SitesBLAST
Comparing RR42_RS32140 FitnessBrowser__Cup4G11:RR42_RS32140 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
48% identity, 97% coverage: 11:492/496 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N171), K188 (= K194), E263 (= E268), C297 (= C302), E394 (= E400), E471 (= E477)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I167), P163 (= P169), K188 (= K194), A190 (= A196), E191 (= E197), Q192 (≠ E198), G221 (= G227), G225 (= G230), G241 (= G246), S242 (= S247), T245 (≠ V250), L264 (= L269), C297 (= C302), E394 (= E400), F396 (= F402)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
48% identity, 97% coverage: 11:492/496 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N171), K188 (= K194), E263 (= E268), C297 (= C302), E394 (= E400), E471 (= E477)
- binding nicotinamide-adenine-dinucleotide: I161 (= I167), I162 (≠ V168), P163 (= P169), W164 (= W170), K188 (= K194), E191 (= E197), G221 (= G227), G225 (= G230), A226 (= A231), F239 (= F244), G241 (= G246), S242 (= S247), T245 (≠ V250), Y248 (≠ L253), L264 (= L269), C297 (= C302), Q344 (≠ H349), R347 (≠ K352), E394 (= E400), F396 (= F402)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
46% identity, 96% coverage: 19:494/496 of query aligns to 40:511/518 of O94788
- E50 (= E29) to G: in dbSNP:rs34266719
- A110 (= A88) to V: in dbSNP:rs35365164
- Q182 (≠ A166) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 168:170) binding
- KPAE 210:213 (= KPAE 194:197) binding
- STE 264:266 (= STE 247:249) binding
- C320 (= C302) active site, Nucleophile
- R347 (≠ T329) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (= V330) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RHRDK 348:352) binding
- A383 (= A365) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E400) binding
- E436 (≠ A419) to K: in dbSNP:rs34744827
- S461 (≠ V444) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
46% identity, 96% coverage: 19:494/496 of query aligns to 14:485/492 of 6b5hA
- active site: N161 (= N171), E260 (= E268), C294 (= C302), E468 (= E477)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ L116), G116 (= G120), F162 (= F172), W169 (= W179), Q284 (≠ G292), F288 (≠ L296), T295 (= T303), N449 (= N458), L451 (≠ V460), N452 (≠ D461), F457 (= F466)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ V168), W160 (= W170), N161 (= N171), K184 (= K194), G217 (= G227), G221 (= G230), F235 (= F244), T236 (= T245), G237 (= G246), S238 (= S247), V241 (= V250), E260 (= E268), L261 (= L269), C294 (= C302), F393 (= F402)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
46% identity, 96% coverage: 19:494/496 of query aligns to 14:485/492 of 6b5gA
- active site: N161 (= N171), E260 (= E268), C294 (= C302), E468 (= E477)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F172), L165 (= L175), W169 (= W179), F288 (≠ L296), C293 (≠ V301), C294 (= C302), T295 (= T303), N449 (= N458), L451 (≠ V460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ V168), P159 (= P169), W160 (= W170), N161 (= N171), M166 (= M176), K184 (= K194), E187 (= E197), G217 (= G227), G221 (= G230), F235 (= F244), T236 (= T245), G237 (= G246), S238 (= S247), V241 (= V250), E260 (= E268), L261 (= L269), C294 (= C302), E391 (= E400), F393 (= F402)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
46% identity, 96% coverage: 19:494/496 of query aligns to 14:485/492 of 6aljA
- active site: N161 (= N171), E260 (= E268), C294 (= C302), E468 (= E477)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G120), F162 (= F172), L165 (= L175), M166 (= M176), W169 (= W179), E260 (= E268), C293 (≠ V301), C294 (= C302), L451 (≠ V460), N452 (≠ D461), A453 (≠ P462)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ V168), P159 (= P169), W160 (= W170), N161 (= N171), K184 (= K194), E187 (= E197), G217 (= G227), G221 (= G230), F235 (= F244), G237 (= G246), S238 (= S247), V241 (= V250), Q341 (≠ H349), K344 (= K352), E391 (= E400), F393 (= F402)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
