SitesBLAST
Comparing CCNA_03541 FitnessBrowser__Caulo:CCNA_03541 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)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
46% identity, 91% coverage: 13:267/279 of query aligns to 21:277/288 of 4gieA
- active site: D55 (= D46), Y60 (= Y51), K85 (= K76), H118 (= H109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G21), W31 (= W23), D55 (= D46), Y60 (= Y51), H118 (= H109), W119 (= W110), N148 (= N140), Q169 (= Q161), W195 (= W187), S196 (= S188), P197 (= P189), L198 (= L190), S200 (≠ Q192), L207 (vs. gap), A224 (≠ G213), I239 (= I228), P240 (= P229), K241 (≠ R230), S242 (≠ T231), R247 (= R236), E250 (= E239), N251 (= N240)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
46% identity, 91% coverage: 13:267/279 of query aligns to 10:266/277 of 4fziA
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
44% identity, 90% coverage: 10:259/279 of query aligns to 10:259/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
44% identity, 90% coverage: 10:259/279 of query aligns to 15:264/281 of 1vbjA
- active site: D52 (= D46), Y57 (= Y51), K82 (= K76), H115 (= H109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G21), M27 (≠ T22), W28 (= W23), D52 (= D46), Y57 (= Y51), H115 (= H109), N145 (= N140), Q166 (= Q161), W192 (= W187), S193 (= S188), P194 (= P189), L195 (= L190), Q197 (= Q192), G198 (= G193), V201 (≠ A196), A218 (≠ G213), I233 (= I228), K235 (≠ R230), S236 (≠ T231), G237 (≠ S232), R241 (= R236), E244 (= E239), N245 (= N240)
A0QV10 Aldo-keto reductase MSMEG_2408/MSMEI_2347; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
45% identity, 88% coverage: 15:259/279 of query aligns to 13:258/275 of A0QV10
Sites not aligning to the query:
- 262 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
42% identity, 92% coverage: 10:267/279 of query aligns to 11:275/283 of 4g5dA
- active site: D48 (= D46), Y53 (= Y51), K78 (= K76), H111 (= H109)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G21), V23 (≠ T22), W24 (= W23), D48 (= D46), Y53 (= Y51), H111 (= H109), S148 (= S139), N149 (= N140), Q170 (= Q161), W196 (= W187), S197 (= S188), P198 (= P189), L199 (= L190), Q201 (= Q192), G202 (= G193), L205 (≠ A196), I237 (= I228), P238 (= P229), K239 (≠ R230), S240 (≠ T231), V241 (≠ S232), H242 (≠ N233), R245 (= R236), E248 (= E239), N249 (= N240)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
43% identity, 91% coverage: 13:267/279 of query aligns to 14:267/275 of 3d3fA
- active site: D48 (= D46), Y53 (= Y51), K78 (= K76), H111 (= H109)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G21), F24 (≠ W23), D48 (= D46), Y53 (= Y51), H111 (= H109), S140 (= S139), N141 (= N140), Q162 (= Q161), W188 (= W187), S189 (= S188), P190 (= P189), L191 (= L190), Q193 (= Q192), L197 (≠ A196), I229 (= I228), K231 (≠ R230), S232 (≠ T231), K234 (≠ N233), R237 (= R236), E240 (= E239), N241 (= N240)
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Rattus norvegicus (Rat) (see paper)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/325 of P51635
- K23 (≠ Q24) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ V31) Not glycated
- K34 (≠ E35) Not glycated
- K61 (≠ R62) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K76) Not glycated
- K85 (≠ Q81) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (= K93) Not glycated
- K127 (vs. gap) Not glycated
- K134 (vs. gap) Not glycated
- K141 (≠ A118) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (= K122) Not glycated
- K153 (= K130) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R134) Not glycated
- K240 (≠ A207) Not glycated
- K257 (≠ G224) Not glycated
- K263 (≠ R230) Not glycated
- K287 (≠ A254) Not glycated
- K294 (≠ R261) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 13 Not glycated
- 308 Not glycated
Q9JII6 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Mus musculus (Mouse)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
A0QV09 Aldo-keto reductase MSMEG_2407/MSMEI_2346; AKR; AKR5H1; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
40% identity, 90% coverage: 12:263/279 of query aligns to 19:276/283 of A0QV09
- G196 (≠ S188) binding
- L198 (= L190) binding
- V200 (≠ Q192) binding
- I236 (= I228) binding
- R238 (= R230) binding
- S239 (≠ T231) binding
- A240 (≠ S232) binding
- R244 (= R236) binding
- S247 (≠ E239) binding
- N248 (= N240) binding
- R274 (= R261) binding
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
40% identity, 90% coverage: 12:263/279 of query aligns to 10:267/274 of 2wzmA
- active site: D44 (= D46), Y49 (= Y51), K74 (= K76), H107 (= H109)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: Y186 (≠ W187), G187 (≠ S188), P188 (= P189), L189 (= L190), G190 (≠ A191), V191 (≠ Q192), G192 (= G193), L195 (≠ A196), A212 (≠ G213), I227 (= I228), R229 (= R230), S230 (≠ T231), R235 (= R236), N239 (= N240), R265 (= R261)
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Homo sapiens (Human) (see 3 papers)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/325 of P14550
- Y50 (= Y51) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N53) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ D56) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K76) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H109) binding ; mutation to Q: Strong decrease in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 299 I→A: No change in enzymatic activity.; I→C: No change in enzymatic activity.
- 300 V→C: No change in enzymatic activity.
