SitesBLAST
Comparing 7026237 FitnessBrowser__ANA3:7026237 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)
1lqaA Tas protein from escherichia coli in complex with NADPH (see paper)
57% identity, 100% coverage: 1:346/346 of query aligns to 1:346/346 of 1lqaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (= M21), D48 (= D48), Y53 (= Y53), H132 (= H131), N180 (= N179), Q205 (= Q204), Y233 (= Y232), S234 (= S233), L236 (= L235), F238 (= F237), G239 (= G238), T242 (≠ S241), K244 (= K243), A254 (= A253), R255 (= R254), G308 (= G308), T310 (= T310), Q314 (= Q314), N318 (= N318)
P0A9T4 Protein tas from Escherichia coli (strain K12) (see paper)
57% identity, 100% coverage: 1:346/346 of query aligns to 1:346/346 of P0A9T4
- 234:244 (vs. 233:243, 64% identical) binding
8hw0A The structure of akr6d1
30% identity, 97% coverage: 1:337/346 of query aligns to 1:318/329 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 (≠ Y232), S208 (= S233), P209 (= P234), L210 (= L235), S212 (≠ F237), K218 (= K243), S227 (≠ A253), R228 (= R254), I285 (= I306), G287 (= G308), S289 (≠ T310), Q293 (= Q314), D296 (≠ E317), N297 (= N318)
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)
31% identity, 97% coverage: 3:337/346 of query aligns to 39:354/367 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 (≠ D81) modified: Phosphoserine
- S188 (= S178) binding
- R189 (≠ N179) binding
- Q214 (= Q204) binding
- W243 (≠ Y232) binding
- S244 (= S233) binding
- P245 (= P234) binding
- L246 (= L235) binding
- A247 (= A236) binding
- C248 (≠ F237) binding
- K254 (= K243) binding
- R264 (≠ G252) 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)
31% identity, 97% coverage: 3:337/346 of query aligns to 6:321/328 of 7wf3C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), R156 (≠ N179), W210 (≠ Y232), S211 (= S233), P212 (= P234), L213 (= L235), C215 (≠ F237), K221 (= K243), 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)
31% identity, 97% coverage: 3:337/346 of query aligns to 39:354/367 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 (≠ D81) modified: Phosphoserine
- N158 (≠ H131) binding
- S188 (= S178) binding
- R189 (≠ N179) binding
- Q214 (= Q204) binding
- W243 (≠ Y232) binding
- S244 (= S233) binding
- P245 (= P234) binding
- L246 (= L235) binding
- A247 (= A236) binding
- C248 (≠ F237) binding
- K254 (= K243) binding
- Y262 (vs. gap) binding
- R264 (≠ G252) 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)
31% identity, 97% coverage: 3:337/346 of query aligns to 39:354/367 of P62482
- Y90 (= Y53) mutation to F: No detectable phenotype.
- S112 (≠ D81) modified: Phosphoserine
Sites not aligning to the query:
- 20 modified: Phosphoserine
1exbA Structure of the cytoplasmic beta subunit-t1 assembly of voltage- dependent k channels (see paper)
31% identity, 97% coverage: 3:337/346 of query aligns to 4:319/326 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 (≠ Y232), S209 (= S233), P210 (= P234), L211 (= L235), C213 (≠ F237), G214 (= G238), S217 (= S241), K219 (= K243), S228 (≠ A253), R229 (= R254), L286 (≠ I306), G288 (= G308), S290 (≠ T310), Q294 (= Q314), E297 (= E317), N298 (= N318)
3eauA Voltage-dependent k+ channel beta subunit in complex with cortisone (see paper)
31% identity, 97% coverage: 3:337/346 of query aligns to 5:320/327 of 3eauA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G19), W23 (vs. gap), Q29 (= Q26), D51 (= D48), Y56 (= Y53), K84 (= K87), S154 (= S178), Q180 (= Q204), W209 (≠ Y232), S210 (= S233), P211 (= P234), L212 (= L235), A213 (= A236), C214 (≠ F237), G215 (= G238), K220 (= K243), 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 (≠ A90), N124 (≠ H131), R155 (≠ N179), I174 (≠ P198), I177 (≠ V201), I202 (≠ E225)
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
30% identity, 97% coverage: 1:337/346 of query aligns to 1:308/310 of P46336
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)
31% identity, 94% coverage: 1:324/346 of query aligns to 71:373/401 of P63144
- K152 (= K87) mutation to M: Loss of enzyme activity.
