SitesBLAST
Comparing Ga0059261_0885 FitnessBrowser__Korea:Ga0059261_0885 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)
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
37% identity, 92% coverage: 1:316/344 of query aligns to 1:313/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ A21), D49 (= D57), Y54 (= Y62), S151 (= S158), Y204 (≠ W212), F205 (≠ S213), L207 (= L215), Q209 (≠ W217), G210 (= G218), T213 (= T221), K215 (= K223), R227 (= R235), V284 (≠ I287), G286 (= G289), Q292 (= Q295), N296 (= N299)
6ow0B Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
35% identity, 92% coverage: 1:316/344 of query aligns to 1:289/301 of 6ow0B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ A21), Y50 (= Y62), H117 (= H128), S147 (= S158), Y200 (≠ W212), F201 (≠ S213), L203 (= L215), Q205 (≠ W217), T209 (= T221), Q268 (= Q295), N272 (= N299)
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)
34% identity, 96% coverage: 1:331/344 of query aligns to 71:400/401 of P63144
- K152 (= K87) mutation to M: Loss of enzyme activity.
8hw0A The structure of akr6d1
34% identity, 96% coverage: 1:331/344 of query aligns to 1:328/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (vs. gap), Q27 (≠ T26), D49 (= D57), Y54 (= Y62), R123 (≠ A129), S152 (= S158), Q178 (= Q184), W207 (= W212), S208 (= S213), P209 (= P214), L210 (= L215), S212 (≠ W217), K218 (= K223), S227 (= S234), R228 (= R235), I285 (= I287), G287 (= G289), S289 (≠ R291), Q293 (= Q295), D296 (≠ Q298), N297 (= N299)
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)
33% identity, 96% coverage: 1:331/344 of query aligns to 89:418/419 of Q14722
- Y307 (≠ I224) mutation to F: Reduces affinity for NADPH.
- R316 (≠ G233) mutation to E: Nearly abolishes NADPH binding.
6hg6A Clostridium beijerinckii aldo-keto reductase cbei_3974 with NADPH (see paper)
33% identity, 93% coverage: 1:319/344 of query aligns to 12:311/313 of 6hg6A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G30 (= G19), W32 (≠ F30), D60 (= D57), Y65 (= Y62), H137 (= H128), Q192 (= Q184), F221 (≠ W212), S222 (= S213), P223 (= P214), L224 (= L215), L278 (≠ I287), I279 (= I288), G280 (= G289), Q286 (= Q295), E289 (≠ Q298), N290 (= N299)
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, 88% coverage: 3:303/344 of query aligns to 39:337/367 of P62483
- T56 (≠ A20) binding
- W57 (vs. gap) binding
- Q63 (≠ T26) binding
- D85 (= D57) binding
- Y90 (= Y62) mutation to F: Abolishes enzyme activity, but has no effect on NADPH binding.
- S112 (≠ Q81) modified: Phosphoserine
- N158 (≠ H128) binding
- S188 (= S158) binding
- R189 (≠ N159) binding
- Q214 (= Q184) binding
- W243 (= W212) binding
- S244 (= S213) binding
- P245 (= P214) binding
- L246 (= L215) binding
- A247 (≠ G216) binding
- C248 (≠ W217) binding
- K254 (= K223) binding
- Y262 (≠ P231) binding
- R264 (≠ G233) binding
- G323 (= G289) binding
- S325 (≠ R291) binding
- Q329 (= Q295) binding
- E332 (≠ Q298) binding
- N333 (= N299) 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, 88% coverage: 3:303/344 of query aligns to 39:337/367 of P62482
- Y90 (= Y62) mutation to F: No detectable phenotype.
- S112 (≠ Q81) 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)
35% identity, 88% coverage: 3:303/344 of query aligns to 4:302/326 of 1exbA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), W22 (vs. gap), Q28 (≠ T26), D50 (= D57), Y55 (= Y62), S153 (= S158), R154 (≠ N159), Q179 (= Q184), W208 (= W212), S209 (= S213), P210 (= P214), L211 (= L215), C213 (≠ W217), G214 (= G218), S217 (≠ T221), K219 (= K223), S228 (≠ A232), R229 (≠ G233), L286 (≠ I287), G288 (= G289), S290 (≠ R291), Q294 (= Q295), E297 (≠ Q298), N298 (= N299)
3eauA Voltage-dependent k+ channel beta subunit in complex with cortisone (see paper)
35% identity, 88% coverage: 3:303/344 of query aligns to 5:303/327 of 3eauA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G19), W23 (vs. gap), Q29 (≠ T26), D51 (= D57), Y56 (= Y62), K84 (= K87), S154 (= S158), Q180 (= Q184), W209 (= W212), S210 (= S213), P211 (= P214), L212 (= L215), A213 (≠ G216), C214 (≠ W217), G215 (= G218), K220 (= K223), R230 (≠ G233), L287 (≠ I287), L288 (≠ I288), G289 (= G289), S291 (≠ R291), Q295 (= Q295), E298 (≠ Q298), N299 (= N299)
- binding 17,21-dihydroxypregna-1,4-diene-3,11,20-trione: W23 (vs. gap), V55 (= V61), Y56 (= Y62), W87 (≠ L90), N124 (≠ H128), R155 (≠ N159), I174 (≠ P178), I177 (≠ V181), I202 (≠ Q205)
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)
33% identity, 96% coverage: 3:331/344 of query aligns to 39:366/367 of Q13303
- T56 (≠ A20) binding
- W57 (vs. gap) binding
- Q63 (≠ T26) binding
- D85 (= D57) binding
- Y90 (= Y62) mutation to F: No effect on its activity in promoting KCNA4 channel closure.
