SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing H281DRAFT_03338 H281DRAFT_03338 MFS transporter, MHS family, citrate/tricarballylate:H+ symporter 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 8 hits to proteins with known functional sites (download)

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
25% identity, 73% coverage: 78:392/432 of query aligns to 63:398/446 of A0A0H2VG78

query
sites
A0A0H2VG78

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R102 (= R125) mutation to A: Loss of transport activity.
I105 (≠ Q128) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E145) mutation to A: Loss of transport activity.
Q137 (≠ S160) mutation to A: Loss of transport activity.
Q250 (vs. gap) mutation to A: Loss of transport activity.
Q251 (≠ Y256) mutation to A: Loss of transport activity.
N256 (≠ Y261) mutation to A: Loss of transport activity.
W357 (vs. gap) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
28% identity, 28% coverage: 72:191/432 of query aligns to 203:306/727 of Q9Z2I6

query
sites
Q9Z2I6

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Sites not aligning to the query:

1:57 Interaction with SYT1
529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.

4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
22% identity, 58% coverage: 122:373/432 of query aligns to 126:407/475 of 4gc0A

query
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4gc0A

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binding 6-bromo-6-deoxy-beta-D-glucopyranose: Q164 (= Q164), Q284 (≠ M250), N290 (≠ Y256), L293 (≠ T259), W388 (≠ V354)

4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
22% identity, 58% coverage: 122:373/432 of query aligns to 126:407/475 of 4gbzA

query
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4gbzA

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binding beta-D-glucopyranose: Q164 (= Q164), Q284 (≠ M250), N290 (≠ Y256), W388 (≠ V354)

4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
22% identity, 58% coverage: 122:373/432 of query aligns to 126:407/475 of 4gbyA

query
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4gbyA

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V

T

L

V

Y

Y

Y

A

A

P

P

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E

F

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F

K

K

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T

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-

L

L

H

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A

D

D

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A

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L

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N

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D

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A

binding beta-D-xylopyranose: Q164 (= Q164), Q284 (≠ M250), N290 (≠ Y256), W388 (≠ V354)

P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
22% identity, 58% coverage: 122:373/432 of query aligns to 130:411/491 of P0AGF4

query
sites
P0AGF4

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V

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E

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R

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Q

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E

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x
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x
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x
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Y

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-

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N

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G

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A

R133 (= R125) mutation R->C,H,L: Abolishes xylose transport.
E153 (= E145) mutation to A: Abolishes xylose transport.
R160 (≠ K152) mutation to A: Abolishes xylose transport.
Q168 (= Q164) binding ; mutation to A: Abolishes xylose transport.
Q288 (≠ M250) mutation to A: Abolishes xylose transport.
QQ 288:289 (≠ MT 250:251) binding
Q289 (≠ T251) mutation to A: Strongly decreases xylose transport.
N294 (≠ Y256) binding ; mutation to A: Abolishes xylose transport.
Y298 (≠ V260) mutation to A: Abolishes xylose transport.
N325 (= N288) mutation to A: No effect on xylose transport.
G340 (= G303) mutation to A: Abolishes xylose transport.
R341 (= R304) mutation R->A,W: Abolishes xylose transport.
W392 (≠ V354) binding ; mutation to A: Abolishes xylose transport.
E397 (= E359) mutation to A: Abolishes xylose transport.
R404 (= R366) mutation to A: Strongly decreases xylose transport.

Sites not aligning to the query:

24 F→A: Decreases xylose transport.
83 G→A: Abolishes xylose transport.
415 binding
416 W→A: Strongly decreases xylose transport.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
28% identity, 28% coverage: 72:191/432 of query aligns to 203:306/727 of Q496J9

query
sites
Q496J9

L

V

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G

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A

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S

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G

W

W

Sites not aligning to the query:

519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
563 F→A: No longer interacts with BoNT/A HC.
565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.

Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
29% identity, 28% coverage: 72:191/432 of query aligns to 217:320/742 of Q02563

query
sites
Q02563

L

V

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G

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A

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A

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-

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W

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I

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A

A

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W

Sites not aligning to the query:

196:200 mutation Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E).
321:331 mutation Missing: No change in uptake of BoNT/D or BoNT/E.
498 N→Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D.
548 N→Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D.
570:573 RLVN→TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E.
573 N→Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D.

Query Sequence

>H281DRAFT_03338 H281DRAFT_03338 MFS transporter, MHS family, citrate/tricarballylate:H+ symporter
MHPSPSTLSSGRSKAAAVFRVTAGNFLEQFDFFLFGFYATQIAKVFFPADSEFASLMMTF
AVFGAGFLMRPLGAIVLGAYIDDVGRRKGLIVTLSIMASGTILIAFVPGYATLGLLAPAL
VLIGRLLQGFSAGAELGGVSVYLAEMATPGRKGFFTSWQSASQQVAIVVAAALGFALNQS
MSAATIASWGWRVPFFVGCMIVPFIFMLRRNLQETEEFKARQHRPSMKEVFRTLVQNWTV
VIAGMMLVAMTTASFYLITVYAPTFGKTVLHLSTADSLLVTLCVAVSNFVWLPIGGALSD
KLGRRPLLVAMTVLAIATAYPALSLLAHAPSFLNMLLALLWLSFMYGIYNGAMVVALTEV
MPAQVRVAGFSLAYSLATAVFGGFTPAISTALIHMTGDKAAPGYWMSFAAACALMATFAL
YRRRATTLTPAH

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