SitesBLAST
Comparing 3607117 FitnessBrowser__Dino:3607117 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
32% identity, 96% coverage: 7:307/312 of query aligns to 8:329/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), W21 (vs. gap), Q27 (≠ T25), D49 (= D47), Y54 (= Y52), R123 (= R112), S152 (= S141), Q178 (= Q166), W207 (≠ Y194), S208 (= S195), P209 (= P196), L210 (= L197), S212 (≠ G199), K218 (= K205), S227 (≠ G212), R228 (= R213), I285 (= I265), G287 (≠ S267), S289 (≠ R269), Q293 (= Q273), D296 (≠ A276), N297 (≠ S277)
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
32% identity, 92% coverage: 7:293/312 of query aligns to 8:312/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), L21 (≠ M20), D49 (= D47), Y54 (= Y52), S151 (= S141), Y204 (= Y194), F205 (≠ S195), L207 (= L197), Q209 (≠ G199), G210 (= G200), T213 (= T203), K215 (= K205), R227 (= R213), V284 (≠ I265), G286 (≠ S267), Q292 (= Q273), N296 (≠ S277)
1lqaA Tas protein from escherichia coli in complex with NADPH (see paper)
31% identity, 94% coverage: 7:298/312 of query aligns to 8:339/346 of 1lqaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), M21 (= M20), D48 (= D47), Y53 (= Y52), H132 (= H111), N180 (= N142), Q205 (= Q166), Y233 (= Y194), S234 (= S195), L236 (= L197), F238 (≠ G199), G239 (= G200), T242 (= T203), K244 (= K205), A254 (≠ T215), R255 (≠ E216), G308 (≠ S267), T310 (≠ R269), Q314 (= Q273), N318 (≠ S277)
P0A9T4 Protein tas from Escherichia coli (strain K12) (see paper)
31% identity, 94% coverage: 7:298/312 of query aligns to 8:339/346 of P0A9T4
- 234:244 (vs. 195:205, 73% identical) binding
6ow0B Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
32% identity, 92% coverage: 7:293/312 of query aligns to 8:288/301 of 6ow0B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), L21 (≠ M20), Y50 (= Y52), H117 (= H111), S147 (= S141), Y200 (= Y194), F201 (≠ S195), L203 (= L197), Q205 (≠ G199), T209 (= T203), Q268 (= Q273), N272 (≠ S277)
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
31% identity, 82% coverage: 36:291/312 of query aligns to 43:310/310 of P46336
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
31% identity, 82% coverage: 36:291/312 of query aligns to 42:309/311 of 1pz0A
- active site: D52 (= D47), Y57 (= Y52), N91 (vs. gap), H124 (= H111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H111), Q174 (= Q166), Y202 (= Y194), F203 (≠ S195), P204 (= P196), L205 (= L197), S207 (≠ G199), G208 (= G200), A211 (≠ T203), K213 (= K205)
3erpA Structure of idp01002, a putative oxidoreductase from and essential gene of salmonella typhimurium (see paper)
32% identity, 86% coverage: 7:275/312 of query aligns to 19:285/312 of 3erpA
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, 86% coverage: 7:275/312 of query aligns to 20:290/315 of 5t79A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G31 (= G18), W33 (≠ M20), Y66 (= Y52), H138 (= H111), N169 (= N142), Q193 (= Q166), F221 (≠ Y194), S222 (= S195), L224 (= L197), G226 (= G199), T230 (= T203), R232 (≠ K205), S263 (≠ A248), L280 (≠ I265), G282 (≠ S267), S284 (≠ R269), Q288 (= Q273)
O95154 Aflatoxin B1 aldehyde reductase member 3; AFB1 aldehyde reductase 2; AFB1-AR 2; EC 1.-.-.- from Homo sapiens (Human) (see 3 papers)
34% identity, 87% coverage: 11:280/312 of query aligns to 10:301/331 of O95154
- D44 (= D47) binding
- V138 (≠ R136) to M: in dbSNP:rs2231198
- SN 143:144 (= SN 141:142) binding
- 198:208 (vs. 195:205, 82% identical) binding
- N215 (vs. gap) to D: in dbSNP:rs1738023
- R222 (= R213) binding
- 290:298 (vs. 269:277, 22% identical) binding
Sites not aligning to the query:
- 323 T → A: in dbSNP:rs1738025
2clpG Crystal structure of human aflatoxin b1 aldehyde reductase member 3
34% identity, 87% coverage: 11:280/312 of query aligns to 2:293/323 of 2clpG
- active site: D36 (= D47), Y41 (= Y52), P72 (≠ G79), H105 (= H111)
- binding calcium ion: H232 (≠ M229), E235 (≠ A232)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G18), M9 (= M20), D36 (= D47), Y41 (= Y52), H105 (= H111), S135 (= S141), N136 (= N142), Q161 (= Q166), F189 (≠ Y194), N190 (≠ S195), P191 (= P196), L192 (= L197), A193 (≠ G198), G194 (= G199), G195 (= G200), T198 (= T203), K200 (= K205), R214 (= R213), I278 (= I265), G280 (≠ S267), M281 (≠ A268), S282 (≠ R269), Q286 (= Q273), Q289 (≠ A276), N290 (≠ S277)