- S112 (≠ Q81) modified: Phosphoserine
- S188 (= S158) binding
- R189 (≠ N159) binding
- Q214 (= Q184) binding
- W243 (= W212) binding
- S244 (= S213) binding
- P245 (= P214) binding
- L246 (= L215) binding
- A247 (≠ G216) binding
- C248 (≠ W217) binding
- K254 (= K223) binding
- R264 (≠ G233) binding
- S325 (≠ R291) binding
- Q329 (= Q295) binding
- E332 (≠ Q298) binding
- N333 (= N299) 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)
34% identity, 88% coverage: 3:303/344 of query aligns to 6:304/328 of 7wf3C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), R156 (≠ N159), W210 (= W212), S211 (= S213), P212 (= P214), L213 (= L215), C215 (≠ W217), K221 (= K223), R231 (≠ G233), Q296 (= Q295), E299 (≠ Q298), N300 (= N299)
Q9P7U2 Putative aryl-alcohol dehydrogenase C977.14c; EC 1.1.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 95% coverage: 3:329/344 of query aligns to 9:346/351 of Q9P7U2
- S113 (vs. gap) modified: Phosphoserine
4aubB The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
33% identity, 92% coverage: 1:316/344 of query aligns to 11:318/335 of 4aubB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (≠ F30), D59 (= D57), Y64 (= Y62), H136 (= H128), Q191 (= Q184), F220 (≠ W212), T221 (≠ S213), P222 (= P214), L223 (= L215), Q225 (≠ W217), G226 (= G218), K231 (= K223), R241 (= R235), R244 (≠ A243), L288 (≠ I287), G290 (= G289), S292 (≠ R291), Q296 (= Q295), E299 (≠ Q298), N300 (= N299)
Sites not aligning to the query:
P80874 Aldo-keto reductase YhdN; AKR11B; General stress protein 69; GSP69; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
33% identity, 90% coverage: 1:310/344 of query aligns to 1:301/331 of P80874
5t79A X-ray crystal structure of a novel aldo-keto reductases for the biocatalytic conversion of 3-hydroxybutanal to 1,3-butanediol (see paper)
35% identity, 94% coverage: 1:322/344 of query aligns to 13:312/315 of 5t79A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G31 (= G19), W33 (≠ F30), Y66 (= Y62), H138 (= H128), N169 (= N159), Q193 (= Q184), F221 (≠ W212), S222 (= S213), L224 (= L215), G226 (≠ W217), T230 (= T221), R232 (≠ K223), S263 (≠ P270), L280 (≠ I287), G282 (= G289), S284 (≠ R291), Q288 (= Q295)
1pz1A Structure of NADPH-dependent family 11 aldo-keto reductase akr11b(holo) (see paper)
32% identity, 90% coverage: 1:310/344 of query aligns to 1:301/333 of 1pz1A
- active site: D52 (= D57), Y57 (= Y62), K90 (≠ G93), Q93 (≠ P96), H125 (= H128)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (≠ A21), Q175 (= Q184), Y203 (≠ W212), G204 (≠ S213), L206 (= L215), R208 (≠ W217), K214 (= K223), G280 (= G289), R282 (= R291), Q286 (= Q295)
3erpA Structure of idp01002, a putative oxidoreductase from and essential gene of salmonella typhimurium (see paper)
34% identity, 94% coverage: 1:322/344 of query aligns to 12:307/312 of 3erpA
3n6qD Crystal structure of yghz from e. Coli (see paper)
32% identity, 92% coverage: 1:316/344 of query aligns to 12:305/315 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: 1:316/344 of query aligns to 1:306/310 of P46336
Query Sequence
>Ga0059261_0885 FitnessBrowser__Korea:Ga0059261_0885
MEYRQLGASGLRVPVLSFGAATFGGTGPLFSAWGTSDAAEARRLVDICLDAGVNLFDTAD
VYSNGASEEVLAEAIKGRRDQVLISTKTGLPLGDGPADWGVSRSRLIAAVDASLKRLGTD
HIDILQLHAFDAHTPVEELLATLDTLVAQGKVRHTGVSNYPGWQLMKALAAADRHGWPRF
VAHQVYYSLIGRAYEADLMPLAADQGIGALVWSPLGWGRLTGKIGRNRPVPAGSRLHDTE
QFAPPVSEEHLYKVIDALEAVAEETGKTVPQVAINWLLQRPTVSSVIIGARNEEQLRQNL
GAVGWSLTREQVAALDAASDVLPPYPHTPYRQQEGFARLNPAIV
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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