SitesBLAST
Comparing Pf6N2E2_739 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_739 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
54% identity, 92% coverage: 10:385/407 of query aligns to 15:387/403 of P77589
- E27 (= E22) mutation to A: Lack of 3HPP transport activity.; mutation to D: Slight decrease in 3HPP transport activity.
- D75 (= D70) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ L270) mutation to H: 30% increase in 3HPP transport activity.
- K276 (≠ R274) mutation to D: Lack of 3HPP transport activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
35% identity, 95% coverage: 2:389/407 of query aligns to 20:437/448 of Q51955
- D41 (≠ E22) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D25) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G66) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D70) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G73) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
- R124 (= R105) mutation to A: Abolishes 4-HBA transport.
- E144 (= E125) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q162) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D273) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ I278) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (= R335) mutation to A: Strong decrease in 4-HBA transport.
- R398 (= R347) mutation to A: Abolishes 4-HBA transport.
Sites not aligning to the query:
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
33% identity, 98% coverage: 7:405/407 of query aligns to 19:448/452 of Q5EXK5
- D82 (= D70) mutation to A: Loss of activity.
- V311 (≠ L270) mutation to W: Loss of activity.
- D314 (= D273) mutation to A: Loss of activity.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
29% identity, 84% coverage: 20:362/407 of query aligns to 52:401/444 of Q8NLB7
- D54 (≠ E22) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (= D25) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R71) mutation to A: Loss of transport activity.
- W309 (≠ L270) mutation to V: Loss of transport activity.
- D312 (= D273) mutation to A: Loss of transport activity.
- R313 (= R274) mutation to A: Loss of transport activity.
- I317 (= I278) mutation I->H,Y: Loss of transport activity.
- R386 (= R347) mutation to A: Loss of transport activity.
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
31% identity, 30% coverage: 48:168/407 of query aligns to 191:311/727 of Q9Z2I6
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.
Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
31% identity, 30% coverage: 48:168/407 of query aligns to 191:311/727 of Q496J9
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.
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
23% identity, 67% coverage: 3:273/407 of query aligns to 9:301/430 of P0AA76
- Y29 (≠ G23) binding
- D31 (= D25) mutation to N: Loss of galactonate transport activity.
- R32 (≠ L26) binding
- Y64 (≠ L58) binding
- E118 (≠ L112) mutation to Q: Loss of galactonate transport activity.
Sites not aligning to the query:
Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 28% coverage: 56:168/407 of query aligns to 213:325/742 of Q02563
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.
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
23% identity, 66% coverage: 6:273/407 of query aligns to 1:282/409 of 6e9nA
Sites not aligning to the query:
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
24% identity, 60% coverage: 3:246/407 of query aligns to 1:274/393 of 6e9oA
Sites not aligning to the query:
Q9U539 Organic cation transporter 1; CeOCT1 from Caenorhabditis elegans (see paper)
26% identity, 42% coverage: 17:186/407 of query aligns to 122:291/585 of Q9U539
Sites not aligning to the query:
- 87 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 98 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9NRA2 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Membrane glycoprotein HP59; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Homo sapiens (Human) (see 8 papers)
22% identity, 58% coverage: 38:274/407 of query aligns to 99:351/495 of Q9NRA2
- K136 (= K75) to E: in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity; dbSNP:rs80338795
- H183 (≠ I120) to R: in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity; dbSNP:rs119491109
- LL 198:199 (≠ AI 135:136) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ TT 202:203) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ QALFG 204:208) natural variant: Missing (in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity)
- G328 (= G251) to E: in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs386833996
- P334 (≠ F257) to R: in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs119491110
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane.; LL→GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R → C: in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity; dbSNP:rs80338794
- 371 G → V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
Q8BN82 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Mus musculus (Mouse) (see paper)
23% identity, 58% coverage: 38:273/407 of query aligns to 99:350/495 of Q8BN82
- H183 (≠ I120) mutation to R: Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.
Sites not aligning to the query:
- 39 R→C: Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.
A2SWM2 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2; Protein two of hearts from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
25% identity, 44% coverage: 25:203/407 of query aligns to 81:254/504 of A2SWM2
- R153 (= R105) mutation to S: In ko157; displays cardia bifida (2 hearts).
Q8VC69 Solute carrier family 22 member 6; Kidney-specific transport protein; Novel kidney transcript; mNKT; Organic anion transporter 1; mOAT1; Renal organic anion transporter 1; mROAT1 from Mus musculus (Mouse) (see 2 papers)
32% identity, 27% coverage: 55:162/407 of query aligns to 136:242/545 of Q8VC69
- C183 (≠ L102) mutation to A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
Sites not aligning to the query:
- 39 N→Q: Complete loss of PAH transport activity.
- 49 C→A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
- 56 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 86 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 91 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 107 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 122 C→A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
- 434 C→A: Decreased cell surface expression level and PAH transport activity. 80% decrease of PAH transport activity; when associated with A-49; A-122 and A-183. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402 and A-427.
8bw7A Cryo-em structure of rat slc22a6 bound to alpha-ketoglutaric acid (see paper)
26% identity, 34% coverage: 26:162/407 of query aligns to 69:230/497 of 8bw7A
Sites not aligning to the query:
8bvsA Cryo-em structure of rat slc22a6 bound to tenofovir (see paper)
26% identity, 34% coverage: 26:162/407 of query aligns to 69:230/502 of 8bvsA
Sites not aligning to the query:
8bvtA Cryo-em structure of rat slc22a6 bound to probenecid (see paper)
32% identity, 27% coverage: 55:162/407 of query aligns to 133:239/508 of 8bvtA
Sites not aligning to the query:
Q497L9 Solute carrier family 22 member 14 from Mus musculus (Mouse) (see paper)
31% identity, 28% coverage: 57:170/407 of query aligns to 192:304/629 of Q497L9
- H275 (vs. gap) mutation to A: Strongly reduced riboflavin transport; when associated with 391-A--A-394.
Sites not aligning to the query:
- 391:394 SYIS→AYIA: Strongly reduced riboflavin transport; when associated with A-275.
8g92A Structure of inhibitor 16d-bound spns2 (see paper)
24% identity, 38% coverage: 35:188/407 of query aligns to 30:195/415 of 8g92A
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_739 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_739
MNRPAHRATLTIALCFIVALIEGFDLQSAGTAAAGLRQTFALDPKMMGWVFSAGIIGLLP
GAFFGGWIADRIGRKKILIAAVLLFGVFSLSTAYVEHFSSLLLVRFMTGLGLGAALPNLI
ALCAEAVGEQRRGTAISVMYAGVPLGGALAAVVAMLFGEHWQMTFFIGGLAPLLVVPLML
LWLPESSAFRQAQDGGTARGSTTQALFGEGRGRTTLALWLSYFFTLTVMYMLLNWLPSLL
LEQGFSKPQAGLVQMLFNIGGALGSLLGGLLLDRCNGIKVVLFVYAGLLSALAGVGFSVG
IVPMAIAGFAAGLFVMAAQLVLYALAPPSYPTSVRATGVGAAVAIGRLGSVAGPLAAGQI
LAAGGGTTAVLLATSPGLVVATLAVLSVIRYSTGPRLGASEPVAGNS
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