SitesBLAST
Comparing H281DRAFT_03217 FitnessBrowser__Burk376:H281DRAFT_03217 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
45% identity, 94% coverage: 23:451/455 of query aligns to 6:429/430 of P0AA76
- Y29 (= Y46) binding
- D31 (= D48) mutation to N: Loss of galactonate transport activity.
- R32 (= R49) binding
- Y64 (= Y81) binding
- E118 (= E135) mutation to Q: Loss of galactonate transport activity.
- W358 (= W379) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
47% identity, 92% coverage: 31:450/455 of query aligns to 3:409/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
44% identity, 93% coverage: 26:450/455 of query aligns to 1:393/393 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)
27% identity, 84% coverage: 31:414/455 of query aligns to 70:465/582 of Q9JI12
- R88 (= R49) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ F74) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R128) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E135) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ G273) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
26% identity, 84% coverage: 31:414/455 of query aligns to 12:407/452 of 7t3nA
- binding (1s,3r)-1-aminocyclopentane-1,3-dicarboxylic acid: Y77 (= Y81), Y137 (≠ F139), Y165 (= Y167), R264 (≠ G273), F268 (≠ L277), Y269 (≠ V278)
- binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: R12 (= R31), Y13 (= Y32), E152 (= E154), G163 (= G165)
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
25% identity, 78% coverage: 62:416/455 of query aligns to 75:430/493 of Q03567
Sites not aligning to the query:
- 69 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, 87% coverage: 58:455/455 of query aligns to 96:489/495 of Q9NRA2
- K136 (= K98) 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 (≠ S143) 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 (≠ AT 158:159) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IE 225:226) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- S----SLRN 268:272 (≠ AGGGLTHRH 227:235) 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 (= G300) 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 (= P306) 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 (≠ A341) 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)
24% identity, 87% coverage: 61:455/455 of query aligns to 99:489/495 of Q5Q0U0
- K136 (= K98) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R128) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L131) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G132) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E135) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A136) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F139) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P140) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ S143) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V146) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- S----SLKN 268:272 (≠ AGGGLTHRH 227:235) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P306) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (≠ A341) 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, 87% coverage: 61:455/455 of query aligns to 99:489/495 of Q8BN82
- H183 (≠ S143) 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)
24% identity, 91% coverage: 9:423/455 of query aligns to 62:457/497 of Q9Y2C5
- N66 (≠ T13) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
- N75 (≠ A22) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-66 and A-90.
- N90 (≠ D48) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
- A372 (≠ I340) to T: in dbSNP:rs11754288
Q91X85 Heme transporter FLVCR2; Calcium-chelate transporter; CCT; Feline leukemia virus subgroup C receptor-related protein 2; Major facilitator superfamily domain containing 7C from Mus musculus (Mouse) (see paper)
20% identity, 98% coverage: 4:450/455 of query aligns to 80:516/551 of Q91X85
Sites not aligning to the query:
- 1:80 mutation Missing: Present at mitochondrial membrane. Impairs interaction with HMOX1. Abolishes the response to heme.
Q9UPI3 Heme transporter FLVCR2; Calcium-chelate transporter; CCT; Feline leukemia virus subgroup C receptor-related protein 2 from Homo sapiens (Human) (see 2 papers)
21% identity, 94% coverage: 23:450/455 of query aligns to 76:493/526 of Q9UPI3
Sites not aligning to the query:
- 16 V → A: in dbSNP:rs2287015
- 30:66 HPSVSVHPSVSINPSVSVHPSSSAHPSALAQPSGLAH→APSVSVAPSVSINPSVSVAPSSSAAPSALAQPSGLAA: Loss of heme-binding activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 36% coverage: 30:195/455 of query aligns to 24:190/448 of Q51955
- D41 (≠ N45) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D48) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G89) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D93) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G96) 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 (= R128) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ T148) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ R187) 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.
Q8IVW8 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2 from Homo sapiens (Human) (see 2 papers)
25% identity, 34% coverage: 2:157/455 of query aligns to 87:229/549 of Q8IVW8
- R200 (≠ L129) mutation to S: Loss of function; does not rescue the cardia bifida phenotype in the morpholino knockdown in zebrafish.
Sites not aligning to the query:
- 319 natural variant: Missing (in DFNB115; uncertain significance; dbSNP:rs749994718)
8g92A Structure of inhibitor 16d-bound spns2 (see paper)
26% identity, 28% coverage: 29:157/455 of query aligns to 1:131/415 of 8g92A
Sites not aligning to the query:
7yubR S1p-bound human spns2 (see paper)
27% identity, 27% coverage: 37:157/455 of query aligns to 15:137/429 of 7yubR
Sites not aligning to the query:
7yudR Fty720p-bound human spns2 (see paper)
27% identity, 27% coverage: 37:157/455 of query aligns to 8:130/417 of 7yudR
Sites not aligning to the query:
Query Sequence
>H281DRAFT_03217 FitnessBrowser__Burk376:H281DRAFT_03217
MPQSTQTRPADVTRQAGASTTASTARRSNARYQILGLLAVGTMINYLDRTVLGIAAPQLT
KELGINAAMMGLLFSVFSWSYVASQIPGGLFLDRFGSKLTYFLSMTFWSLCTLAQGLVHG
IAGLFVFRLGLGVSEAPCFPTNSRVVATWFPQSERAMATGTYTVGEYIGLAFFSPFLFML
MGAFGWRSLFYVVGGVGIVFGVIWWLMYREPRDHPSANQAELDYIEAGGGLTHRHKDGGA
AAAPAKGGFEWRTIGRLLKHRQLTGICLGQFAGNSTLVFFLTWFPTYLATERHMGWLKIG
FFAIMPFIAASIGVMFGGLFSDWLLRRGKSANVARKLPIIAGLLLASTIILANYVESNVA
VIAILSVAFFAQGMAALGWTLVSDIAPEGLLGVTGGIFNFAANLAGIVTPLVVGFIVAAT
GSFVGALVFIGVIALIGALSYIFIVGDIKRIVLVD
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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