45% identity, 96% coverage: 19:494/496 of query aligns to 40:511/518 of Q63639
P51977 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Ovis aries (Sheep) (see 2 papers)
46% identity, 97% coverage: 13:494/496 of query aligns to 17:494/501 of P51977
5ac0A Ovis aries aldehyde dehydrogenase 1a1 in complex with a duocarmycin analog (see paper)
46% identity, 97% coverage: 13:494/496 of query aligns to 10:487/494 of 5ac0A
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one: M114 (≠ L116), F164 (= F172), W171 (= W179), Y290 (≠ L296), C295 (≠ V301), C296 (= C302)
- binding nicotinamide-adenine-dinucleotide: I159 (= I167), I160 (≠ V168), P161 (= P169), W162 (= W170), K186 (= K194), E189 (= E197), G219 (= G227), G223 (= G230), A224 (= A231), F237 (= F244), G239 (= G246), S240 (= S247), V243 (= V250), G264 (= G270), C296 (= C302), Q343 (≠ H349), K346 (= K352), E393 (= E400)
5abmA Sheep aldehyde dehydrogenase 1a1 (see paper)
46% identity, 97% coverage: 13:494/496 of query aligns to 10:487/494 of 5abmA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I159 (= I167), I160 (≠ V168), P161 (= P169), W162 (= W170), K186 (= K194), E189 (= E197), G219 (= G227), G223 (= G230), F237 (= F244), G239 (= G246), S240 (= S247), V243 (= V250), G264 (= G270), Q343 (≠ H349), K346 (= K352), E393 (= E400), F395 (= F402)
1bxsA Sheep liver class 1 aldehyde dehydrogenase with NAD bound (see paper)
46% identity, 97% coverage: 13:494/496 of query aligns to 10:487/494 of 1bxsA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding nicotinamide-adenine-dinucleotide: I159 (= I167), I160 (≠ V168), P161 (= P169), W162 (= W170), K186 (= K194), E189 (= E197), G219 (= G227), G223 (= G230), F237 (= F244), G239 (= G246), S240 (= S247), V243 (= V250), L263 (= L269), C296 (= C302), Q343 (≠ H349), K346 (= K352), E393 (= E400), F395 (= F402)
P15437 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Equus caballus (Horse) (see paper)
46% identity, 96% coverage: 19:492/496 of query aligns to 23:492/501 of P15437
Sites not aligning to the query:
- 2 modified: N-acetylserine
5teiA Structure of human aldh1a1 with inhibitor cm039
45% identity, 96% coverage: 19:492/496 of query aligns to 15:484/493 of 5teiA
- active site: N162 (= N171), K185 (= K194), E261 (= E268), C295 (= C302), E392 (= E400), E469 (= E477)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-5-(2-methylphenyl)-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: S113 (≠ L116), F163 (= F172), H285 (≠ G292), G286 (≠ A293), Y289 (≠ L296), C295 (= C302), G450 (≠ N458), V452 (= V460), F458 (= F466)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I167), I159 (≠ V168), P160 (= P169), W161 (= W170), N162 (= N171), K185 (= K194), E188 (= E197), G218 (= G227), G222 (= G230), A223 (= A231), F236 (= F244), T237 (= T245), G238 (= G246), S239 (= S247), V242 (= V250), C295 (= C302), Q342 (≠ H349), K345 (= K352), E392 (= E400), F394 (= F402)
4x4lA Structure of human aldh1a1 with inhibitor cm037 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 15:484/493 of 4x4lA
- active site: N162 (= N171), K185 (= K194), E261 (= E268), C295 (= C302), E392 (= E400), E469 (= E477)
- binding ethyl ({4-oxo-3-[3-(pyrrolidin-1-yl)propyl]-3,4-dihydro[1]benzothieno[3,2-d]pyrimidin-2-yl}sulfanyl)acetate: S113 (≠ L116), M167 (= M176), W170 (= W179), Y289 (≠ L296), G450 (≠ N458), F458 (= F466)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I167), I159 (≠ V168), P160 (= P169), W161 (= W170), K185 (= K194), E188 (= E197), G218 (= G227), G222 (= G230), F236 (= F244), T237 (= T245), G238 (= G246), S239 (= S247), V242 (= V250), C295 (= C302), Q342 (≠ H349), K345 (= K352), E392 (= E400), F394 (= F402)
