SitesBLAST
Comparing AO356_20660 FitnessBrowser__pseudo5_N2C3_1:AO356_20660 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
43% identity, 96% coverage: 14:438/443 of query aligns to 2:429/430 of P0AA76
- Y29 (= Y41) binding
- D31 (= D43) mutation to N: Loss of galactonate transport activity.
- R32 (= R44) binding
- Y64 (= Y76) binding
- E118 (= E130) mutation to Q: Loss of galactonate transport activity.
- W358 (= W366) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
44% identity, 93% coverage: 24:437/443 of query aligns to 1:409/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
42% identity, 94% coverage: 22:437/443 of query aligns to 2:393/393 of 6e9oA
Q9JI12 Vesicular glutamate transporter 2; VGluT2; Differentiation-associated BNPI; Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter; Solute carrier family 17 member 6 from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 78% coverage: 61:406/443 of query aligns to 120:470/582 of Q9JI12
- H128 (≠ F69) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R123) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E130) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ S260) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
Sites not aligning to the query:
- 88 R→A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
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)
27% identity, 85% coverage: 56:430/443 of query aligns to 99:476/495 of Q9NRA2
- K136 (≠ R93) 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 (≠ S138) 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 (≠ AS 153:154) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IE 220:221) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ AGGGL 222:226) 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 (= G287) 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 (= P293) 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
- G371 (= G329) to V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
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
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 78% coverage: 61:406/443 of query aligns to 62:412/452 of 7t3nA
Sites not aligning to the query:
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)
29% identity, 80% coverage: 47:399/443 of query aligns to 90:443/495 of Q8BN82
- H183 (≠ S138) 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.
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
27% identity, 83% coverage: 66:434/443 of query aligns to 111:482/497 of Q9Y2C5
- A372 (≠ V327) to T: in dbSNP:rs11754288
Sites not aligning to the query:
- 66 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
- 75 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-66 and A-90.
- 90 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
Q5Q0U0 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 (Anion/sugar transporter), member 5; Vesicular excitatory amino acid transporter; VEAT from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 78% coverage: 56:399/443 of query aligns to 99:443/495 of Q5Q0U0
- K136 (≠ R93) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R123) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ V126) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G127) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E130) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A131) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F134) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P135) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ S138) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V141) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ AGGGL 222:226) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P293) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G329) mutation to V: Remains in the endoplasmic reticulum.
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R→C: Markedly decreases H(+)-coupled sialic acid transporter activity.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
23% identity, 93% coverage: 18:430/443 of query aligns to 8:459/493 of Q03567
- N69 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
27% identity, 46% coverage: 15:218/443 of query aligns to 100:305/605 of Q9GQQ0
- E217 (= E130) mutation to K: In bnch(N); leads to storage in yolk spheres during oogenesis and results in widespread accumulation of enlarged lysosomal and late endosomal inclusions.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
22% identity, 64% coverage: 25:309/443 of query aligns to 19:314/452 of Q5EXK5
- D82 (= D88) mutation to A: Loss of activity.
- V311 (≠ I306) mutation to W: Loss of activity.
- D314 (= D309) mutation to A: Loss of activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
22% identity, 37% coverage: 3:166/443 of query aligns to 2:167/448 of Q51955
- D41 (≠ N40) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D43) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G84) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D88) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G91) 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 (= R123) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ V143) mutation to A: Strong decrease in 4-HBA transport.
Sites not aligning to the query:
- 183 H→A: Decrease in 4-HBA transport and chemotaxis.
- 323 D→N: Abolishes 4-HBA transport and chemotaxis.
- 328 H→A: Decrease in 4-HBA transport and chemotaxis.; H→R: Decrease in 4-HBA transport and loss of chemotaxis.
- 386 R→A: Strong decrease in 4-HBA transport.
- 398 R→A: Abolishes 4-HBA transport.
- 444 H→A: No change in 4-HBA transport and chemotaxis.
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
19% identity, 76% coverage: 2:336/443 of query aligns to 50:395/534 of P53322
- K283 (= K214) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
24% identity, 86% coverage: 60:439/443 of query aligns to 47:398/403 of P77589
- D75 (= D88) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ I306) mutation to H: 30% increase in 3HPP transport activity.
- K276 (≠ L310) mutation to D: Lack of 3HPP transport activity.
Sites not aligning to the query:
- 27 E→A: Lack of 3HPP transport activity.; E→D: Slight decrease in 3HPP transport activity.
Q8IVW8 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2 from Homo sapiens (Human) (see 2 papers)
23% identity, 79% coverage: 24:372/443 of query aligns to 99:446/549 of Q8IVW8
- R200 (= R123) mutation to S: Loss of function; does not rescue the cardia bifida phenotype in the morpholino knockdown in zebrafish.
- S319 (≠ C254) natural variant: Missing (in DFNB115; uncertain significance; dbSNP:rs749994718)
Query Sequence
>AO356_20660 FitnessBrowser__pseudo5_N2C3_1:AO356_20660
MSNSHTSQIASARDAVVPERLPSRRRWFMLSLLLIATIINYIDRVNISIAAPFLAKDLGL
DKIEMGLIFSAFAWTYAIALVPAGFIADRFGSRFTYGVSLISWSTVTVCQGFATGFASLF
GLRLAVGAMEAPAFPANSRAVTVWFPARERGLASSIYVCGQYLGTALFTGALLWLATTYD
WRHVFYSTGALGIVFGVAWLFLYRDPMNCKKVSKEELKYIEAGGGLVKSSQERTRFNWRQ
IAELFSYRQVWAICIGKFASTSALYFFLTWFPTYLIEERQLTMIKAGIFAVLPFVGATVG
ILLAGIVSDLLIRRGYSLSFARKLPLVVGSMLGMSIVLVNFTDSNVICIAVLTIAFFAQG
IASSSWAAVSEVAPKELIGLTGGITSLAANIGGIVTPIVIGAIVHKTGSFALAFWFIGGV
ALIGTLSYSLLLGRLYRIELKAR
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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