SitesBLAST
Comparing CCNA_01039 FitnessBrowser__Caulo:CCNA_01039 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
26% identity, 95% coverage: 14:429/438 of query aligns to 4:425/430 of P0AA76
- Y29 (= Y41) binding
- D31 (≠ T43) mutation to N: Loss of galactonate transport activity.
- R32 (= R44) binding
- Y64 (≠ G75) binding
- E118 (= E129) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ I362) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
25% identity, 92% coverage: 26:429/438 of query aligns to 3:406/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
25% identity, 92% coverage: 26:429/438 of query aligns to 6:390/393 of 6e9oA
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)
29% identity, 60% coverage: 120:382/438 of query aligns to 166:440/495 of Q5Q0U0
- R168 (= R122) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L125) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G126) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E129) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (= G130) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ Q133) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P134) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ M137) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V140) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ AGQEA 221:225) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P288) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G324) 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.
- 136 K→E: 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)
29% identity, 60% coverage: 120:382/438 of query aligns to 166:440/495 of Q8BN82
- H183 (≠ M137) 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.
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, 72% coverage: 67:382/438 of query aligns to 110:440/495 of Q9NRA2
- K136 (vs. gap) 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 (≠ M137) 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 (≠ AG 152:153) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IA 219:220) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ AGQEA 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 (≠ A282) 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 (= P288) 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 (= G324) 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
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, 64% coverage: 121:402/438 of query aligns to 183:470/582 of Q9JI12
- R184 (= R122) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E129) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ A255) 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.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 63% coverage: 126:402/438 of query aligns to 130:412/452 of 7t3nA
Sites not aligning to the query:
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
26% identity, 70% coverage: 15:320/438 of query aligns to 3:349/493 of Q03567
- N69 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9C0U9 Uncharacterized transporter PB1C11.03 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 37% coverage: 54:216/438 of query aligns to 128:296/570 of Q9C0U9
Sites not aligning to the query:
- 14 modified: Phosphoserine
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
23% identity, 64% coverage: 55:335/438 of query aligns to 93:384/497 of Q9Y2C5
- A372 (≠ L323) 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.
Query Sequence
>CCNA_01039 FitnessBrowser__Caulo:CCNA_01039
MAVAVPERAPEGSPGGAAMPKLKALRWWIIGLVTLGAVINYLTRSTMGVAAPTLLKELGI
SVTEYSWITSAFQLGIMLQPICGYVLDTLGLRTGFAVFAVAWSLIAMAHGLANSWQGFAV
LRGFLGLAEGSAQPAGMKTVAIWFPAKERGFAGGVFNIGASIGSVLAPPLVVWAVLVWNW
RAAFVLTGVMGLVWVVLWLAFYRSPEKHPSMTDEERAVIAAGQEAHLEAVAARPSILSIL
KQGQFWGIALPRFLADPTWGTLAFWVPLYLSQTRGFDLKQIALFAWMPFVAADLGCMAGP
VIALFLQKRGVTLINARRIAFTLGAVLMTGMMFVGKVESAYAAIALLCLGGFAHQTLSVT
VITMASDLFRRNEVATVAGLAGMMGNLGLLLFSLLIGGLVAKVGYDPFFIALGVLDILGA
ILLWTLVKDPAARAKAAA
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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