SitesBLAST
Comparing H281DRAFT_05028 FitnessBrowser__Burk376:H281DRAFT_05028 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) 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, 81% coverage: 6:352/429 of query aligns to 74:432/534 of P53322
- K283 (≠ D217) 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)
24% identity, 90% coverage: 36:420/429 of query aligns to 29:423/430 of P0AA76
- Y29 (= Y36) binding
- D31 (= D38) mutation to N: Loss of galactonate transport activity.
- R32 (= R39) binding
- Y64 (= Y71) binding
- E118 (= E125) mutation to Q: Loss of galactonate transport activity.
- W358 (= W357) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
24% identity, 90% coverage: 36:420/429 of query aligns to 18:404/409 of 6e9nA
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, 66% coverage: 65:347/429 of query aligns to 113:401/495 of Q9NRA2
- K136 (≠ R88) 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 (≠ I133) 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 (≠ AI 148:149) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ -L 222) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ LEGET 223:227) 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 (= G283) 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 (= P289) 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 (≠ P317) 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)
23% identity, 66% coverage: 65:347/429 of query aligns to 113:401/495 of Q5Q0U0
- K136 (≠ R88) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R118) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L121) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G122) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E125) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A126) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ A129) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P130) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I133) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L136) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ G--ET 225:227) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P289) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (≠ P317) 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)
23% identity, 66% coverage: 65:347/429 of query aligns to 113:401/495 of Q8BN82
- H183 (≠ I133) 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.
6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
25% identity, 89% coverage: 49:429/429 of query aligns to 32:395/404 of 6zguA
6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
25% identity, 89% coverage: 49:429/429 of query aligns to 32:395/404 of 6zgtA
6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
25% identity, 89% coverage: 49:429/429 of query aligns to 32:395/404 of 6zgsA
6zgrA Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
26% identity, 87% coverage: 55:429/429 of query aligns to 36:390/399 of 6zgrA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
24% identity, 90% coverage: 36:420/429 of query aligns to 21:388/393 of 6e9oA
A0LNN5 L-lactate transporter; SfMCT from Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) (see paper)
25% identity, 89% coverage: 49:429/429 of query aligns to 38:411/412 of A0LNN5
- Y119 (= Y134) binding ; mutation Y->A,F: Loss of transport activity.
- L145 (≠ G156) mutation to A: Strong decrease in transport activity.
- H250 (≠ W266) mutation to A: Strong decrease in transport activity.; mutation to F: Loss of transport activity.
- R256 (≠ K272) mutation to A: No change in transport activity.; mutation to D: Increases transport activity.
- D257 (≠ E273) mutation to A: Loss of transport activity.
- N276 (≠ A292) mutation to A: Loss of transport activity.
- R280 (≠ C296) binding ; mutation to A: Abolishes L-lactate binding and L-lactate transport.
- Y331 (≠ C348) mutation to A: Loss of transport activity.; mutation to F: No change in transport activity.
- F335 (≠ Y353) mutation to A: Increases transport activity.
- F359 (≠ N377) mutation to A: Loss of transport activity.
- C362 (≠ G380) mutation to A: Decrease in transport activity.
- K377 (= K395) mutation K->A,D: No change in transport activity.
- D378 (≠ A396) mutation to A: Loss of transport activity.
- Y383 (≠ M401) mutation to A: Loss of transport activity.; mutation to F: Strong decrease in transport activity.
Sites not aligning to the query:
- 28 L→A: Loss of transport activity.
6g9xA Crystal structure of a mfs transporter at 2.54 angstroem resolution (see paper)
26% identity, 83% coverage: 73:429/429 of query aligns to 53:387/396 of 6g9xA
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
24% identity, 80% coverage: 84:428/429 of query aligns to 83:436/452 of Q5EXK5
- V311 (≠ R302) mutation to W: Loss of activity.
- D314 (= D305) mutation to A: Loss of activity.
Sites not aligning to the query:
- 82 D→A: Loss of activity.
6zguB Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
26% identity, 86% coverage: 49:417/429 of query aligns to 26:354/364 of 6zguB
6zgtB Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
26% identity, 86% coverage: 49:417/429 of query aligns to 26:354/364 of 6zgtB
6zgsB Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
26% identity, 86% coverage: 49:417/429 of query aligns to 26:354/364 of 6zgsB
6zgrB Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
26% identity, 85% coverage: 55:417/429 of query aligns to 32:353/364 of 6zgrB
6g9xB Crystal structure of a mfs transporter at 2.54 angstroem resolution (see paper)
26% identity, 85% coverage: 55:417/429 of query aligns to 32:354/368 of 6g9xB
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)
21% identity, 66% coverage: 25:305/429 of query aligns to 83:371/582 of Q9JI12
- R88 (≠ A30) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ A64) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R118) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E125) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ V256) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
Query Sequence
>H281DRAFT_05028 FitnessBrowser__Burk376:H281DRAFT_05028
MSAIHPSAAGDPAAALYSKLNWRLLPFLVACYMFAYLDRVNVGFAKLQMQSDLGFSDAAY
GVGAGIFFIGYVLFELPSNLMLPKVGARKTFSRILVLWGITSACMLFVRSVPAFYAMRFL
LGVFEAGFAPGMIYYLSCWYGPARMARAIALVFVAGPLGGIVGGPVSAWLMTSLAGVGGL
AGWQWMFLVEGLPCIVLGLLTLRVISDRPADARWLDDGEKALLEGETAPTQHRADSFKAV
LKSPRVYVLALAYFSVIFPIYAISFWLPTLLKEQGVTDTVRLGWYTAIPYVAAAVCMYLA
GRSSDRFGERRYHCAIPALGAAACLIATVFADGNLPLTLLALTLGTACLWMAYTVFWAIP
SQLVEGTAAAGGIALINTVGLSGGFWGPAVVGWTKAGTGSMHAGLLVMACAAALAAILIL
KGKLTMKQQ
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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