SitesBLAST
Comparing RR42_RS30395 FitnessBrowser__Cup4G11:RR42_RS30395 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
31% identity, 92% coverage: 5:394/422 of query aligns to 12:415/430 of P0AA76
- Y29 (= Y22) binding
- D31 (= D24) mutation to N: Loss of galactonate transport activity.
- R32 (= R25) binding
- Y64 (= Y57) binding
- E118 (= E111) mutation to Q: Loss of galactonate transport activity.
- W358 (= W339) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
31% identity, 92% coverage: 5:394/422 of query aligns to 1:396/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
30% identity, 92% coverage: 5:394/422 of query aligns to 4:380/393 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, 97% coverage: 9:418/422 of query aligns to 83:513/582 of Q9JI12
- R88 (≠ L14) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ F50) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R104) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E111) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ Y231) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
27% identity, 91% coverage: 38:421/422 of query aligns to 75:483/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 94% coverage: 20:415/422 of query aligns to 35:452/452 of 7t3nA
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)
26% identity, 83% coverage: 36:386/422 of query aligns to 98:460/495 of Q9NRA2
- K136 (= K74) 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 (≠ T119) 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 (≠ AQ 134:135) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ -L 199) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ETLPA 200:204) 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 (≠ A258) 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 (≠ V264) 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 (≠ T304) 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
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)
25% identity, 83% coverage: 36:386/422 of query aligns to 98:460/495 of Q5Q0U0
- K136 (= K74) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R104) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L107) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G108) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E111) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (= G112) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F115) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P116) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ T119) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ M122) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ APRKK 204:208) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (≠ V264) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (≠ A295) 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, 83% coverage: 36:386/422 of query aligns to 98:460/495 of Q8BN82
- H183 (≠ T119) 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)
23% identity, 79% coverage: 47:378/422 of query aligns to 111:453/497 of Q9Y2C5
- A372 (= A298) 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.
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)
27% identity, 59% coverage: 39:289/422 of query aligns to 45:284/403 of P77589
- D75 (= D69) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ V277) mutation to H: 30% increase in 3HPP transport activity.
- K276 (= K281) 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.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
24% identity, 63% coverage: 18:281/422 of query aligns to 28:315/452 of Q5EXK5
- D82 (= D69) mutation to A: Loss of activity.
- V311 (= V277) mutation to W: Loss of activity.
- D314 (= D280) mutation to A: Loss of activity.
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
24% identity, 79% coverage: 13:345/422 of query aligns to 119:449/605 of Q9GQQ0
- E217 (= E111) 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.
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 47% coverage: 10:207/422 of query aligns to 95:294/534 of P53322
- K283 (≠ P196) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
A2SWM2 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2; Protein two of hearts from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
22% identity, 81% coverage: 3:345/422 of query aligns to 50:399/504 of A2SWM2
- R153 (= R104) mutation to S: In ko157; displays cardia bifida (2 hearts).
6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
23% identity, 89% coverage: 38:411/422 of query aligns to 35:396/404 of 6zguA
6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
23% identity, 89% coverage: 38:411/422 of query aligns to 35:396/404 of 6zgtA
6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
23% identity, 89% coverage: 38:411/422 of query aligns to 35:396/404 of 6zgsA
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 61% coverage: 13:270/422 of query aligns to 32:313/448 of Q51955
- D41 (= D24) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (≠ N27) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G65) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D69) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G72) 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 (= R104) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ R124) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ R163) 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.
6zguB Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
23% identity, 87% coverage: 38:405/422 of query aligns to 29:364/364 of 6zguB
Query Sequence
>RR42_RS30395 FitnessBrowser__Cup4G11:RR42_RS30395
MKRLRATSVVLGMLCIMYFITYLDRVNVSTAAAGFGQEFNLSKTEIGLVFSAFAYPYLVF
QIIGGWVSDRFGAKRTLMVCGVLWAAATLLTGFAGGLVSLLAARLLLGLGEGATFPAATA
AMARWVPKEKRGFAQGITHACARVGNAVAPAAVVAIMAVYGWRESFYICGAISLVWVALW
AVTFTEHPKDHPRMTPAELETLPAPRKKAADVPWRRLFKRMAPVTIVYFCYGWTLWLFLS
WIPQYFLHSYDLDLKKSAIFASAVFFAGVIGDTLGGVVTDKLYDRTGSLKRARSAMVAVC
MLLTMLSLLPLLFTHNLYVSMACLAAGFFFAEMTIGPMWAIPMDIAPEHSGTASGMMNSG
SALAAIISPVLSGYLIDRFGSWELPFIGSMVLMGVGVILALRMQPESKFEAEPADASKPL
RA
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