SitesBLAST
Comparing HSERO_RS02860 FitnessBrowser__HerbieS:HSERO_RS02860 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)
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
27% identity, 89% coverage: 9:364/398 of query aligns to 2:376/409 of 6e9nA
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
26% identity, 89% coverage: 9:364/398 of query aligns to 13:395/430 of P0AA76
- Y29 (= Y25) binding
- D31 (= D27) mutation to N: Loss of galactonate transport activity.
- R32 (= R28) binding
- Y64 (= Y60) binding
- E118 (= E114) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ F327) binding
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
27% identity, 89% coverage: 9:364/398 of query aligns to 5:360/393 of 6e9oA
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
26% identity, 80% coverage: 41:360/398 of query aligns to 75:426/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
30% identity, 59% coverage: 42:275/398 of query aligns to 45:276/403 of P77589
- D75 (= D72) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ W271) mutation to H: 30% increase in 3HPP transport activity.
- K276 (= K275) 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.
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)
21% identity, 57% coverage: 40:264/398 of query aligns to 99:340/495 of Q9NRA2
- K136 (≠ R77) 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 (≠ S122) 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 (≠ AK 137:138) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LR 206:207) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ELVKN 208:212) 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 (= G252) 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 (= P258) 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
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
- 371 G → V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
25% identity, 55% coverage: 23:240/398 of query aligns to 126:347/605 of Q9GQQ0
- E217 (= E114) 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.
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)
22% identity, 59% coverage: 40:274/398 of query aligns to 99:350/495 of Q5Q0U0
- K136 (≠ R77) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R107) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ F110) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G111) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E114) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (= G115) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ S118) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P119) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ S122) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V125) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ ELVKN 208:212) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P258) 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.
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)
22% identity, 56% coverage: 40:260/398 of query aligns to 99:336/495 of Q8BN82
- H183 (≠ S122) 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.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
24% identity, 87% coverage: 24:369/398 of query aligns to 55:403/444 of Q8NLB7
- D57 (= D27) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R73) mutation to A: Loss of transport activity.
- W309 (= W271) mutation to V: Loss of transport activity.
- D312 (= D274) mutation to A: Loss of transport activity.
- R313 (≠ K275) mutation to A: Loss of transport activity.
- I317 (≠ G279) mutation I->H,Y: Loss of transport activity.
- R386 (≠ Q351) 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.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
26% identity, 58% coverage: 68:298/398 of query aligns to 78:338/452 of Q5EXK5
- D82 (= D72) mutation to A: Loss of activity.
- V311 (≠ W271) mutation to W: Loss of activity.
- D314 (= D274) mutation to A: Loss of activity.
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)
21% identity, 83% coverage: 35:364/398 of query aligns to 110:467/582 of Q9JI12
- H128 (≠ L53) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R107) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E114) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ T225) 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.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
19% identity, 83% coverage: 35:364/398 of query aligns to 52:409/452 of 7t3nA
Sites not aligning to the query:
Q8IVW8 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2 from Homo sapiens (Human) (see 2 papers)
24% identity, 57% coverage: 17:242/398 of query aligns to 108:342/549 of Q8IVW8
- R200 (= R107) mutation to S: Loss of function; does not rescue the cardia bifida phenotype in the morpholino knockdown in zebrafish.
- S319 (≠ A215) natural variant: Missing (in DFNB115; uncertain significance; dbSNP:rs749994718)
A2SWM2 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2; Protein two of hearts from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
27% identity, 33% coverage: 23:155/398 of query aligns to 67:197/504 of A2SWM2
- R153 (= R107) mutation to S: In ko157; displays cardia bifida (2 hearts).
8jhqA Cryo-em structure of human s1p transporter spns2 bound with s1p (see paper)
23% identity, 57% coverage: 17:242/398 of query aligns to 14:247/446 of 8jhqA
Sites not aligning to the query:
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
23% identity, 77% coverage: 38:345/398 of query aligns to 55:390/448 of Q51955
- G85 (= G68) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D72) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G75) 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 (= R107) mutation to A: Abolishes 4-HBA transport.
- E144 (= E127) mutation to A: Strong decrease in 4-HBA transport.
- H183 (vs. gap) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D274) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ G279) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (≠ S341) mutation to A: Strong decrease in 4-HBA transport.
Sites not aligning to the query:
- 41 mutation D->A,N: Abolishes 4-HBA transport.; D→E: Decrease in 4-HBA transport.
- 44 mutation D->A,N: Abolishes 4-HBA transport.; D→E: Decrease in 4-HBA transport.
- 398 R→A: Abolishes 4-HBA transport.
- 444 H→A: No change in 4-HBA transport and chemotaxis.
7yubR S1p-bound human spns2 (see paper)
22% identity, 57% coverage: 17:242/398 of query aligns to 16:239/429 of 7yubR
Sites not aligning to the query:
P39386 Multidrug resistance protein MdtM; Multidrug resistance transporter MdtM; MDR transporter MdtM; Multidrug transporter MdtM from Escherichia coli (strain K12) (see 3 papers)
27% identity, 59% coverage: 1:236/398 of query aligns to 1:235/410 of P39386
- D22 (≠ W21) mutation to A: Lack of activity. Retains the ability to bind chloramphenicol, but cannot confer resistance to ethidium bromide and chloramphenicol. Cannot grow at pH 9.5 and 9.75.
- R108 (= R107) mutation to K: Decreases resistance to ethidium bromide and chloramphenicol. Retains the ability to bind chloramphenicol.
8g92A Structure of inhibitor 16d-bound spns2 (see paper)
25% identity, 36% coverage: 17:159/398 of query aligns to 10:150/415 of 8g92A
Sites not aligning to the query:
Query Sequence
>HSERO_RS02860 FitnessBrowser__HerbieS:HSERO_RS02860
MPMATTRAQKMICLSALFLAWAVGYADRIVMSTAIIPISKEFALDAQQAGMVLSAFYVSY
ALMQLMGGWLSDRYGSRIVVVMCVVAWSLFTGLTSMAWSFASLLLIRFLFGAGEGCFSPA
SSVTVAEVFPQQERARAKSFLISTVFLGNAVGSGMVALTVVYLGWRGTFHILAFVGMIVA
AILWLALRSGMAAQQARSAARPKNQLRELVKNPTALRLTAIWFCTSIVYIGMISWMPSFL
LKVYQIDLLHIGIASAIPYLLAFLGTNVVGWLLDKHGKGREKYFMMGGALACAVFLALMI
STTVIELLVVYWTLCLLSFNFVYATVFSVPLKHFPSHLIGSATGLMNFGGQLAGSIAPVV
MGSLIVAFNGAYLAAFWFLVGSAMMSFLIAMTWRLAPP
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