SitesBLAST

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.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
31% identity, 25% coverage: 73:178/432 of query aligns to 203:300/727 of Q496J9

query
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Q496J9

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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.

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
23% identity, 73% coverage: 79:393/432 of query aligns to 63:398/446 of A0A0H2VG78

query
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A0A0H2VG78

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R102 (= R126) mutation to A: Loss of transport activity.
I105 (≠ Q129) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E146) mutation to A: Loss of transport activity.
Q137 (= Q165) mutation to A: Loss of transport activity.
Q250 (vs. gap) mutation to A: Loss of transport activity.
Q251 (vs. gap) mutation to A: Loss of transport activity.
N256 (≠ T252) 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.

A1Z8N1 Facilitated trehalose transporter Tret1-1; DmTret1-1 from Drosophila melanogaster (Fruit fly) (see paper)
26% identity, 77% coverage: 82:413/432 of query aligns to 461:811/857 of A1Z8N1

query
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A1Z8N1

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Sites not aligning to the query:

248 modified: Phosphoserine
249 modified: Phosphoserine
250 modified: Phosphoserine
320 modified: Phosphoserine
322 modified: Phosphoserine
845 modified: Phosphoserine
846 modified: Phosphoserine

Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 25% coverage: 73:178/432 of query aligns to 217:314/742 of Q02563

query
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Q02563

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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

>AO353_25075 FitnessBrowser__pseudo3_N2E3:AO353_25075
MMKTTTQDTRSKGSKLGAILRVTSGNFLEQFDFFLFGFYATYISQTFFPTTSEFASLMMT
FAVFGSGFLMRPLGAIVLGAYIDKVGRRKGLIVTLSIMAAGTVLIALVPGYASIGIAAPI
LVLLGRLLQGFSAGAEMGGVSVYLAEIATPGRRGFYTSWQSASQQVAIILAAALGYTINA
SMEAADVAAWGWRIPFFIGCLIIPFIFIIRRSLQETDAFKARSHHPSASEVFRSMRDNWR
TVLAGGLLASMTTTTFYLITVYTPTFGRSVLNLSTSDSLVVTLFVGLSNFIWLPIGGTIS
DRIGRRPLLLAVTLLCIFTAYPAMHWLAAAASFERLLAVLLYFSFFFGIYNGAMVAALTE
VMPQNVRVVGFSLAFSLATAVFGGFTPAVSTILVQATGDKASPAYWLMFAALCGFTATTI
LYRRQKAVPVNV

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