SitesBLAST
Comparing Dsui_1443 FitnessBrowser__PS:Dsui_1443 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)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
68% identity, 98% coverage: 6:436/438 of query aligns to 3:432/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ H140), F140 (= F145), A213 (= A218), E214 (= E219), P215 (= P220), I235 (≠ L240), G237 (= G242), L238 (= L243), S239 (= S244), P244 (= P249), D304 (= D309), R325 (= R330), I331 (= I336), N336 (= N341)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
68% identity, 98% coverage: 6:436/438 of query aligns to 3:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ H140), F140 (= F145), G212 (= G217), A213 (= A218), E214 (= E219), P215 (= P220), I235 (≠ L240), G237 (= G242), L238 (= L243), S239 (= S244), P244 (= P249), D304 (= D309), R325 (= R330), I331 (= I336), N336 (= N341)
- binding magnesium ion: S204 (= S209), V228 (≠ F233)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
67% identity, 97% coverage: 12:436/438 of query aligns to 5:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K72), S90 (= S97), S91 (= S98), G92 (= G99), T93 (= T100), T94 (= T101), F138 (= F145), A211 (= A218), E212 (= E219), P213 (= P220), D232 (= D239), I233 (≠ L240), Y234 (= Y241), G235 (= G242), L236 (= L243), S237 (= S244), D302 (= D309), I320 (= I327), R323 (= R330), K419 (= K428)
- binding magnesium ion: V200 (≠ A207), S202 (= S209), L204 (= L211), M226 (≠ F233), G227 (= G234), Q347 (= Q354), L350 (= L357)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
67% identity, 97% coverage: 12:436/438 of query aligns to 5:425/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (≠ H140), F136 (= F145), G138 (= G147), G208 (= G217), A209 (= A218), E210 (= E219), P211 (= P220), I231 (≠ L240), Y232 (= Y241), G233 (= G242), L234 (= L243), S235 (= S244), P240 (= P249), D300 (= D309), R321 (= R330), K417 (= K428)
- binding magnesium ion: V198 (≠ A207), S200 (= S209), Q345 (= Q354), L348 (= L357)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
42% identity, 97% coverage: 12:436/438 of query aligns to 9:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A218), E216 (= E219), P217 (= P220), N236 (≠ D239), S237 (≠ L240), F238 (≠ Y241), G239 (= G242), M240 (≠ L243), T241 (≠ S244), D305 (= D309), R329 (= R330), I335 (= I336), N340 (= N341)
- binding zinc ion: C252 (= C255), H259 (≠ T263), C314 (vs. gap), C316 (≠ T317)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
41% identity, 97% coverage: 12:436/438 of query aligns to 9:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A218), E216 (= E219), P217 (= P220), S237 (≠ L240), F238 (≠ Y241), G239 (= G242), M240 (≠ L243), T241 (≠ S244), D305 (= D309), R329 (= R330), N340 (= N341)
- binding adenosine monophosphate: A215 (= A218), E216 (= E219), P217 (= P220), S237 (≠ L240), F238 (≠ Y241), G239 (= G242), M240 (≠ L243), T241 (≠ S244), D305 (= D309), R329 (= R330), N340 (= N341)
- binding coenzyme a: S136 (≠ A139), A164 (≠ G167), G165 (= G168), N166 (≠ Q169), S167 (≠ T170), I185 (≠ T188), Y188 (= Y191), K337 (≠ R338), T408 (≠ S410)
- binding zinc ion: C252 (= C255), H259 (≠ T263), C314 (vs. gap), C316 (≠ T317)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
34% identity, 97% coverage: 12:436/438 of query aligns to 30:464/477 of 6he0A
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] 2-methyl-2-oxidanyl-propanoate: S241 (≠ G217), G242 (≠ A218), E243 (= E219), P244 (= P220), G267 (≠ Y241), S268 (≠ G242), M269 (≠ L243), A270 (≠ S244), D335 (= D309), I357 (= I327), N371 (= N341)
- binding adenosine monophosphate: G242 (≠ A218), E243 (= E219), P244 (= P220), C266 (≠ L240), G267 (≠ Y241), S268 (≠ G242), A270 (≠ S244), E271 (= E245), D335 (= D309), N371 (= N341)
