SitesBLAST

Comparing PfGW456L13_2130 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2130 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 15 hits to proteins with known functional sites

P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
56% identity, 96% coverage: 15:434/436 of query aligns to 10:429/430 of P0AA76

• Y29 (= Y34) binding
• D31 (= D36) mutation to N: Loss of galactonate transport activity.
• R32 (= R37) binding
• Y64 (= Y69) binding
• E118 (= E123) mutation to Q: Loss of galactonate transport activity.
• W358 (= W363) binding

6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
57% identity, 96% coverage: 17:433/436 of query aligns to 1:409/409 of 6e9nA

• binding D-gluconic acid: Q57 (= Q73), F111 (≠ Y127), N359 (= N383)

6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
55% identity, 96% coverage: 15:433/436 of query aligns to 2:393/393 of 6e9oA

• binding D-galactonic acid: Y21 (= Y34), R24 (= R37), Y56 (= Y69), F114 (≠ Y127), Q141 (= Q154), Q228 (= Q254), A232 (≠ N258), S320 (= S360), N343 (= N383)

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, 89% coverage: 18:405/436 of query aligns to 69:472/582 of Q9JI12

• R88 (= R37) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
• H128 (≠ F62) mutation to A: Greatly lowers L-glutamate transport.
• R184 (= R116) mutation R->A,E,K: Greatly lowers L-glutamate transport.
• E191 (= E123) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
• R322 (≠ L257) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.

7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 89% coverage: 18:405/436 of query aligns to 11:414/452 of 7t3nA

• binding (1s,3r)-1-aminocyclopentane-1,3-dicarboxylic acid: F27 (≠ Y34), R30 (= R37), Y77 (= Y69), Y137 (= Y127), Y165 (≠ F155), R264 (≠ L257), S265 (≠ N258), F268 (≠ L261), Y269 (≠ W262), N392 (= N383)
• binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: R12 (= R19), Y13 (≠ F20), G20 (≠ F27), L21 (≠ I28), E152 (= E142), T159 (≠ F149), C162 (≠ S152), G163 (= G153), A166 (≠ V156), I170 (≠ F160), E219 (≠ A208), E220 (= E209), Y223 (≠ L212)

Sites not aligning to the query:

• binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: 10

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)
24% identity, 83% coverage: 59:420/436 of query aligns to 109:467/495 of Q8BN82

• H183 (≠ S131) 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.

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)
24% identity, 86% coverage: 59:433/436 of query aligns to 109:484/495 of Q5Q0U0

• K136 (≠ R86) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
• R168 (= R116) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
• E171 (≠ V119) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
• G172 (= G120) mutation to C: Decreases protein levels and alters subcellular localization.
• E175 (= E123) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
• G176 (≠ A124) mutation to C: Decreases protein levels and alters subcellular localization.
• F179 (≠ Y127) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
• P180 (= P128) mutation to C: Decreases protein levels and alters subcellular localization.
• H183 (≠ S131) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
• W186 (≠ V134) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
• SSLKN 268:272 (≠ DIQAE 221:225) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
• P334 (= P290) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
• G371 (= G326) 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, 67% coverage: 19:312/436 of query aligns to 15:338/493 of Q03567

• N69 (vs. gap) 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)
23% identity, 86% coverage: 59:433/436 of query aligns to 109:484/495 of Q9NRA2

• K136 (≠ R86) 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 (≠ S131) 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 146:147) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
• I------L 266:267 (≠ IREGGGLV 213:220) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
• SSLRN 268:272 (≠ DIQAE 221:225) 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 (= G284) 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 (= P290) 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 (= G326) 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

Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
23% identity, 81% coverage: 54:405/436 of query aligns to 106:455/497 of Q9Y2C5

• A372 (≠ I324) 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 tranport 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 tranport 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 tranport of thyroid hormones T3 and T4; when associated with A-75 and A-90.

Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
24% identity, 60% coverage: 16:275/436 of query aligns to 24:280/448 of Q51955

• D41 (≠ N33) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
• D44 (= D36) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
• G85 (= G77) mutation to V: Abolishes 4-HBA transport and chemotaxis.
• D89 (= D81) mutation to N: Abolishes 4-HBA transport and chemotaxis.
• G92 (≠ P84) 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 (= R116) mutation to A: Abolishes 4-HBA transport.
• E144 (≠ T136) mutation to A: Strong decrease in 4-HBA transport.
• H183 (= H175) mutation to A: Decrease in 4-HBA transport and chemotaxis.

Sites not aligning to the query:

• 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.

Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
22% identity, 82% coverage: 11:369/436 of query aligns to 99:449/605 of Q9GQQ0

• E217 (= E123) 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, 60% coverage: 18:280/436 of query aligns to 19:288/452 of Q5EXK5