SitesBLAST
Comparing WP_089217430.1 NCBI__GCF_900188185.1:WP_089217430.1 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)
Q91WL8 WW domain-containing oxidoreductase; EC 1.1.1.- from Mus musculus (Mouse) (see 3 papers)
34% identity, 91% coverage: 14:292/306 of query aligns to 121:401/414 of Q91WL8
Sites not aligning to the query:
- 33 modified: Phosphotyrosine
- 51:54 KRKR→QGTG: Abolishes the TNF-induced nuclear translocation.
- 125:414 Interaction with MAPT
Q9NZC7 WW domain-containing oxidoreductase; Fragile site FRA16D oxidoreductase; Short chain dehydrogenase/reductase family 41C member 1; EC 1.1.1.- from Homo sapiens (Human) (see 8 papers)
33% identity, 91% coverage: 14:292/306 of query aligns to 121:401/414 of Q9NZC7
- A179 (≠ F72) to T: in dbSNP:rs11545029
- L272 (vs. gap) to F: in dbSNP:rs186745328
- P282 (≠ A167) to A: in dbSNP:rs3764340
- Y287 (≠ N172) modified: Phosphotyrosine; by TNK2; mutation to A: Loss of phosphorylation by TNK2.
- L291 (≠ S175) to P: found in a esophageal cancer sample; somatic mutation; dbSNP:rs119487098
- R314 (≠ M200) to H: in dbSNP:rs73572838
Sites not aligning to the query:
- 28 K→T: No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with V-29.
- 29 D→V: No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with T-28.
- 33 modified: Phosphotyrosine; Y→F: Loss of phosphorylation.; Y→R: Abolishes interaction with TP53, TP73, MAPK8 and ERBB4. Partial loss of interaction with TFAP2C. Loss of phosphorylation. Loss of the proapoptotic activity. Abolishes binding to VOPP1.
- 44:47 WEHP→FEHA: Abolishes interaction with LITAF.
- 61 Y→R: No effect on interaction with TP73.
- 85:88 YLDP→ALDA: No effect on interaction with LITAF.
- 98 P → L: in dbSNP:rs144601717
- 111 T → S: in a Burkitt lymphoma cell line; dbSNP:rs114755364
- 120 R → W: in a primary colorectal tumor and a histiocytic lymphoma cell line; dbSNP:rs141361080
5o98B Binary complex of catharanthus roseus vitrosamine synthase with NADP+ (see paper)
29% identity, 66% coverage: 16:218/306 of query aligns to 1:244/283 of 5o98B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G24), N11 (= N26), K12 (≠ S27), G13 (= G28), I14 (≠ V29), R34 (= R49), R38 (≠ K53), D61 (= D76), V62 (≠ L77), N88 (= N102), A89 (= A103), G90 (= G104), I122 (≠ V123), I149 (≠ T150), S150 (= S151), Y207 (≠ N184), K211 (≠ M188), P235 (= P209), G236 (= G210), F237 (= F211), A238 (= A212), T240 (= T214), L242 (≠ F216), N243 (≠ G217)
7jk9A filaments of plant light-dependent protochlorophyllide oxidoreductase (LPOR) bound to NADPH, Pchlide, and membrane (see paper)
28% identity, 91% coverage: 20:298/306 of query aligns to 6:315/316 of 7jk9A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G10 (= G24), S12 (≠ N26), S13 (= S27), L15 (≠ V29), R36 (= R49), K40 (= K53), L60 (= L75), D61 (= D76), L62 (= L77), N88 (= N102), A89 (= A103), A90 (≠ G104), V91 (= V105), V141 (≠ T150), Y191 (= Y177), G223 (= G210), I225 (≠ F211), T228 (= T214), G229 (≠ N215), L230 (≠ F216), R232 (= R218)
- binding Protochlorophyllide: Y92 (≠ T106), L151 (vs. gap), A152 (vs. gap), Y191 (= Y177), Y221 (≠ H208), C224 (vs. gap), L230 (≠ F216), F231 (≠ G217), F238 (≠ R224), F242 (≠ G228)
6r46A Crystal structure of lpor (thermosynechococcus elongatus) complexed with NADP+ at 2.5a resolution (see paper)
30% identity, 91% coverage: 20:298/306 of query aligns to 5:274/275 of 6r46A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G24), S11 (≠ N26), S12 (= S27), G13 (= G28), V14 (= V29), C33 (= C48), R34 (= R49), L58 (= L75), D59 (= D76), N86 (= N102), A88 (≠ G104), V89 (= V105), K181 (= K181)
