SitesBLAST
Comparing Pf1N1B4_5129 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5129 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 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, 91% coverage: 3:426/467 of query aligns to 1:399/430 of P0AA76
- Y29 (= Y35) binding
- D31 (= D37) mutation to N: Loss of galactonate transport activity.
- R32 (= R38) binding
- Y64 (= Y70) binding
- E118 (= E144) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ F385) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
25% identity, 87% coverage: 20:426/467 of query aligns to 3:380/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
23% identity, 88% coverage: 17:426/467 of query aligns to 3:364/393 of 6e9oA
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
24% identity, 63% coverage: 51:344/467 of query aligns to 75:352/493 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)
24% identity, 52% coverage: 51:292/467 of query aligns to 100:317/495 of Q9NRA2
- K136 (= K87) 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 (≠ I152) 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 167:168) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IR 234:235) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ SDQVV 236:240) 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)
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
- 328 G → 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
- 334 P → 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
- 371 G → V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
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)
26% identity, 35% coverage: 130:291/467 of query aligns to 161:316/495 of Q5Q0U0
- R168 (= R137) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L140) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (≠ A141) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E144) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A145) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F148) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P149) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I152) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ T155) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ SDQVV 236:240) mutation Missing: 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.
- 136 K→E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- 334 P→R: Abolishes H(+)-coupled sialic acid transporter activity.
- 371 G→V: Remains in the endoplasmic reticulum.
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)
26% identity, 35% coverage: 130:291/467 of query aligns to 161:316/495 of Q8BN82
- H183 (≠ I152) 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.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 35% coverage: 156:320/467 of query aligns to 145:309/452 of 7t3nA
Sites not aligning to the query:
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)
24% identity, 39% coverage: 137:320/467 of query aligns to 184:367/582 of Q9JI12
- R184 (= R137) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E144) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ T276) 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.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
26% identity, 62% coverage: 37:327/467 of query aligns to 57:314/444 of Q8NLB7
- D57 (= D37) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (≠ K83) mutation to A: Loss of transport activity.
- W309 (= W322) mutation to V: Loss of transport activity.
- D312 (≠ S325) mutation to A: Loss of transport activity.
- R313 (≠ Y326) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
- 317 mutation I->H,Y: Loss of transport activity.
- 386 R→A: Loss of transport activity.
Q6ZSM3 Monocarboxylate transporter 12; MCT 12; Creatine transporter 2; CRT2; Solute carrier family 16 member 12 from Homo sapiens (Human) (see 3 papers)
22% identity, 66% coverage: 17:323/467 of query aligns to 45:339/516 of Q6ZSM3
- R67 (≠ Q39) mutation to A: Abolishes creatine efflux activity. Does not affect plasma membrane localization.
- D95 (≠ Y70) mutation to A: Decreases in the creatine efflux activity. Does not affect plasma membrane localization.
- D329 (≠ T313) mutation to A: Decreases creatine efflux activity. Loss of localization to the plasma membrane.
Sites not aligning to the query:
- 245:516 natural variant: Missing (in CTRCT47; loss of localization to the plasma membrane; retained in the endoplasmic reticulum where it undergoes degradation by the proteasome; has no dominant effect on wild-type protein expression and localization)
- 360 D→A: Does not affect creatine efflux activity. Does not affect plasma membrane localization.
- 387 D→A: Does not affect creatine efflux activity.
- 437 G → S: found in a patient with age-related cataract; uncertain significance; decreases creatine transport; dbSNP:rs759863805
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
20% identity, 50% coverage: 3:236/467 of query aligns to 1:217/452 of Q5EXK5
- D82 (= D82) mutation to A: Loss of activity.
Sites not aligning to the query:
- 311 V→W: Loss of activity.
- 314 D→A: Loss of activity.
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
24% identity, 49% coverage: 15:245/467 of query aligns to 108:318/605 of Q9GQQ0
- E217 (= E144) 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.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
19% identity, 41% coverage: 14:203/467 of query aligns to 21:190/448 of Q51955
- D41 (≠ N34) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D37) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G78) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D82) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G85) 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 (= R137) mutation to A: Abolishes 4-HBA transport.
- E144 (= E157) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ E196) 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.
Query Sequence
>Pf1N1B4_5129 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5129
MNLNEPINAQRIGQAVGNYRWTICALLFFATTVNYLDRQVLSLLAPDLSTQFGWSNSDYA
NIASVFQFVYAISMLFAGRVVDKIGTKTAYVVAICIWSTGAVMHAFAVPMGEGIGAVSSA
LGIAMIPVSIAGFMVSRAVLAIGEAGNFPIAIKATAEYFPKKERSFATGIFNSGANVGAI
LAPICVPLIASLWGWEAAFIVIGMLGFVWVGVWIALYEKPEQQKRLSAQELAYIRSDQVV
PVVTRPVPGVADKKVSWFKLLTYRQTWAFAFGKFMTDGVWWFFLFWLPTYLSAQYGMKGQ
AIVMPLAVLYSMTMIGSIGGGWFPSYFMSRGDAPYDGRMKAMLVIAFFPLLVLLAQPLGY
ISFWVPVLLIGVGASAHQAWSCNIFTTVSDMFPQKSIASVVGIGGLAGGLGGVVMTKIGG
WVIDHYKLIGDIHTGYMIMFAICALAYLVAWSVMKALVPRHKEITDL
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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