SitesBLAST
Comparing WP_011385542.1 NCBI__GCF_000009985.1:WP_011385542.1 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 12 hits to proteins with known functional sites (download)
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 80% coverage: 5:352/437 of query aligns to 80:430/534 of P53322
- K283 (≠ D210) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
21% identity, 92% coverage: 21:423/437 of query aligns to 21:428/430 of P0AA76
- Y29 (= Y29) binding
- D31 (= D31) mutation to N: Loss of galactonate transport activity.
- R32 (= R32) binding
- Y64 (= Y64) binding
- E118 (= E118) mutation to Q: Loss of galactonate transport activity.
- W358 (= W352) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
21% identity, 95% coverage: 11:423/437 of query aligns to 2:409/409 of 6e9nA
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
23% identity, 82% coverage: 76:434/437 of query aligns to 82:447/452 of Q5EXK5
- D82 (≠ E76) mutation to A: Loss of activity.
- V311 (≠ R298) mutation to W: Loss of activity.
- D314 (= D301) mutation to A: Loss of activity.
Q9C0U9 Uncharacterized transporter PB1C11.03 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
22% identity, 53% coverage: 12:241/437 of query aligns to 93:328/570 of Q9C0U9
Sites not aligning to the query:
- 14 modified: Phosphoserine
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
19% identity, 95% coverage: 11:423/437 of query aligns to 5:393/393 of 6e9oA
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)
20% identity, 87% coverage: 44:424/437 of query aligns to 99:484/495 of Q9NRA2
- K136 (≠ R81) 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 (≠ I126) 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 (≠ VT 141:142) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LI 215:216) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ NAMNE 217:221) 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 (= G279) 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 (= P285) 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 (≠ A317) 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
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)
21% identity, 59% coverage: 44:301/437 of query aligns to 99:350/495 of Q8BN82
- H183 (≠ I126) 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.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
25% identity, 54% coverage: 60:293/437 of query aligns to 90:324/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
28% identity, 45% coverage: 31:226/437 of query aligns to 22:199/446 of A0A0H2VG78
- D22 (= D31) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R111) mutation to A: Loss of transport activity.
- I105 (≠ L114) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (≠ Y131) mutation to A: Loss of transport activity.
- Q137 (≠ M146) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 250 Q→A: Loss of transport activity.
- 251 Q→A: Loss of transport activity.
- 256 N→A: Loss of transport activity.
- 357 W→A: Loss of transport 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)
20% identity, 59% coverage: 44:301/437 of query aligns to 99:350/495 of Q5Q0U0
- K136 (≠ R81) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R111) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L114) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G115) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E118) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A119) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F122) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P123) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I126) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L129) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ NAMNE 217:221) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P285) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
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.
- 371 G→V: Remains in the endoplasmic reticulum.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
21% identity, 86% coverage: 5:382/437 of query aligns to 18:404/448 of Q51955
- D41 (≠ A28) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D31) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (≠ N72) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (≠ E76) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G79) 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 (= R111) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ Y131) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q176) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D301) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ R306) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (≠ A364) mutation to A: Strong decrease in 4-HBA transport.
- R398 (≠ N376) mutation to A: Abolishes 4-HBA transport.
Sites not aligning to the query:
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Query Sequence
>WP_011385542.1 NCBI__GCF_000009985.1:WP_011385542.1
MNTDMEKRVLRRISWRIVPFIMLLYFIAYIDRVNIGFASLTMNKDLGFTSSVFGFGAGIF
FFGYFLFEVPSNLILEKVGARLWITRVMITWGLISGAMAFVQGSTSFYVLRFLLGAAEAG
FFPGIILYLSYWFPARHRAGVTALFMAAAPISTALGSPISAALLELHGVMGLAGWQWMFI
IEALPALILGVVVFFYMTDRPEKATWMPEDERAWLINAMNEEAASKSGHAKHSIWRGLAD
PRVLALALIYFGTSAGLYTLGIWAPQIIKQLGVSSMTVGWLNMIPPTASVIAMVLWARHS
DRTSERTWHVVGACLVASAGLVFAGNADGVFTVILALTLVNIGISAAKPPLWSMPTMFLS
GSAAAAGIATINSIGNLGGFAGPAMIGWIKDLTGSFMGGLYFVAALLAISAVTTLLLARS
QRKSAAASAAAAQAASN
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