SitesBLAST
Comparing BWI76_RS09015 FitnessBrowser__Koxy:BWI76_RS09015 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)
8hw0A The structure of akr6d1
37% identity, 92% coverage: 1:320/346 of query aligns to 1:318/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (vs. gap), Q27 (= Q35), D49 (= D57), Y54 (= Y62), R123 (≠ G133), S152 (= S162), Q178 (= Q188), W207 (= W216), S208 (= S217), P209 (= P218), L210 (= L219), S212 (≠ G221), K218 (= K227), S227 (≠ G232), R228 (≠ Q233), I285 (= I289), G287 (= G291), S289 (≠ K293), Q293 (= Q297), D296 (≠ E300), N297 (= N301)
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
36% identity, 92% coverage: 1:320/346 of query aligns to 1:315/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ M21), D49 (= D57), Y54 (= Y62), S151 (= S162), Y204 (≠ W216), F205 (≠ S217), L207 (= L219), Q209 (≠ G221), G210 (= G222), T213 (≠ S225), K215 (= K227), R227 (= R239), V284 (≠ I289), G286 (= G291), Q292 (= Q297), N296 (= N301)
6ow0B Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
36% identity, 92% coverage: 1:320/346 of query aligns to 1:291/301 of 6ow0B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ M21), Y50 (= Y62), H117 (= H132), S147 (= S162), Y200 (≠ W216), F201 (≠ S217), L203 (= L219), Q205 (≠ G221), T209 (≠ S225), Q268 (= Q297), N272 (= N301)
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)
35% identity, 92% coverage: 3:320/346 of query aligns to 39:354/367 of Q13303
- T56 (= T20) binding
- W57 (vs. gap) binding
- Q63 (= Q35) binding
- D85 (= D57) binding
- Y90 (= Y62) mutation to F: No effect on its activity in promoting KCNA4 channel closure.
- S112 (≠ N84) modified: Phosphoserine
- S188 (= S162) binding
- R189 (≠ N163) binding
- Q214 (= Q188) binding
- W243 (= W216) binding
- S244 (= S217) binding
- P245 (= P218) binding
- L246 (= L219) binding
- A247 (= A220) binding
- C248 (≠ G221) binding
- K254 (= K227) binding
- R264 (vs. gap) binding
- S325 (≠ K293) binding
- Q329 (= Q297) binding
- E332 (= E300) binding
- N333 (= N301) 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)
35% identity, 92% coverage: 3:320/346 of query aligns to 6:321/328 of 7wf3C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), R156 (≠ N163), W210 (= W216), S211 (= S217), P212 (= P218), L213 (= L219), C215 (≠ G221), K221 (= K227), R231 (vs. gap), Q296 (= Q297), E299 (= E300), N300 (= N301)
Q9P7U2 Putative aryl-alcohol dehydrogenase C977.14c; EC 1.1.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 91% coverage: 3:318/346 of query aligns to 9:339/351 of Q9P7U2
- S113 (≠ T97) modified: Phosphoserine
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)
35% identity, 92% coverage: 3:320/346 of query aligns to 39:354/367 of P62483
- T56 (= T20) binding
- W57 (vs. gap) binding
- Q63 (= Q35) binding
- D85 (= D57) binding
- Y90 (= Y62) mutation to F: Abolishes enzyme activity, but has no effect on NADPH binding.
- S112 (≠ N84) modified: Phosphoserine
- N158 (≠ H132) binding
- S188 (= S162) binding
- R189 (≠ N163) binding
- Q214 (= Q188) binding
- W243 (= W216) binding
- S244 (= S217) binding
- P245 (= P218) binding
- L246 (= L219) binding
- A247 (= A220) binding
- C248 (≠ G221) binding
- K254 (= K227) binding
- Y262 (vs. gap) binding
- R264 (vs. gap) binding
- G323 (= G291) binding
- S325 (≠ K293) binding
- Q329 (= Q297) binding
- E332 (= E300) binding
- N333 (= N301) 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)
35% identity, 92% coverage: 3:320/346 of query aligns to 39:354/367 of P62482
- Y90 (= Y62) mutation to F: No detectable phenotype.
- S112 (≠ N84) modified: Phosphoserine
Sites not aligning to the query:
- 20 modified: Phosphoserine
3eauA Voltage-dependent k+ channel beta subunit in complex with cortisone (see paper)
35% identity, 92% coverage: 3:320/346 of query aligns to 5:320/327 of 3eauA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G19), W23 (vs. gap), Q29 (= Q35), D51 (= D57), Y56 (= Y62), K84 (= K90), S154 (= S162), Q180 (= Q188), W209 (= W216), S210 (= S217), P211 (= P218), L212 (= L219), A213 (= A220), C214 (≠ G221), G215 (= G222), K220 (= K227), R230 (vs. gap), L287 (≠ I289), L288 (≠ I290), G289 (= G291), S291 (≠ K293), Q295 (= Q297), E298 (= E300), N299 (= N301)
- binding 17,21-dihydroxypregna-1,4-diene-3,11,20-trione: W23 (vs. gap), V55 (= V61), Y56 (= Y62), W87 (≠ G93), N124 (≠ H132), R155 (≠ N163), I174 (≠ A182), I177 (≠ A185), I202 (≠ E209)
1exbA Structure of the cytoplasmic beta subunit-t1 assembly of voltage- dependent k channels (see paper)
35% identity, 92% coverage: 3:320/346 of query aligns to 4:319/326 of 1exbA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), W22 (vs. gap), Q28 (= Q35), D50 (= D57), Y55 (= Y62), S153 (= S162), R154 (≠ N163), Q179 (= Q188), W208 (= W216), S209 (= S217), P210 (= P218), L211 (= L219), C213 (≠ G221), G214 (= G222), S217 (= S225), K219 (= K227), S228 (vs. gap), R229 (vs. gap), L286 (≠ I289), G288 (= G291), S290 (≠ K293), Q294 (= Q297), E297 (= E300), N298 (= N301)
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)
35% identity, 89% coverage: 1:308/346 of query aligns to 71:374/401 of P63144
- K152 (= K90) mutation to M: Loss of enzyme activity.