2clpA Crystal structure of human aflatoxin b1 aldehyde reductase member 3
34% identity, 87% coverage: 11:280/312 of query aligns to 2:293/323 of 2clpA
- active site: D36 (= D47), Y41 (= Y52), P72 (≠ G79), H105 (= H111)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G18), M9 (= M20), D36 (= D47), Y41 (= Y52), H105 (= H111), N136 (= N142), F189 (≠ Y194), N190 (≠ S195), P191 (= P196), L192 (= L197), A193 (≠ G198), G194 (= G199), G195 (= G200), T198 (= T203), K200 (= K205), R214 (= R213), I278 (= I265), G280 (≠ S267), S282 (≠ R269), Q286 (= Q273), Q289 (≠ A276), N290 (≠ S277)
1pz1A Structure of NADPH-dependent family 11 aldo-keto reductase akr11b(holo) (see paper)
31% identity, 86% coverage: 8:276/312 of query aligns to 9:289/333 of 1pz1A
- active site: D52 (= D47), Y57 (= Y52), K90 (vs. gap), Q93 (vs. gap), H125 (= H111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), W21 (≠ M20), Q175 (= Q166), Y203 (= Y194), G204 (≠ S195), L206 (= L197), R208 (≠ G199), K214 (= K205), G280 (≠ S267), R282 (= R269), Q286 (= Q273)
P80874 Aldo-keto reductase YhdN; AKR11B; General stress protein 69; GSP69; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
31% identity, 86% coverage: 8:276/312 of query aligns to 9:289/331 of P80874
Q3L181 Perakine reductase; EC 1.1.1.317 from Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) (see paper)
29% identity, 89% coverage: 9:285/312 of query aligns to 10:297/337 of Q3L181
- D52 (= D47) mutation to A: 99% loss of activity.
- Y57 (= Y52) mutation to A: 99% loss of activity.
- K84 (= K77) mutation to A: Total loss of activity.
- H126 (= H111) mutation to A: 98% loss of activity.
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)
29% identity, 88% coverage: 7:280/312 of query aligns to 78:370/401 of P63144
- K152 (= K77) 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)
29% identity, 88% coverage: 7:280/312 of query aligns to 96:388/419 of Q14722
- Y307 (= Y206) mutation to F: Reduces affinity for NADPH.
- R316 (≠ K219) mutation to E: Nearly abolishes NADPH binding.
3v0sA Crystal structure of perakine reductase, founder member of a novel akr subfamily with unique conformational changes during NADPH binding (see paper)
29% identity, 94% coverage: 8:301/312 of query aligns to 9:286/287 of 3v0sA
- active site: D45 (= D47), Y50 (= Y52), G87 (= G85), H119 (= H111)
- binding 2'-monophosphoadenosine-5'-diphosphate: S198 (= S195), P199 (= P196), I200 (≠ L197), G201 (= G198), L204 (= L201), P246 (≠ I266), G247 (≠ S267), T248 (≠ A268), T249 (≠ R269), N253 (≠ Q273), N256 (≠ A276), N257 (≠ S277)
P38918 Aflatoxin B1 aldehyde reductase member 3; AFB1-AR; Aflatoxin B1 aldehyde reductase member 1; rAFAR1; EC 1.-.-.- from Rattus norvegicus (Rat) (see paper)
32% identity, 86% coverage: 11:279/312 of query aligns to 6:296/327 of P38918
- D40 (= D47) binding
- H109 (= H111) binding
- SN 139:140 (= SN 141:142) binding
- Q165 (= Q166) binding
- 194:204 (vs. 195:205, 73% identical) binding
- R218 (≠ E218) binding
- Y228 (≠ W228) binding
- R231 (vs. gap) binding
- 286:294 (vs. 269:277, 22% identical) binding
Sites not aligning to the query:
1gveA Aflatoxin aldehyde reductase (akr7a1) from rat liver (see paper)
32% identity, 86% coverage: 11:279/312 of query aligns to 3:293/324 of 1gveA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G18), M10 (= M20), R15 (≠ T25), D37 (= D47), Y42 (= Y52), Q162 (= Q166), F190 (≠ Y194), N191 (≠ S195), P192 (= P196), L193 (= L197), G195 (= G199), G196 (= G200), R201 (≠ K205), S214 (≠ N217), R215 (≠ E218), I257 (≠ L250), I279 (= I265), L280 (≠ I266), G281 (≠ S267), S283 (≠ R269), Q287 (= Q273), Q290 (≠ A276), N291 (≠ S277)
Query Sequence
>3607117 FitnessBrowser__Dino:3607117
MTQLTTRSGAPASSLCFGCMQFGGTADKPASAAMFEACRAAGINFFDTAHVYTEGRSETW
LGEMVTDQADDLLIATKVGYVGGSGRANIRTTFDESLRRLGLDAVDILYLHRWDAETPLE
ETFEALADLQSAGRFRYIGVSNFAAWQVMKAQAVAEQFGTRIDILQPMYSLIKRQAEVEI
LPMALSEGIAVAPYSPLGGGLLTGKYAEGGTGRLTENEKYEMRYSMPWMHEAAVALRVLA
AEIGAAPATLAVAWAAAHPGVKAPIISARDVAQLDASLAARDMALPPDLYARITALSQTP
PPATDRLEEALS
Or try a new SitesBLAST search
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