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/322 of 3cv7A
- active site: D45 (= D46), Y50 (= Y51), K80 (= K76), H113 (= H109)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (= W23), Y50 (= Y51), W82 (= W78), H113 (= H109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G21), T21 (= T22), W22 (= W23), Y50 (= Y51), H113 (= H109), Q184 (= Q161), Y210 (≠ W187), S211 (= S188), P212 (= P189), L213 (= L190), S215 (≠ Q192), A246 (≠ G213), I261 (= I228), P262 (= P229), K263 (≠ R230), S264 (≠ T231), V265 (≠ S232), T266 (≠ N233), R269 (= R236), Q272 (≠ E239), N273 (= N240)
Sites not aligning to the query:
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/320 of 3h4gA
- active site: D45 (= D46), Y50 (= Y51), K80 (= K76), H113 (= H109)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (= W23), Y50 (= Y51), H113 (= H109), W114 (= W110), W220 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G21), T21 (= T22), W22 (= W23), D45 (= D46), Y50 (= Y51), H113 (= H109), S162 (= S139), N163 (= N140), Q184 (= Q161), Y210 (≠ W187), S211 (= S188), P212 (= P189), L213 (= L190), S215 (≠ Q192), D217 (≠ K194), A246 (≠ G213), I261 (= I228), P262 (= P229), K263 (≠ R230), S264 (≠ T231), V265 (≠ S232), T266 (≠ N233), R269 (= R236), Q272 (≠ E239), N273 (= N240)
Sites not aligning to the query:
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/325 of 3fx4A
- active site: D45 (= D46), Y50 (= Y51), K80 (= K76), H113 (= H109)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (= W23), Y50 (= Y51), H113 (= H109), R218 (≠ V195), A219 (= A196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G21), T21 (= T22), W22 (= W23), D45 (= D46), Y50 (= Y51), H113 (= H109), Q184 (= Q161), Y210 (≠ W187), S211 (= S188), P212 (= P189), L213 (= L190), S215 (≠ Q192), A246 (≠ G213), I261 (= I228), P262 (= P229), K263 (≠ R230), S264 (≠ T231), V265 (≠ S232), T266 (≠ N233), R269 (= R236), Q272 (≠ E239), N273 (= N240)
Sites not aligning to the query:
P50578 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Sus scrofa (Pig) (see paper)
36% identity, 89% coverage: 15:261/279 of query aligns to 14:294/325 of P50578
- Y50 (= Y51) active site, Proton donor
- H113 (= H109) binding
- 211:273 (vs. 188:240, 33% identical) binding
3wbwA Crystal structure of gox0644 in complex with NADPH
36% identity, 91% coverage: 15:267/279 of query aligns to 14:263/271 of 3wbwA
- active site: D45 (= D46), Y50 (= Y51), K71 (= K76), H104 (= H109)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G21), H104 (= H109), N136 (= N140), W183 (= W187), R184 (≠ S188), P185 (= P189), L186 (= L190), L192 (≠ A196), A209 (≠ G213), K226 (≠ R230), S227 (≠ T231), V228 (≠ S232), R232 (= R236), E235 (= E239), N236 (= N240)
P06632 2,5-diketo-D-gluconic acid reductase A; 2,5-DKG reductase A; 2,5-DKGR A; 25DKGR-A; AKR5C; EC 1.1.1.346 from Corynebacterium sp. (strain ATCC 31090) (see 3 papers)
42% identity, 90% coverage: 15:264/279 of query aligns to 14:266/278 of P06632
- Y50 (= Y51) active site, Proton donor
- H108 (= H109) binding
- 188:242 (vs. 188:240, 43% identical) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3h7uA Crystal structure of the plant stress-response enzyme akr4c9 (see paper)
36% identity, 87% coverage: 15:256/279 of query aligns to 13:279/312 of 3h7uA
- active site: S24 (≠ E26), D44 (= D46), Y49 (= Y51), K78 (= K76), H111 (= H109)
- binding acetate ion: W21 (= W23), Y49 (= Y51), H111 (= H109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G21), T20 (= T22), W21 (= W23), D44 (= D46), Y49 (= Y51), H111 (= H109), W112 (= W110), N156 (= N140), Q177 (= Q161), Y203 (≠ W187), S204 (= S188), P205 (= P189), L206 (= L190), S208 (vs. gap), P209 (vs. gap), G210 (vs. gap), A236 (≠ G213), L251 (≠ I228), P252 (= P229), K253 (≠ R230), S254 (≠ T231), R259 (= R236), E262 (= E239), N263 (= N240)
Q0PGJ6 NADPH-dependent aldo-keto reductase, chloroplastic; AtChlAKR; Aldo-keto reductase family 4 member C9; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 87% coverage: 15:256/279 of query aligns to 16:282/315 of Q0PGJ6
Query Sequence
>CCNA_03541 FitnessBrowser__Caulo:CCNA_03541
MSKLVPAVRSGDVLMPALGFGTWQLENGTAVPLVEKALEIGYRHIDTAQIYGNERDVGAA
IRNSGVKRDEIFLTTKVWIDQFADGDLQRSAEKSLEKLGVDQVDLLLLHWPKPEVPLAET
LKALNAVRAKGWTRAIGLSNFPSAQLEEAAKLSEAPIATDQVEYHPYLSLKTLKAKADQL
GVSITAWSPLAQGKVAQDPVLIEIGRAHGKTPGQVTLRWIIQQGIIAIPRTSNPKRIEEN
FDILDFELSEKEMAQIHGLARPDGRIGDWIDRAYAWDAE
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