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)
34% identity, 89% coverage: 1:308/346 of query aligns to 89:392/419 of Q14722
- Y307 (= Y228) mutation to F: Reduces affinity for NADPH.
- R316 (= R240) mutation to E: Nearly abolishes NADPH binding.
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
33% identity, 93% coverage: 1:322/346 of query aligns to 1:310/310 of P46336
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
33% identity, 92% coverage: 5:322/346 of query aligns to 4:309/311 of 1pz0A
- active site: D52 (= D57), Y57 (= Y62), N91 (≠ A98), H124 (= H132)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H132), Q174 (= Q188), Y202 (≠ W216), F203 (≠ S217), P204 (= P218), L205 (= L219), S207 (≠ G221), G208 (= G222), A211 (≠ S225), K213 (= K227)
1lqaA Tas protein from escherichia coli in complex with NADPH (see paper)
32% identity, 92% coverage: 1:320/346 of query aligns to 1:337/346 of 1lqaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (= M21), D48 (= D57), Y53 (= Y62), H132 (= H132), N180 (= N163), Q205 (= Q188), Y233 (≠ W216), S234 (= S217), L236 (= L219), F238 (≠ G221), G239 (= G222), T242 (≠ S225), K244 (= K227), A254 (≠ G238), R255 (= R239), G308 (= G291), T310 (≠ K293), Q314 (= Q297), N318 (= N301)
P0A9T4 Protein tas from Escherichia coli (strain K12) (see paper)
32% identity, 92% coverage: 1:320/346 of query aligns to 1:337/346 of P0A9T4
- 234:244 (vs. 217:227, 55% identical) binding
Q3L181 Perakine reductase; EC 1.1.1.317 from Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) (see paper)
32% identity, 92% coverage: 1:320/346 of query aligns to 1:309/337 of Q3L181
- D52 (= D57) mutation to A: 99% loss of activity.
- Y57 (= Y62) mutation to A: 99% loss of activity.
- K84 (= K90) mutation to A: Total loss of activity.
- H126 (= H132) mutation to A: 98% loss of activity.
P77256 NADH-specific methylglyoxal reductase; AKR11B2; EC 1.1.1.- from Escherichia coli (strain K12) (see paper)
36% identity, 94% coverage: 1:326/346 of query aligns to 1:319/326 of P77256
- D232 (= D231) 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.
4aubB The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
32% identity, 92% coverage: 1:318/346 of query aligns to 11:318/335 of 4aubB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (= W30), D59 (= D57), Y64 (= Y62), H136 (= H132), Q191 (= Q188), F220 (≠ W216), T221 (≠ S217), P222 (= P218), L223 (= L219), Q225 (≠ G221), G226 (= G222), K231 (= K227), R241 (≠ G237), R244 (= R240), L288 (≠ I289), G290 (= G291), S292 (≠ K293), Q296 (= Q297), E299 (= E300), N300 (= N301)
Sites not aligning to the query:
6kiyA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor epalrestat (see paper)
34% identity, 92% coverage: 1:320/346 of query aligns to 2:274/275 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 (= Y62), W87 (≠ F92), H118 (= H132), R204 (≠ G221)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), T21 (= T20), W22 (≠ M21), Y59 (= Y62), H118 (= H132), N149 (= N163), Q170 (= Q188), Y199 (≠ W216), S200 (= S217), P201 (= P218), L202 (= L219), R204 (≠ G221), T205 (≠ G222), Y227 (≠ A272), I243 (= I289), P244 (≠ I290), K245 (≠ G291), G247 (≠ K293), R248 (= R294), H251 (≠ Q297), E254 (= E300), N255 (= N301)
Query Sequence
>BWI76_RS09015 FitnessBrowser__Koxy:BWI76_RS09015
MRYQKLGHTGLFVSELCLGTMTFGGEGGLWGKVGQLRQAEAEQLVGSALDAGINFIDTAN
VYSEGRSEEITGQALKNLKVPRENVVVATKVFGETGTAGVNSRGSSRYHIIGSVKESLRR
LQLDHIDLYQLHGFDPATPIEETLYALDNLVQHGHVRYIGVSNWAAWQIVKALGISERLG
LARFASLQAYYTIAGRDLERELAPMMQSEGLGLMVWSPLAGGLLSGKYDRDGQSASGGRR
QEFDFPPVNKARAFDCIDVMREIADAKGVSVAQIALAWLLHQPAVSSVIIGAKRAEQLAE
NLAATSIVLSGDELARLDAVSALPREYPGWMLERQGEYRRDQLAQQ
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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