- binding coenzyme a: Y166 (≠ F145), A188 (≠ G167), G189 (vs. gap), P191 (vs. gap), S194 (≠ T170), Y210 (≠ V186), G211 (≠ V187), T212 (= T188), Y215 (= Y191), H218 (≠ N194), R368 (= R338), G369 (= G339), M401 (≠ L371), V439 (≠ I409), R440 (≠ S410)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
33% identity, 97% coverage: 12:436/438 of query aligns to 30:461/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F145), S237 (≠ G217), G263 (≠ Y241), S264 (≠ G242), M265 (≠ L243), A266 (≠ S244), F271 (≠ G250)
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (3~{S})-3-oxidanylbutanoate: Y162 (≠ F145), G164 (= G147), S237 (≠ G217), G238 (≠ A218), E239 (= E219), P240 (= P220), C262 (≠ L240), G263 (≠ Y241), S264 (≠ G242), A266 (≠ S244), F271 (≠ G250), D331 (= D309), I353 (= I327), R356 (= R330), K453 (= K428)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
33% identity, 97% coverage: 12:436/438 of query aligns to 30:461/474 of 6hdxA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (2~{R})-2-methyl-3-oxidanyl-propanoate: Y162 (≠ F145), G164 (= G147), S237 (≠ G217), G238 (≠ A218), E239 (= E219), P240 (= P220), C262 (≠ L240), G263 (≠ Y241), S264 (≠ G242), A266 (≠ S244), F271 (≠ G250), D331 (= D309), I353 (= I327), R356 (= R330), K453 (= K428)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F145), G164 (= G147), S237 (≠ G217), G263 (≠ Y241), S264 (≠ G242), A266 (≠ S244), F271 (≠ G250)
6siwA Paak family amp-ligase with amp (see paper)
30% identity, 96% coverage: 17:435/438 of query aligns to 8:414/432 of 6siwA
- binding adenosine monophosphate: S84 (= S98), A208 (= A218), E209 (= E219), P210 (= P220), E231 (≠ L240), Y232 (= Y241), G233 (= G242), S234 (≠ L243), T235 (≠ S244), D295 (= D309), V315 (≠ I327)
- binding magnesium ion: E75 (≠ R89), L77 (≠ I91), S83 (= S97), P116 (= P132), G143 (= G159), T145 (= T161), E236 (= E245)
- binding zinc ion: C244 (= C255), H250 (≠ G261), C304 (≠ P316), C306 (≠ A318)
6siyA Paak family amp-ligase with amp and substrate (see paper)
30% identity, 96% coverage: 17:435/438 of query aligns to 9:415/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ H140), P126 (≠ G141), T132 (= T146), L135 (= L149), R153 (vs. gap), N177 (≠ T188), A209 (= A218), E232 (≠ L240), G234 (= G242), S235 (≠ L243)
- binding adenosine monophosphate: S85 (= S98), A209 (= A218), E210 (= E219), P211 (= P220), E232 (≠ L240), Y233 (= Y241), G234 (= G242), S235 (≠ L243), T236 (≠ S244), D296 (= D309), V316 (≠ I327)
- binding magnesium ion: R75 (≠ M88), E76 (≠ R89), L78 (≠ I91), P117 (= P132), G144 (= G159), A145 (= A160), T146 (= T161)
6sixB Paak family amp-ligase with anp (see paper)
30% identity, 96% coverage: 17:435/438 of query aligns to 13:419/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S97), S89 (= S98), A213 (= A218), E214 (= E219), P215 (= P220), E236 (≠ L240), Y237 (= Y241), G238 (= G242), S239 (≠ L243), T240 (≠ S244), E241 (= E245), D300 (= D309), V320 (≠ I327), R323 (= R330)
- binding magnesium ion: R79 (≠ M88), E80 (≠ R89), P121 (= P132), T150 (= T161)
- binding zinc ion: C249 (= C255), H255 (≠ G261), C309 (≠ P316), C311 (≠ A318)
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
28% identity, 46% coverage: 90:292/438 of query aligns to 196:404/556 of Q9S725
- K211 (≠ T105) mutation to S: Drastically reduces the activity.
- M293 (≠ V186) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L215) mutation K->L,A: Affects the substrate specificity.
- E401 (= E289) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V291) mutation to A: Significantly reduces the substrate specificity.
Sites not aligning to the query:
- 449 R→Q: Drastically reduces the activity.
- 457 K→S: Drastically reduces the activity.
- 540 K→N: Abolishes the activity.