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 7jwwA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G120), T122 (≠ W124), F164 (= F172), M168 (= M176), Y290 (≠ L296), C295 (≠ V301), C296 (= C302), I297 (≠ T303), V453 (= V460), F459 (= F466)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 7jwvA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G120), T122 (≠ W124), F164 (= F172), M168 (= M176), Y290 (≠ L296), C295 (≠ V301), I297 (≠ T303), V453 (= V460), F459 (= F466)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 7jwuA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding nicotinamide-adenine-dinucleotide: I159 (= I167), I160 (≠ V168), P161 (= P169), W162 (= W170), N163 (= N171), K186 (= K194), E189 (= E197), G219 (= G227), G223 (= G230), A224 (= A231), F237 (= F244), T238 (= T245), G239 (= G246), S240 (= S247), V243 (= V250), L263 (= L269), C296 (= C302), Q343 (≠ H349), K346 (= K352), E393 (= E400), F395 (= F402)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-(pyridin-2-yl)ethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: T122 (≠ W124), F164 (= F172), W171 (= W179), Y290 (≠ L296), C295 (≠ V301), I297 (≠ T303), V453 (= V460), F459 (= F466)
7jwtA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 7jwtA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 6-{[(1R)-1-(3-hydroxyphenyl)ethyl]sulfanyl}-1-methyl-5-phenyl-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G120), T122 (≠ W124), F164 (= F172), M168 (= M176), W171 (= W179), Y290 (≠ L296), C295 (≠ V301), V453 (= V460), F459 (= F466)
7jwsA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 7jwsA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G120), T122 (≠ W124), F164 (= F172), M168 (= M176), W171 (= W179), Y290 (≠ L296), C295 (≠ V301), I297 (≠ T303), V453 (= V460), F459 (= F466)
6dumA Aldh1a1 n121s in complex with 6-{[(3-fluorophenyl)methyl]sulfanyl}-2- (oxetan-3-yl)-5-phenyl-2,5-dihydro-4h-pyrazolo[3,4-d]pyrimidin-4-one (compound 13g) (see paper)
45% identity, 96% coverage: 19:492/496 of query aligns to 16:485/494 of 6dumA
- active site: N163 (= N171), K186 (= K194), E262 (= E268), C296 (= C302), E393 (= E400), E470 (= E477)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-2-(oxetan-3-yl)-5-phenyl-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G120), T122 (≠ W124), F164 (= F172), M168 (= M176), W171 (= W179), H286 (≠ G292), Y290 (≠ L296), C295 (≠ V301), C296 (= C302), I297 (≠ T303), G451 (≠ N458), V453 (= V460), F459 (= F466)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I167), I160 (≠ V168), P161 (= P169), W162 (= W170), N163 (= N171), K186 (= K194), E189 (= E197), G219 (= G227), P220 (vs. gap), G223 (= G230), A224 (= A231), F237 (= F244), T238 (= T245), G239 (= G246), S240 (= S247), V243 (= V250), L263 (= L269), C296 (= C302), Q343 (≠ H349), K346 (= K352), E393 (= E400), F395 (= F402)
Query Sequence
>RR42_RS32140 FitnessBrowser__Cup4G11:RR42_RS32140
MNAPKEARSGLNQAIRNAMLIDGEWRQAESGETFAVFDPATGEEIARVPAGGAADIDAAV
AAAGRAFAGGTWRAMMPAQRERLLLKLADLVEQHGDELARLETLNNGKLLAFSQGLEVGG
SAQWLRYMAGWATKIEGSTLDVSVPFPPGTRYSAMTRRSPVGVVGAIVPWNFPLLMAVWK
IAPALACGCTVVLKPAEETPLTALRLAELALEAGFPPGVLNVVTGDGVPGAALVAHPGVN
KITFTGSTEVGRLIGARCGQDIRRVSLELGGKSPVIVLDDCDPAHAIQGAAGAIFLNQGQ
VCTAGSRLYVARRHYDQVVEGLGKVANATVLGSGLDPASQMGPLVSSRHRDKVMGLIGTG
RSEGADIVAGGTALDRPGYFVRPTVVANAACKDLTLVREEVFGPVVVAMPFDDPEAVLAE
ANRSEYGLGASIWSNDLRAVQRLVDGLDAGTVWVNTHNIVDPNMPFGGYKASGVGREHGR
SAIEAYTEIKSVCMAY
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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