SitesBLAST
Comparing Dsui_3371 FitnessBrowser__PS:Dsui_3371 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)
1lqaA Tas protein from escherichia coli in complex with NADPH (see paper)
50% identity, 100% coverage: 1:349/350 of query aligns to 1:345/346 of 1lqaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (= M21), D48 (= D48), Y53 (= Y53), H132 (= H131), N180 (= N179), Q205 (= Q204), Y233 (= Y233), S234 (= S234), L236 (= L236), F238 (= F238), G239 (= G239), T242 (≠ S242), K244 (= K244), A254 (vs. gap), R255 (= R254), G308 (= G308), T310 (= T310), Q314 (= Q314), N318 (= N318)
P0A9T4 Protein tas from Escherichia coli (strain K12) (see paper)
50% identity, 100% coverage: 1:349/350 of query aligns to 1:345/346 of P0A9T4
- 234:244 (vs. 234:244, 64% identical) binding
8hw0A The structure of akr6d1
33% identity, 92% coverage: 1:321/350 of query aligns to 1:300/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (vs. gap), Q27 (= Q26), D49 (= D48), Y54 (= Y53), R123 (≠ W132), S152 (= S178), Q178 (= Q204), W207 (≠ Y233), S208 (= S234), P209 (= P235), L210 (= L236), S212 (≠ F238), K218 (= K244), S227 (≠ G253), R228 (= R254), I285 (= I306), G287 (= G308), S289 (≠ T310), Q293 (= Q314), D296 (≠ E317), N297 (= N318)
4aubB The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
32% identity, 92% coverage: 1:321/350 of query aligns to 11:303/335 of 4aubB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (vs. gap), D59 (= D48), Y64 (= Y53), H136 (= H131), Q191 (= Q204), F220 (≠ Y233), T221 (≠ S234), P222 (= P235), L223 (= L236), Q225 (≠ F238), G226 (= G239), K231 (= K244), R241 (= R254), R244 (≠ A257), L288 (≠ I306), G290 (= G308), S292 (≠ T310), Q296 (= Q314), E299 (= E317), N300 (= N318)
Sites not aligning to the query:
3n6qD Crystal structure of yghz from e. Coli (see paper)
32% identity, 92% coverage: 1:321/350 of query aligns to 12:290/315 of 3n6qD
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
30% identity, 92% coverage: 1:323/350 of query aligns to 1:294/310 of P46336
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
30% identity, 91% coverage: 6:323/350 of query aligns to 5:293/311 of 1pz0A
- active site: D52 (= D48), Y57 (= Y53), N91 (≠ M94), H124 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H131), Q174 (= Q204), Y202 (= Y233), F203 (≠ S234), P204 (= P235), L205 (= L236), S207 (≠ F238), G208 (= G239), A211 (≠ S242), K213 (= K244)
4aubE The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
31% identity, 92% coverage: 1:321/350 of query aligns to 12:278/297 of 4aubE
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G30 (= G19), W32 (vs. gap), D60 (= D48), Y65 (= Y53), Q192 (= Q204), F221 (≠ Y233), T222 (≠ S234), P223 (= P235), L224 (= L236), Q226 (≠ F238), T230 (≠ S242), K232 (= K244), L263 (≠ I306), G265 (= G308), S267 (≠ T310), Q271 (= Q314), E274 (= E317), N275 (= N318)
Sites not aligning to the query:
P63144 Voltage-gated potassium channel subunit beta-1; K(+) channel subunit beta-1; Kv-beta-1; EC 1.1.1.- from Rattus norvegicus (Rat) (see paper)
30% identity, 99% coverage: 1:346/350 of query aligns to 71:393/401 of P63144
- K152 (= K86) mutation to M: Loss of enzyme activity.
Q13303 Voltage-gated potassium channel subunit beta-2; K(+) channel subunit beta-2; Kv-beta-2; hKvbeta2; EC 1.1.1.- from Homo sapiens (Human) (see 2 papers)
29% identity, 98% coverage: 3:346/350 of query aligns to 39:359/367 of Q13303
- T56 (= T20) binding
- W57 (vs. gap) binding
- Q63 (= Q26) binding
- D85 (= D48) binding
- Y90 (= Y53) mutation to F: No effect on its activity in promoting KCNA4 channel closure.