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
30% identity, 96% coverage: 5:337/346 of query aligns to 4:307/311 of 1pz0A
- active site: D52 (= D48), Y57 (= Y53), N91 (≠ S95), H124 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H131), Q174 (= Q204), Y202 (= Y232), F203 (≠ S233), P204 (= P234), L205 (= L235), S207 (≠ F237), G208 (= G238), A211 (≠ S241), K213 (= K243)
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)
31% identity, 94% coverage: 1:324/346 of query aligns to 89:391/419 of Q14722
- Y307 (= Y244) mutation to F: Reduces affinity for NADPH.
- R316 (= R254) mutation to E: Nearly abolishes NADPH binding.
P80874 Aldo-keto reductase YhdN; AKR11B; General stress protein 69; GSP69; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
31% identity, 87% coverage: 1:300/346 of query aligns to 1:283/331 of P80874
Sites not aligning to the query:
1pz1A Structure of NADPH-dependent family 11 aldo-keto reductase akr11b(holo) (see paper)
30% identity, 87% coverage: 1:300/346 of query aligns to 1:283/333 of 1pz1A
- active site: D52 (= D48), Y57 (= Y53), K90 (≠ N107), Q93 (vs. gap), H125 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (vs. gap), Q175 (= Q204), Y203 (= Y232), G204 (≠ S233), L206 (= L235), R208 (≠ F237), K214 (= K243), G280 (≠ N297), R282 (= R299)
Sites not aligning to the query:
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
27% identity, 97% coverage: 1:335/346 of query aligns to 1:313/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ M21), D49 (= D48), Y54 (= Y53), S151 (= S178), Y204 (= Y232), F205 (≠ S233), L207 (= L235), Q209 (≠ F237), G210 (= G238), T213 (≠ S241), K215 (= K243), R227 (vs. gap), V284 (≠ I306), G286 (= G308), Q292 (= Q314), N296 (= N318)
4aubB The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
28% identity, 93% coverage: 1:322/346 of query aligns to 11:304/335 of 4aubB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (≠ M21), D59 (= D48), Y64 (= Y53), H136 (= H131), Q191 (= Q204), F220 (≠ Y232), T221 (≠ S233), P222 (= P234), L223 (= L235), Q225 (≠ F237), G226 (= G238), K231 (= K243), R241 (= R254), R244 (≠ L257), L288 (≠ I306), G290 (= G308), S292 (≠ T310), Q296 (= Q314), E299 (= E317), N300 (= N318)
Sites not aligning to the query:
Q3L181 Perakine reductase; EC 1.1.1.317 from Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) (see paper)
25% identity, 97% coverage: 1:335/346 of query aligns to 1:306/337 of Q3L181
- D52 (= D48) mutation to A: 99% loss of activity.
- Y57 (= Y53) mutation to A: 99% loss of activity.
- K84 (= K87) mutation to A: Total loss of activity.
- H126 (= H131) mutation to A: 98% loss of activity.
Q9P7U2 Putative aryl-alcohol dehydrogenase C977.14c; EC 1.1.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 95% coverage: 3:329/346 of query aligns to 9:333/351 of Q9P7U2
- S113 (vs. gap) modified: Phosphoserine
3n6qD Crystal structure of yghz from e. Coli (see paper)
28% identity, 93% coverage: 1:322/346 of query aligns to 12:291/315 of 3n6qD
Query Sequence
>7026237 FitnessBrowser__ANA3:7026237
MEYRRIPHSNLEVSKICLGTMTWGEQNTQAEAFAQLDYAIGSGINFIDTAEMYPVPPKPE
TQGETERILGQYIKARGNRDDLVIATKIAAPGGKSDYIRKNMALDWNNIHQAVDASLERL
QIDTIDLYQVHWPDRNTNFFGELFYDEQEIEQQTPILETLEALAEVIRQGKVRYIGVSNE
TPWGLMKYLQLAEKHGLPRIVTVQNPYNLLNRSFEVGMSEISHREELPLLAYSPLAFGAL
SGKYCNNQWPEGARLTLFKRFARYTGSQMALDATAAYVDLAREFNLSPAQMALAFVNSRK
FVGSNIIGATDLYQLKENIDSLKVSLSPELLSRLNALSDQFRLPCP
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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