SitesBLAST
Comparing AO356_26160 FitnessBrowser__pseudo5_N2C3_1:AO356_26160 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
25% identity, 92% coverage: 17:412/431 of query aligns to 18:417/430 of P0AA76
- Y29 (≠ F28) binding D-galactonate
- D31 (= D30) mutation to N: Loss of galactonate transport activity.
- R32 (= R31) binding D-galactonate
- Y64 (= Y63) binding D-galactonate
- E118 (= E117) mutation to Q: Loss of galactonate transport activity.
- W358 (= W352) binding D-galactonate
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
25% identity, 92% coverage: 17:412/431 of query aligns to 10:382/393 of 6e9oA
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
25% identity, 92% coverage: 17:412/431 of query aligns to 7:398/409 of 6e9nA
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 48% coverage: 8:216/431 of query aligns to 84:291/534 of P53322
- K283 (≠ L208) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
23% identity, 76% coverage: 57:385/431 of query aligns to 113:443/495 of Q5Q0U0
- K136 (≠ R80) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R110) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L113) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G114) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E117) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A118) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F121) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P122) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I125) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L128) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSL--KN 268:272 (≠ ELLDAED 216:222) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P285) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (vs. gap) 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.
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, 76% coverage: 57:385/431 of query aligns to 113:443/495 of Q8BN82
- H183 (≠ I125) 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.
8u3gA Structure of naag-bound sialin (see paper)
21% identity, 76% coverage: 57:385/431 of query aligns to 52:382/427 of 8u3gA
Sites not aligning to the query:
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, 76% coverage: 57:385/431 of query aligns to 113:443/495 of Q9NRA2
- K136 (≠ R80) 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 (≠ I125) 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 (≠ AM 140:141) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ VQ 214:215) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ELLDA 216:220) 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 (= G275) 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 (≠ V281) 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 (vs. gap) 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
8u3hA Structure of fmoc-leu-oh bound sialin (see paper)
21% identity, 76% coverage: 57:385/431 of query aligns to 50:380/425 of 8u3hA
Sites not aligning to the query:
Q9C0U9 Uncharacterized transporter PB1C11.03 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
20% identity, 68% coverage: 10:300/431 of query aligns to 92:393/570 of Q9C0U9
Sites not aligning to the query:
- 14 modified: Phosphoserine
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
25% identity, 53% coverage: 59:287/431 of query aligns to 90:318/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
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, 76% coverage: 57:385/431 of query aligns to 129:463/582 of Q9JI12
- R184 (= R110) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E117) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ Q238) 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.
- 128 H→A: Greatly lowers L-glutamate transport.
Query Sequence
>AO356_26160 FitnessBrowser__pseudo5_N2C3_1:AO356_26160
MKTLPVSVLAKISWRLLPFLLLMYIMAFLDRANVGFAKQAFQADTGIGDAAFAFGAGVFF
AGYALLEVPSNLILHRVGARLWMCRIMVTWGLVSAAMVFAHNETSFYVLRFLLGVAEAGF
FPGVILYLTYWFPSAARGKAMGFFYFGAPLAFIFGSPLSGLLLELDGFVGVHGWQWLFAV
EGLMASAVGVWAYWYLDNRPADAKWLTLEERRQVQELLDAEDQHKQSHGRSLLSVLCQPS
VLYLCLIYLLIQASVYGVVFYLPSQVAGLLGSKVGLLVGLVTAIPWVCALCAAYLIPGYS
DRTGQRRRTATLTLLMAAAGIACSVSVSSPLLGIIALCFAASGFIAVQPVFWTFPSSYLA
GSAAAAGIALINSFGALGGFIAPVLKNWAEGAFHSPAAGLYLLAATTVIAALLVLGIHSP
GQRASNTPATV
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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