1t5dX 4-chlorobenzoyl-coa ligase/synthetase bound to 4-chlorobenzoate (see paper)
25% identity, 65% coverage: 65:348/438 of query aligns to 124:416/502 of 1t5dX
Sites not aligning to the query:
3cw8X 4-chlorobenzoyl-coa ligase/synthetase, bound to 4cba-adenylate (see paper)
26% identity, 65% coverage: 65:348/438 of query aligns to 124:418/501 of 3cw8X
- binding 5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine: H207 (≠ G154), V208 (= V155), V209 (≠ L158), G281 (≠ A218), A282 (≠ E219), T283 (≠ P220), I303 (≠ L240), Y304 (= Y241), G305 (= G242), T306 (≠ L243), T307 (≠ S244), M310 (= M247), N311 (≠ G248), M324 (≠ W265), D385 (= D309)
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
25% identity, 65% coverage: 65:348/438 of query aligns to 124:418/503 of 3cw9A
- active site: T161 (= T110), R181 (≠ A128), H207 (≠ G154), T307 (≠ S244), E308 (= E245), I406 (= I336), N411 (= N341)
- binding 4-Chlorophenacyl-coenzyme A: M203 (≠ G150), P204 (≠ V151), H207 (≠ G154), V208 (= V155), V209 (≠ L158), A280 (≠ G217), G305 (= G242), T306 (≠ L243), M310 (= M247), N311 (≠ G248), S407 (≠ I337), G408 (≠ R338), G409 (= G339), E410 (≠ V340)
- binding adenosine monophosphate: T161 (= T110), G281 (≠ A218), A282 (≠ E219), T283 (≠ P220), I303 (≠ L240), Y304 (= Y241), G305 (= G242), T306 (≠ L243), T307 (≠ S244), D385 (= D309), R400 (= R330), I406 (= I336), N411 (= N341)
Sites not aligning to the query:
5wm4A Crystal structure of cahj in complex with 6-methylsalicyl adenylate (see paper)
29% identity, 40% coverage: 69:245/438 of query aligns to 166:337/534 of 5wm4A
- active site: S193 (= S97), N213 (≠ M121), H237 (= H140), A336 (≠ S244), E337 (= E245)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ G141), F239 (≠ Y142), C243 (≠ T146), G309 (= G217), G310 (≠ A218), S311 (≠ E219), K312 (≠ P220), V332 (≠ L240), F333 (≠ Y241), G334 (= G242), M335 (≠ L243), A336 (≠ S244)
Sites not aligning to the query:
5wm5A Crystal structure of cahj in complex with 5-methylsalicyl adenylate (see paper)
29% identity, 40% coverage: 69:245/438 of query aligns to 166:337/533 of 5wm5A
- active site: S193 (= S97), N213 (≠ M121), H237 (= H140), A336 (≠ S244), E337 (= E245)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: H237 (= H140), N238 (≠ G141), F239 (≠ Y142), G309 (= G217), G310 (≠ A218), S311 (≠ E219), K312 (≠ P220), V332 (≠ L240), F333 (≠ Y241), G334 (= G242), M335 (≠ L243), A336 (≠ S244)
Sites not aligning to the query:
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 40% coverage: 69:245/438 of query aligns to 166:337/535 of 5wm6A
- active site: S193 (= S97), N213 (≠ M121), H237 (= H140), A336 (≠ S244), E337 (= E245)
- binding magnesium ion: S301 (= S209), L303 (= L211), G326 (= G234)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ Y142), G310 (≠ A218), S311 (≠ E219), K312 (≠ P220), V332 (≠ L240), F333 (≠ Y241), G334 (= G242), M335 (≠ L243), A336 (≠ S244)
Sites not aligning to the query:
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
29% identity, 40% coverage: 69:245/438 of query aligns to 166:337/536 of 5wm2A
- active site: S193 (= S97), N213 (≠ M121), H237 (= H140), A336 (≠ S244), E337 (= E245)
- binding adenosine monophosphate: G310 (≠ A218), S311 (≠ E219), K312 (≠ P220), V332 (≠ L240), F333 (≠ Y241), G334 (= G242), M335 (≠ L243), A336 (≠ S244), E337 (= E245)
Sites not aligning to the query:
Query Sequence
>Dsui_1443 FitnessBrowser__PS:Dsui_1443
MHRESAAALEGERIARASRDEIAALQLKRLQQSLRHAYEKVPHTRAKFDAHGVHPDDLKT
LADLARFPFTGKQDLRDNYPYGLFAVPMRDIVRVHASSGTTGKPTVVGYTAGDIDRWADI
MARALRAAGAGPEDIVHVAHGYGLFTGGLGVHYGVERLGATAVPVSGGQTERQVQLIADF
KPTVLVVTPSYALNLADECEHQGFDLAGSSLRIGLFGAEPWGESMRAEIERRFGIAAMDL
YGLSEVMGPGVASECIESRDGPTIWEDHFYPEIIDPNTGEVLPDGAHGELVFTSLTKEGM
PVVRYRTRDLTTLLPPTARSFRRIGKITGRSDDMLIIRGVNVFPSQIEEFVLKQAELSPH
YQLEVWREGHLDKLDIRVELKPEFANAGTHVSEQAARELQHHIKSYIGISTRVRVEAVGS
IERAVGGKARRVVDKRPQ
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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