SitesBLAST
Comparing RR42_RS04270 FitnessBrowser__Cup4G11:RR42_RS04270 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
25% identity, 78% coverage: 1:337/434 of query aligns to 64:406/534 of P53322
- K283 (vs. gap) 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)
22% identity, 92% coverage: 21:418/434 of query aligns to 12:414/430 of P0AA76
- Y29 (= Y39) binding
- D31 (= D41) mutation to N: Loss of galactonate transport activity.
- R32 (= R42) binding
- Y64 (= Y74) binding
- E118 (= E128) mutation to Q: Loss of galactonate transport activity.
- W358 (= W362) binding
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, 60% coverage: 68:329/434 of query aligns to 113:374/495 of Q9NRA2
- K136 (≠ R91) 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 (≠ I136) 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 (≠ TT 151:152) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LQ 226:227) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ RNIAA 228:232) 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 (= G288) 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 (= P294) 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 (= G326) 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
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
22% identity, 92% coverage: 21:419/434 of query aligns to 1:396/409 of 6e9nA
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, 61% coverage: 68:331/434 of query aligns to 113:373/495 of Q8BN82
- H183 (≠ I136) 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.
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
21% identity, 92% coverage: 21:419/434 of query aligns to 4:380/393 of 6e9oA
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, 49% coverage: 119:329/434 of query aligns to 166:374/495 of Q5Q0U0
- R168 (= R121) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L124) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G125) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E128) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A129) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F132) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P133) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I136) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L139) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ RNIAA 228:232) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P294) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G326) 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.
- 136 K→E: Markedly decreases H(+)-coupled sialic acid transporter activity.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
24% identity, 56% coverage: 51:295/434 of query aligns to 71:317/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
21% identity, 78% coverage: 86:425/434 of query aligns to 82:428/452 of Q5EXK5
- D82 (≠ H86) mutation to A: Loss of activity.
- V311 (≠ Y307) mutation to W: Loss of activity.
- D314 (= D310) mutation to A: Loss of activity.
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
23% identity, 79% coverage: 73:415/434 of query aligns to 120:467/497 of Q9Y2C5
- A372 (= A327) 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.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
23% identity, 62% coverage: 44:311/434 of query aligns to 73:313/444 of Q8NLB7
- R103 (≠ K87) mutation to A: Loss of transport activity.
- W309 (≠ Y307) mutation to V: Loss of transport activity.
- D312 (= D310) mutation to A: Loss of transport activity.
- R313 (= R311) 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.
- 57 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.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
23% identity, 77% coverage: 55:387/434 of query aligns to 36:385/446 of A0A0H2VG78
- R102 (= R121) mutation to A: Loss of transport activity.
- I105 (≠ L124) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (≠ Y141) mutation to A: Loss of transport activity.
- Q137 (≠ M156) mutation to A: Loss of transport activity.
- Q250 (≠ S260) mutation to A: Loss of transport activity.
- Q251 (≠ F261) mutation to A: Loss of transport activity.
- N256 (≠ Y266) mutation to A: Loss of transport activity.
- W357 (= W362) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
Query Sequence
>RR42_RS04270 FitnessBrowser__Cup4G11:RR42_RS04270
MTTTAVHSGAADPAFEDATYRKVTLRLVPFLLLCYVVAYLDRVNVGFAKLQMLGDLKFSE
TIYGLGAGIFFIGYFLFEVPSNVILHKVGARIWIARIMITWGVISAAMMFVTTPTMFYVL
RFLLGIAEAGFFPGIILYLTYWYPSHRRGRTTTFFMTAIALSGVIGGPLSGWMMQSFDGR
NGWSGWQWMFLLEGIPSVLVGLVVLAYLDDRIVHAKWLSNEEKALLQRNIAAEDMHKEDA
PIGKVLSSPRVWLMSAIYFSFVMGLYGVSFWLPTIIKQTGVKSPLDIGLLTAIPYGCAVA
GMVLVAYSADRTRERRWHIAIPALLGAVGLVLSVQWHNNTVLALLGLTLATIGILTTLPL
FWSLPTAFLAGTGAAAGIALINSLGNLAGFISPYAVGWLKDMTQSTDSGMYLLAACLVAG
AALTVSVPARMVNK
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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