- S112 (≠ Q80) modified: Phosphoserine
- S188 (= S178) binding
- R189 (≠ N179) binding
- Q214 (= Q204) binding
- W243 (≠ Y233) binding
- S244 (= S234) binding
- P245 (= P235) binding
- L246 (= L236) binding
- A247 (= A237) binding
- C248 (≠ F238) binding
- K254 (= K244) binding
- R264 (= R254) binding
- S325 (≠ T310) binding
- Q329 (= Q314) binding
- E332 (= E317) binding
- N333 (= N318) binding
Sites not aligning to the query:
- 31 modified: Phosphoserine
7wf3C Composite map of human kv1.3 channel in apo state with beta subunits (see paper)
29% identity, 98% coverage: 3:346/350 of query aligns to 6:326/328 of 7wf3C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), R156 (≠ N179), W210 (≠ Y233), S211 (= S234), P212 (= P235), L213 (= L236), C215 (≠ F238), K221 (= K244), R231 (= R254), Q296 (= Q314), E299 (= E317), N300 (= N318)
P62483 Voltage-gated potassium channel subunit beta-2; K(+) channel subunit beta-2; Kv-beta-2; EC 1.1.1.- from Rattus norvegicus (Rat) (see 11 papers)
29% identity, 98% coverage: 3:346/350 of query aligns to 39:359/367 of P62483
- T56 (= T20) binding
- W57 (vs. gap) binding
- Q63 (= Q26) binding
- D85 (= D48) binding
- Y90 (= Y53) mutation to F: Abolishes enzyme activity, but has no effect on NADPH binding.
- S112 (≠ Q80) modified: Phosphoserine
- N158 (≠ H131) binding
- S188 (= S178) binding
- R189 (≠ N179) binding
- Q214 (= Q204) binding
- W243 (≠ Y233) binding
- S244 (= S234) binding
- P245 (= P235) binding
- L246 (= L236) binding
- A247 (= A237) binding
- C248 (≠ F238) binding
- K254 (= K244) binding
- Y262 (≠ A252) binding
- R264 (= R254) binding
- G323 (= G308) binding
- S325 (≠ T310) binding
- Q329 (= Q314) binding
- E332 (= E317) binding
- N333 (= N318) binding
Sites not aligning to the query:
- 9 modified: Phosphoserine; S→A: Impairs interaction with MAPRE1 and association with microtubules.
- 20 modified: Phosphoserine; S→A: No effect on interaction with MAPRE1 and association with microtubules.
- 31 S→A: Impairs interaction with MAPRE1 and association with microtubules.
P62482 Voltage-gated potassium channel subunit beta-2; K(+) channel subunit beta-2; Kv-beta-2; Neuroimmune protein F5; EC 1.1.1.- from Mus musculus (Mouse) (see 2 papers)
29% identity, 98% coverage: 3:346/350 of query aligns to 39:359/367 of P62482
- Y90 (= Y53) mutation to F: No detectable phenotype.
- S112 (≠ Q80) modified: Phosphoserine
Sites not aligning to the query:
- 20 modified: Phosphoserine
3eauA Voltage-dependent k+ channel beta subunit in complex with cortisone (see paper)
29% identity, 98% coverage: 3:346/350 of query aligns to 5:325/327 of 3eauA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G19), W23 (vs. gap), Q29 (= Q26), D51 (= D48), Y56 (= Y53), K84 (= K86), S154 (= S178), Q180 (= Q204), W209 (≠ Y233), S210 (= S234), P211 (= P235), L212 (= L236), A213 (= A237), C214 (≠ F238), G215 (= G239), K220 (= K244), R230 (= R254), L287 (≠ I306), L288 (≠ I307), G289 (= G308), S291 (≠ T310), Q295 (= Q314), E298 (= E317), N299 (= N318)
- binding 17,21-dihydroxypregna-1,4-diene-3,11,20-trione: W23 (vs. gap), V55 (≠ M52), Y56 (= Y53), W87 (vs. gap), N124 (≠ H131), R155 (≠ N179), I174 (≠ P198), I177 (≠ A201), I202 (≠ E226)
1exbA Structure of the cytoplasmic beta subunit-t1 assembly of voltage- dependent k channels (see paper)
29% identity, 98% coverage: 3:346/350 of query aligns to 4:324/326 of 1exbA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), W22 (vs. gap), Q28 (= Q26), D50 (= D48), Y55 (= Y53), S153 (= S178), R154 (≠ N179), Q179 (= Q204), W208 (≠ Y233), S209 (= S234), P210 (= P235), L211 (= L236), C213 (≠ F238), G214 (= G239), S217 (= S242), K219 (= K244), S228 (≠ G253), R229 (= R254), L286 (≠ I306), G288 (= G308), S290 (≠ T310), Q294 (= Q314), E297 (= E317), N298 (= N318)
Q14722 Voltage-gated potassium channel subunit beta-1; K(+) channel subunit beta-1; Kv-beta-1; EC 1.1.1.- from Homo sapiens (Human) (see paper)
29% identity, 99% coverage: 1:346/350 of query aligns to 89:411/419 of Q14722
- Y307 (= Y245) mutation to F: Reduces affinity for NADPH.