6l1hB Crystal structure of light-dependent protochlorophyllide oxidoreductase from thermosynechococcus elongatus (see paper)
29% identity, 91% coverage: 20:298/306 of query aligns to 5:305/305 of 6l1hB
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G24), S11 (≠ N26), S12 (= S27), G13 (= G28), R34 (= R49), K38 (= K53), L58 (= L75), D59 (= D76), L60 (= L77), N86 (= N102), A87 (= A103), A88 (≠ G104), V89 (= V105), T110 (≠ V123), G140 (≠ S151), Y177 (= Y177), K181 (= K181), Y207 (≠ H208), V211 (vs. gap), T214 (vs. gap), P215 (vs. gap), L216 (≠ F211), R218 (= R213)
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
34% identity, 65% coverage: 17:214/306 of query aligns to 6:183/241 of 5t2uA
- active site: G17 (= G28), T135 (≠ S151), T145 (≠ L174), Y148 (= Y177), K152 (= K181)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G24), G17 (= G28), R38 (= R49), D39 (= D50), R42 (≠ K53), D60 (= D76), L61 (= L77), N83 (= N102), A84 (= A103), Y87 (≠ V107), I133 (= I149), T135 (≠ S151), Y148 (= Y177), K152 (= K181), P178 (= P209), P180 (≠ F211), T181 (≠ A212), T183 (= T214)
Sites not aligning to the query:
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 44% coverage: 18:152/306 of query aligns to 8:139/244 of 4nbuB
- active site: G18 (= G28), N111 (= N124), S139 (= S152)
- binding acetoacetyl-coenzyme a: D93 (vs. gap), K98 (≠ R110), S139 (= S152)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G24), N17 (≠ S27), G18 (= G28), I19 (≠ V29), D38 (≠ C48), F39 (≠ R49), V59 (≠ L75), D60 (= D76), V61 (≠ L77), N87 (= N102), A88 (= A103), G89 (= G104), I90 (≠ V105), T137 (= T150), S139 (= S152)
Sites not aligning to the query:
- active site: 149, 152, 156
- binding acetoacetyl-coenzyme a: 146, 147, 149, 152, 184, 189, 200
- binding 1,4-dihydronicotinamide adenine dinucleotide: 152, 156, 182, 184, 185, 187, 189
3o26A The structure of salutaridine reductase from papaver somniferum. (see paper)
36% identity, 29% coverage: 18:105/306 of query aligns to 2:90/294 of 3o26A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G24), N10 (= N26), K11 (≠ S27), G12 (= G28), I13 (≠ V29), R33 (= R49), D59 (= D76), V60 (≠ L77), N87 (= N102), A88 (= A103), G89 (= G104)
Sites not aligning to the query:
- active site: 129, 142, 144, 185
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 140, 167, 168, 225, 229, 253, 255, 256, 258, 260, 261
Q071N0 Salutaridine reductase; EC 1.1.1.248 from Papaver somniferum (Opium poppy) (see 2 papers)
36% identity, 29% coverage: 18:105/306 of query aligns to 13:101/311 of Q071N0
- NKGI 21:24 (≠ NSGV 26:29) binding NADP(+)
- R44 (= R49) binding NADP(+)
- DV 70:71 (≠ DL 76:77) binding NADP(+)
- N98 (= N102) binding NADP(+)
Sites not aligning to the query:
- 104 F→A: Weak substrate inhibition, decreased substrate affinity and increased reaction velocity. Loss of substrate inhibition and doubled maximal velocity; when associated with A-275.
- 106 V→A: Decreased substrate affinity.
- 107 D→A: Decreased substrate affinity.
- 129 binding substrate
- 180 binding substrate
- 181 S→A: No effect on activity.
- 182 T→A: Slightly decreased affinity, but strongly reduced activity.
- 185 L→A: Very low activity.; L→S: Increased substrate affinity, but low activity.; L→V: Reduced activity.
- 186 K→V: No effect on activity.
- 236 active site, Proton acceptor; binding NADP(+)
- 240 binding NADP(+)
- 263 modified: Disulfide link with 305
- 266 L→A: Decreased substrate affinity.; L→V: No effect on substrate affinity.
- 267:272 binding NADP(+)
- 271 M→A: Abrogate substrate inhibition. Decreased substrate affinity and decreased reductase activity.
