SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_100845372.1 NCBI__GCF_003031005.1:WP_100845372.1 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 4 hits to proteins with known functional sites (download)

P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
25% identity, 82% coverage: 33:482/552 of query aligns to 3:462/502 of P07117

query
sites
P07117

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R257 (= R286) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ T314) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
C344 (≠ G376) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
C349 (≠ G381) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
R376 (≠ K409) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.

B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
21% identity, 52% coverage: 44:330/552 of query aligns to 17:304/496 of B4EZY7

query
sites
B4EZY7

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A56 (≠ G83) binding Na(+)
T58 (≠ Y85) mutation to A: 2-fold increase in Neu5Ac transport.
L59 (≠ M86) binding Na(+)
S60 (= S87) mutation to A: Abolishes Neu5Ac transport.
T63 (≠ S90) mutation to A: Abolishes Neu5Ac transport.
Q82 (≠ S109) mutation to D: Abolishes Neu5Ac transport.
R135 (≠ S156) mutation to E: Abolishes Neu5Ac transport.
D182 (≠ Q210) binding Na(+); mutation to A: Abolishes Neu5Ac transport.

Sites not aligning to the query:

339 binding Na(+)
342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
343 binding Na(+); S→A: Abolishes Neu5Ac transport.
345 binding Na(+); S→A: Reduces Neu5Ac transport.
346 binding Na(+); S→A: Slightly increases Neu5Ac transport.

5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 53% coverage: 44:334/552 of query aligns to 13:304/480 of 5nv9A

query
sites
5nv9A

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A

binding sodium ion: A52 (≠ G83), T53 (≠ D84), L55 (≠ M86), S56 (= S87), V174 (≠ T206), D178 (≠ Q210)
binding N-acetyl-beta-neuraminic acid: T54 (≠ Y85), S56 (= S87), I58 (≠ A89), T59 (≠ S90), G77 (≠ Y108), Q78 (≠ S109), R131 (≠ S156), F239 (≠ L269)

Sites not aligning to the query:

binding sodium ion: 335, 338, 338, 339, 341, 342

Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 33% coverage: 39:220/552 of query aligns to 22:201/643 of Q92911

query
sites
Q92911

L

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T

S

F

T

A

Y

D

E

V

Y

A

L

S

E

Y

M

R

R

L

F

G

S

Q

-

T

-

Q

-

I

-

R

R

T

A

L

V

S

R

A

L

C

C

G

G

S

T

L

L

V

Q

V

-

V

-

A

-

F

-

Y

Y

L

I

I

V

A

A

Q

T

M

M

V

L

G

Y

A

T

G

G

K

I

L

V

I

I

-

Y

-

A

-

P

-

A

-

L

-

I

-

L

Q

N

L

Q

L

V

F

T

G

G

L

L

D

D

Y

I

H

W

V

A

A

S

V

L

I

L

L

S

V

T

G

G

V

I

L

I

M

C

C

T

M

F

Y

Y

V

T

L

A

F

V

G

G

G

G

M

M

L

K

A

A

T

V

T

V

W

W

V

T

Q

D

I

V

I

F

K

Q

A

V

V

V

L

V

L

M

L

L

S

S

G

G

A102 (≠ L120) natural variant: A -> P

Sites not aligning to the query:

226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
536 T → Q: requires 2 nucleotide substitutions
556 S → Q: requires 2 nucleotide substitutions

Query Sequence

>WP_100845372.1 NCBI__GCF_003031005.1:WP_100845372.1
MIRRLLSLLTVAAFAPCAFAADALTGAVAKQPLNIPAILMFVAFVGATLYITYWASKKNN
SAADYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPIIL
FLIAERLRNLGKYTFADVASYRLGQTQIRTLSACGSLVVVAFYLIAQMVGAGKLIQLLFG
LDYHVAVILVGVLMCMYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVNFDFNMLF
SEAIKVHPKGEAIMSPGGLVKDPVSAFSLGLALMFGTAGLPHILMRFFTVSDAKEARKSV
LYATGFIGYFYILTFIIGFGAILLVSTNPAFKDAAGALLGGNNMAAVHLANAVGGSIFLG
FISAVAFATILAVVAGLTLAGASAVSHDLYASVIKKGKANEKDEIRVSKITTIALAVLAI
GLGILFESQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMIGGWLGLVSAVGLMV
LGPTIWVQILHHEKAIFPYEYPALFSMIIAFVGIWFFSITDKSAAADNERALFFPQFVRS
QTGLGVSGAVSH

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