- R316 (≠ A251) mutation to E: Nearly abolishes NADPH binding.
P77256 NADH-specific methylglyoxal reductase; AKR11B2; EC 1.1.1.- from Escherichia coli (strain K12) (see paper)
29% identity, 92% coverage: 1:321/350 of query aligns to 1:304/326 of P77256
- D232 (= D248) mutation D->A,E: Converts the protein into an enzyme with dual specificity, i.e. that is able to use both NADPH and NADH as cosubstrates.
5t79A X-ray crystal structure of a novel aldo-keto reductases for the biocatalytic conversion of 3-hydroxybutanal to 1,3-butanediol (see paper)
32% identity, 97% coverage: 1:341/350 of query aligns to 13:312/315 of 5t79A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G31 (= G19), W33 (vs. gap), Y66 (= Y53), H138 (= H131), N169 (= N179), Q193 (= Q204), F221 (≠ Y233), S222 (= S234), L224 (= L236), G226 (≠ F238), T230 (≠ S242), R232 (≠ K244), S263 (≠ T289), L280 (≠ I306), G282 (= G308), S284 (≠ T310), Q288 (= Q314)
6kiyA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor epalrestat (see paper)
30% identity, 96% coverage: 1:336/350 of query aligns to 2:273/275 of 6kiyA
- binding {5-[(2E)-2-methyl-3-phenylprop-2-en-1-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl}acetic acid: W22 (≠ M21), Y59 (= Y53), W87 (= W96), H118 (= H131), R204 (≠ F238)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), T21 (= T20), W22 (≠ M21), Y59 (= Y53), H118 (= H131), N149 (= N179), Q170 (= Q204), Y199 (= Y233), S200 (= S234), P201 (= P235), L202 (= L236), R204 (≠ F238), T205 (≠ G239), Y227 (≠ T289), I243 (= I306), P244 (≠ I307), K245 (≠ G308), G247 (≠ T310), R248 (≠ S311), H251 (≠ Q314), E254 (= E317), N255 (= N318)
6kikA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor tolrestat (see paper)
30% identity, 96% coverage: 1:336/350 of query aligns to 2:273/275 of 6kikA
Query Sequence
>Dsui_3371 FitnessBrowser__PS:Dsui_3371
MEYRALGRSELKVSAVCLGTMTFGQQNSEAEGHAQLDRAVAAGINFIDTAEMYPVPARAE
TYGATERIVGSWLKRQARDQVVIATKAAGPARRMEWIRGGPLAFDLANLRRALEDSLQRL
QTDYVDLYQLHWPARNQPMFGQWQFEPEQERESTPLRETLEALAVLVQEGKIRQVGVSNE
HPWGVMEFLRLAREHGLPAIASTQNAYNLINRLYDTGGLSEVCFRERVSLLAYSPLAFGH
LSGKYLADAKAAGRITAFPGFGQRYEKVNVPPALAAYRELAARHGLSMTGLALAFCYNRP
GVTSTIIGATSLAQLEENLEAWERRPGAEQWRAIQAEIDAVHQRYPNPAL
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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