- 272 N→A: Abrogate substrate inhibition. Decreased substrate affinity and decreased reductase activity.
- 275 I→A: Weak substrate inhibition, decreased substrate affinity and increased reaction velocity. Loss of substrate inhibition and doubled maximal velocity; when associated with A-104.; I→V: No effect on substrate affinity.
- 305 modified: Disulfide link with 263
A4UHT7 Salutaridine reductase; EC 1.1.1.248 from Papaver bracteatum (Great scarlet poppy) (see 2 papers)
26% identity, 44% coverage: 18:152/306 of query aligns to 13:180/311 of A4UHT7
- R44 (= R49) mutation to E: More than 50-fold decrease in affinity towards NADPH.
- R48 (≠ K53) mutation to E: 30-fold decrease in affinity towards NADPH. 1.5-fold increase in affinity towards NADH.; mutation to K: 2.5-fold decrease in affinity towards NADPH. 2-fold increase in affinity towards NADH.
- F104 (vs. gap) mutation to A: Strong decrease in substrate affinity and catalytic efficiency. Strongly reduced substrate inhibition. Almost 200-fold decrease in substrate affinity and 112-fold decrease in catalytic efficiency but no substrate inhibition; when associated with A-275.
- V106 (vs. gap) mutation to A: Decrease in substrate affinity. Increase in catalytic efficiency.
- D107 (vs. gap) mutation to A: 7-fold decrease in substrate affinity. 15-fold decrease in catalytic efficiency. Strongly reduced substrate inhibition.
- N152 (= N124) mutation to A: 6-fold decrease in catalytic efficiency.
- S180 (= S152) mutation to A: 3-fold decrease in substrate affinity. More than 2300-fold decrease in catalytic efficiency.
Sites not aligning to the query:
- 181 S→A: More than 2-fold decrease in substrate affinity. 1.5-fold decrease in catalytic efficiency.
- 182 T→A: 2-fold decrease in substrate affinity. 20-fold decrease in catalytic efficiency.
- 185 L→A: 6-fold decrease in substrate affinity. 550-fold decrease in catalytic efficiency. No substrate inhibition.; L→S: Almost 2-fold increase in substrate affinity. Almost 5-fold decrease in catalytic efficiency.; L→V: Almost 2-fold decrease in catalytic efficiency.
- 186 K→V: Almost 4-fold decrease in substrate affinity. More than 4-fold decrease in catalytic efficiency.
- 236 Y→F: Inactive.
- 240 K→E: Inactive.
- 266 L→A: Strong decrease in substrate affinity and catalytic efficiency. No substrate inhibition.; L→S: 12-fold decrease in substrate affinity and 26-fold decrease in catalytic efficiency.; L→V: 6-fold decrease in substrate affinity. 7-fold decrease in catalytic efficiency.
- 271 M→A: Almost 11-fold decrease in substrate affinity and 2200-fold decrease in catalytic efficiency but no substrate inhibition.; M→T: Inactive.
- 272 N→A: Almost 43-fold decrease in substrate affinity and 3300-fold decrease in catalytic efficiency but no substrate inhibition.; N→T: Inactive.
- 275 I→A: 15-fold decrease in substrate affinity. Almost 7-fold decrease in catalytic efficiency and strongly reduced substrate inhibition. Almost 200-fold decrease in substrate affinity and 112-fold decrease in catalytic efficiency but no substrate inhibition; when associated with A-104.; I→V: Slight decrease in catalytic efficiency.
