SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012469464.1 NCBI__GCF_000020385.1:WP_012469464.1 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 2 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)
24% identity, 56% coverage: 166:538/661 of query aligns to 104:442/502 of P07117

query
sites
P07117

N

N

A

N

G

N

K

A

Y

L

T

T

L

L

G

P

D

D

I

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C

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R257 (= R346) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ I367) 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 (≠ G438) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
C349 (≠ A443) 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 (= R471) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.

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)
22% identity, 30% coverage: 97:294/661 of query aligns to 42:236/643 of Q92911

query
sites
Q92911

K

R

S

S

A

A

A

E

D

D

F

F

Y

F

T

T

A

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G

G

G

R

G

R

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G

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Y

Y

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G

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K

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F

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L
x
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N

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x
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P

A102 (≠ L157) natural variant: A -> P
H226 (≠ Q284) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.

Sites not aligning to the query:

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_012469464.1 NCBI__GCF_000020385.1:WP_012469464.1
MKRLLVAIGCVLSLSFAAYAEPAKAPAAPEAKPAVAAPAATVALAADAAKVAAPAPAKPA
EEKKASLKANPKVTIPIFLAIIGATMAVVVWSAKQTKSAADFYTAGGGITGTQNGWAIAG
DYMSAASFLGISGMISLYGYDGFMYSVGWLVAYITVLLIVAEPCRNAGKYTLGDILSFRT
SPKPVRAVAAISTVSVSTFYLTAQMVGAGKLMQLLLGVPYKTAIIGVGILMVGYVVFGGM
TATTWVQIIKAGLLMTGAALLSILVSIKSGFSPLQFFTDIATNQNIIDHVKLLPIYLKES
AAGTATADAGQRFLEPGLFLTNPLDQISLGMALVLGTAGMPHILMRFFTVPTAQAARKSV
IVAMFIIGSFYILTTLLGFGAAIHLSPQGIKQVDAGGNMAAMMLAKQMGGEFSPFLGDLL
LAFLCAVAFATILAVVSGLVLAASAAIAHDIYVNVIKDGHADQKEQVFAARATSFIVGAC
GIVIGIAAEKQNVAHLVALAFAVASSGNLPVVVMSLFWKKFNTAGVIAGLVVGTIASVGL
VMVSPNMTYPEVVAKNAKAAYTKLEKEIADGKVKPEAMEKTLKTIEAKKAEEAKNLGGKS
MLGLSKPLFTLKNPGILSIPLGFIAAILATLMFPCKKAEEMWDEIYVRQNTGIGMAKAID
H

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