274 (= FS 334:335) binding D-alanine
FSNE 273:276 (= FSNE 334:337) binding L-alanine
S274 (= S335) mutation to A: Markedly reduces L-alanine uptake; when associated with A-80 and A-308.
D308 (= D369) mutation to A: Markedly reduces L-alanine uptake; when associated with A-80 and A-274.
W370 (= W432) mutation to Q: Does not change uptake of L-alanine, but reduces the ability to transport D-alanine.

6csfM Crystal structure of sodium/alanine symporter agcs with d-alanine bound (see paper)
38% identity, 89% coverage: 47:502/515 of query aligns to 5:418/431 of 6csfM

query
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6csfM

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binding d-alanine: T58 (= T127), G60 (= G129), G62 (= G131), N63 (= N132), Q150 (= Q225), F253 (= F334), S254 (= S335)
binding sodium ion: T58 (= T127), I59 (≠ V128), N63 (= N132), S254 (= S335), D288 (= D369)

6cseM Crystal structure of sodium/alanine symporter agcs with l-alanine bound (see paper)
38% identity, 89% coverage: 47:502/515 of query aligns to 5:418/431 of 6cseM

query
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6cseM

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A

V

A

K

K

T

T

R

D

F

H

P

P

A

G

S

R

E

Q

G

A

L

L

V

V

A

S

L

M

L

T

E

G

P

T

F

F

I

L

D
|
D

T

T

V

I

V

V

V

V

C

C

T

T

M

I

T

T

A

G

L

L

V

V

L

L

I

T

I

I

T

A

G

G

Q

L

V

K

D

A

T

F

S

P

T

G

E

L

I

T

D

D

F

L

E

-

Q

T

G

G

V

A

L

S

L

L

T

T

A

A

S

A

A

S

L

F

E

D

S

A

G

L

V

M

S

P

W

M

F

G

P

G

Y

L

L

I

L

V

T

T

I

I

A

G

V

L

L

V

L

F

F

F

A

A

F

Y

S

S

S

T

M

V

I

L

S

G

W

W

S

S

Y

Y

Y

Y

G

G

Y

E

Q

K

A

C

W

F

S

E

Y

Y

L

L

F

I

G

G

R

-

S

-

K

T

R

K

T

G

E

I

Y

R

L

L

Y

Y

K

R

F

I

I

A

F

F

C

V

C

L

F

V

T

A

V

F

I

W

G

G

A

A

A

T

A

A

T

S

L

L

N

P

A

L

V

V

T

W

D

N

F

I

S

A

D

D

A

T

M

L

I

N

F

G

A

A

M

M

M

A

V

I

P

P

N

N

M

L

I

I

G

G

L

L

F

L

L

L

L

L

S

S

P

G

K

V

V

V

K

V

D

S

E

E

binding alanine: A57 (= A126), T58 (= T127), G60 (= G129), N63 (= N132), Q150 (= Q225), F253 (= F334), S254 (= S335), E256 (= E337)
binding sodium ion: T58 (= T127), I59 (≠ V128), N63 (= N132), S254 (= S335), D288 (= D369)

Query Sequence

>WP_024772127.1 NCBI__GCF_000520995.1:WP_024772127.1
MLFPCIISEQNLDENINRVFGDATSWFVDAILAEIPITETVGVPWVVVVLILGAGYFTLY
FKFINVRSFYTAIQVVRGKYDAVENLDHDGSSDLSSESALVKEKNTDDDVNGEVSHFQAL
TTAVSATVGLGNIAGVAIALSIGGAGATLWMIIIGVLGMSSKFVECTLGVKYREVDSDGK
VFGGPMYYLTKGLGEKGYAKLGKVLSVLFAIMCIGGSFGGGNMFQVNQAFKLFDHVIISD
NSMLHGQGWVFGVIMAILVGVVIIGGIKKIASVTDKIVPFMVLIYIVAVLIVLVLYSSAI
PAAFRAIWEGAFHPEGVMGGFVGVLVQGFRRGAFSNEAGVGSASIAHSAVKTRFPASEGL
VALLEPFIDTVVVCTMTALVLIITGQVDTSTEIDFEQGVLLTASALESGVSWFPYLLTIA
VLLFAFSSMISWSYYGYQAWSYLFGRSKRTEYLYKFIFCCFTVIGAAATLNAVTDFSDAM
IFAMMVPNMIGLFLLSPKVKDELIRYKKSIAGRMK

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