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
31% identity, 66% coverage: 18:218/306 of query aligns to 9:194/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G24), R18 (≠ S27), G19 (= G28), I20 (≠ V29), D39 (≠ C48), R40 (= R49), C63 (≠ L75), I65 (≠ L77), N91 (= N102), G93 (= G104), I94 (≠ V105), V114 (= V123), Y155 (= Y171), K159 (= K181), I188 (≠ A212), T190 (= T214), T193 (≠ G217)
6gtuA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with fragment j6
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/268 of 6gtuA
Sites not aligning to the query:
- active site: 17, 151, 155
- binding N-(1,3-benzodioxol-5-ylmethyl)cyclopentanamine: 183, 253
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 182, 184, 186, 188
6emmA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with salicylic acid
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/268 of 6emmA
Sites not aligning to the query:
- active site: 17, 151, 155
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 181, 182, 184, 186, 188
5hs6A Human 17beta-hydroxysteroid dehydrogenase type 14 in complex with estrone (see paper)
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/257 of 5hs6A
Sites not aligning to the query:
- active site: 17, 148, 151, 155
- binding (9beta,13alpha)-3-hydroxyestra-1,3,5(10)-trien-17-one: 145, 151, 192
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 181, 182, 183, 184, 186, 188
5o6oA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with a non-steroidal 2,6-pyridinketone inhibitor (see paper)
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/256 of 5o6oA
Sites not aligning to the query:
- active site: 17, 151, 155
- binding 2-fluoranyl-3-[6-(4-fluoranyl-3-oxidanyl-phenoxy)pyridin-2-yl]phenol: 145, 146, 147, 151, 183, 189, 192
- binding beta-D-glucopyranose: 185, 186, 187, 190
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 181, 182, 183, 184, 186, 188
5o42A 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with a non-steroidal 2,6-pyridinketone inhibitor. (see paper)
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/256 of 5o42A
Sites not aligning to the query:
- active site: 17, 151, 155
- binding 2-fluoranyl-3-[6-[1-(4-fluoranyl-3-oxidanyl-phenyl)ethenyl]pyridin-2-yl]phenol: 145, 146, 151, 183, 189, 192
- binding beta-D-glucopyranose: 17, 185, 186, 187, 190
- binding nicotinamide-adenine-dinucleotide: 13, 16, 18, 151, 155, 181, 182, 183, 184, 186, 188
5l7wA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with a non-steroidal inhibitor. (see paper)
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/254 of 5l7wA
- active site: S138 (= S151)
- binding [4-fluoranyl-2,3-bis(oxidanyl)phenyl]-[6-(2-fluoranyl-3-oxidanyl-phenyl)pyridin-2-yl]methanone: H90 (≠ T106), S138 (= S151)
- binding nicotinamide-adenine-dinucleotide: D37 (≠ C48), K38 (≠ R49), D59 (= D76), V60 (≠ L77), N86 (= N102), A87 (= A103), G88 (= G104), L110 (≠ V123), S138 (= S151)
Sites not aligning to the query:
- active site: 17, 148, 151, 155
- binding [4-fluoranyl-2,3-bis(oxidanyl)phenyl]-[6-(2-fluoranyl-3-oxidanyl-phenyl)pyridin-2-yl]methanone: 145, 146, 147, 151, 183, 189, 192
- binding beta-D-glucopyranose: 185, 186, 187, 190
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 181, 182, 183, 184, 186, 188
6qckA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with fb262 (see paper)
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/258 of 6qckA
Sites not aligning to the query:
- active site: 17, 151, 155
- binding beta-D-glucopyranose: 185, 186, 187, 190
- binding 2-[2-(1,3-benzodioxol-2-yl)ethyl]benzoic acid: 145, 151, 188, 189, 192
- binding nicotinamide-adenine-dinucleotide: 13, 16, 18, 151, 155, 181, 182, 183, 184, 186, 188
6gtbA 17beta-hydroxysteroid dehydrogenase 14 variant t205 in complex with fb211
36% identity, 36% coverage: 42:151/306 of query aligns to 31:138/257 of 6gtbA
Sites not aligning to the query:
- active site: 17, 151, 155
- binding beta-D-glucopyranose: 17, 185, 186, 187, 190
- binding 3-[6-(3-hydroxyphenyl)pyridin-2-yl]benzoic acid: 145, 146, 147, 151, 189, 192, 196
- binding nicotinamide-adenine-dinucleotide: 13, 16, 17, 18, 151, 155, 181, 182, 183, 184, 186, 188
Query Sequence
>WP_089217430.1 NCBI__GCF_900188185.1:WP_089217430.1
MPSRAGFTAADVPDQSGKCLIVTGANSGVGFEVASALAARRARVLLACRDESKARAAMDK
IRQRSSGADLAFLPLDLADLASVRKAAEVAAKEPRIDVLINNAGVTVPTRQTTRQGFELL
FGVNHLGSFALTALMLPKLRETPGSRIVITSSGQHKGAKIEWDDLNAEKNYNWLSRYGAS
KLANLLFMLELNRRLQAAEMPVTTVGCHPGFARTNFGRASLAGRLAVGVGGLLFNTPAMG
AWPTLQAATGNVKPGGYYGPTAFAELRGPSFECTPSDDARNPQLARRLWDVSIEMTGIDP
DLAPAS
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